data_3KLS
# 
_entry.id   3KLS 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.294 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   3KLS         
RCSB  RCSB056151   
WWPDB D_1000056151 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 3CU7 'Structure of complement C5'                                                      unspecified 
PDB 2QEJ 'Structure of the complex between SSL7 and IgA Fc'                                unspecified 
PDB 3KM9 'Structure of complement C5 in complex with C-terminal beta-grasp domain of SSL7' unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        3KLS 
_pdbx_database_status.recvd_initial_deposition_date   2009-11-09 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Laursen, N.S.'      1  
'Gordon, N.'         2  
'Hermans, S.'        3  
'Lorenz, N.'         4  
'Jackson, N.'        5  
'Wines, B.'          6  
'Spillner, E.'       7  
'Christensen, J.B.'  8  
'Jensen, M.'         9  
'Fredslund, F.'      10 
'Bjerre, M.'         11 
'Sottrup-Jensen, L.' 12 
'Fraser, J.D.'       13 
'Andersen, G.R.'     14 
# 
_citation.id                        primary 
_citation.title                     
'Structural basis for inhibition of complement C5 by the SSL7 protein from Staphylococcus aureus' 
_citation.journal_abbrev            Proc.Natl.Acad.Sci.USA 
_citation.journal_volume            107 
_citation.page_first                3681 
_citation.page_last                 3686 
_citation.year                      2010 
_citation.journal_id_ASTM           PNASA6 
_citation.country                   US 
_citation.journal_id_ISSN           0027-8424 
_citation.journal_id_CSD            0040 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   20133685 
_citation.pdbx_database_id_DOI      10.1073/pnas.0910565107 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Laursen, N.S.'      1  
primary 'Gordon, N.'         2  
primary 'Hermans, S.'        3  
primary 'Lorenz, N.'         4  
primary 'Jackson, N.'        5  
primary 'Wines, B.'          6  
primary 'Spillner, E.'       7  
primary 'Christensen, J.B.'  8  
primary 'Jensen, M.'         9  
primary 'Fredslund, F.'      10 
primary 'Bjerre, M.'         11 
primary 'Sottrup-Jensen, L.' 12 
primary 'Fraser, J.D.'       13 
primary 'Andersen, G.R.'     14 
# 
_cell.entry_id           3KLS 
_cell.length_a           143.875 
_cell.length_b           143.875 
_cell.length_c           241.240 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        120.00 
_cell.Z_PDB              6 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         3KLS 
_symmetry.space_group_name_H-M             'P 31' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                144 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     nat 'Complement C5'        188526.125 2 ? ?    ? ? 
2 polymer     man 'Exotoxin 1'           26014.383  2 ? E35G ? ? 
3 non-polymer syn 'CADMIUM ION'          112.411    9 ? ?    ? ? 
4 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208    6 ? ?    ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 
;C3 and PZP-like alpha-2-macroglobulin domain-containing protein 4, Complement C5 beta chain, Complement C5 alpha chain, C5a anaphylatoxin, Complement C5 alpha' chain
;
2 SSL7 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;MGLLGILCFLIFLGKTWGQEQTYVISAPKIFRVGASENIVIQVYGYTEAFDATISIKSYPDKKFSYSSGHVHLSSENKFQ
NSAILTIQPKQLPGGQNPVSYVYLEVVSKHFSKSKRMPITYDNGFLFIHTDKPVYTPDQSVKVRVYSLNDDLKPAKRETV
LTFIDPEGSEVDMVEEIDHIGIISFPDFKIPSNPRYGMWTIKAKYKEDFSTTGTAYFEVKEYVLPHFSVSIEPEYNFIGY
KNFKNFEITIKARYFYNKVVTEADVYITFGIREDLKDDQKEMMQTAMQNTMLINGIAQVTFDSETAVKELSYYSLEDLNN
KYLYIAVTVIESTGGFSEEAEIPGIKYVLSPYKLNLVATPLFLKPGIPYPIKVQVKDSLDQLVGGVPVTLNAQTIDVNQE
TSDLDPSKSVTRVDDGVASFVLNLPSGVTVLEFNVKTDAPDLPEENQAREGYRAIAYSSLSQSYLYIDWTDNHKALLVGE
HLNIIVTPKSPYIDKITHYNYLILSKGKIIHFGTREKFSDASYQSINIPVTQNMVPSSRLLVYYIVTGEQTAELVSDSVW
LNIEEKCGNQLQVHLSPDADAYSPGQTVSLNMATGMDSWVALAAVDSAVYGVQRGAKKPLERVFQFLEKSDLGCGAGGGL
NNANVFHLAGLTFLTNANADDSQENDEPCKEILRPRRTLQKKIEEIAAKYKHSVVKKCCYDGACVNNDETCEQRAARISL
GPRCIKAFTECCVVASQLRANISHKDMQLGRLHMKTLLPVSKPEIRSYFPESWLWEVHLVPRRKQLQFALPDSLTTWEIQ
GIGISNTGICVADTVKAKVFKDVFLEMNIPYSVVRGEQIQLKGTVYNYRTSGMQFCVKMSAVEGICTSESPVIDHQGTKS
SKCVRQKVEGSSSHLVTFTVLPLEIGLHNINFSLETWFGKEILVKTLRVVPEGVKRESYSGVTLDPRGIYGTISRRKEFP
YRIPLDLVPKTEIKRILSVKGLLVGEILSAVLSQEGINILTHLPKGSAEAELMSVVPVFYVFHYLETGNHWNIFHSDPLI
EKQKLKKKLKEGMLSIMSYRNADYSYSVWKGGSASTWLTAFALRVLGQVNKYVEQNQNSICNSLLWLVENYQLDNGSFKE
NSQYQPIKLQGTLPVEARENSLYLTAFTVIGIRKAFDICPLVKIDTALIKADNFLLENTLPAQSTFTLAISAYALSLGDK
THPQFRSIVSALKREALVKGNPPIYRFWKDNLQHKDSSVPNTGTARMVETTAYALLTSLNLKDINYVNPVIKWLSEEQRY
GGGFYSTQDTINAIEGLTEYSLLVKQLRLSMDIDVSYKHKGALHNYKMTDKNFLGRPVEVLLNDDLIVSTGFGSGLATVH
VTTVVHKTSTSEEVCSFYLKIDTQDIEASHYRGYGNSDYKRIVACASYKPSREESSSGSSHAVMDISLPTGISANEEDLK
ALVEGVDQLFTDYQIKDGHVILQLNSIPSSDFLCVRFRIFELFEVGFLSPATFTVYEYHRPDKQCTMFYSTSNIKIQKVC
EGAACKCVEADCGQMQEELDLTISAETRKQTACKPEIAYAYKVSITSITVENVFVKYKATLLDIYKTGEAVAEKDSEITF
IKKVTCTNAELVKGRQYLIMGKEALQIKYNFSFRYIYPLDSLTWIEYWPRDTTCSSCQAFLANLDEFAEDIFLNGC
;
;MGLLGILCFLIFLGKTWGQEQTYVISAPKIFRVGASENIVIQVYGYTEAFDATISIKSYPDKKFSYSSGHVHLSSENKFQ
NSAILTIQPKQLPGGQNPVSYVYLEVVSKHFSKSKRMPITYDNGFLFIHTDKPVYTPDQSVKVRVYSLNDDLKPAKRETV
LTFIDPEGSEVDMVEEIDHIGIISFPDFKIPSNPRYGMWTIKAKYKEDFSTTGTAYFEVKEYVLPHFSVSIEPEYNFIGY
KNFKNFEITIKARYFYNKVVTEADVYITFGIREDLKDDQKEMMQTAMQNTMLINGIAQVTFDSETAVKELSYYSLEDLNN
KYLYIAVTVIESTGGFSEEAEIPGIKYVLSPYKLNLVATPLFLKPGIPYPIKVQVKDSLDQLVGGVPVTLNAQTIDVNQE
TSDLDPSKSVTRVDDGVASFVLNLPSGVTVLEFNVKTDAPDLPEENQAREGYRAIAYSSLSQSYLYIDWTDNHKALLVGE
HLNIIVTPKSPYIDKITHYNYLILSKGKIIHFGTREKFSDASYQSINIPVTQNMVPSSRLLVYYIVTGEQTAELVSDSVW
LNIEEKCGNQLQVHLSPDADAYSPGQTVSLNMATGMDSWVALAAVDSAVYGVQRGAKKPLERVFQFLEKSDLGCGAGGGL
NNANVFHLAGLTFLTNANADDSQENDEPCKEILRPRRTLQKKIEEIAAKYKHSVVKKCCYDGACVNNDETCEQRAARISL
GPRCIKAFTECCVVASQLRANISHKDMQLGRLHMKTLLPVSKPEIRSYFPESWLWEVHLVPRRKQLQFALPDSLTTWEIQ
GIGISNTGICVADTVKAKVFKDVFLEMNIPYSVVRGEQIQLKGTVYNYRTSGMQFCVKMSAVEGICTSESPVIDHQGTKS
SKCVRQKVEGSSSHLVTFTVLPLEIGLHNINFSLETWFGKEILVKTLRVVPEGVKRESYSGVTLDPRGIYGTISRRKEFP
YRIPLDLVPKTEIKRILSVKGLLVGEILSAVLSQEGINILTHLPKGSAEAELMSVVPVFYVFHYLETGNHWNIFHSDPLI
EKQKLKKKLKEGMLSIMSYRNADYSYSVWKGGSASTWLTAFALRVLGQVNKYVEQNQNSICNSLLWLVENYQLDNGSFKE
NSQYQPIKLQGTLPVEARENSLYLTAFTVIGIRKAFDICPLVKIDTALIKADNFLLENTLPAQSTFTLAISAYALSLGDK
THPQFRSIVSALKREALVKGNPPIYRFWKDNLQHKDSSVPNTGTARMVETTAYALLTSLNLKDINYVNPVIKWLSEEQRY
GGGFYSTQDTINAIEGLTEYSLLVKQLRLSMDIDVSYKHKGALHNYKMTDKNFLGRPVEVLLNDDLIVSTGFGSGLATVH
VTTVVHKTSTSEEVCSFYLKIDTQDIEASHYRGYGNSDYKRIVACASYKPSREESSSGSSHAVMDISLPTGISANEEDLK
ALVEGVDQLFTDYQIKDGHVILQLNSIPSSDFLCVRFRIFELFEVGFLSPATFTVYEYHRPDKQCTMFYSTSNIKIQKVC
EGAACKCVEADCGQMQEELDLTISAETRKQTACKPEIAYAYKVSITSITVENVFVKYKATLLDIYKTGEAVAEKDSEITF
IKKVTCTNAELVKGRQYLIMGKEALQIKYNFSFRYIYPLDSLTWIEYWPRDTTCSSCQAFLANLDEFAEDIFLNGC
;
A,B ? 
2 'polypeptide(L)' no no 
;MKLKTLAKATLALGLLTTGVITSEGQAVQAAEKQGRVQHLHDIRDLHRYYSSESFEYSNVSGKVENYNGSNVVRFNPKDQ
NHQLFLLGKDKEQYKEGLQGQNVFVVQELIDPNGRLSTVGGVTKKNNKTSETNTPLFVNKVNGEDLDASIDSFLIQKEEI
SLKELDFKIRQQLVNNYGLYKGTSKYGKIIINLKDENKVEIDLGDKLQFERMGDVLNSKDIRGISVTINQI
;
;MKLKTLAKATLALGLLTTGVITSEGQAVQAAEKQGRVQHLHDIRDLHRYYSSESFEYSNVSGKVENYNGSNVVRFNPKDQ
NHQLFLLGKDKEQYKEGLQGQNVFVVQELIDPNGRLSTVGGVTKKNNKTSETNTPLFVNKVNGEDLDASIDSFLIQKEEI
SLKELDFKIRQQLVNNYGLYKGTSKYGKIIINLKDENKVEIDLGDKLQFERMGDVLNSKDIRGISVTINQI
;
X,Y ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    MET n 
1 2    GLY n 
1 3    LEU n 
1 4    LEU n 
1 5    GLY n 
1 6    ILE n 
1 7    LEU n 
1 8    CYS n 
1 9    PHE n 
1 10   LEU n 
1 11   ILE n 
1 12   PHE n 
1 13   LEU n 
1 14   GLY n 
1 15   LYS n 
1 16   THR n 
1 17   TRP n 
1 18   GLY n 
1 19   GLN n 
1 20   GLU n 
1 21   GLN n 
1 22   THR n 
1 23   TYR n 
1 24   VAL n 
1 25   ILE n 
1 26   SER n 
1 27   ALA n 
1 28   PRO n 
1 29   LYS n 
1 30   ILE n 
1 31   PHE n 
1 32   ARG n 
1 33   VAL n 
1 34   GLY n 
1 35   ALA n 
1 36   SER n 
1 37   GLU n 
1 38   ASN n 
1 39   ILE n 
1 40   VAL n 
1 41   ILE n 
1 42   GLN n 
1 43   VAL n 
1 44   TYR n 
1 45   GLY n 
1 46   TYR n 
1 47   THR n 
1 48   GLU n 
1 49   ALA n 
1 50   PHE n 
1 51   ASP n 
1 52   ALA n 
1 53   THR n 
1 54   ILE n 
1 55   SER n 
1 56   ILE n 
1 57   LYS n 
1 58   SER n 
1 59   TYR n 
1 60   PRO n 
1 61   ASP n 
1 62   LYS n 
1 63   LYS n 
1 64   PHE n 
1 65   SER n 
1 66   TYR n 
1 67   SER n 
1 68   SER n 
1 69   GLY n 
1 70   HIS n 
1 71   VAL n 
1 72   HIS n 
1 73   LEU n 
1 74   SER n 
1 75   SER n 
1 76   GLU n 
1 77   ASN n 
1 78   LYS n 
1 79   PHE n 
1 80   GLN n 
1 81   ASN n 
1 82   SER n 
1 83   ALA n 
1 84   ILE n 
1 85   LEU n 
1 86   THR n 
1 87   ILE n 
1 88   GLN n 
1 89   PRO n 
1 90   LYS n 
1 91   GLN n 
1 92   LEU n 
1 93   PRO n 
1 94   GLY n 
1 95   GLY n 
1 96   GLN n 
1 97   ASN n 
1 98   PRO n 
1 99   VAL n 
1 100  SER n 
1 101  TYR n 
1 102  VAL n 
1 103  TYR n 
1 104  LEU n 
1 105  GLU n 
1 106  VAL n 
1 107  VAL n 
1 108  SER n 
1 109  LYS n 
1 110  HIS n 
1 111  PHE n 
1 112  SER n 
1 113  LYS n 
1 114  SER n 
1 115  LYS n 
1 116  ARG n 
1 117  MET n 
1 118  PRO n 
1 119  ILE n 
1 120  THR n 
1 121  TYR n 
1 122  ASP n 
1 123  ASN n 
1 124  GLY n 
1 125  PHE n 
1 126  LEU n 
1 127  PHE n 
1 128  ILE n 
1 129  HIS n 
1 130  THR n 
1 131  ASP n 
1 132  LYS n 
1 133  PRO n 
1 134  VAL n 
1 135  TYR n 
1 136  THR n 
1 137  PRO n 
1 138  ASP n 
1 139  GLN n 
1 140  SER n 
1 141  VAL n 
1 142  LYS n 
1 143  VAL n 
1 144  ARG n 
1 145  VAL n 
1 146  TYR n 
1 147  SER n 
1 148  LEU n 
1 149  ASN n 
1 150  ASP n 
1 151  ASP n 
1 152  LEU n 
1 153  LYS n 
1 154  PRO n 
1 155  ALA n 
1 156  LYS n 
1 157  ARG n 
1 158  GLU n 
1 159  THR n 
1 160  VAL n 
1 161  LEU n 
1 162  THR n 
1 163  PHE n 
1 164  ILE n 
1 165  ASP n 
1 166  PRO n 
1 167  GLU n 
1 168  GLY n 
1 169  SER n 
1 170  GLU n 
1 171  VAL n 
1 172  ASP n 
1 173  MET n 
1 174  VAL n 
1 175  GLU n 
1 176  GLU n 
1 177  ILE n 
1 178  ASP n 
1 179  HIS n 
1 180  ILE n 
1 181  GLY n 
1 182  ILE n 
1 183  ILE n 
1 184  SER n 
1 185  PHE n 
1 186  PRO n 
1 187  ASP n 
1 188  PHE n 
1 189  LYS n 
1 190  ILE n 
1 191  PRO n 
1 192  SER n 
1 193  ASN n 
1 194  PRO n 
1 195  ARG n 
1 196  TYR n 
1 197  GLY n 
1 198  MET n 
1 199  TRP n 
1 200  THR n 
1 201  ILE n 
1 202  LYS n 
1 203  ALA n 
1 204  LYS n 
1 205  TYR n 
1 206  LYS n 
1 207  GLU n 
1 208  ASP n 
1 209  PHE n 
1 210  SER n 
1 211  THR n 
1 212  THR n 
1 213  GLY n 
1 214  THR n 
1 215  ALA n 
1 216  TYR n 
1 217  PHE n 
1 218  GLU n 
1 219  VAL n 
1 220  LYS n 
1 221  GLU n 
1 222  TYR n 
1 223  VAL n 
1 224  LEU n 
1 225  PRO n 
1 226  HIS n 
1 227  PHE n 
1 228  SER n 
1 229  VAL n 
1 230  SER n 
1 231  ILE n 
1 232  GLU n 
1 233  PRO n 
1 234  GLU n 
1 235  TYR n 
1 236  ASN n 
1 237  PHE n 
1 238  ILE n 
1 239  GLY n 
1 240  TYR n 
1 241  LYS n 
1 242  ASN n 
1 243  PHE n 
1 244  LYS n 
1 245  ASN n 
1 246  PHE n 
1 247  GLU n 
1 248  ILE n 
1 249  THR n 
1 250  ILE n 
1 251  LYS n 
1 252  ALA n 
1 253  ARG n 
1 254  TYR n 
1 255  PHE n 
1 256  TYR n 
1 257  ASN n 
1 258  LYS n 
1 259  VAL n 
1 260  VAL n 
1 261  THR n 
1 262  GLU n 
1 263  ALA n 
1 264  ASP n 
1 265  VAL n 
1 266  TYR n 
1 267  ILE n 
1 268  THR n 
1 269  PHE n 
1 270  GLY n 
1 271  ILE n 
1 272  ARG n 
1 273  GLU n 
1 274  ASP n 
1 275  LEU n 
1 276  LYS n 
1 277  ASP n 
1 278  ASP n 
1 279  GLN n 
1 280  LYS n 
1 281  GLU n 
1 282  MET n 
1 283  MET n 
1 284  GLN n 
1 285  THR n 
1 286  ALA n 
1 287  MET n 
1 288  GLN n 
1 289  ASN n 
1 290  THR n 
1 291  MET n 
1 292  LEU n 
1 293  ILE n 
1 294  ASN n 
1 295  GLY n 
1 296  ILE n 
1 297  ALA n 
1 298  GLN n 
1 299  VAL n 
1 300  THR n 
1 301  PHE n 
1 302  ASP n 
1 303  SER n 
1 304  GLU n 
1 305  THR n 
1 306  ALA n 
1 307  VAL n 
1 308  LYS n 
1 309  GLU n 
1 310  LEU n 
1 311  SER n 
1 312  TYR n 
1 313  TYR n 
1 314  SER n 
1 315  LEU n 
1 316  GLU n 
1 317  ASP n 
1 318  LEU n 
1 319  ASN n 
1 320  ASN n 
1 321  LYS n 
1 322  TYR n 
1 323  LEU n 
1 324  TYR n 
1 325  ILE n 
1 326  ALA n 
1 327  VAL n 
1 328  THR n 
1 329  VAL n 
1 330  ILE n 
1 331  GLU n 
1 332  SER n 
1 333  THR n 
1 334  GLY n 
1 335  GLY n 
1 336  PHE n 
1 337  SER n 
1 338  GLU n 
1 339  GLU n 
1 340  ALA n 
1 341  GLU n 
1 342  ILE n 
1 343  PRO n 
1 344  GLY n 
1 345  ILE n 
1 346  LYS n 
1 347  TYR n 
1 348  VAL n 
1 349  LEU n 
1 350  SER n 
1 351  PRO n 
1 352  TYR n 
1 353  LYS n 
1 354  LEU n 
1 355  ASN n 
1 356  LEU n 
1 357  VAL n 
1 358  ALA n 
1 359  THR n 
1 360  PRO n 
1 361  LEU n 
1 362  PHE n 
1 363  LEU n 
1 364  LYS n 
1 365  PRO n 
1 366  GLY n 
1 367  ILE n 
1 368  PRO n 
1 369  TYR n 
1 370  PRO n 
1 371  ILE n 
1 372  LYS n 
1 373  VAL n 
1 374  GLN n 
1 375  VAL n 
1 376  LYS n 
1 377  ASP n 
1 378  SER n 
1 379  LEU n 
1 380  ASP n 
1 381  GLN n 
1 382  LEU n 
1 383  VAL n 
1 384  GLY n 
1 385  GLY n 
1 386  VAL n 
1 387  PRO n 
1 388  VAL n 
1 389  THR n 
1 390  LEU n 
1 391  ASN n 
1 392  ALA n 
1 393  GLN n 
1 394  THR n 
1 395  ILE n 
1 396  ASP n 
1 397  VAL n 
1 398  ASN n 
1 399  GLN n 
1 400  GLU n 
1 401  THR n 
1 402  SER n 
1 403  ASP n 
1 404  LEU n 
1 405  ASP n 
1 406  PRO n 
1 407  SER n 
1 408  LYS n 
1 409  SER n 
1 410  VAL n 
1 411  THR n 
1 412  ARG n 
1 413  VAL n 
1 414  ASP n 
1 415  ASP n 
1 416  GLY n 
1 417  VAL n 
1 418  ALA n 
1 419  SER n 
1 420  PHE n 
1 421  VAL n 
1 422  LEU n 
1 423  ASN n 
1 424  LEU n 
1 425  PRO n 
1 426  SER n 
1 427  GLY n 
1 428  VAL n 
1 429  THR n 
1 430  VAL n 
1 431  LEU n 
1 432  GLU n 
1 433  PHE n 
1 434  ASN n 
1 435  VAL n 
1 436  LYS n 
1 437  THR n 
1 438  ASP n 
1 439  ALA n 
1 440  PRO n 
1 441  ASP n 
1 442  LEU n 
1 443  PRO n 
1 444  GLU n 
1 445  GLU n 
1 446  ASN n 
1 447  GLN n 
1 448  ALA n 
1 449  ARG n 
1 450  GLU n 
1 451  GLY n 
1 452  TYR n 
1 453  ARG n 
1 454  ALA n 
1 455  ILE n 
1 456  ALA n 
1 457  TYR n 
1 458  SER n 
1 459  SER n 
1 460  LEU n 
1 461  SER n 
1 462  GLN n 
1 463  SER n 
1 464  TYR n 
1 465  LEU n 
1 466  TYR n 
1 467  ILE n 
1 468  ASP n 
1 469  TRP n 
1 470  THR n 
1 471  ASP n 
1 472  ASN n 
1 473  HIS n 
1 474  LYS n 
1 475  ALA n 
1 476  LEU n 
1 477  LEU n 
1 478  VAL n 
1 479  GLY n 
1 480  GLU n 
1 481  HIS n 
1 482  LEU n 
1 483  ASN n 
1 484  ILE n 
1 485  ILE n 
1 486  VAL n 
1 487  THR n 
1 488  PRO n 
1 489  LYS n 
1 490  SER n 
1 491  PRO n 
1 492  TYR n 
1 493  ILE n 
1 494  ASP n 
1 495  LYS n 
1 496  ILE n 
1 497  THR n 
1 498  HIS n 
1 499  TYR n 
1 500  ASN n 
1 501  TYR n 
1 502  LEU n 
1 503  ILE n 
1 504  LEU n 
1 505  SER n 
1 506  LYS n 
1 507  GLY n 
1 508  LYS n 
1 509  ILE n 
1 510  ILE n 
1 511  HIS n 
1 512  PHE n 
1 513  GLY n 
1 514  THR n 
1 515  ARG n 
1 516  GLU n 
1 517  LYS n 
1 518  PHE n 
1 519  SER n 
1 520  ASP n 
1 521  ALA n 
1 522  SER n 
1 523  TYR n 
1 524  GLN n 
1 525  SER n 
1 526  ILE n 
1 527  ASN n 
1 528  ILE n 
1 529  PRO n 
1 530  VAL n 
1 531  THR n 
1 532  GLN n 
1 533  ASN n 
1 534  MET n 
1 535  VAL n 
1 536  PRO n 
1 537  SER n 
1 538  SER n 
1 539  ARG n 
1 540  LEU n 
1 541  LEU n 
1 542  VAL n 
1 543  TYR n 
1 544  TYR n 
1 545  ILE n 
1 546  VAL n 
1 547  THR n 
1 548  GLY n 
1 549  GLU n 
1 550  GLN n 
1 551  THR n 
1 552  ALA n 
1 553  GLU n 
1 554  LEU n 
1 555  VAL n 
1 556  SER n 
1 557  ASP n 
1 558  SER n 
1 559  VAL n 
1 560  TRP n 
1 561  LEU n 
1 562  ASN n 
1 563  ILE n 
1 564  GLU n 
1 565  GLU n 
1 566  LYS n 
1 567  CYS n 
1 568  GLY n 
1 569  ASN n 
1 570  GLN n 
1 571  LEU n 
1 572  GLN n 
1 573  VAL n 
1 574  HIS n 
1 575  LEU n 
1 576  SER n 
1 577  PRO n 
1 578  ASP n 
1 579  ALA n 
1 580  ASP n 
1 581  ALA n 
1 582  TYR n 
1 583  SER n 
1 584  PRO n 
1 585  GLY n 
1 586  GLN n 
1 587  THR n 
1 588  VAL n 
1 589  SER n 
1 590  LEU n 
1 591  ASN n 
1 592  MET n 
1 593  ALA n 
1 594  THR n 
1 595  GLY n 
1 596  MET n 
1 597  ASP n 
1 598  SER n 
1 599  TRP n 
1 600  VAL n 
1 601  ALA n 
1 602  LEU n 
1 603  ALA n 
1 604  ALA n 
1 605  VAL n 
1 606  ASP n 
1 607  SER n 
1 608  ALA n 
1 609  VAL n 
1 610  TYR n 
1 611  GLY n 
1 612  VAL n 
1 613  GLN n 
1 614  ARG n 
1 615  GLY n 
1 616  ALA n 
1 617  LYS n 
1 618  LYS n 
1 619  PRO n 
1 620  LEU n 
1 621  GLU n 
1 622  ARG n 
1 623  VAL n 
1 624  PHE n 
1 625  GLN n 
1 626  PHE n 
1 627  LEU n 
1 628  GLU n 
1 629  LYS n 
1 630  SER n 
1 631  ASP n 
1 632  LEU n 
1 633  GLY n 
1 634  CYS n 
1 635  GLY n 
1 636  ALA n 
1 637  GLY n 
1 638  GLY n 
1 639  GLY n 
1 640  LEU n 
1 641  ASN n 
1 642  ASN n 
1 643  ALA n 
1 644  ASN n 
1 645  VAL n 
1 646  PHE n 
1 647  HIS n 
1 648  LEU n 
1 649  ALA n 
1 650  GLY n 
1 651  LEU n 
1 652  THR n 
1 653  PHE n 
1 654  LEU n 
1 655  THR n 
1 656  ASN n 
1 657  ALA n 
1 658  ASN n 
1 659  ALA n 
1 660  ASP n 
1 661  ASP n 
1 662  SER n 
1 663  GLN n 
1 664  GLU n 
1 665  ASN n 
1 666  ASP n 
1 667  GLU n 
1 668  PRO n 
1 669  CYS n 
1 670  LYS n 
1 671  GLU n 
1 672  ILE n 
1 673  LEU n 
1 674  ARG n 
1 675  PRO n 
1 676  ARG n 
1 677  ARG n 
1 678  THR n 
1 679  LEU n 
1 680  GLN n 
1 681  LYS n 
1 682  LYS n 
1 683  ILE n 
1 684  GLU n 
1 685  GLU n 
1 686  ILE n 
1 687  ALA n 
1 688  ALA n 
1 689  LYS n 
1 690  TYR n 
1 691  LYS n 
1 692  HIS n 
1 693  SER n 
1 694  VAL n 
1 695  VAL n 
1 696  LYS n 
1 697  LYS n 
1 698  CYS n 
1 699  CYS n 
1 700  TYR n 
1 701  ASP n 
1 702  GLY n 
1 703  ALA n 
1 704  CYS n 
1 705  VAL n 
1 706  ASN n 
1 707  ASN n 
1 708  ASP n 
1 709  GLU n 
1 710  THR n 
1 711  CYS n 
1 712  GLU n 
1 713  GLN n 
1 714  ARG n 
1 715  ALA n 
1 716  ALA n 
1 717  ARG n 
1 718  ILE n 
1 719  SER n 
1 720  LEU n 
1 721  GLY n 
1 722  PRO n 
1 723  ARG n 
1 724  CYS n 
1 725  ILE n 
1 726  LYS n 
1 727  ALA n 
1 728  PHE n 
1 729  THR n 
1 730  GLU n 
1 731  CYS n 
1 732  CYS n 
1 733  VAL n 
1 734  VAL n 
1 735  ALA n 
1 736  SER n 
1 737  GLN n 
1 738  LEU n 
1 739  ARG n 
1 740  ALA n 
1 741  ASN n 
1 742  ILE n 
1 743  SER n 
1 744  HIS n 
1 745  LYS n 
1 746  ASP n 
1 747  MET n 
1 748  GLN n 
1 749  LEU n 
1 750  GLY n 
1 751  ARG n 
1 752  LEU n 
1 753  HIS n 
1 754  MET n 
1 755  LYS n 
1 756  THR n 
1 757  LEU n 
1 758  LEU n 
1 759  PRO n 
1 760  VAL n 
1 761  SER n 
1 762  LYS n 
1 763  PRO n 
1 764  GLU n 
1 765  ILE n 
1 766  ARG n 
1 767  SER n 
1 768  TYR n 
1 769  PHE n 
1 770  PRO n 
1 771  GLU n 
1 772  SER n 
1 773  TRP n 
1 774  LEU n 
1 775  TRP n 
1 776  GLU n 
1 777  VAL n 
1 778  HIS n 
1 779  LEU n 
1 780  VAL n 
1 781  PRO n 
1 782  ARG n 
1 783  ARG n 
1 784  LYS n 
1 785  GLN n 
1 786  LEU n 
1 787  GLN n 
1 788  PHE n 
1 789  ALA n 
1 790  LEU n 
1 791  PRO n 
1 792  ASP n 
1 793  SER n 
1 794  LEU n 
1 795  THR n 
1 796  THR n 
1 797  TRP n 
1 798  GLU n 
1 799  ILE n 
1 800  GLN n 
1 801  GLY n 
1 802  ILE n 
1 803  GLY n 
1 804  ILE n 
1 805  SER n 
1 806  ASN n 
1 807  THR n 
1 808  GLY n 
1 809  ILE n 
1 810  CYS n 
1 811  VAL n 
1 812  ALA n 
1 813  ASP n 
1 814  THR n 
1 815  VAL n 
1 816  LYS n 
1 817  ALA n 
1 818  LYS n 
1 819  VAL n 
1 820  PHE n 
1 821  LYS n 
1 822  ASP n 
1 823  VAL n 
1 824  PHE n 
1 825  LEU n 
1 826  GLU n 
1 827  MET n 
1 828  ASN n 
1 829  ILE n 
1 830  PRO n 
1 831  TYR n 
1 832  SER n 
1 833  VAL n 
1 834  VAL n 
1 835  ARG n 
1 836  GLY n 
1 837  GLU n 
1 838  GLN n 
1 839  ILE n 
1 840  GLN n 
1 841  LEU n 
1 842  LYS n 
1 843  GLY n 
1 844  THR n 
1 845  VAL n 
1 846  TYR n 
1 847  ASN n 
1 848  TYR n 
1 849  ARG n 
1 850  THR n 
1 851  SER n 
1 852  GLY n 
1 853  MET n 
1 854  GLN n 
1 855  PHE n 
1 856  CYS n 
1 857  VAL n 
1 858  LYS n 
1 859  MET n 
1 860  SER n 
1 861  ALA n 
1 862  VAL n 
1 863  GLU n 
1 864  GLY n 
1 865  ILE n 
1 866  CYS n 
1 867  THR n 
1 868  SER n 
1 869  GLU n 
1 870  SER n 
1 871  PRO n 
1 872  VAL n 
1 873  ILE n 
1 874  ASP n 
1 875  HIS n 
1 876  GLN n 
1 877  GLY n 
1 878  THR n 
1 879  LYS n 
1 880  SER n 
1 881  SER n 
1 882  LYS n 
1 883  CYS n 
1 884  VAL n 
1 885  ARG n 
1 886  GLN n 
1 887  LYS n 
1 888  VAL n 
1 889  GLU n 
1 890  GLY n 
1 891  SER n 
1 892  SER n 
1 893  SER n 
1 894  HIS n 
1 895  LEU n 
1 896  VAL n 
1 897  THR n 
1 898  PHE n 
1 899  THR n 
1 900  VAL n 
1 901  LEU n 
1 902  PRO n 
1 903  LEU n 
1 904  GLU n 
1 905  ILE n 
1 906  GLY n 
1 907  LEU n 
1 908  HIS n 
1 909  ASN n 
1 910  ILE n 
1 911  ASN n 
1 912  PHE n 
1 913  SER n 
1 914  LEU n 
1 915  GLU n 
1 916  THR n 
1 917  TRP n 
1 918  PHE n 
1 919  GLY n 
1 920  LYS n 
1 921  GLU n 
1 922  ILE n 
1 923  LEU n 
1 924  VAL n 
1 925  LYS n 
1 926  THR n 
1 927  LEU n 
1 928  ARG n 
1 929  VAL n 
1 930  VAL n 
1 931  PRO n 
1 932  GLU n 
1 933  GLY n 
1 934  VAL n 
1 935  LYS n 
1 936  ARG n 
1 937  GLU n 
1 938  SER n 
1 939  TYR n 
1 940  SER n 
1 941  GLY n 
1 942  VAL n 
1 943  THR n 
1 944  LEU n 
1 945  ASP n 
1 946  PRO n 
1 947  ARG n 
1 948  GLY n 
1 949  ILE n 
1 950  TYR n 
1 951  GLY n 
1 952  THR n 
1 953  ILE n 
1 954  SER n 
1 955  ARG n 
1 956  ARG n 
1 957  LYS n 
1 958  GLU n 
1 959  PHE n 
1 960  PRO n 
1 961  TYR n 
1 962  ARG n 
1 963  ILE n 
1 964  PRO n 
1 965  LEU n 
1 966  ASP n 
1 967  LEU n 
1 968  VAL n 
1 969  PRO n 
1 970  LYS n 
1 971  THR n 
1 972  GLU n 
1 973  ILE n 
1 974  LYS n 
1 975  ARG n 
1 976  ILE n 
1 977  LEU n 
1 978  SER n 
1 979  VAL n 
1 980  LYS n 
1 981  GLY n 
1 982  LEU n 
1 983  LEU n 
1 984  VAL n 
1 985  GLY n 
1 986  GLU n 
1 987  ILE n 
1 988  LEU n 
1 989  SER n 
1 990  ALA n 
1 991  VAL n 
1 992  LEU n 
1 993  SER n 
1 994  GLN n 
1 995  GLU n 
1 996  GLY n 
1 997  ILE n 
1 998  ASN n 
1 999  ILE n 
1 1000 LEU n 
1 1001 THR n 
1 1002 HIS n 
1 1003 LEU n 
1 1004 PRO n 
1 1005 LYS n 
1 1006 GLY n 
1 1007 SER n 
1 1008 ALA n 
1 1009 GLU n 
1 1010 ALA n 
1 1011 GLU n 
1 1012 LEU n 
1 1013 MET n 
1 1014 SER n 
1 1015 VAL n 
1 1016 VAL n 
1 1017 PRO n 
1 1018 VAL n 
1 1019 PHE n 
1 1020 TYR n 
1 1021 VAL n 
1 1022 PHE n 
1 1023 HIS n 
1 1024 TYR n 
1 1025 LEU n 
1 1026 GLU n 
1 1027 THR n 
1 1028 GLY n 
1 1029 ASN n 
1 1030 HIS n 
1 1031 TRP n 
1 1032 ASN n 
1 1033 ILE n 
1 1034 PHE n 
1 1035 HIS n 
1 1036 SER n 
1 1037 ASP n 
1 1038 PRO n 
1 1039 LEU n 
1 1040 ILE n 
1 1041 GLU n 
1 1042 LYS n 
1 1043 GLN n 
1 1044 LYS n 
1 1045 LEU n 
1 1046 LYS n 
1 1047 LYS n 
1 1048 LYS n 
1 1049 LEU n 
1 1050 LYS n 
1 1051 GLU n 
1 1052 GLY n 
1 1053 MET n 
1 1054 LEU n 
1 1055 SER n 
1 1056 ILE n 
1 1057 MET n 
1 1058 SER n 
1 1059 TYR n 
1 1060 ARG n 
1 1061 ASN n 
1 1062 ALA n 
1 1063 ASP n 
1 1064 TYR n 
1 1065 SER n 
1 1066 TYR n 
1 1067 SER n 
1 1068 VAL n 
1 1069 TRP n 
1 1070 LYS n 
1 1071 GLY n 
1 1072 GLY n 
1 1073 SER n 
1 1074 ALA n 
1 1075 SER n 
1 1076 THR n 
1 1077 TRP n 
1 1078 LEU n 
1 1079 THR n 
1 1080 ALA n 
1 1081 PHE n 
1 1082 ALA n 
1 1083 LEU n 
1 1084 ARG n 
1 1085 VAL n 
1 1086 LEU n 
1 1087 GLY n 
1 1088 GLN n 
1 1089 VAL n 
1 1090 ASN n 
1 1091 LYS n 
1 1092 TYR n 
1 1093 VAL n 
1 1094 GLU n 
1 1095 GLN n 
1 1096 ASN n 
1 1097 GLN n 
1 1098 ASN n 
1 1099 SER n 
1 1100 ILE n 
1 1101 CYS n 
1 1102 ASN n 
1 1103 SER n 
1 1104 LEU n 
1 1105 LEU n 
1 1106 TRP n 
1 1107 LEU n 
1 1108 VAL n 
1 1109 GLU n 
1 1110 ASN n 
1 1111 TYR n 
1 1112 GLN n 
1 1113 LEU n 
1 1114 ASP n 
1 1115 ASN n 
1 1116 GLY n 
1 1117 SER n 
1 1118 PHE n 
1 1119 LYS n 
1 1120 GLU n 
1 1121 ASN n 
1 1122 SER n 
1 1123 GLN n 
1 1124 TYR n 
1 1125 GLN n 
1 1126 PRO n 
1 1127 ILE n 
1 1128 LYS n 
1 1129 LEU n 
1 1130 GLN n 
1 1131 GLY n 
1 1132 THR n 
1 1133 LEU n 
1 1134 PRO n 
1 1135 VAL n 
1 1136 GLU n 
1 1137 ALA n 
1 1138 ARG n 
1 1139 GLU n 
1 1140 ASN n 
1 1141 SER n 
1 1142 LEU n 
1 1143 TYR n 
1 1144 LEU n 
1 1145 THR n 
1 1146 ALA n 
1 1147 PHE n 
1 1148 THR n 
1 1149 VAL n 
1 1150 ILE n 
1 1151 GLY n 
1 1152 ILE n 
1 1153 ARG n 
1 1154 LYS n 
1 1155 ALA n 
1 1156 PHE n 
1 1157 ASP n 
1 1158 ILE n 
1 1159 CYS n 
1 1160 PRO n 
1 1161 LEU n 
1 1162 VAL n 
1 1163 LYS n 
1 1164 ILE n 
1 1165 ASP n 
1 1166 THR n 
1 1167 ALA n 
1 1168 LEU n 
1 1169 ILE n 
1 1170 LYS n 
1 1171 ALA n 
1 1172 ASP n 
1 1173 ASN n 
1 1174 PHE n 
1 1175 LEU n 
1 1176 LEU n 
1 1177 GLU n 
1 1178 ASN n 
1 1179 THR n 
1 1180 LEU n 
1 1181 PRO n 
1 1182 ALA n 
1 1183 GLN n 
1 1184 SER n 
1 1185 THR n 
1 1186 PHE n 
1 1187 THR n 
1 1188 LEU n 
1 1189 ALA n 
1 1190 ILE n 
1 1191 SER n 
1 1192 ALA n 
1 1193 TYR n 
1 1194 ALA n 
1 1195 LEU n 
1 1196 SER n 
1 1197 LEU n 
1 1198 GLY n 
1 1199 ASP n 
1 1200 LYS n 
1 1201 THR n 
1 1202 HIS n 
1 1203 PRO n 
1 1204 GLN n 
1 1205 PHE n 
1 1206 ARG n 
1 1207 SER n 
1 1208 ILE n 
1 1209 VAL n 
1 1210 SER n 
1 1211 ALA n 
1 1212 LEU n 
1 1213 LYS n 
1 1214 ARG n 
1 1215 GLU n 
1 1216 ALA n 
1 1217 LEU n 
1 1218 VAL n 
1 1219 LYS n 
1 1220 GLY n 
1 1221 ASN n 
1 1222 PRO n 
1 1223 PRO n 
1 1224 ILE n 
1 1225 TYR n 
1 1226 ARG n 
1 1227 PHE n 
1 1228 TRP n 
1 1229 LYS n 
1 1230 ASP n 
1 1231 ASN n 
1 1232 LEU n 
1 1233 GLN n 
1 1234 HIS n 
1 1235 LYS n 
1 1236 ASP n 
1 1237 SER n 
1 1238 SER n 
1 1239 VAL n 
1 1240 PRO n 
1 1241 ASN n 
1 1242 THR n 
1 1243 GLY n 
1 1244 THR n 
1 1245 ALA n 
1 1246 ARG n 
1 1247 MET n 
1 1248 VAL n 
1 1249 GLU n 
1 1250 THR n 
1 1251 THR n 
1 1252 ALA n 
1 1253 TYR n 
1 1254 ALA n 
1 1255 LEU n 
1 1256 LEU n 
1 1257 THR n 
1 1258 SER n 
1 1259 LEU n 
1 1260 ASN n 
1 1261 LEU n 
1 1262 LYS n 
1 1263 ASP n 
1 1264 ILE n 
1 1265 ASN n 
1 1266 TYR n 
1 1267 VAL n 
1 1268 ASN n 
1 1269 PRO n 
1 1270 VAL n 
1 1271 ILE n 
1 1272 LYS n 
1 1273 TRP n 
1 1274 LEU n 
1 1275 SER n 
1 1276 GLU n 
1 1277 GLU n 
1 1278 GLN n 
1 1279 ARG n 
1 1280 TYR n 
1 1281 GLY n 
1 1282 GLY n 
1 1283 GLY n 
1 1284 PHE n 
1 1285 TYR n 
1 1286 SER n 
1 1287 THR n 
1 1288 GLN n 
1 1289 ASP n 
1 1290 THR n 
1 1291 ILE n 
1 1292 ASN n 
1 1293 ALA n 
1 1294 ILE n 
1 1295 GLU n 
1 1296 GLY n 
1 1297 LEU n 
1 1298 THR n 
1 1299 GLU n 
1 1300 TYR n 
1 1301 SER n 
1 1302 LEU n 
1 1303 LEU n 
1 1304 VAL n 
1 1305 LYS n 
1 1306 GLN n 
1 1307 LEU n 
1 1308 ARG n 
1 1309 LEU n 
1 1310 SER n 
1 1311 MET n 
1 1312 ASP n 
1 1313 ILE n 
1 1314 ASP n 
1 1315 VAL n 
1 1316 SER n 
1 1317 TYR n 
1 1318 LYS n 
1 1319 HIS n 
1 1320 LYS n 
1 1321 GLY n 
1 1322 ALA n 
1 1323 LEU n 
1 1324 HIS n 
1 1325 ASN n 
1 1326 TYR n 
1 1327 LYS n 
1 1328 MET n 
1 1329 THR n 
1 1330 ASP n 
1 1331 LYS n 
1 1332 ASN n 
1 1333 PHE n 
1 1334 LEU n 
1 1335 GLY n 
1 1336 ARG n 
1 1337 PRO n 
1 1338 VAL n 
1 1339 GLU n 
1 1340 VAL n 
1 1341 LEU n 
1 1342 LEU n 
1 1343 ASN n 
1 1344 ASP n 
1 1345 ASP n 
1 1346 LEU n 
1 1347 ILE n 
1 1348 VAL n 
1 1349 SER n 
1 1350 THR n 
1 1351 GLY n 
1 1352 PHE n 
1 1353 GLY n 
1 1354 SER n 
1 1355 GLY n 
1 1356 LEU n 
1 1357 ALA n 
1 1358 THR n 
1 1359 VAL n 
1 1360 HIS n 
1 1361 VAL n 
1 1362 THR n 
1 1363 THR n 
1 1364 VAL n 
1 1365 VAL n 
1 1366 HIS n 
1 1367 LYS n 
1 1368 THR n 
1 1369 SER n 
1 1370 THR n 
1 1371 SER n 
1 1372 GLU n 
1 1373 GLU n 
1 1374 VAL n 
1 1375 CYS n 
1 1376 SER n 
1 1377 PHE n 
1 1378 TYR n 
1 1379 LEU n 
1 1380 LYS n 
1 1381 ILE n 
1 1382 ASP n 
1 1383 THR n 
1 1384 GLN n 
1 1385 ASP n 
1 1386 ILE n 
1 1387 GLU n 
1 1388 ALA n 
1 1389 SER n 
1 1390 HIS n 
1 1391 TYR n 
1 1392 ARG n 
1 1393 GLY n 
1 1394 TYR n 
1 1395 GLY n 
1 1396 ASN n 
1 1397 SER n 
1 1398 ASP n 
1 1399 TYR n 
1 1400 LYS n 
1 1401 ARG n 
1 1402 ILE n 
1 1403 VAL n 
1 1404 ALA n 
1 1405 CYS n 
1 1406 ALA n 
1 1407 SER n 
1 1408 TYR n 
1 1409 LYS n 
1 1410 PRO n 
1 1411 SER n 
1 1412 ARG n 
1 1413 GLU n 
1 1414 GLU n 
1 1415 SER n 
1 1416 SER n 
1 1417 SER n 
1 1418 GLY n 
1 1419 SER n 
1 1420 SER n 
1 1421 HIS n 
1 1422 ALA n 
1 1423 VAL n 
1 1424 MET n 
1 1425 ASP n 
1 1426 ILE n 
1 1427 SER n 
1 1428 LEU n 
1 1429 PRO n 
1 1430 THR n 
1 1431 GLY n 
1 1432 ILE n 
1 1433 SER n 
1 1434 ALA n 
1 1435 ASN n 
1 1436 GLU n 
1 1437 GLU n 
1 1438 ASP n 
1 1439 LEU n 
1 1440 LYS n 
1 1441 ALA n 
1 1442 LEU n 
1 1443 VAL n 
1 1444 GLU n 
1 1445 GLY n 
1 1446 VAL n 
1 1447 ASP n 
1 1448 GLN n 
1 1449 LEU n 
1 1450 PHE n 
1 1451 THR n 
1 1452 ASP n 
1 1453 TYR n 
1 1454 GLN n 
1 1455 ILE n 
1 1456 LYS n 
1 1457 ASP n 
1 1458 GLY n 
1 1459 HIS n 
1 1460 VAL n 
1 1461 ILE n 
1 1462 LEU n 
1 1463 GLN n 
1 1464 LEU n 
1 1465 ASN n 
1 1466 SER n 
1 1467 ILE n 
1 1468 PRO n 
1 1469 SER n 
1 1470 SER n 
1 1471 ASP n 
1 1472 PHE n 
1 1473 LEU n 
1 1474 CYS n 
1 1475 VAL n 
1 1476 ARG n 
1 1477 PHE n 
1 1478 ARG n 
1 1479 ILE n 
1 1480 PHE n 
1 1481 GLU n 
1 1482 LEU n 
1 1483 PHE n 
1 1484 GLU n 
1 1485 VAL n 
1 1486 GLY n 
1 1487 PHE n 
1 1488 LEU n 
1 1489 SER n 
1 1490 PRO n 
1 1491 ALA n 
1 1492 THR n 
1 1493 PHE n 
1 1494 THR n 
1 1495 VAL n 
1 1496 TYR n 
1 1497 GLU n 
1 1498 TYR n 
1 1499 HIS n 
1 1500 ARG n 
1 1501 PRO n 
1 1502 ASP n 
1 1503 LYS n 
1 1504 GLN n 
1 1505 CYS n 
1 1506 THR n 
1 1507 MET n 
1 1508 PHE n 
1 1509 TYR n 
1 1510 SER n 
1 1511 THR n 
1 1512 SER n 
1 1513 ASN n 
1 1514 ILE n 
1 1515 LYS n 
1 1516 ILE n 
1 1517 GLN n 
1 1518 LYS n 
1 1519 VAL n 
1 1520 CYS n 
1 1521 GLU n 
1 1522 GLY n 
1 1523 ALA n 
1 1524 ALA n 
1 1525 CYS n 
1 1526 LYS n 
1 1527 CYS n 
1 1528 VAL n 
1 1529 GLU n 
1 1530 ALA n 
1 1531 ASP n 
1 1532 CYS n 
1 1533 GLY n 
1 1534 GLN n 
1 1535 MET n 
1 1536 GLN n 
1 1537 GLU n 
1 1538 GLU n 
1 1539 LEU n 
1 1540 ASP n 
1 1541 LEU n 
1 1542 THR n 
1 1543 ILE n 
1 1544 SER n 
1 1545 ALA n 
1 1546 GLU n 
1 1547 THR n 
1 1548 ARG n 
1 1549 LYS n 
1 1550 GLN n 
1 1551 THR n 
1 1552 ALA n 
1 1553 CYS n 
1 1554 LYS n 
1 1555 PRO n 
1 1556 GLU n 
1 1557 ILE n 
1 1558 ALA n 
1 1559 TYR n 
1 1560 ALA n 
1 1561 TYR n 
1 1562 LYS n 
1 1563 VAL n 
1 1564 SER n 
1 1565 ILE n 
1 1566 THR n 
1 1567 SER n 
1 1568 ILE n 
1 1569 THR n 
1 1570 VAL n 
1 1571 GLU n 
1 1572 ASN n 
1 1573 VAL n 
1 1574 PHE n 
1 1575 VAL n 
1 1576 LYS n 
1 1577 TYR n 
1 1578 LYS n 
1 1579 ALA n 
1 1580 THR n 
1 1581 LEU n 
1 1582 LEU n 
1 1583 ASP n 
1 1584 ILE n 
1 1585 TYR n 
1 1586 LYS n 
1 1587 THR n 
1 1588 GLY n 
1 1589 GLU n 
1 1590 ALA n 
1 1591 VAL n 
1 1592 ALA n 
1 1593 GLU n 
1 1594 LYS n 
1 1595 ASP n 
1 1596 SER n 
1 1597 GLU n 
1 1598 ILE n 
1 1599 THR n 
1 1600 PHE n 
1 1601 ILE n 
1 1602 LYS n 
1 1603 LYS n 
1 1604 VAL n 
1 1605 THR n 
1 1606 CYS n 
1 1607 THR n 
1 1608 ASN n 
1 1609 ALA n 
1 1610 GLU n 
1 1611 LEU n 
1 1612 VAL n 
1 1613 LYS n 
1 1614 GLY n 
1 1615 ARG n 
1 1616 GLN n 
1 1617 TYR n 
1 1618 LEU n 
1 1619 ILE n 
1 1620 MET n 
1 1621 GLY n 
1 1622 LYS n 
1 1623 GLU n 
1 1624 ALA n 
1 1625 LEU n 
1 1626 GLN n 
1 1627 ILE n 
1 1628 LYS n 
1 1629 TYR n 
1 1630 ASN n 
1 1631 PHE n 
1 1632 SER n 
1 1633 PHE n 
1 1634 ARG n 
1 1635 TYR n 
1 1636 ILE n 
1 1637 TYR n 
1 1638 PRO n 
1 1639 LEU n 
1 1640 ASP n 
1 1641 SER n 
1 1642 LEU n 
1 1643 THR n 
1 1644 TRP n 
1 1645 ILE n 
1 1646 GLU n 
1 1647 TYR n 
1 1648 TRP n 
1 1649 PRO n 
1 1650 ARG n 
1 1651 ASP n 
1 1652 THR n 
1 1653 THR n 
1 1654 CYS n 
1 1655 SER n 
1 1656 SER n 
1 1657 CYS n 
1 1658 GLN n 
1 1659 ALA n 
1 1660 PHE n 
1 1661 LEU n 
1 1662 ALA n 
1 1663 ASN n 
1 1664 LEU n 
1 1665 ASP n 
1 1666 GLU n 
1 1667 PHE n 
1 1668 ALA n 
1 1669 GLU n 
1 1670 ASP n 
1 1671 ILE n 
1 1672 PHE n 
1 1673 LEU n 
1 1674 ASN n 
1 1675 GLY n 
1 1676 CYS n 
2 1    MET n 
2 2    LYS n 
2 3    LEU n 
2 4    LYS n 
2 5    THR n 
2 6    LEU n 
2 7    ALA n 
2 8    LYS n 
2 9    ALA n 
2 10   THR n 
2 11   LEU n 
2 12   ALA n 
2 13   LEU n 
2 14   GLY n 
2 15   LEU n 
2 16   LEU n 
2 17   THR n 
2 18   THR n 
2 19   GLY n 
2 20   VAL n 
2 21   ILE n 
2 22   THR n 
2 23   SER n 
2 24   GLU n 
2 25   GLY n 
2 26   GLN n 
2 27   ALA n 
2 28   VAL n 
2 29   GLN n 
2 30   ALA n 
2 31   ALA n 
2 32   GLU n 
2 33   LYS n 
2 34   GLN n 
2 35   GLY n 
2 36   ARG n 
2 37   VAL n 
2 38   GLN n 
2 39   HIS n 
2 40   LEU n 
2 41   HIS n 
2 42   ASP n 
2 43   ILE n 
2 44   ARG n 
2 45   ASP n 
2 46   LEU n 
2 47   HIS n 
2 48   ARG n 
2 49   TYR n 
2 50   TYR n 
2 51   SER n 
2 52   SER n 
2 53   GLU n 
2 54   SER n 
2 55   PHE n 
2 56   GLU n 
2 57   TYR n 
2 58   SER n 
2 59   ASN n 
2 60   VAL n 
2 61   SER n 
2 62   GLY n 
2 63   LYS n 
2 64   VAL n 
2 65   GLU n 
2 66   ASN n 
2 67   TYR n 
2 68   ASN n 
2 69   GLY n 
2 70   SER n 
2 71   ASN n 
2 72   VAL n 
2 73   VAL n 
2 74   ARG n 
2 75   PHE n 
2 76   ASN n 
2 77   PRO n 
2 78   LYS n 
2 79   ASP n 
2 80   GLN n 
2 81   ASN n 
2 82   HIS n 
2 83   GLN n 
2 84   LEU n 
2 85   PHE n 
2 86   LEU n 
2 87   LEU n 
2 88   GLY n 
2 89   LYS n 
2 90   ASP n 
2 91   LYS n 
2 92   GLU n 
2 93   GLN n 
2 94   TYR n 
2 95   LYS n 
2 96   GLU n 
2 97   GLY n 
2 98   LEU n 
2 99   GLN n 
2 100  GLY n 
2 101  GLN n 
2 102  ASN n 
2 103  VAL n 
2 104  PHE n 
2 105  VAL n 
2 106  VAL n 
2 107  GLN n 
2 108  GLU n 
2 109  LEU n 
2 110  ILE n 
2 111  ASP n 
2 112  PRO n 
2 113  ASN n 
2 114  GLY n 
2 115  ARG n 
2 116  LEU n 
2 117  SER n 
2 118  THR n 
2 119  VAL n 
2 120  GLY n 
2 121  GLY n 
2 122  VAL n 
2 123  THR n 
2 124  LYS n 
2 125  LYS n 
2 126  ASN n 
2 127  ASN n 
2 128  LYS n 
2 129  THR n 
2 130  SER n 
2 131  GLU n 
2 132  THR n 
2 133  ASN n 
2 134  THR n 
2 135  PRO n 
2 136  LEU n 
2 137  PHE n 
2 138  VAL n 
2 139  ASN n 
2 140  LYS n 
2 141  VAL n 
2 142  ASN n 
2 143  GLY n 
2 144  GLU n 
2 145  ASP n 
2 146  LEU n 
2 147  ASP n 
2 148  ALA n 
2 149  SER n 
2 150  ILE n 
2 151  ASP n 
2 152  SER n 
2 153  PHE n 
2 154  LEU n 
2 155  ILE n 
2 156  GLN n 
2 157  LYS n 
2 158  GLU n 
2 159  GLU n 
2 160  ILE n 
2 161  SER n 
2 162  LEU n 
2 163  LYS n 
2 164  GLU n 
2 165  LEU n 
2 166  ASP n 
2 167  PHE n 
2 168  LYS n 
2 169  ILE n 
2 170  ARG n 
2 171  GLN n 
2 172  GLN n 
2 173  LEU n 
2 174  VAL n 
2 175  ASN n 
2 176  ASN n 
2 177  TYR n 
2 178  GLY n 
2 179  LEU n 
2 180  TYR n 
2 181  LYS n 
2 182  GLY n 
2 183  THR n 
2 184  SER n 
2 185  LYS n 
2 186  TYR n 
2 187  GLY n 
2 188  LYS n 
2 189  ILE n 
2 190  ILE n 
2 191  ILE n 
2 192  ASN n 
2 193  LEU n 
2 194  LYS n 
2 195  ASP n 
2 196  GLU n 
2 197  ASN n 
2 198  LYS n 
2 199  VAL n 
2 200  GLU n 
2 201  ILE n 
2 202  ASP n 
2 203  LEU n 
2 204  GLY n 
2 205  ASP n 
2 206  LYS n 
2 207  LEU n 
2 208  GLN n 
2 209  PHE n 
2 210  GLU n 
2 211  ARG n 
2 212  MET n 
2 213  GLY n 
2 214  ASP n 
2 215  VAL n 
2 216  LEU n 
2 217  ASN n 
2 218  SER n 
2 219  LYS n 
2 220  ASP n 
2 221  ILE n 
2 222  ARG n 
2 223  GLY n 
2 224  ILE n 
2 225  SER n 
2 226  VAL n 
2 227  THR n 
2 228  ILE n 
2 229  ASN n 
2 230  GLN n 
2 231  ILE n 
# 
_entity_src_gen.entity_id                          2 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    MRSA252 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Staphylococcus aureus subsp. aureus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     282458 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_entity_src_nat.entity_id                  1 
_entity_src_nat.pdbx_src_id                1 
_entity_src_nat.pdbx_alt_source_flag       sample 
_entity_src_nat.pdbx_beg_seq_num           ? 
_entity_src_nat.pdbx_end_seq_num           ? 
_entity_src_nat.common_name                human 
_entity_src_nat.pdbx_organism_scientific   'Homo sapiens' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      9606 
_entity_src_nat.genus                      ? 
_entity_src_nat.species                    ? 
_entity_src_nat.strain                     ? 
_entity_src_nat.tissue                     Blood 
_entity_src_nat.tissue_fraction            ? 
_entity_src_nat.pdbx_secretion             ? 
_entity_src_nat.pdbx_fragment              ? 
_entity_src_nat.pdbx_variant               ? 
_entity_src_nat.pdbx_cell_line             ? 
_entity_src_nat.pdbx_atcc                  ? 
_entity_src_nat.pdbx_cellular_location     ? 
_entity_src_nat.pdbx_organ                 ? 
_entity_src_nat.pdbx_organelle             ? 
_entity_src_nat.pdbx_cell                  ? 
_entity_src_nat.pdbx_plasmid_name          ? 
_entity_src_nat.pdbx_plasmid_details       ? 
_entity_src_nat.details                    'Outdated plasma pools' 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
_struct_ref.pdbx_db_isoform 
1 UNP CO5_HUMAN    P01031 1 
;MGLLGILCFLIFLGKTWGQEQTYVISAPKIFRVGASENIVIQVYGYTEAFDATISIKSYPDKKFSYSSGHVHLSSENKFQ
NSAILTIQPKQLPGGQNPVSYVYLEVVSKHFSKSKRMPITYDNGFLFIHTDKPVYTPDQSVKVRVYSLNDDLKPAKRETV
LTFIDPEGSEVDMVEEIDHIGIISFPDFKIPSNPRYGMWTIKAKYKEDFSTTGTAYFEVKEYVLPHFSVSIEPEYNFIGY
KNFKNFEITIKARYFYNKVVTEADVYITFGIREDLKDDQKEMMQTAMQNTMLINGIAQVTFDSETAVKELSYYSLEDLNN
KYLYIAVTVIESTGGFSEEAEIPGIKYVLSPYKLNLVATPLFLKPGIPYPIKVQVKDSLDQLVGGVPVTLNAQTIDVNQE
TSDLDPSKSVTRVDDGVASFVLNLPSGVTVLEFNVKTDAPDLPEENQAREGYRAIAYSSLSQSYLYIDWTDNHKALLVGE
HLNIIVTPKSPYIDKITHYNYLILSKGKIIHFGTREKFSDASYQSINIPVTQNMVPSSRLLVYYIVTGEQTAELVSDSVW
LNIEEKCGNQLQVHLSPDADAYSPGQTVSLNMATGMDSWVALAAVDSAVYGVQRGAKKPLERVFQFLEKSDLGCGAGGGL
NNANVFHLAGLTFLTNANADDSQENDEPCKEILRPRRTLQKKIEEIAAKYKHSVVKKCCYDGACVNNDETCEQRAARISL
GPRCIKAFTECCVVASQLRANISHKDMQLGRLHMKTLLPVSKPEIRSYFPESWLWEVHLVPRRKQLQFALPDSLTTWEIQ
GIGISNTGICVADTVKAKVFKDVFLEMNIPYSVVRGEQIQLKGTVYNYRTSGMQFCVKMSAVEGICTSESPVIDHQGTKS
SKCVRQKVEGSSSHLVTFTVLPLEIGLHNINFSLETWFGKEILVKTLRVVPEGVKRESYSGVTLDPRGIYGTISRRKEFP
YRIPLDLVPKTEIKRILSVKGLLVGEILSAVLSQEGINILTHLPKGSAEAELMSVVPVFYVFHYLETGNHWNIFHSDPLI
EKQKLKKKLKEGMLSIMSYRNADYSYSVWKGGSASTWLTAFALRVLGQVNKYVEQNQNSICNSLLWLVENYQLDNGSFKE
NSQYQPIKLQGTLPVEARENSLYLTAFTVIGIRKAFDICPLVKIDTALIKADNFLLENTLPAQSTFTLAISAYALSLGDK
THPQFRSIVSALKREALVKGNPPIYRFWKDNLQHKDSSVPNTGTARMVETTAYALLTSLNLKDINYVNPVIKWLSEEQRY
GGGFYSTQDTINAIEGLTEYSLLVKQLRLSMDIDVSYKHKGALHNYKMTDKNFLGRPVEVLLNDDLIVSTGFGSGLATVH
VTTVVHKTSTSEEVCSFYLKIDTQDIEASHYRGYGNSDYKRIVACASYKPSREESSSGSSHAVMDISLPTGISANEEDLK
ALVEGVDQLFTDYQIKDGHVILQLNSIPSSDFLCVRFRIFELFEVGFLSPATFTVYEYHRPDKQCTMFYSTSNIKIQKVC
EGAACKCVEADCGQMQEELDLTISAETRKQTACKPEIAYAYKVSITSITVENVFVKYKATLLDIYKTGEAVAEKDSEITF
IKKVTCTNAELVKGRQYLIMGKEALQIKYNFSFRYIYPLDSLTWIEYWPRDTTCSSCQAFLANLDEFAEDIFLNGC
;
1 ? 
2 UNP Q6GJP2_STAAR Q6GJP2 2 
;MKLKTLAKATLALGLLTTGVITSEGQAVQAAEKQERVQHLHDIRDLHRYYSSESFEYSNVSGKVENYNGSNVVRFNPKDQ
NHQLFLLGKDKEQYKEGLQGQNVFVVQELIDPNGRLSTVGGVTKKNNKTSETNTPLFVNKVNGEDLDASIDSFLIQKEEI
SLKELDFKIRQQLVNNYGLYKGTSKYGKIIINLKDENKVEIDLGDKLQFERMGDVLNSKDIRGISVTINQI
;
1 ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 3KLS A 1 ? 1676 ? P01031 1 ? 1676 ? 1 1676 
2 2 3KLS X 1 ? 231  ? Q6GJP2 1 ? 231  ? 1 231  
3 1 3KLS B 1 ? 1676 ? P01031 1 ? 1676 ? 1 1676 
4 2 3KLS Y 1 ? 231  ? Q6GJP2 1 ? 231  ? 1 231  
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
2 3KLS GLY X 35 ? UNP Q6GJP2 GLU 35 ENGINEERED 35 1 
4 3KLS GLY Y 35 ? UNP Q6GJP2 GLU 35 ENGINEERED 35 2 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE               ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE             ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'        ? 'C4 H7 N O4'     133.103 
CD  non-polymer         . 'CADMIUM ION'          ? 'Cd 2'           112.411 
CYS 'L-peptide linking' y CYSTEINE               ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE              ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'        ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE              ? 'C6 H10 N3 O2 1' 156.162 
ILE 'L-peptide linking' y ISOLEUCINE             ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                 ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE             ? 'C5 H11 N O2 S'  149.211 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6'    221.208 
PHE 'L-peptide linking' y PHENYLALANINE          ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                 ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE              ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN             ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE               ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                 ? 'C5 H11 N O2'    117.146 
# 
_exptl.entry_id          3KLS 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.36 
_exptl_crystal.density_percent_sol   63.39 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION' 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              6.2 
_exptl_crystal_grow.pdbx_details    
'Reservoir contains 50mM MgAc2, 50 mM MES pH 6.2, mixed 1:1 with protein, VAPOR DIFFUSION, temperature 277K' 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'MAR CCD 165 mm' 
_diffrn_detector.pdbx_collection_date   2008-09-18 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'Bent Si (111) crystal, horizontally focusing' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0379 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'MAX II BEAMLINE I911-2' 
_diffrn_source.pdbx_synchrotron_site       'MAX II' 
_diffrn_source.pdbx_synchrotron_beamline   I911-2 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.0379 
# 
_reflns.entry_id                     3KLS 
_reflns.observed_criterion_sigma_I   -3 
_reflns.observed_criterion_sigma_F   0 
_reflns.d_resolution_low             29.047 
_reflns.d_resolution_high            3.6 
_reflns.number_obs                   64555 
_reflns.number_all                   64230 
_reflns.percent_possible_obs         99.4 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.085 
_reflns.pdbx_netI_over_sigmaI        11 
_reflns.B_iso_Wilson_estimate        110.890 
_reflns.pdbx_redundancy              2.9 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             3.6 
_reflns_shell.d_res_low              3.8 
_reflns_shell.percent_possible_all   99.4 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    ? 
_reflns_shell.pdbx_redundancy        ? 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 3KLS 
_refine.ls_number_reflns_obs                     64230 
_refine.ls_number_reflns_all                     64555 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.99 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             29.047 
_refine.ls_d_res_high                            3.600 
_refine.ls_percent_reflns_obs                    99.49 
_refine.ls_R_factor_obs                          0.2009 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1977 
_refine.ls_R_factor_R_free                       0.2626 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.99 
_refine.ls_number_reflns_R_free                  3205 
_refine.ls_number_reflns_R_work                  61025 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               156.921 
_refine.aniso_B[1][1]                            0.000 
_refine.aniso_B[2][2]                            0.000 
_refine.aniso_B[3][3]                            0.000 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.000 
_refine.aniso_B[2][3]                            0.000 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_ksol                 0.299 
_refine.solvent_model_param_bsol                 120.556 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      'PDB ENTRY 3CU7 chain A residues 20-1510' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            random 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.370 
_refine.overall_SU_B                             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   0.803 
_refine.B_iso_max                                414.93 
_refine.B_iso_min                                43.25 
_refine.pdbx_overall_phase_error                 27.160 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.50 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        27590 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         93 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               27683 
_refine_hist.d_res_high                       3.600 
_refine_hist.d_res_low                        29.047 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' f_bond_d           28268 0.012  ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          38275 1.658  ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     4359  0.105  ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      4875  0.007  ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 10296 21.163 ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.number_reflns_obs 
'X-RAY DIFFRACTION' . 3.6002  3.6538  2584 0.3042 100.00 0.3475 . . 168 . . . . 
'X-RAY DIFFRACTION' . 3.6538  3.7108  2654 0.3001 99.00  0.3997 . . 149 . . . . 
'X-RAY DIFFRACTION' . 3.7108  3.7715  2678 0.2921 99.00  0.3823 . . 140 . . . . 
'X-RAY DIFFRACTION' . 3.7715  3.8364  2637 0.2717 100.00 0.3203 . . 131 . . . . 
'X-RAY DIFFRACTION' . 3.8364  3.9060  2666 0.2443 99.00  0.3510 . . 137 . . . . 
'X-RAY DIFFRACTION' . 3.9060  3.9809  2648 0.2397 100.00 0.2740 . . 129 . . . . 
'X-RAY DIFFRACTION' . 3.9809  4.0620  2636 0.2176 99.00  0.2786 . . 143 . . . . 
'X-RAY DIFFRACTION' . 4.0620  4.1501  2649 0.2079 100.00 0.2627 . . 161 . . . . 
'X-RAY DIFFRACTION' . 4.1501  4.2463  2705 0.1983 100.00 0.2482 . . 135 . . . . 
'X-RAY DIFFRACTION' . 4.2463  4.3522  2628 0.1897 100.00 0.2524 . . 121 . . . . 
'X-RAY DIFFRACTION' . 4.3522  4.4694  2726 0.1731 100.00 0.2434 . . 140 . . . . 
'X-RAY DIFFRACTION' . 4.4694  4.6005  2586 0.1614 100.00 0.2295 . . 139 . . . . 
'X-RAY DIFFRACTION' . 4.6005  4.7483  2676 0.1542 100.00 0.1833 . . 156 . . . . 
'X-RAY DIFFRACTION' . 4.7483  4.9173  2632 0.1554 100.00 0.2084 . . 154 . . . . 
'X-RAY DIFFRACTION' . 4.9173  5.1131  2689 0.1437 100.00 0.2218 . . 107 . . . . 
'X-RAY DIFFRACTION' . 5.1131  5.3445  2672 0.1531 100.00 0.2226 . . 152 . . . . 
'X-RAY DIFFRACTION' . 5.3445  5.6243  2620 0.1724 100.00 0.2023 . . 142 . . . . 
'X-RAY DIFFRACTION' . 5.6243  5.9738  2700 0.1748 100.00 0.2794 . . 149 . . . . 
'X-RAY DIFFRACTION' . 5.9738  6.4305  2638 0.1941 100.00 0.2649 . . 125 . . . . 
'X-RAY DIFFRACTION' . 6.4305  7.0691  2675 0.1908 99.00  0.2890 . . 115 . . . . 
'X-RAY DIFFRACTION' . 7.0691  8.0728  2625 0.1920 99.00  0.3085 . . 165 . . . . 
'X-RAY DIFFRACTION' . 8.0728  10.0993 2674 0.1611 99.00  0.2006 . . 120 . . . . 
'X-RAY DIFFRACTION' . 10.0993 29.0476 2627 0.2058 98.00  0.2556 . . 127 . . . . 
# 
_struct.entry_id                  3KLS 
_struct.title                     'Structure of complement C5 in complex with SSL7' 
_struct.pdbx_descriptor           'Complement C5, Exotoxin 1' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3KLS 
_struct_keywords.pdbx_keywords   'IMMUNE SYSTEM' 
_struct_keywords.text            
;OB-fold, b-grasp domain, FN3 domain, Cleavage on pair of basic residues, Complement alternate pathway, Complement pathway, Cytolysis, Disulfide bond, Glycoprotein, Immune response, Inflammatory response, Innate immunity, Membrane attack complex, Secreted, IMMUNE SYSTEM
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 1 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 4 ? 
H N N 3 ? 
I N N 3 ? 
J N N 3 ? 
K N N 3 ? 
L N N 4 ? 
M N N 4 ? 
N N N 4 ? 
O N N 3 ? 
P N N 3 ? 
Q N N 3 ? 
R N N 3 ? 
S N N 4 ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  THR A 531  ? VAL A 535  ? THR A 531  VAL A 535  5 ? 5  
HELX_P HELX_P2  2  LEU A 620  ? LEU A 627  ? LEU A 620  LEU A 627  1 ? 8  
HELX_P HELX_P3  3  ASN A 641  ? ALA A 649  ? ASN A 641  ALA A 649  1 ? 9  
HELX_P HELX_P4  4  GLN A 680  ? GLU A 685  ? GLN A 680  GLU A 685  1 ? 6  
HELX_P HELX_P5  5  ILE A 686  ? TYR A 690  ? ILE A 686  TYR A 690  5 ? 5  
HELX_P HELX_P6  6  HIS A 692  ? CYS A 704  ? HIS A 692  CYS A 704  1 ? 13 
HELX_P HELX_P7  7  THR A 710  ? ARG A 717  ? THR A 710  ARG A 717  1 ? 8  
HELX_P HELX_P8  8  GLY A 721  ? ARG A 739  ? GLY A 721  ARG A 739  1 ? 19 
HELX_P HELX_P9  9  GLY A 985  ? ALA A 990  ? GLY A 985  ALA A 990  1 ? 6  
HELX_P HELX_P10 10 ALA A 1008 ? THR A 1027 ? ALA A 1008 THR A 1027 1 ? 20 
HELX_P HELX_P11 11 HIS A 1030 ? PHE A 1034 ? HIS A 1030 PHE A 1034 5 ? 5  
HELX_P HELX_P12 12 ASP A 1037 ? SER A 1055 ? ASP A 1037 SER A 1055 1 ? 19 
HELX_P HELX_P13 13 ILE A 1056 ? ARG A 1060 ? ILE A 1056 ARG A 1060 5 ? 5  
HELX_P HELX_P14 14 SER A 1075 ? LYS A 1091 ? SER A 1075 LYS A 1091 1 ? 17 
HELX_P HELX_P15 15 ASN A 1096 ? TYR A 1111 ? ASN A 1096 TYR A 1111 1 ? 16 
HELX_P HELX_P16 16 THR A 1132 ? PHE A 1156 ? THR A 1132 PHE A 1156 1 ? 25 
HELX_P HELX_P17 17 ASP A 1157 ? CYS A 1159 ? ASP A 1157 CYS A 1159 5 ? 3  
HELX_P HELX_P18 18 LEU A 1161 ? LEU A 1180 ? LEU A 1161 LEU A 1180 1 ? 20 
HELX_P HELX_P19 19 SER A 1184 ? SER A 1196 ? SER A 1184 SER A 1196 1 ? 13 
HELX_P HELX_P20 20 HIS A 1202 ? ALA A 1216 ? HIS A 1202 ALA A 1216 1 ? 15 
HELX_P HELX_P21 21 THR A 1244 ? LEU A 1261 ? THR A 1244 LEU A 1261 1 ? 18 
HELX_P HELX_P22 22 ASP A 1263 ? SER A 1275 ? ASP A 1263 SER A 1275 1 ? 13 
HELX_P HELX_P23 23 THR A 1287 ? VAL A 1304 ? THR A 1287 VAL A 1304 1 ? 18 
HELX_P HELX_P24 24 ASN A 1435 ? GLU A 1444 ? ASN A 1435 GLU A 1444 1 ? 10 
HELX_P HELX_P25 25 SER A 1544 ? THR A 1551 ? SER A 1544 THR A 1551 1 ? 8  
HELX_P HELX_P26 26 PHE A 1660 ? GLY A 1675 ? PHE A 1660 GLY A 1675 1 ? 16 
HELX_P HELX_P27 27 ASP B 42   ? TYR B 50   ? ASP X 42   TYR X 50   1 ? 9  
HELX_P HELX_P28 28 LEU B 162  ? TYR B 177  ? LEU X 162  TYR X 177  1 ? 16 
HELX_P HELX_P29 29 LYS B 219  ? ILE B 221  ? LYS X 219  ILE X 221  5 ? 3  
HELX_P HELX_P30 30 THR C 531  ? VAL C 535  ? THR B 531  VAL B 535  5 ? 5  
HELX_P HELX_P31 31 LEU C 620  ? LEU C 627  ? LEU B 620  LEU B 627  1 ? 8  
HELX_P HELX_P32 32 ASN C 641  ? ALA C 649  ? ASN B 641  ALA B 649  1 ? 9  
HELX_P HELX_P33 33 GLN C 680  ? GLU C 685  ? GLN B 680  GLU B 685  1 ? 6  
HELX_P HELX_P34 34 ILE C 686  ? TYR C 690  ? ILE B 686  TYR B 690  5 ? 5  
HELX_P HELX_P35 35 HIS C 692  ? CYS C 704  ? HIS B 692  CYS B 704  1 ? 13 
HELX_P HELX_P36 36 THR C 710  ? ARG C 717  ? THR B 710  ARG B 717  1 ? 8  
HELX_P HELX_P37 37 GLY C 721  ? ARG C 739  ? GLY B 721  ARG B 739  1 ? 19 
HELX_P HELX_P38 38 GLY C 985  ? ALA C 990  ? GLY B 985  ALA B 990  1 ? 6  
HELX_P HELX_P39 39 ALA C 1008 ? THR C 1027 ? ALA B 1008 THR B 1027 1 ? 20 
HELX_P HELX_P40 40 HIS C 1030 ? PHE C 1034 ? HIS B 1030 PHE B 1034 5 ? 5  
HELX_P HELX_P41 41 ASP C 1037 ? SER C 1055 ? ASP B 1037 SER B 1055 1 ? 19 
HELX_P HELX_P42 42 ILE C 1056 ? ARG C 1060 ? ILE B 1056 ARG B 1060 5 ? 5  
HELX_P HELX_P43 43 SER C 1075 ? LYS C 1091 ? SER B 1075 LYS B 1091 1 ? 17 
HELX_P HELX_P44 44 ASN C 1096 ? TYR C 1111 ? ASN B 1096 TYR B 1111 1 ? 16 
HELX_P HELX_P45 45 THR C 1132 ? PHE C 1156 ? THR B 1132 PHE B 1156 1 ? 25 
HELX_P HELX_P46 46 ASP C 1157 ? CYS C 1159 ? ASP B 1157 CYS B 1159 5 ? 3  
HELX_P HELX_P47 47 LEU C 1161 ? LEU C 1180 ? LEU B 1161 LEU B 1180 1 ? 20 
HELX_P HELX_P48 48 SER C 1184 ? SER C 1196 ? SER B 1184 SER B 1196 1 ? 13 
HELX_P HELX_P49 49 HIS C 1202 ? ALA C 1216 ? HIS B 1202 ALA B 1216 1 ? 15 
HELX_P HELX_P50 50 THR C 1244 ? LEU C 1261 ? THR B 1244 LEU B 1261 1 ? 18 
HELX_P HELX_P51 51 ASP C 1263 ? SER C 1275 ? ASP B 1263 SER B 1275 1 ? 13 
HELX_P HELX_P52 52 THR C 1287 ? VAL C 1304 ? THR B 1287 VAL B 1304 1 ? 18 
HELX_P HELX_P53 53 ASN C 1435 ? GLU C 1444 ? ASN B 1435 GLU B 1444 1 ? 10 
HELX_P HELX_P54 54 ARG C 1500 ? GLN C 1504 ? ARG B 1500 GLN B 1504 5 ? 5  
HELX_P HELX_P55 55 ASP D 42   ? TYR D 50   ? ASP Y 42   TYR Y 50   1 ? 9  
HELX_P HELX_P56 56 LEU D 162  ? TYR D 177  ? LEU Y 162  TYR Y 177  1 ? 16 
HELX_P HELX_P57 57 LYS D 219  ? ILE D 221  ? LYS Y 219  ILE Y 221  5 ? 3  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ? ? A CYS 567  SG  ? ? ? 1_555 A CYS 810  SG ? ? A CYS 567  A CYS 810  1_555 ? ? ? ? ? ? ? 2.037 ? 
disulf2  disulf ? ? A CYS 634  SG  ? ? ? 1_555 A CYS 669  SG ? ? A CYS 634  A CYS 669  1_555 ? ? ? ? ? ? ? 2.022 ? 
disulf3  disulf ? ? A CYS 698  SG  ? ? ? 1_555 A CYS 724  SG ? ? A CYS 698  A CYS 724  1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf4  disulf ? ? A CYS 699  SG  ? ? ? 1_555 A CYS 731  SG ? ? A CYS 699  A CYS 731  1_555 ? ? ? ? ? ? ? 2.025 ? 
disulf5  disulf ? ? A CYS 711  SG  ? ? ? 1_555 A CYS 732  SG ? ? A CYS 711  A CYS 732  1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf6  disulf ? ? A CYS 856  SG  ? ? ? 1_555 A CYS 883  SG ? ? A CYS 856  A CYS 883  1_555 ? ? ? ? ? ? ? 2.038 ? 
disulf7  disulf ? ? A CYS 866  SG  ? ? ? 1_555 A CYS 1527 SG ? ? A CYS 866  A CYS 1527 1_555 ? ? ? ? ? ? ? 2.041 ? 
disulf8  disulf ? ? A CYS 1101 SG  ? ? ? 1_555 A CYS 1159 SG ? ? A CYS 1101 A CYS 1159 1_555 ? ? ? ? ? ? ? 2.008 ? 
disulf9  disulf ? ? A CYS 1375 SG  ? ? ? 1_555 A CYS 1505 SG ? ? A CYS 1375 A CYS 1505 1_555 ? ? ? ? ? ? ? 2.023 ? 
disulf10 disulf ? ? A CYS 1405 SG  ? ? ? 1_555 A CYS 1474 SG ? ? A CYS 1405 A CYS 1474 1_555 ? ? ? ? ? ? ? 2.027 ? 
disulf11 disulf ? ? A CYS 1520 SG  ? ? ? 1_555 A CYS 1525 SG ? ? A CYS 1520 A CYS 1525 1_555 ? ? ? ? ? ? ? 2.040 ? 
disulf12 disulf ? ? A CYS 1532 SG  ? ? ? 1_555 A CYS 1606 SG ? ? A CYS 1532 A CYS 1606 1_555 ? ? ? ? ? ? ? 2.042 ? 
disulf13 disulf ? ? A CYS 1553 SG  ? ? ? 1_555 A CYS 1676 SG ? ? A CYS 1553 A CYS 1676 1_555 ? ? ? ? ? ? ? 2.046 ? 
disulf14 disulf ? ? A CYS 1654 SG  ? ? ? 1_555 A CYS 1657 SG ? ? A CYS 1654 A CYS 1657 1_555 ? ? ? ? ? ? ? 2.047 ? 
disulf15 disulf ? ? C CYS 567  SG  ? ? ? 1_555 C CYS 810  SG ? ? B CYS 567  B CYS 810  1_555 ? ? ? ? ? ? ? 2.037 ? 
disulf16 disulf ? ? C CYS 634  SG  ? ? ? 1_555 C CYS 669  SG ? ? B CYS 634  B CYS 669  1_555 ? ? ? ? ? ? ? 2.029 ? 
disulf17 disulf ? ? C CYS 698  SG  ? ? ? 1_555 C CYS 724  SG ? ? B CYS 698  B CYS 724  1_555 ? ? ? ? ? ? ? 2.042 ? 
disulf18 disulf ? ? C CYS 699  SG  ? ? ? 1_555 C CYS 731  SG ? ? B CYS 699  B CYS 731  1_555 ? ? ? ? ? ? ? 2.020 ? 
disulf19 disulf ? ? C CYS 711  SG  ? ? ? 1_555 C CYS 732  SG ? ? B CYS 711  B CYS 732  1_555 ? ? ? ? ? ? ? 2.037 ? 
disulf20 disulf ? ? C CYS 856  SG  ? ? ? 1_555 C CYS 883  SG ? ? B CYS 856  B CYS 883  1_555 ? ? ? ? ? ? ? 2.039 ? 
disulf21 disulf ? ? C CYS 866  SG  ? ? ? 1_555 C CYS 1527 SG ? ? B CYS 866  B CYS 1527 1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf22 disulf ? ? C CYS 1101 SG  ? ? ? 1_555 C CYS 1159 SG ? ? B CYS 1101 B CYS 1159 1_555 ? ? ? ? ? ? ? 1.999 ? 
disulf23 disulf ? ? C CYS 1375 SG  ? ? ? 1_555 C CYS 1505 SG ? ? B CYS 1375 B CYS 1505 1_555 ? ? ? ? ? ? ? 2.027 ? 
disulf24 disulf ? ? C CYS 1405 SG  ? ? ? 1_555 C CYS 1474 SG ? ? B CYS 1405 B CYS 1474 1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf25 disulf ? ? C CYS 1520 SG  ? ? ? 1_555 C CYS 1525 SG ? ? B CYS 1520 B CYS 1525 1_555 ? ? ? ? ? ? ? 2.041 ? 
metalc1  metalc ? ? A GLU 247  OE2 ? ? ? 1_555 E CD  .    CD ? ? A GLU 247  A CD  1677 1_555 ? ? ? ? ? ? ? 2.357 ? 
metalc2  metalc ? ? A ASP 264  OD2 ? ? ? 1_555 I CD  .    CD ? ? A ASP 264  A CD  1679 1_555 ? ? ? ? ? ? ? 2.368 ? 
metalc3  metalc ? ? A GLU 339  OE1 ? ? ? 1_555 J CD  .    CD ? ? A GLU 339  A CD  1680 1_555 ? ? ? ? ? ? ? 2.362 ? 
metalc4  metalc ? ? A ASP 471  OD1 ? ? ? 1_555 H CD  .    CD ? ? A ASP 471  A CD  1678 1_555 ? ? ? ? ? ? ? 2.373 ? 
metalc5  metalc ? ? A ASP 471  OD2 ? ? ? 1_555 H CD  .    CD ? ? A ASP 471  A CD  1678 1_555 ? ? ? ? ? ? ? 2.363 ? 
metalc6  metalc ? ? A GLU 480  OE1 ? ? ? 1_555 H CD  .    CD ? ? A GLU 480  A CD  1678 1_555 ? ? ? ? ? ? ? 2.375 ? 
metalc7  metalc ? ? A GLU 480  OE2 ? ? ? 1_555 H CD  .    CD ? ? A GLU 480  A CD  1678 1_555 ? ? ? ? ? ? ? 2.361 ? 
covale1  covale ? ? A ASN 741  ND2 ? ? ? 1_555 L NAG .    C1 ? ? A ASN 741  A NAG 1682 1_555 ? ? ? ? ? ? ? 1.446 ? 
metalc8  metalc ? ? A HIS 753  ND1 ? ? ? 1_555 I CD  .    CD ? ? A HIS 753  A CD  1679 1_555 ? ? ? ? ? ? ? 2.351 ? 
metalc9  metalc ? ? A GLU 764  OE1 ? ? ? 1_555 J CD  .    CD ? ? A GLU 764  A CD  1680 1_555 ? ? ? ? ? ? ? 2.351 ? 
metalc10 metalc ? ? A GLU 764  OE2 ? ? ? 1_555 J CD  .    CD ? ? A GLU 764  A CD  1680 1_555 ? ? ? ? ? ? ? 2.229 ? 
metalc11 metalc ? ? A GLN 886  OE1 ? ? ? 1_555 K CD  .    CD ? ? A GLN 886  A CD  1681 1_555 ? ? ? ? ? ? ? 2.366 ? 
covale2  covale ? ? A ASN 911  ND2 ? ? ? 1_555 F NAG .    C1 ? ? A ASN 911  A NAG 2001 1_555 ? ? ? ? ? ? ? 1.447 ? 
metalc12 metalc ? ? A GLU 1589 OE1 ? ? ? 1_555 K CD  .    CD ? ? A GLU 1589 A CD  1681 1_555 ? ? ? ? ? ? ? 2.355 ? 
metalc13 metalc ? ? A GLU 1589 OE2 ? ? ? 1_555 K CD  .    CD ? ? A GLU 1589 A CD  1681 1_555 ? ? ? ? ? ? ? 2.353 ? 
metalc14 metalc ? ? A GLU 1666 OE1 ? ? ? 1_555 R CD  .    CD ? ? A GLU 1666 B CD  1680 1_555 ? ? ? ? ? ? ? 2.356 ? 
metalc15 metalc ? ? A GLU 1666 OE2 ? ? ? 1_555 R CD  .    CD ? ? A GLU 1666 B CD  1680 1_555 ? ? ? ? ? ? ? 2.350 ? 
metalc16 metalc ? ? C GLU 247  OE2 ? ? ? 1_555 E CD  .    CD ? ? B GLU 247  A CD  1677 1_555 ? ? ? ? ? ? ? 2.309 ? 
metalc17 metalc ? ? C ASP 264  OD2 ? ? ? 1_555 P CD  .    CD ? ? B ASP 264  B CD  1678 1_555 ? ? ? ? ? ? ? 2.368 ? 
metalc18 metalc ? ? C GLU 339  OE1 ? ? ? 1_555 Q CD  .    CD ? ? B GLU 339  B CD  1679 1_555 ? ? ? ? ? ? ? 2.352 ? 
metalc19 metalc ? ? C ASP 471  OD1 ? ? ? 1_555 O CD  .    CD ? ? B ASP 471  B CD  1677 1_555 ? ? ? ? ? ? ? 2.368 ? 
metalc20 metalc ? ? C ASP 471  OD2 ? ? ? 1_555 O CD  .    CD ? ? B ASP 471  B CD  1677 1_555 ? ? ? ? ? ? ? 2.366 ? 
metalc21 metalc ? ? C GLU 480  OE1 ? ? ? 1_555 O CD  .    CD ? ? B GLU 480  B CD  1677 1_555 ? ? ? ? ? ? ? 2.364 ? 
metalc22 metalc ? ? C GLU 480  OE2 ? ? ? 1_555 O CD  .    CD ? ? B GLU 480  B CD  1677 1_555 ? ? ? ? ? ? ? 2.366 ? 
covale3  covale ? ? C ASN 741  ND2 ? ? ? 1_555 S NAG .    C1 ? ? B ASN 741  B NAG 1681 1_555 ? ? ? ? ? ? ? 1.446 ? 
metalc23 metalc ? ? C HIS 753  ND1 ? ? ? 1_555 P CD  .    CD ? ? B HIS 753  B CD  1678 1_555 ? ? ? ? ? ? ? 2.375 ? 
metalc24 metalc ? ? C GLU 764  OE1 ? ? ? 1_555 Q CD  .    CD ? ? B GLU 764  B CD  1679 1_555 ? ? ? ? ? ? ? 2.352 ? 
metalc25 metalc ? ? C GLU 764  OE2 ? ? ? 1_555 Q CD  .    CD ? ? B GLU 764  B CD  1679 1_555 ? ? ? ? ? ? ? 2.238 ? 
metalc26 metalc ? ? C GLN 886  OE1 ? ? ? 1_555 R CD  .    CD ? ? B GLN 886  B CD  1680 1_555 ? ? ? ? ? ? ? 2.359 ? 
covale4  covale ? ? C ASN 911  ND2 ? ? ? 1_555 M NAG .    C1 ? ? B ASN 911  B NAG 2001 1_555 ? ? ? ? ? ? ? 1.444 ? 
covale5  covale ? ? F NAG .    O4  ? ? ? 1_555 G NAG .    C1 ? ? A NAG 2001 A NAG 2002 1_555 ? ? ? ? ? ? ? 1.367 ? 
covale6  covale ? ? M NAG .    O4  ? ? ? 1_555 N NAG .    C1 ? ? B NAG 2001 B NAG 2002 1_555 ? ? ? ? ? ? ? 1.367 ? 
metalc27 metalc ? ? A HIS 894  NE2 ? ? ? 1_555 K CD  .    CD ? ? A HIS 894  A CD  1681 1_555 ? ? ? ? ? ? ? 2.612 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
covale ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ASN 1221 A . ? ASN 1221 A PRO 1222 A ? PRO 1222 A 1 5.52 
2 LYS 125  B . ? LYS 125  X ASN 126  B ? ASN 126  X 1 3.49 
3 ASN 1221 C . ? ASN 1221 B PRO 1222 C ? PRO 1222 B 1 5.04 
4 LYS 125  D . ? LYS 125  Y ASN 126  D ? ASN 126  Y 1 3.64 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A  ? 4 ? 
B  ? 2 ? 
C  ? 4 ? 
D  ? 3 ? 
E  ? 5 ? 
F  ? 2 ? 
G  ? 2 ? 
H  ? 3 ? 
I  ? 3 ? 
J  ? 2 ? 
K  ? 3 ? 
L  ? 3 ? 
M  ? 2 ? 
N  ? 2 ? 
O  ? 3 ? 
P  ? 4 ? 
Q  ? 3 ? 
R  ? 9 ? 
S  ? 3 ? 
T  ? 2 ? 
U  ? 3 ? 
V  ? 2 ? 
W  ? 4 ? 
X  ? 2 ? 
Y  ? 2 ? 
Z  ? 3 ? 
AA ? 3 ? 
AB ? 4 ? 
AC ? 2 ? 
AD ? 2 ? 
AE ? 3 ? 
AF ? 4 ? 
AG ? 5 ? 
AH ? 5 ? 
AI ? 3 ? 
AJ ? 2 ? 
AK ? 3 ? 
AL ? 2 ? 
AM ? 2 ? 
AN ? 2 ? 
AO ? 4 ? 
AP ? 2 ? 
AQ ? 4 ? 
AR ? 3 ? 
AS ? 5 ? 
AT ? 2 ? 
AU ? 2 ? 
AV ? 3 ? 
AW ? 3 ? 
AX ? 2 ? 
AY ? 3 ? 
AZ ? 3 ? 
BA ? 2 ? 
BB ? 2 ? 
BC ? 3 ? 
BD ? 4 ? 
BE ? 3 ? 
BF ? 8 ? 
BG ? 3 ? 
BH ? 2 ? 
BI ? 3 ? 
BJ ? 2 ? 
BK ? 4 ? 
BL ? 2 ? 
BM ? 2 ? 
BN ? 3 ? 
BO ? 3 ? 
BP ? 4 ? 
BQ ? 2 ? 
BR ? 2 ? 
BS ? 3 ? 
BT ? 4 ? 
BU ? 5 ? 
BV ? 3 ? 
BW ? 2 ? 
BX ? 2 ? 
BY ? 2 ? 
BZ ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A  1 2 ? anti-parallel 
A  2 3 ? anti-parallel 
A  3 4 ? anti-parallel 
B  1 2 ? parallel      
C  1 2 ? anti-parallel 
C  2 3 ? anti-parallel 
C  3 4 ? anti-parallel 
D  1 2 ? anti-parallel 
D  2 3 ? anti-parallel 
E  1 2 ? parallel      
E  2 3 ? anti-parallel 
E  3 4 ? anti-parallel 
E  4 5 ? anti-parallel 
F  1 2 ? anti-parallel 
G  1 2 ? parallel      
H  1 2 ? anti-parallel 
H  2 3 ? anti-parallel 
I  1 2 ? anti-parallel 
I  2 3 ? anti-parallel 
J  1 2 ? parallel      
K  1 2 ? anti-parallel 
K  2 3 ? anti-parallel 
L  1 2 ? anti-parallel 
L  2 3 ? anti-parallel 
M  1 2 ? anti-parallel 
N  1 2 ? anti-parallel 
O  1 2 ? anti-parallel 
O  2 3 ? anti-parallel 
P  1 2 ? anti-parallel 
P  2 3 ? anti-parallel 
P  3 4 ? anti-parallel 
Q  1 2 ? anti-parallel 
Q  2 3 ? anti-parallel 
R  1 2 ? anti-parallel 
R  2 3 ? anti-parallel 
R  3 4 ? anti-parallel 
R  4 5 ? anti-parallel 
R  5 6 ? anti-parallel 
R  6 7 ? parallel      
R  7 8 ? anti-parallel 
R  8 9 ? anti-parallel 
S  1 2 ? anti-parallel 
S  2 3 ? anti-parallel 
T  1 2 ? anti-parallel 
U  1 2 ? anti-parallel 
U  2 3 ? anti-parallel 
V  1 2 ? anti-parallel 
W  1 2 ? anti-parallel 
W  2 3 ? anti-parallel 
W  3 4 ? anti-parallel 
X  1 2 ? parallel      
Y  1 2 ? anti-parallel 
Z  1 2 ? anti-parallel 
Z  2 3 ? anti-parallel 
AA 1 2 ? anti-parallel 
AA 2 3 ? anti-parallel 
AB 1 2 ? anti-parallel 
AB 2 3 ? anti-parallel 
AB 3 4 ? anti-parallel 
AC 1 2 ? anti-parallel 
AD 1 2 ? anti-parallel 
AE 1 2 ? anti-parallel 
AE 2 3 ? anti-parallel 
AF 1 2 ? anti-parallel 
AF 2 3 ? anti-parallel 
AF 3 4 ? anti-parallel 
AG 1 2 ? anti-parallel 
AG 2 3 ? anti-parallel 
AG 3 4 ? anti-parallel 
AG 4 5 ? anti-parallel 
AH 1 2 ? anti-parallel 
AH 2 3 ? anti-parallel 
AH 3 4 ? anti-parallel 
AH 4 5 ? anti-parallel 
AI 1 2 ? anti-parallel 
AI 2 3 ? anti-parallel 
AJ 1 2 ? anti-parallel 
AK 1 2 ? anti-parallel 
AK 2 3 ? anti-parallel 
AL 1 2 ? anti-parallel 
AM 1 2 ? anti-parallel 
AN 1 2 ? anti-parallel 
AO 1 2 ? anti-parallel 
AO 2 3 ? anti-parallel 
AO 3 4 ? anti-parallel 
AP 1 2 ? parallel      
AQ 1 2 ? anti-parallel 
AQ 2 3 ? anti-parallel 
AQ 3 4 ? anti-parallel 
AR 1 2 ? anti-parallel 
AR 2 3 ? anti-parallel 
AS 1 2 ? parallel      
AS 2 3 ? anti-parallel 
AS 3 4 ? anti-parallel 
AS 4 5 ? anti-parallel 
AT 1 2 ? anti-parallel 
AU 1 2 ? parallel      
AV 1 2 ? anti-parallel 
AV 2 3 ? anti-parallel 
AW 1 2 ? anti-parallel 
AW 2 3 ? anti-parallel 
AX 1 2 ? parallel      
AY 1 2 ? anti-parallel 
AY 2 3 ? anti-parallel 
AZ 1 2 ? anti-parallel 
AZ 2 3 ? anti-parallel 
BA 1 2 ? anti-parallel 
BB 1 2 ? anti-parallel 
BC 1 2 ? anti-parallel 
BC 2 3 ? anti-parallel 
BD 1 2 ? anti-parallel 
BD 2 3 ? anti-parallel 
BD 3 4 ? anti-parallel 
BE 1 2 ? anti-parallel 
BE 2 3 ? anti-parallel 
BF 1 2 ? anti-parallel 
BF 2 3 ? anti-parallel 
BF 3 4 ? anti-parallel 
BF 4 5 ? anti-parallel 
BF 5 6 ? anti-parallel 
BF 6 7 ? parallel      
BF 7 8 ? anti-parallel 
BG 1 2 ? anti-parallel 
BG 2 3 ? anti-parallel 
BH 1 2 ? anti-parallel 
BI 1 2 ? anti-parallel 
BI 2 3 ? anti-parallel 
BJ 1 2 ? anti-parallel 
BK 1 2 ? anti-parallel 
BK 2 3 ? anti-parallel 
BK 3 4 ? anti-parallel 
BL 1 2 ? parallel      
BM 1 2 ? anti-parallel 
BN 1 2 ? anti-parallel 
BN 2 3 ? anti-parallel 
BO 1 2 ? anti-parallel 
BO 2 3 ? anti-parallel 
BP 1 2 ? anti-parallel 
BP 2 3 ? anti-parallel 
BP 3 4 ? anti-parallel 
BQ 1 2 ? anti-parallel 
BR 1 2 ? anti-parallel 
BS 1 2 ? anti-parallel 
BS 2 3 ? anti-parallel 
BT 1 2 ? anti-parallel 
BT 2 3 ? anti-parallel 
BT 3 4 ? anti-parallel 
BU 1 2 ? anti-parallel 
BU 2 3 ? anti-parallel 
BU 3 4 ? anti-parallel 
BU 4 5 ? anti-parallel 
BV 1 2 ? anti-parallel 
BV 2 3 ? anti-parallel 
BW 1 2 ? anti-parallel 
BX 1 2 ? anti-parallel 
BY 1 2 ? anti-parallel 
BZ 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A  1 GLN A 80   ? LEU A 85   ? GLN A 80   LEU A 85   
A  2 GLU A 37   ? VAL A 43   ? GLU A 37   VAL A 43   
A  3 TYR A 23   ? PRO A 28   ? TYR A 23   PRO A 28   
A  4 LEU A 651  ? PHE A 653  ? LEU A 651  PHE A 653  
B  1 PHE A 31   ? ARG A 32   ? PHE A 31   ARG A 32   
B  2 ILE A 119  ? THR A 120  ? ILE A 119  THR A 120  
C  1 SER A 65   ? HIS A 70   ? SER A 65   HIS A 70   
C  2 THR A 53   ? LYS A 57   ? THR A 53   LYS A 57   
C  3 VAL A 102  ? VAL A 107  ? VAL A 102  VAL A 107  
C  4 SER A 112  ? MET A 117  ? SER A 112  MET A 117  
D  1 PHE A 125  ? THR A 130  ? PHE A 125  THR A 130  
D  2 VAL A 143  ? LEU A 148  ? VAL A 143  LEU A 148  
D  3 ILE A 182  ? SER A 184  ? ILE A 182  SER A 184  
E  1 VAL A 134  ? TYR A 135  ? VAL A 134  TYR A 135  
E  2 THR A 212  ? VAL A 219  ? THR A 212  VAL A 219  
E  3 GLY A 197  ? TYR A 205  ? GLY A 197  TYR A 205  
E  4 THR A 159  ? ILE A 164  ? THR A 159  ILE A 164  
E  5 VAL A 174  ? GLU A 176  ? VAL A 174  GLU A 176  
F  1 SER A 140  ? VAL A 141  ? SER A 140  VAL A 141  
F  2 PHE A 188  ? LYS A 189  ? PHE A 188  LYS A 189  
G  1 GLU A 221  ? TYR A 222  ? GLU A 221  TYR A 222  
G  2 GLU A 764  ? ILE A 765  ? GLU A 764  ILE A 765  
H  1 SER A 228  ? GLU A 232  ? SER A 228  GLU A 232  
H  2 ILE A 248  ? TYR A 254  ? ILE A 248  TYR A 254  
H  3 LYS A 258  ? VAL A 259  ? LYS A 258  VAL A 259  
I  1 SER A 228  ? GLU A 232  ? SER A 228  GLU A 232  
I  2 ILE A 248  ? TYR A 254  ? ILE A 248  TYR A 254  
I  3 ALA A 297  ? VAL A 299  ? ALA A 297  VAL A 299  
J  1 PHE A 237  ? ILE A 238  ? PHE A 237  ILE A 238  
J  2 LYS A 346  ? TYR A 347  ? LYS A 346  TYR A 347  
K  1 ALA A 263  ? VAL A 265  ? ALA A 263  VAL A 265  
K  2 TYR A 322  ? GLU A 331  ? TYR A 322  GLU A 331  
K  3 THR A 268  ? ARG A 272  ? THR A 268  ARG A 272  
L  1 ALA A 263  ? VAL A 265  ? ALA A 263  VAL A 265  
L  2 TYR A 322  ? GLU A 331  ? TYR A 322  GLU A 331  
L  3 GLU A 338  ? ILE A 342  ? GLU A 338  ILE A 342  
M  1 TYR A 369  ? PRO A 370  ? TYR A 369  PRO A 370  
M  2 VAL A 421  ? LEU A 422  ? VAL A 421  LEU A 422  
N  1 VAL A 373  ? GLN A 374  ? VAL A 373  GLN A 374  
N  2 VAL A 417  ? ALA A 418  ? VAL A 417  ALA A 418  
O  1 THR A 401  ? ASP A 403  ? THR A 401  ASP A 403  
O  2 PRO A 387  ? ASP A 396  ? PRO A 387  ASP A 396  
O  3 SER A 407  ? VAL A 410  ? SER A 407  VAL A 410  
P  1 THR A 401  ? ASP A 403  ? THR A 401  ASP A 403  
P  2 PRO A 387  ? ASP A 396  ? PRO A 387  ASP A 396  
P  3 VAL A 428  ? THR A 437  ? VAL A 428  THR A 437  
P  4 ARG A 449  ? ILE A 455  ? ARG A 449  ILE A 455  
Q  1 TYR A 466  ? TRP A 469  ? TYR A 466  TRP A 469  
Q  2 HIS A 481  ? THR A 487  ? HIS A 481  THR A 487  
Q  3 GLN A 524  ? PRO A 529  ? GLN A 524  PRO A 529  
R  1 ALA A 552  ? ASN A 562  ? ALA A 552  ASN A 562  
R  2 SER A 537  ? THR A 547  ? SER A 537  THR A 547  
R  3 HIS A 498  ? LEU A 504  ? HIS A 498  LEU A 504  
R  4 ILE A 509  ? GLU A 516  ? ILE A 509  GLU A 516  
R  5 ASP B 145  ? ILE B 150  ? ASP X 145  ILE X 150  
R  6 LEU B 136  ? ASN B 142  ? LEU X 136  ASN X 142  
R  7 ILE B 224  ? ASN B 229  ? ILE X 224  ASN X 229  
R  8 TYR B 186  ? LYS B 194  ? TYR X 186  LYS X 194  
R  9 ASN B 197  ? VAL B 199  ? ASN X 197  VAL X 199  
S  1 HIS A 574  ? LEU A 575  ? HIS A 574  LEU A 575  
S  2 LEU A 590  ? ALA A 593  ? LEU A 590  ALA A 593  
S  3 ARG A 783  ? GLN A 785  ? ARG A 783  GLN A 785  
T  1 SER A 598  ? TRP A 599  ? SER A 598  TRP A 599  
T  2 LEU A 779  ? VAL A 780  ? LEU A 779  VAL A 780  
U  1 VAL A 605  ? ASP A 606  ? VAL A 605  ASP A 606  
U  2 THR A 795  ? GLU A 798  ? THR A 795  GLU A 798  
U  3 LYS A 816  ? VAL A 819  ? LYS A 816  VAL A 819  
V  1 ILE A 804  ? SER A 805  ? ILE A 804  SER A 805  
V  2 GLY A 808  ? ILE A 809  ? GLY A 808  ILE A 809  
W  1 VAL A 823  ? MET A 827  ? VAL A 823  MET A 827  
W  2 ILE A 839  ? ASN A 847  ? ILE A 839  ASN A 847  
W  3 SER A 893  ? PRO A 902  ? SER A 893  PRO A 902  
W  4 ILE A 865  ? CYS A 866  ? ILE A 865  CYS A 866  
X  1 SER A 832  ? VAL A 834  ? SER A 832  VAL A 834  
X  2 ARG A 928  ? VAL A 930  ? ARG A 928  VAL A 930  
Y  1 MET A 853  ? GLN A 854  ? MET A 853  GLN A 854  
Y  2 LYS A 887  ? VAL A 888  ? LYS A 887  VAL A 888  
Z  1 LYS A 858  ? MET A 859  ? LYS A 858  MET A 859  
Z  2 ILE A 910  ? THR A 916  ? ILE A 910  THR A 916  
Z  3 GLY A 919  ? LYS A 925  ? GLY A 919  LYS A 925  
AA 1 VAL A 934  ? GLU A 937  ? VAL A 934  GLU A 937  
AA 2 ALA A 1357 ? HIS A 1366 ? ALA A 1357 HIS A 1366 
AA 3 GLY A 941  ? LEU A 944  ? GLY A 941  LEU A 944  
AB 1 VAL A 934  ? GLU A 937  ? VAL A 934  GLU A 937  
AB 2 ALA A 1357 ? HIS A 1366 ? ALA A 1357 HIS A 1366 
AB 3 LYS A 974  ? GLY A 981  ? LYS A 974  GLY A 981  
AB 4 VAL A 1338 ? GLU A 1339 ? VAL A 1338 GLU A 1339 
AC 1 LYS A 957  ? PHE A 959  ? LYS A 957  PHE A 959  
AC 2 LEU A 1346 ? VAL A 1348 ? LEU A 1346 VAL A 1348 
AD 1 LEU A 1217 ? LYS A 1219 ? LEU A 1217 LYS A 1219 
AD 2 TYR A 1225 ? PHE A 1227 ? TYR A 1225 PHE A 1227 
AE 1 PHE A 1377 ? LYS A 1380 ? PHE A 1377 LYS A 1380 
AE 2 ARG A 1401 ? TYR A 1408 ? ARG A 1401 TYR A 1408 
AE 3 THR A 1383 ? GLN A 1384 ? THR A 1383 GLN A 1384 
AF 1 PHE A 1377 ? LYS A 1380 ? PHE A 1377 LYS A 1380 
AF 2 ARG A 1401 ? TYR A 1408 ? ARG A 1401 TYR A 1408 
AF 3 LEU A 1473 ? PHE A 1480 ? LEU A 1473 PHE A 1480 
AF 4 SER A 1433 ? ALA A 1434 ? SER A 1433 ALA A 1434 
AG 1 ILE A 1455 ? LYS A 1456 ? ILE A 1455 LYS A 1456 
AG 2 HIS A 1459 ? LEU A 1464 ? HIS A 1459 LEU A 1464 
AG 3 ALA A 1422 ? SER A 1427 ? ALA A 1422 SER A 1427 
AG 4 ALA A 1491 ? GLU A 1497 ? ALA A 1491 GLU A 1497 
AG 5 ARG A 1500 ? CYS A 1505 ? ARG A 1500 CYS A 1505 
AH 1 ILE A 1455 ? LYS A 1456 ? ILE A 1455 LYS A 1456 
AH 2 HIS A 1459 ? LEU A 1464 ? HIS A 1459 LEU A 1464 
AH 3 ALA A 1422 ? SER A 1427 ? ALA A 1422 SER A 1427 
AH 4 ALA A 1491 ? GLU A 1497 ? ALA A 1491 GLU A 1497 
AH 5 PHE A 1508 ? TYR A 1509 ? PHE A 1508 TYR A 1509 
AI 1 ALA A 1560 ? ILE A 1565 ? ALA A 1560 ILE A 1565 
AI 2 TYR A 1577 ? LYS A 1586 ? TYR A 1577 LYS A 1586 
AI 3 GLU A 1597 ? PHE A 1600 ? GLU A 1597 PHE A 1600 
AJ 1 TYR A 1617 ? LEU A 1618 ? TYR A 1617 LEU A 1618 
AJ 2 GLU A 1646 ? TYR A 1647 ? GLU A 1646 TYR A 1647 
AK 1 TYR B 57   ? VAL B 60   ? TYR X 57   VAL X 60   
AK 2 GLN B 101  ? VAL B 103  ? GLN X 101  VAL X 103  
AK 3 VAL B 122  ? THR B 123  ? VAL X 122  THR X 123  
AL 1 LEU B 109  ? ILE B 110  ? LEU X 109  ILE X 110  
AL 2 LEU B 116  ? SER B 117  ? LEU X 116  SER X 117  
AM 1 THR B 132  ? THR B 134  ? THR X 132  THR X 134  
AM 2 PHE B 153  ? ILE B 155  ? PHE X 153  ILE X 155  
AN 1 GLU B 159  ? SER B 161  ? GLU X 159  SER X 161  
AN 2 VAL B 215  ? ASN B 217  ? VAL X 215  ASN X 217  
AO 1 GLN C 80   ? LEU C 85   ? GLN B 80   LEU B 85   
AO 2 GLU C 37   ? VAL C 43   ? GLU B 37   VAL B 43   
AO 3 TYR C 23   ? PRO C 28   ? TYR B 23   PRO B 28   
AO 4 LEU C 651  ? PHE C 653  ? LEU B 651  PHE B 653  
AP 1 PHE C 31   ? ARG C 32   ? PHE B 31   ARG B 32   
AP 2 ILE C 119  ? THR C 120  ? ILE B 119  THR B 120  
AQ 1 SER C 65   ? HIS C 70   ? SER B 65   HIS B 70   
AQ 2 THR C 53   ? LYS C 57   ? THR B 53   LYS B 57   
AQ 3 VAL C 102  ? VAL C 107  ? VAL B 102  VAL B 107  
AQ 4 SER C 112  ? MET C 117  ? SER B 112  MET B 117  
AR 1 PHE C 125  ? THR C 130  ? PHE B 125  THR B 130  
AR 2 VAL C 143  ? LEU C 148  ? VAL B 143  LEU B 148  
AR 3 ILE C 182  ? ILE C 183  ? ILE B 182  ILE B 183  
AS 1 VAL C 134  ? TYR C 135  ? VAL B 134  TYR B 135  
AS 2 THR C 212  ? VAL C 219  ? THR B 212  VAL B 219  
AS 3 GLY C 197  ? TYR C 205  ? GLY B 197  TYR B 205  
AS 4 THR C 159  ? ILE C 164  ? THR B 159  ILE B 164  
AS 5 VAL C 174  ? GLU C 176  ? VAL B 174  GLU B 176  
AT 1 SER C 140  ? VAL C 141  ? SER B 140  VAL B 141  
AT 2 PHE C 188  ? LYS C 189  ? PHE B 188  LYS B 189  
AU 1 GLU C 221  ? TYR C 222  ? GLU B 221  TYR B 222  
AU 2 GLU C 764  ? ILE C 765  ? GLU B 764  ILE B 765  
AV 1 SER C 228  ? GLU C 232  ? SER B 228  GLU B 232  
AV 2 ILE C 248  ? TYR C 254  ? ILE B 248  TYR B 254  
AV 3 LYS C 258  ? VAL C 259  ? LYS B 258  VAL B 259  
AW 1 SER C 228  ? GLU C 232  ? SER B 228  GLU B 232  
AW 2 ILE C 248  ? TYR C 254  ? ILE B 248  TYR B 254  
AW 3 ALA C 297  ? VAL C 299  ? ALA B 297  VAL B 299  
AX 1 PHE C 237  ? ILE C 238  ? PHE B 237  ILE B 238  
AX 2 LYS C 346  ? TYR C 347  ? LYS B 346  TYR B 347  
AY 1 ALA C 263  ? VAL C 265  ? ALA B 263  VAL B 265  
AY 2 TYR C 322  ? GLU C 331  ? TYR B 322  GLU B 331  
AY 3 THR C 268  ? ARG C 272  ? THR B 268  ARG B 272  
AZ 1 ALA C 263  ? VAL C 265  ? ALA B 263  VAL B 265  
AZ 2 TYR C 322  ? GLU C 331  ? TYR B 322  GLU B 331  
AZ 3 GLU C 338  ? ILE C 342  ? GLU B 338  ILE B 342  
BA 1 TYR C 369  ? PRO C 370  ? TYR B 369  PRO B 370  
BA 2 VAL C 421  ? LEU C 422  ? VAL B 421  LEU B 422  
BB 1 VAL C 373  ? GLN C 374  ? VAL B 373  GLN B 374  
BB 2 VAL C 417  ? ALA C 418  ? VAL B 417  ALA B 418  
BC 1 THR C 401  ? ASP C 403  ? THR B 401  ASP B 403  
BC 2 PRO C 387  ? ASP C 396  ? PRO B 387  ASP B 396  
BC 3 SER C 407  ? VAL C 410  ? SER B 407  VAL B 410  
BD 1 THR C 401  ? ASP C 403  ? THR B 401  ASP B 403  
BD 2 PRO C 387  ? ASP C 396  ? PRO B 387  ASP B 396  
BD 3 VAL C 428  ? THR C 437  ? VAL B 428  THR B 437  
BD 4 ARG C 449  ? ILE C 455  ? ARG B 449  ILE B 455  
BE 1 TYR C 466  ? TRP C 469  ? TYR B 466  TRP B 469  
BE 2 HIS C 481  ? THR C 487  ? HIS B 481  THR B 487  
BE 3 GLN C 524  ? PRO C 529  ? GLN B 524  PRO B 529  
BF 1 ALA C 552  ? ASN C 562  ? ALA B 552  ASN B 562  
BF 2 SER C 537  ? THR C 547  ? SER B 537  THR B 547  
BF 3 HIS C 498  ? LEU C 504  ? HIS B 498  LEU B 504  
BF 4 ILE C 509  ? GLU C 516  ? ILE B 509  GLU B 516  
BF 5 ASP D 145  ? ILE D 150  ? ASP Y 145  ILE Y 150  
BF 6 LEU D 136  ? ASN D 142  ? LEU Y 136  ASN Y 142  
BF 7 ILE D 224  ? ASN D 229  ? ILE Y 224  ASN Y 229  
BF 8 TYR D 186  ? ILE D 189  ? TYR Y 186  ILE Y 189  
BG 1 HIS C 574  ? LEU C 575  ? HIS B 574  LEU B 575  
BG 2 LEU C 590  ? ALA C 593  ? LEU B 590  ALA B 593  
BG 3 ARG C 783  ? GLN C 785  ? ARG B 783  GLN B 785  
BH 1 SER C 598  ? TRP C 599  ? SER B 598  TRP B 599  
BH 2 LEU C 779  ? VAL C 780  ? LEU B 779  VAL B 780  
BI 1 VAL C 605  ? ASP C 606  ? VAL B 605  ASP B 606  
BI 2 THR C 795  ? GLU C 798  ? THR B 795  GLU B 798  
BI 3 LYS C 816  ? VAL C 819  ? LYS B 816  VAL B 819  
BJ 1 ILE C 804  ? SER C 805  ? ILE B 804  SER B 805  
BJ 2 GLY C 808  ? ILE C 809  ? GLY B 808  ILE B 809  
BK 1 VAL C 823  ? MET C 827  ? VAL B 823  MET B 827  
BK 2 ILE C 839  ? ASN C 847  ? ILE B 839  ASN B 847  
BK 3 SER C 893  ? PRO C 902  ? SER B 893  PRO B 902  
BK 4 ILE C 865  ? CYS C 866  ? ILE B 865  CYS B 866  
BL 1 SER C 832  ? VAL C 834  ? SER B 832  VAL B 834  
BL 2 ARG C 928  ? VAL C 930  ? ARG B 928  VAL B 930  
BM 1 MET C 853  ? GLN C 854  ? MET B 853  GLN B 854  
BM 2 LYS C 887  ? VAL C 888  ? LYS B 887  VAL B 888  
BN 1 LYS C 858  ? MET C 859  ? LYS B 858  MET B 859  
BN 2 ILE C 910  ? THR C 916  ? ILE B 910  THR B 916  
BN 3 GLY C 919  ? LYS C 925  ? GLY B 919  LYS B 925  
BO 1 VAL C 934  ? GLU C 937  ? VAL B 934  GLU B 937  
BO 2 ALA C 1357 ? HIS C 1366 ? ALA B 1357 HIS B 1366 
BO 3 GLY C 941  ? LEU C 944  ? GLY B 941  LEU B 944  
BP 1 VAL C 934  ? GLU C 937  ? VAL B 934  GLU B 937  
BP 2 ALA C 1357 ? HIS C 1366 ? ALA B 1357 HIS B 1366 
BP 3 LYS C 974  ? GLY C 981  ? LYS B 974  GLY B 981  
BP 4 VAL C 1338 ? GLU C 1339 ? VAL B 1338 GLU B 1339 
BQ 1 LYS C 957  ? PHE C 959  ? LYS B 957  PHE B 959  
BQ 2 LEU C 1346 ? VAL C 1348 ? LEU B 1346 VAL B 1348 
BR 1 LEU C 1217 ? LYS C 1219 ? LEU B 1217 LYS B 1219 
BR 2 TYR C 1225 ? PHE C 1227 ? TYR B 1225 PHE B 1227 
BS 1 PHE C 1377 ? LYS C 1380 ? PHE B 1377 LYS B 1380 
BS 2 ARG C 1401 ? TYR C 1408 ? ARG B 1401 TYR B 1408 
BS 3 THR C 1383 ? GLN C 1384 ? THR B 1383 GLN B 1384 
BT 1 PHE C 1377 ? LYS C 1380 ? PHE B 1377 LYS B 1380 
BT 2 ARG C 1401 ? TYR C 1408 ? ARG B 1401 TYR B 1408 
BT 3 LEU C 1473 ? PHE C 1480 ? LEU B 1473 PHE B 1480 
BT 4 SER C 1433 ? ALA C 1434 ? SER B 1433 ALA B 1434 
BU 1 ILE C 1455 ? LYS C 1456 ? ILE B 1455 LYS B 1456 
BU 2 HIS C 1459 ? LEU C 1464 ? HIS B 1459 LEU B 1464 
BU 3 ALA C 1422 ? SER C 1427 ? ALA B 1422 SER B 1427 
BU 4 ALA C 1491 ? GLU C 1497 ? ALA B 1491 GLU B 1497 
BU 5 CYS C 1505 ? TYR C 1509 ? CYS B 1505 TYR B 1509 
BV 1 TYR D 57   ? VAL D 60   ? TYR Y 57   VAL Y 60   
BV 2 GLN D 101  ? VAL D 103  ? GLN Y 101  VAL Y 103  
BV 3 VAL D 122  ? THR D 123  ? VAL Y 122  THR Y 123  
BW 1 LEU D 109  ? ILE D 110  ? LEU Y 109  ILE Y 110  
BW 2 LEU D 116  ? SER D 117  ? LEU Y 116  SER Y 117  
BX 1 THR D 132  ? THR D 134  ? THR Y 132  THR Y 134  
BX 2 PHE D 153  ? ILE D 155  ? PHE Y 153  ILE Y 155  
BY 1 GLU D 159  ? SER D 161  ? GLU Y 159  SER Y 161  
BY 2 VAL D 215  ? ASN D 217  ? VAL Y 215  ASN Y 217  
BZ 1 ILE D 191  ? LYS D 194  ? ILE Y 191  LYS Y 194  
BZ 2 ASN D 197  ? VAL D 199  ? ASN Y 197  VAL Y 199  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A  1 2 O ASN A 81   ? O ASN A 81   N ILE A 41   ? N ILE A 41   
A  2 3 O GLN A 42   ? O GLN A 42   N VAL A 24   ? N VAL A 24   
A  3 4 N ALA A 27   ? N ALA A 27   O THR A 652  ? O THR A 652  
B  1 2 N PHE A 31   ? N PHE A 31   O THR A 120  ? O THR A 120  
C  1 2 O SER A 67   ? O SER A 67   N ILE A 56   ? N ILE A 56   
C  2 3 N LYS A 57   ? N LYS A 57   O TYR A 103  ? O TYR A 103  
C  3 4 N VAL A 102  ? N VAL A 102  O MET A 117  ? O MET A 117  
D  1 2 N PHE A 125  ? N PHE A 125  O LEU A 148  ? O LEU A 148  
D  2 3 N VAL A 145  ? N VAL A 145  O ILE A 183  ? O ILE A 183  
E  1 2 N TYR A 135  ? N TYR A 135  O GLU A 218  ? O GLU A 218  
E  2 3 O GLY A 213  ? O GLY A 213  N ALA A 203  ? N ALA A 203  
E  3 4 O LYS A 204  ? O LYS A 204  N VAL A 160  ? N VAL A 160  
E  4 5 N LEU A 161  ? N LEU A 161  O VAL A 174  ? O VAL A 174  
F  1 2 N VAL A 141  ? N VAL A 141  O PHE A 188  ? O PHE A 188  
G  1 2 N GLU A 221  ? N GLU A 221  O ILE A 765  ? O ILE A 765  
H  1 2 N GLU A 232  ? N GLU A 232  O THR A 249  ? O THR A 249  
H  2 3 N TYR A 254  ? N TYR A 254  O LYS A 258  ? O LYS A 258  
I  1 2 N GLU A 232  ? N GLU A 232  O THR A 249  ? O THR A 249  
I  2 3 N ILE A 248  ? N ILE A 248  O VAL A 299  ? O VAL A 299  
J  1 2 N ILE A 238  ? N ILE A 238  O LYS A 346  ? O LYS A 346  
K  1 2 N ASP A 264  ? N ASP A 264  O ILE A 330  ? O ILE A 330  
K  2 3 O TYR A 324  ? O TYR A 324  N GLY A 270  ? N GLY A 270  
L  1 2 N ASP A 264  ? N ASP A 264  O ILE A 330  ? O ILE A 330  
L  2 3 N ILE A 325  ? N ILE A 325  O ILE A 342  ? O ILE A 342  
M  1 2 N TYR A 369  ? N TYR A 369  O LEU A 422  ? O LEU A 422  
N  1 2 N VAL A 373  ? N VAL A 373  O ALA A 418  ? O ALA A 418  
O  1 2 O SER A 402  ? O SER A 402  N THR A 394  ? N THR A 394  
O  2 3 N LEU A 390  ? N LEU A 390  O SER A 407  ? O SER A 407  
P  1 2 O SER A 402  ? O SER A 402  N THR A 394  ? N THR A 394  
P  2 3 N GLN A 393  ? N GLN A 393  O GLU A 432  ? O GLU A 432  
P  3 4 N LEU A 431  ? N LEU A 431  O ALA A 454  ? O ALA A 454  
Q  1 2 N TYR A 466  ? N TYR A 466  O THR A 487  ? O THR A 487  
Q  2 3 N LEU A 482  ? N LEU A 482  O ILE A 528  ? O ILE A 528  
R  1 2 O GLU A 553  ? O GLU A 553  N VAL A 546  ? N VAL A 546  
R  2 3 O TYR A 543  ? O TYR A 543  N ASN A 500  ? N ASN A 500  
R  3 4 N ILE A 503  ? N ILE A 503  O ILE A 510  ? O ILE A 510  
R  4 5 N PHE A 512  ? N PHE A 512  O ALA B 148  ? O ALA X 148  
R  5 6 O ASP B 145  ? O ASP X 145  N ASN B 142  ? N ASN X 142  
R  6 7 N VAL B 141  ? N VAL X 141  O ILE B 228  ? O ILE X 228  
R  7 8 O SER B 225  ? O SER X 225  N ILE B 190  ? N ILE X 190  
R  8 9 N LYS B 194  ? N LYS X 194  O ASN B 197  ? O ASN X 197  
S  1 2 N HIS A 574  ? N HIS A 574  O ASN A 591  ? O ASN A 591  
S  2 3 N MET A 592  ? N MET A 592  O LYS A 784  ? O LYS A 784  
T  1 2 N SER A 598  ? N SER A 598  O VAL A 780  ? O VAL A 780  
U  1 2 N VAL A 605  ? N VAL A 605  O GLU A 798  ? O GLU A 798  
U  2 3 N THR A 795  ? N THR A 795  O VAL A 819  ? O VAL A 819  
V  1 2 N SER A 805  ? N SER A 805  O GLY A 808  ? O GLY A 808  
W  1 2 N PHE A 824  ? N PHE A 824  O TYR A 846  ? O TYR A 846  
W  2 3 N LEU A 841  ? N LEU A 841  O PHE A 898  ? O PHE A 898  
W  3 4 O LEU A 901  ? O LEU A 901  N CYS A 866  ? N CYS A 866  
X  1 2 N VAL A 833  ? N VAL A 833  O VAL A 930  ? O VAL A 930  
Y  1 2 N MET A 853  ? N MET A 853  O VAL A 888  ? O VAL A 888  
Z  1 2 N LYS A 858  ? N LYS A 858  O SER A 913  ? O SER A 913  
Z  2 3 N THR A 916  ? N THR A 916  O GLY A 919  ? O GLY A 919  
AA 1 2 N LYS A 935  ? N LYS A 935  O VAL A 1365 ? O VAL A 1365 
AA 2 3 O VAL A 1359 ? O VAL A 1359 N VAL A 942  ? N VAL A 942  
AB 1 2 N LYS A 935  ? N LYS A 935  O VAL A 1365 ? O VAL A 1365 
AB 2 3 O HIS A 1360 ? O HIS A 1360 N SER A 978  ? N SER A 978  
AB 3 4 N LEU A 977  ? N LEU A 977  O VAL A 1338 ? O VAL A 1338 
AC 1 2 N PHE A 959  ? N PHE A 959  O LEU A 1346 ? O LEU A 1346 
AD 1 2 N LYS A 1219 ? N LYS A 1219 O TYR A 1225 ? O TYR A 1225 
AE 1 2 N TYR A 1378 ? N TYR A 1378 O SER A 1407 ? O SER A 1407 
AE 2 3 O ARG A 1401 ? O ARG A 1401 N GLN A 1384 ? N GLN A 1384 
AF 1 2 N TYR A 1378 ? N TYR A 1378 O SER A 1407 ? O SER A 1407 
AF 2 3 N ILE A 1402 ? N ILE A 1402 O PHE A 1477 ? O PHE A 1477 
AF 3 4 O PHE A 1480 ? O PHE A 1480 N SER A 1433 ? N SER A 1433 
AG 1 2 N LYS A 1456 ? N LYS A 1456 O HIS A 1459 ? O HIS A 1459 
AG 2 3 O LEU A 1464 ? O LEU A 1464 N ALA A 1422 ? N ALA A 1422 
AG 3 4 N ASP A 1425 ? N ASP A 1425 O THR A 1494 ? O THR A 1494 
AG 4 5 N VAL A 1495 ? N VAL A 1495 O CYS A 1505 ? O CYS A 1505 
AH 1 2 N LYS A 1456 ? N LYS A 1456 O HIS A 1459 ? O HIS A 1459 
AH 2 3 O LEU A 1464 ? O LEU A 1464 N ALA A 1422 ? N ALA A 1422 
AH 3 4 N ASP A 1425 ? N ASP A 1425 O THR A 1494 ? O THR A 1494 
AH 4 5 N ALA A 1491 ? N ALA A 1491 O TYR A 1509 ? O TYR A 1509 
AI 1 2 N SER A 1564 ? N SER A 1564 O THR A 1580 ? O THR A 1580 
AI 2 3 N ALA A 1579 ? N ALA A 1579 O ILE A 1598 ? O ILE A 1598 
AJ 1 2 N LEU A 1618 ? N LEU A 1618 O GLU A 1646 ? O GLU A 1646 
AK 1 2 N TYR B 57   ? N TYR X 57   O VAL B 103  ? O VAL X 103  
AK 2 3 N ASN B 102  ? N ASN X 102  O THR B 123  ? O THR X 123  
AL 1 2 N LEU B 109  ? N LEU X 109  O SER B 117  ? O SER X 117  
AM 1 2 N THR B 134  ? N THR X 134  O PHE B 153  ? O PHE X 153  
AN 1 2 N ILE B 160  ? N ILE X 160  O LEU B 216  ? O LEU X 216  
AO 1 2 O ASN C 81   ? O ASN B 81   N ILE C 41   ? N ILE B 41   
AO 2 3 O GLN C 42   ? O GLN B 42   N VAL C 24   ? N VAL B 24   
AO 3 4 N ALA C 27   ? N ALA B 27   O THR C 652  ? O THR B 652  
AP 1 2 N PHE C 31   ? N PHE B 31   O THR C 120  ? O THR B 120  
AQ 1 2 O SER C 67   ? O SER B 67   N ILE C 56   ? N ILE B 56   
AQ 2 3 N LYS C 57   ? N LYS B 57   O TYR C 103  ? O TYR B 103  
AQ 3 4 N VAL C 102  ? N VAL B 102  O MET C 117  ? O MET B 117  
AR 1 2 N PHE C 127  ? N PHE B 127  O TYR C 146  ? O TYR B 146  
AR 2 3 N VAL C 145  ? N VAL B 145  O ILE C 183  ? O ILE B 183  
AS 1 2 N TYR C 135  ? N TYR B 135  O GLU C 218  ? O GLU B 218  
AS 2 3 O GLY C 213  ? O GLY B 213  N ALA C 203  ? N ALA B 203  
AS 3 4 O LYS C 204  ? O LYS B 204  N VAL C 160  ? N VAL B 160  
AS 4 5 N LEU C 161  ? N LEU B 161  O VAL C 174  ? O VAL B 174  
AT 1 2 N VAL C 141  ? N VAL B 141  O PHE C 188  ? O PHE B 188  
AU 1 2 N GLU C 221  ? N GLU B 221  O ILE C 765  ? O ILE B 765  
AV 1 2 N GLU C 232  ? N GLU B 232  O THR C 249  ? O THR B 249  
AV 2 3 N TYR C 254  ? N TYR B 254  O LYS C 258  ? O LYS B 258  
AW 1 2 N GLU C 232  ? N GLU B 232  O THR C 249  ? O THR B 249  
AW 2 3 N ILE C 248  ? N ILE B 248  O VAL C 299  ? O VAL B 299  
AX 1 2 N ILE C 238  ? N ILE B 238  O LYS C 346  ? O LYS B 346  
AY 1 2 N ASP C 264  ? N ASP B 264  O ILE C 330  ? O ILE B 330  
AY 2 3 O TYR C 324  ? O TYR B 324  N GLY C 270  ? N GLY B 270  
AZ 1 2 N ASP C 264  ? N ASP B 264  O ILE C 330  ? O ILE B 330  
AZ 2 3 N ILE C 325  ? N ILE B 325  O ILE C 342  ? O ILE B 342  
BA 1 2 N TYR C 369  ? N TYR B 369  O LEU C 422  ? O LEU B 422  
BB 1 2 N VAL C 373  ? N VAL B 373  O ALA C 418  ? O ALA B 418  
BC 1 2 O SER C 402  ? O SER B 402  N THR C 394  ? N THR B 394  
BC 2 3 N LEU C 390  ? N LEU B 390  O SER C 407  ? O SER B 407  
BD 1 2 O SER C 402  ? O SER B 402  N THR C 394  ? N THR B 394  
BD 2 3 N GLN C 393  ? N GLN B 393  O GLU C 432  ? O GLU B 432  
BD 3 4 N LEU C 431  ? N LEU B 431  O ALA C 454  ? O ALA B 454  
BE 1 2 N TYR C 466  ? N TYR B 466  O THR C 487  ? O THR B 487  
BE 2 3 N LEU C 482  ? N LEU B 482  O ILE C 528  ? O ILE B 528  
BF 1 2 O GLU C 553  ? O GLU B 553  N VAL C 546  ? N VAL B 546  
BF 2 3 O TYR C 543  ? O TYR B 543  N ASN C 500  ? N ASN B 500  
BF 3 4 N ILE C 503  ? N ILE B 503  O ILE C 510  ? O ILE B 510  
BF 4 5 N ILE C 510  ? N ILE B 510  O ILE D 150  ? O ILE Y 150  
BF 5 6 O ASP D 145  ? O ASP Y 145  N ASN D 142  ? N ASN Y 142  
BF 6 7 N VAL D 141  ? N VAL Y 141  O ILE D 228  ? O ILE Y 228  
BF 7 8 O ASN D 229  ? O ASN Y 229  N TYR D 186  ? N TYR Y 186  
BG 1 2 N HIS C 574  ? N HIS B 574  O ASN C 591  ? O ASN B 591  
BG 2 3 N MET C 592  ? N MET B 592  O LYS C 784  ? O LYS B 784  
BH 1 2 N SER C 598  ? N SER B 598  O VAL C 780  ? O VAL B 780  
BI 1 2 N VAL C 605  ? N VAL B 605  O GLU C 798  ? O GLU B 798  
BI 2 3 N THR C 795  ? N THR B 795  O VAL C 819  ? O VAL B 819  
BJ 1 2 N SER C 805  ? N SER B 805  O GLY C 808  ? O GLY B 808  
BK 1 2 N PHE C 824  ? N PHE B 824  O TYR C 846  ? O TYR B 846  
BK 2 3 N LEU C 841  ? N LEU B 841  O PHE C 898  ? O PHE B 898  
BK 3 4 O LEU C 901  ? O LEU B 901  N CYS C 866  ? N CYS B 866  
BL 1 2 N VAL C 833  ? N VAL B 833  O VAL C 930  ? O VAL B 930  
BM 1 2 N MET C 853  ? N MET B 853  O VAL C 888  ? O VAL B 888  
BN 1 2 N LYS C 858  ? N LYS B 858  O SER C 913  ? O SER B 913  
BN 2 3 N THR C 916  ? N THR B 916  O GLY C 919  ? O GLY B 919  
BO 1 2 N LYS C 935  ? N LYS B 935  O VAL C 1365 ? O VAL B 1365 
BO 2 3 O VAL C 1359 ? O VAL B 1359 N VAL C 942  ? N VAL B 942  
BP 1 2 N LYS C 935  ? N LYS B 935  O VAL C 1365 ? O VAL B 1365 
BP 2 3 O HIS C 1360 ? O HIS B 1360 N SER C 978  ? N SER B 978  
BP 3 4 N LEU C 977  ? N LEU B 977  O VAL C 1338 ? O VAL B 1338 
BQ 1 2 N PHE C 959  ? N PHE B 959  O LEU C 1346 ? O LEU B 1346 
BR 1 2 N LYS C 1219 ? N LYS B 1219 O TYR C 1225 ? O TYR B 1225 
BS 1 2 N TYR C 1378 ? N TYR B 1378 O SER C 1407 ? O SER B 1407 
BS 2 3 O ARG C 1401 ? O ARG B 1401 N GLN C 1384 ? N GLN B 1384 
BT 1 2 N TYR C 1378 ? N TYR B 1378 O SER C 1407 ? O SER B 1407 
BT 2 3 N ILE C 1402 ? N ILE B 1402 O PHE C 1477 ? O PHE B 1477 
BT 3 4 O PHE C 1480 ? O PHE B 1480 N SER C 1433 ? N SER B 1433 
BU 1 2 N LYS C 1456 ? N LYS B 1456 O HIS C 1459 ? O HIS B 1459 
BU 2 3 O LEU C 1464 ? O LEU B 1464 N ALA C 1422 ? N ALA B 1422 
BU 3 4 N ASP C 1425 ? N ASP B 1425 O THR C 1494 ? O THR B 1494 
BU 4 5 N PHE C 1493 ? N PHE B 1493 O MET C 1507 ? O MET B 1507 
BV 1 2 N TYR D 57   ? N TYR Y 57   O VAL D 103  ? O VAL Y 103  
BV 2 3 N ASN D 102  ? N ASN Y 102  O THR D 123  ? O THR Y 123  
BW 1 2 N LEU D 109  ? N LEU Y 109  O SER D 117  ? O SER Y 117  
BX 1 2 N THR D 134  ? N THR Y 134  O PHE D 153  ? O PHE Y 153  
BY 1 2 N ILE D 160  ? N ILE Y 160  O LEU D 216  ? O LEU Y 216  
BZ 1 2 N LYS D 194  ? N LYS Y 194  O ASN D 197  ? O ASN Y 197  
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE CD A 1677'  
AC2 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 2001' 
AC3 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG A 2002' 
AC4 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE CD A 1678'  
AC5 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG B 2001' 
AC6 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG B 2002' 
AC7 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE CD A 1679'  
AC8 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE CD A 1680'  
AC9 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE CD A 1681'  
BC1 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE CD B 1677'  
BC2 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE CD B 1678'  
BC3 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE CD B 1679'  
BC4 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE CD B 1680'  
BC5 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG A 1682' 
BC6 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG B 1681' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 2 GLU A 247  ? GLU A 247  . ? 1_555 ? 
2  AC1 2 GLU C 247  ? GLU B 247  . ? 1_555 ? 
3  AC2 3 ASN A 911  ? ASN A 911  . ? 1_555 ? 
4  AC2 3 ILE A 922  ? ILE A 922  . ? 1_555 ? 
5  AC2 3 NAG G .    ? NAG A 2002 . ? 1_555 ? 
6  AC3 1 NAG F .    ? NAG A 2001 . ? 1_555 ? 
7  AC4 3 ASP A 471  ? ASP A 471  . ? 1_555 ? 
8  AC4 3 HIS A 473  ? HIS A 473  . ? 1_555 ? 
9  AC4 3 GLU A 480  ? GLU A 480  . ? 1_555 ? 
10 AC5 3 ASN C 911  ? ASN B 911  . ? 1_555 ? 
11 AC5 3 ILE C 922  ? ILE B 922  . ? 1_555 ? 
12 AC5 3 NAG N .    ? NAG B 2002 . ? 1_555 ? 
13 AC6 1 NAG M .    ? NAG B 2001 . ? 1_555 ? 
14 AC7 2 ASP A 264  ? ASP A 264  . ? 1_555 ? 
15 AC7 2 HIS A 753  ? HIS A 753  . ? 1_555 ? 
16 AC8 2 GLU A 339  ? GLU A 339  . ? 1_555 ? 
17 AC8 2 GLU A 764  ? GLU A 764  . ? 1_555 ? 
18 AC9 3 GLN A 886  ? GLN A 886  . ? 1_555 ? 
19 AC9 3 HIS A 894  ? HIS A 894  . ? 1_555 ? 
20 AC9 3 GLU A 1589 ? GLU A 1589 . ? 1_555 ? 
21 BC1 3 ASP C 471  ? ASP B 471  . ? 1_555 ? 
22 BC1 3 HIS C 473  ? HIS B 473  . ? 1_555 ? 
23 BC1 3 GLU C 480  ? GLU B 480  . ? 1_555 ? 
24 BC2 2 ASP C 264  ? ASP B 264  . ? 1_555 ? 
25 BC2 2 HIS C 753  ? HIS B 753  . ? 1_555 ? 
26 BC3 2 GLU C 339  ? GLU B 339  . ? 1_555 ? 
27 BC3 2 GLU C 764  ? GLU B 764  . ? 1_555 ? 
28 BC4 3 GLU A 1666 ? GLU A 1666 . ? 1_555 ? 
29 BC4 3 GLN C 886  ? GLN B 886  . ? 1_555 ? 
30 BC4 3 HIS C 894  ? HIS B 894  . ? 1_555 ? 
31 BC5 1 ASN A 741  ? ASN A 741  . ? 1_555 ? 
32 BC6 1 ASN C 741  ? ASN B 741  . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          3KLS 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    3KLS 
_atom_sites.fract_transf_matrix[1][1]   0.006950 
_atom_sites.fract_transf_matrix[1][2]   0.004013 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008026 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.004145 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CD 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N   . THR A 1 22   ? -96.624  77.182  13.560  1.00 166.54 ? 22   THR A N   1 
ATOM   2     C  CA  . THR A 1 22   ? -95.561  76.824  12.624  1.00 164.61 ? 22   THR A CA  1 
ATOM   3     C  C   . THR A 1 22   ? -95.291  75.319  12.643  1.00 160.25 ? 22   THR A C   1 
ATOM   4     O  O   . THR A 1 22   ? -95.710  74.620  13.563  1.00 158.38 ? 22   THR A O   1 
ATOM   5     C  CB  . THR A 1 22   ? -94.269  77.625  12.914  1.00 163.74 ? 22   THR A CB  1 
ATOM   6     O  OG1 . THR A 1 22   ? -94.238  78.006  14.304  1.00 161.18 ? 22   THR A OG1 1 
ATOM   7     C  CG2 . THR A 1 22   ? -94.211  78.881  12.017  1.00 165.11 ? 22   THR A CG2 1 
ATOM   8     N  N   . TYR A 1 23   ? -94.624  74.822  11.609  1.00 159.92 ? 23   TYR A N   1 
ATOM   9     C  CA  . TYR A 1 23   ? -94.239  73.424  11.576  1.00 163.10 ? 23   TYR A CA  1 
ATOM   10    C  C   . TYR A 1 23   ? -92.744  73.217  11.756  1.00 161.48 ? 23   TYR A C   1 
ATOM   11    O  O   . TYR A 1 23   ? -91.936  74.066  11.374  1.00 159.80 ? 23   TYR A O   1 
ATOM   12    C  CB  . TYR A 1 23   ? -94.664  72.760  10.281  1.00 170.03 ? 23   TYR A CB  1 
ATOM   13    C  CG  . TYR A 1 23   ? -94.479  73.618  9.050   1.00 178.05 ? 23   TYR A CG  1 
ATOM   14    C  CD1 . TYR A 1 23   ? -93.552  74.664  9.021   1.00 179.28 ? 23   TYR A CD1 1 
ATOM   15    C  CD2 . TYR A 1 23   ? -95.237  73.367  7.897   1.00 183.41 ? 23   TYR A CD2 1 
ATOM   16    C  CE1 . TYR A 1 23   ? -93.402  75.441  7.880   1.00 182.70 ? 23   TYR A CE1 1 
ATOM   17    C  CE2 . TYR A 1 23   ? -95.097  74.128  6.756   1.00 185.62 ? 23   TYR A CE2 1 
ATOM   18    C  CZ  . TYR A 1 23   ? -94.180  75.160  6.743   1.00 186.08 ? 23   TYR A CZ  1 
ATOM   19    O  OH  . TYR A 1 23   ? -94.062  75.900  5.581   1.00 187.78 ? 23   TYR A OH  1 
ATOM   20    N  N   . VAL A 1 24   ? -92.402  72.060  12.325  1.00 161.02 ? 24   VAL A N   1 
ATOM   21    C  CA  . VAL A 1 24   ? -91.031  71.600  12.490  1.00 157.19 ? 24   VAL A CA  1 
ATOM   22    C  C   . VAL A 1 24   ? -90.948  70.164  12.004  1.00 154.56 ? 24   VAL A C   1 
ATOM   23    O  O   . VAL A 1 24   ? -91.765  69.311  12.348  1.00 154.28 ? 24   VAL A O   1 
ATOM   24    C  CB  . VAL A 1 24   ? -90.558  71.686  13.955  1.00 158.12 ? 24   VAL A CB  1 
ATOM   25    C  CG1 . VAL A 1 24   ? -89.389  70.721  14.226  1.00 157.50 ? 24   VAL A CG1 1 
ATOM   26    C  CG2 . VAL A 1 24   ? -90.183  73.126  14.307  1.00 157.29 ? 24   VAL A CG2 1 
ATOM   27    N  N   . ILE A 1 25   ? -89.944  69.917  11.184  1.00 154.59 ? 25   ILE A N   1 
ATOM   28    C  CA  . ILE A 1 25   ? -89.752  68.631  10.555  1.00 158.81 ? 25   ILE A CA  1 
ATOM   29    C  C   . ILE A 1 25   ? -88.272  68.359  10.654  1.00 156.59 ? 25   ILE A C   1 
ATOM   30    O  O   . ILE A 1 25   ? -87.482  68.817  9.827   1.00 157.03 ? 25   ILE A O   1 
ATOM   31    C  CB  . ILE A 1 25   ? -90.137  68.692  9.065   1.00 165.37 ? 25   ILE A CB  1 
ATOM   32    C  CG1 . ILE A 1 25   ? -91.633  69.001  8.905   1.00 170.46 ? 25   ILE A CG1 1 
ATOM   33    C  CG2 . ILE A 1 25   ? -89.739  67.398  8.352   1.00 166.94 ? 25   ILE A CG2 1 
ATOM   34    C  CD1 . ILE A 1 25   ? -92.503  67.784  8.756   1.00 173.05 ? 25   ILE A CD1 1 
ATOM   35    N  N   . SER A 1 26   ? -87.883  67.635  11.684  1.00 153.22 ? 26   SER A N   1 
ATOM   36    C  CA  . SER A 1 26   ? -86.474  67.453  11.928  1.00 150.05 ? 26   SER A CA  1 
ATOM   37    C  C   . SER A 1 26   ? -85.949  66.314  11.085  1.00 144.74 ? 26   SER A C   1 
ATOM   38    O  O   . SER A 1 26   ? -86.714  65.435  10.682  1.00 144.88 ? 26   SER A O   1 
ATOM   39    C  CB  . SER A 1 26   ? -86.247  67.186  13.410  1.00 152.34 ? 26   SER A CB  1 
ATOM   40    O  OG  . SER A 1 26   ? -86.863  68.201  14.179  1.00 153.89 ? 26   SER A OG  1 
ATOM   41    N  N   . ALA A 1 27   ? -84.648  66.341  10.810  1.00 138.46 ? 27   ALA A N   1 
ATOM   42    C  CA  . ALA A 1 27   ? -83.988  65.203  10.188  1.00 135.63 ? 27   ALA A CA  1 
ATOM   43    C  C   . ALA A 1 27   ? -82.481  65.386  10.132  1.00 129.14 ? 27   ALA A C   1 
ATOM   44    O  O   . ALA A 1 27   ? -81.982  66.507  10.219  1.00 126.99 ? 27   ALA A O   1 
ATOM   45    C  CB  . ALA A 1 27   ? -84.541  64.955  8.807   1.00 136.94 ? 27   ALA A CB  1 
ATOM   46    N  N   . PRO A 1 28   ? -81.752  64.273  9.975   1.00 129.27 ? 28   PRO A N   1 
ATOM   47    C  CA  . PRO A 1 28   ? -80.290  64.255  9.993   1.00 130.13 ? 28   PRO A CA  1 
ATOM   48    C  C   . PRO A 1 28   ? -79.662  65.324  9.114   1.00 134.52 ? 28   PRO A C   1 
ATOM   49    O  O   . PRO A 1 28   ? -80.324  65.902  8.266   1.00 137.36 ? 28   PRO A O   1 
ATOM   50    C  CB  . PRO A 1 28   ? -79.975  62.871  9.445   1.00 127.78 ? 28   PRO A CB  1 
ATOM   51    C  CG  . PRO A 1 28   ? -81.101  62.040  9.937   1.00 127.67 ? 28   PRO A CG  1 
ATOM   52    C  CD  . PRO A 1 28   ? -82.310  62.916  9.840   1.00 128.22 ? 28   PRO A CD  1 
ATOM   53    N  N   . LYS A 1 29   ? -78.385  65.595  9.342   1.00 137.49 ? 29   LYS A N   1 
ATOM   54    C  CA  . LYS A 1 29   ? -77.633  66.514  8.496   1.00 138.50 ? 29   LYS A CA  1 
ATOM   55    C  C   . LYS A 1 29   ? -77.364  65.843  7.122   1.00 139.92 ? 29   LYS A C   1 
ATOM   56    O  O   . LYS A 1 29   ? -77.291  66.514  6.076   1.00 138.77 ? 29   LYS A O   1 
ATOM   57    C  CB  . LYS A 1 29   ? -76.341  66.965  9.222   1.00 139.00 ? 29   LYS A CB  1 
ATOM   58    C  CG  . LYS A 1 29   ? -75.352  67.849  8.421   1.00 142.21 ? 29   LYS A CG  1 
ATOM   59    C  CD  . LYS A 1 29   ? -76.005  69.037  7.659   1.00 185.79 ? 29   LYS A CD  1 
ATOM   60    C  CE  . LYS A 1 29   ? -75.413  69.177  6.225   1.00 178.58 ? 29   LYS A CE  1 
ATOM   61    N  NZ  . LYS A 1 29   ? -75.793  70.409  5.467   1.00 178.28 ? 29   LYS A NZ  1 
ATOM   62    N  N   . ILE A 1 30   ? -77.262  64.514  7.126   1.00 138.84 ? 30   ILE A N   1 
ATOM   63    C  CA  . ILE A 1 30   ? -76.993  63.750  5.904   1.00 138.19 ? 30   ILE A CA  1 
ATOM   64    C  C   . ILE A 1 30   ? -77.957  62.573  5.809   1.00 136.82 ? 30   ILE A C   1 
ATOM   65    O  O   . ILE A 1 30   ? -78.502  62.137  6.819   1.00 136.52 ? 30   ILE A O   1 
ATOM   66    C  CB  . ILE A 1 30   ? -75.529  63.185  5.871   1.00 129.72 ? 30   ILE A CB  1 
ATOM   67    C  CG1 . ILE A 1 30   ? -74.507  64.313  5.943   1.00 129.15 ? 30   ILE A CG1 1 
ATOM   68    C  CG2 . ILE A 1 30   ? -75.266  62.373  4.601   1.00 128.57 ? 30   ILE A CG2 1 
ATOM   69    C  CD1 . ILE A 1 30   ? -74.571  65.276  4.773   1.00 130.38 ? 30   ILE A CD1 1 
ATOM   70    N  N   . PHE A 1 31   ? -78.196  62.074  4.597   1.00 134.84 ? 31   PHE A N   1 
ATOM   71    C  CA  . PHE A 1 31   ? -78.824  60.767  4.457   1.00 132.64 ? 31   PHE A CA  1 
ATOM   72    C  C   . PHE A 1 31   ? -77.813  59.697  4.089   1.00 131.20 ? 31   PHE A C   1 
ATOM   73    O  O   . PHE A 1 31   ? -76.652  59.962  3.728   1.00 128.31 ? 31   PHE A O   1 
ATOM   74    C  CB  . PHE A 1 31   ? -79.968  60.748  3.448   1.00 132.23 ? 31   PHE A CB  1 
ATOM   75    C  CG  . PHE A 1 31   ? -81.072  61.733  3.746   1.00 133.80 ? 31   PHE A CG  1 
ATOM   76    C  CD1 . PHE A 1 31   ? -81.327  62.802  2.876   1.00 134.44 ? 31   PHE A CD1 1 
ATOM   77    C  CD2 . PHE A 1 31   ? -81.872  61.597  4.868   1.00 133.37 ? 31   PHE A CD2 1 
ATOM   78    C  CE1 . PHE A 1 31   ? -82.351  63.724  3.120   1.00 133.24 ? 31   PHE A CE1 1 
ATOM   79    C  CE2 . PHE A 1 31   ? -82.895  62.518  5.118   1.00 133.75 ? 31   PHE A CE2 1 
ATOM   80    C  CZ  . PHE A 1 31   ? -83.131  63.584  4.239   1.00 133.35 ? 31   PHE A CZ  1 
ATOM   81    N  N   . ARG A 1 32   ? -78.284  58.466  4.178   1.00 132.71 ? 32   ARG A N   1 
ATOM   82    C  CA  . ARG A 1 32   ? -77.471  57.319  3.839   1.00 130.87 ? 32   ARG A CA  1 
ATOM   83    C  C   . ARG A 1 32   ? -78.323  56.365  3.047   1.00 127.78 ? 32   ARG A C   1 
ATOM   84    O  O   . ARG A 1 32   ? -79.519  56.165  3.320   1.00 126.38 ? 32   ARG A O   1 
ATOM   85    C  CB  . ARG A 1 32   ? -76.968  56.598  5.092   1.00 134.85 ? 32   ARG A CB  1 
ATOM   86    C  CG  . ARG A 1 32   ? -75.845  57.293  5.843   1.00 135.97 ? 32   ARG A CG  1 
ATOM   87    C  CD  . ARG A 1 32   ? -75.389  56.461  7.066   1.00 137.32 ? 32   ARG A CD  1 
ATOM   88    N  NE  . ARG A 1 32   ? -74.081  56.897  7.551   1.00 134.86 ? 32   ARG A NE  1 
ATOM   89    C  CZ  . ARG A 1 32   ? -73.850  57.470  8.723   1.00 133.69 ? 32   ARG A CZ  1 
ATOM   90    N  NH1 . ARG A 1 32   ? -74.836  57.675  9.597   1.00 134.31 ? 32   ARG A NH1 1 
ATOM   91    N  NH2 . ARG A 1 32   ? -72.611  57.827  9.006   1.00 131.81 ? 32   ARG A NH2 1 
ATOM   92    N  N   . VAL A 1 33   ? -77.674  55.790  2.054   1.00 124.86 ? 33   VAL A N   1 
ATOM   93    C  CA  . VAL A 1 33   ? -78.241  54.760  1.242   1.00 126.56 ? 33   VAL A CA  1 
ATOM   94    C  C   . VAL A 1 33   ? -78.448  53.518  2.082   1.00 128.78 ? 33   VAL A C   1 
ATOM   95    O  O   . VAL A 1 33   ? -77.648  53.223  2.943   1.00 127.62 ? 33   VAL A O   1 
ATOM   96    C  CB  . VAL A 1 33   ? -77.261  54.486  0.142   1.00 126.71 ? 33   VAL A CB  1 
ATOM   97    C  CG1 . VAL A 1 33   ? -77.900  53.633  -0.952  1.00 129.60 ? 33   VAL A CG1 1 
ATOM   98    C  CG2 . VAL A 1 33   ? -76.769  55.827  -0.390  1.00 125.75 ? 33   VAL A CG2 1 
ATOM   99    N  N   . GLY A 1 34   ? -79.537  52.800  1.849   1.00 133.49 ? 34   GLY A N   1 
ATOM   100   C  CA  . GLY A 1 34   ? -79.856  51.636  2.654   1.00 138.42 ? 34   GLY A CA  1 
ATOM   101   C  C   . GLY A 1 34   ? -80.135  52.026  4.093   1.00 142.35 ? 34   GLY A C   1 
ATOM   102   O  O   . GLY A 1 34   ? -80.280  51.181  4.985   1.00 143.68 ? 34   GLY A O   1 
ATOM   103   N  N   . ALA A 1 35   ? -80.200  53.326  4.328   1.00 143.88 ? 35   ALA A N   1 
ATOM   104   C  CA  . ALA A 1 35   ? -80.400  53.802  5.674   1.00 145.71 ? 35   ALA A CA  1 
ATOM   105   C  C   . ALA A 1 35   ? -81.846  54.174  5.888   1.00 150.13 ? 35   ALA A C   1 
ATOM   106   O  O   . ALA A 1 35   ? -82.426  54.909  5.082   1.00 148.89 ? 35   ALA A O   1 
ATOM   107   C  CB  . ALA A 1 35   ? -79.511  54.976  5.948   1.00 144.04 ? 35   ALA A CB  1 
ATOM   108   N  N   . SER A 1 36   ? -82.409  53.653  6.978   1.00 153.83 ? 36   SER A N   1 
ATOM   109   C  CA  . SER A 1 36   ? -83.757  53.986  7.416   1.00 155.93 ? 36   SER A CA  1 
ATOM   110   C  C   . SER A 1 36   ? -83.686  55.360  8.019   1.00 155.89 ? 36   SER A C   1 
ATOM   111   O  O   . SER A 1 36   ? -83.368  55.511  9.185   1.00 156.42 ? 36   SER A O   1 
ATOM   112   C  CB  . SER A 1 36   ? -84.214  53.014  8.495   1.00 155.36 ? 36   SER A CB  1 
ATOM   113   O  OG  . SER A 1 36   ? -83.314  51.920  8.594   1.00 154.14 ? 36   SER A OG  1 
ATOM   114   N  N   . GLU A 1 37   ? -83.967  56.376  7.225   1.00 157.30 ? 37   GLU A N   1 
ATOM   115   C  CA  . GLU A 1 37   ? -83.797  57.734  7.711   1.00 158.94 ? 37   GLU A CA  1 
ATOM   116   C  C   . GLU A 1 37   ? -84.985  58.208  8.558   1.00 158.05 ? 37   GLU A C   1 
ATOM   117   O  O   . GLU A 1 37   ? -86.107  58.377  8.061   1.00 158.22 ? 37   GLU A O   1 
ATOM   118   C  CB  . GLU A 1 37   ? -83.462  58.698  6.563   1.00 163.57 ? 37   GLU A CB  1 
ATOM   119   C  CG  . GLU A 1 37   ? -82.194  58.310  5.773   1.00 168.25 ? 37   GLU A CG  1 
ATOM   120   C  CD  . GLU A 1 37   ? -80.916  58.344  6.609   1.00 171.85 ? 37   GLU A CD  1 
ATOM   121   O  OE1 . GLU A 1 37   ? -80.904  57.835  7.757   1.00 173.35 ? 37   GLU A OE1 1 
ATOM   122   O  OE2 . GLU A 1 37   ? -79.910  58.884  6.108   1.00 172.80 ? 37   GLU A OE2 1 
ATOM   123   N  N   . ASN A 1 38   ? -84.714  58.399  9.848   1.00 155.46 ? 38   ASN A N   1 
ATOM   124   C  CA  . ASN A 1 38   ? -85.712  58.861  10.798  1.00 153.76 ? 38   ASN A CA  1 
ATOM   125   C  C   . ASN A 1 38   ? -86.019  60.347  10.667  1.00 151.86 ? 38   ASN A C   1 
ATOM   126   O  O   . ASN A 1 38   ? -85.106  61.175  10.675  1.00 150.57 ? 38   ASN A O   1 
ATOM   127   C  CB  . ASN A 1 38   ? -85.240  58.563  12.213  1.00 151.94 ? 38   ASN A CB  1 
ATOM   128   C  CG  . ASN A 1 38   ? -85.710  57.221  12.712  1.00 150.54 ? 38   ASN A CG  1 
ATOM   129   O  OD1 . ASN A 1 38   ? -85.542  56.198  12.049  1.00 150.23 ? 38   ASN A OD1 1 
ATOM   130   N  ND2 . ASN A 1 38   ? -86.308  57.219  13.895  1.00 149.79 ? 38   ASN A ND2 1 
ATOM   131   N  N   . ILE A 1 39   ? -87.313  60.665  10.571  1.00 151.10 ? 39   ILE A N   1 
ATOM   132   C  CA  . ILE A 1 39   ? -87.798  62.033  10.374  1.00 148.49 ? 39   ILE A CA  1 
ATOM   133   C  C   . ILE A 1 39   ? -89.056  62.312  11.186  1.00 147.27 ? 39   ILE A C   1 
ATOM   134   O  O   . ILE A 1 39   ? -90.152  61.917  10.786  1.00 147.29 ? 39   ILE A O   1 
ATOM   135   C  CB  . ILE A 1 39   ? -88.192  62.277  8.901   1.00 147.88 ? 39   ILE A CB  1 
ATOM   136   C  CG1 . ILE A 1 39   ? -87.197  61.607  7.956   1.00 145.61 ? 39   ILE A CG1 1 
ATOM   137   C  CG2 . ILE A 1 39   ? -88.344  63.767  8.620   1.00 147.98 ? 39   ILE A CG2 1 
ATOM   138   C  CD1 . ILE A 1 39   ? -85.781  62.102  8.097   1.00 142.11 ? 39   ILE A CD1 1 
ATOM   139   N  N   . VAL A 1 40   ? -88.908  62.993  12.322  1.00 148.47 ? 40   VAL A N   1 
ATOM   140   C  CA  . VAL A 1 40   ? -90.086  63.413  13.087  1.00 152.10 ? 40   VAL A CA  1 
ATOM   141   C  C   . VAL A 1 40   ? -90.730  64.624  12.440  1.00 156.09 ? 40   VAL A C   1 
ATOM   142   O  O   . VAL A 1 40   ? -90.072  65.452  11.791  1.00 153.97 ? 40   VAL A O   1 
ATOM   143   C  CB  . VAL A 1 40   ? -89.850  63.730  14.629  1.00 156.44 ? 40   VAL A CB  1 
ATOM   144   C  CG1 . VAL A 1 40   ? -88.906  62.733  15.285  1.00 155.95 ? 40   VAL A CG1 1 
ATOM   145   C  CG2 . VAL A 1 40   ? -89.393  65.175  14.866  1.00 155.08 ? 40   VAL A CG2 1 
ATOM   146   N  N   . ILE A 1 41   ? -92.039  64.701  12.629  1.00 160.25 ? 41   ILE A N   1 
ATOM   147   C  CA  . ILE A 1 41   ? -92.813  65.859  12.259  1.00 162.94 ? 41   ILE A CA  1 
ATOM   148   C  C   . ILE A 1 41   ? -93.718  66.111  13.419  1.00 161.70 ? 41   ILE A C   1 
ATOM   149   O  O   . ILE A 1 41   ? -94.260  65.196  14.023  1.00 160.15 ? 41   ILE A O   1 
ATOM   150   C  CB  . ILE A 1 41   ? -93.703  65.615  11.057  1.00 169.94 ? 41   ILE A CB  1 
ATOM   151   C  CG1 . ILE A 1 41   ? -94.689  66.777  10.907  1.00 172.07 ? 41   ILE A CG1 1 
ATOM   152   C  CG2 . ILE A 1 41   ? -94.463  64.307  11.221  1.00 171.40 ? 41   ILE A CG2 1 
ATOM   153   C  CD1 . ILE A 1 41   ? -95.742  66.545  9.856   1.00 175.11 ? 41   ILE A CD1 1 
ATOM   154   N  N   . GLN A 1 42   ? -93.888  67.377  13.709  1.00 164.16 ? 42   GLN A N   1 
ATOM   155   C  CA  . GLN A 1 42   ? -94.584  67.795  14.891  1.00 169.86 ? 42   GLN A CA  1 
ATOM   156   C  C   . GLN A 1 42   ? -94.860  69.235  14.563  1.00 174.57 ? 42   GLN A C   1 
ATOM   157   O  O   . GLN A 1 42   ? -94.053  69.843  13.860  1.00 173.17 ? 42   GLN A O   1 
ATOM   158   C  CB  . GLN A 1 42   ? -93.644  67.670  16.085  1.00 170.59 ? 42   GLN A CB  1 
ATOM   159   C  CG  . GLN A 1 42   ? -93.638  68.851  17.006  1.00 171.56 ? 42   GLN A CG  1 
ATOM   160   C  CD  . GLN A 1 42   ? -92.242  69.189  17.435  1.00 171.64 ? 42   GLN A CD  1 
ATOM   161   O  OE1 . GLN A 1 42   ? -92.039  70.148  18.175  1.00 173.05 ? 42   GLN A OE1 1 
ATOM   162   N  NE2 . GLN A 1 42   ? -91.259  68.409  16.964  1.00 170.55 ? 42   GLN A NE2 1 
ATOM   163   N  N   . VAL A 1 43   ? -95.985  69.784  15.029  1.00 177.71 ? 43   VAL A N   1 
ATOM   164   C  CA  . VAL A 1 43   ? -96.381  71.119  14.591  1.00 176.09 ? 43   VAL A CA  1 
ATOM   165   C  C   . VAL A 1 43   ? -97.383  71.793  15.515  1.00 180.67 ? 43   VAL A C   1 
ATOM   166   O  O   . VAL A 1 43   ? -98.019  71.130  16.327  1.00 181.96 ? 43   VAL A O   1 
ATOM   167   C  CB  . VAL A 1 43   ? -96.908  71.066  13.152  1.00 170.86 ? 43   VAL A CB  1 
ATOM   168   C  CG1 . VAL A 1 43   ? -98.193  70.272  13.099  1.00 169.66 ? 43   VAL A CG1 1 
ATOM   169   C  CG2 . VAL A 1 43   ? -97.077  72.448  12.602  1.00 167.51 ? 43   VAL A CG2 1 
ATOM   170   N  N   . TYR A 1 44   ? -97.484  73.117  15.392  1.00 184.54 ? 44   TYR A N   1 
ATOM   171   C  CA  . TYR A 1 44   ? -98.354  73.956  16.227  1.00 190.67 ? 44   TYR A CA  1 
ATOM   172   C  C   . TYR A 1 44   ? -99.754  74.270  15.613  1.00 209.79 ? 44   TYR A C   1 
ATOM   173   O  O   . TYR A 1 44   ? -100.448 75.195  16.050  1.00 206.75 ? 44   TYR A O   1 
ATOM   174   C  CB  . TYR A 1 44   ? -97.605  75.249  16.609  1.00 199.36 ? 44   TYR A CB  1 
ATOM   175   C  CG  . TYR A 1 44   ? -98.224  76.043  17.753  1.00 211.60 ? 44   TYR A CG  1 
ATOM   176   C  CD1 . TYR A 1 44   ? -98.026  75.666  19.083  1.00 215.67 ? 44   TYR A CD1 1 
ATOM   177   C  CD2 . TYR A 1 44   ? -99.000  77.179  17.503  1.00 217.81 ? 44   TYR A CD2 1 
ATOM   178   C  CE1 . TYR A 1 44   ? -98.593  76.389  20.126  1.00 218.09 ? 44   TYR A CE1 1 
ATOM   179   C  CE2 . TYR A 1 44   ? -99.568  77.910  18.543  1.00 220.29 ? 44   TYR A CE2 1 
ATOM   180   C  CZ  . TYR A 1 44   ? -99.359  77.511  19.849  1.00 219.80 ? 44   TYR A CZ  1 
ATOM   181   O  OH  . TYR A 1 44   ? -99.922  78.237  20.877  1.00 219.65 ? 44   TYR A OH  1 
ATOM   182   N  N   . GLY A 1 45   ? -100.168 73.491  14.615  1.00 214.31 ? 45   GLY A N   1 
ATOM   183   C  CA  . GLY A 1 45   ? -101.448 73.697  13.958  1.00 216.99 ? 45   GLY A CA  1 
ATOM   184   C  C   . GLY A 1 45   ? -102.615 73.610  14.922  1.00 217.07 ? 45   GLY A C   1 
ATOM   185   O  O   . GLY A 1 45   ? -102.610 72.808  15.850  1.00 214.25 ? 45   GLY A O   1 
ATOM   186   N  N   . TYR A 1 46   ? -103.617 74.449  14.691  1.00 221.24 ? 46   TYR A N   1 
ATOM   187   C  CA  . TYR A 1 46   ? -104.854 74.451  15.473  1.00 224.89 ? 46   TYR A CA  1 
ATOM   188   C  C   . TYR A 1 46   ? -105.573 73.092  15.509  1.00 225.21 ? 46   TYR A C   1 
ATOM   189   O  O   . TYR A 1 46   ? -104.989 72.061  15.176  1.00 229.58 ? 46   TYR A O   1 
ATOM   190   C  CB  . TYR A 1 46   ? -105.800 75.519  14.927  1.00 229.77 ? 46   TYR A CB  1 
ATOM   191   C  CG  . TYR A 1 46   ? -105.742 75.625  13.422  1.00 234.40 ? 46   TYR A CG  1 
ATOM   192   C  CD1 . TYR A 1 46   ? -106.454 74.744  12.616  1.00 237.45 ? 46   TYR A CD1 1 
ATOM   193   C  CD2 . TYR A 1 46   ? -104.959 76.594  12.805  1.00 235.59 ? 46   TYR A CD2 1 
ATOM   194   C  CE1 . TYR A 1 46   ? -106.396 74.832  11.235  1.00 239.80 ? 46   TYR A CE1 1 
ATOM   195   C  CE2 . TYR A 1 46   ? -104.894 76.691  11.426  1.00 237.80 ? 46   TYR A CE2 1 
ATOM   196   C  CZ  . TYR A 1 46   ? -105.614 75.808  10.644  1.00 240.22 ? 46   TYR A CZ  1 
ATOM   197   O  OH  . TYR A 1 46   ? -105.551 75.901  9.269   1.00 242.43 ? 46   TYR A OH  1 
ATOM   198   N  N   . THR A 1 47   ? -106.848 73.118  15.907  1.00 220.73 ? 47   THR A N   1 
ATOM   199   C  CA  . THR A 1 47   ? -107.649 71.915  16.195  1.00 216.72 ? 47   THR A CA  1 
ATOM   200   C  C   . THR A 1 47   ? -107.775 70.965  15.012  1.00 215.62 ? 47   THR A C   1 
ATOM   201   O  O   . THR A 1 47   ? -107.751 69.739  15.160  1.00 214.64 ? 47   THR A O   1 
ATOM   202   C  CB  . THR A 1 47   ? -109.099 72.289  16.636  1.00 268.51 ? 47   THR A CB  1 
ATOM   203   O  OG1 . THR A 1 47   ? -109.063 73.290  17.662  1.00 266.74 ? 47   THR A OG1 1 
ATOM   204   C  CG2 . THR A 1 47   ? -109.855 71.057  17.144  1.00 268.99 ? 47   THR A CG2 1 
ATOM   205   N  N   . GLU A 1 48   ? -107.929 71.543  13.835  1.00 213.79 ? 48   GLU A N   1 
ATOM   206   C  CA  . GLU A 1 48   ? -108.179 70.756  12.656  1.00 213.75 ? 48   GLU A CA  1 
ATOM   207   C  C   . GLU A 1 48   ? -107.076 69.739  12.455  1.00 209.01 ? 48   GLU A C   1 
ATOM   208   O  O   . GLU A 1 48   ? -105.991 70.102  12.020  1.00 207.82 ? 48   GLU A O   1 
ATOM   209   C  CB  . GLU A 1 48   ? -108.226 71.673  11.441  1.00 215.79 ? 48   GLU A CB  1 
ATOM   210   C  CG  . GLU A 1 48   ? -108.692 70.984  10.175  1.00 217.50 ? 48   GLU A CG  1 
ATOM   211   C  CD  . GLU A 1 48   ? -110.193 70.777  10.154  1.00 218.50 ? 48   GLU A CD  1 
ATOM   212   O  OE1 . GLU A 1 48   ? -110.884 71.354  11.024  1.00 217.46 ? 48   GLU A OE1 1 
ATOM   213   O  OE2 . GLU A 1 48   ? -110.679 70.044  9.266   1.00 219.76 ? 48   GLU A OE2 1 
ATOM   214   N  N   . ALA A 1 49   ? -107.346 68.470  12.750  1.00 206.35 ? 49   ALA A N   1 
ATOM   215   C  CA  . ALA A 1 49   ? -106.414 67.409  12.375  1.00 202.36 ? 49   ALA A CA  1 
ATOM   216   C  C   . ALA A 1 49   ? -105.946 67.665  10.940  1.00 201.21 ? 49   ALA A C   1 
ATOM   217   O  O   . ALA A 1 49   ? -106.532 68.493  10.248  1.00 203.36 ? 49   ALA A O   1 
ATOM   218   C  CB  . ALA A 1 49   ? -107.082 66.052  12.485  1.00 202.76 ? 49   ALA A CB  1 
ATOM   219   N  N   . PHE A 1 50   ? -104.893 66.983  10.487  1.00 198.05 ? 50   PHE A N   1 
ATOM   220   C  CA  . PHE A 1 50   ? -104.472 67.114  9.078   1.00 199.32 ? 50   PHE A CA  1 
ATOM   221   C  C   . PHE A 1 50   ? -103.343 66.186  8.585   1.00 193.86 ? 50   PHE A C   1 
ATOM   222   O  O   . PHE A 1 50   ? -102.283 66.111  9.192   1.00 190.44 ? 50   PHE A O   1 
ATOM   223   C  CB  . PHE A 1 50   ? -104.165 68.580  8.731   1.00 206.67 ? 50   PHE A CB  1 
ATOM   224   C  CG  . PHE A 1 50   ? -102.843 69.069  9.239   1.00 213.37 ? 50   PHE A CG  1 
ATOM   225   C  CD1 . PHE A 1 50   ? -101.782 69.269  8.365   1.00 216.97 ? 50   PHE A CD1 1 
ATOM   226   C  CD2 . PHE A 1 50   ? -102.662 69.346  10.591  1.00 216.75 ? 50   PHE A CD2 1 
ATOM   227   C  CE1 . PHE A 1 50   ? -100.563 69.729  8.831   1.00 217.64 ? 50   PHE A CE1 1 
ATOM   228   C  CE2 . PHE A 1 50   ? -101.444 69.806  11.070  1.00 216.87 ? 50   PHE A CE2 1 
ATOM   229   C  CZ  . PHE A 1 50   ? -100.394 69.997  10.191  1.00 217.37 ? 50   PHE A CZ  1 
ATOM   230   N  N   . ASP A 1 51   ? -103.583 65.506  7.464   1.00 193.46 ? 51   ASP A N   1 
ATOM   231   C  CA  . ASP A 1 51   ? -102.644 64.533  6.913   1.00 191.66 ? 51   ASP A CA  1 
ATOM   232   C  C   . ASP A 1 51   ? -101.254 65.095  6.652   1.00 190.00 ? 51   ASP A C   1 
ATOM   233   O  O   . ASP A 1 51   ? -101.090 66.304  6.461   1.00 190.37 ? 51   ASP A O   1 
ATOM   234   C  CB  . ASP A 1 51   ? -103.184 63.930  5.618   1.00 191.59 ? 51   ASP A CB  1 
ATOM   235   C  CG  . ASP A 1 51   ? -103.891 62.605  5.832   1.00 190.31 ? 51   ASP A CG  1 
ATOM   236   O  OD1 . ASP A 1 51   ? -104.051 62.174  6.988   1.00 187.74 ? 51   ASP A OD1 1 
ATOM   237   O  OD2 . ASP A 1 51   ? -104.290 61.988  4.823   1.00 191.54 ? 51   ASP A OD2 1 
ATOM   238   N  N   . ALA A 1 52   ? -100.274 64.182  6.623   1.00 186.84 ? 52   ALA A N   1 
ATOM   239   C  CA  . ALA A 1 52   ? -98.850  64.487  6.450   1.00 181.86 ? 52   ALA A CA  1 
ATOM   240   C  C   . ALA A 1 52   ? -98.104  63.332  5.754   1.00 180.52 ? 52   ALA A C   1 
ATOM   241   O  O   . ALA A 1 52   ? -97.913  62.267  6.340   1.00 180.38 ? 52   ALA A O   1 
ATOM   242   C  CB  . ALA A 1 52   ? -98.213  64.773  7.796   1.00 177.62 ? 52   ALA A CB  1 
ATOM   243   N  N   . THR A 1 53   ? -97.692  63.551  4.505   1.00 180.52 ? 53   THR A N   1 
ATOM   244   C  CA  . THR A 1 53   ? -96.924  62.569  3.731   1.00 178.35 ? 53   THR A CA  1 
ATOM   245   C  C   . THR A 1 53   ? -95.534  63.100  3.401   1.00 174.71 ? 53   THR A C   1 
ATOM   246   O  O   . THR A 1 53   ? -95.370  64.261  3.044   1.00 174.01 ? 53   THR A O   1 
ATOM   247   C  CB  . THR A 1 53   ? -97.633  62.203  2.402   1.00 185.57 ? 53   THR A CB  1 
ATOM   248   O  OG1 . THR A 1 53   ? -98.555  61.127  2.620   1.00 186.94 ? 53   THR A OG1 1 
ATOM   249   C  CG2 . THR A 1 53   ? -96.618  61.785  1.344   1.00 184.95 ? 53   THR A CG2 1 
ATOM   250   N  N   . ILE A 1 54   ? -94.529  62.247  3.493   1.00 170.12 ? 54   ILE A N   1 
ATOM   251   C  CA  . ILE A 1 54   ? -93.175  62.695  3.233   1.00 167.27 ? 54   ILE A CA  1 
ATOM   252   C  C   . ILE A 1 54   ? -92.623  61.755  2.191   1.00 165.00 ? 54   ILE A C   1 
ATOM   253   O  O   . ILE A 1 54   ? -93.248  60.746  1.892   1.00 162.60 ? 54   ILE A O   1 
ATOM   254   C  CB  . ILE A 1 54   ? -92.294  62.626  4.510   1.00 168.35 ? 54   ILE A CB  1 
ATOM   255   C  CG1 . ILE A 1 54   ? -92.907  63.417  5.665   1.00 168.28 ? 54   ILE A CG1 1 
ATOM   256   C  CG2 . ILE A 1 54   ? -90.893  63.144  4.248   1.00 166.47 ? 54   ILE A CG2 1 
ATOM   257   C  CD1 . ILE A 1 54   ? -92.144  63.244  6.975   1.00 166.24 ? 54   ILE A CD1 1 
ATOM   258   N  N   . SER A 1 55   ? -91.455  62.084  1.646   1.00 167.89 ? 55   SER A N   1 
ATOM   259   C  CA  . SER A 1 55   ? -90.813  61.247  0.647   1.00 170.71 ? 55   SER A CA  1 
ATOM   260   C  C   . SER A 1 55   ? -89.501  61.834  0.139   1.00 172.23 ? 55   SER A C   1 
ATOM   261   O  O   . SER A 1 55   ? -89.163  62.983  0.425   1.00 170.17 ? 55   SER A O   1 
ATOM   262   C  CB  . SER A 1 55   ? -91.769  61.034  -0.510  1.00 174.43 ? 55   SER A CB  1 
ATOM   263   O  OG  . SER A 1 55   ? -92.698  62.102  -0.571  1.00 176.45 ? 55   SER A OG  1 
ATOM   264   N  N   . ILE A 1 56   ? -88.779  61.033  -0.635  1.00 177.25 ? 56   ILE A N   1 
ATOM   265   C  CA  . ILE A 1 56   ? -87.435  61.379  -1.085  1.00 183.57 ? 56   ILE A CA  1 
ATOM   266   C  C   . ILE A 1 56   ? -87.355  61.556  -2.598  1.00 189.20 ? 56   ILE A C   1 
ATOM   267   O  O   . ILE A 1 56   ? -87.571  60.596  -3.336  1.00 188.66 ? 56   ILE A O   1 
ATOM   268   C  CB  . ILE A 1 56   ? -86.485  60.260  -0.703  1.00 186.99 ? 56   ILE A CB  1 
ATOM   269   C  CG1 . ILE A 1 56   ? -87.167  58.919  -0.994  1.00 191.12 ? 56   ILE A CG1 1 
ATOM   270   C  CG2 . ILE A 1 56   ? -86.069  60.373  0.788   1.00 193.60 ? 56   ILE A CG2 1 
ATOM   271   C  CD1 . ILE A 1 56   ? -86.549  57.749  -0.258  1.00 192.62 ? 56   ILE A CD1 1 
ATOM   272   N  N   . LYS A 1 57   ? -87.002  62.766  -3.048  1.00 194.29 ? 57   LYS A N   1 
ATOM   273   C  CA  . LYS A 1 57   ? -87.075  63.142  -4.477  1.00 199.13 ? 57   LYS A CA  1 
ATOM   274   C  C   . LYS A 1 57   ? -85.839  63.887  -5.009  1.00 199.72 ? 57   LYS A C   1 
ATOM   275   O  O   . LYS A 1 57   ? -85.236  64.694  -4.311  1.00 199.85 ? 57   LYS A O   1 
ATOM   276   C  CB  . LYS A 1 57   ? -88.355  63.939  -4.777  1.00 199.85 ? 57   LYS A CB  1 
ATOM   277   C  CG  . LYS A 1 57   ? -89.635  63.137  -4.556  1.00 200.32 ? 57   LYS A CG  1 
ATOM   278   C  CD  . LYS A 1 57   ? -90.892  63.976  -4.701  1.00 200.79 ? 57   LYS A CD  1 
ATOM   279   C  CE  . LYS A 1 57   ? -92.129  63.145  -4.382  1.00 201.93 ? 57   LYS A CE  1 
ATOM   280   N  NZ  . LYS A 1 57   ? -93.390  63.802  -4.822  1.00 203.79 ? 57   LYS A NZ  1 
ATOM   281   N  N   . SER A 1 58   ? -85.521  63.637  -6.278  1.00 201.03 ? 58   SER A N   1 
ATOM   282   C  CA  . SER A 1 58   ? -84.157  63.746  -6.817  1.00 201.06 ? 58   SER A CA  1 
ATOM   283   C  C   . SER A 1 58   ? -83.705  65.084  -7.399  1.00 199.25 ? 58   SER A C   1 
ATOM   284   O  O   . SER A 1 58   ? -84.194  65.504  -8.439  1.00 201.35 ? 58   SER A O   1 
ATOM   285   C  CB  . SER A 1 58   ? -83.998  62.682  -7.900  1.00 203.33 ? 58   SER A CB  1 
ATOM   286   O  OG  . SER A 1 58   ? -85.103  62.716  -8.803  1.00 206.80 ? 58   SER A OG  1 
ATOM   287   N  N   . TYR A 1 59   ? -82.708  65.698  -6.774  1.00 197.79 ? 59   TYR A N   1 
ATOM   288   C  CA  . TYR A 1 59   ? -82.251  67.043  -7.139  1.00 196.72 ? 59   TYR A CA  1 
ATOM   289   C  C   . TYR A 1 59   ? -83.327  67.956  -7.799  1.00 227.45 ? 59   TYR A C   1 
ATOM   290   O  O   . TYR A 1 59   ? -84.429  68.051  -7.259  1.00 230.05 ? 59   TYR A O   1 
ATOM   291   C  CB  . TYR A 1 59   ? -80.891  67.031  -7.840  1.00 193.62 ? 59   TYR A CB  1 
ATOM   292   C  CG  . TYR A 1 59   ? -80.096  68.264  -7.485  1.00 190.70 ? 59   TYR A CG  1 
ATOM   293   C  CD1 . TYR A 1 59   ? -80.479  69.060  -6.413  1.00 189.78 ? 59   TYR A CD1 1 
ATOM   294   C  CD2 . TYR A 1 59   ? -78.969  68.630  -8.200  1.00 188.55 ? 59   TYR A CD2 1 
ATOM   295   C  CE1 . TYR A 1 59   ? -79.776  70.194  -6.065  1.00 187.81 ? 59   TYR A CE1 1 
ATOM   296   C  CE2 . TYR A 1 59   ? -78.248  69.763  -7.854  1.00 186.64 ? 59   TYR A CE2 1 
ATOM   297   C  CZ  . TYR A 1 59   ? -78.658  70.541  -6.785  1.00 186.30 ? 59   TYR A CZ  1 
ATOM   298   O  OH  . TYR A 1 59   ? -77.945  71.667  -6.441  1.00 184.67 ? 59   TYR A OH  1 
ATOM   299   N  N   . PRO A 1 60   ? -83.037  68.640  -8.935  1.00 225.43 ? 60   PRO A N   1 
ATOM   300   C  CA  . PRO A 1 60   ? -84.051  69.655  -9.292  1.00 223.69 ? 60   PRO A CA  1 
ATOM   301   C  C   . PRO A 1 60   ? -85.362  69.149  -9.941  1.00 221.17 ? 60   PRO A C   1 
ATOM   302   O  O   . PRO A 1 60   ? -86.308  69.921  -10.055 1.00 221.41 ? 60   PRO A O   1 
ATOM   303   C  CB  . PRO A 1 60   ? -83.290  70.591  -10.248 1.00 224.52 ? 60   PRO A CB  1 
ATOM   304   C  CG  . PRO A 1 60   ? -81.820  70.174  -10.147 1.00 222.68 ? 60   PRO A CG  1 
ATOM   305   C  CD  . PRO A 1 60   ? -81.878  68.714  -9.842  1.00 223.22 ? 60   PRO A CD  1 
ATOM   306   N  N   . ASP A 1 61   ? -85.411  67.890  -10.364 1.00 217.94 ? 61   ASP A N   1 
ATOM   307   C  CA  . ASP A 1 61   ? -86.633  67.299  -10.904 1.00 217.51 ? 61   ASP A CA  1 
ATOM   308   C  C   . ASP A 1 61   ? -87.325  66.451  -9.846  1.00 215.98 ? 61   ASP A C   1 
ATOM   309   O  O   . ASP A 1 61   ? -86.810  65.406  -9.456  1.00 214.57 ? 61   ASP A O   1 
ATOM   310   C  CB  . ASP A 1 61   ? -86.298  66.402  -12.095 1.00 218.73 ? 61   ASP A CB  1 
ATOM   311   C  CG  . ASP A 1 61   ? -85.523  65.144  -11.686 1.00 219.04 ? 61   ASP A CG  1 
ATOM   312   O  OD1 . ASP A 1 61   ? -86.058  64.027  -11.868 1.00 220.93 ? 61   ASP A OD1 1 
ATOM   313   O  OD2 . ASP A 1 61   ? -84.388  65.265  -11.164 1.00 216.38 ? 61   ASP A OD2 1 
ATOM   314   N  N   . LYS A 1 62   ? -88.493  66.875  -9.381  1.00 215.64 ? 62   LYS A N   1 
ATOM   315   C  CA  . LYS A 1 62   ? -89.218  66.084  -8.385  1.00 215.30 ? 62   LYS A CA  1 
ATOM   316   C  C   . LYS A 1 62   ? -89.905  64.854  -9.000  1.00 217.13 ? 62   LYS A C   1 
ATOM   317   O  O   . LYS A 1 62   ? -91.038  64.519  -8.642  1.00 220.66 ? 62   LYS A O   1 
ATOM   318   C  CB  . LYS A 1 62   ? -90.203  66.958  -7.588  1.00 212.73 ? 62   LYS A CB  1 
ATOM   319   C  CG  . LYS A 1 62   ? -89.565  67.617  -6.355  1.00 206.06 ? 62   LYS A CG  1 
ATOM   320   C  CD  . LYS A 1 62   ? -90.231  68.930  -5.932  1.00 201.60 ? 62   LYS A CD  1 
ATOM   321   C  CE  . LYS A 1 62   ? -89.309  69.691  -4.982  1.00 195.24 ? 62   LYS A CE  1 
ATOM   322   N  NZ  . LYS A 1 62   ? -89.801  71.031  -4.597  1.00 193.43 ? 62   LYS A NZ  1 
ATOM   323   N  N   . LYS A 1 63   ? -89.206  64.187  -9.921  1.00 215.30 ? 63   LYS A N   1 
ATOM   324   C  CA  . LYS A 1 63   ? -89.742  63.011  -10.611 1.00 215.80 ? 63   LYS A CA  1 
ATOM   325   C  C   . LYS A 1 63   ? -89.592  61.704  -9.825  1.00 213.14 ? 63   LYS A C   1 
ATOM   326   O  O   . LYS A 1 63   ? -90.589  61.100  -9.432  1.00 214.63 ? 63   LYS A O   1 
ATOM   327   C  CB  . LYS A 1 63   ? -89.131  62.864  -12.008 1.00 216.88 ? 63   LYS A CB  1 
ATOM   328   C  CG  . LYS A 1 63   ? -89.477  64.001  -12.966 1.00 220.59 ? 63   LYS A CG  1 
ATOM   329   C  CD  . LYS A 1 63   ? -90.987  64.205  -13.104 1.00 225.77 ? 63   LYS A CD  1 
ATOM   330   C  CE  . LYS A 1 63   ? -91.644  63.086  -13.897 1.00 228.70 ? 63   LYS A CE  1 
ATOM   331   N  NZ  . LYS A 1 63   ? -93.126  63.147  -13.788 1.00 231.85 ? 63   LYS A NZ  1 
ATOM   332   N  N   . PHE A 1 64   ? -88.360  61.256  -9.604  1.00 209.34 ? 64   PHE A N   1 
ATOM   333   C  CA  . PHE A 1 64   ? -88.156  60.039  -8.830  1.00 205.39 ? 64   PHE A CA  1 
ATOM   334   C  C   . PHE A 1 64   ? -88.527  60.275  -7.373  1.00 205.19 ? 64   PHE A C   1 
ATOM   335   O  O   . PHE A 1 64   ? -88.101  61.264  -6.783  1.00 204.27 ? 64   PHE A O   1 
ATOM   336   C  CB  . PHE A 1 64   ? -86.707  59.568  -8.931  1.00 200.68 ? 64   PHE A CB  1 
ATOM   337   C  CG  . PHE A 1 64   ? -86.512  58.355  -9.810  1.00 198.13 ? 64   PHE A CG  1 
ATOM   338   C  CD1 . PHE A 1 64   ? -85.894  58.469  -11.051 1.00 196.14 ? 64   PHE A CD1 1 
ATOM   339   C  CD2 . PHE A 1 64   ? -86.934  57.096  -9.388  1.00 196.91 ? 64   PHE A CD2 1 
ATOM   340   C  CE1 . PHE A 1 64   ? -85.704  57.350  -11.857 1.00 195.03 ? 64   PHE A CE1 1 
ATOM   341   C  CE2 . PHE A 1 64   ? -86.749  55.975  -10.188 1.00 195.87 ? 64   PHE A CE2 1 
ATOM   342   C  CZ  . PHE A 1 64   ? -86.133  56.102  -11.424 1.00 195.05 ? 64   PHE A CZ  1 
ATOM   343   N  N   . SER A 1 65   ? -89.330  59.375  -6.801  1.00 205.29 ? 65   SER A N   1 
ATOM   344   C  CA  . SER A 1 65   ? -89.618  59.394  -5.358  1.00 206.04 ? 65   SER A CA  1 
ATOM   345   C  C   . SER A 1 65   ? -89.487  57.979  -4.785  1.00 205.46 ? 65   SER A C   1 
ATOM   346   O  O   . SER A 1 65   ? -90.408  57.157  -4.870  1.00 208.07 ? 65   SER A O   1 
ATOM   347   C  CB  . SER A 1 65   ? -90.998  59.994  -5.041  1.00 210.18 ? 65   SER A CB  1 
ATOM   348   O  OG  . SER A 1 65   ? -91.859  59.059  -4.407  1.00 212.97 ? 65   SER A OG  1 
ATOM   349   N  N   . TYR A 1 66   ? -88.323  57.713  -4.197  1.00 200.00 ? 66   TYR A N   1 
ATOM   350   C  CA  . TYR A 1 66   ? -87.919  56.357  -3.851  1.00 194.34 ? 66   TYR A CA  1 
ATOM   351   C  C   . TYR A 1 66   ? -88.899  55.770  -2.845  1.00 195.61 ? 66   TYR A C   1 
ATOM   352   O  O   . TYR A 1 66   ? -89.414  54.662  -3.029  1.00 195.69 ? 66   TYR A O   1 
ATOM   353   C  CB  . TYR A 1 66   ? -86.474  56.364  -3.342  1.00 184.89 ? 66   TYR A CB  1 
ATOM   354   C  CG  . TYR A 1 66   ? -85.580  57.329  -4.114  1.00 176.89 ? 66   TYR A CG  1 
ATOM   355   C  CD1 . TYR A 1 66   ? -84.760  56.883  -5.152  1.00 173.52 ? 66   TYR A CD1 1 
ATOM   356   C  CD2 . TYR A 1 66   ? -85.570  58.690  -3.819  1.00 173.25 ? 66   TYR A CD2 1 
ATOM   357   C  CE1 . TYR A 1 66   ? -83.944  57.770  -5.868  1.00 169.34 ? 66   TYR A CE1 1 
ATOM   358   C  CE2 . TYR A 1 66   ? -84.758  59.577  -4.528  1.00 169.52 ? 66   TYR A CE2 1 
ATOM   359   C  CZ  . TYR A 1 66   ? -83.946  59.114  -5.549  1.00 166.59 ? 66   TYR A CZ  1 
ATOM   360   O  OH  . TYR A 1 66   ? -83.138  59.993  -6.250  1.00 161.40 ? 66   TYR A OH  1 
ATOM   361   N  N   . SER A 1 67   ? -89.200  56.550  -1.814  1.00 195.45 ? 67   SER A N   1 
ATOM   362   C  CA  . SER A 1 67   ? -90.200  56.156  -0.837  1.00 194.59 ? 67   SER A CA  1 
ATOM   363   C  C   . SER A 1 67   ? -90.785  57.349  -0.092  1.00 192.03 ? 67   SER A C   1 
ATOM   364   O  O   . SER A 1 67   ? -90.368  58.494  -0.285  1.00 190.14 ? 67   SER A O   1 
ATOM   365   C  CB  . SER A 1 67   ? -89.633  55.124  0.141   1.00 193.08 ? 67   SER A CB  1 
ATOM   366   O  OG  . SER A 1 67   ? -88.400  55.550  0.690   1.00 190.37 ? 67   SER A OG  1 
ATOM   367   N  N   . SER A 1 68   ? -91.746  57.048  0.773   1.00 192.22 ? 68   SER A N   1 
ATOM   368   C  CA  . SER A 1 68   ? -92.610  58.050  1.371   1.00 194.78 ? 68   SER A CA  1 
ATOM   369   C  C   . SER A 1 68   ? -93.307  57.491  2.606   1.00 196.65 ? 68   SER A C   1 
ATOM   370   O  O   . SER A 1 68   ? -92.950  56.420  3.098   1.00 193.62 ? 68   SER A O   1 
ATOM   371   C  CB  . SER A 1 68   ? -93.655  58.501  0.346   1.00 198.41 ? 68   SER A CB  1 
ATOM   372   O  OG  . SER A 1 68   ? -94.248  57.398  -0.328  1.00 201.33 ? 68   SER A OG  1 
ATOM   373   N  N   . GLY A 1 69   ? -94.304  58.216  3.105   1.00 203.26 ? 69   GLY A N   1 
ATOM   374   C  CA  . GLY A 1 69   ? -95.046  57.759  4.265   1.00 207.66 ? 69   GLY A CA  1 
ATOM   375   C  C   . GLY A 1 69   ? -96.267  58.592  4.585   1.00 210.97 ? 69   GLY A C   1 
ATOM   376   O  O   . GLY A 1 69   ? -96.184  59.812  4.703   1.00 210.35 ? 69   GLY A O   1 
ATOM   377   N  N   . HIS A 1 70   ? -97.404  57.919  4.729   1.00 213.34 ? 70   HIS A N   1 
ATOM   378   C  CA  . HIS A 1 70   ? -98.676  58.573  5.012   1.00 216.89 ? 70   HIS A CA  1 
ATOM   379   C  C   . HIS A 1 70   ? -98.936  58.574  6.515   1.00 212.57 ? 70   HIS A C   1 
ATOM   380   O  O   . HIS A 1 70   ? -99.662  57.724  7.030   1.00 211.24 ? 70   HIS A O   1 
ATOM   381   C  CB  . HIS A 1 70   ? -99.803  57.838  4.284   1.00 225.35 ? 70   HIS A CB  1 
ATOM   382   C  CG  . HIS A 1 70   ? -100.927 58.725  3.844   1.00 234.01 ? 70   HIS A CG  1 
ATOM   383   N  ND1 . HIS A 1 70   ? -100.840 59.545  2.740   1.00 237.94 ? 70   HIS A ND1 1 
ATOM   384   C  CD2 . HIS A 1 70   ? -102.173 58.900  4.345   1.00 238.81 ? 70   HIS A CD2 1 
ATOM   385   C  CE1 . HIS A 1 70   ? -101.979 60.197  2.586   1.00 241.18 ? 70   HIS A CE1 1 
ATOM   386   N  NE2 . HIS A 1 70   ? -102.805 59.823  3.546   1.00 241.83 ? 70   HIS A NE2 1 
ATOM   387   N  N   . VAL A 1 71   ? -98.349  59.540  7.212   1.00 210.80 ? 71   VAL A N   1 
ATOM   388   C  CA  . VAL A 1 71   ? -98.399  59.580  8.669   1.00 208.88 ? 71   VAL A CA  1 
ATOM   389   C  C   . VAL A 1 71   ? -99.250  60.741  9.202   1.00 209.62 ? 71   VAL A C   1 
ATOM   390   O  O   . VAL A 1 71   ? -98.799  61.886  9.285   1.00 208.01 ? 71   VAL A O   1 
ATOM   391   C  CB  . VAL A 1 71   ? -96.978  59.617  9.237   1.00 204.19 ? 71   VAL A CB  1 
ATOM   392   C  CG1 . VAL A 1 71   ? -96.139  58.528  8.573   1.00 202.87 ? 71   VAL A CG1 1 
ATOM   393   C  CG2 . VAL A 1 71   ? -96.343  60.972  8.990   1.00 202.66 ? 71   VAL A CG2 1 
ATOM   394   N  N   . HIS A 1 72   ? -100.486 60.429  9.575   1.00 213.54 ? 72   HIS A N   1 
ATOM   395   C  CA  . HIS A 1 72   ? -101.487 61.459  9.848   1.00 218.01 ? 72   HIS A CA  1 
ATOM   396   C  C   . HIS A 1 72   ? -101.569 61.901  11.294  1.00 216.54 ? 72   HIS A C   1 
ATOM   397   O  O   . HIS A 1 72   ? -102.182 61.228  12.112  1.00 215.97 ? 72   HIS A O   1 
ATOM   398   C  CB  . HIS A 1 72   ? -102.876 60.979  9.425   1.00 226.14 ? 72   HIS A CB  1 
ATOM   399   C  CG  . HIS A 1 72   ? -103.991 61.807  9.985   1.00 232.39 ? 72   HIS A CG  1 
ATOM   400   N  ND1 . HIS A 1 72   ? -104.443 62.957  9.374   1.00 235.92 ? 72   HIS A ND1 1 
ATOM   401   C  CD2 . HIS A 1 72   ? -104.736 61.661  11.106  1.00 234.64 ? 72   HIS A CD2 1 
ATOM   402   C  CE1 . HIS A 1 72   ? -105.424 63.477  10.089  1.00 237.58 ? 72   HIS A CE1 1 
ATOM   403   N  NE2 . HIS A 1 72   ? -105.621 62.711  11.146  1.00 236.77 ? 72   HIS A NE2 1 
ATOM   404   N  N   . LEU A 1 73   ? -100.994 63.054  11.601  1.00 216.15 ? 73   LEU A N   1 
ATOM   405   C  CA  . LEU A 1 73   ? -101.086 63.599  12.950  1.00 217.19 ? 73   LEU A CA  1 
ATOM   406   C  C   . LEU A 1 73   ? -102.491 64.116  13.245  1.00 222.62 ? 73   LEU A C   1 
ATOM   407   O  O   . LEU A 1 73   ? -103.389 64.016  12.405  1.00 223.72 ? 73   LEU A O   1 
ATOM   408   C  CB  . LEU A 1 73   ? -100.064 64.713  13.150  1.00 212.26 ? 73   LEU A CB  1 
ATOM   409   C  CG  . LEU A 1 73   ? -99.706  65.448  11.862  1.00 210.70 ? 73   LEU A CG  1 
ATOM   410   C  CD1 . LEU A 1 73   ? -99.238  66.864  12.159  1.00 208.24 ? 73   LEU A CD1 1 
ATOM   411   C  CD2 . LEU A 1 73   ? -98.658  64.657  11.080  1.00 209.71 ? 73   LEU A CD2 1 
ATOM   412   N  N   . SER A 1 74   ? -102.666 64.659  14.448  1.00 226.84 ? 74   SER A N   1 
ATOM   413   C  CA  . SER A 1 74   ? -103.948 65.172  14.917  1.00 231.69 ? 74   SER A CA  1 
ATOM   414   C  C   . SER A 1 74   ? -103.731 65.698  16.321  1.00 234.11 ? 74   SER A C   1 
ATOM   415   O  O   . SER A 1 74   ? -102.636 65.577  16.849  1.00 235.36 ? 74   SER A O   1 
ATOM   416   C  CB  . SER A 1 74   ? -104.998 64.065  14.946  1.00 231.96 ? 74   SER A CB  1 
ATOM   417   O  OG  . SER A 1 74   ? -104.707 63.110  15.950  1.00 229.48 ? 74   SER A OG  1 
ATOM   418   N  N   . SER A 1 75   ? -104.761 66.278  16.931  1.00 237.67 ? 75   SER A N   1 
ATOM   419   C  CA  . SER A 1 75   ? -104.673 66.717  18.331  1.00 240.00 ? 75   SER A CA  1 
ATOM   420   C  C   . SER A 1 75   ? -104.477 65.530  19.283  1.00 240.01 ? 75   SER A C   1 
ATOM   421   O  O   . SER A 1 75   ? -104.197 65.708  20.474  1.00 237.48 ? 75   SER A O   1 
ATOM   422   C  CB  . SER A 1 75   ? -105.923 67.511  18.747  1.00 245.11 ? 75   SER A CB  1 
ATOM   423   O  OG  . SER A 1 75   ? -105.792 68.896  18.470  1.00 247.38 ? 75   SER A OG  1 
ATOM   424   N  N   . GLU A 1 76   ? -104.640 64.325  18.743  1.00 240.50 ? 76   GLU A N   1 
ATOM   425   C  CA  . GLU A 1 76   ? -104.514 63.086  19.505  1.00 237.67 ? 76   GLU A CA  1 
ATOM   426   C  C   . GLU A 1 76   ? -103.056 62.646  19.607  1.00 230.28 ? 76   GLU A C   1 
ATOM   427   O  O   . GLU A 1 76   ? -102.619 62.109  20.625  1.00 230.02 ? 76   GLU A O   1 
ATOM   428   C  CB  . GLU A 1 76   ? -105.339 62.000  18.822  1.00 241.50 ? 76   GLU A CB  1 
ATOM   429   C  CG  . GLU A 1 76   ? -105.135 60.606  19.359  1.00 241.46 ? 76   GLU A CG  1 
ATOM   430   C  CD  . GLU A 1 76   ? -105.800 59.568  18.483  1.00 243.07 ? 76   GLU A CD  1 
ATOM   431   O  OE1 . GLU A 1 76   ? -106.088 59.878  17.306  1.00 244.22 ? 76   GLU A OE1 1 
ATOM   432   O  OE2 . GLU A 1 76   ? -106.034 58.445  18.972  1.00 242.84 ? 76   GLU A OE2 1 
ATOM   433   N  N   . ASN A 1 77   ? -102.326 62.868  18.518  1.00 221.23 ? 77   ASN A N   1 
ATOM   434   C  CA  . ASN A 1 77   ? -100.898 62.597  18.415  1.00 212.04 ? 77   ASN A CA  1 
ATOM   435   C  C   . ASN A 1 77   ? -100.127 63.894  18.661  1.00 197.82 ? 77   ASN A C   1 
ATOM   436   O  O   . ASN A 1 77   ? -99.016  64.066  18.177  1.00 192.37 ? 77   ASN A O   1 
ATOM   437   C  CB  . ASN A 1 77   ? -100.597 62.068  17.004  1.00 217.62 ? 77   ASN A CB  1 
ATOM   438   C  CG  . ASN A 1 77   ? -99.346  61.204  16.940  1.00 223.93 ? 77   ASN A CG  1 
ATOM   439   O  OD1 . ASN A 1 77   ? -98.552  61.165  17.877  1.00 225.49 ? 77   ASN A OD1 1 
ATOM   440   N  ND2 . ASN A 1 77   ? -99.167  60.507  15.820  1.00 226.69 ? 77   ASN A ND2 1 
ATOM   441   N  N   . LYS A 1 78   ? -100.742 64.819  19.388  1.00 192.00 ? 78   LYS A N   1 
ATOM   442   C  CA  . LYS A 1 78   ? -100.184 66.153  19.597  1.00 182.59 ? 78   LYS A CA  1 
ATOM   443   C  C   . LYS A 1 78   ? -99.546  66.727  18.347  1.00 176.32 ? 78   LYS A C   1 
ATOM   444   O  O   . LYS A 1 78   ? -98.645  67.559  18.408  1.00 173.96 ? 78   LYS A O   1 
ATOM   445   C  CB  . LYS A 1 78   ? -99.191  66.138  20.732  1.00 172.97 ? 78   LYS A CB  1 
ATOM   446   C  CG  . LYS A 1 78   ? -99.806  65.661  22.017  1.00 164.26 ? 78   LYS A CG  1 
ATOM   447   C  CD  . LYS A 1 78   ? -101.032 66.468  22.342  1.00 153.91 ? 78   LYS A CD  1 
ATOM   448   C  CE  . LYS A 1 78   ? -101.613 66.009  23.647  1.00 147.90 ? 78   LYS A CE  1 
ATOM   449   N  NZ  . LYS A 1 78   ? -103.031 66.415  23.782  1.00 146.67 ? 78   LYS A NZ  1 
ATOM   450   N  N   . PHE A 1 79   ? -100.037 66.270  17.206  1.00 175.83 ? 79   PHE A N   1 
ATOM   451   C  CA  . PHE A 1 79   ? -99.552  66.731  15.922  1.00 174.99 ? 79   PHE A CA  1 
ATOM   452   C  C   . PHE A 1 79   ? -98.079  66.466  15.891  1.00 175.63 ? 79   PHE A C   1 
ATOM   453   O  O   . PHE A 1 79   ? -97.285  67.398  15.936  1.00 176.01 ? 79   PHE A O   1 
ATOM   454   C  CB  . PHE A 1 79   ? -99.842  68.219  15.728  1.00 173.76 ? 79   PHE A CB  1 
ATOM   455   C  CG  . PHE A 1 79   ? -101.313 68.525  15.528  1.00 177.58 ? 79   PHE A CG  1 
ATOM   456   C  CD1 . PHE A 1 79   ? -102.019 69.271  16.458  1.00 176.61 ? 79   PHE A CD1 1 
ATOM   457   C  CD2 . PHE A 1 79   ? -101.988 68.049  14.416  1.00 179.62 ? 79   PHE A CD2 1 
ATOM   458   C  CE1 . PHE A 1 79   ? -103.345 69.541  16.277  1.00 177.54 ? 79   PHE A CE1 1 
ATOM   459   C  CE2 . PHE A 1 79   ? -103.318 68.321  14.242  1.00 180.87 ? 79   PHE A CE2 1 
ATOM   460   C  CZ  . PHE A 1 79   ? -103.994 69.064  15.173  1.00 179.63 ? 79   PHE A CZ  1 
ATOM   461   N  N   . GLN A 1 80   ? -97.737  65.178  15.840  1.00 178.13 ? 80   GLN A N   1 
ATOM   462   C  CA  . GLN A 1 80   ? -96.356  64.693  15.798  1.00 179.26 ? 80   GLN A CA  1 
ATOM   463   C  C   . GLN A 1 80   ? -96.323  63.268  15.245  1.00 178.91 ? 80   GLN A C   1 
ATOM   464   O  O   . GLN A 1 80   ? -97.216  62.473  15.519  1.00 180.03 ? 80   GLN A O   1 
ATOM   465   C  CB  . GLN A 1 80   ? -95.744  64.691  17.199  1.00 180.26 ? 80   GLN A CB  1 
ATOM   466   C  CG  . GLN A 1 80   ? -95.921  65.981  17.975  1.00 181.01 ? 80   GLN A CG  1 
ATOM   467   C  CD  . GLN A 1 80   ? -94.938  66.102  19.113  1.00 179.87 ? 80   GLN A CD  1 
ATOM   468   O  OE1 . GLN A 1 80   ? -94.578  65.110  19.751  1.00 179.52 ? 80   GLN A OE1 1 
ATOM   469   N  NE2 . GLN A 1 80   ? -94.495  67.322  19.376  1.00 178.90 ? 80   GLN A NE2 1 
ATOM   470   N  N   . ASN A 1 81   ? -95.293  62.928  14.482  1.00 178.52 ? 81   ASN A N   1 
ATOM   471   C  CA  . ASN A 1 81   ? -95.270  61.611  13.854  1.00 180.42 ? 81   ASN A CA  1 
ATOM   472   C  C   . ASN A 1 81   ? -93.920  61.250  13.228  1.00 176.27 ? 81   ASN A C   1 
ATOM   473   O  O   . ASN A 1 81   ? -92.991  62.049  13.212  1.00 173.25 ? 81   ASN A O   1 
ATOM   474   C  CB  . ASN A 1 81   ? -96.390  61.522  12.813  1.00 186.31 ? 81   ASN A CB  1 
ATOM   475   C  CG  . ASN A 1 81   ? -97.198  60.241  12.923  1.00 190.56 ? 81   ASN A CG  1 
ATOM   476   O  OD1 . ASN A 1 81   ? -96.660  59.167  13.200  1.00 190.27 ? 81   ASN A OD1 1 
ATOM   477   N  ND2 . ASN A 1 81   ? -98.503  60.352  12.697  1.00 193.52 ? 81   ASN A ND2 1 
ATOM   478   N  N   . SER A 1 82   ? -93.808  60.045  12.702  1.00 176.74 ? 82   SER A N   1 
ATOM   479   C  CA  . SER A 1 82   ? -92.527  59.602  12.217  1.00 176.75 ? 82   SER A CA  1 
ATOM   480   C  C   . SER A 1 82   ? -92.628  58.718  10.995  1.00 180.34 ? 82   SER A C   1 
ATOM   481   O  O   . SER A 1 82   ? -93.629  58.043  10.792  1.00 183.22 ? 82   SER A O   1 
ATOM   482   C  CB  . SER A 1 82   ? -91.783  58.896  13.334  1.00 176.49 ? 82   SER A CB  1 
ATOM   483   O  OG  . SER A 1 82   ? -90.606  59.599  13.667  1.00 175.59 ? 82   SER A OG  1 
ATOM   484   N  N   . ALA A 1 83   ? -91.586  58.721  10.175  1.00 179.95 ? 83   ALA A N   1 
ATOM   485   C  CA  . ALA A 1 83   ? -91.619  57.959  8.941   1.00 180.32 ? 83   ALA A CA  1 
ATOM   486   C  C   . ALA A 1 83   ? -90.245  57.390  8.608   1.00 181.36 ? 83   ALA A C   1 
ATOM   487   O  O   . ALA A 1 83   ? -89.219  58.049  8.805   1.00 182.14 ? 83   ALA A O   1 
ATOM   488   C  CB  . ALA A 1 83   ? -92.120  58.834  7.812   1.00 180.83 ? 83   ALA A CB  1 
ATOM   489   N  N   . ILE A 1 84   ? -90.224  56.156  8.119   1.00 179.17 ? 84   ILE A N   1 
ATOM   490   C  CA  . ILE A 1 84   ? -88.983  55.575  7.619   1.00 176.42 ? 84   ILE A CA  1 
ATOM   491   C  C   . ILE A 1 84   ? -88.874  55.675  6.084   1.00 175.79 ? 84   ILE A C   1 
ATOM   492   O  O   . ILE A 1 84   ? -89.162  54.721  5.355   1.00 175.81 ? 84   ILE A O   1 
ATOM   493   C  CB  . ILE A 1 84   ? -88.766  54.113  8.114   1.00 235.49 ? 84   ILE A CB  1 
ATOM   494   C  CG1 . ILE A 1 84   ? -89.959  53.227  7.747   1.00 237.14 ? 84   ILE A CG1 1 
ATOM   495   C  CG2 . ILE A 1 84   ? -88.511  54.081  9.620   1.00 234.04 ? 84   ILE A CG2 1 
ATOM   496   C  CD1 . ILE A 1 84   ? -89.687  51.747  7.894   1.00 236.50 ? 84   ILE A CD1 1 
ATOM   497   N  N   . LEU A 1 85   ? -88.460  56.851  5.615   1.00 173.26 ? 85   LEU A N   1 
ATOM   498   C  CA  . LEU A 1 85   ? -88.074  57.047  4.226   1.00 170.56 ? 85   LEU A CA  1 
ATOM   499   C  C   . LEU A 1 85   ? -86.898  56.148  4.011   1.00 164.29 ? 85   LEU A C   1 
ATOM   500   O  O   . LEU A 1 85   ? -86.512  55.421  4.915   1.00 163.86 ? 85   LEU A O   1 
ATOM   501   C  CB  . LEU A 1 85   ? -87.654  58.492  3.972   1.00 169.59 ? 85   LEU A CB  1 
ATOM   502   C  CG  . LEU A 1 85   ? -88.796  59.452  4.269   1.00 170.74 ? 85   LEU A CG  1 
ATOM   503   C  CD1 . LEU A 1 85   ? -90.082  58.804  3.794   1.00 173.54 ? 85   LEU A CD1 1 
ATOM   504   C  CD2 . LEU A 1 85   ? -88.897  59.779  5.751   1.00 169.28 ? 85   LEU A CD2 1 
ATOM   505   N  N   . THR A 1 86   ? -86.306  56.189  2.829   1.00 160.39 ? 86   THR A N   1 
ATOM   506   C  CA  . THR A 1 86   ? -85.136  55.359  2.623   1.00 155.97 ? 86   THR A CA  1 
ATOM   507   C  C   . THR A 1 86   ? -84.676  55.285  1.169   1.00 155.59 ? 86   THR A C   1 
ATOM   508   O  O   . THR A 1 86   ? -85.289  54.626  0.327   1.00 154.91 ? 86   THR A O   1 
ATOM   509   C  CB  . THR A 1 86   ? -85.344  53.958  3.263   1.00 141.86 ? 86   THR A CB  1 
ATOM   510   O  OG1 . THR A 1 86   ? -84.085  53.435  3.696   1.00 140.88 ? 86   THR A OG1 1 
ATOM   511   C  CG2 . THR A 1 86   ? -86.038  52.995  2.313   1.00 143.24 ? 86   THR A CG2 1 
ATOM   512   N  N   . ILE A 1 87   ? -83.585  55.993  0.897   1.00 152.89 ? 87   ILE A N   1 
ATOM   513   C  CA  . ILE A 1 87   ? -82.994  56.040  -0.424  1.00 153.89 ? 87   ILE A CA  1 
ATOM   514   C  C   . ILE A 1 87   ? -82.205  54.779  -0.686  1.00 169.47 ? 87   ILE A C   1 
ATOM   515   O  O   . ILE A 1 87   ? -81.116  54.622  -0.149  1.00 172.56 ? 87   ILE A O   1 
ATOM   516   C  CB  . ILE A 1 87   ? -82.000  57.189  -0.523  1.00 139.77 ? 87   ILE A CB  1 
ATOM   517   C  CG1 . ILE A 1 87   ? -82.623  58.474  0.003   1.00 135.40 ? 87   ILE A CG1 1 
ATOM   518   C  CG2 . ILE A 1 87   ? -81.496  57.336  -1.951  1.00 134.04 ? 87   ILE A CG2 1 
ATOM   519   C  CD1 . ILE A 1 87   ? -81.796  59.689  -0.285  1.00 132.23 ? 87   ILE A CD1 1 
ATOM   520   N  N   . GLN A 1 88   ? -82.740  53.878  -1.500  1.00 179.78 ? 88   GLN A N   1 
ATOM   521   C  CA  . GLN A 1 88   ? -81.997  52.687  -1.883  1.00 186.93 ? 88   GLN A CA  1 
ATOM   522   C  C   . GLN A 1 88   ? -81.091  53.034  -3.056  1.00 196.32 ? 88   GLN A C   1 
ATOM   523   O  O   . GLN A 1 88   ? -80.980  54.203  -3.415  1.00 196.40 ? 88   GLN A O   1 
ATOM   524   C  CB  . GLN A 1 88   ? -82.955  51.571  -2.268  1.00 189.66 ? 88   GLN A CB  1 
ATOM   525   C  CG  . GLN A 1 88   ? -84.036  51.318  -1.264  1.00 191.30 ? 88   GLN A CG  1 
ATOM   526   C  CD  . GLN A 1 88   ? -84.236  49.844  -1.039  1.00 192.55 ? 88   GLN A CD  1 
ATOM   527   O  OE1 . GLN A 1 88   ? -85.285  49.410  -0.563  1.00 194.51 ? 88   GLN A OE1 1 
ATOM   528   N  NE2 . GLN A 1 88   ? -83.220  49.057  -1.378  1.00 190.37 ? 88   GLN A NE2 1 
ATOM   529   N  N   . PRO A 1 89   ? -80.419  52.023  -3.637  1.00 201.52 ? 89   PRO A N   1 
ATOM   530   C  CA  . PRO A 1 89   ? -79.683  52.091  -4.922  1.00 204.67 ? 89   PRO A CA  1 
ATOM   531   C  C   . PRO A 1 89   ? -80.465  52.485  -6.224  1.00 201.80 ? 89   PRO A C   1 
ATOM   532   O  O   . PRO A 1 89   ? -81.403  51.806  -6.658  1.00 197.00 ? 89   PRO A O   1 
ATOM   533   C  CB  . PRO A 1 89   ? -79.096  50.680  -5.043  1.00 204.83 ? 89   PRO A CB  1 
ATOM   534   C  CG  . PRO A 1 89   ? -78.859  50.279  -3.597  1.00 203.70 ? 89   PRO A CG  1 
ATOM   535   C  CD  . PRO A 1 89   ? -80.000  50.864  -2.822  1.00 203.45 ? 89   PRO A CD  1 
ATOM   536   N  N   . LYS A 1 90   ? -80.029  53.580  -6.850  1.00 207.87 ? 90   LYS A N   1 
ATOM   537   C  CA  . LYS A 1 90   ? -80.612  54.075  -8.096  1.00 213.09 ? 90   LYS A CA  1 
ATOM   538   C  C   . LYS A 1 90   ? -79.520  54.359  -9.110  1.00 223.90 ? 90   LYS A C   1 
ATOM   539   O  O   . LYS A 1 90   ? -79.246  53.541  -9.976  1.00 223.52 ? 90   LYS A O   1 
ATOM   540   C  CB  . LYS A 1 90   ? -81.401  55.354  -7.852  1.00 202.31 ? 90   LYS A CB  1 
ATOM   541   C  CG  . LYS A 1 90   ? -82.520  55.179  -6.881  1.00 193.46 ? 90   LYS A CG  1 
ATOM   542   C  CD  . LYS A 1 90   ? -83.525  54.183  -7.388  1.00 187.23 ? 90   LYS A CD  1 
ATOM   543   C  CE  . LYS A 1 90   ? -84.490  53.806  -6.291  1.00 184.93 ? 90   LYS A CE  1 
ATOM   544   N  NZ  . LYS A 1 90   ? -85.894  53.724  -6.776  1.00 187.22 ? 90   LYS A NZ  1 
ATOM   545   N  N   . GLN A 1 91   ? -78.892  55.523  -9.000  1.00 237.91 ? 91   GLN A N   1 
ATOM   546   C  CA  . GLN A 1 91   ? -77.773  55.853  -9.874  1.00 253.43 ? 91   GLN A CA  1 
ATOM   547   C  C   . GLN A 1 91   ? -76.538  55.009  -9.578  1.00 267.91 ? 91   GLN A C   1 
ATOM   548   O  O   . GLN A 1 91   ? -75.877  55.196  -8.554  1.00 268.13 ? 91   GLN A O   1 
ATOM   549   C  CB  . GLN A 1 91   ? -77.423  57.335  -9.772  1.00 255.21 ? 91   GLN A CB  1 
ATOM   550   C  CG  . GLN A 1 91   ? -78.324  58.219  -10.596 1.00 260.55 ? 91   GLN A CG  1 
ATOM   551   C  CD  . GLN A 1 91   ? -78.799  57.530  -11.855 1.00 264.76 ? 91   GLN A CD  1 
ATOM   552   O  OE1 . GLN A 1 91   ? -79.826  56.852  -11.852 1.00 267.59 ? 91   GLN A OE1 1 
ATOM   553   N  NE2 . GLN A 1 91   ? -78.056  57.702  -12.943 1.00 264.82 ? 91   GLN A NE2 1 
ATOM   554   N  N   . LEU A 1 92   ? -76.232  54.083  -10.484 1.00 283.80 ? 92   LEU A N   1 
ATOM   555   C  CA  . LEU A 1 92   ? -75.045  53.233  -10.369 1.00 297.09 ? 92   LEU A CA  1 
ATOM   556   C  C   . LEU A 1 92   ? -73.869  53.601  -11.293 1.00 306.44 ? 92   LEU A C   1 
ATOM   557   O  O   . LEU A 1 92   ? -72.810  52.978  -11.205 1.00 305.20 ? 92   LEU A O   1 
ATOM   558   C  CB  . LEU A 1 92   ? -75.414  51.757  -10.587 1.00 302.04 ? 92   LEU A CB  1 
ATOM   559   C  CG  . LEU A 1 92   ? -76.245  51.025  -9.528  1.00 306.40 ? 92   LEU A CG  1 
ATOM   560   C  CD1 . LEU A 1 92   ? -76.636  49.637  -10.025 1.00 308.41 ? 92   LEU A CD1 1 
ATOM   561   C  CD2 . LEU A 1 92   ? -75.502  50.932  -8.201  1.00 305.82 ? 92   LEU A CD2 1 
ATOM   562   N  N   . PRO A 1 93   ? -74.038  54.602  -12.181 1.00 315.64 ? 93   PRO A N   1 
ATOM   563   C  CA  . PRO A 1 93   ? -72.959  54.811  -13.154 1.00 320.14 ? 93   PRO A CA  1 
ATOM   564   C  C   . PRO A 1 93   ? -71.658  55.251  -12.495 1.00 323.48 ? 93   PRO A C   1 
ATOM   565   O  O   . PRO A 1 93   ? -71.583  56.354  -11.951 1.00 324.68 ? 93   PRO A O   1 
ATOM   566   C  CB  . PRO A 1 93   ? -73.498  55.940  -14.046 1.00 319.94 ? 93   PRO A CB  1 
ATOM   567   C  CG  . PRO A 1 93   ? -74.963  56.018  -13.755 1.00 321.55 ? 93   PRO A CG  1 
ATOM   568   C  CD  . PRO A 1 93   ? -75.092  55.619  -12.324 1.00 320.11 ? 93   PRO A CD  1 
ATOM   569   N  N   . GLY A 1 94   ? -70.645  54.393  -12.547 1.00 325.55 ? 94   GLY A N   1 
ATOM   570   C  CA  . GLY A 1 94   ? -69.334  54.750  -12.044 1.00 326.37 ? 94   GLY A CA  1 
ATOM   571   C  C   . GLY A 1 94   ? -68.789  55.899  -12.864 1.00 327.88 ? 94   GLY A C   1 
ATOM   572   O  O   . GLY A 1 94   ? -68.879  55.890  -14.091 1.00 329.14 ? 94   GLY A O   1 
ATOM   573   N  N   . GLY A 1 95   ? -68.220  56.891  -12.190 1.00 328.38 ? 95   GLY A N   1 
ATOM   574   C  CA  . GLY A 1 95   ? -67.719  58.070  -12.868 1.00 327.65 ? 95   GLY A CA  1 
ATOM   575   C  C   . GLY A 1 95   ? -68.671  59.243  -12.751 1.00 329.63 ? 95   GLY A C   1 
ATOM   576   O  O   . GLY A 1 95   ? -68.287  60.304  -12.253 1.00 328.84 ? 95   GLY A O   1 
ATOM   577   N  N   . GLN A 1 96   ? -69.909  59.069  -13.208 1.00 330.58 ? 96   GLN A N   1 
ATOM   578   C  CA  . GLN A 1 96   ? -70.901  60.104  -12.985 1.00 330.34 ? 96   GLN A CA  1 
ATOM   579   C  C   . GLN A 1 96   ? -70.815  60.373  -11.506 1.00 332.30 ? 96   GLN A C   1 
ATOM   580   O  O   . GLN A 1 96   ? -70.707  59.439  -10.719 1.00 334.26 ? 96   GLN A O   1 
ATOM   581   C  CB  . GLN A 1 96   ? -72.315  59.641  -13.341 1.00 328.58 ? 96   GLN A CB  1 
ATOM   582   C  CG  . GLN A 1 96   ? -73.396  60.596  -12.840 1.00 327.42 ? 96   GLN A CG  1 
ATOM   583   C  CD  . GLN A 1 96   ? -74.774  60.275  -13.375 1.00 328.76 ? 96   GLN A CD  1 
ATOM   584   O  OE1 . GLN A 1 96   ? -74.968  59.274  -14.063 1.00 328.89 ? 96   GLN A OE1 1 
ATOM   585   N  NE2 . GLN A 1 96   ? -75.744  61.129  -13.063 1.00 330.24 ? 96   GLN A NE2 1 
ATOM   586   N  N   . ASN A 1 97   ? -70.800  61.642  -11.127 1.00 331.22 ? 97   ASN A N   1 
ATOM   587   C  CA  . ASN A 1 97   ? -70.894  61.990  -9.723  1.00 329.14 ? 97   ASN A CA  1 
ATOM   588   C  C   . ASN A 1 97   ? -72.355  61.860  -9.334  1.00 324.83 ? 97   ASN A C   1 
ATOM   589   O  O   . ASN A 1 97   ? -73.071  62.857  -9.236  1.00 326.33 ? 97   ASN A O   1 
ATOM   590   C  CB  . ASN A 1 97   ? -70.383  63.410  -9.493  1.00 332.61 ? 97   ASN A CB  1 
ATOM   591   C  CG  . ASN A 1 97   ? -68.960  63.597  -9.982  1.00 333.13 ? 97   ASN A CG  1 
ATOM   592   O  OD1 . ASN A 1 97   ? -68.205  62.633  -10.102 1.00 333.14 ? 97   ASN A OD1 1 
ATOM   593   N  ND2 . ASN A 1 97   ? -68.586  64.838  -10.268 1.00 333.30 ? 97   ASN A ND2 1 
ATOM   594   N  N   . PRO A 1 98   ? -72.807  60.618  -9.107  1.00 316.87 ? 98   PRO A N   1 
ATOM   595   C  CA  . PRO A 1 98   ? -74.242  60.388  -9.008  1.00 310.34 ? 98   PRO A CA  1 
ATOM   596   C  C   . PRO A 1 98   ? -74.662  60.787  -7.620  1.00 296.12 ? 98   PRO A C   1 
ATOM   597   O  O   . PRO A 1 98   ? -73.795  61.059  -6.794  1.00 295.72 ? 98   PRO A O   1 
ATOM   598   C  CB  . PRO A 1 98   ? -74.356  58.862  -9.134  1.00 315.06 ? 98   PRO A CB  1 
ATOM   599   C  CG  . PRO A 1 98   ? -72.920  58.320  -9.053  1.00 315.39 ? 98   PRO A CG  1 
ATOM   600   C  CD  . PRO A 1 98   ? -72.063  59.458  -8.598  1.00 315.39 ? 98   PRO A CD  1 
ATOM   601   N  N   . VAL A 1 99   ? -75.959  60.841  -7.361  1.00 281.77 ? 99   VAL A N   1 
ATOM   602   C  CA  . VAL A 1 99   ? -76.402  60.785  -5.989  1.00 266.41 ? 99   VAL A CA  1 
ATOM   603   C  C   . VAL A 1 99   ? -76.043  62.043  -5.182  1.00 247.07 ? 99   VAL A C   1 
ATOM   604   O  O   . VAL A 1 99   ? -76.721  62.372  -4.210  1.00 247.64 ? 99   VAL A O   1 
ATOM   605   C  CB  . VAL A 1 99   ? -75.782  59.527  -5.339  1.00 269.18 ? 99   VAL A CB  1 
ATOM   606   C  CG1 . VAL A 1 99   ? -76.102  59.441  -3.864  1.00 271.31 ? 99   VAL A CG1 1 
ATOM   607   C  CG2 . VAL A 1 99   ? -76.228  58.265  -6.084  1.00 270.96 ? 99   VAL A CG2 1 
ATOM   608   N  N   . SER A 1 100  ? -74.990  62.751  -5.578  1.00 226.33 ? 100  SER A N   1 
ATOM   609   C  CA  . SER A 1 100  ? -74.567  63.932  -4.832  1.00 207.19 ? 100  SER A CA  1 
ATOM   610   C  C   . SER A 1 100  ? -75.740  64.887  -4.742  1.00 193.58 ? 100  SER A C   1 
ATOM   611   O  O   . SER A 1 100  ? -76.094  65.509  -5.738  1.00 196.54 ? 100  SER A O   1 
ATOM   612   C  CB  . SER A 1 100  ? -73.414  64.627  -5.545  1.00 201.41 ? 100  SER A CB  1 
ATOM   613   O  OG  . SER A 1 100  ? -72.862  63.774  -6.517  1.00 198.54 ? 100  SER A OG  1 
ATOM   614   N  N   . TYR A 1 101  ? -76.347  64.996  -3.563  1.00 176.82 ? 101  TYR A N   1 
ATOM   615   C  CA  . TYR A 1 101  ? -77.495  65.881  -3.371  1.00 164.09 ? 101  TYR A CA  1 
ATOM   616   C  C   . TYR A 1 101  ? -78.839  65.244  -3.706  1.00 157.95 ? 101  TYR A C   1 
ATOM   617   O  O   . TYR A 1 101  ? -78.995  64.615  -4.740  1.00 158.13 ? 101  TYR A O   1 
ATOM   618   C  CB  . TYR A 1 101  ? -77.328  67.146  -4.204  1.00 159.40 ? 101  TYR A CB  1 
ATOM   619   C  CG  . TYR A 1 101  ? -76.353  68.122  -3.629  1.00 155.55 ? 101  TYR A CG  1 
ATOM   620   C  CD1 . TYR A 1 101  ? -76.803  69.279  -3.030  1.00 156.92 ? 101  TYR A CD1 1 
ATOM   621   C  CD2 . TYR A 1 101  ? -74.985  67.887  -3.667  1.00 152.59 ? 101  TYR A CD2 1 
ATOM   622   C  CE1 . TYR A 1 101  ? -75.932  70.183  -2.490  1.00 156.06 ? 101  TYR A CE1 1 
ATOM   623   C  CE2 . TYR A 1 101  ? -74.092  68.799  -3.127  1.00 151.91 ? 101  TYR A CE2 1 
ATOM   624   C  CZ  . TYR A 1 101  ? -74.582  69.955  -2.536  1.00 154.11 ? 101  TYR A CZ  1 
ATOM   625   O  OH  . TYR A 1 101  ? -73.749  70.902  -1.972  1.00 153.39 ? 101  TYR A OH  1 
ATOM   626   N  N   . VAL A 1 102  ? -79.813  65.424  -2.823  1.00 154.84 ? 102  VAL A N   1 
ATOM   627   C  CA  . VAL A 1 102  ? -81.183  65.021  -3.099  1.00 152.88 ? 102  VAL A CA  1 
ATOM   628   C  C   . VAL A 1 102  ? -82.122  65.982  -2.421  1.00 155.47 ? 102  VAL A C   1 
ATOM   629   O  O   . VAL A 1 102  ? -81.685  66.954  -1.788  1.00 154.18 ? 102  VAL A O   1 
ATOM   630   C  CB  . VAL A 1 102  ? -81.545  63.634  -2.555  1.00 149.19 ? 102  VAL A CB  1 
ATOM   631   C  CG1 . VAL A 1 102  ? -80.470  62.632  -2.878  1.00 145.46 ? 102  VAL A CG1 1 
ATOM   632   C  CG2 . VAL A 1 102  ? -81.799  63.712  -1.058  1.00 147.97 ? 102  VAL A CG2 1 
ATOM   633   N  N   . TYR A 1 103  ? -83.416  65.676  -2.538  1.00 160.50 ? 103  TYR A N   1 
ATOM   634   C  CA  . TYR A 1 103  ? -84.480  66.551  -2.055  1.00 162.79 ? 103  TYR A CA  1 
ATOM   635   C  C   . TYR A 1 103  ? -85.407  65.838  -1.064  1.00 161.79 ? 103  TYR A C   1 
ATOM   636   O  O   . TYR A 1 103  ? -85.979  64.778  -1.355  1.00 157.15 ? 103  TYR A O   1 
ATOM   637   C  CB  . TYR A 1 103  ? -85.266  67.180  -3.232  1.00 175.44 ? 103  TYR A CB  1 
ATOM   638   C  CG  . TYR A 1 103  ? -84.647  68.471  -3.789  1.00 182.16 ? 103  TYR A CG  1 
ATOM   639   C  CD1 . TYR A 1 103  ? -83.447  68.446  -4.499  1.00 186.36 ? 103  TYR A CD1 1 
ATOM   640   C  CD2 . TYR A 1 103  ? -85.267  69.711  -3.606  1.00 187.78 ? 103  TYR A CD2 1 
ATOM   641   C  CE1 . TYR A 1 103  ? -82.875  69.616  -5.002  1.00 189.09 ? 103  TYR A CE1 1 
ATOM   642   C  CE2 . TYR A 1 103  ? -84.700  70.891  -4.110  1.00 190.44 ? 103  TYR A CE2 1 
ATOM   643   C  CZ  . TYR A 1 103  ? -83.498  70.829  -4.807  1.00 191.50 ? 103  TYR A CZ  1 
ATOM   644   O  OH  . TYR A 1 103  ? -82.901  71.962  -5.316  1.00 192.70 ? 103  TYR A OH  1 
ATOM   645   N  N   . LEU A 1 104  ? -85.497  66.422  0.129   1.00 162.30 ? 104  LEU A N   1 
ATOM   646   C  CA  . LEU A 1 104  ? -86.412  65.962  1.163   1.00 164.05 ? 104  LEU A CA  1 
ATOM   647   C  C   . LEU A 1 104  ? -87.689  66.696  0.890   1.00 166.19 ? 104  LEU A C   1 
ATOM   648   O  O   . LEU A 1 104  ? -87.653  67.866  0.537   1.00 163.32 ? 104  LEU A O   1 
ATOM   649   C  CB  . LEU A 1 104  ? -85.895  66.308  2.579   1.00 162.32 ? 104  LEU A CB  1 
ATOM   650   C  CG  . LEU A 1 104  ? -86.570  65.720  3.841   1.00 159.77 ? 104  LEU A CG  1 
ATOM   651   C  CD1 . LEU A 1 104  ? -86.656  64.190  3.817   1.00 159.30 ? 104  LEU A CD1 1 
ATOM   652   C  CD2 . LEU A 1 104  ? -85.864  66.172  5.107   1.00 156.84 ? 104  LEU A CD2 1 
ATOM   653   N  N   . GLU A 1 105  ? -88.813  66.010  1.045   1.00 169.69 ? 105  GLU A N   1 
ATOM   654   C  CA  . GLU A 1 105  ? -90.096  66.635  0.807   1.00 175.23 ? 105  GLU A CA  1 
ATOM   655   C  C   . GLU A 1 105  ? -91.122  66.205  1.834   1.00 176.70 ? 105  GLU A C   1 
ATOM   656   O  O   . GLU A 1 105  ? -91.125  65.068  2.301   1.00 176.51 ? 105  GLU A O   1 
ATOM   657   C  CB  . GLU A 1 105  ? -90.599  66.300  -0.596  1.00 179.24 ? 105  GLU A CB  1 
ATOM   658   C  CG  . GLU A 1 105  ? -91.715  67.215  -1.096  1.00 182.86 ? 105  GLU A CG  1 
ATOM   659   C  CD  . GLU A 1 105  ? -91.947  67.072  -2.591  1.00 185.93 ? 105  GLU A CD  1 
ATOM   660   O  OE1 . GLU A 1 105  ? -92.437  66.003  -3.022  1.00 187.71 ? 105  GLU A OE1 1 
ATOM   661   O  OE2 . GLU A 1 105  ? -91.638  68.031  -3.335  1.00 186.41 ? 105  GLU A OE2 1 
ATOM   662   N  N   . VAL A 1 106  ? -92.004  67.133  2.171   1.00 177.27 ? 106  VAL A N   1 
ATOM   663   C  CA  . VAL A 1 106  ? -93.106  66.841  3.057   1.00 178.66 ? 106  VAL A CA  1 
ATOM   664   C  C   . VAL A 1 106  ? -94.357  67.433  2.444   1.00 181.16 ? 106  VAL A C   1 
ATOM   665   O  O   . VAL A 1 106  ? -94.277  68.370  1.656   1.00 181.75 ? 106  VAL A O   1 
ATOM   666   C  CB  . VAL A 1 106  ? -92.869  67.446  4.420   1.00 177.58 ? 106  VAL A CB  1 
ATOM   667   C  CG1 . VAL A 1 106  ? -94.084  67.243  5.293   1.00 179.27 ? 106  VAL A CG1 1 
ATOM   668   C  CG2 . VAL A 1 106  ? -91.649  66.804  5.040   1.00 176.28 ? 106  VAL A CG2 1 
ATOM   669   N  N   . VAL A 1 107  ? -95.513  66.880  2.795   1.00 182.89 ? 107  VAL A N   1 
ATOM   670   C  CA  . VAL A 1 107  ? -96.765  67.248  2.149   1.00 184.74 ? 107  VAL A CA  1 
ATOM   671   C  C   . VAL A 1 107  ? -97.880  67.291  3.193   1.00 184.00 ? 107  VAL A C   1 
ATOM   672   O  O   . VAL A 1 107  ? -97.849  66.543  4.165   1.00 182.99 ? 107  VAL A O   1 
ATOM   673   C  CB  . VAL A 1 107  ? -97.122  66.232  1.024   1.00 192.33 ? 107  VAL A CB  1 
ATOM   674   C  CG1 . VAL A 1 107  ? -98.266  66.742  0.175   1.00 194.45 ? 107  VAL A CG1 1 
ATOM   675   C  CG2 . VAL A 1 107  ? -95.904  65.930  0.145   1.00 191.18 ? 107  VAL A CG2 1 
ATOM   676   N  N   . SER A 1 108  ? -98.852  68.176  3.004   1.00 187.03 ? 108  SER A N   1 
ATOM   677   C  CA  . SER A 1 108  ? -99.985  68.289  3.922   1.00 190.29 ? 108  SER A CA  1 
ATOM   678   C  C   . SER A 1 108  ? -101.157 68.951  3.206   1.00 198.42 ? 108  SER A C   1 
ATOM   679   O  O   . SER A 1 108  ? -101.181 68.990  1.977   1.00 200.35 ? 108  SER A O   1 
ATOM   680   C  CB  . SER A 1 108  ? -99.597  69.102  5.157   1.00 188.75 ? 108  SER A CB  1 
ATOM   681   O  OG  . SER A 1 108  ? -99.032  70.349  4.792   1.00 187.87 ? 108  SER A OG  1 
ATOM   682   N  N   . LYS A 1 109  ? -102.138 69.451  3.957   1.00 203.44 ? 109  LYS A N   1 
ATOM   683   C  CA  . LYS A 1 109  ? -103.201 70.272  3.359   1.00 210.09 ? 109  LYS A CA  1 
ATOM   684   C  C   . LYS A 1 109  ? -102.842 71.758  3.372   1.00 213.98 ? 109  LYS A C   1 
ATOM   685   O  O   . LYS A 1 109  ? -103.320 72.524  2.532   1.00 215.55 ? 109  LYS A O   1 
ATOM   686   C  CB  . LYS A 1 109  ? -104.579 70.051  4.025   1.00 211.38 ? 109  LYS A CB  1 
ATOM   687   C  CG  . LYS A 1 109  ? -104.660 70.192  5.579   1.00 212.34 ? 109  LYS A CG  1 
ATOM   688   C  CD  . LYS A 1 109  ? -103.917 71.409  6.162   1.00 209.39 ? 109  LYS A CD  1 
ATOM   689   C  CE  . LYS A 1 109  ? -104.182 71.632  7.643   1.00 206.71 ? 109  LYS A CE  1 
ATOM   690   N  NZ  . LYS A 1 109  ? -105.246 72.637  7.868   1.00 207.63 ? 109  LYS A NZ  1 
ATOM   691   N  N   . HIS A 1 110  ? -101.992 72.147  4.329   1.00 215.45 ? 110  HIS A N   1 
ATOM   692   C  CA  . HIS A 1 110  ? -101.749 73.559  4.643   1.00 217.80 ? 110  HIS A CA  1 
ATOM   693   C  C   . HIS A 1 110  ? -100.465 74.169  4.082   1.00 213.41 ? 110  HIS A C   1 
ATOM   694   O  O   . HIS A 1 110  ? -100.406 75.376  3.819   1.00 213.70 ? 110  HIS A O   1 
ATOM   695   C  CB  . HIS A 1 110  ? -101.788 73.806  6.146   1.00 222.97 ? 110  HIS A CB  1 
ATOM   696   C  CG  . HIS A 1 110  ? -101.514 75.227  6.507   1.00 230.14 ? 110  HIS A CG  1 
ATOM   697   N  ND1 . HIS A 1 110  ? -100.662 75.591  7.524   1.00 232.08 ? 110  HIS A ND1 1 
ATOM   698   C  CD2 . HIS A 1 110  ? -101.949 76.380  5.948   1.00 234.03 ? 110  HIS A CD2 1 
ATOM   699   C  CE1 . HIS A 1 110  ? -100.606 76.910  7.596   1.00 233.63 ? 110  HIS A CE1 1 
ATOM   700   N  NE2 . HIS A 1 110  ? -101.376 77.412  6.648   1.00 234.75 ? 110  HIS A NE2 1 
ATOM   701   N  N   . PHE A 1 111  ? -99.431  73.351  3.925   1.00 208.31 ? 111  PHE A N   1 
ATOM   702   C  CA  . PHE A 1 111  ? -98.214  73.810  3.258   1.00 202.21 ? 111  PHE A CA  1 
ATOM   703   C  C   . PHE A 1 111  ? -97.505  72.652  2.562   1.00 192.72 ? 111  PHE A C   1 
ATOM   704   O  O   . PHE A 1 111  ? -97.856  71.481  2.730   1.00 189.45 ? 111  PHE A O   1 
ATOM   705   C  CB  . PHE A 1 111  ? -97.258  74.527  4.243   1.00 202.92 ? 111  PHE A CB  1 
ATOM   706   C  CG  . PHE A 1 111  ? -96.352  75.563  3.587   1.00 204.17 ? 111  PHE A CG  1 
ATOM   707   C  CD1 . PHE A 1 111  ? -96.722  76.898  3.537   1.00 206.08 ? 111  PHE A CD1 1 
ATOM   708   C  CD2 . PHE A 1 111  ? -95.136  75.199  3.026   1.00 203.31 ? 111  PHE A CD2 1 
ATOM   709   C  CE1 . PHE A 1 111  ? -95.898  77.838  2.938   1.00 206.05 ? 111  PHE A CE1 1 
ATOM   710   C  CE2 . PHE A 1 111  ? -94.312  76.139  2.425   1.00 202.83 ? 111  PHE A CE2 1 
ATOM   711   C  CZ  . PHE A 1 111  ? -94.690  77.452  2.384   1.00 204.22 ? 111  PHE A CZ  1 
ATOM   712   N  N   . SER A 1 112  ? -96.516  72.993  1.757   1.00 186.16 ? 112  SER A N   1 
ATOM   713   C  CA  . SER A 1 112  ? -95.585  71.995  1.311   1.00 180.53 ? 112  SER A CA  1 
ATOM   714   C  C   . SER A 1 112  ? -94.206  72.630  1.240   1.00 178.49 ? 112  SER A C   1 
ATOM   715   O  O   . SER A 1 112  ? -94.066  73.790  0.818   1.00 178.96 ? 112  SER A O   1 
ATOM   716   C  CB  . SER A 1 112  ? -96.003  71.419  -0.026  1.00 177.82 ? 112  SER A CB  1 
ATOM   717   O  OG  . SER A 1 112  ? -95.601  70.066  -0.112  1.00 175.12 ? 112  SER A OG  1 
ATOM   718   N  N   . LYS A 1 113  ? -93.204  71.866  1.691   1.00 175.58 ? 113  LYS A N   1 
ATOM   719   C  CA  . LYS A 1 113  ? -91.812  72.313  1.749   1.00 170.50 ? 113  LYS A CA  1 
ATOM   720   C  C   . LYS A 1 113  ? -90.811  71.163  1.673   1.00 164.95 ? 113  LYS A C   1 
ATOM   721   O  O   . LYS A 1 113  ? -91.097  70.027  2.051   1.00 163.43 ? 113  LYS A O   1 
ATOM   722   C  CB  . LYS A 1 113  ? -91.553  73.150  3.003   1.00 170.99 ? 113  LYS A CB  1 
ATOM   723   C  CG  . LYS A 1 113  ? -90.178  73.808  3.020   1.00 172.40 ? 113  LYS A CG  1 
ATOM   724   C  CD  . LYS A 1 113  ? -90.184  75.214  2.420   1.00 175.63 ? 113  LYS A CD  1 
ATOM   725   C  CE  . LYS A 1 113  ? -88.816  75.883  2.576   1.00 175.13 ? 113  LYS A CE  1 
ATOM   726   N  NZ  . LYS A 1 113  ? -88.847  77.378  2.530   1.00 175.08 ? 113  LYS A NZ  1 
ATOM   727   N  N   . SER A 1 114  ? -89.622  71.495  1.196   1.00 165.01 ? 114  SER A N   1 
ATOM   728   C  CA  . SER A 1 114  ? -88.610  70.503  0.883   1.00 168.58 ? 114  SER A CA  1 
ATOM   729   C  C   . SER A 1 114  ? -87.205  71.082  1.114   1.00 168.57 ? 114  SER A C   1 
ATOM   730   O  O   . SER A 1 114  ? -87.085  72.200  1.633   1.00 167.09 ? 114  SER A O   1 
ATOM   731   C  CB  . SER A 1 114  ? -88.799  70.010  -0.559  1.00 172.36 ? 114  SER A CB  1 
ATOM   732   O  OG  . SER A 1 114  ? -89.609  70.901  -1.316  1.00 175.00 ? 114  SER A OG  1 
ATOM   733   N  N   . LYS A 1 115  ? -86.152  70.337  0.755   1.00 168.57 ? 115  LYS A N   1 
ATOM   734   C  CA  . LYS A 1 115  ? -84.786  70.783  1.054   1.00 166.86 ? 115  LYS A CA  1 
ATOM   735   C  C   . LYS A 1 115  ? -83.720  70.145  0.178   1.00 166.07 ? 115  LYS A C   1 
ATOM   736   O  O   . LYS A 1 115  ? -83.825  68.973  -0.166  1.00 164.75 ? 115  LYS A O   1 
ATOM   737   C  CB  . LYS A 1 115  ? -84.451  70.496  2.523   1.00 165.69 ? 115  LYS A CB  1 
ATOM   738   C  CG  . LYS A 1 115  ? -83.055  70.937  2.971   1.00 161.63 ? 115  LYS A CG  1 
ATOM   739   C  CD  . LYS A 1 115  ? -83.031  72.352  3.556   1.00 158.77 ? 115  LYS A CD  1 
ATOM   740   C  CE  . LYS A 1 115  ? -81.734  72.604  4.335   1.00 154.67 ? 115  LYS A CE  1 
ATOM   741   N  NZ  . LYS A 1 115  ? -81.582  74.017  4.780   1.00 153.01 ? 115  LYS A NZ  1 
ATOM   742   N  N   . ARG A 1 116  ? -82.700  70.929  -0.175  1.00 167.05 ? 116  ARG A N   1 
ATOM   743   C  CA  . ARG A 1 116  ? -81.490  70.415  -0.828  1.00 170.28 ? 116  ARG A CA  1 
ATOM   744   C  C   . ARG A 1 116  ? -80.448  70.084  0.224   1.00 169.80 ? 116  ARG A C   1 
ATOM   745   O  O   . ARG A 1 116  ? -80.014  70.963  0.962   1.00 171.27 ? 116  ARG A O   1 
ATOM   746   C  CB  . ARG A 1 116  ? -80.919  71.452  -1.797  1.00 173.69 ? 116  ARG A CB  1 
ATOM   747   C  CG  . ARG A 1 116  ? -79.539  71.126  -2.375  1.00 176.65 ? 116  ARG A CG  1 
ATOM   748   C  CD  . ARG A 1 116  ? -78.438  71.988  -1.743  1.00 180.39 ? 116  ARG A CD  1 
ATOM   749   N  NE  . ARG A 1 116  ? -77.516  72.548  -2.739  1.00 183.89 ? 116  ARG A NE  1 
ATOM   750   C  CZ  . ARG A 1 116  ? -76.289  73.006  -2.474  1.00 185.55 ? 116  ARG A CZ  1 
ATOM   751   N  NH1 . ARG A 1 116  ? -75.802  72.954  -1.236  1.00 185.74 ? 116  ARG A NH1 1 
ATOM   752   N  NH2 . ARG A 1 116  ? -75.532  73.497  -3.452  1.00 185.68 ? 116  ARG A NH2 1 
ATOM   753   N  N   . MET A 1 117  ? -80.027  68.829  0.294   1.00 168.19 ? 117  MET A N   1 
ATOM   754   C  CA  . MET A 1 117  ? -79.155  68.422  1.390   1.00 165.26 ? 117  MET A CA  1 
ATOM   755   C  C   . MET A 1 117  ? -78.347  67.162  1.073   1.00 161.34 ? 117  MET A C   1 
ATOM   756   O  O   . MET A 1 117  ? -78.919  66.097  0.811   1.00 159.82 ? 117  MET A O   1 
ATOM   757   C  CB  . MET A 1 117  ? -79.984  68.210  2.653   1.00 166.58 ? 117  MET A CB  1 
ATOM   758   C  CG  . MET A 1 117  ? -81.160  67.271  2.438   1.00 168.42 ? 117  MET A CG  1 
ATOM   759   S  SD  . MET A 1 117  ? -81.945  66.848  3.989   1.00 170.47 ? 117  MET A SD  1 
ATOM   760   C  CE  . MET A 1 117  ? -81.843  68.434  4.796   1.00 131.93 ? 117  MET A CE  1 
ATOM   761   N  N   . PRO A 1 118  ? -77.006  67.285  1.118   1.00 159.11 ? 118  PRO A N   1 
ATOM   762   C  CA  . PRO A 1 118  ? -76.064  66.239  0.706   1.00 156.29 ? 118  PRO A CA  1 
ATOM   763   C  C   . PRO A 1 118  ? -76.316  64.864  1.325   1.00 154.85 ? 118  PRO A C   1 
ATOM   764   O  O   . PRO A 1 118  ? -76.890  64.765  2.415   1.00 153.55 ? 118  PRO A O   1 
ATOM   765   C  CB  . PRO A 1 118  ? -74.712  66.801  1.149   1.00 154.33 ? 118  PRO A CB  1 
ATOM   766   C  CG  . PRO A 1 118  ? -74.889  68.278  1.051   1.00 155.29 ? 118  PRO A CG  1 
ATOM   767   C  CD  . PRO A 1 118  ? -76.310  68.536  1.477   1.00 158.15 ? 118  PRO A CD  1 
ATOM   768   N  N   . ILE A 1 119  ? -75.881  63.820  0.610   1.00 155.05 ? 119  ILE A N   1 
ATOM   769   C  CA  . ILE A 1 119  ? -76.053  62.431  1.047   1.00 153.42 ? 119  ILE A CA  1 
ATOM   770   C  C   . ILE A 1 119  ? -74.827  61.575  0.757   1.00 151.31 ? 119  ILE A C   1 
ATOM   771   O  O   . ILE A 1 119  ? -73.943  61.990  0.003   1.00 148.36 ? 119  ILE A O   1 
ATOM   772   C  CB  . ILE A 1 119  ? -77.249  61.759  0.368   1.00 152.87 ? 119  ILE A CB  1 
ATOM   773   C  CG1 . ILE A 1 119  ? -76.875  61.288  -1.032  1.00 150.06 ? 119  ILE A CG1 1 
ATOM   774   C  CG2 . ILE A 1 119  ? -78.459  62.684  0.343   1.00 153.79 ? 119  ILE A CG2 1 
ATOM   775   C  CD1 . ILE A 1 119  ? -77.976  60.486  -1.647  1.00 151.34 ? 119  ILE A CD1 1 
ATOM   776   N  N   . THR A 1 120  ? -74.791  60.381  1.351   1.00 152.16 ? 120  THR A N   1 
ATOM   777   C  CA  . THR A 1 120  ? -73.594  59.547  1.293   1.00 152.70 ? 120  THR A CA  1 
ATOM   778   C  C   . THR A 1 120  ? -73.831  58.054  1.247   1.00 153.01 ? 120  THR A C   1 
ATOM   779   O  O   . THR A 1 120  ? -74.934  57.565  1.523   1.00 154.12 ? 120  THR A O   1 
ATOM   780   C  CB  . THR A 1 120  ? -72.650  59.814  2.467   1.00 153.99 ? 120  THR A CB  1 
ATOM   781   O  OG1 . THR A 1 120  ? -72.661  61.215  2.755   1.00 155.22 ? 120  THR A OG1 1 
ATOM   782   C  CG2 . THR A 1 120  ? -71.198  59.330  2.146   1.00 115.32 ? 120  THR A CG2 1 
ATOM   783   N  N   . TYR A 1 121  ? -72.739  57.359  0.920   1.00 174.91 ? 121  TYR A N   1 
ATOM   784   C  CA  . TYR A 1 121  ? -72.730  55.955  0.567   1.00 174.68 ? 121  TYR A CA  1 
ATOM   785   C  C   . TYR A 1 121  ? -72.176  55.103  1.665   1.00 166.26 ? 121  TYR A C   1 
ATOM   786   O  O   . TYR A 1 121  ? -72.036  53.901  1.497   1.00 167.12 ? 121  TYR A O   1 
ATOM   787   C  CB  . TYR A 1 121  ? -71.829  55.735  -0.629  1.00 180.17 ? 121  TYR A CB  1 
ATOM   788   C  CG  . TYR A 1 121  ? -72.180  56.529  -1.861  1.00 185.55 ? 121  TYR A CG  1 
ATOM   789   C  CD1 . TYR A 1 121  ? -73.367  56.305  -2.545  1.00 189.52 ? 121  TYR A CD1 1 
ATOM   790   C  CD2 . TYR A 1 121  ? -71.300  57.477  -2.361  1.00 186.05 ? 121  TYR A CD2 1 
ATOM   791   C  CE1 . TYR A 1 121  ? -73.670  57.017  -3.668  1.00 192.89 ? 121  TYR A CE1 1 
ATOM   792   C  CE2 . TYR A 1 121  ? -71.592  58.188  -3.483  1.00 188.83 ? 121  TYR A CE2 1 
ATOM   793   C  CZ  . TYR A 1 121  ? -72.777  57.957  -4.134  1.00 193.69 ? 121  TYR A CZ  1 
ATOM   794   O  OH  . TYR A 1 121  ? -73.066  58.671  -5.271  1.00 199.19 ? 121  TYR A OH  1 
ATOM   795   N  N   . ASP A 1 122  ? -71.809  55.730  2.770   1.00 158.84 ? 122  ASP A N   1 
ATOM   796   C  CA  . ASP A 1 122  ? -71.402  55.002  3.961   1.00 151.21 ? 122  ASP A CA  1 
ATOM   797   C  C   . ASP A 1 122  ? -72.577  54.374  4.682   1.00 146.18 ? 122  ASP A C   1 
ATOM   798   O  O   . ASP A 1 122  ? -73.267  55.069  5.404   1.00 147.84 ? 122  ASP A O   1 
ATOM   799   C  CB  . ASP A 1 122  ? -70.768  55.981  4.929   1.00 150.88 ? 122  ASP A CB  1 
ATOM   800   C  CG  . ASP A 1 122  ? -69.313  55.737  5.116   1.00 151.01 ? 122  ASP A CG  1 
ATOM   801   O  OD1 . ASP A 1 122  ? -68.555  56.731  5.169   1.00 150.59 ? 122  ASP A OD1 1 
ATOM   802   O  OD2 . ASP A 1 122  ? -68.934  54.551  5.212   1.00 151.17 ? 122  ASP A OD2 1 
ATOM   803   N  N   . ASN A 1 123  ? -72.810  53.077  4.535   1.00 141.69 ? 123  ASN A N   1 
ATOM   804   C  CA  . ASN A 1 123  ? -73.859  52.456  5.335   1.00 139.44 ? 123  ASN A CA  1 
ATOM   805   C  C   . ASN A 1 123  ? -73.303  51.320  6.154   1.00 139.00 ? 123  ASN A C   1 
ATOM   806   O  O   . ASN A 1 123  ? -72.894  50.302  5.592   1.00 140.01 ? 123  ASN A O   1 
ATOM   807   C  CB  . ASN A 1 123  ? -75.025  51.958  4.482   1.00 141.57 ? 123  ASN A CB  1 
ATOM   808   C  CG  . ASN A 1 123  ? -76.103  51.230  5.299   1.00 140.63 ? 123  ASN A CG  1 
ATOM   809   O  OD1 . ASN A 1 123  ? -77.244  51.086  4.859   1.00 142.75 ? 123  ASN A OD1 1 
ATOM   810   N  ND2 . ASN A 1 123  ? -75.739  50.760  6.474   1.00 139.20 ? 123  ASN A ND2 1 
ATOM   811   N  N   . GLY A 1 124  ? -73.309  51.513  7.484   1.00 139.67 ? 124  GLY A N   1 
ATOM   812   C  CA  . GLY A 1 124  ? -72.902  50.503  8.446   1.00 140.84 ? 124  GLY A CA  1 
ATOM   813   C  C   . GLY A 1 124  ? -71.445  50.554  8.850   1.00 121.61 ? 124  GLY A C   1 
ATOM   814   O  O   . GLY A 1 124  ? -70.811  51.594  8.775   1.00 120.80 ? 124  GLY A O   1 
ATOM   815   N  N   . PHE A 1 125  ? -70.921  49.403  9.250   1.00 120.52 ? 125  PHE A N   1 
ATOM   816   C  CA  . PHE A 1 125  ? -69.628  49.296  9.899   1.00 118.02 ? 125  PHE A CA  1 
ATOM   817   C  C   . PHE A 1 125  ? -68.958  47.961  9.588   1.00 118.00 ? 125  PHE A C   1 
ATOM   818   O  O   . PHE A 1 125  ? -69.569  46.916  9.798   1.00 118.65 ? 125  PHE A O   1 
ATOM   819   C  CB  . PHE A 1 125  ? -69.841  49.323  11.412  1.00 116.07 ? 125  PHE A CB  1 
ATOM   820   C  CG  . PHE A 1 125  ? -70.541  50.543  11.908  1.00 115.97 ? 125  PHE A CG  1 
ATOM   821   C  CD1 . PHE A 1 125  ? -71.889  50.495  12.242  1.00 117.49 ? 125  PHE A CD1 1 
ATOM   822   C  CD2 . PHE A 1 125  ? -69.849  51.745  12.057  1.00 114.80 ? 125  PHE A CD2 1 
ATOM   823   C  CE1 . PHE A 1 125  ? -72.545  51.626  12.709  1.00 117.75 ? 125  PHE A CE1 1 
ATOM   824   C  CE2 . PHE A 1 125  ? -70.496  52.881  12.512  1.00 116.27 ? 125  PHE A CE2 1 
ATOM   825   C  CZ  . PHE A 1 125  ? -71.855  52.821  12.846  1.00 117.44 ? 125  PHE A CZ  1 
ATOM   826   N  N   . LEU A 1 126  ? -67.705  47.969  9.132   1.00 117.26 ? 126  LEU A N   1 
ATOM   827   C  CA  . LEU A 1 126  ? -66.969  46.713  8.976   1.00 117.03 ? 126  LEU A CA  1 
ATOM   828   C  C   . LEU A 1 126  ? -65.970  46.485  10.133  1.00 121.28 ? 126  LEU A C   1 
ATOM   829   O  O   . LEU A 1 126  ? -65.111  47.331  10.406  1.00 120.63 ? 126  LEU A O   1 
ATOM   830   C  CB  . LEU A 1 126  ? -66.271  46.646  7.618   1.00 118.33 ? 126  LEU A CB  1 
ATOM   831   C  CG  . LEU A 1 126  ? -67.006  46.254  6.327   1.00 121.29 ? 126  LEU A CG  1 
ATOM   832   C  CD1 . LEU A 1 126  ? -68.192  45.328  6.593   1.00 122.51 ? 126  LEU A CD1 1 
ATOM   833   C  CD2 . LEU A 1 126  ? -67.436  47.480  5.515   1.00 122.76 ? 126  LEU A CD2 1 
ATOM   834   N  N   . PHE A 1 127  ? -66.090  45.347  10.819  1.00 118.15 ? 127  PHE A N   1 
ATOM   835   C  CA  . PHE A 1 127  ? -65.276  45.058  12.006  1.00 113.52 ? 127  PHE A CA  1 
ATOM   836   C  C   . PHE A 1 127  ? -64.359  43.863  11.794  1.00 112.11 ? 127  PHE A C   1 
ATOM   837   O  O   . PHE A 1 127  ? -64.827  42.733  11.869  1.00 114.13 ? 127  PHE A O   1 
ATOM   838   C  CB  . PHE A 1 127  ? -66.182  44.732  13.193  1.00 115.76 ? 127  PHE A CB  1 
ATOM   839   C  CG  . PHE A 1 127  ? -66.770  45.950  13.877  1.00 116.62 ? 127  PHE A CG  1 
ATOM   840   C  CD1 . PHE A 1 127  ? -66.028  47.105  14.052  1.00 115.60 ? 127  PHE A CD1 1 
ATOM   841   C  CD2 . PHE A 1 127  ? -68.063  45.921  14.374  1.00 115.62 ? 127  PHE A CD2 1 
ATOM   842   C  CE1 . PHE A 1 127  ? -66.572  48.201  14.681  1.00 112.19 ? 127  PHE A CE1 1 
ATOM   843   C  CE2 . PHE A 1 127  ? -68.607  47.017  14.999  1.00 111.84 ? 127  PHE A CE2 1 
ATOM   844   C  CZ  . PHE A 1 127  ? -67.857  48.158  15.147  1.00 112.06 ? 127  PHE A CZ  1 
ATOM   845   N  N   . ILE A 1 128  ? -63.059  44.089  11.591  1.00 111.49 ? 128  ILE A N   1 
ATOM   846   C  CA  . ILE A 1 128  ? -62.154  42.994  11.182  1.00 112.36 ? 128  ILE A CA  1 
ATOM   847   C  C   . ILE A 1 128  ? -61.408  42.251  12.300  1.00 112.40 ? 128  ILE A C   1 
ATOM   848   O  O   . ILE A 1 128  ? -60.365  42.691  12.791  1.00 107.35 ? 128  ILE A O   1 
ATOM   849   C  CB  . ILE A 1 128  ? -61.127  43.457  10.140  1.00 110.88 ? 128  ILE A CB  1 
ATOM   850   C  CG1 . ILE A 1 128  ? -61.637  44.682  9.380   1.00 112.30 ? 128  ILE A CG1 1 
ATOM   851   C  CG2 . ILE A 1 128  ? -60.842  42.338  9.182   1.00 112.41 ? 128  ILE A CG2 1 
ATOM   852   C  CD1 . ILE A 1 128  ? -60.653  45.205  8.380   1.00 112.08 ? 128  ILE A CD1 1 
ATOM   853   N  N   . HIS A 1 129  ? -61.931  41.087  12.653  1.00 114.55 ? 129  HIS A N   1 
ATOM   854   C  CA  . HIS A 1 129  ? -61.434  40.328  13.794  1.00 115.78 ? 129  HIS A CA  1 
ATOM   855   C  C   . HIS A 1 129  ? -60.361  39.305  13.423  1.00 118.54 ? 129  HIS A C   1 
ATOM   856   O  O   . HIS A 1 129  ? -60.642  38.125  13.202  1.00 121.99 ? 129  HIS A O   1 
ATOM   857   C  CB  . HIS A 1 129  ? -62.616  39.652  14.495  1.00 113.91 ? 129  HIS A CB  1 
ATOM   858   C  CG  . HIS A 1 129  ? -62.248  38.918  15.743  1.00 110.76 ? 129  HIS A CG  1 
ATOM   859   N  ND1 . HIS A 1 129  ? -63.179  38.247  16.511  1.00 110.55 ? 129  HIS A ND1 1 
ATOM   860   C  CD2 . HIS A 1 129  ? -61.051  38.734  16.352  1.00 108.97 ? 129  HIS A CD2 1 
ATOM   861   C  CE1 . HIS A 1 129  ? -62.572  37.692  17.546  1.00 111.07 ? 129  HIS A CE1 1 
ATOM   862   N  NE2 . HIS A 1 129  ? -61.281  37.970  17.471  1.00 110.57 ? 129  HIS A NE2 1 
ATOM   863   N  N   . THR A 1 130  ? -59.124  39.766  13.345  1.00 118.22 ? 130  THR A N   1 
ATOM   864   C  CA  . THR A 1 130  ? -58.022  38.853  13.147  1.00 118.77 ? 130  THR A CA  1 
ATOM   865   C  C   . THR A 1 130  ? -57.849  38.170  14.493  1.00 118.82 ? 130  THR A C   1 
ATOM   866   O  O   . THR A 1 130  ? -58.127  38.777  15.526  1.00 119.66 ? 130  THR A O   1 
ATOM   867   C  CB  . THR A 1 130  ? -56.774  39.611  12.772  1.00 116.78 ? 130  THR A CB  1 
ATOM   868   O  OG1 . THR A 1 130  ? -55.639  38.807  13.079  1.00 115.61 ? 130  THR A OG1 1 
ATOM   869   C  CG2 . THR A 1 130  ? -56.695  40.900  13.569  1.00 115.55 ? 130  THR A CG2 1 
ATOM   870   N  N   . ASP A 1 131  ? -57.430  36.911  14.512  1.00 118.63 ? 131  ASP A N   1 
ATOM   871   C  CA  . ASP A 1 131  ? -57.418  36.195  15.782  1.00 118.25 ? 131  ASP A CA  1 
ATOM   872   C  C   . ASP A 1 131  ? -56.411  36.793  16.757  1.00 119.72 ? 131  ASP A C   1 
ATOM   873   O  O   . ASP A 1 131  ? -56.759  37.102  17.891  1.00 120.69 ? 131  ASP A O   1 
ATOM   874   C  CB  . ASP A 1 131  ? -57.198  34.696  15.604  1.00 117.83 ? 131  ASP A CB  1 
ATOM   875   C  CG  . ASP A 1 131  ? -55.772  34.362  15.310  1.00 117.11 ? 131  ASP A CG  1 
ATOM   876   O  OD1 . ASP A 1 131  ? -55.114  35.207  14.686  1.00 116.50 ? 131  ASP A OD1 1 
ATOM   877   O  OD2 . ASP A 1 131  ? -55.305  33.265  15.686  1.00 117.53 ? 131  ASP A OD2 1 
ATOM   878   N  N   . LYS A 1 132  ? -55.175  36.987  16.324  1.00 120.29 ? 132  LYS A N   1 
ATOM   879   C  CA  . LYS A 1 132  ? -54.200  37.655  17.180  1.00 120.45 ? 132  LYS A CA  1 
ATOM   880   C  C   . LYS A 1 132  ? -53.432  38.720  16.397  1.00 123.06 ? 132  LYS A C   1 
ATOM   881   O  O   . LYS A 1 132  ? -53.609  38.817  15.197  1.00 129.22 ? 132  LYS A O   1 
ATOM   882   C  CB  . LYS A 1 132  ? -53.311  36.639  17.908  1.00 115.23 ? 132  LYS A CB  1 
ATOM   883   C  CG  . LYS A 1 132  ? -52.118  36.104  17.180  1.00 109.90 ? 132  LYS A CG  1 
ATOM   884   C  CD  . LYS A 1 132  ? -51.810  34.716  17.732  1.00 104.77 ? 132  LYS A CD  1 
ATOM   885   C  CE  . LYS A 1 132  ? -50.585  34.108  17.089  1.00 103.18 ? 132  LYS A CE  1 
ATOM   886   N  NZ  . LYS A 1 132  ? -50.883  32.684  16.828  1.00 106.89 ? 132  LYS A NZ  1 
ATOM   887   N  N   . PRO A 1 133  ? -52.626  39.561  17.066  1.00 119.25 ? 133  PRO A N   1 
ATOM   888   C  CA  . PRO A 1 133  ? -52.240  40.710  16.271  1.00 111.27 ? 133  PRO A CA  1 
ATOM   889   C  C   . PRO A 1 133  ? -50.770  40.601  15.945  1.00 110.68 ? 133  PRO A C   1 
ATOM   890   O  O   . PRO A 1 133  ? -50.195  41.619  15.577  1.00 109.90 ? 133  PRO A O   1 
ATOM   891   C  CB  . PRO A 1 133  ? -52.393  41.845  17.261  1.00 109.43 ? 133  PRO A CB  1 
ATOM   892   C  CG  . PRO A 1 133  ? -52.002  41.170  18.627  1.00 116.80 ? 133  PRO A CG  1 
ATOM   893   C  CD  . PRO A 1 133  ? -52.000  39.655  18.393  1.00 117.61 ? 133  PRO A CD  1 
ATOM   894   N  N   . VAL A 1 134  ? -50.150  39.437  16.115  1.00 104.87 ? 134  VAL A N   1 
ATOM   895   C  CA  . VAL A 1 134  ? -48.775  39.302  15.657  1.00 101.92 ? 134  VAL A CA  1 
ATOM   896   C  C   . VAL A 1 134  ? -48.441  37.903  15.215  1.00 106.64 ? 134  VAL A C   1 
ATOM   897   O  O   . VAL A 1 134  ? -48.695  36.932  15.933  1.00 110.94 ? 134  VAL A O   1 
ATOM   898   C  CB  . VAL A 1 134  ? -47.741  39.763  16.691  1.00 98.21  ? 134  VAL A CB  1 
ATOM   899   C  CG1 . VAL A 1 134  ? -46.447  39.064  16.472  1.00 98.42  ? 134  VAL A CG1 1 
ATOM   900   C  CG2 . VAL A 1 134  ? -47.508  41.248  16.555  1.00 97.26  ? 134  VAL A CG2 1 
ATOM   901   N  N   . TYR A 1 135  ? -47.845  37.817  14.024  1.00 112.00 ? 135  TYR A N   1 
ATOM   902   C  CA  . TYR A 1 135  ? -47.504  36.539  13.401  1.00 110.98 ? 135  TYR A CA  1 
ATOM   903   C  C   . TYR A 1 135  ? -46.060  36.396  12.992  1.00 107.14 ? 135  TYR A C   1 
ATOM   904   O  O   . TYR A 1 135  ? -45.331  37.374  12.769  1.00 102.16 ? 135  TYR A O   1 
ATOM   905   C  CB  . TYR A 1 135  ? -48.362  36.300  12.180  1.00 104.66 ? 135  TYR A CB  1 
ATOM   906   C  CG  . TYR A 1 135  ? -49.803  36.348  12.510  1.00 104.94 ? 135  TYR A CG  1 
ATOM   907   C  CD1 . TYR A 1 135  ? -50.503  35.190  12.799  1.00 105.88 ? 135  TYR A CD1 1 
ATOM   908   C  CD2 . TYR A 1 135  ? -50.466  37.559  12.577  1.00 104.30 ? 135  TYR A CD2 1 
ATOM   909   C  CE1 . TYR A 1 135  ? -51.840  35.237  13.118  1.00 106.18 ? 135  TYR A CE1 1 
ATOM   910   C  CE2 . TYR A 1 135  ? -51.796  37.619  12.893  1.00 104.62 ? 135  TYR A CE2 1 
ATOM   911   C  CZ  . TYR A 1 135  ? -52.481  36.458  13.162  1.00 105.54 ? 135  TYR A CZ  1 
ATOM   912   O  OH  . TYR A 1 135  ? -53.815  36.524  13.471  1.00 105.90 ? 135  TYR A OH  1 
ATOM   913   N  N   . THR A 1 136  ? -45.671  35.138  12.873  1.00 106.70 ? 136  THR A N   1 
ATOM   914   C  CA  . THR A 1 136  ? -44.323  34.790  12.509  1.00 107.66 ? 136  THR A CA  1 
ATOM   915   C  C   . THR A 1 136  ? -44.406  33.918  11.288  1.00 110.93 ? 136  THR A C   1 
ATOM   916   O  O   . THR A 1 136  ? -45.359  33.158  11.136  1.00 109.45 ? 136  THR A O   1 
ATOM   917   C  CB  . THR A 1 136  ? -43.681  33.963  13.602  1.00 110.21 ? 136  THR A CB  1 
ATOM   918   O  OG1 . THR A 1 136  ? -44.719  33.370  14.403  1.00 111.48 ? 136  THR A OG1 1 
ATOM   919   C  CG2 . THR A 1 136  ? -42.800  34.850  14.462  1.00 108.47 ? 136  THR A CG2 1 
ATOM   920   N  N   . PRO A 1 137  ? -43.400  34.018  10.415  1.00 110.11 ? 137  PRO A N   1 
ATOM   921   C  CA  . PRO A 1 137  ? -43.366  33.252  9.179   1.00 108.26 ? 137  PRO A CA  1 
ATOM   922   C  C   . PRO A 1 137  ? -44.088  31.921  9.316   1.00 109.58 ? 137  PRO A C   1 
ATOM   923   O  O   . PRO A 1 137  ? -43.734  31.114  10.187  1.00 109.39 ? 137  PRO A O   1 
ATOM   924   C  CB  . PRO A 1 137  ? -41.878  33.008  8.997   1.00 110.78 ? 137  PRO A CB  1 
ATOM   925   C  CG  . PRO A 1 137  ? -41.233  34.218  9.571   1.00 107.16 ? 137  PRO A CG  1 
ATOM   926   C  CD  . PRO A 1 137  ? -42.154  34.775  10.621  1.00 108.11 ? 137  PRO A CD  1 
ATOM   927   N  N   . ASP A 1 138  ? -45.101  31.731  8.470   1.00 110.98 ? 138  ASP A N   1 
ATOM   928   C  CA  . ASP A 1 138  ? -45.763  30.441  8.248   1.00 112.68 ? 138  ASP A CA  1 
ATOM   929   C  C   . ASP A 1 138  ? -46.964  30.147  9.118   1.00 116.54 ? 138  ASP A C   1 
ATOM   930   O  O   . ASP A 1 138  ? -47.598  29.111  8.932   1.00 117.26 ? 138  ASP A O   1 
ATOM   931   C  CB  . ASP A 1 138  ? -44.767  29.284  8.301   1.00 123.98 ? 138  ASP A CB  1 
ATOM   932   C  CG  . ASP A 1 138  ? -43.920  29.212  7.050   1.00 128.99 ? 138  ASP A CG  1 
ATOM   933   O  OD1 . ASP A 1 138  ? -44.479  29.489  5.965   1.00 131.06 ? 138  ASP A OD1 1 
ATOM   934   O  OD2 . ASP A 1 138  ? -42.709  28.898  7.135   1.00 128.69 ? 138  ASP A OD2 1 
ATOM   935   N  N   . GLN A 1 139  ? -47.283  31.041  10.059  1.00 118.20 ? 139  GLN A N   1 
ATOM   936   C  CA  . GLN A 1 139  ? -48.488  30.871  10.873  1.00 118.95 ? 139  GLN A CA  1 
ATOM   937   C  C   . GLN A 1 139  ? -49.644  31.102  9.921   1.00 121.96 ? 139  GLN A C   1 
ATOM   938   O  O   . GLN A 1 139  ? -49.448  31.653  8.830   1.00 122.32 ? 139  GLN A O   1 
ATOM   939   C  CB  . GLN A 1 139  ? -48.574  31.859  12.058  1.00 119.68 ? 139  GLN A CB  1 
ATOM   940   C  CG  . GLN A 1 139  ? -47.327  32.037  12.960  1.00 119.07 ? 139  GLN A CG  1 
ATOM   941   C  CD  . GLN A 1 139  ? -47.701  32.398  14.404  1.00 118.58 ? 139  GLN A CD  1 
ATOM   942   O  OE1 . GLN A 1 139  ? -47.315  33.451  14.947  1.00 115.35 ? 139  GLN A OE1 1 
ATOM   943   N  NE2 . GLN A 1 139  ? -48.477  31.516  15.025  1.00 120.23 ? 139  GLN A NE2 1 
ATOM   944   N  N   . SER A 1 140  ? -50.841  30.670  10.302  1.00 122.46 ? 140  SER A N   1 
ATOM   945   C  CA  . SER A 1 140  ? -52.002  30.963  9.469   1.00 124.01 ? 140  SER A CA  1 
ATOM   946   C  C   . SER A 1 140  ? -52.920  31.927  10.182  1.00 120.78 ? 140  SER A C   1 
ATOM   947   O  O   . SER A 1 140  ? -53.475  31.599  11.225  1.00 119.95 ? 140  SER A O   1 
ATOM   948   C  CB  . SER A 1 140  ? -52.756  29.697  9.032   1.00 126.17 ? 140  SER A CB  1 
ATOM   949   O  OG  . SER A 1 140  ? -52.367  29.297  7.713   1.00 127.00 ? 140  SER A OG  1 
ATOM   950   N  N   . VAL A 1 141  ? -53.056  33.121  9.614   1.00 121.24 ? 141  VAL A N   1 
ATOM   951   C  CA  . VAL A 1 141  ? -53.888  34.172  10.180  1.00 114.95 ? 141  VAL A CA  1 
ATOM   952   C  C   . VAL A 1 141  ? -55.343  33.754  10.181  1.00 120.11 ? 141  VAL A C   1 
ATOM   953   O  O   . VAL A 1 141  ? -55.930  33.572  9.124   1.00 120.78 ? 141  VAL A O   1 
ATOM   954   C  CB  . VAL A 1 141  ? -53.806  35.450  9.334   1.00 111.91 ? 141  VAL A CB  1 
ATOM   955   C  CG1 . VAL A 1 141  ? -54.664  36.513  9.944   1.00 110.22 ? 141  VAL A CG1 1 
ATOM   956   C  CG2 . VAL A 1 141  ? -52.368  35.926  9.195   1.00 110.11 ? 141  VAL A CG2 1 
ATOM   957   N  N   . LYS A 1 142  ? -55.933  33.589  11.355  1.00 117.52 ? 142  LYS A N   1 
ATOM   958   C  CA  . LYS A 1 142  ? -57.372  33.376  11.410  1.00 122.23 ? 142  LYS A CA  1 
ATOM   959   C  C   . LYS A 1 142  ? -58.042  34.734  11.209  1.00 124.75 ? 142  LYS A C   1 
ATOM   960   O  O   . LYS A 1 142  ? -57.503  35.751  11.636  1.00 125.63 ? 142  LYS A O   1 
ATOM   961   C  CB  . LYS A 1 142  ? -57.801  32.731  12.733  1.00 120.99 ? 142  LYS A CB  1 
ATOM   962   C  CG  . LYS A 1 142  ? -57.540  31.232  12.795  1.00 123.19 ? 142  LYS A CG  1 
ATOM   963   C  CD  . LYS A 1 142  ? -58.564  30.525  13.673  1.00 124.49 ? 142  LYS A CD  1 
ATOM   964   C  CE  . LYS A 1 142  ? -58.495  29.000  13.530  1.00 126.78 ? 142  LYS A CE  1 
ATOM   965   N  NZ  . LYS A 1 142  ? -57.175  28.411  13.940  1.00 125.94 ? 142  LYS A NZ  1 
ATOM   966   N  N   . VAL A 1 143  ? -59.193  34.766  10.540  1.00 127.03 ? 143  VAL A N   1 
ATOM   967   C  CA  . VAL A 1 143  ? -59.915  36.027  10.337  1.00 125.32 ? 143  VAL A CA  1 
ATOM   968   C  C   . VAL A 1 143  ? -61.422  35.879  10.148  1.00 124.42 ? 143  VAL A C   1 
ATOM   969   O  O   . VAL A 1 143  ? -61.913  34.909  9.577   1.00 126.94 ? 143  VAL A O   1 
ATOM   970   C  CB  . VAL A 1 143  ? -59.300  36.900  9.185   1.00 114.21 ? 143  VAL A CB  1 
ATOM   971   C  CG1 . VAL A 1 143  ? -58.308  36.111  8.352   1.00 115.06 ? 143  VAL A CG1 1 
ATOM   972   C  CG2 . VAL A 1 143  ? -60.384  37.511  8.308   1.00 115.87 ? 143  VAL A CG2 1 
ATOM   973   N  N   . ARG A 1 144  ? -62.149  36.856  10.662  1.00 121.99 ? 144  ARG A N   1 
ATOM   974   C  CA  . ARG A 1 144  ? -63.560  37.006  10.340  1.00 123.17 ? 144  ARG A CA  1 
ATOM   975   C  C   . ARG A 1 144  ? -63.943  38.487  10.371  1.00 121.32 ? 144  ARG A C   1 
ATOM   976   O  O   . ARG A 1 144  ? -63.117  39.339  10.715  1.00 117.35 ? 144  ARG A O   1 
ATOM   977   C  CB  . ARG A 1 144  ? -64.453  36.165  11.264  1.00 125.82 ? 144  ARG A CB  1 
ATOM   978   C  CG  . ARG A 1 144  ? -64.127  36.269  12.740  1.00 126.17 ? 144  ARG A CG  1 
ATOM   979   C  CD  . ARG A 1 144  ? -65.301  35.845  13.620  1.00 128.52 ? 144  ARG A CD  1 
ATOM   980   N  NE  . ARG A 1 144  ? -64.830  35.608  14.973  1.00 128.28 ? 144  ARG A NE  1 
ATOM   981   C  CZ  . ARG A 1 144  ? -64.225  34.489  15.350  1.00 130.26 ? 144  ARG A CZ  1 
ATOM   982   N  NH1 . ARG A 1 144  ? -64.044  33.505  14.470  1.00 131.72 ? 144  ARG A NH1 1 
ATOM   983   N  NH2 . ARG A 1 144  ? -63.806  34.357  16.605  1.00 129.92 ? 144  ARG A NH2 1 
ATOM   984   N  N   . VAL A 1 145  ? -65.182  38.786  9.987   1.00 123.94 ? 145  VAL A N   1 
ATOM   985   C  CA  . VAL A 1 145  ? -65.650  40.156  9.895   1.00 116.95 ? 145  VAL A CA  1 
ATOM   986   C  C   . VAL A 1 145  ? -67.008  40.223  10.536  1.00 121.98 ? 145  VAL A C   1 
ATOM   987   O  O   . VAL A 1 145  ? -67.892  39.455  10.172  1.00 119.16 ? 145  VAL A O   1 
ATOM   988   C  CB  . VAL A 1 145  ? -65.843  40.601  8.446   1.00 119.01 ? 145  VAL A CB  1 
ATOM   989   C  CG1 . VAL A 1 145  ? -66.692  41.827  8.420   1.00 119.35 ? 145  VAL A CG1 1 
ATOM   990   C  CG2 . VAL A 1 145  ? -64.521  40.894  7.788   1.00 118.51 ? 145  VAL A CG2 1 
ATOM   991   N  N   . TYR A 1 146  ? -67.156  41.117  11.516  1.00 122.13 ? 146  TYR A N   1 
ATOM   992   C  CA  . TYR A 1 146  ? -68.460  41.480  12.057  1.00 122.96 ? 146  TYR A CA  1 
ATOM   993   C  C   . TYR A 1 146  ? -68.878  42.718  11.315  1.00 126.53 ? 146  TYR A C   1 
ATOM   994   O  O   . TYR A 1 146  ? -68.148  43.704  11.315  1.00 126.87 ? 146  TYR A O   1 
ATOM   995   C  CB  . TYR A 1 146  ? -68.382  41.765  13.550  1.00 115.10 ? 146  TYR A CB  1 
ATOM   996   C  CG  . TYR A 1 146  ? -67.676  40.673  14.306  1.00 123.13 ? 146  TYR A CG  1 
ATOM   997   C  CD1 . TYR A 1 146  ? -68.174  39.380  14.337  1.00 126.72 ? 146  TYR A CD1 1 
ATOM   998   C  CD2 . TYR A 1 146  ? -66.493  40.926  14.979  1.00 123.44 ? 146  TYR A CD2 1 
ATOM   999   C  CE1 . TYR A 1 146  ? -67.503  38.369  15.032  1.00 126.27 ? 146  TYR A CE1 1 
ATOM   1000  C  CE2 . TYR A 1 146  ? -65.822  39.927  15.682  1.00 122.05 ? 146  TYR A CE2 1 
ATOM   1001  C  CZ  . TYR A 1 146  ? -66.326  38.658  15.704  1.00 122.96 ? 146  TYR A CZ  1 
ATOM   1002  O  OH  . TYR A 1 146  ? -65.650  37.684  16.396  1.00 120.55 ? 146  TYR A OH  1 
ATOM   1003  N  N   . SER A 1 147  ? -70.037  42.656  10.662  1.00 132.26 ? 147  SER A N   1 
ATOM   1004  C  CA  . SER A 1 147  ? -70.517  43.778  9.860   1.00 135.62 ? 147  SER A CA  1 
ATOM   1005  C  C   . SER A 1 147  ? -71.953  44.151  10.221  1.00 137.91 ? 147  SER A C   1 
ATOM   1006  O  O   . SER A 1 147  ? -72.825  43.291  10.332  1.00 139.71 ? 147  SER A O   1 
ATOM   1007  C  CB  . SER A 1 147  ? -70.393  43.490  8.349   1.00 139.27 ? 147  SER A CB  1 
ATOM   1008  O  OG  . SER A 1 147  ? -71.514  42.778  7.830   1.00 142.80 ? 147  SER A OG  1 
ATOM   1009  N  N   . LEU A 1 148  ? -72.181  45.445  10.375  1.00 138.40 ? 148  LEU A N   1 
ATOM   1010  C  CA  . LEU A 1 148  ? -73.486  45.964  10.736  1.00 139.01 ? 148  LEU A CA  1 
ATOM   1011  C  C   . LEU A 1 148  ? -73.880  47.083  9.790   1.00 145.80 ? 148  LEU A C   1 
ATOM   1012  O  O   . LEU A 1 148  ? -73.031  47.694  9.158   1.00 149.23 ? 148  LEU A O   1 
ATOM   1013  C  CB  . LEU A 1 148  ? -73.456  46.551  12.167  1.00 135.47 ? 148  LEU A CB  1 
ATOM   1014  C  CG  . LEU A 1 148  ? -73.624  45.552  13.310  1.00 133.98 ? 148  LEU A CG  1 
ATOM   1015  C  CD1 . LEU A 1 148  ? -73.183  44.150  12.894  1.00 133.73 ? 148  LEU A CD1 1 
ATOM   1016  C  CD2 . LEU A 1 148  ? -72.843  45.995  14.539  1.00 132.53 ? 148  LEU A CD2 1 
ATOM   1017  N  N   . ASN A 1 149  ? -75.170  47.332  9.731   1.00 144.49 ? 149  ASN A N   1 
ATOM   1018  C  CA  . ASN A 1 149  ? -75.675  48.408  8.902   1.00 144.27 ? 149  ASN A CA  1 
ATOM   1019  C  C   . ASN A 1 149  ? -75.878  49.625  9.785   1.00 141.33 ? 149  ASN A C   1 
ATOM   1020  O  O   . ASN A 1 149  ? -75.485  49.646  10.941  1.00 138.19 ? 149  ASN A O   1 
ATOM   1021  C  CB  . ASN A 1 149  ? -76.940  47.992  8.166   1.00 150.04 ? 149  ASN A CB  1 
ATOM   1022  C  CG  . ASN A 1 149  ? -78.035  47.532  9.097   1.00 153.95 ? 149  ASN A CG  1 
ATOM   1023  O  OD1 . ASN A 1 149  ? -77.776  46.979  10.152  1.00 153.00 ? 149  ASN A OD1 1 
ATOM   1024  N  ND2 . ASN A 1 149  ? -79.273  47.765  8.706   1.00 157.84 ? 149  ASN A ND2 1 
ATOM   1025  N  N   . ASP A 1 150  ? -76.513  50.638  9.200   1.00 139.04 ? 150  ASP A N   1 
ATOM   1026  C  CA  . ASP A 1 150  ? -76.847  51.904  9.865   1.00 141.00 ? 150  ASP A CA  1 
ATOM   1027  C  C   . ASP A 1 150  ? -77.656  51.710  11.126  1.00 137.79 ? 150  ASP A C   1 
ATOM   1028  O  O   . ASP A 1 150  ? -77.693  52.560  12.019  1.00 136.53 ? 150  ASP A O   1 
ATOM   1029  C  CB  . ASP A 1 150  ? -77.665  52.780  8.897   1.00 144.60 ? 150  ASP A CB  1 
ATOM   1030  C  CG  . ASP A 1 150  ? -78.917  52.075  8.345   1.00 161.31 ? 150  ASP A CG  1 
ATOM   1031  O  OD1 . ASP A 1 150  ? -80.045  52.542  8.625   1.00 161.40 ? 150  ASP A OD1 1 
ATOM   1032  O  OD2 . ASP A 1 150  ? -78.764  51.060  7.651   1.00 163.12 ? 150  ASP A OD2 1 
ATOM   1033  N  N   . ASP A 1 151  ? -78.306  50.559  11.175  1.00 142.17 ? 151  ASP A N   1 
ATOM   1034  C  CA  . ASP A 1 151  ? -79.179  50.199  12.269  1.00 145.87 ? 151  ASP A CA  1 
ATOM   1035  C  C   . ASP A 1 151  ? -78.572  49.166  13.191  1.00 143.85 ? 151  ASP A C   1 
ATOM   1036  O  O   . ASP A 1 151  ? -79.290  48.490  13.940  1.00 145.59 ? 151  ASP A O   1 
ATOM   1037  C  CB  . ASP A 1 151  ? -80.502  49.666  11.712  1.00 151.91 ? 151  ASP A CB  1 
ATOM   1038  C  CG  . ASP A 1 151  ? -81.725  50.148  12.493  1.00 155.08 ? 151  ASP A CG  1 
ATOM   1039  O  OD1 . ASP A 1 151  ? -82.845  49.696  12.194  1.00 158.04 ? 151  ASP A OD1 1 
ATOM   1040  O  OD2 . ASP A 1 151  ? -81.551  50.978  13.413  1.00 153.84 ? 151  ASP A OD2 1 
ATOM   1041  N  N   . LEU A 1 152  ? -77.254  49.034  13.155  1.00 143.73 ? 152  LEU A N   1 
ATOM   1042  C  CA  . LEU A 1 152  ? -76.541  48.102  14.032  1.00 145.19 ? 152  LEU A CA  1 
ATOM   1043  C  C   . LEU A 1 152  ? -77.211  46.734  14.156  1.00 148.92 ? 152  LEU A C   1 
ATOM   1044  O  O   . LEU A 1 152  ? -77.290  46.157  15.252  1.00 147.54 ? 152  LEU A O   1 
ATOM   1045  C  CB  . LEU A 1 152  ? -76.390  48.679  15.441  1.00 144.05 ? 152  LEU A CB  1 
ATOM   1046  C  CG  . LEU A 1 152  ? -75.595  49.988  15.573  1.00 144.01 ? 152  LEU A CG  1 
ATOM   1047  C  CD1 . LEU A 1 152  ? -74.425  50.035  14.606  1.00 143.30 ? 152  LEU A CD1 1 
ATOM   1048  C  CD2 . LEU A 1 152  ? -76.522  51.184  15.361  1.00 146.59 ? 152  LEU A CD2 1 
ATOM   1049  N  N   . LYS A 1 153  ? -77.689  46.208  13.026  1.00 153.06 ? 153  LYS A N   1 
ATOM   1050  C  CA  . LYS A 1 153  ? -78.295  44.873  12.989  1.00 154.57 ? 153  LYS A CA  1 
ATOM   1051  C  C   . LYS A 1 153  ? -77.531  44.073  11.932  1.00 156.27 ? 153  LYS A C   1 
ATOM   1052  O  O   . LYS A 1 153  ? -76.861  44.655  11.080  1.00 153.28 ? 153  LYS A O   1 
ATOM   1053  C  CB  . LYS A 1 153  ? -79.796  44.936  12.716  1.00 159.26 ? 153  LYS A CB  1 
ATOM   1054  C  CG  . LYS A 1 153  ? -80.661  45.024  13.961  1.00 159.62 ? 153  LYS A CG  1 
ATOM   1055  C  CD  . LYS A 1 153  ? -82.132  45.206  13.619  1.00 163.97 ? 153  LYS A CD  1 
ATOM   1056  C  CE  . LYS A 1 153  ? -82.996  45.292  14.881  1.00 165.27 ? 153  LYS A CE  1 
ATOM   1057  N  NZ  . LYS A 1 153  ? -82.490  46.312  15.839  1.00 163.53 ? 153  LYS A NZ  1 
ATOM   1058  N  N   . PRO A 1 154  ? -77.641  42.734  11.980  1.00 160.24 ? 154  PRO A N   1 
ATOM   1059  C  CA  . PRO A 1 154  ? -76.825  41.811  11.184  1.00 164.97 ? 154  PRO A CA  1 
ATOM   1060  C  C   . PRO A 1 154  ? -76.225  42.441  9.936   1.00 167.64 ? 154  PRO A C   1 
ATOM   1061  O  O   . PRO A 1 154  ? -75.021  42.319  9.720   1.00 168.57 ? 154  PRO A O   1 
ATOM   1062  C  CB  . PRO A 1 154  ? -77.830  40.725  10.802  1.00 166.24 ? 154  PRO A CB  1 
ATOM   1063  C  CG  . PRO A 1 154  ? -78.750  40.655  11.992  1.00 166.20 ? 154  PRO A CG  1 
ATOM   1064  C  CD  . PRO A 1 154  ? -78.685  42.003  12.717  1.00 163.37 ? 154  PRO A CD  1 
ATOM   1065  N  N   . ALA A 1 155  ? -77.054  43.094  9.128   1.00 173.03 ? 155  ALA A N   1 
ATOM   1066  C  CA  . ALA A 1 155  ? -76.579  43.820  7.949   1.00 175.36 ? 155  ALA A CA  1 
ATOM   1067  C  C   . ALA A 1 155  ? -76.143  42.917  6.783   1.00 180.77 ? 155  ALA A C   1 
ATOM   1068  O  O   . ALA A 1 155  ? -75.226  43.269  6.035   1.00 180.75 ? 155  ALA A O   1 
ATOM   1069  C  CB  . ALA A 1 155  ? -75.441  44.755  8.342   1.00 171.86 ? 155  ALA A CB  1 
ATOM   1070  N  N   . LYS A 1 156  ? -76.796  41.768  6.622   1.00 183.49 ? 156  LYS A N   1 
ATOM   1071  C  CA  . LYS A 1 156  ? -76.332  40.766  5.668   1.00 184.71 ? 156  LYS A CA  1 
ATOM   1072  C  C   . LYS A 1 156  ? -75.998  41.425  4.347   1.00 182.70 ? 156  LYS A C   1 
ATOM   1073  O  O   . LYS A 1 156  ? -76.746  42.272  3.876   1.00 183.46 ? 156  LYS A O   1 
ATOM   1074  C  CB  . LYS A 1 156  ? -77.387  39.680  5.471   1.00 189.72 ? 156  LYS A CB  1 
ATOM   1075  C  CG  . LYS A 1 156  ? -77.627  38.839  6.701   1.00 190.48 ? 156  LYS A CG  1 
ATOM   1076  C  CD  . LYS A 1 156  ? -79.072  38.403  6.803   1.00 195.02 ? 156  LYS A CD  1 
ATOM   1077  C  CE  . LYS A 1 156  ? -79.491  38.287  8.264   1.00 196.04 ? 156  LYS A CE  1 
ATOM   1078  N  NZ  . LYS A 1 156  ? -80.967  38.203  8.436   1.00 200.04 ? 156  LYS A NZ  1 
ATOM   1079  N  N   . ARG A 1 157  ? -74.869  41.038  3.766   1.00 178.42 ? 157  ARG A N   1 
ATOM   1080  C  CA  . ARG A 1 157  ? -74.385  41.625  2.531   1.00 176.90 ? 157  ARG A CA  1 
ATOM   1081  C  C   . ARG A 1 157  ? -73.213  40.787  2.095   1.00 178.72 ? 157  ARG A C   1 
ATOM   1082  O  O   . ARG A 1 157  ? -72.746  39.963  2.859   1.00 178.64 ? 157  ARG A O   1 
ATOM   1083  C  CB  . ARG A 1 157  ? -73.910  43.050  2.794   1.00 169.49 ? 157  ARG A CB  1 
ATOM   1084  C  CG  . ARG A 1 157  ? -75.002  44.003  3.210   1.00 164.69 ? 157  ARG A CG  1 
ATOM   1085  C  CD  . ARG A 1 157  ? -74.472  45.313  3.703   1.00 158.42 ? 157  ARG A CD  1 
ATOM   1086  N  NE  . ARG A 1 157  ? -75.567  46.191  4.093   1.00 157.14 ? 157  ARG A NE  1 
ATOM   1087  C  CZ  . ARG A 1 157  ? -75.416  47.463  4.448   1.00 155.37 ? 157  ARG A CZ  1 
ATOM   1088  N  NH1 . ARG A 1 157  ? -74.206  48.005  4.456   1.00 152.92 ? 157  ARG A NH1 1 
ATOM   1089  N  NH2 . ARG A 1 157  ? -76.475  48.195  4.792   1.00 155.73 ? 157  ARG A NH2 1 
ATOM   1090  N  N   . GLU A 1 158  ? -72.720  40.982  0.880   1.00 182.05 ? 158  GLU A N   1 
ATOM   1091  C  CA  . GLU A 1 158  ? -71.445  40.356  0.535   1.00 183.11 ? 158  GLU A CA  1 
ATOM   1092  C  C   . GLU A 1 158  ? -70.269  41.340  0.582   1.00 178.81 ? 158  GLU A C   1 
ATOM   1093  O  O   . GLU A 1 158  ? -70.300  42.393  -0.060  1.00 180.42 ? 158  GLU A O   1 
ATOM   1094  C  CB  . GLU A 1 158  ? -71.516  39.635  -0.801  1.00 190.86 ? 158  GLU A CB  1 
ATOM   1095  C  CG  . GLU A 1 158  ? -72.348  38.374  -0.741  1.00 197.69 ? 158  GLU A CG  1 
ATOM   1096  C  CD  . GLU A 1 158  ? -72.135  37.497  -1.952  1.00 204.30 ? 158  GLU A CD  1 
ATOM   1097  O  OE1 . GLU A 1 158  ? -70.971  37.115  -2.198  1.00 204.60 ? 158  GLU A OE1 1 
ATOM   1098  O  OE2 . GLU A 1 158  ? -73.126  37.188  -2.652  1.00 208.92 ? 158  GLU A OE2 1 
ATOM   1099  N  N   . THR A 1 159  ? -69.242  40.976  1.352   1.00 171.63 ? 159  THR A N   1 
ATOM   1100  C  CA  . THR A 1 159  ? -68.123  41.859  1.671   1.00 163.20 ? 159  THR A CA  1 
ATOM   1101  C  C   . THR A 1 159  ? -66.806  41.370  1.078   1.00 153.88 ? 159  THR A C   1 
ATOM   1102  O  O   . THR A 1 159  ? -66.644  40.180  0.816   1.00 153.16 ? 159  THR A O   1 
ATOM   1103  C  CB  . THR A 1 159  ? -67.954  41.970  3.192   1.00 164.29 ? 159  THR A CB  1 
ATOM   1104  O  OG1 . THR A 1 159  ? -69.208  42.337  3.794   1.00 165.75 ? 159  THR A OG1 1 
ATOM   1105  C  CG2 . THR A 1 159  ? -66.886  43.002  3.537   1.00 163.09 ? 159  THR A CG2 1 
ATOM   1106  N  N   . VAL A 1 160  ? -65.856  42.279  0.886   1.00 146.24 ? 160  VAL A N   1 
ATOM   1107  C  CA  . VAL A 1 160  ? -64.602  41.893  0.255   1.00 141.68 ? 160  VAL A CA  1 
ATOM   1108  C  C   . VAL A 1 160  ? -63.346  42.547  0.776   1.00 139.05 ? 160  VAL A C   1 
ATOM   1109  O  O   . VAL A 1 160  ? -63.142  43.756  0.627   1.00 137.78 ? 160  VAL A O   1 
ATOM   1110  C  CB  . VAL A 1 160  ? -64.621  42.174  -1.208  1.00 142.88 ? 160  VAL A CB  1 
ATOM   1111  C  CG1 . VAL A 1 160  ? -63.315  42.819  -1.618  1.00 141.36 ? 160  VAL A CG1 1 
ATOM   1112  C  CG2 . VAL A 1 160  ? -64.810  40.894  -1.949  1.00 145.20 ? 160  VAL A CG2 1 
ATOM   1113  N  N   . LEU A 1 161  ? -62.477  41.726  1.348   1.00 139.07 ? 161  LEU A N   1 
ATOM   1114  C  CA  . LEU A 1 161  ? -61.229  42.240  1.872   1.00 136.95 ? 161  LEU A CA  1 
ATOM   1115  C  C   . LEU A 1 161  ? -60.052  41.944  0.969   1.00 137.89 ? 161  LEU A C   1 
ATOM   1116  O  O   . LEU A 1 161  ? -60.166  41.208  -0.015  1.00 140.09 ? 161  LEU A O   1 
ATOM   1117  C  CB  . LEU A 1 161  ? -60.981  41.770  3.305   1.00 134.46 ? 161  LEU A CB  1 
ATOM   1118  C  CG  . LEU A 1 161  ? -61.618  40.449  3.702   1.00 134.04 ? 161  LEU A CG  1 
ATOM   1119  C  CD1 . LEU A 1 161  ? -60.933  39.342  2.957   1.00 134.52 ? 161  LEU A CD1 1 
ATOM   1120  C  CD2 . LEU A 1 161  ? -61.511  40.258  5.207   1.00 131.14 ? 161  LEU A CD2 1 
ATOM   1121  N  N   . THR A 1 162  ? -58.916  42.520  1.339   1.00 133.68 ? 162  THR A N   1 
ATOM   1122  C  CA  . THR A 1 162  ? -57.775  42.632  0.452   1.00 132.19 ? 162  THR A CA  1 
ATOM   1123  C  C   . THR A 1 162  ? -56.524  42.958  1.273   1.00 129.89 ? 162  THR A C   1 
ATOM   1124  O  O   . THR A 1 162  ? -56.199  44.130  1.478   1.00 129.29 ? 162  THR A O   1 
ATOM   1125  C  CB  . THR A 1 162  ? -58.038  43.721  -0.644  1.00 155.77 ? 162  THR A CB  1 
ATOM   1126  O  OG1 . THR A 1 162  ? -56.824  44.408  -0.981  1.00 154.68 ? 162  THR A OG1 1 
ATOM   1127  C  CG2 . THR A 1 162  ? -59.092  44.752  -0.177  1.00 154.29 ? 162  THR A CG2 1 
ATOM   1128  N  N   . PHE A 1 163  ? -55.828  41.920  1.739   1.00 128.53 ? 163  PHE A N   1 
ATOM   1129  C  CA  . PHE A 1 163  ? -54.578  42.077  2.500   1.00 126.00 ? 163  PHE A CA  1 
ATOM   1130  C  C   . PHE A 1 163  ? -53.510  42.914  1.812   1.00 126.24 ? 163  PHE A C   1 
ATOM   1131  O  O   . PHE A 1 163  ? -53.264  42.776  0.618   1.00 128.42 ? 163  PHE A O   1 
ATOM   1132  C  CB  . PHE A 1 163  ? -53.964  40.717  2.756   1.00 125.77 ? 163  PHE A CB  1 
ATOM   1133  C  CG  . PHE A 1 163  ? -54.896  39.750  3.364   1.00 125.51 ? 163  PHE A CG  1 
ATOM   1134  C  CD1 . PHE A 1 163  ? -56.035  39.360  2.686   1.00 127.64 ? 163  PHE A CD1 1 
ATOM   1135  C  CD2 . PHE A 1 163  ? -54.626  39.216  4.616   1.00 122.72 ? 163  PHE A CD2 1 
ATOM   1136  C  CE1 . PHE A 1 163  ? -56.890  38.458  3.247   1.00 129.55 ? 163  PHE A CE1 1 
ATOM   1137  C  CE2 . PHE A 1 163  ? -55.475  38.316  5.195   1.00 123.61 ? 163  PHE A CE2 1 
ATOM   1138  C  CZ  . PHE A 1 163  ? -56.610  37.929  4.516   1.00 127.63 ? 163  PHE A CZ  1 
ATOM   1139  N  N   . ILE A 1 164  ? -52.814  43.735  2.572   1.00 124.25 ? 164  ILE A N   1 
ATOM   1140  C  CA  . ILE A 1 164  ? -51.864  44.620  1.947   1.00 127.31 ? 164  ILE A CA  1 
ATOM   1141  C  C   . ILE A 1 164  ? -50.519  44.585  2.611   1.00 128.33 ? 164  ILE A C   1 
ATOM   1142  O  O   . ILE A 1 164  ? -50.364  45.029  3.742   1.00 126.42 ? 164  ILE A O   1 
ATOM   1143  C  CB  . ILE A 1 164  ? -52.341  46.043  2.022   1.00 131.02 ? 164  ILE A CB  1 
ATOM   1144  C  CG1 . ILE A 1 164  ? -53.777  46.164  1.486   1.00 134.57 ? 164  ILE A CG1 1 
ATOM   1145  C  CG2 . ILE A 1 164  ? -51.369  46.935  1.275   1.00 132.03 ? 164  ILE A CG2 1 
ATOM   1146  C  CD1 . ILE A 1 164  ? -54.317  47.604  1.465   1.00 134.96 ? 164  ILE A CD1 1 
ATOM   1147  N  N   . ASP A 1 165  ? -49.528  44.088  1.891   1.00 132.44 ? 165  ASP A N   1 
ATOM   1148  C  CA  . ASP A 1 165  ? -48.227  43.854  2.497   1.00 135.15 ? 165  ASP A CA  1 
ATOM   1149  C  C   . ASP A 1 165  ? -47.674  45.136  3.095   1.00 128.64 ? 165  ASP A C   1 
ATOM   1150  O  O   . ASP A 1 165  ? -48.130  46.229  2.782   1.00 125.73 ? 165  ASP A O   1 
ATOM   1151  C  CB  . ASP A 1 165  ? -47.246  43.193  1.505   1.00 144.99 ? 165  ASP A CB  1 
ATOM   1152  C  CG  . ASP A 1 165  ? -46.552  44.198  0.585   1.00 154.72 ? 165  ASP A CG  1 
ATOM   1153  O  OD1 . ASP A 1 165  ? -46.886  45.413  0.625   1.00 157.86 ? 165  ASP A OD1 1 
ATOM   1154  O  OD2 . ASP A 1 165  ? -45.667  43.755  -0.190  1.00 157.89 ? 165  ASP A OD2 1 
ATOM   1155  N  N   . PRO A 1 166  ? -46.683  44.994  3.959   1.00 128.82 ? 166  PRO A N   1 
ATOM   1156  C  CA  . PRO A 1 166  ? -46.099  46.106  4.706   1.00 127.17 ? 166  PRO A CA  1 
ATOM   1157  C  C   . PRO A 1 166  ? -45.469  47.152  3.816   1.00 125.67 ? 166  PRO A C   1 
ATOM   1158  O  O   . PRO A 1 166  ? -44.784  48.029  4.321   1.00 123.47 ? 166  PRO A O   1 
ATOM   1159  C  CB  . PRO A 1 166  ? -45.007  45.436  5.532   1.00 128.62 ? 166  PRO A CB  1 
ATOM   1160  C  CG  . PRO A 1 166  ? -45.386  44.000  5.584   1.00 130.52 ? 166  PRO A CG  1 
ATOM   1161  C  CD  . PRO A 1 166  ? -46.081  43.700  4.307   1.00 130.87 ? 166  PRO A CD  1 
ATOM   1162  N  N   . GLU A 1 167  ? -45.668  47.067  2.516   1.00 127.02 ? 167  GLU A N   1 
ATOM   1163  C  CA  . GLU A 1 167  ? -45.088  48.073  1.663   1.00 129.14 ? 167  GLU A CA  1 
ATOM   1164  C  C   . GLU A 1 167  ? -46.186  48.753  0.909   1.00 130.51 ? 167  GLU A C   1 
ATOM   1165  O  O   . GLU A 1 167  ? -45.974  49.778  0.273   1.00 132.86 ? 167  GLU A O   1 
ATOM   1166  C  CB  . GLU A 1 167  ? -44.090  47.468  0.703   1.00 133.18 ? 167  GLU A CB  1 
ATOM   1167  C  CG  . GLU A 1 167  ? -42.702  47.311  1.279   1.00 135.36 ? 167  GLU A CG  1 
ATOM   1168  C  CD  . GLU A 1 167  ? -41.713  46.790  0.237   1.00 140.52 ? 167  GLU A CD  1 
ATOM   1169  O  OE1 . GLU A 1 167  ? -41.330  47.570  -0.667  1.00 142.02 ? 167  GLU A OE1 1 
ATOM   1170  O  OE2 . GLU A 1 167  ? -41.316  45.602  0.316   1.00 142.11 ? 167  GLU A OE2 1 
ATOM   1171  N  N   . GLY A 1 168  ? -47.377  48.189  0.999   1.00 131.01 ? 168  GLY A N   1 
ATOM   1172  C  CA  . GLY A 1 168  ? -48.537  48.869  0.475   1.00 132.85 ? 168  GLY A CA  1 
ATOM   1173  C  C   . GLY A 1 168  ? -48.888  48.455  -0.927  1.00 138.06 ? 168  GLY A C   1 
ATOM   1174  O  O   . GLY A 1 168  ? -49.513  49.229  -1.664  1.00 139.63 ? 168  GLY A O   1 
ATOM   1175  N  N   . SER A 1 169  ? -48.466  47.255  -1.315  1.00 139.79 ? 169  SER A N   1 
ATOM   1176  C  CA  . SER A 1 169  ? -49.065  46.643  -2.483  1.00 145.69 ? 169  SER A CA  1 
ATOM   1177  C  C   . SER A 1 169  ? -50.022  45.557  -2.034  1.00 143.76 ? 169  SER A C   1 
ATOM   1178  O  O   . SER A 1 169  ? -49.790  44.887  -1.030  1.00 141.23 ? 169  SER A O   1 
ATOM   1179  C  CB  . SER A 1 169  ? -48.032  46.085  -3.452  1.00 150.42 ? 169  SER A CB  1 
ATOM   1180  O  OG  . SER A 1 169  ? -48.650  45.819  -4.705  1.00 154.59 ? 169  SER A OG  1 
ATOM   1181  N  N   . GLU A 1 170  ? -51.116  45.409  -2.769  1.00 145.58 ? 170  GLU A N   1 
ATOM   1182  C  CA  . GLU A 1 170  ? -52.083  44.369  -2.464  1.00 146.25 ? 170  GLU A CA  1 
ATOM   1183  C  C   . GLU A 1 170  ? -51.335  43.053  -2.528  1.00 141.47 ? 170  GLU A C   1 
ATOM   1184  O  O   . GLU A 1 170  ? -50.191  43.020  -2.975  1.00 138.80 ? 170  GLU A O   1 
ATOM   1185  C  CB  . GLU A 1 170  ? -53.232  44.385  -3.479  1.00 154.94 ? 170  GLU A CB  1 
ATOM   1186  C  CG  . GLU A 1 170  ? -54.010  45.703  -3.571  1.00 160.80 ? 170  GLU A CG  1 
ATOM   1187  C  CD  . GLU A 1 170  ? -55.165  45.630  -4.562  1.00 169.39 ? 170  GLU A CD  1 
ATOM   1188  O  OE1 . GLU A 1 170  ? -54.947  45.182  -5.718  1.00 173.62 ? 170  GLU A OE1 1 
ATOM   1189  O  OE2 . GLU A 1 170  ? -56.290  46.020  -4.175  1.00 171.53 ? 170  GLU A OE2 1 
ATOM   1190  N  N   . VAL A 1 171  ? -51.960  41.971  -2.086  1.00 140.49 ? 171  VAL A N   1 
ATOM   1191  C  CA  . VAL A 1 171  ? -51.315  40.672  -2.202  1.00 140.90 ? 171  VAL A CA  1 
ATOM   1192  C  C   . VAL A 1 171  ? -52.333  39.556  -2.334  1.00 138.80 ? 171  VAL A C   1 
ATOM   1193  O  O   . VAL A 1 171  ? -51.994  38.438  -2.724  1.00 139.47 ? 171  VAL A O   1 
ATOM   1194  C  CB  . VAL A 1 171  ? -50.362  40.372  -1.018  1.00 143.53 ? 171  VAL A CB  1 
ATOM   1195  C  CG1 . VAL A 1 171  ? -49.890  38.923  -1.056  1.00 144.82 ? 171  VAL A CG1 1 
ATOM   1196  C  CG2 . VAL A 1 171  ? -49.156  41.312  -1.020  1.00 142.72 ? 171  VAL A CG2 1 
ATOM   1197  N  N   . ASP A 1 172  ? -53.586  39.857  -2.028  1.00 136.30 ? 172  ASP A N   1 
ATOM   1198  C  CA  . ASP A 1 172  ? -54.631  38.840  -2.106  1.00 138.99 ? 172  ASP A CA  1 
ATOM   1199  C  C   . ASP A 1 172  ? -55.988  39.538  -2.187  1.00 140.20 ? 172  ASP A C   1 
ATOM   1200  O  O   . ASP A 1 172  ? -56.067  40.760  -2.359  1.00 139.14 ? 172  ASP A O   1 
ATOM   1201  C  CB  . ASP A 1 172  ? -54.560  37.909  -0.877  1.00 139.61 ? 172  ASP A CB  1 
ATOM   1202  C  CG  . ASP A 1 172  ? -55.245  36.551  -1.096  1.00 144.58 ? 172  ASP A CG  1 
ATOM   1203  O  OD1 . ASP A 1 172  ? -54.761  35.543  -0.517  1.00 144.26 ? 172  ASP A OD1 1 
ATOM   1204  O  OD2 . ASP A 1 172  ? -56.263  36.490  -1.825  1.00 147.55 ? 172  ASP A OD2 1 
ATOM   1205  N  N   . MET A 1 173  ? -57.056  38.766  -2.066  1.00 141.47 ? 173  MET A N   1 
ATOM   1206  C  CA  . MET A 1 173  ? -58.382  39.322  -2.106  1.00 141.72 ? 173  MET A CA  1 
ATOM   1207  C  C   . MET A 1 173  ? -59.299  38.148  -1.932  1.00 140.50 ? 173  MET A C   1 
ATOM   1208  O  O   . MET A 1 173  ? -58.929  37.026  -2.236  1.00 142.29 ? 173  MET A O   1 
ATOM   1209  C  CB  . MET A 1 173  ? -58.618  39.990  -3.456  1.00 145.82 ? 173  MET A CB  1 
ATOM   1210  C  CG  . MET A 1 173  ? -59.562  41.174  -3.400  1.00 147.89 ? 173  MET A CG  1 
ATOM   1211  S  SD  . MET A 1 173  ? -59.463  42.343  -4.783  1.00 164.84 ? 173  MET A SD  1 
ATOM   1212  C  CE  . MET A 1 173  ? -57.686  42.440  -5.009  1.00 156.32 ? 173  MET A CE  1 
ATOM   1213  N  N   . VAL A 1 174  ? -60.487  38.400  -1.410  1.00 139.19 ? 174  VAL A N   1 
ATOM   1214  C  CA  . VAL A 1 174  ? -61.541  37.385  -1.394  1.00 142.13 ? 174  VAL A CA  1 
ATOM   1215  C  C   . VAL A 1 174  ? -62.881  37.908  -0.843  1.00 141.97 ? 174  VAL A C   1 
ATOM   1216  O  O   . VAL A 1 174  ? -62.907  38.666  0.129   1.00 142.09 ? 174  VAL A O   1 
ATOM   1217  C  CB  . VAL A 1 174  ? -61.102  36.102  -0.657  1.00 144.11 ? 174  VAL A CB  1 
ATOM   1218  C  CG1 . VAL A 1 174  ? -60.150  36.431  0.479   1.00 142.04 ? 174  VAL A CG1 1 
ATOM   1219  C  CG2 . VAL A 1 174  ? -62.320  35.333  -0.161  1.00 145.83 ? 174  VAL A CG2 1 
ATOM   1220  N  N   . GLU A 1 175  ? -63.979  37.525  -1.493  1.00 141.54 ? 175  GLU A N   1 
ATOM   1221  C  CA  . GLU A 1 175  ? -65.314  37.871  -1.043  1.00 142.11 ? 175  GLU A CA  1 
ATOM   1222  C  C   . GLU A 1 175  ? -65.927  36.676  -0.332  1.00 140.92 ? 175  GLU A C   1 
ATOM   1223  O  O   . GLU A 1 175  ? -65.348  35.599  -0.364  1.00 139.27 ? 175  GLU A O   1 
ATOM   1224  C  CB  . GLU A 1 175  ? -66.152  38.285  -2.242  1.00 148.88 ? 175  GLU A CB  1 
ATOM   1225  C  CG  . GLU A 1 175  ? -65.564  37.841  -3.584  1.00 153.87 ? 175  GLU A CG  1 
ATOM   1226  C  CD  . GLU A 1 175  ? -65.877  38.794  -4.752  1.00 156.55 ? 175  GLU A CD  1 
ATOM   1227  O  OE1 . GLU A 1 175  ? -67.065  39.117  -5.003  1.00 157.35 ? 175  GLU A OE1 1 
ATOM   1228  O  OE2 . GLU A 1 175  ? -64.910  39.213  -5.426  1.00 156.47 ? 175  GLU A OE2 1 
ATOM   1229  N  N   . GLU A 1 176  ? -67.075  36.867  0.323   1.00 144.21 ? 176  GLU A N   1 
ATOM   1230  C  CA  . GLU A 1 176  ? -67.785  35.785  1.032   1.00 146.81 ? 176  GLU A CA  1 
ATOM   1231  C  C   . GLU A 1 176  ? -69.199  36.265  1.396   1.00 152.72 ? 176  GLU A C   1 
ATOM   1232  O  O   . GLU A 1 176  ? -69.458  37.468  1.426   1.00 152.11 ? 176  GLU A O   1 
ATOM   1233  C  CB  . GLU A 1 176  ? -67.006  35.326  2.284   1.00 142.90 ? 176  GLU A CB  1 
ATOM   1234  C  CG  . GLU A 1 176  ? -67.267  33.870  2.766   1.00 160.60 ? 176  GLU A CG  1 
ATOM   1235  C  CD  . GLU A 1 176  ? -66.189  32.831  2.329   1.00 173.99 ? 176  GLU A CD  1 
ATOM   1236  O  OE1 . GLU A 1 176  ? -65.871  32.739  1.117   1.00 175.37 ? 176  GLU A OE1 1 
ATOM   1237  O  OE2 . GLU A 1 176  ? -65.671  32.085  3.204   1.00 171.97 ? 176  GLU A OE2 1 
ATOM   1238  N  N   . ILE A 1 177  ? -70.112  35.330  1.653   1.00 158.08 ? 177  ILE A N   1 
ATOM   1239  C  CA  . ILE A 1 177  ? -71.531  35.662  1.856   1.00 163.23 ? 177  ILE A CA  1 
ATOM   1240  C  C   . ILE A 1 177  ? -71.891  35.891  3.322   1.00 164.52 ? 177  ILE A C   1 
ATOM   1241  O  O   . ILE A 1 177  ? -71.317  35.253  4.204   1.00 161.23 ? 177  ILE A O   1 
ATOM   1242  C  CB  . ILE A 1 177  ? -72.459  34.570  1.251   1.00 167.43 ? 177  ILE A CB  1 
ATOM   1243  C  CG1 . ILE A 1 177  ? -72.522  33.328  2.150   1.00 166.78 ? 177  ILE A CG1 1 
ATOM   1244  C  CG2 . ILE A 1 177  ? -71.984  34.190  -0.136  1.00 169.48 ? 177  ILE A CG2 1 
ATOM   1245  C  CD1 . ILE A 1 177  ? -73.555  33.400  3.286   1.00 165.33 ? 177  ILE A CD1 1 
ATOM   1246  N  N   . ASP A 1 178  ? -72.846  36.787  3.577   1.00 168.44 ? 178  ASP A N   1 
ATOM   1247  C  CA  . ASP A 1 178  ? -73.204  37.158  4.955   1.00 170.53 ? 178  ASP A CA  1 
ATOM   1248  C  C   . ASP A 1 178  ? -74.485  36.517  5.467   1.00 175.36 ? 178  ASP A C   1 
ATOM   1249  O  O   . ASP A 1 178  ? -75.559  37.117  5.419   1.00 178.00 ? 178  ASP A O   1 
ATOM   1250  C  CB  . ASP A 1 178  ? -73.310  38.677  5.111   1.00 167.17 ? 178  ASP A CB  1 
ATOM   1251  C  CG  . ASP A 1 178  ? -73.168  39.123  6.548   1.00 160.08 ? 178  ASP A CG  1 
ATOM   1252  O  OD1 . ASP A 1 178  ? -72.987  40.340  6.773   1.00 157.62 ? 178  ASP A OD1 1 
ATOM   1253  O  OD2 . ASP A 1 178  ? -73.227  38.248  7.440   1.00 157.62 ? 178  ASP A OD2 1 
ATOM   1254  N  N   . HIS A 1 179  ? -74.356  35.310  5.996   1.00 177.49 ? 179  HIS A N   1 
ATOM   1255  C  CA  . HIS A 1 179  ? -75.515  34.569  6.453   1.00 180.80 ? 179  HIS A CA  1 
ATOM   1256  C  C   . HIS A 1 179  ? -76.063  35.118  7.764   1.00 176.94 ? 179  HIS A C   1 
ATOM   1257  O  O   . HIS A 1 179  ? -77.274  35.078  7.988   1.00 177.37 ? 179  HIS A O   1 
ATOM   1258  C  CB  . HIS A 1 179  ? -75.189  33.083  6.592   1.00 187.22 ? 179  HIS A CB  1 
ATOM   1259  C  CG  . HIS A 1 179  ? -76.348  32.184  6.294   1.00 196.75 ? 179  HIS A CG  1 
ATOM   1260  N  ND1 . HIS A 1 179  ? -76.408  31.405  5.159   1.00 201.67 ? 179  HIS A ND1 1 
ATOM   1261  C  CD2 . HIS A 1 179  ? -77.493  31.945  6.977   1.00 200.14 ? 179  HIS A CD2 1 
ATOM   1262  C  CE1 . HIS A 1 179  ? -77.537  30.719  5.159   1.00 205.87 ? 179  HIS A CE1 1 
ATOM   1263  N  NE2 . HIS A 1 179  ? -78.213  31.028  6.251   1.00 204.92 ? 179  HIS A NE2 1 
ATOM   1264  N  N   . ILE A 1 180  ? -75.194  35.638  8.629   1.00 171.78 ? 180  ILE A N   1 
ATOM   1265  C  CA  . ILE A 1 180  ? -75.690  36.151  9.913   1.00 167.97 ? 180  ILE A CA  1 
ATOM   1266  C  C   . ILE A 1 180  ? -75.113  37.492  10.396  1.00 160.78 ? 180  ILE A C   1 
ATOM   1267  O  O   . ILE A 1 180  ? -75.763  38.216  11.149  1.00 155.93 ? 180  ILE A O   1 
ATOM   1268  C  CB  . ILE A 1 180  ? -75.643  35.080  11.037  1.00 150.78 ? 180  ILE A CB  1 
ATOM   1269  C  CG1 . ILE A 1 180  ? -74.238  34.542  11.254  1.00 147.55 ? 180  ILE A CG1 1 
ATOM   1270  C  CG2 . ILE A 1 180  ? -76.525  33.905  10.686  1.00 153.98 ? 180  ILE A CG2 1 
ATOM   1271  C  CD1 . ILE A 1 180  ? -74.222  33.437  12.287  1.00 145.32 ? 180  ILE A CD1 1 
ATOM   1272  N  N   . GLY A 1 181  ? -73.916  37.831  9.944   1.00 157.40 ? 181  GLY A N   1 
ATOM   1273  C  CA  . GLY A 1 181  ? -73.303  39.085  10.328  1.00 152.78 ? 181  GLY A CA  1 
ATOM   1274  C  C   . GLY A 1 181  ? -71.880  38.799  10.741  1.00 147.21 ? 181  GLY A C   1 
ATOM   1275  O  O   . GLY A 1 181  ? -71.075  39.708  10.932  1.00 146.40 ? 181  GLY A O   1 
ATOM   1276  N  N   . ILE A 1 182  ? -71.591  37.510  10.888  1.00 144.94 ? 182  ILE A N   1 
ATOM   1277  C  CA  . ILE A 1 182  ? -70.256  37.030  11.216  1.00 142.20 ? 182  ILE A CA  1 
ATOM   1278  C  C   . ILE A 1 182  ? -69.608  36.364  10.009  1.00 141.35 ? 182  ILE A C   1 
ATOM   1279  O  O   . ILE A 1 182  ? -69.293  35.177  10.036  1.00 142.26 ? 182  ILE A O   1 
ATOM   1280  C  CB  . ILE A 1 182  ? -70.302  36.028  12.375  1.00 140.51 ? 182  ILE A CB  1 
ATOM   1281  C  CG1 . ILE A 1 182  ? -71.247  36.556  13.457  1.00 140.68 ? 182  ILE A CG1 1 
ATOM   1282  C  CG2 . ILE A 1 182  ? -68.891  35.772  12.913  1.00 138.01 ? 182  ILE A CG2 1 
ATOM   1283  C  CD1 . ILE A 1 182  ? -71.900  35.490  14.316  1.00 141.33 ? 182  ILE A CD1 1 
ATOM   1284  N  N   . ILE A 1 183  ? -69.436  37.136  8.946   1.00 141.06 ? 183  ILE A N   1 
ATOM   1285  C  CA  . ILE A 1 183  ? -68.716  36.693  7.770   1.00 139.89 ? 183  ILE A CA  1 
ATOM   1286  C  C   . ILE A 1 183  ? -67.422  35.973  8.124   1.00 137.90 ? 183  ILE A C   1 
ATOM   1287  O  O   . ILE A 1 183  ? -66.553  36.542  8.783   1.00 137.61 ? 183  ILE A O   1 
ATOM   1288  C  CB  . ILE A 1 183  ? -68.334  37.894  6.936   1.00 138.97 ? 183  ILE A CB  1 
ATOM   1289  C  CG1 . ILE A 1 183  ? -69.584  38.596  6.420   1.00 139.44 ? 183  ILE A CG1 1 
ATOM   1290  C  CG2 . ILE A 1 183  ? -67.473  37.469  5.794   1.00 140.61 ? 183  ILE A CG2 1 
ATOM   1291  C  CD1 . ILE A 1 183  ? -69.272  39.801  5.559   1.00 139.98 ? 183  ILE A CD1 1 
ATOM   1292  N  N   . SER A 1 184  ? -67.287  34.729  7.672   1.00 140.27 ? 184  SER A N   1 
ATOM   1293  C  CA  . SER A 1 184  ? -66.123  33.901  8.016   1.00 137.51 ? 184  SER A CA  1 
ATOM   1294  C  C   . SER A 1 184  ? -65.185  33.597  6.822   1.00 145.27 ? 184  SER A C   1 
ATOM   1295  O  O   . SER A 1 184  ? -65.449  32.707  5.990   1.00 147.60 ? 184  SER A O   1 
ATOM   1296  C  CB  . SER A 1 184  ? -66.598  32.597  8.672   1.00 138.75 ? 184  SER A CB  1 
ATOM   1297  O  OG  . SER A 1 184  ? -67.841  32.786  9.356   1.00 137.78 ? 184  SER A OG  1 
ATOM   1298  N  N   . PHE A 1 185  ? -64.082  34.336  6.761   1.00 141.26 ? 185  PHE A N   1 
ATOM   1299  C  CA  . PHE A 1 185  ? -63.143  34.245  5.651   1.00 141.78 ? 185  PHE A CA  1 
ATOM   1300  C  C   . PHE A 1 185  ? -62.134  33.132  5.826   1.00 139.30 ? 185  PHE A C   1 
ATOM   1301  O  O   . PHE A 1 185  ? -62.058  32.520  6.886   1.00 136.09 ? 185  PHE A O   1 
ATOM   1302  C  CB  . PHE A 1 185  ? -62.373  35.544  5.531   1.00 140.34 ? 185  PHE A CB  1 
ATOM   1303  C  CG  . PHE A 1 185  ? -63.186  36.686  5.063   1.00 140.76 ? 185  PHE A CG  1 
ATOM   1304  C  CD1 . PHE A 1 185  ? -63.267  36.984  3.721   1.00 142.87 ? 185  PHE A CD1 1 
ATOM   1305  C  CD2 . PHE A 1 185  ? -63.850  37.481  5.969   1.00 140.34 ? 185  PHE A CD2 1 
ATOM   1306  C  CE1 . PHE A 1 185  ? -64.001  38.058  3.295   1.00 144.45 ? 185  PHE A CE1 1 
ATOM   1307  C  CE2 . PHE A 1 185  ? -64.586  38.558  5.551   1.00 141.84 ? 185  PHE A CE2 1 
ATOM   1308  C  CZ  . PHE A 1 185  ? -64.666  38.848  4.212   1.00 144.61 ? 185  PHE A CZ  1 
ATOM   1309  N  N   . PRO A 1 186  ? -61.314  32.900  4.794   1.00 142.37 ? 186  PRO A N   1 
ATOM   1310  C  CA  . PRO A 1 186  ? -60.402  31.771  4.831   1.00 145.44 ? 186  PRO A CA  1 
ATOM   1311  C  C   . PRO A 1 186  ? -59.055  32.235  5.331   1.00 143.82 ? 186  PRO A C   1 
ATOM   1312  O  O   . PRO A 1 186  ? -58.601  33.312  4.930   1.00 144.69 ? 186  PRO A O   1 
ATOM   1313  C  CB  . PRO A 1 186  ? -60.271  31.402  3.357   1.00 148.39 ? 186  PRO A CB  1 
ATOM   1314  C  CG  . PRO A 1 186  ? -60.742  32.651  2.584   1.00 149.58 ? 186  PRO A CG  1 
ATOM   1315  C  CD  . PRO A 1 186  ? -61.070  33.707  3.593   1.00 145.56 ? 186  PRO A CD  1 
ATOM   1316  N  N   . ASP A 1 187  ? -58.430  31.412  6.174   1.00 144.22 ? 187  ASP A N   1 
ATOM   1317  C  CA  . ASP A 1 187  ? -57.108  31.682  6.750   1.00 141.59 ? 187  ASP A CA  1 
ATOM   1318  C  C   . ASP A 1 187  ? -56.081  32.113  5.673   1.00 139.63 ? 187  ASP A C   1 
ATOM   1319  O  O   . ASP A 1 187  ? -56.113  31.639  4.527   1.00 138.57 ? 187  ASP A O   1 
ATOM   1320  C  CB  . ASP A 1 187  ? -56.595  30.461  7.549   1.00 143.88 ? 187  ASP A CB  1 
ATOM   1321  C  CG  . ASP A 1 187  ? -57.434  30.167  8.803   1.00 146.48 ? 187  ASP A CG  1 
ATOM   1322  O  OD1 . ASP A 1 187  ? -58.619  30.578  8.858   1.00 147.39 ? 187  ASP A OD1 1 
ATOM   1323  O  OD2 . ASP A 1 187  ? -56.907  29.511  9.731   1.00 146.87 ? 187  ASP A OD2 1 
ATOM   1324  N  N   . PHE A 1 188  ? -55.188  33.023  6.065   1.00 134.80 ? 188  PHE A N   1 
ATOM   1325  C  CA  . PHE A 1 188  ? -54.209  33.633  5.179   1.00 131.00 ? 188  PHE A CA  1 
ATOM   1326  C  C   . PHE A 1 188  ? -52.847  33.256  5.682   1.00 130.26 ? 188  PHE A C   1 
ATOM   1327  O  O   . PHE A 1 188  ? -52.382  33.784  6.668   1.00 128.73 ? 188  PHE A O   1 
ATOM   1328  C  CB  . PHE A 1 188  ? -54.377  35.136  5.236   1.00 127.70 ? 188  PHE A CB  1 
ATOM   1329  C  CG  . PHE A 1 188  ? -53.304  35.915  4.537   1.00 124.55 ? 188  PHE A CG  1 
ATOM   1330  C  CD1 . PHE A 1 188  ? -52.237  36.439  5.231   1.00 123.73 ? 188  PHE A CD1 1 
ATOM   1331  C  CD2 . PHE A 1 188  ? -53.399  36.191  3.203   1.00 127.18 ? 188  PHE A CD2 1 
ATOM   1332  C  CE1 . PHE A 1 188  ? -51.262  37.198  4.598   1.00 122.98 ? 188  PHE A CE1 1 
ATOM   1333  C  CE2 . PHE A 1 188  ? -52.425  36.943  2.564   1.00 127.06 ? 188  PHE A CE2 1 
ATOM   1334  C  CZ  . PHE A 1 188  ? -51.357  37.448  3.270   1.00 124.97 ? 188  PHE A CZ  1 
ATOM   1335  N  N   . LYS A 1 189  ? -52.219  32.313  5.000   1.00 133.25 ? 189  LYS A N   1 
ATOM   1336  C  CA  . LYS A 1 189  ? -50.954  31.724  5.427   1.00 130.22 ? 189  LYS A CA  1 
ATOM   1337  C  C   . LYS A 1 189  ? -49.794  32.693  5.218   1.00 129.48 ? 189  LYS A C   1 
ATOM   1338  O  O   . LYS A 1 189  ? -49.513  33.119  4.100   1.00 129.54 ? 189  LYS A O   1 
ATOM   1339  C  CB  . LYS A 1 189  ? -50.726  30.415  4.655   1.00 134.75 ? 189  LYS A CB  1 
ATOM   1340  C  CG  . LYS A 1 189  ? -49.291  30.062  4.377   1.00 137.24 ? 189  LYS A CG  1 
ATOM   1341  C  CD  . LYS A 1 189  ? -48.692  29.249  5.511   1.00 139.36 ? 189  LYS A CD  1 
ATOM   1342  C  CE  . LYS A 1 189  ? -47.478  28.469  5.019   1.00 141.51 ? 189  LYS A CE  1 
ATOM   1343  N  NZ  . LYS A 1 189  ? -46.729  29.242  3.974   1.00 141.70 ? 189  LYS A NZ  1 
ATOM   1344  N  N   . ILE A 1 190  ? -49.127  33.051  6.301   1.00 123.04 ? 190  ILE A N   1 
ATOM   1345  C  CA  . ILE A 1 190  ? -47.959  33.900  6.207   1.00 123.10 ? 190  ILE A CA  1 
ATOM   1346  C  C   . ILE A 1 190  ? -46.857  33.164  5.422   1.00 127.70 ? 190  ILE A C   1 
ATOM   1347  O  O   . ILE A 1 190  ? -46.551  32.008  5.720   1.00 134.73 ? 190  ILE A O   1 
ATOM   1348  C  CB  . ILE A 1 190  ? -47.483  34.244  7.625   1.00 118.35 ? 190  ILE A CB  1 
ATOM   1349  C  CG1 . ILE A 1 190  ? -48.705  34.520  8.513   1.00 110.02 ? 190  ILE A CG1 1 
ATOM   1350  C  CG2 . ILE A 1 190  ? -46.488  35.407  7.616   1.00 110.62 ? 190  ILE A CG2 1 
ATOM   1351  C  CD1 . ILE A 1 190  ? -49.132  35.992  8.615   1.00 108.96 ? 190  ILE A CD1 1 
ATOM   1352  N  N   . PRO A 1 191  ? -46.274  33.820  4.401   1.00 128.75 ? 191  PRO A N   1 
ATOM   1353  C  CA  . PRO A 1 191  ? -45.196  33.290  3.555   1.00 128.33 ? 191  PRO A CA  1 
ATOM   1354  C  C   . PRO A 1 191  ? -44.055  32.598  4.317   1.00 132.58 ? 191  PRO A C   1 
ATOM   1355  O  O   . PRO A 1 191  ? -43.777  32.925  5.474   1.00 129.40 ? 191  PRO A O   1 
ATOM   1356  C  CB  . PRO A 1 191  ? -44.657  34.546  2.878   1.00 126.80 ? 191  PRO A CB  1 
ATOM   1357  C  CG  . PRO A 1 191  ? -45.842  35.375  2.710   1.00 126.02 ? 191  PRO A CG  1 
ATOM   1358  C  CD  . PRO A 1 191  ? -46.723  35.133  3.918   1.00 125.63 ? 191  PRO A CD  1 
ATOM   1359  N  N   . SER A 1 192  ? -43.398  31.652  3.644   1.00 134.40 ? 192  SER A N   1 
ATOM   1360  C  CA  . SER A 1 192  ? -42.274  30.911  4.211   1.00 133.12 ? 192  SER A CA  1 
ATOM   1361  C  C   . SER A 1 192  ? -41.242  31.899  4.719   1.00 125.39 ? 192  SER A C   1 
ATOM   1362  O  O   . SER A 1 192  ? -40.648  31.725  5.771   1.00 121.17 ? 192  SER A O   1 
ATOM   1363  C  CB  . SER A 1 192  ? -41.647  30.006  3.139   1.00 136.83 ? 192  SER A CB  1 
ATOM   1364  O  OG  . SER A 1 192  ? -42.622  29.389  2.316   1.00 139.84 ? 192  SER A OG  1 
ATOM   1365  N  N   . ASN A 1 193  ? -41.052  32.945  3.933   1.00 125.98 ? 193  ASN A N   1 
ATOM   1366  C  CA  . ASN A 1 193  ? -40.136  34.018  4.251   1.00 126.96 ? 193  ASN A CA  1 
ATOM   1367  C  C   . ASN A 1 193  ? -40.762  35.332  3.789   1.00 127.48 ? 193  ASN A C   1 
ATOM   1368  O  O   . ASN A 1 193  ? -40.468  35.810  2.684   1.00 129.77 ? 193  ASN A O   1 
ATOM   1369  C  CB  . ASN A 1 193  ? -38.815  33.776  3.530   1.00 128.84 ? 193  ASN A CB  1 
ATOM   1370  C  CG  . ASN A 1 193  ? -38.035  35.042  3.307   1.00 129.47 ? 193  ASN A CG  1 
ATOM   1371  O  OD1 . ASN A 1 193  ? -38.294  36.058  3.948   1.00 128.03 ? 193  ASN A OD1 1 
ATOM   1372  N  ND2 . ASN A 1 193  ? -37.070  34.991  2.391   1.00 130.99 ? 193  ASN A ND2 1 
ATOM   1373  N  N   . PRO A 1 194  ? -41.638  35.910  4.634   1.00 127.90 ? 194  PRO A N   1 
ATOM   1374  C  CA  . PRO A 1 194  ? -42.514  37.018  4.273   1.00 125.86 ? 194  PRO A CA  1 
ATOM   1375  C  C   . PRO A 1 194  ? -41.808  38.348  4.222   1.00 122.67 ? 194  PRO A C   1 
ATOM   1376  O  O   . PRO A 1 194  ? -40.616  38.450  4.501   1.00 120.60 ? 194  PRO A O   1 
ATOM   1377  C  CB  . PRO A 1 194  ? -43.532  37.046  5.414   1.00 126.62 ? 194  PRO A CB  1 
ATOM   1378  C  CG  . PRO A 1 194  ? -43.337  35.792  6.167   1.00 128.50 ? 194  PRO A CG  1 
ATOM   1379  C  CD  . PRO A 1 194  ? -41.904  35.454  6.004   1.00 128.02 ? 194  PRO A CD  1 
ATOM   1380  N  N   . ARG A 1 195  ? -42.585  39.355  3.837   1.00 126.50 ? 195  ARG A N   1 
ATOM   1381  C  CA  . ARG A 1 195  ? -42.189  40.751  3.831   1.00 128.04 ? 195  ARG A CA  1 
ATOM   1382  C  C   . ARG A 1 195  ? -42.516  41.249  5.235   1.00 127.03 ? 195  ARG A C   1 
ATOM   1383  O  O   . ARG A 1 195  ? -43.683  41.464  5.556   1.00 127.24 ? 195  ARG A O   1 
ATOM   1384  C  CB  . ARG A 1 195  ? -43.048  41.498  2.810   1.00 132.14 ? 195  ARG A CB  1 
ATOM   1385  C  CG  . ARG A 1 195  ? -42.302  42.465  1.899   1.00 135.49 ? 195  ARG A CG  1 
ATOM   1386  C  CD  . ARG A 1 195  ? -42.042  41.842  0.546   1.00 141.37 ? 195  ARG A CD  1 
ATOM   1387  N  NE  . ARG A 1 195  ? -42.304  42.778  -0.542  1.00 146.09 ? 195  ARG A NE  1 
ATOM   1388  C  CZ  . ARG A 1 195  ? -41.370  43.340  -1.300  1.00 148.22 ? 195  ARG A CZ  1 
ATOM   1389  N  NH1 . ARG A 1 195  ? -40.093  43.062  -1.101  1.00 146.85 ? 195  ARG A NH1 1 
ATOM   1390  N  NH2 . ARG A 1 195  ? -41.724  44.184  -2.259  1.00 150.90 ? 195  ARG A NH2 1 
ATOM   1391  N  N   . TYR A 1 196  ? -41.499  41.419  6.074   1.00 124.73 ? 196  TYR A N   1 
ATOM   1392  C  CA  . TYR A 1 196  ? -41.723  41.547  7.502   1.00 119.97 ? 196  TYR A CA  1 
ATOM   1393  C  C   . TYR A 1 196  ? -42.151  42.936  7.867   1.00 115.98 ? 196  TYR A C   1 
ATOM   1394  O  O   . TYR A 1 196  ? -41.511  43.903  7.463   1.00 114.60 ? 196  TYR A O   1 
ATOM   1395  C  CB  . TYR A 1 196  ? -40.439  41.219  8.245   1.00 122.19 ? 196  TYR A CB  1 
ATOM   1396  C  CG  . TYR A 1 196  ? -40.087  39.752  8.280   1.00 123.72 ? 196  TYR A CG  1 
ATOM   1397  C  CD1 . TYR A 1 196  ? -40.902  38.846  8.937   1.00 122.79 ? 196  TYR A CD1 1 
ATOM   1398  C  CD2 . TYR A 1 196  ? -38.926  39.277  7.669   1.00 124.19 ? 196  TYR A CD2 1 
ATOM   1399  C  CE1 . TYR A 1 196  ? -40.584  37.506  8.979   1.00 123.87 ? 196  TYR A CE1 1 
ATOM   1400  C  CE2 . TYR A 1 196  ? -38.592  37.930  7.704   1.00 124.36 ? 196  TYR A CE2 1 
ATOM   1401  C  CZ  . TYR A 1 196  ? -39.427  37.054  8.364   1.00 123.86 ? 196  TYR A CZ  1 
ATOM   1402  O  OH  . TYR A 1 196  ? -39.106  35.725  8.415   1.00 123.65 ? 196  TYR A OH  1 
ATOM   1403  N  N   . GLY A 1 197  ? -43.223  43.040  8.643   1.00 111.87 ? 197  GLY A N   1 
ATOM   1404  C  CA  . GLY A 1 197  ? -43.669  44.345  9.089   1.00 112.51 ? 197  GLY A CA  1 
ATOM   1405  C  C   . GLY A 1 197  ? -45.170  44.571  9.214   1.00 112.09 ? 197  GLY A C   1 
ATOM   1406  O  O   . GLY A 1 197  ? -45.942  43.656  9.485   1.00 113.80 ? 197  GLY A O   1 
ATOM   1407  N  N   . MET A 1 198  ? -45.589  45.812  9.014   1.00 111.89 ? 198  MET A N   1 
ATOM   1408  C  CA  . MET A 1 198  ? -46.965  46.190  9.296   1.00 112.26 ? 198  MET A CA  1 
ATOM   1409  C  C   . MET A 1 198  ? -47.960  45.799  8.186   1.00 109.50 ? 198  MET A C   1 
ATOM   1410  O  O   . MET A 1 198  ? -48.062  46.468  7.149   1.00 105.97 ? 198  MET A O   1 
ATOM   1411  C  CB  . MET A 1 198  ? -47.003  47.700  9.612   1.00 115.94 ? 198  MET A CB  1 
ATOM   1412  C  CG  . MET A 1 198  ? -48.313  48.283  10.208  1.00 140.49 ? 198  MET A CG  1 
ATOM   1413  S  SD  . MET A 1 198  ? -49.182  47.218  11.368  1.00 153.17 ? 198  MET A SD  1 
ATOM   1414  C  CE  . MET A 1 198  ? -47.815  46.446  12.235  1.00 98.06  ? 198  MET A CE  1 
ATOM   1415  N  N   . TRP A 1 199  ? -48.704  44.719  8.402   1.00 109.68 ? 199  TRP A N   1 
ATOM   1416  C  CA  . TRP A 1 199  ? -49.736  44.331  7.433   1.00 111.84 ? 199  TRP A CA  1 
ATOM   1417  C  C   . TRP A 1 199  ? -50.999  45.167  7.588   1.00 113.06 ? 199  TRP A C   1 
ATOM   1418  O  O   . TRP A 1 199  ? -51.189  45.800  8.611   1.00 114.46 ? 199  TRP A O   1 
ATOM   1419  C  CB  . TRP A 1 199  ? -50.024  42.827  7.523   1.00 114.68 ? 199  TRP A CB  1 
ATOM   1420  C  CG  . TRP A 1 199  ? -48.900  42.072  6.927   1.00 118.79 ? 199  TRP A CG  1 
ATOM   1421  C  CD1 . TRP A 1 199  ? -47.617  42.076  7.367   1.00 119.70 ? 199  TRP A CD1 1 
ATOM   1422  C  CD2 . TRP A 1 199  ? -48.916  41.254  5.735   1.00 121.46 ? 199  TRP A CD2 1 
ATOM   1423  N  NE1 . TRP A 1 199  ? -46.830  41.300  6.541   1.00 122.77 ? 199  TRP A NE1 1 
ATOM   1424  C  CE2 . TRP A 1 199  ? -47.603  40.785  5.535   1.00 122.77 ? 199  TRP A CE2 1 
ATOM   1425  C  CE3 . TRP A 1 199  ? -49.912  40.859  4.837   1.00 122.97 ? 199  TRP A CE3 1 
ATOM   1426  C  CZ2 . TRP A 1 199  ? -47.263  39.943  4.480   1.00 122.25 ? 199  TRP A CZ2 1 
ATOM   1427  C  CZ3 . TRP A 1 199  ? -49.571  40.028  3.790   1.00 123.45 ? 199  TRP A CZ3 1 
ATOM   1428  C  CH2 . TRP A 1 199  ? -48.262  39.580  3.623   1.00 123.81 ? 199  TRP A CH2 1 
ATOM   1429  N  N   . THR A 1 200  ? -51.861  45.189  6.586   1.00 111.67 ? 200  THR A N   1 
ATOM   1430  C  CA  . THR A 1 200  ? -53.092  45.948  6.699   1.00 107.79 ? 200  THR A CA  1 
ATOM   1431  C  C   . THR A 1 200  ? -54.157  45.126  6.035   1.00 110.26 ? 200  THR A C   1 
ATOM   1432  O  O   . THR A 1 200  ? -53.967  44.682  4.916   1.00 113.49 ? 200  THR A O   1 
ATOM   1433  C  CB  . THR A 1 200  ? -53.004  47.269  5.915   1.00 108.23 ? 200  THR A CB  1 
ATOM   1434  O  OG1 . THR A 1 200  ? -51.765  47.926  6.193   1.00 106.67 ? 200  THR A OG1 1 
ATOM   1435  C  CG2 . THR A 1 200  ? -54.148  48.175  6.264   1.00 108.31 ? 200  THR A CG2 1 
ATOM   1436  N  N   . ILE A 1 201  ? -55.272  44.882  6.700   1.00 109.94 ? 201  ILE A N   1 
ATOM   1437  C  CA  . ILE A 1 201  ? -56.390  44.266  5.997   1.00 112.55 ? 201  ILE A CA  1 
ATOM   1438  C  C   . ILE A 1 201  ? -57.518  45.283  5.821   1.00 115.79 ? 201  ILE A C   1 
ATOM   1439  O  O   . ILE A 1 201  ? -58.133  45.686  6.804   1.00 120.67 ? 201  ILE A O   1 
ATOM   1440  C  CB  . ILE A 1 201  ? -56.974  43.048  6.748   1.00 112.10 ? 201  ILE A CB  1 
ATOM   1441  C  CG1 . ILE A 1 201  ? -55.985  41.900  6.874   1.00 111.72 ? 201  ILE A CG1 1 
ATOM   1442  C  CG2 . ILE A 1 201  ? -58.144  42.499  5.993   1.00 116.87 ? 201  ILE A CG2 1 
ATOM   1443  C  CD1 . ILE A 1 201  ? -56.700  40.568  7.094   1.00 112.72 ? 201  ILE A CD1 1 
ATOM   1444  N  N   . LYS A 1 202  ? -57.809  45.704  4.594   1.00 122.59 ? 202  LYS A N   1 
ATOM   1445  C  CA  . LYS A 1 202  ? -58.983  46.560  4.375   1.00 122.53 ? 202  LYS A CA  1 
ATOM   1446  C  C   . LYS A 1 202  ? -60.217  45.738  3.975   1.00 123.38 ? 202  LYS A C   1 
ATOM   1447  O  O   . LYS A 1 202  ? -60.087  44.610  3.514   1.00 123.61 ? 202  LYS A O   1 
ATOM   1448  C  CB  . LYS A 1 202  ? -58.709  47.628  3.313   1.00 129.21 ? 202  LYS A CB  1 
ATOM   1449  C  CG  . LYS A 1 202  ? -57.679  48.698  3.684   1.00 131.79 ? 202  LYS A CG  1 
ATOM   1450  C  CD  . LYS A 1 202  ? -57.492  49.693  2.530   1.00 137.47 ? 202  LYS A CD  1 
ATOM   1451  C  CE  . LYS A 1 202  ? -56.118  50.353  2.563   1.00 138.91 ? 202  LYS A CE  1 
ATOM   1452  N  NZ  . LYS A 1 202  ? -55.524  50.463  1.195   1.00 141.94 ? 202  LYS A NZ  1 
ATOM   1453  N  N   . ALA A 1 203  ? -61.412  46.296  4.136   1.00 121.57 ? 203  ALA A N   1 
ATOM   1454  C  CA  . ALA A 1 203  ? -62.616  45.581  3.713   1.00 124.61 ? 203  ALA A CA  1 
ATOM   1455  C  C   . ALA A 1 203  ? -63.716  46.532  3.248   1.00 128.49 ? 203  ALA A C   1 
ATOM   1456  O  O   . ALA A 1 203  ? -64.005  47.522  3.924   1.00 126.80 ? 203  ALA A O   1 
ATOM   1457  C  CB  . ALA A 1 203  ? -63.118  44.668  4.812   1.00 120.25 ? 203  ALA A CB  1 
ATOM   1458  N  N   . LYS A 1 204  ? -64.329  46.213  2.098   1.00 134.18 ? 204  LYS A N   1 
ATOM   1459  C  CA  . LYS A 1 204  ? -65.373  47.047  1.472   1.00 139.18 ? 204  LYS A CA  1 
ATOM   1460  C  C   . LYS A 1 204  ? -66.568  46.223  1.053   1.00 139.24 ? 204  LYS A C   1 
ATOM   1461  O  O   . LYS A 1 204  ? -66.462  45.013  0.855   1.00 137.65 ? 204  LYS A O   1 
ATOM   1462  C  CB  . LYS A 1 204  ? -64.838  47.772  0.249   1.00 144.31 ? 204  LYS A CB  1 
ATOM   1463  C  CG  . LYS A 1 204  ? -64.043  46.858  -0.646  1.00 151.30 ? 204  LYS A CG  1 
ATOM   1464  C  CD  . LYS A 1 204  ? -63.260  47.643  -1.672  1.00 156.46 ? 204  LYS A CD  1 
ATOM   1465  C  CE  . LYS A 1 204  ? -62.039  46.870  -2.137  1.00 159.23 ? 204  LYS A CE  1 
ATOM   1466  N  NZ  . LYS A 1 204  ? -61.534  47.464  -3.408  1.00 162.72 ? 204  LYS A NZ  1 
ATOM   1467  N  N   . TYR A 1 205  ? -67.716  46.874  0.933   1.00 143.53 ? 205  TYR A N   1 
ATOM   1468  C  CA  . TYR A 1 205  ? -68.918  46.126  0.632   1.00 151.72 ? 205  TYR A CA  1 
ATOM   1469  C  C   . TYR A 1 205  ? -68.893  45.817  -0.850  1.00 161.53 ? 205  TYR A C   1 
ATOM   1470  O  O   . TYR A 1 205  ? -68.693  46.726  -1.648  1.00 165.82 ? 205  TYR A O   1 
ATOM   1471  C  CB  . TYR A 1 205  ? -70.171  46.900  1.055   1.00 151.96 ? 205  TYR A CB  1 
ATOM   1472  C  CG  . TYR A 1 205  ? -70.600  46.552  2.465   1.00 151.01 ? 205  TYR A CG  1 
ATOM   1473  C  CD1 . TYR A 1 205  ? -70.564  47.495  3.489   1.00 149.17 ? 205  TYR A CD1 1 
ATOM   1474  C  CD2 . TYR A 1 205  ? -71.000  45.255  2.785   1.00 152.38 ? 205  TYR A CD2 1 
ATOM   1475  C  CE1 . TYR A 1 205  ? -70.936  47.157  4.789   1.00 147.66 ? 205  TYR A CE1 1 
ATOM   1476  C  CE2 . TYR A 1 205  ? -71.372  44.911  4.079   1.00 150.66 ? 205  TYR A CE2 1 
ATOM   1477  C  CZ  . TYR A 1 205  ? -71.339  45.865  5.073   1.00 148.35 ? 205  TYR A CZ  1 
ATOM   1478  O  OH  . TYR A 1 205  ? -71.714  45.509  6.347   1.00 146.08 ? 205  TYR A OH  1 
ATOM   1479  N  N   . LYS A 1 206  ? -69.051  44.547  -1.233  1.00 166.90 ? 206  LYS A N   1 
ATOM   1480  C  CA  . LYS A 1 206  ? -68.911  44.193  -2.653  1.00 170.62 ? 206  LYS A CA  1 
ATOM   1481  C  C   . LYS A 1 206  ? -69.776  45.136  -3.456  1.00 174.08 ? 206  LYS A C   1 
ATOM   1482  O  O   . LYS A 1 206  ? -69.282  45.958  -4.228  1.00 174.11 ? 206  LYS A O   1 
ATOM   1483  C  CB  . LYS A 1 206  ? -69.308  42.740  -2.952  1.00 173.54 ? 206  LYS A CB  1 
ATOM   1484  C  CG  . LYS A 1 206  ? -69.079  42.351  -4.421  1.00 177.17 ? 206  LYS A CG  1 
ATOM   1485  C  CD  . LYS A 1 206  ? -69.257  40.859  -4.682  1.00 179.90 ? 206  LYS A CD  1 
ATOM   1486  C  CE  . LYS A 1 206  ? -70.721  40.436  -4.606  1.00 183.46 ? 206  LYS A CE  1 
ATOM   1487  N  NZ  . LYS A 1 206  ? -70.991  39.120  -5.277  1.00 186.27 ? 206  LYS A NZ  1 
ATOM   1488  N  N   . GLU A 1 207  ? -71.076  45.028  -3.225  1.00 175.92 ? 207  GLU A N   1 
ATOM   1489  C  CA  . GLU A 1 207  ? -72.053  45.888  -3.863  1.00 178.90 ? 207  GLU A CA  1 
ATOM   1490  C  C   . GLU A 1 207  ? -71.872  47.369  -3.501  1.00 175.07 ? 207  GLU A C   1 
ATOM   1491  O  O   . GLU A 1 207  ? -70.799  47.777  -3.071  1.00 171.50 ? 207  GLU A O   1 
ATOM   1492  C  CB  . GLU A 1 207  ? -73.450  45.381  -3.525  1.00 183.97 ? 207  GLU A CB  1 
ATOM   1493  C  CG  . GLU A 1 207  ? -73.814  44.122  -4.309  1.00 188.26 ? 207  GLU A CG  1 
ATOM   1494  C  CD  . GLU A 1 207  ? -74.277  44.441  -5.718  1.00 192.75 ? 207  GLU A CD  1 
ATOM   1495  O  OE1 . GLU A 1 207  ? -73.783  45.433  -6.293  1.00 193.08 ? 207  GLU A OE1 1 
ATOM   1496  O  OE2 . GLU A 1 207  ? -75.142  43.708  -6.242  1.00 196.12 ? 207  GLU A OE2 1 
ATOM   1497  N  N   . ASP A 1 208  ? -72.905  48.176  -3.714  1.00 172.53 ? 208  ASP A N   1 
ATOM   1498  C  CA  . ASP A 1 208  ? -72.827  49.605  -3.438  1.00 166.68 ? 208  ASP A CA  1 
ATOM   1499  C  C   . ASP A 1 208  ? -72.732  49.792  -1.958  1.00 160.66 ? 208  ASP A C   1 
ATOM   1500  O  O   . ASP A 1 208  ? -73.088  48.883  -1.208  1.00 160.76 ? 208  ASP A O   1 
ATOM   1501  C  CB  . ASP A 1 208  ? -74.096  50.252  -3.907  1.00 165.77 ? 208  ASP A CB  1 
ATOM   1502  C  CG  . ASP A 1 208  ? -75.219  49.285  -3.918  1.00 164.01 ? 208  ASP A CG  1 
ATOM   1503  O  OD1 . ASP A 1 208  ? -75.686  48.921  -2.816  1.00 159.38 ? 208  ASP A OD1 1 
ATOM   1504  O  OD2 . ASP A 1 208  ? -75.602  48.870  -5.037  1.00 167.26 ? 208  ASP A OD2 1 
ATOM   1505  N  N   . PHE A 1 209  ? -72.317  50.995  -1.560  1.00 155.99 ? 209  PHE A N   1 
ATOM   1506  C  CA  . PHE A 1 209  ? -71.957  51.326  -0.179  1.00 150.33 ? 209  PHE A CA  1 
ATOM   1507  C  C   . PHE A 1 209  ? -70.442  51.563  -0.054  1.00 148.23 ? 209  PHE A C   1 
ATOM   1508  O  O   . PHE A 1 209  ? -69.644  50.676  -0.365  1.00 148.93 ? 209  PHE A O   1 
ATOM   1509  C  CB  . PHE A 1 209  ? -72.376  50.215  0.782   1.00 145.66 ? 209  PHE A CB  1 
ATOM   1510  C  CG  . PHE A 1 209  ? -73.852  50.157  1.051   1.00 144.02 ? 209  PHE A CG  1 
ATOM   1511  C  CD1 . PHE A 1 209  ? -74.451  48.957  1.421   1.00 143.33 ? 209  PHE A CD1 1 
ATOM   1512  C  CD2 . PHE A 1 209  ? -74.639  51.297  0.947   1.00 141.55 ? 209  PHE A CD2 1 
ATOM   1513  C  CE1 . PHE A 1 209  ? -75.812  48.890  1.691   1.00 142.09 ? 209  PHE A CE1 1 
ATOM   1514  C  CE2 . PHE A 1 209  ? -76.005  51.243  1.218   1.00 142.73 ? 209  PHE A CE2 1 
ATOM   1515  C  CZ  . PHE A 1 209  ? -76.591  50.034  1.592   1.00 142.33 ? 209  PHE A CZ  1 
ATOM   1516  N  N   . SER A 1 210  ? -70.050  52.750  0.411   1.00 146.56 ? 210  SER A N   1 
ATOM   1517  C  CA  . SER A 1 210  ? -68.629  53.113  0.499   1.00 144.26 ? 210  SER A CA  1 
ATOM   1518  C  C   . SER A 1 210  ? -67.938  52.642  1.787   1.00 140.39 ? 210  SER A C   1 
ATOM   1519  O  O   . SER A 1 210  ? -66.718  52.798  1.960   1.00 136.77 ? 210  SER A O   1 
ATOM   1520  C  CB  . SER A 1 210  ? -68.446  54.622  0.357   1.00 144.31 ? 210  SER A CB  1 
ATOM   1521  O  OG  . SER A 1 210  ? -67.063  54.946  0.407   1.00 143.01 ? 210  SER A OG  1 
ATOM   1522  N  N   . THR A 1 211  ? -68.734  52.069  2.680   1.00 140.94 ? 211  THR A N   1 
ATOM   1523  C  CA  . THR A 1 211  ? -68.293  51.737  4.028   1.00 138.55 ? 211  THR A CA  1 
ATOM   1524  C  C   . THR A 1 211  ? -67.017  50.893  4.061   1.00 136.43 ? 211  THR A C   1 
ATOM   1525  O  O   . THR A 1 211  ? -66.877  49.935  3.322   1.00 136.49 ? 211  THR A O   1 
ATOM   1526  C  CB  . THR A 1 211  ? -69.443  51.079  4.823   1.00 139.55 ? 211  THR A CB  1 
ATOM   1527  O  OG1 . THR A 1 211  ? -70.172  50.185  3.973   1.00 142.94 ? 211  THR A OG1 1 
ATOM   1528  C  CG2 . THR A 1 211  ? -70.393  52.142  5.300   1.00 138.55 ? 211  THR A CG2 1 
ATOM   1529  N  N   . THR A 1 212  ? -66.105  51.263  4.950   1.00 134.47 ? 212  THR A N   1 
ATOM   1530  C  CA  . THR A 1 212  ? -64.749  50.731  4.977   1.00 133.75 ? 212  THR A CA  1 
ATOM   1531  C  C   . THR A 1 212  ? -64.389  50.094  6.302   1.00 133.83 ? 212  THR A C   1 
ATOM   1532  O  O   . THR A 1 212  ? -64.567  50.677  7.371   1.00 135.56 ? 212  THR A O   1 
ATOM   1533  C  CB  . THR A 1 212  ? -63.744  51.870  4.848   1.00 132.23 ? 212  THR A CB  1 
ATOM   1534  O  OG1 . THR A 1 212  ? -64.188  52.784  3.845   1.00 134.54 ? 212  THR A OG1 1 
ATOM   1535  C  CG2 . THR A 1 212  ? -62.342  51.345  4.540   1.00 131.24 ? 212  THR A CG2 1 
ATOM   1536  N  N   . GLY A 1 213  ? -63.845  48.899  6.238   1.00 132.12 ? 213  GLY A N   1 
ATOM   1537  C  CA  . GLY A 1 213  ? -63.209  48.352  7.410   1.00 130.07 ? 213  GLY A CA  1 
ATOM   1538  C  C   . GLY A 1 213  ? -61.709  48.411  7.237   1.00 128.33 ? 213  GLY A C   1 
ATOM   1539  O  O   . GLY A 1 213  ? -61.192  48.346  6.127   1.00 130.23 ? 213  GLY A O   1 
ATOM   1540  N  N   . THR A 1 214  ? -60.998  48.532  8.340   1.00 126.16 ? 214  THR A N   1 
ATOM   1541  C  CA  . THR A 1 214  ? -59.563  48.379  8.297   1.00 123.10 ? 214  THR A CA  1 
ATOM   1542  C  C   . THR A 1 214  ? -59.115  47.752  9.592   1.00 116.80 ? 214  THR A C   1 
ATOM   1543  O  O   . THR A 1 214  ? -59.757  47.906  10.628  1.00 115.48 ? 214  THR A O   1 
ATOM   1544  C  CB  . THR A 1 214  ? -58.837  49.717  8.057   1.00 124.81 ? 214  THR A CB  1 
ATOM   1545  O  OG1 . THR A 1 214  ? -58.869  50.052  6.654   1.00 127.07 ? 214  THR A OG1 1 
ATOM   1546  C  CG2 . THR A 1 214  ? -57.381  49.636  8.545   1.00 121.71 ? 214  THR A CG2 1 
ATOM   1547  N  N   . ALA A 1 215  ? -58.019  47.018  9.511   1.00 113.18 ? 215  ALA A N   1 
ATOM   1548  C  CA  . ALA A 1 215  ? -57.489  46.301  10.645  1.00 109.14 ? 215  ALA A CA  1 
ATOM   1549  C  C   . ALA A 1 215  ? -55.995  46.231  10.418  1.00 108.16 ? 215  ALA A C   1 
ATOM   1550  O  O   . ALA A 1 215  ? -55.513  46.669  9.378   1.00 107.49 ? 215  ALA A O   1 
ATOM   1551  C  CB  . ALA A 1 215  ? -58.089  44.917  10.702  1.00 108.08 ? 215  ALA A CB  1 
ATOM   1552  N  N   . TYR A 1 216  ? -55.240  45.725  11.382  1.00 106.11 ? 216  TYR A N   1 
ATOM   1553  C  CA  . TYR A 1 216  ? -53.846  45.450  11.087  1.00 112.73 ? 216  TYR A CA  1 
ATOM   1554  C  C   . TYR A 1 216  ? -53.373  44.212  11.803  1.00 102.71 ? 216  TYR A C   1 
ATOM   1555  O  O   . TYR A 1 216  ? -54.065  43.683  12.676  1.00 106.38 ? 216  TYR A O   1 
ATOM   1556  C  CB  . TYR A 1 216  ? -52.934  46.616  11.455  1.00 115.69 ? 216  TYR A CB  1 
ATOM   1557  C  CG  . TYR A 1 216  ? -53.378  47.955  10.938  1.00 121.00 ? 216  TYR A CG  1 
ATOM   1558  C  CD1 . TYR A 1 216  ? -52.559  48.717  10.116  1.00 124.55 ? 216  TYR A CD1 1 
ATOM   1559  C  CD2 . TYR A 1 216  ? -54.607  48.471  11.294  1.00 126.50 ? 216  TYR A CD2 1 
ATOM   1560  C  CE1 . TYR A 1 216  ? -52.972  49.952  9.651   1.00 127.79 ? 216  TYR A CE1 1 
ATOM   1561  C  CE2 . TYR A 1 216  ? -55.030  49.688  10.828  1.00 129.95 ? 216  TYR A CE2 1 
ATOM   1562  C  CZ  . TYR A 1 216  ? -54.214  50.427  10.014  1.00 130.77 ? 216  TYR A CZ  1 
ATOM   1563  O  OH  . TYR A 1 216  ? -54.665  51.646  9.573   1.00 133.40 ? 216  TYR A OH  1 
ATOM   1564  N  N   . PHE A 1 217  ? -52.200  43.750  11.380  1.00 102.66 ? 217  PHE A N   1 
ATOM   1565  C  CA  . PHE A 1 217  ? -51.402  42.769  12.095  1.00 103.83 ? 217  PHE A CA  1 
ATOM   1566  C  C   . PHE A 1 217  ? -49.939  42.952  11.715  1.00 105.79 ? 217  PHE A C   1 
ATOM   1567  O  O   . PHE A 1 217  ? -49.619  43.542  10.685  1.00 107.63 ? 217  PHE A O   1 
ATOM   1568  C  CB  . PHE A 1 217  ? -51.913  41.323  11.914  1.00 103.27 ? 217  PHE A CB  1 
ATOM   1569  C  CG  . PHE A 1 217  ? -51.798  40.778  10.523  1.00 105.00 ? 217  PHE A CG  1 
ATOM   1570  C  CD1 . PHE A 1 217  ? -50.918  39.752  10.237  1.00 110.71 ? 217  PHE A CD1 1 
ATOM   1571  C  CD2 . PHE A 1 217  ? -52.583  41.251  9.507   1.00 107.29 ? 217  PHE A CD2 1 
ATOM   1572  C  CE1 . PHE A 1 217  ? -50.809  39.218  8.946   1.00 110.24 ? 217  PHE A CE1 1 
ATOM   1573  C  CE2 . PHE A 1 217  ? -52.470  40.723  8.223   1.00 111.60 ? 217  PHE A CE2 1 
ATOM   1574  C  CZ  . PHE A 1 217  ? -51.585  39.701  7.952   1.00 111.35 ? 217  PHE A CZ  1 
ATOM   1575  N  N   . GLU A 1 218  ? -49.044  42.518  12.585  1.00 110.35 ? 218  GLU A N   1 
ATOM   1576  C  CA  . GLU A 1 218  ? -47.627  42.696  12.314  1.00 114.03 ? 218  GLU A CA  1 
ATOM   1577  C  C   . GLU A 1 218  ? -46.962  41.352  12.133  1.00 112.87 ? 218  GLU A C   1 
ATOM   1578  O  O   . GLU A 1 218  ? -47.125  40.448  12.944  1.00 111.77 ? 218  GLU A O   1 
ATOM   1579  C  CB  . GLU A 1 218  ? -46.930  43.508  13.414  1.00 120.44 ? 218  GLU A CB  1 
ATOM   1580  C  CG  . GLU A 1 218  ? -45.569  44.076  13.004  1.00 127.52 ? 218  GLU A CG  1 
ATOM   1581  C  CD  . GLU A 1 218  ? -44.960  45.016  14.041  1.00 132.44 ? 218  GLU A CD  1 
ATOM   1582  O  OE1 . GLU A 1 218  ? -43.713  45.168  14.031  1.00 134.46 ? 218  GLU A OE1 1 
ATOM   1583  O  OE2 . GLU A 1 218  ? -45.719  45.594  14.859  1.00 134.18 ? 218  GLU A OE2 1 
ATOM   1584  N  N   . VAL A 1 219  ? -46.242  41.218  11.031  1.00 113.91 ? 219  VAL A N   1 
ATOM   1585  C  CA  . VAL A 1 219  ? -45.514  40.005  10.762  1.00 113.33 ? 219  VAL A CA  1 
ATOM   1586  C  C   . VAL A 1 219  ? -44.131  40.297  11.214  1.00 112.50 ? 219  VAL A C   1 
ATOM   1587  O  O   . VAL A 1 219  ? -43.467  41.175  10.649  1.00 112.09 ? 219  VAL A O   1 
ATOM   1588  C  CB  . VAL A 1 219  ? -45.492  39.665  9.273   1.00 112.21 ? 219  VAL A CB  1 
ATOM   1589  C  CG1 . VAL A 1 219  ? -44.156  39.042  8.882   1.00 109.28 ? 219  VAL A CG1 1 
ATOM   1590  C  CG2 . VAL A 1 219  ? -46.658  38.744  8.930   1.00 105.37 ? 219  VAL A CG2 1 
ATOM   1591  N  N   . LYS A 1 220  ? -43.725  39.596  12.267  1.00 112.81 ? 220  LYS A N   1 
ATOM   1592  C  CA  . LYS A 1 220  ? -42.355  39.666  12.742  1.00 111.37 ? 220  LYS A CA  1 
ATOM   1593  C  C   . LYS A 1 220  ? -41.654  38.318  12.573  1.00 109.74 ? 220  LYS A C   1 
ATOM   1594  O  O   . LYS A 1 220  ? -42.291  37.256  12.532  1.00 103.75 ? 220  LYS A O   1 
ATOM   1595  C  CB  . LYS A 1 220  ? -42.292  40.169  14.185  1.00 109.39 ? 220  LYS A CB  1 
ATOM   1596  C  CG  . LYS A 1 220  ? -42.771  41.609  14.370  1.00 109.84 ? 220  LYS A CG  1 
ATOM   1597  C  CD  . LYS A 1 220  ? -43.353  41.826  15.790  1.00 114.54 ? 220  LYS A CD  1 
ATOM   1598  C  CE  . LYS A 1 220  ? -43.498  43.311  16.204  1.00 113.42 ? 220  LYS A CE  1 
ATOM   1599  N  NZ  . LYS A 1 220  ? -42.321  43.871  16.954  1.00 112.47 ? 220  LYS A NZ  1 
ATOM   1600  N  N   . GLU A 1 221  ? -40.331  38.399  12.457  1.00 117.93 ? 221  GLU A N   1 
ATOM   1601  C  CA  . GLU A 1 221  ? -39.459  37.254  12.210  1.00 127.98 ? 221  GLU A CA  1 
ATOM   1602  C  C   . GLU A 1 221  ? -38.944  36.576  13.473  1.00 125.61 ? 221  GLU A C   1 
ATOM   1603  O  O   . GLU A 1 221  ? -38.054  37.096  14.150  1.00 123.30 ? 221  GLU A O   1 
ATOM   1604  C  CB  . GLU A 1 221  ? -38.251  37.697  11.392  1.00 138.53 ? 221  GLU A CB  1 
ATOM   1605  C  CG  . GLU A 1 221  ? -37.164  36.645  11.332  1.00 149.18 ? 221  GLU A CG  1 
ATOM   1606  C  CD  . GLU A 1 221  ? -35.794  37.261  11.242  1.00 156.37 ? 221  GLU A CD  1 
ATOM   1607  O  OE1 . GLU A 1 221  ? -35.727  38.520  11.229  1.00 157.40 ? 221  GLU A OE1 1 
ATOM   1608  O  OE2 . GLU A 1 221  ? -34.800  36.489  11.187  1.00 159.65 ? 221  GLU A OE2 1 
ATOM   1609  N  N   . TYR A 1 222  ? -39.472  35.395  13.765  1.00 125.33 ? 222  TYR A N   1 
ATOM   1610  C  CA  . TYR A 1 222  ? -39.098  34.700  14.981  1.00 124.33 ? 222  TYR A CA  1 
ATOM   1611  C  C   . TYR A 1 222  ? -37.638  34.233  14.970  1.00 125.34 ? 222  TYR A C   1 
ATOM   1612  O  O   . TYR A 1 222  ? -37.145  33.722  13.961  1.00 126.45 ? 222  TYR A O   1 
ATOM   1613  C  CB  . TYR A 1 222  ? -40.014  33.512  15.236  1.00 123.11 ? 222  TYR A CB  1 
ATOM   1614  C  CG  . TYR A 1 222  ? -39.546  32.753  16.423  1.00 121.85 ? 222  TYR A CG  1 
ATOM   1615  C  CD1 . TYR A 1 222  ? -40.212  32.824  17.625  1.00 120.31 ? 222  TYR A CD1 1 
ATOM   1616  C  CD2 . TYR A 1 222  ? -38.391  32.007  16.355  1.00 123.67 ? 222  TYR A CD2 1 
ATOM   1617  C  CE1 . TYR A 1 222  ? -39.753  32.141  18.727  1.00 121.24 ? 222  TYR A CE1 1 
ATOM   1618  C  CE2 . TYR A 1 222  ? -37.917  31.330  17.439  1.00 124.38 ? 222  TYR A CE2 1 
ATOM   1619  C  CZ  . TYR A 1 222  ? -38.595  31.391  18.628  1.00 123.09 ? 222  TYR A CZ  1 
ATOM   1620  O  OH  . TYR A 1 222  ? -38.098  30.691  19.707  1.00 123.00 ? 222  TYR A OH  1 
ATOM   1621  N  N   . VAL A 1 223  ? -36.965  34.411  16.108  1.00 124.40 ? 223  VAL A N   1 
ATOM   1622  C  CA  . VAL A 1 223  ? -35.593  33.967  16.305  1.00 121.92 ? 223  VAL A CA  1 
ATOM   1623  C  C   . VAL A 1 223  ? -35.514  33.234  17.607  1.00 123.06 ? 223  VAL A C   1 
ATOM   1624  O  O   . VAL A 1 223  ? -36.069  33.668  18.606  1.00 121.61 ? 223  VAL A O   1 
ATOM   1625  C  CB  . VAL A 1 223  ? -34.611  35.113  16.518  1.00 119.06 ? 223  VAL A CB  1 
ATOM   1626  C  CG1 . VAL A 1 223  ? -33.188  34.567  16.541  1.00 117.79 ? 223  VAL A CG1 1 
ATOM   1627  C  CG2 . VAL A 1 223  ? -34.774  36.199  15.474  1.00 118.46 ? 223  VAL A CG2 1 
ATOM   1628  N  N   . LEU A 1 224  ? -34.766  32.143  17.602  1.00 126.94 ? 224  LEU A N   1 
ATOM   1629  C  CA  . LEU A 1 224  ? -34.549  31.345  18.802  1.00 129.65 ? 224  LEU A CA  1 
ATOM   1630  C  C   . LEU A 1 224  ? -33.671  32.119  19.782  1.00 130.36 ? 224  LEU A C   1 
ATOM   1631  O  O   . LEU A 1 224  ? -32.623  32.663  19.399  1.00 130.87 ? 224  LEU A O   1 
ATOM   1632  C  CB  . LEU A 1 224  ? -33.911  29.996  18.439  1.00 128.84 ? 224  LEU A CB  1 
ATOM   1633  C  CG  . LEU A 1 224  ? -34.432  28.802  19.228  1.00 130.44 ? 224  LEU A CG  1 
ATOM   1634  C  CD1 . LEU A 1 224  ? -33.693  28.677  20.526  1.00 131.00 ? 224  LEU A CD1 1 
ATOM   1635  C  CD2 . LEU A 1 224  ? -35.917  28.953  19.478  1.00 129.53 ? 224  LEU A CD2 1 
ATOM   1636  N  N   . PRO A 1 225  ? -34.104  32.180  21.052  1.00 144.70 ? 225  PRO A N   1 
ATOM   1637  C  CA  . PRO A 1 225  ? -33.399  32.938  22.086  1.00 138.74 ? 225  PRO A CA  1 
ATOM   1638  C  C   . PRO A 1 225  ? -32.332  32.091  22.761  1.00 139.69 ? 225  PRO A C   1 
ATOM   1639  O  O   . PRO A 1 225  ? -32.573  30.923  23.076  1.00 138.70 ? 225  PRO A O   1 
ATOM   1640  C  CB  . PRO A 1 225  ? -34.513  33.280  23.084  1.00 138.91 ? 225  PRO A CB  1 
ATOM   1641  C  CG  . PRO A 1 225  ? -35.805  32.652  22.522  1.00 141.72 ? 225  PRO A CG  1 
ATOM   1642  C  CD  . PRO A 1 225  ? -35.347  31.590  21.574  1.00 144.96 ? 225  PRO A CD  1 
ATOM   1643  N  N   . HIS A 1 226  ? -31.164  32.677  22.981  1.00 139.50 ? 226  HIS A N   1 
ATOM   1644  C  CA  . HIS A 1 226  ? -30.075  31.964  23.641  1.00 144.25 ? 226  HIS A CA  1 
ATOM   1645  C  C   . HIS A 1 226  ? -30.133  32.054  25.172  1.00 139.42 ? 226  HIS A C   1 
ATOM   1646  O  O   . HIS A 1 226  ? -29.763  31.124  25.893  1.00 137.45 ? 226  HIS A O   1 
ATOM   1647  C  CB  . HIS A 1 226  ? -28.732  32.486  23.138  1.00 149.92 ? 226  HIS A CB  1 
ATOM   1648  C  CG  . HIS A 1 226  ? -28.369  31.999  21.769  1.00 158.95 ? 226  HIS A CG  1 
ATOM   1649  N  ND1 . HIS A 1 226  ? -28.180  32.854  20.700  1.00 162.37 ? 226  HIS A ND1 1 
ATOM   1650  C  CD2 . HIS A 1 226  ? -28.159  30.747  21.293  1.00 163.15 ? 226  HIS A CD2 1 
ATOM   1651  C  CE1 . HIS A 1 226  ? -27.867  32.148  19.627  1.00 166.44 ? 226  HIS A CE1 1 
ATOM   1652  N  NE2 . HIS A 1 226  ? -27.846  30.866  19.960  1.00 166.98 ? 226  HIS A NE2 1 
ATOM   1653  N  N   . PHE A 1 227  ? -30.598  33.194  25.661  1.00 136.96 ? 227  PHE A N   1 
ATOM   1654  C  CA  . PHE A 1 227  ? -30.689  33.437  27.090  1.00 133.41 ? 227  PHE A CA  1 
ATOM   1655  C  C   . PHE A 1 227  ? -31.551  34.628  27.311  1.00 132.75 ? 227  PHE A C   1 
ATOM   1656  O  O   . PHE A 1 227  ? -31.463  35.600  26.578  1.00 135.76 ? 227  PHE A O   1 
ATOM   1657  C  CB  . PHE A 1 227  ? -29.317  33.722  27.688  1.00 127.86 ? 227  PHE A CB  1 
ATOM   1658  C  CG  . PHE A 1 227  ? -28.561  34.792  26.982  1.00 121.30 ? 227  PHE A CG  1 
ATOM   1659  C  CD1 . PHE A 1 227  ? -28.804  36.113  27.256  1.00 116.82 ? 227  PHE A CD1 1 
ATOM   1660  C  CD2 . PHE A 1 227  ? -27.597  34.466  26.044  1.00 121.40 ? 227  PHE A CD2 1 
ATOM   1661  C  CE1 . PHE A 1 227  ? -28.104  37.088  26.603  1.00 116.07 ? 227  PHE A CE1 1 
ATOM   1662  C  CE2 . PHE A 1 227  ? -26.890  35.435  25.388  1.00 119.89 ? 227  PHE A CE2 1 
ATOM   1663  C  CZ  . PHE A 1 227  ? -27.142  36.748  25.664  1.00 117.76 ? 227  PHE A CZ  1 
ATOM   1664  N  N   . SER A 1 228  ? -32.360  34.563  28.348  1.00 131.35 ? 228  SER A N   1 
ATOM   1665  C  CA  . SER A 1 228  ? -33.317  35.618  28.611  1.00 132.19 ? 228  SER A CA  1 
ATOM   1666  C  C   . SER A 1 228  ? -32.668  36.991  28.914  1.00 126.10 ? 228  SER A C   1 
ATOM   1667  O  O   . SER A 1 228  ? -32.001  37.146  29.931  1.00 124.02 ? 228  SER A O   1 
ATOM   1668  C  CB  . SER A 1 228  ? -34.235  35.167  29.755  1.00 136.46 ? 228  SER A CB  1 
ATOM   1669  O  OG  . SER A 1 228  ? -35.097  36.206  30.183  1.00 137.49 ? 228  SER A OG  1 
ATOM   1670  N  N   . VAL A 1 229  ? -32.848  37.969  28.024  1.00 123.48 ? 229  VAL A N   1 
ATOM   1671  C  CA  . VAL A 1 229  ? -32.453  39.335  28.315  1.00 110.28 ? 229  VAL A CA  1 
ATOM   1672  C  C   . VAL A 1 229  ? -33.693  40.141  28.654  1.00 113.92 ? 229  VAL A C   1 
ATOM   1673  O  O   . VAL A 1 229  ? -34.644  40.153  27.884  1.00 112.35 ? 229  VAL A O   1 
ATOM   1674  C  CB  . VAL A 1 229  ? -31.647  39.982  27.177  1.00 94.42  ? 229  VAL A CB  1 
ATOM   1675  C  CG1 . VAL A 1 229  ? -31.768  41.473  27.252  1.00 89.57  ? 229  VAL A CG1 1 
ATOM   1676  C  CG2 . VAL A 1 229  ? -30.202  39.591  27.281  1.00 92.14  ? 229  VAL A CG2 1 
ATOM   1677  N  N   . SER A 1 230  ? -33.694  40.735  29.853  1.00 111.16 ? 230  SER A N   1 
ATOM   1678  C  CA  . SER A 1 230  ? -34.759  41.630  30.341  1.00 108.44 ? 230  SER A CA  1 
ATOM   1679  C  C   . SER A 1 230  ? -34.263  43.059  30.406  1.00 106.19 ? 230  SER A C   1 
ATOM   1680  O  O   . SER A 1 230  ? -33.071  43.316  30.598  1.00 106.18 ? 230  SER A O   1 
ATOM   1681  C  CB  . SER A 1 230  ? -35.234  41.260  31.744  1.00 106.88 ? 230  SER A CB  1 
ATOM   1682  O  OG  . SER A 1 230  ? -34.278  41.572  32.724  1.00 105.24 ? 230  SER A OG  1 
ATOM   1683  N  N   . ILE A 1 231  ? -35.178  44.005  30.291  1.00 104.22 ? 231  ILE A N   1 
ATOM   1684  C  CA  . ILE A 1 231  ? -34.779  45.395  30.365  1.00 103.58 ? 231  ILE A CA  1 
ATOM   1685  C  C   . ILE A 1 231  ? -35.870  46.239  31.012  1.00 108.48 ? 231  ILE A C   1 
ATOM   1686  O  O   . ILE A 1 231  ? -37.001  46.281  30.532  1.00 110.89 ? 231  ILE A O   1 
ATOM   1687  C  CB  . ILE A 1 231  ? -34.372  45.920  28.989  1.00 100.12 ? 231  ILE A CB  1 
ATOM   1688  C  CG1 . ILE A 1 231  ? -34.583  47.407  28.914  1.00 98.87  ? 231  ILE A CG1 1 
ATOM   1689  C  CG2 . ILE A 1 231  ? -35.167  45.271  27.899  1.00 101.01 ? 231  ILE A CG2 1 
ATOM   1690  C  CD1 . ILE A 1 231  ? -34.299  47.928  27.567  1.00 100.13 ? 231  ILE A CD1 1 
ATOM   1691  N  N   . GLU A 1 232  ? -35.518  46.877  32.129  1.00 111.82 ? 232  GLU A N   1 
ATOM   1692  C  CA  . GLU A 1 232  ? -36.469  47.598  32.974  1.00 115.67 ? 232  GLU A CA  1 
ATOM   1693  C  C   . GLU A 1 232  ? -36.015  49.036  33.209  1.00 113.77 ? 232  GLU A C   1 
ATOM   1694  O  O   . GLU A 1 232  ? -34.866  49.308  33.552  1.00 111.92 ? 232  GLU A O   1 
ATOM   1695  C  CB  . GLU A 1 232  ? -36.652  46.884  34.318  1.00 122.17 ? 232  GLU A CB  1 
ATOM   1696  C  CG  . GLU A 1 232  ? -36.714  45.358  34.205  1.00 131.38 ? 232  GLU A CG  1 
ATOM   1697  C  CD  . GLU A 1 232  ? -36.126  44.603  35.412  1.00 137.69 ? 232  GLU A CD  1 
ATOM   1698  O  OE1 . GLU A 1 232  ? -36.135  45.133  36.555  1.00 139.34 ? 232  GLU A OE1 1 
ATOM   1699  O  OE2 . GLU A 1 232  ? -35.668  43.454  35.207  1.00 140.21 ? 232  GLU A OE2 1 
ATOM   1700  N  N   . PRO A 1 233  ? -36.939  49.971  33.037  1.00 115.26 ? 233  PRO A N   1 
ATOM   1701  C  CA  . PRO A 1 233  ? -36.630  51.389  32.949  1.00 116.66 ? 233  PRO A CA  1 
ATOM   1702  C  C   . PRO A 1 233  ? -36.919  52.047  34.283  1.00 115.39 ? 233  PRO A C   1 
ATOM   1703  O  O   . PRO A 1 233  ? -37.811  51.556  34.978  1.00 117.52 ? 233  PRO A O   1 
ATOM   1704  C  CB  . PRO A 1 233  ? -37.649  51.872  31.915  1.00 117.60 ? 233  PRO A CB  1 
ATOM   1705  C  CG  . PRO A 1 233  ? -38.685  50.710  31.785  1.00 115.42 ? 233  PRO A CG  1 
ATOM   1706  C  CD  . PRO A 1 233  ? -38.376  49.746  32.874  1.00 115.38 ? 233  PRO A CD  1 
ATOM   1707  N  N   . GLU A 1 234  ? -36.230  53.136  34.629  1.00 113.02 ? 234  GLU A N   1 
ATOM   1708  C  CA  . GLU A 1 234  ? -36.439  53.719  35.949  1.00 109.27 ? 234  GLU A CA  1 
ATOM   1709  C  C   . GLU A 1 234  ? -37.927  53.874  36.279  1.00 105.96 ? 234  GLU A C   1 
ATOM   1710  O  O   . GLU A 1 234  ? -38.394  53.318  37.265  1.00 107.43 ? 234  GLU A O   1 
ATOM   1711  C  CB  . GLU A 1 234  ? -35.663  55.025  36.183  1.00 110.11 ? 234  GLU A CB  1 
ATOM   1712  C  CG  . GLU A 1 234  ? -35.459  55.240  37.707  1.00 125.28 ? 234  GLU A CG  1 
ATOM   1713  C  CD  . GLU A 1 234  ? -34.732  56.521  38.122  1.00 126.83 ? 234  GLU A CD  1 
ATOM   1714  O  OE1 . GLU A 1 234  ? -34.007  57.109  37.287  1.00 128.29 ? 234  GLU A OE1 1 
ATOM   1715  O  OE2 . GLU A 1 234  ? -34.877  56.918  39.310  1.00 126.29 ? 234  GLU A OE2 1 
ATOM   1716  N  N   . TYR A 1 235  ? -38.676  54.605  35.460  1.00 100.18 ? 235  TYR A N   1 
ATOM   1717  C  CA  . TYR A 1 235  ? -40.127  54.625  35.604  1.00 96.64  ? 235  TYR A CA  1 
ATOM   1718  C  C   . TYR A 1 235  ? -40.780  54.521  34.223  1.00 94.19  ? 235  TYR A C   1 
ATOM   1719  O  O   . TYR A 1 235  ? -40.102  54.446  33.219  1.00 94.12  ? 235  TYR A O   1 
ATOM   1720  C  CB  . TYR A 1 235  ? -40.637  55.898  36.290  1.00 97.62  ? 235  TYR A CB  1 
ATOM   1721  C  CG  . TYR A 1 235  ? -39.883  56.451  37.489  1.00 100.47 ? 235  TYR A CG  1 
ATOM   1722  C  CD1 . TYR A 1 235  ? -40.571  57.146  38.482  1.00 103.98 ? 235  TYR A CD1 1 
ATOM   1723  C  CD2 . TYR A 1 235  ? -38.498  56.339  37.616  1.00 102.00 ? 235  TYR A CD2 1 
ATOM   1724  C  CE1 . TYR A 1 235  ? -39.911  57.698  39.596  1.00 107.23 ? 235  TYR A CE1 1 
ATOM   1725  C  CE2 . TYR A 1 235  ? -37.821  56.880  38.731  1.00 104.98 ? 235  TYR A CE2 1 
ATOM   1726  C  CZ  . TYR A 1 235  ? -38.536  57.557  39.714  1.00 108.07 ? 235  TYR A CZ  1 
ATOM   1727  O  OH  . TYR A 1 235  ? -37.893  58.098  40.811  1.00 110.01 ? 235  TYR A OH  1 
ATOM   1728  N  N   . ASN A 1 236  ? -42.104  54.560  34.187  1.00 91.55  ? 236  ASN A N   1 
ATOM   1729  C  CA  . ASN A 1 236  ? -42.863  54.314  32.971  1.00 91.23  ? 236  ASN A CA  1 
ATOM   1730  C  C   . ASN A 1 236  ? -43.140  55.522  32.093  1.00 87.64  ? 236  ASN A C   1 
ATOM   1731  O  O   . ASN A 1 236  ? -43.669  55.393  30.973  1.00 92.62  ? 236  ASN A O   1 
ATOM   1732  C  CB  . ASN A 1 236  ? -44.184  53.667  33.319  1.00 95.89  ? 236  ASN A CB  1 
ATOM   1733  C  CG  . ASN A 1 236  ? -44.044  52.209  33.550  1.00 102.82 ? 236  ASN A CG  1 
ATOM   1734  O  OD1 . ASN A 1 236  ? -42.921  51.666  33.592  1.00 103.49 ? 236  ASN A OD1 1 
ATOM   1735  N  ND2 . ASN A 1 236  ? -45.179  51.539  33.706  1.00 107.29 ? 236  ASN A ND2 1 
ATOM   1736  N  N   . PHE A 1 237  ? -42.847  56.702  32.607  1.00 79.45  ? 237  PHE A N   1 
ATOM   1737  C  CA  . PHE A 1 237  ? -42.884  57.874  31.767  1.00 78.44  ? 237  PHE A CA  1 
ATOM   1738  C  C   . PHE A 1 237  ? -41.721  58.690  32.203  1.00 75.66  ? 237  PHE A C   1 
ATOM   1739  O  O   . PHE A 1 237  ? -41.230  58.503  33.287  1.00 72.18  ? 237  PHE A O   1 
ATOM   1740  C  CB  . PHE A 1 237  ? -44.116  58.730  31.982  1.00 72.41  ? 237  PHE A CB  1 
ATOM   1741  C  CG  . PHE A 1 237  ? -45.377  57.987  32.008  1.00 73.06  ? 237  PHE A CG  1 
ATOM   1742  C  CD1 . PHE A 1 237  ? -46.465  58.472  31.380  1.00 73.89  ? 237  PHE A CD1 1 
ATOM   1743  C  CD2 . PHE A 1 237  ? -45.502  56.840  32.708  1.00 73.05  ? 237  PHE A CD2 1 
ATOM   1744  C  CE1 . PHE A 1 237  ? -47.664  57.810  31.435  1.00 76.62  ? 237  PHE A CE1 1 
ATOM   1745  C  CE2 . PHE A 1 237  ? -46.692  56.180  32.759  1.00 80.17  ? 237  PHE A CE2 1 
ATOM   1746  C  CZ  . PHE A 1 237  ? -47.777  56.672  32.116  1.00 76.24  ? 237  PHE A CZ  1 
ATOM   1747  N  N   . ILE A 1 238  ? -41.291  59.608  31.357  1.00 79.70  ? 238  ILE A N   1 
ATOM   1748  C  CA  . ILE A 1 238  ? -40.310  60.564  31.772  1.00 81.04  ? 238  ILE A CA  1 
ATOM   1749  C  C   . ILE A 1 238  ? -40.926  61.932  32.018  1.00 87.04  ? 238  ILE A C   1 
ATOM   1750  O  O   . ILE A 1 238  ? -41.770  62.404  31.246  1.00 88.25  ? 238  ILE A O   1 
ATOM   1751  C  CB  . ILE A 1 238  ? -39.201  60.596  30.822  1.00 73.05  ? 238  ILE A CB  1 
ATOM   1752  C  CG1 . ILE A 1 238  ? -38.948  59.169  30.333  1.00 73.69  ? 238  ILE A CG1 1 
ATOM   1753  C  CG2 . ILE A 1 238  ? -38.019  61.116  31.533  1.00 81.06  ? 238  ILE A CG2 1 
ATOM   1754  C  CD1 . ILE A 1 238  ? -37.551  58.919  29.788  1.00 74.58  ? 238  ILE A CD1 1 
ATOM   1755  N  N   . GLY A 1 239  ? -40.510  62.531  33.137  1.00 91.10  ? 239  GLY A N   1 
ATOM   1756  C  CA  . GLY A 1 239  ? -41.174  63.693  33.729  1.00 93.20  ? 239  GLY A CA  1 
ATOM   1757  C  C   . GLY A 1 239  ? -40.115  64.639  34.258  1.00 96.58  ? 239  GLY A C   1 
ATOM   1758  O  O   . GLY A 1 239  ? -38.973  64.211  34.468  1.00 96.60  ? 239  GLY A O   1 
ATOM   1759  N  N   . TYR A 1 240  ? -40.448  65.911  34.455  1.00 97.63  ? 240  TYR A N   1 
ATOM   1760  C  CA  . TYR A 1 240  ? -39.362  66.880  34.553  1.00 101.80 ? 240  TYR A CA  1 
ATOM   1761  C  C   . TYR A 1 240  ? -38.353  66.381  35.549  1.00 104.66 ? 240  TYR A C   1 
ATOM   1762  O  O   . TYR A 1 240  ? -37.165  66.614  35.378  1.00 103.20 ? 240  TYR A O   1 
ATOM   1763  C  CB  . TYR A 1 240  ? -39.835  68.261  34.987  1.00 102.19 ? 240  TYR A CB  1 
ATOM   1764  C  CG  . TYR A 1 240  ? -40.222  68.296  36.435  1.00 98.04  ? 240  TYR A CG  1 
ATOM   1765  C  CD1 . TYR A 1 240  ? -39.310  68.628  37.418  1.00 94.28  ? 240  TYR A CD1 1 
ATOM   1766  C  CD2 . TYR A 1 240  ? -41.495  67.955  36.812  1.00 97.44  ? 240  TYR A CD2 1 
ATOM   1767  C  CE1 . TYR A 1 240  ? -39.672  68.626  38.725  1.00 92.76  ? 240  TYR A CE1 1 
ATOM   1768  C  CE2 . TYR A 1 240  ? -41.863  67.965  38.108  1.00 96.52  ? 240  TYR A CE2 1 
ATOM   1769  C  CZ  . TYR A 1 240  ? -40.960  68.290  39.066  1.00 95.37  ? 240  TYR A CZ  1 
ATOM   1770  O  OH  . TYR A 1 240  ? -41.417  68.271  40.368  1.00 98.47  ? 240  TYR A OH  1 
ATOM   1771  N  N   . LYS A 1 241  ? -38.845  65.683  36.578  1.00 108.72 ? 241  LYS A N   1 
ATOM   1772  C  CA  . LYS A 1 241  ? -38.009  65.214  37.686  1.00 113.19 ? 241  LYS A CA  1 
ATOM   1773  C  C   . LYS A 1 241  ? -36.724  64.541  37.169  1.00 117.22 ? 241  LYS A C   1 
ATOM   1774  O  O   . LYS A 1 241  ? -35.607  65.018  37.424  1.00 118.90 ? 241  LYS A O   1 
ATOM   1775  C  CB  . LYS A 1 241  ? -38.804  64.320  38.678  1.00 96.24  ? 241  LYS A CB  1 
ATOM   1776  C  CG  . LYS A 1 241  ? -39.526  65.076  39.841  1.00 78.13  ? 241  LYS A CG  1 
ATOM   1777  C  CD  . LYS A 1 241  ? -40.424  64.155  40.707  1.00 92.11  ? 241  LYS A CD  1 
ATOM   1778  C  CE  . LYS A 1 241  ? -41.142  64.874  41.909  1.00 124.01 ? 241  LYS A CE  1 
ATOM   1779  N  NZ  . LYS A 1 241  ? -42.559  65.401  41.701  1.00 122.67 ? 241  LYS A NZ  1 
ATOM   1780  N  N   . ASN A 1 242  ? -36.879  63.447  36.431  1.00 117.73 ? 242  ASN A N   1 
ATOM   1781  C  CA  . ASN A 1 242  ? -35.741  62.841  35.733  1.00 118.24 ? 242  ASN A CA  1 
ATOM   1782  C  C   . ASN A 1 242  ? -35.781  63.147  34.252  1.00 121.70 ? 242  ASN A C   1 
ATOM   1783  O  O   . ASN A 1 242  ? -36.821  63.034  33.620  1.00 119.71 ? 242  ASN A O   1 
ATOM   1784  C  CB  . ASN A 1 242  ? -35.620  61.332  35.980  1.00 112.13 ? 242  ASN A CB  1 
ATOM   1785  C  CG  . ASN A 1 242  ? -36.860  60.727  36.610  1.00 105.99 ? 242  ASN A CG  1 
ATOM   1786  O  OD1 . ASN A 1 242  ? -36.767  59.688  37.253  1.00 103.99 ? 242  ASN A OD1 1 
ATOM   1787  N  ND2 . ASN A 1 242  ? -38.020  61.364  36.433  1.00 102.19 ? 242  ASN A ND2 1 
ATOM   1788  N  N   . PHE A 1 243  ? -34.637  63.548  33.719  1.00 127.44 ? 243  PHE A N   1 
ATOM   1789  C  CA  . PHE A 1 243  ? -34.552  64.090  32.376  1.00 135.18 ? 243  PHE A CA  1 
ATOM   1790  C  C   . PHE A 1 243  ? -33.156  64.610  32.283  1.00 141.08 ? 243  PHE A C   1 
ATOM   1791  O  O   . PHE A 1 243  ? -32.712  65.079  31.242  1.00 141.83 ? 243  PHE A O   1 
ATOM   1792  C  CB  . PHE A 1 243  ? -35.515  65.252  32.183  1.00 136.63 ? 243  PHE A CB  1 
ATOM   1793  C  CG  . PHE A 1 243  ? -35.475  65.861  30.795  1.00 139.67 ? 243  PHE A CG  1 
ATOM   1794  C  CD1 . PHE A 1 243  ? -36.166  65.276  29.750  1.00 139.59 ? 243  PHE A CD1 1 
ATOM   1795  C  CD2 . PHE A 1 243  ? -34.780  67.029  30.549  1.00 142.13 ? 243  PHE A CD2 1 
ATOM   1796  C  CE1 . PHE A 1 243  ? -36.153  65.827  28.506  1.00 140.66 ? 243  PHE A CE1 1 
ATOM   1797  C  CE2 . PHE A 1 243  ? -34.775  67.581  29.293  1.00 143.37 ? 243  PHE A CE2 1 
ATOM   1798  C  CZ  . PHE A 1 243  ? -35.460  66.979  28.278  1.00 142.70 ? 243  PHE A CZ  1 
ATOM   1799  N  N   . LYS A 1 244  ? -32.484  64.581  33.419  1.00 148.36 ? 244  LYS A N   1 
ATOM   1800  C  CA  . LYS A 1 244  ? -31.047  64.605  33.411  1.00 156.63 ? 244  LYS A CA  1 
ATOM   1801  C  C   . LYS A 1 244  ? -30.598  63.210  33.812  1.00 157.18 ? 244  LYS A C   1 
ATOM   1802  O  O   . LYS A 1 244  ? -29.406  62.913  33.806  1.00 163.28 ? 244  LYS A O   1 
ATOM   1803  C  CB  . LYS A 1 244  ? -30.490  65.706  34.319  1.00 161.72 ? 244  LYS A CB  1 
ATOM   1804  C  CG  . LYS A 1 244  ? -30.610  67.117  33.729  1.00 165.93 ? 244  LYS A CG  1 
ATOM   1805  C  CD  . LYS A 1 244  ? -29.528  68.053  34.277  1.00 169.65 ? 244  LYS A CD  1 
ATOM   1806  C  CE  . LYS A 1 244  ? -29.735  69.510  33.853  1.00 171.26 ? 244  LYS A CE  1 
ATOM   1807  N  NZ  . LYS A 1 244  ? -30.742  70.231  34.676  1.00 169.65 ? 244  LYS A NZ  1 
ATOM   1808  N  N   . ASN A 1 245  ? -31.565  62.347  34.129  1.00 152.47 ? 245  ASN A N   1 
ATOM   1809  C  CA  . ASN A 1 245  ? -31.261  60.937  34.388  1.00 150.04 ? 245  ASN A CA  1 
ATOM   1810  C  C   . ASN A 1 245  ? -32.486  59.987  34.417  1.00 143.29 ? 245  ASN A C   1 
ATOM   1811  O  O   . ASN A 1 245  ? -33.616  60.434  34.668  1.00 143.29 ? 245  ASN A O   1 
ATOM   1812  C  CB  . ASN A 1 245  ? -30.469  60.806  35.681  1.00 151.76 ? 245  ASN A CB  1 
ATOM   1813  C  CG  . ASN A 1 245  ? -31.310  61.081  36.875  1.00 153.84 ? 245  ASN A CG  1 
ATOM   1814  O  OD1 . ASN A 1 245  ? -32.372  61.698  36.774  1.00 154.55 ? 245  ASN A OD1 1 
ATOM   1815  N  ND2 . ASN A 1 245  ? -30.862  60.614  38.017  1.00 156.80 ? 245  ASN A ND2 1 
ATOM   1816  N  N   . PHE A 1 246  ? -32.227  58.683  34.179  1.00 134.27 ? 246  PHE A N   1 
ATOM   1817  C  CA  . PHE A 1 246  ? -33.241  57.617  34.030  1.00 118.41 ? 246  PHE A CA  1 
ATOM   1818  C  C   . PHE A 1 246  ? -32.608  56.236  34.200  1.00 112.02 ? 246  PHE A C   1 
ATOM   1819  O  O   . PHE A 1 246  ? -32.141  55.694  33.218  1.00 110.63 ? 246  PHE A O   1 
ATOM   1820  C  CB  . PHE A 1 246  ? -33.770  57.666  32.608  1.00 108.27 ? 246  PHE A CB  1 
ATOM   1821  C  CG  . PHE A 1 246  ? -35.134  57.096  32.447  1.00 96.87  ? 246  PHE A CG  1 
ATOM   1822  C  CD1 . PHE A 1 246  ? -36.211  57.702  33.024  1.00 90.12  ? 246  PHE A CD1 1 
ATOM   1823  C  CD2 . PHE A 1 246  ? -35.346  55.975  31.679  1.00 94.01  ? 246  PHE A CD2 1 
ATOM   1824  C  CE1 . PHE A 1 246  ? -37.463  57.187  32.860  1.00 86.39  ? 246  PHE A CE1 1 
ATOM   1825  C  CE2 . PHE A 1 246  ? -36.611  55.469  31.510  1.00 90.20  ? 246  PHE A CE2 1 
ATOM   1826  C  CZ  . PHE A 1 246  ? -37.664  56.079  32.105  1.00 86.99  ? 246  PHE A CZ  1 
ATOM   1827  N  N   . GLU A 1 247  ? -32.609  55.658  35.409  1.00 109.59 ? 247  GLU A N   1 
ATOM   1828  C  CA  . GLU A 1 247  ? -31.842  54.414  35.731  1.00 109.98 ? 247  GLU A CA  1 
ATOM   1829  C  C   . GLU A 1 247  ? -32.465  53.179  34.988  1.00 114.48 ? 247  GLU A C   1 
ATOM   1830  O  O   . GLU A 1 247  ? -33.430  52.576  35.468  1.00 115.08 ? 247  GLU A O   1 
ATOM   1831  C  CB  . GLU A 1 247  ? -31.707  54.217  37.304  1.00 154.34 ? 247  GLU A CB  1 
ATOM   1832  C  CG  . GLU A 1 247  ? -30.241  54.160  37.990  1.00 135.60 ? 247  GLU A CG  1 
ATOM   1833  C  CD  . GLU A 1 247  ? -30.104  54.869  39.401  1.00 84.09  ? 247  GLU A CD  1 
ATOM   1834  O  OE1 . GLU A 1 247  ? -30.979  55.710  39.720  1.00 79.89  ? 247  GLU A OE1 1 
ATOM   1835  O  OE2 . GLU A 1 247  ? -29.118  54.621  40.173  1.00 77.74  ? 247  GLU A OE2 1 
ATOM   1836  N  N   . ILE A 1 248  ? -31.939  52.842  33.802  1.00 111.76 ? 248  ILE A N   1 
ATOM   1837  C  CA  . ILE A 1 248  ? -32.396  51.685  33.023  1.00 106.42 ? 248  ILE A CA  1 
ATOM   1838  C  C   . ILE A 1 248  ? -31.594  50.470  33.418  1.00 104.05 ? 248  ILE A C   1 
ATOM   1839  O  O   . ILE A 1 248  ? -30.396  50.423  33.157  1.00 105.52 ? 248  ILE A O   1 
ATOM   1840  C  CB  . ILE A 1 248  ? -32.132  51.858  31.507  1.00 105.59 ? 248  ILE A CB  1 
ATOM   1841  C  CG1 . ILE A 1 248  ? -32.651  53.188  30.976  1.00 104.33 ? 248  ILE A CG1 1 
ATOM   1842  C  CG2 . ILE A 1 248  ? -32.777  50.736  30.720  1.00 106.06 ? 248  ILE A CG2 1 
ATOM   1843  C  CD1 . ILE A 1 248  ? -32.684  53.246  29.478  1.00 104.76 ? 248  ILE A CD1 1 
ATOM   1844  N  N   . THR A 1 249  ? -32.238  49.487  34.040  1.00 101.88 ? 249  THR A N   1 
ATOM   1845  C  CA  . THR A 1 249  ? -31.530  48.289  34.516  1.00 102.94 ? 249  THR A CA  1 
ATOM   1846  C  C   . THR A 1 249  ? -31.759  47.062  33.619  1.00 106.14 ? 249  THR A C   1 
ATOM   1847  O  O   . THR A 1 249  ? -32.893  46.581  33.505  1.00 105.49 ? 249  THR A O   1 
ATOM   1848  C  CB  . THR A 1 249  ? -31.994  47.878  35.939  1.00 109.46 ? 249  THR A CB  1 
ATOM   1849  O  OG1 . THR A 1 249  ? -32.591  48.995  36.620  1.00 108.65 ? 249  THR A OG1 1 
ATOM   1850  C  CG2 . THR A 1 249  ? -30.832  47.269  36.745  1.00 109.08 ? 249  THR A CG2 1 
ATOM   1851  N  N   . ILE A 1 250  ? -30.704  46.523  33.011  1.00 109.23 ? 250  ILE A N   1 
ATOM   1852  C  CA  . ILE A 1 250  ? -30.865  45.325  32.187  1.00 111.90 ? 250  ILE A CA  1 
ATOM   1853  C  C   . ILE A 1 250  ? -30.301  44.079  32.877  1.00 116.07 ? 250  ILE A C   1 
ATOM   1854  O  O   . ILE A 1 250  ? -29.270  44.154  33.525  1.00 115.57 ? 250  ILE A O   1 
ATOM   1855  C  CB  . ILE A 1 250  ? -30.244  45.538  30.835  1.00 111.37 ? 250  ILE A CB  1 
ATOM   1856  C  CG1 . ILE A 1 250  ? -28.749  45.438  30.936  1.00 113.83 ? 250  ILE A CG1 1 
ATOM   1857  C  CG2 . ILE A 1 250  ? -30.504  46.934  30.375  1.00 108.72 ? 250  ILE A CG2 1 
ATOM   1858  C  CD1 . ILE A 1 250  ? -28.083  45.885  29.690  1.00 115.78 ? 250  ILE A CD1 1 
ATOM   1859  N  N   . LYS A 1 251  ? -30.972  42.936  32.739  1.00 121.74 ? 251  LYS A N   1 
ATOM   1860  C  CA  . LYS A 1 251  ? -30.618  41.744  33.525  1.00 129.46 ? 251  LYS A CA  1 
ATOM   1861  C  C   . LYS A 1 251  ? -30.605  40.429  32.710  1.00 137.99 ? 251  LYS A C   1 
ATOM   1862  O  O   . LYS A 1 251  ? -31.653  39.915  32.307  1.00 139.02 ? 251  LYS A O   1 
ATOM   1863  C  CB  . LYS A 1 251  ? -31.560  41.600  34.731  1.00 130.51 ? 251  LYS A CB  1 
ATOM   1864  C  CG  . LYS A 1 251  ? -31.745  42.874  35.560  1.00 130.58 ? 251  LYS A CG  1 
ATOM   1865  C  CD  . LYS A 1 251  ? -32.429  42.610  36.919  1.00 131.80 ? 251  LYS A CD  1 
ATOM   1866  C  CE  . LYS A 1 251  ? -33.904  42.287  36.773  1.00 132.37 ? 251  LYS A CE  1 
ATOM   1867  N  NZ  . LYS A 1 251  ? -34.656  42.338  38.060  1.00 131.48 ? 251  LYS A NZ  1 
ATOM   1868  N  N   . ALA A 1 252  ? -29.406  39.881  32.510  1.00 142.64 ? 252  ALA A N   1 
ATOM   1869  C  CA  . ALA A 1 252  ? -29.182  38.746  31.610  1.00 146.56 ? 252  ALA A CA  1 
ATOM   1870  C  C   . ALA A 1 252  ? -28.950  37.416  32.326  1.00 147.90 ? 252  ALA A C   1 
ATOM   1871  O  O   . ALA A 1 252  ? -28.252  37.360  33.320  1.00 148.37 ? 252  ALA A O   1 
ATOM   1872  C  CB  . ALA A 1 252  ? -28.015  39.051  30.679  1.00 147.57 ? 252  ALA A CB  1 
ATOM   1873  N  N   . ARG A 1 253  ? -29.497  36.338  31.779  1.00 149.68 ? 253  ARG A N   1 
ATOM   1874  C  CA  . ARG A 1 253  ? -29.487  35.057  32.463  1.00 152.28 ? 253  ARG A CA  1 
ATOM   1875  C  C   . ARG A 1 253  ? -29.884  33.889  31.553  1.00 148.63 ? 253  ARG A C   1 
ATOM   1876  O  O   . ARG A 1 253  ? -30.829  33.997  30.772  1.00 149.74 ? 253  ARG A O   1 
ATOM   1877  C  CB  . ARG A 1 253  ? -30.489  35.130  33.592  1.00 158.19 ? 253  ARG A CB  1 
ATOM   1878  C  CG  . ARG A 1 253  ? -31.898  35.348  33.094  1.00 165.98 ? 253  ARG A CG  1 
ATOM   1879  C  CD  . ARG A 1 253  ? -32.882  34.758  34.068  1.00 174.47 ? 253  ARG A CD  1 
ATOM   1880  N  NE  . ARG A 1 253  ? -32.426  33.462  34.578  1.00 182.85 ? 253  ARG A NE  1 
ATOM   1881  C  CZ  . ARG A 1 253  ? -31.715  33.294  35.697  1.00 187.06 ? 253  ARG A CZ  1 
ATOM   1882  N  NH1 . ARG A 1 253  ? -31.361  34.338  36.435  1.00 186.66 ? 253  ARG A NH1 1 
ATOM   1883  N  NH2 . ARG A 1 253  ? -31.350  32.080  36.084  1.00 189.99 ? 253  ARG A NH2 1 
ATOM   1884  N  N   . TYR A 1 254  ? -29.181  32.765  31.670  1.00 144.14 ? 254  TYR A N   1 
ATOM   1885  C  CA  . TYR A 1 254  ? -29.503  31.579  30.873  1.00 139.00 ? 254  TYR A CA  1 
ATOM   1886  C  C   . TYR A 1 254  ? -30.712  30.836  31.419  1.00 134.78 ? 254  TYR A C   1 
ATOM   1887  O  O   . TYR A 1 254  ? -31.126  31.062  32.535  1.00 131.72 ? 254  TYR A O   1 
ATOM   1888  C  CB  . TYR A 1 254  ? -28.307  30.638  30.767  1.00 139.89 ? 254  TYR A CB  1 
ATOM   1889  C  CG  . TYR A 1 254  ? -27.002  31.325  30.428  1.00 139.40 ? 254  TYR A CG  1 
ATOM   1890  C  CD1 . TYR A 1 254  ? -25.921  31.267  31.286  1.00 140.53 ? 254  TYR A CD1 1 
ATOM   1891  C  CD2 . TYR A 1 254  ? -26.853  32.032  29.259  1.00 139.30 ? 254  TYR A CD2 1 
ATOM   1892  C  CE1 . TYR A 1 254  ? -24.731  31.887  30.981  1.00 140.18 ? 254  TYR A CE1 1 
ATOM   1893  C  CE2 . TYR A 1 254  ? -25.668  32.660  28.947  1.00 139.08 ? 254  TYR A CE2 1 
ATOM   1894  C  CZ  . TYR A 1 254  ? -24.612  32.583  29.810  1.00 139.30 ? 254  TYR A CZ  1 
ATOM   1895  O  OH  . TYR A 1 254  ? -23.431  33.207  29.506  1.00 139.52 ? 254  TYR A OH  1 
ATOM   1896  N  N   . PHE A 1 255  ? -31.287  29.958  30.615  1.00 137.27 ? 255  PHE A N   1 
ATOM   1897  C  CA  . PHE A 1 255  ? -32.547  29.323  30.965  1.00 140.36 ? 255  PHE A CA  1 
ATOM   1898  C  C   . PHE A 1 255  ? -32.324  28.304  32.036  1.00 148.19 ? 255  PHE A C   1 
ATOM   1899  O  O   . PHE A 1 255  ? -33.277  27.782  32.609  1.00 147.37 ? 255  PHE A O   1 
ATOM   1900  C  CB  . PHE A 1 255  ? -33.134  28.617  29.752  1.00 141.24 ? 255  PHE A CB  1 
ATOM   1901  C  CG  . PHE A 1 255  ? -33.679  29.543  28.720  1.00 138.73 ? 255  PHE A CG  1 
ATOM   1902  C  CD1 . PHE A 1 255  ? -35.019  29.509  28.390  1.00 138.54 ? 255  PHE A CD1 1 
ATOM   1903  C  CD2 . PHE A 1 255  ? -32.855  30.455  28.081  1.00 136.63 ? 255  PHE A CD2 1 
ATOM   1904  C  CE1 . PHE A 1 255  ? -35.524  30.362  27.444  1.00 137.75 ? 255  PHE A CE1 1 
ATOM   1905  C  CE2 . PHE A 1 255  ? -33.353  31.318  27.141  1.00 135.36 ? 255  PHE A CE2 1 
ATOM   1906  C  CZ  . PHE A 1 255  ? -34.687  31.271  26.822  1.00 136.36 ? 255  PHE A CZ  1 
ATOM   1907  N  N   . TYR A 1 256  ? -31.054  27.994  32.273  1.00 157.49 ? 256  TYR A N   1 
ATOM   1908  C  CA  . TYR A 1 256  ? -30.679  26.995  33.269  1.00 168.16 ? 256  TYR A CA  1 
ATOM   1909  C  C   . TYR A 1 256  ? -30.478  27.580  34.672  1.00 180.95 ? 256  TYR A C   1 
ATOM   1910  O  O   . TYR A 1 256  ? -29.605  27.138  35.412  1.00 186.43 ? 256  TYR A O   1 
ATOM   1911  C  CB  . TYR A 1 256  ? -29.475  26.137  32.817  1.00 165.92 ? 256  TYR A CB  1 
ATOM   1912  C  CG  . TYR A 1 256  ? -28.305  26.836  32.109  1.00 160.23 ? 256  TYR A CG  1 
ATOM   1913  C  CD1 . TYR A 1 256  ? -27.115  27.114  32.784  1.00 158.33 ? 256  TYR A CD1 1 
ATOM   1914  C  CD2 . TYR A 1 256  ? -28.362  27.152  30.754  1.00 158.55 ? 256  TYR A CD2 1 
ATOM   1915  C  CE1 . TYR A 1 256  ? -26.034  27.720  32.137  1.00 155.59 ? 256  TYR A CE1 1 
ATOM   1916  C  CE2 . TYR A 1 256  ? -27.286  27.756  30.103  1.00 155.89 ? 256  TYR A CE2 1 
ATOM   1917  C  CZ  . TYR A 1 256  ? -26.129  28.037  30.798  1.00 154.00 ? 256  TYR A CZ  1 
ATOM   1918  O  OH  . TYR A 1 256  ? -25.066  28.637  30.155  1.00 151.72 ? 256  TYR A OH  1 
ATOM   1919  N  N   . ASN A 1 257  ? -31.299  28.572  35.021  1.00 185.26 ? 257  ASN A N   1 
ATOM   1920  C  CA  . ASN A 1 257  ? -31.261  29.261  36.324  1.00 190.11 ? 257  ASN A CA  1 
ATOM   1921  C  C   . ASN A 1 257  ? -29.892  29.760  36.796  1.00 185.45 ? 257  ASN A C   1 
ATOM   1922  O  O   . ASN A 1 257  ? -29.560  29.676  37.974  1.00 184.06 ? 257  ASN A O   1 
ATOM   1923  C  CB  . ASN A 1 257  ? -31.974  28.452  37.423  1.00 202.50 ? 257  ASN A CB  1 
ATOM   1924  C  CG  . ASN A 1 257  ? -31.415  27.046  37.586  1.00 215.60 ? 257  ASN A CG  1 
ATOM   1925  O  OD1 . ASN A 1 257  ? -31.615  26.183  36.727  1.00 220.73 ? 257  ASN A OD1 1 
ATOM   1926  N  ND2 . ASN A 1 257  ? -30.735  26.803  38.706  1.00 218.73 ? 257  ASN A ND2 1 
ATOM   1927  N  N   . LYS A 1 258  ? -29.119  30.309  35.870  1.00 181.51 ? 258  LYS A N   1 
ATOM   1928  C  CA  . LYS A 1 258  ? -27.759  30.709  36.165  1.00 180.81 ? 258  LYS A CA  1 
ATOM   1929  C  C   . LYS A 1 258  ? -27.374  31.928  35.360  1.00 172.01 ? 258  LYS A C   1 
ATOM   1930  O  O   . LYS A 1 258  ? -27.143  31.834  34.165  1.00 173.23 ? 258  LYS A O   1 
ATOM   1931  C  CB  . LYS A 1 258  ? -26.798  29.564  35.853  1.00 186.59 ? 258  LYS A CB  1 
ATOM   1932  C  CG  . LYS A 1 258  ? -26.206  28.899  37.085  1.00 191.70 ? 258  LYS A CG  1 
ATOM   1933  C  CD  . LYS A 1 258  ? -25.450  29.940  37.888  1.00 192.92 ? 258  LYS A CD  1 
ATOM   1934  C  CE  . LYS A 1 258  ? -24.880  29.391  39.179  1.00 196.39 ? 258  LYS A CE  1 
ATOM   1935  N  NZ  . LYS A 1 258  ? -24.405  30.510  40.043  1.00 196.27 ? 258  LYS A NZ  1 
ATOM   1936  N  N   . VAL A 1 259  ? -27.275  33.069  36.034  1.00 166.85 ? 259  VAL A N   1 
ATOM   1937  C  CA  . VAL A 1 259  ? -27.112  34.360  35.361  1.00 159.36 ? 259  VAL A CA  1 
ATOM   1938  C  C   . VAL A 1 259  ? -25.895  34.436  34.451  1.00 156.36 ? 259  VAL A C   1 
ATOM   1939  O  O   . VAL A 1 259  ? -24.898  33.755  34.665  1.00 156.33 ? 259  VAL A O   1 
ATOM   1940  C  CB  . VAL A 1 259  ? -27.066  35.553  36.360  1.00 152.13 ? 259  VAL A CB  1 
ATOM   1941  C  CG1 . VAL A 1 259  ? -28.093  35.373  37.477  1.00 151.81 ? 259  VAL A CG1 1 
ATOM   1942  C  CG2 . VAL A 1 259  ? -25.676  35.737  36.923  1.00 152.75 ? 259  VAL A CG2 1 
ATOM   1943  N  N   . VAL A 1 260  ? -26.001  35.264  33.421  1.00 153.19 ? 260  VAL A N   1 
ATOM   1944  C  CA  . VAL A 1 260  ? -24.864  35.587  32.588  1.00 154.11 ? 260  VAL A CA  1 
ATOM   1945  C  C   . VAL A 1 260  ? -23.775  36.110  33.490  1.00 157.08 ? 260  VAL A C   1 
ATOM   1946  O  O   . VAL A 1 260  ? -24.076  36.637  34.551  1.00 155.76 ? 260  VAL A O   1 
ATOM   1947  C  CB  . VAL A 1 260  ? -25.233  36.686  31.610  1.00 151.06 ? 260  VAL A CB  1 
ATOM   1948  C  CG1 . VAL A 1 260  ? -23.994  37.172  30.877  1.00 151.43 ? 260  VAL A CG1 1 
ATOM   1949  C  CG2 . VAL A 1 260  ? -26.283  36.173  30.653  1.00 150.62 ? 260  VAL A CG2 1 
ATOM   1950  N  N   . THR A 1 261  ? -22.514  35.949  33.102  1.00 161.51 ? 261  THR A N   1 
ATOM   1951  C  CA  . THR A 1 261  ? -21.432  36.538  33.881  1.00 165.40 ? 261  THR A CA  1 
ATOM   1952  C  C   . THR A 1 261  ? -20.906  37.794  33.208  1.00 166.78 ? 261  THR A C   1 
ATOM   1953  O  O   . THR A 1 261  ? -21.493  38.860  33.344  1.00 166.93 ? 261  THR A O   1 
ATOM   1954  C  CB  . THR A 1 261  ? -20.293  35.553  34.145  1.00 169.00 ? 261  THR A CB  1 
ATOM   1955  O  OG1 . THR A 1 261  ? -20.755  34.516  35.018  1.00 170.63 ? 261  THR A OG1 1 
ATOM   1956  C  CG2 . THR A 1 261  ? -19.149  36.268  34.815  1.00 170.52 ? 261  THR A CG2 1 
ATOM   1957  N  N   . GLU A 1 262  ? -19.802  37.685  32.485  1.00 170.47 ? 262  GLU A N   1 
ATOM   1958  C  CA  . GLU A 1 262  ? -19.375  38.806  31.676  1.00 174.76 ? 262  GLU A CA  1 
ATOM   1959  C  C   . GLU A 1 262  ? -20.259  38.793  30.442  1.00 173.12 ? 262  GLU A C   1 
ATOM   1960  O  O   . GLU A 1 262  ? -20.724  37.736  30.014  1.00 171.86 ? 262  GLU A O   1 
ATOM   1961  C  CB  . GLU A 1 262  ? -17.901  38.692  31.289  1.00 184.20 ? 262  GLU A CB  1 
ATOM   1962  C  CG  . GLU A 1 262  ? -17.385  39.860  30.449  1.00 192.07 ? 262  GLU A CG  1 
ATOM   1963  C  CD  . GLU A 1 262  ? -15.959  39.646  29.959  1.00 201.61 ? 262  GLU A CD  1 
ATOM   1964  O  OE1 . GLU A 1 262  ? -15.701  39.820  28.746  1.00 205.01 ? 262  GLU A OE1 1 
ATOM   1965  O  OE2 . GLU A 1 262  ? -15.096  39.294  30.789  1.00 205.31 ? 262  GLU A OE2 1 
ATOM   1966  N  N   . ALA A 1 263  ? -20.503  39.972  29.887  1.00 173.94 ? 263  ALA A N   1 
ATOM   1967  C  CA  . ALA A 1 263  ? -21.297  40.096  28.682  1.00 174.25 ? 263  ALA A CA  1 
ATOM   1968  C  C   . ALA A 1 263  ? -21.014  41.449  28.090  1.00 171.65 ? 263  ALA A C   1 
ATOM   1969  O  O   . ALA A 1 263  ? -20.574  42.356  28.787  1.00 172.60 ? 263  ALA A O   1 
ATOM   1970  C  CB  . ALA A 1 263  ? -22.760  39.962  28.997  1.00 174.75 ? 263  ALA A CB  1 
ATOM   1971  N  N   . ASP A 1 264  ? -21.237  41.576  26.791  1.00 168.75 ? 264  ASP A N   1 
ATOM   1972  C  CA  . ASP A 1 264  ? -21.077  42.862  26.134  1.00 168.40 ? 264  ASP A CA  1 
ATOM   1973  C  C   . ASP A 1 264  ? -22.471  43.459  25.855  1.00 166.14 ? 264  ASP A C   1 
ATOM   1974  O  O   . ASP A 1 264  ? -23.271  42.843  25.145  1.00 163.46 ? 264  ASP A O   1 
ATOM   1975  C  CB  . ASP A 1 264  ? -20.247  42.711  24.850  1.00 175.50 ? 264  ASP A CB  1 
ATOM   1976  C  CG  . ASP A 1 264  ? -19.136  43.757  24.739  1.00 183.89 ? 264  ASP A CG  1 
ATOM   1977  O  OD1 . ASP A 1 264  ? -19.275  44.842  25.360  1.00 184.56 ? 264  ASP A OD1 1 
ATOM   1978  O  OD2 . ASP A 1 264  ? -18.114  43.494  24.039  1.00 189.79 ? 264  ASP A OD2 1 
ATOM   1979  N  N   . VAL A 1 265  ? -22.766  44.636  26.434  1.00 165.05 ? 265  VAL A N   1 
ATOM   1980  C  CA  . VAL A 1 265  ? -24.075  45.289  26.273  1.00 160.68 ? 265  VAL A CA  1 
ATOM   1981  C  C   . VAL A 1 265  ? -24.066  46.461  25.325  1.00 162.79 ? 265  VAL A C   1 
ATOM   1982  O  O   . VAL A 1 265  ? -23.227  47.343  25.454  1.00 165.53 ? 265  VAL A O   1 
ATOM   1983  C  CB  . VAL A 1 265  ? -24.609  45.894  27.561  1.00 150.36 ? 265  VAL A CB  1 
ATOM   1984  C  CG1 . VAL A 1 265  ? -25.991  46.413  27.277  1.00 146.26 ? 265  VAL A CG1 1 
ATOM   1985  C  CG2 . VAL A 1 265  ? -24.639  44.884  28.688  1.00 148.03 ? 265  VAL A CG2 1 
ATOM   1986  N  N   . TYR A 1 266  ? -25.045  46.508  24.426  1.00 164.02 ? 266  TYR A N   1 
ATOM   1987  C  CA  . TYR A 1 266  ? -25.152  47.609  23.469  1.00 166.88 ? 266  TYR A CA  1 
ATOM   1988  C  C   . TYR A 1 266  ? -26.547  48.232  23.386  1.00 161.19 ? 266  TYR A C   1 
ATOM   1989  O  O   . TYR A 1 266  ? -27.418  47.740  22.649  1.00 160.77 ? 266  TYR A O   1 
ATOM   1990  C  CB  . TYR A 1 266  ? -24.748  47.152  22.074  1.00 176.77 ? 266  TYR A CB  1 
ATOM   1991  C  CG  . TYR A 1 266  ? -23.269  46.971  21.882  1.00 188.03 ? 266  TYR A CG  1 
ATOM   1992  C  CD1 . TYR A 1 266  ? -22.577  45.984  22.572  1.00 193.50 ? 266  TYR A CD1 1 
ATOM   1993  C  CD2 . TYR A 1 266  ? -22.566  47.763  20.986  1.00 195.58 ? 266  TYR A CD2 1 
ATOM   1994  C  CE1 . TYR A 1 266  ? -21.219  45.796  22.385  1.00 198.94 ? 266  TYR A CE1 1 
ATOM   1995  C  CE2 . TYR A 1 266  ? -21.206  47.586  20.794  1.00 201.30 ? 266  TYR A CE2 1 
ATOM   1996  C  CZ  . TYR A 1 266  ? -20.537  46.597  21.496  1.00 203.05 ? 266  TYR A CZ  1 
ATOM   1997  O  OH  . TYR A 1 266  ? -19.185  46.408  21.312  1.00 206.29 ? 266  TYR A OH  1 
ATOM   1998  N  N   . ILE A 1 267  ? -26.732  49.343  24.102  1.00 155.49 ? 267  ILE A N   1 
ATOM   1999  C  CA  . ILE A 1 267  ? -28.017  50.025  24.143  1.00 148.63 ? 267  ILE A CA  1 
ATOM   2000  C  C   . ILE A 1 267  ? -28.090  51.304  23.329  1.00 148.70 ? 267  ILE A C   1 
ATOM   2001  O  O   . ILE A 1 267  ? -27.284  52.211  23.518  1.00 151.75 ? 267  ILE A O   1 
ATOM   2002  C  CB  . ILE A 1 267  ? -28.357  50.398  25.540  1.00 139.77 ? 267  ILE A CB  1 
ATOM   2003  C  CG1 . ILE A 1 267  ? -28.226  49.181  26.435  1.00 136.48 ? 267  ILE A CG1 1 
ATOM   2004  C  CG2 . ILE A 1 267  ? -29.758  50.921  25.574  1.00 139.09 ? 267  ILE A CG2 1 
ATOM   2005  C  CD1 . ILE A 1 267  ? -28.319  49.515  27.893  1.00 132.74 ? 267  ILE A CD1 1 
ATOM   2006  N  N   . THR A 1 268  ? -29.081  51.377  22.446  1.00 147.02 ? 268  THR A N   1 
ATOM   2007  C  CA  . THR A 1 268  ? -29.249  52.521  21.564  1.00 146.88 ? 268  THR A CA  1 
ATOM   2008  C  C   . THR A 1 268  ? -30.655  53.044  21.741  1.00 146.40 ? 268  THR A C   1 
ATOM   2009  O  O   . THR A 1 268  ? -31.596  52.257  21.767  1.00 146.19 ? 268  THR A O   1 
ATOM   2010  C  CB  . THR A 1 268  ? -29.132  52.108  20.097  1.00 151.71 ? 268  THR A CB  1 
ATOM   2011  O  OG1 . THR A 1 268  ? -29.934  50.941  19.878  1.00 152.23 ? 268  THR A OG1 1 
ATOM   2012  C  CG2 . THR A 1 268  ? -27.687  51.807  19.731  1.00 153.85 ? 268  THR A CG2 1 
ATOM   2013  N  N   . PHE A 1 269  ? -30.803  54.365  21.842  1.00 144.11 ? 269  PHE A N   1 
ATOM   2014  C  CA  . PHE A 1 269  ? -32.109  54.991  22.071  1.00 138.96 ? 269  PHE A CA  1 
ATOM   2015  C  C   . PHE A 1 269  ? -32.692  55.649  20.860  1.00 133.03 ? 269  PHE A C   1 
ATOM   2016  O  O   . PHE A 1 269  ? -32.067  55.698  19.802  1.00 135.96 ? 269  PHE A O   1 
ATOM   2017  C  CB  . PHE A 1 269  ? -31.990  56.043  23.140  1.00 139.11 ? 269  PHE A CB  1 
ATOM   2018  C  CG  . PHE A 1 269  ? -31.312  55.560  24.349  1.00 138.30 ? 269  PHE A CG  1 
ATOM   2019  C  CD1 . PHE A 1 269  ? -30.042  55.983  24.649  1.00 138.96 ? 269  PHE A CD1 1 
ATOM   2020  C  CD2 . PHE A 1 269  ? -31.936  54.649  25.169  1.00 136.20 ? 269  PHE A CD2 1 
ATOM   2021  C  CE1 . PHE A 1 269  ? -29.420  55.530  25.764  1.00 138.56 ? 269  PHE A CE1 1 
ATOM   2022  C  CE2 . PHE A 1 269  ? -31.324  54.192  26.281  1.00 135.53 ? 269  PHE A CE2 1 
ATOM   2023  C  CZ  . PHE A 1 269  ? -30.062  54.628  26.586  1.00 136.94 ? 269  PHE A CZ  1 
ATOM   2024  N  N   . GLY A 1 270  ? -33.889  56.187  21.030  1.00 125.14 ? 270  GLY A N   1 
ATOM   2025  C  CA  . GLY A 1 270  ? -34.553  56.857  19.929  1.00 124.30 ? 270  GLY A CA  1 
ATOM   2026  C  C   . GLY A 1 270  ? -35.923  57.405  20.273  1.00 118.85 ? 270  GLY A C   1 
ATOM   2027  O  O   . GLY A 1 270  ? -36.581  56.889  21.177  1.00 119.91 ? 270  GLY A O   1 
ATOM   2028  N  N   . ILE A 1 271  ? -36.347  58.444  19.553  1.00 112.97 ? 271  ILE A N   1 
ATOM   2029  C  CA  . ILE A 1 271  ? -37.633  59.080  19.795  1.00 104.47 ? 271  ILE A CA  1 
ATOM   2030  C  C   . ILE A 1 271  ? -38.702  58.317  19.087  1.00 106.94 ? 271  ILE A C   1 
ATOM   2031  O  O   . ILE A 1 271  ? -38.427  57.266  18.553  1.00 108.87 ? 271  ILE A O   1 
ATOM   2032  C  CB  . ILE A 1 271  ? -37.638  60.471  19.299  1.00 99.34  ? 271  ILE A CB  1 
ATOM   2033  C  CG1 . ILE A 1 271  ? -36.304  61.102  19.658  1.00 96.90  ? 271  ILE A CG1 1 
ATOM   2034  C  CG2 . ILE A 1 271  ? -38.784  61.224  19.937  1.00 98.21  ? 271  ILE A CG2 1 
ATOM   2035  C  CD1 . ILE A 1 271  ? -36.006  61.073  21.146  1.00 91.94  ? 271  ILE A CD1 1 
ATOM   2036  N  N   . ARG A 1 272  ? -39.925  58.823  19.081  1.00 111.11 ? 272  ARG A N   1 
ATOM   2037  C  CA  . ARG A 1 272  ? -41.023  58.053  18.508  1.00 119.31 ? 272  ARG A CA  1 
ATOM   2038  C  C   . ARG A 1 272  ? -42.332  58.801  18.548  1.00 127.08 ? 272  ARG A C   1 
ATOM   2039  O  O   . ARG A 1 272  ? -42.738  59.270  19.600  1.00 125.70 ? 272  ARG A O   1 
ATOM   2040  C  CB  . ARG A 1 272  ? -41.177  56.745  19.278  1.00 115.98 ? 272  ARG A CB  1 
ATOM   2041  C  CG  . ARG A 1 272  ? -42.110  55.735  18.662  1.00 116.07 ? 272  ARG A CG  1 
ATOM   2042  C  CD  . ARG A 1 272  ? -41.605  54.359  19.013  1.00 114.02 ? 272  ARG A CD  1 
ATOM   2043  N  NE  . ARG A 1 272  ? -42.620  53.331  18.864  1.00 115.25 ? 272  ARG A NE  1 
ATOM   2044  C  CZ  . ARG A 1 272  ? -42.332  52.043  18.727  1.00 116.82 ? 272  ARG A CZ  1 
ATOM   2045  N  NH1 . ARG A 1 272  ? -41.061  51.656  18.704  1.00 116.80 ? 272  ARG A NH1 1 
ATOM   2046  N  NH2 . ARG A 1 272  ? -43.303  51.146  18.603  1.00 117.89 ? 272  ARG A NH2 1 
ATOM   2047  N  N   . GLU A 1 273  ? -42.998  58.898  17.405  1.00 137.17 ? 273  GLU A N   1 
ATOM   2048  C  CA  . GLU A 1 273  ? -44.287  59.565  17.365  1.00 144.04 ? 273  GLU A CA  1 
ATOM   2049  C  C   . GLU A 1 273  ? -45.308  58.800  18.206  1.00 143.40 ? 273  GLU A C   1 
ATOM   2050  O  O   . GLU A 1 273  ? -45.994  59.378  19.046  1.00 142.15 ? 273  GLU A O   1 
ATOM   2051  C  CB  . GLU A 1 273  ? -44.785  59.718  15.920  1.00 154.61 ? 273  GLU A CB  1 
ATOM   2052  C  CG  . GLU A 1 273  ? -44.456  61.061  15.275  1.00 160.75 ? 273  GLU A CG  1 
ATOM   2053  C  CD  . GLU A 1 273  ? -44.568  62.222  16.257  1.00 161.64 ? 273  GLU A CD  1 
ATOM   2054  O  OE1 . GLU A 1 273  ? -45.649  62.415  16.877  1.00 160.74 ? 273  GLU A OE1 1 
ATOM   2055  O  OE2 . GLU A 1 273  ? -43.556  62.941  16.408  1.00 162.71 ? 273  GLU A OE2 1 
ATOM   2056  N  N   . ASP A 1 274  ? -45.389  57.493  17.987  1.00 144.76 ? 274  ASP A N   1 
ATOM   2057  C  CA  . ASP A 1 274  ? -46.433  56.674  18.599  1.00 143.88 ? 274  ASP A CA  1 
ATOM   2058  C  C   . ASP A 1 274  ? -46.056  55.204  18.670  1.00 145.76 ? 274  ASP A C   1 
ATOM   2059  O  O   . ASP A 1 274  ? -44.900  54.829  18.469  1.00 144.12 ? 274  ASP A O   1 
ATOM   2060  C  CB  . ASP A 1 274  ? -47.785  56.837  17.868  1.00 147.32 ? 274  ASP A CB  1 
ATOM   2061  C  CG  . ASP A 1 274  ? -47.706  56.575  16.331  1.00 181.91 ? 274  ASP A CG  1 
ATOM   2062  O  OD1 . ASP A 1 274  ? -48.554  55.807  15.803  1.00 184.00 ? 274  ASP A OD1 1 
ATOM   2063  O  OD2 . ASP A 1 274  ? -46.829  57.152  15.637  1.00 183.03 ? 274  ASP A OD2 1 
ATOM   2064  N  N   . LEU A 1 275  ? -47.040  54.368  18.963  1.00 147.75 ? 275  LEU A N   1 
ATOM   2065  C  CA  . LEU A 1 275  ? -46.803  52.932  18.946  1.00 151.84 ? 275  LEU A CA  1 
ATOM   2066  C  C   . LEU A 1 275  ? -47.493  52.190  17.777  1.00 162.85 ? 275  LEU A C   1 
ATOM   2067  O  O   . LEU A 1 275  ? -47.665  50.973  17.831  1.00 163.93 ? 275  LEU A O   1 
ATOM   2068  C  CB  . LEU A 1 275  ? -47.124  52.309  20.310  1.00 145.34 ? 275  LEU A CB  1 
ATOM   2069  C  CG  . LEU A 1 275  ? -46.212  52.809  21.431  1.00 138.62 ? 275  LEU A CG  1 
ATOM   2070  C  CD1 . LEU A 1 275  ? -46.728  52.315  22.751  1.00 136.10 ? 275  LEU A CD1 1 
ATOM   2071  C  CD2 . LEU A 1 275  ? -44.777  52.370  21.222  1.00 137.04 ? 275  LEU A CD2 1 
ATOM   2072  N  N   . LYS A 1 276  ? -47.899  52.922  16.736  1.00 170.20 ? 276  LYS A N   1 
ATOM   2073  C  CA  . LYS A 1 276  ? -48.301  52.314  15.461  1.00 178.84 ? 276  LYS A CA  1 
ATOM   2074  C  C   . LYS A 1 276  ? -47.277  52.692  14.388  1.00 189.55 ? 276  LYS A C   1 
ATOM   2075  O  O   . LYS A 1 276  ? -47.468  52.446  13.200  1.00 196.25 ? 276  LYS A O   1 
ATOM   2076  C  CB  . LYS A 1 276  ? -49.718  52.746  15.050  1.00 174.89 ? 276  LYS A CB  1 
ATOM   2077  C  CG  . LYS A 1 276  ? -50.241  52.081  13.767  1.00 173.29 ? 276  LYS A CG  1 
ATOM   2078  C  CD  . LYS A 1 276  ? -51.705  52.437  13.463  1.00 169.12 ? 276  LYS A CD  1 
ATOM   2079  C  CE  . LYS A 1 276  ? -51.882  53.867  12.955  1.00 163.76 ? 276  LYS A CE  1 
ATOM   2080  N  NZ  . LYS A 1 276  ? -51.612  53.987  11.507  1.00 165.05 ? 276  LYS A NZ  1 
ATOM   2081  N  N   . ASP A 1 277  ? -46.188  53.307  14.839  1.00 194.00 ? 277  ASP A N   1 
ATOM   2082  C  CA  . ASP A 1 277  ? -45.117  53.802  13.975  1.00 203.86 ? 277  ASP A CA  1 
ATOM   2083  C  C   . ASP A 1 277  ? -43.969  52.795  13.951  1.00 206.65 ? 277  ASP A C   1 
ATOM   2084  O  O   . ASP A 1 277  ? -43.209  52.682  14.912  1.00 205.16 ? 277  ASP A O   1 
ATOM   2085  C  CB  . ASP A 1 277  ? -44.639  55.177  14.489  1.00 208.27 ? 277  ASP A CB  1 
ATOM   2086  C  CG  . ASP A 1 277  ? -43.506  55.783  13.661  1.00 217.56 ? 277  ASP A CG  1 
ATOM   2087  O  OD1 . ASP A 1 277  ? -43.163  55.243  12.587  1.00 223.80 ? 277  ASP A OD1 1 
ATOM   2088  O  OD2 . ASP A 1 277  ? -42.955  56.819  14.103  1.00 217.94 ? 277  ASP A OD2 1 
ATOM   2089  N  N   . ASP A 1 278  ? -43.859  52.058  12.848  1.00 211.09 ? 278  ASP A N   1 
ATOM   2090  C  CA  . ASP A 1 278  ? -42.784  51.084  12.666  1.00 210.27 ? 278  ASP A CA  1 
ATOM   2091  C  C   . ASP A 1 278  ? -41.413  51.751  12.694  1.00 205.80 ? 278  ASP A C   1 
ATOM   2092  O  O   . ASP A 1 278  ? -40.394  51.076  12.840  1.00 205.11 ? 278  ASP A O   1 
ATOM   2093  C  CB  . ASP A 1 278  ? -42.973  50.251  11.372  1.00 246.26 ? 278  ASP A CB  1 
ATOM   2094  C  CG  . ASP A 1 278  ? -43.434  51.088  10.153  1.00 247.58 ? 278  ASP A CG  1 
ATOM   2095  O  OD1 . ASP A 1 278  ? -43.278  52.329  10.151  1.00 245.32 ? 278  ASP A OD1 1 
ATOM   2096  O  OD2 . ASP A 1 278  ? -43.950  50.488  9.180   1.00 250.37 ? 278  ASP A OD2 1 
ATOM   2097  N  N   . GLN A 1 279  ? -41.404  53.080  12.582  1.00 202.73 ? 279  GLN A N   1 
ATOM   2098  C  CA  . GLN A 1 279  ? -40.164  53.836  12.442  1.00 197.59 ? 279  GLN A CA  1 
ATOM   2099  C  C   . GLN A 1 279  ? -39.985  54.914  13.482  1.00 185.58 ? 279  GLN A C   1 
ATOM   2100  O  O   . GLN A 1 279  ? -40.928  55.553  13.928  1.00 180.86 ? 279  GLN A O   1 
ATOM   2101  C  CB  . GLN A 1 279  ? -40.052  54.487  11.065  1.00 206.30 ? 279  GLN A CB  1 
ATOM   2102  C  CG  . GLN A 1 279  ? -38.711  55.191  10.852  1.00 209.99 ? 279  GLN A CG  1 
ATOM   2103  C  CD  . GLN A 1 279  ? -37.521  54.234  10.936  1.00 212.55 ? 279  GLN A CD  1 
ATOM   2104  O  OE1 . GLN A 1 279  ? -36.670  54.355  11.820  1.00 210.65 ? 279  GLN A OE1 1 
ATOM   2105  N  NE2 . GLN A 1 279  ? -37.463  53.276  10.013  1.00 216.78 ? 279  GLN A NE2 1 
ATOM   2106  N  N   . LYS A 1 280  ? -38.734  55.134  13.829  1.00 179.12 ? 280  LYS A N   1 
ATOM   2107  C  CA  . LYS A 1 280  ? -38.413  56.016  14.911  1.00 171.14 ? 280  LYS A CA  1 
ATOM   2108  C  C   . LYS A 1 280  ? -36.980  56.498  14.752  1.00 171.19 ? 280  LYS A C   1 
ATOM   2109  O  O   . LYS A 1 280  ? -36.057  55.708  14.588  1.00 174.02 ? 280  LYS A O   1 
ATOM   2110  C  CB  . LYS A 1 280  ? -38.625  55.292  16.249  1.00 163.41 ? 280  LYS A CB  1 
ATOM   2111  C  CG  . LYS A 1 280  ? -37.855  53.981  16.433  1.00 158.46 ? 280  LYS A CG  1 
ATOM   2112  C  CD  . LYS A 1 280  ? -38.690  52.721  16.182  1.00 156.75 ? 280  LYS A CD  1 
ATOM   2113  C  CE  . LYS A 1 280  ? -37.817  51.457  16.323  1.00 155.01 ? 280  LYS A CE  1 
ATOM   2114  N  NZ  . LYS A 1 280  ? -38.523  50.145  16.152  1.00 155.19 ? 280  LYS A NZ  1 
ATOM   2115  N  N   . GLU A 1 281  ? -36.805  57.809  14.790  1.00 168.41 ? 281  GLU A N   1 
ATOM   2116  C  CA  . GLU A 1 281  ? -35.505  58.413  14.577  1.00 170.20 ? 281  GLU A CA  1 
ATOM   2117  C  C   . GLU A 1 281  ? -34.541  58.103  15.707  1.00 161.59 ? 281  GLU A C   1 
ATOM   2118  O  O   . GLU A 1 281  ? -34.550  58.777  16.727  1.00 156.71 ? 281  GLU A O   1 
ATOM   2119  C  CB  . GLU A 1 281  ? -35.675  59.924  14.444  1.00 179.12 ? 281  GLU A CB  1 
ATOM   2120  C  CG  . GLU A 1 281  ? -36.820  60.339  13.515  1.00 192.23 ? 281  GLU A CG  1 
ATOM   2121  C  CD  . GLU A 1 281  ? -36.789  59.633  12.148  1.00 206.57 ? 281  GLU A CD  1 
ATOM   2122  O  OE1 . GLU A 1 281  ? -35.799  58.923  11.832  1.00 211.15 ? 281  GLU A OE1 1 
ATOM   2123  O  OE2 . GLU A 1 281  ? -37.770  59.791  11.383  1.00 212.25 ? 281  GLU A OE2 1 
ATOM   2124  N  N   . MET A 1 282  ? -33.691  57.102  15.525  1.00 162.03 ? 282  MET A N   1 
ATOM   2125  C  CA  . MET A 1 282  ? -32.698  56.791  16.540  1.00 160.59 ? 282  MET A CA  1 
ATOM   2126  C  C   . MET A 1 282  ? -31.868  58.013  16.856  1.00 162.17 ? 282  MET A C   1 
ATOM   2127  O  O   . MET A 1 282  ? -32.160  59.103  16.397  1.00 163.76 ? 282  MET A O   1 
ATOM   2128  C  CB  . MET A 1 282  ? -31.777  55.677  16.083  1.00 162.14 ? 282  MET A CB  1 
ATOM   2129  C  CG  . MET A 1 282  ? -32.424  54.315  15.970  1.00 162.23 ? 282  MET A CG  1 
ATOM   2130  S  SD  . MET A 1 282  ? -33.186  53.785  17.507  1.00 165.14 ? 282  MET A SD  1 
ATOM   2131  C  CE  . MET A 1 282  ? -34.819  54.473  17.258  1.00 120.62 ? 282  MET A CE  1 
ATOM   2132  N  N   . MET A 1 283  ? -30.825  57.833  17.646  1.00 164.86 ? 283  MET A N   1 
ATOM   2133  C  CA  . MET A 1 283  ? -30.041  58.972  18.085  1.00 171.34 ? 283  MET A CA  1 
ATOM   2134  C  C   . MET A 1 283  ? -28.610  58.523  18.336  1.00 182.84 ? 283  MET A C   1 
ATOM   2135  O  O   . MET A 1 283  ? -28.376  57.556  19.062  1.00 182.40 ? 283  MET A O   1 
ATOM   2136  C  CB  . MET A 1 283  ? -30.629  59.579  19.373  1.00 167.30 ? 283  MET A CB  1 
ATOM   2137  C  CG  . MET A 1 283  ? -32.091  60.090  19.298  1.00 179.73 ? 283  MET A CG  1 
ATOM   2138  S  SD  . MET A 1 283  ? -32.862  60.489  20.922  1.00 115.05 ? 283  MET A SD  1 
ATOM   2139  C  CE  . MET A 1 283  ? -32.872  58.879  21.709  1.00 109.41 ? 283  MET A CE  1 
ATOM   2140  N  N   . GLN A 1 284  ? -27.658  59.230  17.735  1.00 193.70 ? 284  GLN A N   1 
ATOM   2141  C  CA  . GLN A 1 284  ? -26.236  58.981  17.939  1.00 202.20 ? 284  GLN A CA  1 
ATOM   2142  C  C   . GLN A 1 284  ? -25.869  59.001  19.410  1.00 204.65 ? 284  GLN A C   1 
ATOM   2143  O  O   . GLN A 1 284  ? -26.697  59.309  20.274  1.00 203.52 ? 284  GLN A O   1 
ATOM   2144  C  CB  . GLN A 1 284  ? -25.424  60.065  17.246  1.00 206.21 ? 284  GLN A CB  1 
ATOM   2145  C  CG  . GLN A 1 284  ? -25.666  61.456  17.815  1.00 205.00 ? 284  GLN A CG  1 
ATOM   2146  C  CD  . GLN A 1 284  ? -26.990  62.046  17.363  1.00 204.01 ? 284  GLN A CD  1 
ATOM   2147  O  OE1 . GLN A 1 284  ? -28.059  61.543  17.696  1.00 201.40 ? 284  GLN A OE1 1 
ATOM   2148  N  NE2 . GLN A 1 284  ? -26.920  63.127  16.605  1.00 206.53 ? 284  GLN A NE2 1 
ATOM   2149  N  N   . THR A 1 285  ? -24.611  58.694  19.692  1.00 207.79 ? 285  THR A N   1 
ATOM   2150  C  CA  . THR A 1 285  ? -24.128  58.778  21.054  1.00 208.24 ? 285  THR A CA  1 
ATOM   2151  C  C   . THR A 1 285  ? -25.164  58.115  21.969  1.00 203.79 ? 285  THR A C   1 
ATOM   2152  O  O   . THR A 1 285  ? -25.651  58.707  22.940  1.00 200.81 ? 285  THR A O   1 
ATOM   2153  C  CB  . THR A 1 285  ? -23.863  60.242  21.451  1.00 211.68 ? 285  THR A CB  1 
ATOM   2154  O  OG1 . THR A 1 285  ? -23.386  60.961  20.304  1.00 215.78 ? 285  THR A OG1 1 
ATOM   2155  C  CG2 . THR A 1 285  ? -22.828  60.322  22.563  1.00 213.37 ? 285  THR A CG2 1 
ATOM   2156  N  N   . ALA A 1 286  ? -25.539  56.896  21.589  1.00 202.39 ? 286  ALA A N   1 
ATOM   2157  C  CA  . ALA A 1 286  ? -26.299  56.000  22.448  1.00 197.35 ? 286  ALA A CA  1 
ATOM   2158  C  C   . ALA A 1 286  ? -25.327  55.044  23.139  1.00 194.58 ? 286  ALA A C   1 
ATOM   2159  O  O   . ALA A 1 286  ? -24.793  54.119  22.521  1.00 193.14 ? 286  ALA A O   1 
ATOM   2160  C  CB  . ALA A 1 286  ? -27.319  55.231  21.641  1.00 197.27 ? 286  ALA A CB  1 
ATOM   2161  N  N   . MET A 1 287  ? -25.115  55.284  24.429  1.00 193.18 ? 287  MET A N   1 
ATOM   2162  C  CA  . MET A 1 287  ? -24.094  54.599  25.216  1.00 191.10 ? 287  MET A CA  1 
ATOM   2163  C  C   . MET A 1 287  ? -23.779  53.189  24.777  1.00 192.39 ? 287  MET A C   1 
ATOM   2164  O  O   . MET A 1 287  ? -24.665  52.397  24.460  1.00 190.97 ? 287  MET A O   1 
ATOM   2165  C  CB  . MET A 1 287  ? -24.486  54.565  26.687  1.00 186.16 ? 287  MET A CB  1 
ATOM   2166  C  CG  . MET A 1 287  ? -24.117  55.804  27.450  1.00 184.15 ? 287  MET A CG  1 
ATOM   2167  S  SD  . MET A 1 287  ? -24.723  55.695  29.137  1.00 222.33 ? 287  MET A SD  1 
ATOM   2168  C  CE  . MET A 1 287  ? -26.483  55.820  28.837  1.00 183.25 ? 287  MET A CE  1 
ATOM   2169  N  N   . GLN A 1 288  ? -22.487  52.894  24.779  1.00 196.93 ? 288  GLN A N   1 
ATOM   2170  C  CA  . GLN A 1 288  ? -21.991  51.562  24.484  1.00 202.42 ? 288  GLN A CA  1 
ATOM   2171  C  C   . GLN A 1 288  ? -21.375  50.927  25.723  1.00 202.84 ? 288  GLN A C   1 
ATOM   2172  O  O   . GLN A 1 288  ? -20.858  51.611  26.605  1.00 201.93 ? 288  GLN A O   1 
ATOM   2173  C  CB  . GLN A 1 288  ? -20.982  51.592  23.320  1.00 210.55 ? 288  GLN A CB  1 
ATOM   2174  C  CG  . GLN A 1 288  ? -19.909  52.687  23.419  1.00 217.87 ? 288  GLN A CG  1 
ATOM   2175  C  CD  . GLN A 1 288  ? -19.040  52.824  22.161  1.00 226.59 ? 288  GLN A CD  1 
ATOM   2176  O  OE1 . GLN A 1 288  ? -18.821  51.859  21.423  1.00 229.76 ? 288  GLN A OE1 1 
ATOM   2177  N  NE2 . GLN A 1 288  ? -18.526  54.032  21.930  1.00 230.76 ? 288  GLN A NE2 1 
ATOM   2178  N  N   . ASN A 1 289  ? -21.464  49.609  25.785  1.00 205.37 ? 289  ASN A N   1 
ATOM   2179  C  CA  . ASN A 1 289  ? -20.783  48.836  26.804  1.00 207.94 ? 289  ASN A CA  1 
ATOM   2180  C  C   . ASN A 1 289  ? -20.837  49.435  28.196  1.00 201.53 ? 289  ASN A C   1 
ATOM   2181  O  O   . ASN A 1 289  ? -20.177  50.426  28.494  1.00 198.90 ? 289  ASN A O   1 
ATOM   2182  C  CB  . ASN A 1 289  ? -19.309  48.633  26.428  1.00 217.86 ? 289  ASN A CB  1 
ATOM   2183  C  CG  . ASN A 1 289  ? -19.109  48.315  24.955  1.00 224.90 ? 289  ASN A CG  1 
ATOM   2184  O  OD1 . ASN A 1 289  ? -20.063  48.020  24.236  1.00 226.52 ? 289  ASN A OD1 1 
ATOM   2185  N  ND2 . ASN A 1 289  ? -17.858  48.377  24.498  1.00 228.50 ? 289  ASN A ND2 1 
ATOM   2186  N  N   . THR A 1 290  ? -21.642  48.827  29.045  1.00 197.64 ? 290  THR A N   1 
ATOM   2187  C  CA  . THR A 1 290  ? -21.373  48.850  30.468  1.00 194.99 ? 290  THR A CA  1 
ATOM   2188  C  C   . THR A 1 290  ? -21.424  47.375  30.753  1.00 191.23 ? 290  THR A C   1 
ATOM   2189  O  O   . THR A 1 290  ? -22.228  46.899  31.549  1.00 191.98 ? 290  THR A O   1 
ATOM   2190  C  CB  . THR A 1 290  ? -22.390  49.679  31.308  1.00 162.33 ? 290  THR A CB  1 
ATOM   2191  O  OG1 . THR A 1 290  ? -21.946  51.039  31.373  1.00 162.69 ? 290  THR A OG1 1 
ATOM   2192  C  CG2 . THR A 1 290  ? -22.484  49.167  32.741  1.00 160.83 ? 290  THR A CG2 1 
ATOM   2193  N  N   . MET A 1 291  ? -20.569  46.662  30.025  1.00 186.50 ? 291  MET A N   1 
ATOM   2194  C  CA  . MET A 1 291  ? -20.511  45.213  30.068  1.00 183.00 ? 291  MET A CA  1 
ATOM   2195  C  C   . MET A 1 291  ? -21.348  44.665  31.211  1.00 175.78 ? 291  MET A C   1 
ATOM   2196  O  O   . MET A 1 291  ? -21.078  44.945  32.383  1.00 175.29 ? 291  MET A O   1 
ATOM   2197  C  CB  . MET A 1 291  ? -19.070  44.734  30.260  1.00 187.05 ? 291  MET A CB  1 
ATOM   2198  C  CG  . MET A 1 291  ? -18.036  45.271  29.289  1.00 190.54 ? 291  MET A CG  1 
ATOM   2199  S  SD  . MET A 1 291  ? -16.421  44.572  29.711  1.00 216.68 ? 291  MET A SD  1 
ATOM   2200  C  CE  . MET A 1 291  ? -16.369  44.888  31.471  1.00 212.48 ? 291  MET A CE  1 
ATOM   2201  N  N   . LEU A 1 292  ? -22.365  43.884  30.864  1.00 170.41 ? 292  LEU A N   1 
ATOM   2202  C  CA  . LEU A 1 292  ? -23.157  43.184  31.861  1.00 163.91 ? 292  LEU A CA  1 
ATOM   2203  C  C   . LEU A 1 292  ? -22.179  42.502  32.793  1.00 159.43 ? 292  LEU A C   1 
ATOM   2204  O  O   . LEU A 1 292  ? -21.117  42.058  32.372  1.00 160.95 ? 292  LEU A O   1 
ATOM   2205  C  CB  . LEU A 1 292  ? -24.050  42.141  31.191  1.00 163.97 ? 292  LEU A CB  1 
ATOM   2206  C  CG  . LEU A 1 292  ? -25.309  41.643  31.911  1.00 162.24 ? 292  LEU A CG  1 
ATOM   2207  C  CD1 . LEU A 1 292  ? -24.980  40.863  33.165  1.00 162.16 ? 292  LEU A CD1 1 
ATOM   2208  C  CD2 . LEU A 1 292  ? -26.229  42.800  32.223  1.00 159.34 ? 292  LEU A CD2 1 
ATOM   2209  N  N   . ILE A 1 293  ? -22.534  42.412  34.061  1.00 153.24 ? 293  ILE A N   1 
ATOM   2210  C  CA  . ILE A 1 293  ? -21.610  41.876  35.030  1.00 148.85 ? 293  ILE A CA  1 
ATOM   2211  C  C   . ILE A 1 293  ? -22.389  41.230  36.150  1.00 145.51 ? 293  ILE A C   1 
ATOM   2212  O  O   . ILE A 1 293  ? -23.057  41.897  36.927  1.00 144.20 ? 293  ILE A O   1 
ATOM   2213  C  CB  . ILE A 1 293  ? -20.694  42.985  35.556  1.00 147.46 ? 293  ILE A CB  1 
ATOM   2214  C  CG1 . ILE A 1 293  ? -19.491  43.148  34.619  1.00 146.32 ? 293  ILE A CG1 1 
ATOM   2215  C  CG2 . ILE A 1 293  ? -20.272  42.699  36.984  1.00 148.41 ? 293  ILE A CG2 1 
ATOM   2216  C  CD1 . ILE A 1 293  ? -18.550  44.280  34.987  1.00 145.80 ? 293  ILE A CD1 1 
ATOM   2217  N  N   . ASN A 1 294  ? -22.322  39.909  36.200  1.00 144.92 ? 294  ASN A N   1 
ATOM   2218  C  CA  . ASN A 1 294  ? -23.069  39.143  37.186  1.00 144.74 ? 294  ASN A CA  1 
ATOM   2219  C  C   . ASN A 1 294  ? -24.601  39.267  37.118  1.00 137.30 ? 294  ASN A C   1 
ATOM   2220  O  O   . ASN A 1 294  ? -25.303  39.152  38.127  1.00 135.43 ? 294  ASN A O   1 
ATOM   2221  C  CB  . ASN A 1 294  ? -22.588  39.474  38.584  1.00 151.33 ? 294  ASN A CB  1 
ATOM   2222  C  CG  . ASN A 1 294  ? -23.075  38.477  39.599  1.00 157.57 ? 294  ASN A CG  1 
ATOM   2223  O  OD1 . ASN A 1 294  ? -24.023  38.753  40.341  1.00 158.59 ? 294  ASN A OD1 1 
ATOM   2224  N  ND2 . ASN A 1 294  ? -22.456  37.289  39.619  1.00 160.80 ? 294  ASN A ND2 1 
ATOM   2225  N  N   . GLY A 1 295  ? -25.109  39.484  35.913  1.00 133.39 ? 295  GLY A N   1 
ATOM   2226  C  CA  . GLY A 1 295  ? -26.534  39.393  35.663  1.00 129.90 ? 295  GLY A CA  1 
ATOM   2227  C  C   . GLY A 1 295  ? -27.192  40.741  35.624  1.00 126.19 ? 295  GLY A C   1 
ATOM   2228  O  O   . GLY A 1 295  ? -28.414  40.834  35.490  1.00 123.80 ? 295  GLY A O   1 
ATOM   2229  N  N   . ILE A 1 296  ? -26.368  41.779  35.754  1.00 124.49 ? 296  ILE A N   1 
ATOM   2230  C  CA  . ILE A 1 296  ? -26.841  43.162  35.732  1.00 119.53 ? 296  ILE A CA  1 
ATOM   2231  C  C   . ILE A 1 296  ? -25.853  44.146  35.099  1.00 123.03 ? 296  ILE A C   1 
ATOM   2232  O  O   . ILE A 1 296  ? -24.633  43.943  35.114  1.00 125.01 ? 296  ILE A O   1 
ATOM   2233  C  CB  . ILE A 1 296  ? -27.190  43.701  37.142  1.00 109.24 ? 296  ILE A CB  1 
ATOM   2234  C  CG1 . ILE A 1 296  ? -27.934  42.653  37.965  1.00 106.94 ? 296  ILE A CG1 1 
ATOM   2235  C  CG2 . ILE A 1 296  ? -28.028  44.954  37.017  1.00 102.57 ? 296  ILE A CG2 1 
ATOM   2236  C  CD1 . ILE A 1 296  ? -29.395  42.907  38.065  1.00 104.71 ? 296  ILE A CD1 1 
ATOM   2237  N  N   . ALA A 1 297  ? -26.424  45.194  34.509  1.00 122.24 ? 297  ALA A N   1 
ATOM   2238  C  CA  . ALA A 1 297  ? -25.717  46.411  34.146  1.00 121.31 ? 297  ALA A CA  1 
ATOM   2239  C  C   . ALA A 1 297  ? -26.762  47.506  34.189  1.00 122.18 ? 297  ALA A C   1 
ATOM   2240  O  O   . ALA A 1 297  ? -27.963  47.233  34.239  1.00 122.67 ? 297  ALA A O   1 
ATOM   2241  C  CB  . ALA A 1 297  ? -25.091  46.315  32.784  1.00 120.51 ? 297  ALA A CB  1 
ATOM   2242  N  N   . GLN A 1 298  ? -26.299  48.746  34.181  1.00 122.55 ? 298  GLN A N   1 
ATOM   2243  C  CA  . GLN A 1 298  ? -27.166  49.889  34.390  1.00 121.79 ? 298  GLN A CA  1 
ATOM   2244  C  C   . GLN A 1 298  ? -26.528  51.076  33.693  1.00 119.56 ? 298  GLN A C   1 
ATOM   2245  O  O   . GLN A 1 298  ? -25.317  51.129  33.534  1.00 120.87 ? 298  GLN A O   1 
ATOM   2246  C  CB  . GLN A 1 298  ? -27.310  50.185  35.887  1.00 124.84 ? 298  GLN A CB  1 
ATOM   2247  C  CG  . GLN A 1 298  ? -28.535  49.558  36.556  1.00 129.82 ? 298  GLN A CG  1 
ATOM   2248  C  CD  . GLN A 1 298  ? -29.213  50.500  37.565  1.00 135.37 ? 298  GLN A CD  1 
ATOM   2249  O  OE1 . GLN A 1 298  ? -28.829  51.659  37.701  1.00 138.39 ? 298  GLN A OE1 1 
ATOM   2250  N  NE2 . GLN A 1 298  ? -30.232  50.002  38.262  1.00 136.30 ? 298  GLN A NE2 1 
ATOM   2251  N  N   . VAL A 1 299  ? -27.338  52.012  33.242  1.00 117.46 ? 299  VAL A N   1 
ATOM   2252  C  CA  . VAL A 1 299  ? -26.820  53.306  32.856  1.00 119.69 ? 299  VAL A CA  1 
ATOM   2253  C  C   . VAL A 1 299  ? -27.978  54.224  33.007  1.00 122.16 ? 299  VAL A C   1 
ATOM   2254  O  O   . VAL A 1 299  ? -29.110  53.799  32.809  1.00 126.56 ? 299  VAL A O   1 
ATOM   2255  C  CB  . VAL A 1 299  ? -26.411  53.359  31.407  1.00 120.34 ? 299  VAL A CB  1 
ATOM   2256  C  CG1 . VAL A 1 299  ? -25.010  52.842  31.235  1.00 121.70 ? 299  VAL A CG1 1 
ATOM   2257  C  CG2 . VAL A 1 299  ? -27.419  52.597  30.558  1.00 120.38 ? 299  VAL A CG2 1 
ATOM   2258  N  N   . THR A 1 300  ? -27.706  55.469  33.387  1.00 121.18 ? 300  THR A N   1 
ATOM   2259  C  CA  . THR A 1 300  ? -28.744  56.490  33.424  1.00 119.55 ? 300  THR A CA  1 
ATOM   2260  C  C   . THR A 1 300  ? -28.653  57.300  32.139  1.00 124.43 ? 300  THR A C   1 
ATOM   2261  O  O   . THR A 1 300  ? -27.584  57.413  31.532  1.00 123.75 ? 300  THR A O   1 
ATOM   2262  C  CB  . THR A 1 300  ? -28.712  57.379  34.725  1.00 157.33 ? 300  THR A CB  1 
ATOM   2263  O  OG1 . THR A 1 300  ? -27.364  57.707  35.083  1.00 159.59 ? 300  THR A OG1 1 
ATOM   2264  C  CG2 . THR A 1 300  ? -29.340  56.643  35.894  1.00 156.02 ? 300  THR A CG2 1 
ATOM   2265  N  N   . PHE A 1 301  ? -29.780  57.840  31.709  1.00 129.35 ? 301  PHE A N   1 
ATOM   2266  C  CA  . PHE A 1 301  ? -29.854  58.400  30.371  1.00 138.10 ? 301  PHE A CA  1 
ATOM   2267  C  C   . PHE A 1 301  ? -30.251  59.878  30.468  1.00 146.73 ? 301  PHE A C   1 
ATOM   2268  O  O   . PHE A 1 301  ? -31.396  60.205  30.772  1.00 149.67 ? 301  PHE A O   1 
ATOM   2269  C  CB  . PHE A 1 301  ? -30.844  57.547  29.561  1.00 134.55 ? 301  PHE A CB  1 
ATOM   2270  C  CG  . PHE A 1 301  ? -31.249  58.127  28.242  1.00 130.76 ? 301  PHE A CG  1 
ATOM   2271  C  CD1 . PHE A 1 301  ? -30.320  58.416  27.282  1.00 130.32 ? 301  PHE A CD1 1 
ATOM   2272  C  CD2 . PHE A 1 301  ? -32.593  58.333  27.951  1.00 128.55 ? 301  PHE A CD2 1 
ATOM   2273  C  CE1 . PHE A 1 301  ? -30.720  58.930  26.069  1.00 130.43 ? 301  PHE A CE1 1 
ATOM   2274  C  CE2 . PHE A 1 301  ? -32.998  58.852  26.744  1.00 127.52 ? 301  PHE A CE2 1 
ATOM   2275  C  CZ  . PHE A 1 301  ? -32.059  59.149  25.803  1.00 129.40 ? 301  PHE A CZ  1 
ATOM   2276  N  N   . ASP A 1 302  ? -29.278  60.769  30.258  1.00 151.33 ? 302  ASP A N   1 
ATOM   2277  C  CA  . ASP A 1 302  ? -29.529  62.214  30.264  1.00 153.56 ? 302  ASP A CA  1 
ATOM   2278  C  C   . ASP A 1 302  ? -30.252  62.563  28.967  1.00 151.68 ? 302  ASP A C   1 
ATOM   2279  O  O   . ASP A 1 302  ? -29.635  62.691  27.905  1.00 150.98 ? 302  ASP A O   1 
ATOM   2280  C  CB  . ASP A 1 302  ? -28.214  63.010  30.424  1.00 160.93 ? 302  ASP A CB  1 
ATOM   2281  C  CG  . ASP A 1 302  ? -28.438  64.520  30.676  1.00 168.62 ? 302  ASP A CG  1 
ATOM   2282  O  OD1 . ASP A 1 302  ? -27.533  65.158  31.254  1.00 173.28 ? 302  ASP A OD1 1 
ATOM   2283  O  OD2 . ASP A 1 302  ? -29.490  65.083  30.293  1.00 169.84 ? 302  ASP A OD2 1 
ATOM   2284  N  N   . SER A 1 303  ? -31.570  62.684  29.064  1.00 150.52 ? 303  SER A N   1 
ATOM   2285  C  CA  . SER A 1 303  ? -32.409  62.943  27.911  1.00 149.71 ? 303  SER A CA  1 
ATOM   2286  C  C   . SER A 1 303  ? -32.162  64.338  27.318  1.00 151.92 ? 303  SER A C   1 
ATOM   2287  O  O   . SER A 1 303  ? -32.302  64.550  26.112  1.00 153.88 ? 303  SER A O   1 
ATOM   2288  C  CB  . SER A 1 303  ? -33.874  62.768  28.301  1.00 145.56 ? 303  SER A CB  1 
ATOM   2289  O  OG  . SER A 1 303  ? -34.075  61.528  28.951  1.00 140.94 ? 303  SER A OG  1 
ATOM   2290  N  N   . GLU A 1 304  ? -31.788  65.290  28.167  1.00 149.38 ? 304  GLU A N   1 
ATOM   2291  C  CA  . GLU A 1 304  ? -31.590  66.669  27.726  1.00 147.08 ? 304  GLU A CA  1 
ATOM   2292  C  C   . GLU A 1 304  ? -30.512  66.728  26.657  1.00 145.24 ? 304  GLU A C   1 
ATOM   2293  O  O   . GLU A 1 304  ? -30.760  67.142  25.527  1.00 142.58 ? 304  GLU A O   1 
ATOM   2294  C  CB  . GLU A 1 304  ? -31.188  67.541  28.911  1.00 149.05 ? 304  GLU A CB  1 
ATOM   2295  C  CG  . GLU A 1 304  ? -31.501  69.008  28.729  1.00 152.52 ? 304  GLU A CG  1 
ATOM   2296  C  CD  . GLU A 1 304  ? -30.837  69.833  29.789  1.00 155.91 ? 304  GLU A CD  1 
ATOM   2297  O  OE1 . GLU A 1 304  ? -29.910  69.275  30.424  1.00 157.56 ? 304  GLU A OE1 1 
ATOM   2298  O  OE2 . GLU A 1 304  ? -31.233  71.012  29.980  1.00 156.74 ? 304  GLU A OE2 1 
ATOM   2299  N  N   . THR A 1 305  ? -29.312  66.320  27.049  1.00 145.90 ? 305  THR A N   1 
ATOM   2300  C  CA  . THR A 1 305  ? -28.210  66.103  26.140  1.00 150.38 ? 305  THR A CA  1 
ATOM   2301  C  C   . THR A 1 305  ? -28.696  65.333  24.933  1.00 151.09 ? 305  THR A C   1 
ATOM   2302  O  O   . THR A 1 305  ? -28.770  65.845  23.812  1.00 149.77 ? 305  THR A O   1 
ATOM   2303  C  CB  . THR A 1 305  ? -27.175  65.209  26.837  1.00 148.63 ? 305  THR A CB  1 
ATOM   2304  O  OG1 . THR A 1 305  ? -26.707  65.853  28.029  1.00 149.51 ? 305  THR A OG1 1 
ATOM   2305  C  CG2 . THR A 1 305  ? -26.001  64.883  25.916  1.00 151.37 ? 305  THR A CG2 1 
ATOM   2306  N  N   . ALA A 1 306  ? -29.060  64.091  25.212  1.00 155.58 ? 306  ALA A N   1 
ATOM   2307  C  CA  . ALA A 1 306  ? -29.282  63.064  24.212  1.00 164.88 ? 306  ALA A CA  1 
ATOM   2308  C  C   . ALA A 1 306  ? -30.405  63.305  23.208  1.00 172.46 ? 306  ALA A C   1 
ATOM   2309  O  O   . ALA A 1 306  ? -30.918  62.360  22.617  1.00 173.50 ? 306  ALA A O   1 
ATOM   2310  C  CB  . ALA A 1 306  ? -29.503  61.748  24.912  1.00 161.05 ? 306  ALA A CB  1 
ATOM   2311  N  N   . VAL A 1 307  ? -30.789  64.555  23.002  1.00 186.46 ? 307  VAL A N   1 
ATOM   2312  C  CA  . VAL A 1 307  ? -31.853  64.852  22.048  1.00 200.50 ? 307  VAL A CA  1 
ATOM   2313  C  C   . VAL A 1 307  ? -31.508  66.141  21.328  1.00 221.20 ? 307  VAL A C   1 
ATOM   2314  O  O   . VAL A 1 307  ? -31.626  66.238  20.104  1.00 221.09 ? 307  VAL A O   1 
ATOM   2315  C  CB  . VAL A 1 307  ? -33.255  64.990  22.744  1.00 138.04 ? 307  VAL A CB  1 
ATOM   2316  C  CG1 . VAL A 1 307  ? -34.253  65.619  21.825  1.00 138.93 ? 307  VAL A CG1 1 
ATOM   2317  C  CG2 . VAL A 1 307  ? -33.784  63.644  23.179  1.00 136.14 ? 307  VAL A CG2 1 
ATOM   2318  N  N   . LYS A 1 308  ? -31.046  67.115  22.103  1.00 238.17 ? 308  LYS A N   1 
ATOM   2319  C  CA  . LYS A 1 308  ? -30.843  68.460  21.594  1.00 259.14 ? 308  LYS A CA  1 
ATOM   2320  C  C   . LYS A 1 308  ? -30.276  68.402  20.178  1.00 279.77 ? 308  LYS A C   1 
ATOM   2321  O  O   . LYS A 1 308  ? -31.033  68.286  19.215  1.00 282.63 ? 308  LYS A O   1 
ATOM   2322  C  CB  . LYS A 1 308  ? -29.960  69.292  22.540  1.00 259.63 ? 308  LYS A CB  1 
ATOM   2323  C  CG  . LYS A 1 308  ? -30.667  69.763  23.823  1.00 254.85 ? 308  LYS A CG  1 
ATOM   2324  C  CD  . LYS A 1 308  ? -29.888  70.875  24.537  1.00 255.11 ? 308  LYS A CD  1 
ATOM   2325  C  CE  . LYS A 1 308  ? -28.479  70.432  24.920  1.00 254.85 ? 308  LYS A CE  1 
ATOM   2326  N  NZ  . LYS A 1 308  ? -27.702  71.506  25.600  1.00 256.38 ? 308  LYS A NZ  1 
ATOM   2327  N  N   . GLU A 1 309  ? -28.955  68.447  20.046  1.00 294.99 ? 309  GLU A N   1 
ATOM   2328  C  CA  . GLU A 1 309  ? -28.339  68.485  18.722  1.00 308.97 ? 309  GLU A CA  1 
ATOM   2329  C  C   . GLU A 1 309  ? -28.672  67.222  17.945  1.00 299.29 ? 309  GLU A C   1 
ATOM   2330  O  O   . GLU A 1 309  ? -28.428  67.132  16.744  1.00 313.88 ? 309  GLU A O   1 
ATOM   2331  C  CB  . GLU A 1 309  ? -26.819  68.670  18.826  1.00 332.55 ? 309  GLU A CB  1 
ATOM   2332  C  CG  . GLU A 1 309  ? -26.064  68.614  17.491  1.00 359.56 ? 309  GLU A CG  1 
ATOM   2333  C  CD  . GLU A 1 309  ? -26.284  69.838  16.611  1.00 378.04 ? 309  GLU A CD  1 
ATOM   2334  O  OE1 . GLU A 1 309  ? -26.705  70.891  17.135  1.00 384.13 ? 309  GLU A OE1 1 
ATOM   2335  O  OE2 . GLU A 1 309  ? -26.027  69.747  15.392  1.00 386.85 ? 309  GLU A OE2 1 
ATOM   2336  N  N   . LEU A 1 310  ? -29.245  66.246  18.635  1.00 281.12 ? 310  LEU A N   1 
ATOM   2337  C  CA  . LEU A 1 310  ? -29.495  64.960  18.014  1.00 269.48 ? 310  LEU A CA  1 
ATOM   2338  C  C   . LEU A 1 310  ? -30.902  64.848  17.420  1.00 252.55 ? 310  LEU A C   1 
ATOM   2339  O  O   . LEU A 1 310  ? -31.308  63.778  16.983  1.00 249.58 ? 310  LEU A O   1 
ATOM   2340  C  CB  . LEU A 1 310  ? -29.207  63.830  19.006  1.00 270.36 ? 310  LEU A CB  1 
ATOM   2341  C  CG  . LEU A 1 310  ? -27.969  63.993  19.906  1.00 270.53 ? 310  LEU A CG  1 
ATOM   2342  C  CD1 . LEU A 1 310  ? -27.531  62.652  20.504  1.00 268.28 ? 310  LEU A CD1 1 
ATOM   2343  C  CD2 . LEU A 1 310  ? -26.798  64.657  19.183  1.00 274.38 ? 310  LEU A CD2 1 
ATOM   2344  N  N   . SER A 1 311  ? -31.636  65.956  17.400  1.00 239.00 ? 311  SER A N   1 
ATOM   2345  C  CA  . SER A 1 311  ? -32.956  66.003  16.771  1.00 226.34 ? 311  SER A CA  1 
ATOM   2346  C  C   . SER A 1 311  ? -33.546  67.413  16.883  1.00 220.69 ? 311  SER A C   1 
ATOM   2347  O  O   . SER A 1 311  ? -32.926  68.294  17.468  1.00 218.83 ? 311  SER A O   1 
ATOM   2348  C  CB  . SER A 1 311  ? -33.903  64.972  17.396  1.00 217.69 ? 311  SER A CB  1 
ATOM   2349  O  OG  . SER A 1 311  ? -33.691  63.667  16.886  1.00 214.07 ? 311  SER A OG  1 
ATOM   2350  N  N   . TYR A 1 312  ? -34.734  67.630  16.320  1.00 217.83 ? 312  TYR A N   1 
ATOM   2351  C  CA  . TYR A 1 312  ? -35.432  68.919  16.452  1.00 217.42 ? 312  TYR A CA  1 
ATOM   2352  C  C   . TYR A 1 312  ? -35.792  69.275  17.920  1.00 171.87 ? 312  TYR A C   1 
ATOM   2353  O  O   . TYR A 1 312  ? -36.398  70.331  18.180  1.00 170.43 ? 312  TYR A O   1 
ATOM   2354  C  CB  . TYR A 1 312  ? -36.716  68.948  15.592  1.00 219.77 ? 312  TYR A CB  1 
ATOM   2355  C  CG  . TYR A 1 312  ? -36.588  69.539  14.195  1.00 225.71 ? 312  TYR A CG  1 
ATOM   2356  C  CD1 . TYR A 1 312  ? -37.153  68.901  13.097  1.00 228.75 ? 312  TYR A CD1 1 
ATOM   2357  C  CD2 . TYR A 1 312  ? -35.927  70.744  13.974  1.00 228.60 ? 312  TYR A CD2 1 
ATOM   2358  C  CE1 . TYR A 1 312  ? -37.052  69.438  11.818  1.00 233.30 ? 312  TYR A CE1 1 
ATOM   2359  C  CE2 . TYR A 1 312  ? -35.823  71.288  12.694  1.00 232.84 ? 312  TYR A CE2 1 
ATOM   2360  C  CZ  . TYR A 1 312  ? -36.386  70.628  11.623  1.00 234.81 ? 312  TYR A CZ  1 
ATOM   2361  O  OH  . TYR A 1 312  ? -36.284  71.150  10.352  1.00 238.93 ? 312  TYR A OH  1 
ATOM   2362  N  N   . TYR A 1 313  ? -35.430  68.399  18.865  1.00 168.45 ? 313  TYR A N   1 
ATOM   2363  C  CA  . TYR A 1 313  ? -35.872  68.525  20.260  1.00 161.53 ? 313  TYR A CA  1 
ATOM   2364  C  C   . TYR A 1 313  ? -34.877  69.161  21.256  1.00 164.77 ? 313  TYR A C   1 
ATOM   2365  O  O   . TYR A 1 313  ? -33.984  68.496  21.794  1.00 165.49 ? 313  TYR A O   1 
ATOM   2366  C  CB  . TYR A 1 313  ? -36.330  67.176  20.792  1.00 150.21 ? 313  TYR A CB  1 
ATOM   2367  C  CG  . TYR A 1 313  ? -37.167  66.366  19.848  1.00 143.01 ? 313  TYR A CG  1 
ATOM   2368  C  CD1 . TYR A 1 313  ? -36.695  65.184  19.339  1.00 141.54 ? 313  TYR A CD1 1 
ATOM   2369  C  CD2 . TYR A 1 313  ? -38.440  66.769  19.486  1.00 140.67 ? 313  TYR A CD2 1 
ATOM   2370  C  CE1 . TYR A 1 313  ? -37.455  64.412  18.466  1.00 141.94 ? 313  TYR A CE1 1 
ATOM   2371  C  CE2 . TYR A 1 313  ? -39.225  66.004  18.620  1.00 140.76 ? 313  TYR A CE2 1 
ATOM   2372  C  CZ  . TYR A 1 313  ? -38.725  64.818  18.106  1.00 140.88 ? 313  TYR A CZ  1 
ATOM   2373  O  OH  . TYR A 1 313  ? -39.482  64.044  17.233  1.00 140.99 ? 313  TYR A OH  1 
ATOM   2374  N  N   . SER A 1 314  ? -35.096  70.447  21.526  1.00 165.79 ? 314  SER A N   1 
ATOM   2375  C  CA  . SER A 1 314  ? -34.220  71.275  22.357  1.00 164.93 ? 314  SER A CA  1 
ATOM   2376  C  C   . SER A 1 314  ? -34.853  71.665  23.707  1.00 155.92 ? 314  SER A C   1 
ATOM   2377  O  O   . SER A 1 314  ? -34.164  71.783  24.725  1.00 153.01 ? 314  SER A O   1 
ATOM   2378  C  CB  . SER A 1 314  ? -33.872  72.533  21.571  1.00 173.49 ? 314  SER A CB  1 
ATOM   2379  O  OG  . SER A 1 314  ? -35.047  73.047  20.955  1.00 177.18 ? 314  SER A OG  1 
ATOM   2380  N  N   . LEU A 1 315  ? -36.158  71.896  23.705  1.00 151.60 ? 315  LEU A N   1 
ATOM   2381  C  CA  . LEU A 1 315  ? -36.883  72.018  24.955  1.00 147.46 ? 315  LEU A CA  1 
ATOM   2382  C  C   . LEU A 1 315  ? -37.573  70.672  25.221  1.00 137.38 ? 315  LEU A C   1 
ATOM   2383  O  O   . LEU A 1 315  ? -38.105  70.068  24.290  1.00 135.96 ? 315  LEU A O   1 
ATOM   2384  C  CB  . LEU A 1 315  ? -37.912  73.169  24.875  1.00 154.63 ? 315  LEU A CB  1 
ATOM   2385  C  CG  . LEU A 1 315  ? -37.577  74.679  25.045  1.00 162.05 ? 315  LEU A CG  1 
ATOM   2386  C  CD1 . LEU A 1 315  ? -38.411  75.555  24.099  1.00 163.40 ? 315  LEU A CD1 1 
ATOM   2387  C  CD2 . LEU A 1 315  ? -37.723  75.189  26.498  1.00 159.68 ? 315  LEU A CD2 1 
ATOM   2388  N  N   . GLU A 1 316  ? -37.544  70.194  26.468  1.00 127.76 ? 316  GLU A N   1 
ATOM   2389  C  CA  . GLU A 1 316  ? -38.271  68.980  26.845  1.00 120.80 ? 316  GLU A CA  1 
ATOM   2390  C  C   . GLU A 1 316  ? -39.758  69.221  26.610  1.00 115.46 ? 316  GLU A C   1 
ATOM   2391  O  O   . GLU A 1 316  ? -40.469  68.344  26.130  1.00 112.48 ? 316  GLU A O   1 
ATOM   2392  C  CB  . GLU A 1 316  ? -38.020  68.628  28.307  1.00 121.75 ? 316  GLU A CB  1 
ATOM   2393  C  CG  . GLU A 1 316  ? -38.640  67.300  28.745  1.00 125.40 ? 316  GLU A CG  1 
ATOM   2394  C  CD  . GLU A 1 316  ? -39.976  67.430  29.508  1.00 130.32 ? 316  GLU A CD  1 
ATOM   2395  O  OE1 . GLU A 1 316  ? -40.207  68.448  30.202  1.00 132.53 ? 316  GLU A OE1 1 
ATOM   2396  O  OE2 . GLU A 1 316  ? -40.801  66.491  29.432  1.00 131.05 ? 316  GLU A OE2 1 
ATOM   2397  N  N   . ASP A 1 317  ? -40.202  70.425  26.973  1.00 113.97 ? 317  ASP A N   1 
ATOM   2398  C  CA  . ASP A 1 317  ? -41.465  71.010  26.539  1.00 116.15 ? 317  ASP A CA  1 
ATOM   2399  C  C   . ASP A 1 317  ? -41.894  70.298  25.262  1.00 119.40 ? 317  ASP A C   1 
ATOM   2400  O  O   . ASP A 1 317  ? -42.764  69.422  25.285  1.00 117.01 ? 317  ASP A O   1 
ATOM   2401  C  CB  . ASP A 1 317  ? -41.191  72.508  26.267  1.00 119.21 ? 317  ASP A CB  1 
ATOM   2402  C  CG  . ASP A 1 317  ? -42.447  73.413  26.358  1.00 133.91 ? 317  ASP A CG  1 
ATOM   2403  O  OD1 . ASP A 1 317  ? -43.590  72.952  26.116  1.00 135.43 ? 317  ASP A OD1 1 
ATOM   2404  O  OD2 . ASP A 1 317  ? -42.275  74.626  26.650  1.00 134.19 ? 317  ASP A OD2 1 
ATOM   2405  N  N   . LEU A 1 318  ? -41.236  70.707  24.165  1.00 126.92 ? 318  LEU A N   1 
ATOM   2406  C  CA  . LEU A 1 318  ? -41.241  70.103  22.811  1.00 130.67 ? 318  LEU A CA  1 
ATOM   2407  C  C   . LEU A 1 318  ? -40.986  68.597  22.828  1.00 127.59 ? 318  LEU A C   1 
ATOM   2408  O  O   . LEU A 1 318  ? -39.929  68.141  22.411  1.00 126.43 ? 318  LEU A O   1 
ATOM   2409  C  CB  . LEU A 1 318  ? -40.082  70.688  21.986  1.00 135.61 ? 318  LEU A CB  1 
ATOM   2410  C  CG  . LEU A 1 318  ? -40.085  72.071  21.357  1.00 142.74 ? 318  LEU A CG  1 
ATOM   2411  C  CD1 . LEU A 1 318  ? -38.666  72.447  20.982  1.00 146.39 ? 318  LEU A CD1 1 
ATOM   2412  C  CD2 . LEU A 1 318  ? -40.966  72.070  20.139  1.00 147.33 ? 318  LEU A CD2 1 
ATOM   2413  N  N   . ASN A 1 319  ? -41.953  67.822  23.292  1.00 123.56 ? 319  ASN A N   1 
ATOM   2414  C  CA  . ASN A 1 319  ? -41.726  66.409  23.454  1.00 115.39 ? 319  ASN A CA  1 
ATOM   2415  C  C   . ASN A 1 319  ? -42.779  65.805  24.352  1.00 107.73 ? 319  ASN A C   1 
ATOM   2416  O  O   . ASN A 1 319  ? -42.603  65.792  25.548  1.00 105.72 ? 319  ASN A O   1 
ATOM   2417  C  CB  . ASN A 1 319  ? -40.356  66.207  24.077  1.00 113.92 ? 319  ASN A CB  1 
ATOM   2418  C  CG  . ASN A 1 319  ? -39.754  64.915  23.671  1.00 118.93 ? 319  ASN A CG  1 
ATOM   2419  O  OD1 . ASN A 1 319  ? -40.403  64.127  22.984  1.00 121.60 ? 319  ASN A OD1 1 
ATOM   2420  N  ND2 . ASN A 1 319  ? -38.503  64.668  24.076  1.00 120.57 ? 319  ASN A ND2 1 
ATOM   2421  N  N   . ASN A 1 320  ? -43.888  65.341  23.791  1.00 105.72 ? 320  ASN A N   1 
ATOM   2422  C  CA  . ASN A 1 320  ? -44.860  64.579  24.569  1.00 103.94 ? 320  ASN A CA  1 
ATOM   2423  C  C   . ASN A 1 320  ? -45.195  63.308  23.843  1.00 105.99 ? 320  ASN A C   1 
ATOM   2424  O  O   . ASN A 1 320  ? -46.330  62.795  23.917  1.00 106.14 ? 320  ASN A O   1 
ATOM   2425  C  CB  . ASN A 1 320  ? -46.104  65.376  24.914  1.00 104.92 ? 320  ASN A CB  1 
ATOM   2426  C  CG  . ASN A 1 320  ? -45.822  66.421  25.981  1.00 107.07 ? 320  ASN A CG  1 
ATOM   2427  O  OD1 . ASN A 1 320  ? -46.275  66.318  27.134  1.00 106.20 ? 320  ASN A OD1 1 
ATOM   2428  N  ND2 . ASN A 1 320  ? -45.027  67.424  25.611  1.00 109.18 ? 320  ASN A ND2 1 
ATOM   2429  N  N   . LYS A 1 321  ? -44.152  62.848  23.141  1.00 107.53 ? 321  LYS A N   1 
ATOM   2430  C  CA  . LYS A 1 321  ? -44.053  61.595  22.398  1.00 109.85 ? 321  LYS A CA  1 
ATOM   2431  C  C   . LYS A 1 321  ? -43.173  60.596  23.138  1.00 105.26 ? 321  LYS A C   1 
ATOM   2432  O  O   . LYS A 1 321  ? -42.880  60.788  24.302  1.00 102.72 ? 321  LYS A O   1 
ATOM   2433  C  CB  . LYS A 1 321  ? -43.414  61.873  21.045  1.00 118.82 ? 321  LYS A CB  1 
ATOM   2434  C  CG  . LYS A 1 321  ? -42.316  62.943  21.053  1.00 124.29 ? 321  LYS A CG  1 
ATOM   2435  C  CD  . LYS A 1 321  ? -42.062  63.481  19.623  1.00 133.09 ? 321  LYS A CD  1 
ATOM   2436  C  CE  . LYS A 1 321  ? -42.356  64.990  19.463  1.00 136.43 ? 321  LYS A CE  1 
ATOM   2437  N  NZ  . LYS A 1 321  ? -42.180  65.443  18.047  1.00 140.55 ? 321  LYS A NZ  1 
ATOM   2438  N  N   . TYR A 1 322  ? -42.712  59.554  22.451  1.00 103.90 ? 322  TYR A N   1 
ATOM   2439  C  CA  . TYR A 1 322  ? -42.127  58.401  23.131  1.00 101.71 ? 322  TYR A CA  1 
ATOM   2440  C  C   . TYR A 1 322  ? -40.606  58.345  23.187  1.00 103.99 ? 322  TYR A C   1 
ATOM   2441  O  O   . TYR A 1 322  ? -39.939  58.985  22.389  1.00 107.38 ? 322  TYR A O   1 
ATOM   2442  C  CB  . TYR A 1 322  ? -42.707  57.112  22.555  1.00 100.97 ? 322  TYR A CB  1 
ATOM   2443  C  CG  . TYR A 1 322  ? -44.126  56.961  22.960  1.00 100.55 ? 322  TYR A CG  1 
ATOM   2444  C  CD1 . TYR A 1 322  ? -44.545  55.887  23.716  1.00 98.51  ? 322  TYR A CD1 1 
ATOM   2445  C  CD2 . TYR A 1 322  ? -45.044  57.950  22.635  1.00 105.20 ? 322  TYR A CD2 1 
ATOM   2446  C  CE1 . TYR A 1 322  ? -45.855  55.781  24.111  1.00 102.40 ? 322  TYR A CE1 1 
ATOM   2447  C  CE2 . TYR A 1 322  ? -46.362  57.864  23.012  1.00 108.02 ? 322  TYR A CE2 1 
ATOM   2448  C  CZ  . TYR A 1 322  ? -46.768  56.781  23.756  1.00 108.03 ? 322  TYR A CZ  1 
ATOM   2449  O  OH  . TYR A 1 322  ? -48.097  56.717  24.134  1.00 110.84 ? 322  TYR A OH  1 
ATOM   2450  N  N   . LEU A 1 323  ? -40.069  57.595  24.149  1.00 102.60 ? 323  LEU A N   1 
ATOM   2451  C  CA  . LEU A 1 323  ? -38.649  57.292  24.180  1.00 105.25 ? 323  LEU A CA  1 
ATOM   2452  C  C   . LEU A 1 323  ? -38.452  55.789  23.947  1.00 109.27 ? 323  LEU A C   1 
ATOM   2453  O  O   . LEU A 1 323  ? -39.007  54.988  24.684  1.00 109.20 ? 323  LEU A O   1 
ATOM   2454  C  CB  . LEU A 1 323  ? -38.055  57.716  25.513  1.00 103.24 ? 323  LEU A CB  1 
ATOM   2455  C  CG  . LEU A 1 323  ? -36.544  57.539  25.621  1.00 103.66 ? 323  LEU A CG  1 
ATOM   2456  C  CD1 . LEU A 1 323  ? -36.147  56.077  25.816  1.00 102.83 ? 323  LEU A CD1 1 
ATOM   2457  C  CD2 . LEU A 1 323  ? -35.917  58.099  24.379  1.00 106.18 ? 323  LEU A CD2 1 
ATOM   2458  N  N   . TYR A 1 324  ? -37.671  55.411  22.928  1.00 115.17 ? 324  TYR A N   1 
ATOM   2459  C  CA  . TYR A 1 324  ? -37.449  53.995  22.556  1.00 120.19 ? 324  TYR A CA  1 
ATOM   2460  C  C   . TYR A 1 324  ? -36.101  53.434  23.013  1.00 120.39 ? 324  TYR A C   1 
ATOM   2461  O  O   . TYR A 1 324  ? -35.044  54.000  22.688  1.00 120.07 ? 324  TYR A O   1 
ATOM   2462  C  CB  . TYR A 1 324  ? -37.573  53.809  21.039  1.00 127.50 ? 324  TYR A CB  1 
ATOM   2463  C  CG  . TYR A 1 324  ? -37.076  52.473  20.478  1.00 133.61 ? 324  TYR A CG  1 
ATOM   2464  C  CD1 . TYR A 1 324  ? -37.976  51.481  20.100  1.00 137.77 ? 324  TYR A CD1 1 
ATOM   2465  C  CD2 . TYR A 1 324  ? -35.716  52.219  20.284  1.00 135.82 ? 324  TYR A CD2 1 
ATOM   2466  C  CE1 . TYR A 1 324  ? -37.542  50.261  19.565  1.00 140.27 ? 324  TYR A CE1 1 
ATOM   2467  C  CE2 . TYR A 1 324  ? -35.274  50.995  19.746  1.00 138.30 ? 324  TYR A CE2 1 
ATOM   2468  C  CZ  . TYR A 1 324  ? -36.198  50.024  19.392  1.00 139.71 ? 324  TYR A CZ  1 
ATOM   2469  O  OH  . TYR A 1 324  ? -35.798  48.820  18.858  1.00 140.37 ? 324  TYR A OH  1 
ATOM   2470  N  N   . ILE A 1 325  ? -36.148  52.305  23.731  1.00 118.36 ? 325  ILE A N   1 
ATOM   2471  C  CA  . ILE A 1 325  ? -34.942  51.666  24.263  1.00 115.42 ? 325  ILE A CA  1 
ATOM   2472  C  C   . ILE A 1 325  ? -34.866  50.234  23.793  1.00 115.00 ? 325  ILE A C   1 
ATOM   2473  O  O   . ILE A 1 325  ? -35.870  49.525  23.757  1.00 115.12 ? 325  ILE A O   1 
ATOM   2474  C  CB  . ILE A 1 325  ? -34.909  51.603  25.797  1.00 110.82 ? 325  ILE A CB  1 
ATOM   2475  C  CG1 . ILE A 1 325  ? -35.724  52.729  26.430  1.00 110.79 ? 325  ILE A CG1 1 
ATOM   2476  C  CG2 . ILE A 1 325  ? -33.483  51.645  26.295  1.00 109.68 ? 325  ILE A CG2 1 
ATOM   2477  C  CD1 . ILE A 1 325  ? -35.644  52.730  27.934  1.00 108.22 ? 325  ILE A CD1 1 
ATOM   2478  N  N   . ALA A 1 326  ? -33.654  49.814  23.457  1.00 114.62 ? 326  ALA A N   1 
ATOM   2479  C  CA  . ALA A 1 326  ? -33.409  48.493  22.913  1.00 115.57 ? 326  ALA A CA  1 
ATOM   2480  C  C   . ALA A 1 326  ? -31.952  48.134  23.108  1.00 115.47 ? 326  ALA A C   1 
ATOM   2481  O  O   . ALA A 1 326  ? -31.039  48.779  22.576  1.00 114.53 ? 326  ALA A O   1 
ATOM   2482  C  CB  . ALA A 1 326  ? -33.782  48.437  21.453  1.00 116.57 ? 326  ALA A CB  1 
ATOM   2483  N  N   . VAL A 1 327  ? -31.763  47.088  23.896  1.00 117.68 ? 327  VAL A N   1 
ATOM   2484  C  CA  . VAL A 1 327  ? -30.458  46.627  24.298  1.00 119.31 ? 327  VAL A CA  1 
ATOM   2485  C  C   . VAL A 1 327  ? -30.064  45.479  23.397  1.00 122.74 ? 327  VAL A C   1 
ATOM   2486  O  O   . VAL A 1 327  ? -30.942  44.786  22.887  1.00 125.69 ? 327  VAL A O   1 
ATOM   2487  C  CB  . VAL A 1 327  ? -30.529  46.104  25.727  1.00 113.53 ? 327  VAL A CB  1 
ATOM   2488  C  CG1 . VAL A 1 327  ? -29.129  45.840  26.279  1.00 113.88 ? 327  VAL A CG1 1 
ATOM   2489  C  CG2 . VAL A 1 327  ? -31.290  47.084  26.586  1.00 109.76 ? 327  VAL A CG2 1 
ATOM   2490  N  N   . THR A 1 328  ? -28.754  45.288  23.205  1.00 125.50 ? 328  THR A N   1 
ATOM   2491  C  CA  . THR A 1 328  ? -28.206  44.029  22.673  1.00 128.78 ? 328  THR A CA  1 
ATOM   2492  C  C   . THR A 1 328  ? -27.080  43.483  23.571  1.00 129.14 ? 328  THR A C   1 
ATOM   2493  O  O   . THR A 1 328  ? -26.020  44.093  23.702  1.00 125.49 ? 328  THR A O   1 
ATOM   2494  C  CB  . THR A 1 328  ? -27.707  44.156  21.234  1.00 133.46 ? 328  THR A CB  1 
ATOM   2495  O  OG1 . THR A 1 328  ? -28.740  44.718  20.418  1.00 136.25 ? 328  THR A OG1 1 
ATOM   2496  C  CG2 . THR A 1 328  ? -27.360  42.791  20.696  1.00 134.58 ? 328  THR A CG2 1 
ATOM   2497  N  N   . VAL A 1 329  ? -27.344  42.338  24.195  1.00 132.19 ? 329  VAL A N   1 
ATOM   2498  C  CA  . VAL A 1 329  ? -26.467  41.747  25.189  1.00 135.01 ? 329  VAL A CA  1 
ATOM   2499  C  C   . VAL A 1 329  ? -25.775  40.556  24.601  1.00 145.36 ? 329  VAL A C   1 
ATOM   2500  O  O   . VAL A 1 329  ? -26.387  39.494  24.513  1.00 150.67 ? 329  VAL A O   1 
ATOM   2501  C  CB  . VAL A 1 329  ? -27.281  41.176  26.336  1.00 128.12 ? 329  VAL A CB  1 
ATOM   2502  C  CG1 . VAL A 1 329  ? -26.348  40.641  27.423  1.00 125.27 ? 329  VAL A CG1 1 
ATOM   2503  C  CG2 . VAL A 1 329  ? -28.255  42.210  26.868  1.00 125.08 ? 329  VAL A CG2 1 
ATOM   2504  N  N   . ILE A 1 330  ? -24.513  40.706  24.205  1.00 150.99 ? 330  ILE A N   1 
ATOM   2505  C  CA  . ILE A 1 330  ? -23.776  39.580  23.619  1.00 158.33 ? 330  ILE A CA  1 
ATOM   2506  C  C   . ILE A 1 330  ? -22.920  38.846  24.658  1.00 165.66 ? 330  ILE A C   1 
ATOM   2507  O  O   . ILE A 1 330  ? -22.031  39.428  25.283  1.00 162.91 ? 330  ILE A O   1 
ATOM   2508  C  CB  . ILE A 1 330  ? -22.970  39.973  22.335  1.00 171.25 ? 330  ILE A CB  1 
ATOM   2509  C  CG1 . ILE A 1 330  ? -22.035  41.156  22.588  1.00 170.92 ? 330  ILE A CG1 1 
ATOM   2510  C  CG2 . ILE A 1 330  ? -23.912  40.310  21.192  1.00 171.06 ? 330  ILE A CG2 1 
ATOM   2511  C  CD1 . ILE A 1 330  ? -21.432  41.728  21.310  1.00 173.00 ? 330  ILE A CD1 1 
ATOM   2512  N  N   . GLU A 1 331  ? -23.217  37.566  24.848  1.00 176.10 ? 331  GLU A N   1 
ATOM   2513  C  CA  . GLU A 1 331  ? -22.599  36.816  25.917  1.00 185.67 ? 331  GLU A CA  1 
ATOM   2514  C  C   . GLU A 1 331  ? -21.112  36.676  25.686  1.00 195.92 ? 331  GLU A C   1 
ATOM   2515  O  O   . GLU A 1 331  ? -20.685  36.327  24.591  1.00 198.93 ? 331  GLU A O   1 
ATOM   2516  C  CB  . GLU A 1 331  ? -23.223  35.446  26.015  1.00 187.16 ? 331  GLU A CB  1 
ATOM   2517  C  CG  . GLU A 1 331  ? -22.391  34.512  26.830  1.00 188.79 ? 331  GLU A CG  1 
ATOM   2518  C  CD  . GLU A 1 331  ? -22.667  33.090  26.462  1.00 191.25 ? 331  GLU A CD  1 
ATOM   2519  O  OE1 . GLU A 1 331  ? -23.691  32.880  25.788  1.00 191.43 ? 331  GLU A OE1 1 
ATOM   2520  O  OE2 . GLU A 1 331  ? -21.878  32.189  26.828  1.00 193.02 ? 331  GLU A OE2 1 
ATOM   2521  N  N   . SER A 1 332  ? -20.329  36.937  26.728  1.00 202.55 ? 332  SER A N   1 
ATOM   2522  C  CA  . SER A 1 332  ? -18.873  36.968  26.615  1.00 212.10 ? 332  SER A CA  1 
ATOM   2523  C  C   . SER A 1 332  ? -18.235  35.595  26.435  1.00 220.69 ? 332  SER A C   1 
ATOM   2524  O  O   . SER A 1 332  ? -17.287  35.437  25.664  1.00 222.74 ? 332  SER A O   1 
ATOM   2525  C  CB  . SER A 1 332  ? -18.259  37.658  27.830  1.00 213.20 ? 332  SER A CB  1 
ATOM   2526  O  OG  . SER A 1 332  ? -16.859  37.800  27.665  1.00 216.72 ? 332  SER A OG  1 
ATOM   2527  N  N   . THR A 1 333  ? -18.743  34.606  27.157  1.00 226.42 ? 333  THR A N   1 
ATOM   2528  C  CA  . THR A 1 333  ? -18.201  33.255  27.072  1.00 233.05 ? 333  THR A CA  1 
ATOM   2529  C  C   . THR A 1 333  ? -18.431  32.594  25.711  1.00 236.34 ? 333  THR A C   1 
ATOM   2530  O  O   . THR A 1 333  ? -17.491  32.403  24.945  1.00 239.40 ? 333  THR A O   1 
ATOM   2531  C  CB  . THR A 1 333  ? -18.743  32.365  28.203  1.00 234.00 ? 333  THR A CB  1 
ATOM   2532  O  OG1 . THR A 1 333  ? -19.283  31.158  27.651  1.00 235.76 ? 333  THR A OG1 1 
ATOM   2533  C  CG2 . THR A 1 333  ? -19.832  33.098  28.972  1.00 231.18 ? 333  THR A CG2 1 
ATOM   2534  N  N   . GLY A 1 334  ? -19.678  32.254  25.408  1.00 235.48 ? 334  GLY A N   1 
ATOM   2535  C  CA  . GLY A 1 334  ? -19.995  31.568  24.168  1.00 236.04 ? 334  GLY A CA  1 
ATOM   2536  C  C   . GLY A 1 334  ? -19.863  32.406  22.906  1.00 233.85 ? 334  GLY A C   1 
ATOM   2537  O  O   . GLY A 1 334  ? -19.641  31.873  21.817  1.00 239.18 ? 334  GLY A O   1 
ATOM   2538  N  N   . GLY A 1 335  ? -19.998  33.722  23.047  1.00 223.51 ? 335  GLY A N   1 
ATOM   2539  C  CA  . GLY A 1 335  ? -19.984  34.621  21.904  1.00 215.37 ? 335  GLY A CA  1 
ATOM   2540  C  C   . GLY A 1 335  ? -21.337  34.730  21.224  1.00 205.66 ? 335  GLY A C   1 
ATOM   2541  O  O   . GLY A 1 335  ? -21.458  35.306  20.142  1.00 205.81 ? 335  GLY A O   1 
ATOM   2542  N  N   . PHE A 1 336  ? -22.356  34.166  21.864  1.00 198.52 ? 336  PHE A N   1 
ATOM   2543  C  CA  . PHE A 1 336  ? -23.713  34.190  21.341  1.00 188.07 ? 336  PHE A CA  1 
ATOM   2544  C  C   . PHE A 1 336  ? -24.123  35.617  21.094  1.00 179.26 ? 336  PHE A C   1 
ATOM   2545  O  O   . PHE A 1 336  ? -23.282  36.490  20.937  1.00 178.39 ? 336  PHE A O   1 
ATOM   2546  C  CB  . PHE A 1 336  ? -24.680  33.608  22.363  1.00 181.87 ? 336  PHE A CB  1 
ATOM   2547  C  CG  . PHE A 1 336  ? -24.782  32.107  22.343  1.00 177.44 ? 336  PHE A CG  1 
ATOM   2548  C  CD1 . PHE A 1 336  ? -24.533  31.367  23.490  1.00 173.34 ? 336  PHE A CD1 1 
ATOM   2549  C  CD2 . PHE A 1 336  ? -25.156  31.441  21.198  1.00 177.62 ? 336  PHE A CD2 1 
ATOM   2550  C  CE1 . PHE A 1 336  ? -24.649  29.997  23.496  1.00 173.92 ? 336  PHE A CE1 1 
ATOM   2551  C  CE2 . PHE A 1 336  ? -25.273  30.070  21.198  1.00 178.85 ? 336  PHE A CE2 1 
ATOM   2552  C  CZ  . PHE A 1 336  ? -25.019  29.350  22.351  1.00 177.45 ? 336  PHE A CZ  1 
ATOM   2553  N  N   . SER A 1 337  ? -25.430  35.845  21.066  1.00 172.01 ? 337  SER A N   1 
ATOM   2554  C  CA  . SER A 1 337  ? -25.971  37.200  21.072  1.00 163.91 ? 337  SER A CA  1 
ATOM   2555  C  C   . SER A 1 337  ? -27.470  37.221  21.273  1.00 162.60 ? 337  SER A C   1 
ATOM   2556  O  O   . SER A 1 337  ? -28.205  36.358  20.779  1.00 164.12 ? 337  SER A O   1 
ATOM   2557  C  CB  . SER A 1 337  ? -25.629  37.962  19.796  1.00 161.45 ? 337  SER A CB  1 
ATOM   2558  O  OG  . SER A 1 337  ? -26.280  39.222  19.786  1.00 155.29 ? 337  SER A OG  1 
ATOM   2559  N  N   . GLU A 1 338  ? -27.915  38.243  21.988  1.00 158.93 ? 338  GLU A N   1 
ATOM   2560  C  CA  . GLU A 1 338  ? -29.305  38.358  22.357  1.00 158.10 ? 338  GLU A CA  1 
ATOM   2561  C  C   . GLU A 1 338  ? -29.717  39.810  22.367  1.00 153.53 ? 338  GLU A C   1 
ATOM   2562  O  O   . GLU A 1 338  ? -29.002  40.661  22.887  1.00 150.60 ? 338  GLU A O   1 
ATOM   2563  C  CB  . GLU A 1 338  ? -29.532  37.743  23.729  1.00 160.31 ? 338  GLU A CB  1 
ATOM   2564  C  CG  . GLU A 1 338  ? -30.918  37.183  23.901  1.00 164.91 ? 338  GLU A CG  1 
ATOM   2565  C  CD  . GLU A 1 338  ? -31.373  36.403  22.684  1.00 171.97 ? 338  GLU A CD  1 
ATOM   2566  O  OE1 . GLU A 1 338  ? -30.641  35.484  22.232  1.00 174.39 ? 338  GLU A OE1 1 
ATOM   2567  O  OE2 . GLU A 1 338  ? -32.473  36.720  22.180  1.00 174.99 ? 338  GLU A OE2 1 
ATOM   2568  N  N   . GLU A 1 339  ? -30.867  40.077  21.760  1.00 153.25 ? 339  GLU A N   1 
ATOM   2569  C  CA  . GLU A 1 339  ? -31.418  41.415  21.667  1.00 152.56 ? 339  GLU A CA  1 
ATOM   2570  C  C   . GLU A 1 339  ? -32.709  41.491  22.462  1.00 144.08 ? 339  GLU A C   1 
ATOM   2571  O  O   . GLU A 1 339  ? -33.364  40.465  22.693  1.00 140.66 ? 339  GLU A O   1 
ATOM   2572  C  CB  . GLU A 1 339  ? -31.686  41.784  20.208  1.00 162.76 ? 339  GLU A CB  1 
ATOM   2573  C  CG  . GLU A 1 339  ? -30.452  42.224  19.436  1.00 172.93 ? 339  GLU A CG  1 
ATOM   2574  C  CD  . GLU A 1 339  ? -30.455  41.756  17.974  1.00 185.45 ? 339  GLU A CD  1 
ATOM   2575  O  OE1 . GLU A 1 339  ? -31.527  41.731  17.326  1.00 189.94 ? 339  GLU A OE1 1 
ATOM   2576  O  OE2 . GLU A 1 339  ? -29.370  41.400  17.463  1.00 189.84 ? 339  GLU A OE2 1 
ATOM   2577  N  N   . ALA A 1 340  ? -33.042  42.717  22.881  1.00 142.37 ? 340  ALA A N   1 
ATOM   2578  C  CA  . ALA A 1 340  ? -34.268  43.052  23.617  1.00 140.25 ? 340  ALA A CA  1 
ATOM   2579  C  C   . ALA A 1 340  ? -34.599  44.518  23.420  1.00 136.97 ? 340  ALA A C   1 
ATOM   2580  O  O   . ALA A 1 340  ? -33.691  45.333  23.271  1.00 135.80 ? 340  ALA A O   1 
ATOM   2581  C  CB  . ALA A 1 340  ? -34.096  42.776  25.100  1.00 140.79 ? 340  ALA A CB  1 
ATOM   2582  N  N   . GLU A 1 341  ? -35.888  44.860  23.454  1.00 134.90 ? 341  GLU A N   1 
ATOM   2583  C  CA  . GLU A 1 341  ? -36.305  46.264  23.302  1.00 135.83 ? 341  GLU A CA  1 
ATOM   2584  C  C   . GLU A 1 341  ? -37.501  46.716  24.186  1.00 109.19 ? 341  GLU A C   1 
ATOM   2585  O  O   . GLU A 1 341  ? -38.331  45.899  24.587  1.00 108.49 ? 341  GLU A O   1 
ATOM   2586  C  CB  . GLU A 1 341  ? -36.623  46.556  21.826  1.00 139.87 ? 341  GLU A CB  1 
ATOM   2587  C  CG  . GLU A 1 341  ? -37.669  45.623  21.206  1.00 143.78 ? 341  GLU A CG  1 
ATOM   2588  C  CD  . GLU A 1 341  ? -38.409  46.254  20.032  1.00 147.04 ? 341  GLU A CD  1 
ATOM   2589  O  OE1 . GLU A 1 341  ? -38.066  47.390  19.640  1.00 147.21 ? 341  GLU A OE1 1 
ATOM   2590  O  OE2 . GLU A 1 341  ? -39.335  45.607  19.500  1.00 149.60 ? 341  GLU A OE2 1 
ATOM   2591  N  N   . ILE A 1 342  ? -37.571  48.012  24.496  1.00 107.91 ? 342  ILE A N   1 
ATOM   2592  C  CA  . ILE A 1 342  ? -38.789  48.613  25.031  1.00 104.68 ? 342  ILE A CA  1 
ATOM   2593  C  C   . ILE A 1 342  ? -39.346  49.524  23.980  1.00 107.23 ? 342  ILE A C   1 
ATOM   2594  O  O   . ILE A 1 342  ? -38.664  50.448  23.551  1.00 108.08 ? 342  ILE A O   1 
ATOM   2595  C  CB  . ILE A 1 342  ? -38.523  49.481  26.247  1.00 97.46  ? 342  ILE A CB  1 
ATOM   2596  C  CG1 . ILE A 1 342  ? -38.091  48.621  27.425  1.00 97.75  ? 342  ILE A CG1 1 
ATOM   2597  C  CG2 . ILE A 1 342  ? -39.766  50.263  26.613  1.00 92.28  ? 342  ILE A CG2 1 
ATOM   2598  C  CD1 . ILE A 1 342  ? -37.382  49.401  28.500  1.00 96.14  ? 342  ILE A CD1 1 
ATOM   2599  N  N   . PRO A 1 343  ? -40.609  49.303  23.597  1.00 107.90 ? 343  PRO A N   1 
ATOM   2600  C  CA  . PRO A 1 343  ? -41.169  49.950  22.407  1.00 109.13 ? 343  PRO A CA  1 
ATOM   2601  C  C   . PRO A 1 343  ? -41.088  51.454  22.554  1.00 105.81 ? 343  PRO A C   1 
ATOM   2602  O  O   . PRO A 1 343  ? -40.511  52.164  21.733  1.00 109.92 ? 343  PRO A O   1 
ATOM   2603  C  CB  . PRO A 1 343  ? -42.650  49.533  22.431  1.00 109.19 ? 343  PRO A CB  1 
ATOM   2604  C  CG  . PRO A 1 343  ? -42.794  48.565  23.541  1.00 109.00 ? 343  PRO A CG  1 
ATOM   2605  C  CD  . PRO A 1 343  ? -41.669  48.811  24.486  1.00 107.25 ? 343  PRO A CD  1 
ATOM   2606  N  N   . GLY A 1 344  ? -41.671  51.931  23.641  1.00 102.33 ? 344  GLY A N   1 
ATOM   2607  C  CA  . GLY A 1 344  ? -41.674  53.349  23.945  1.00 99.46  ? 344  GLY A CA  1 
ATOM   2608  C  C   . GLY A 1 344  ? -42.008  53.624  25.402  1.00 93.76  ? 344  GLY A C   1 
ATOM   2609  O  O   . GLY A 1 344  ? -42.473  52.731  26.114  1.00 94.60  ? 344  GLY A O   1 
ATOM   2610  N  N   . ILE A 1 345  ? -41.776  54.861  25.832  1.00 92.43  ? 345  ILE A N   1 
ATOM   2611  C  CA  . ILE A 1 345  ? -41.907  55.264  27.217  1.00 91.07  ? 345  ILE A CA  1 
ATOM   2612  C  C   . ILE A 1 345  ? -42.332  56.681  27.017  1.00 90.69  ? 345  ILE A C   1 
ATOM   2613  O  O   . ILE A 1 345  ? -41.541  57.461  26.509  1.00 92.54  ? 345  ILE A O   1 
ATOM   2614  C  CB  . ILE A 1 345  ? -40.516  55.288  27.897  1.00 88.85  ? 345  ILE A CB  1 
ATOM   2615  C  CG1 . ILE A 1 345  ? -40.047  53.893  28.273  1.00 77.63  ? 345  ILE A CG1 1 
ATOM   2616  C  CG2 . ILE A 1 345  ? -40.524  56.081  29.160  1.00 87.88  ? 345  ILE A CG2 1 
ATOM   2617  C  CD1 . ILE A 1 345  ? -38.797  53.928  29.079  1.00 76.62  ? 345  ILE A CD1 1 
ATOM   2618  N  N   . LYS A 1 346  ? -43.570  57.025  27.357  1.00 88.68  ? 346  LYS A N   1 
ATOM   2619  C  CA  . LYS A 1 346  ? -44.093  58.345  27.007  1.00 78.36  ? 346  LYS A CA  1 
ATOM   2620  C  C   . LYS A 1 346  ? -43.321  59.448  27.736  1.00 76.81  ? 346  LYS A C   1 
ATOM   2621  O  O   . LYS A 1 346  ? -43.047  59.302  28.900  1.00 81.25  ? 346  LYS A O   1 
ATOM   2622  C  CB  . LYS A 1 346  ? -45.587  58.409  27.321  1.00 78.47  ? 346  LYS A CB  1 
ATOM   2623  C  CG  . LYS A 1 346  ? -46.302  59.577  26.672  1.00 82.53  ? 346  LYS A CG  1 
ATOM   2624  C  CD  . LYS A 1 346  ? -47.772  59.723  27.128  1.00 85.08  ? 346  LYS A CD  1 
ATOM   2625  C  CE  . LYS A 1 346  ? -48.721  58.644  26.555  1.00 88.20  ? 346  LYS A CE  1 
ATOM   2626  N  NZ  . LYS A 1 346  ? -50.166  59.060  26.571  1.00 89.50  ? 346  LYS A NZ  1 
ATOM   2627  N  N   . TYR A 1 347  ? -42.928  60.533  27.073  1.00 77.48  ? 347  TYR A N   1 
ATOM   2628  C  CA  . TYR A 1 347  ? -42.372  61.688  27.806  1.00 81.77  ? 347  TYR A CA  1 
ATOM   2629  C  C   . TYR A 1 347  ? -43.550  62.511  28.323  1.00 81.19  ? 347  TYR A C   1 
ATOM   2630  O  O   . TYR A 1 347  ? -44.612  62.539  27.698  1.00 78.44  ? 347  TYR A O   1 
ATOM   2631  C  CB  . TYR A 1 347  ? -41.490  62.594  26.927  1.00 81.22  ? 347  TYR A CB  1 
ATOM   2632  C  CG  . TYR A 1 347  ? -40.015  62.246  26.880  1.00 81.94  ? 347  TYR A CG  1 
ATOM   2633  C  CD1 . TYR A 1 347  ? -39.136  62.748  27.834  1.00 82.11  ? 347  TYR A CD1 1 
ATOM   2634  C  CD2 . TYR A 1 347  ? -39.496  61.433  25.862  1.00 84.62  ? 347  TYR A CD2 1 
ATOM   2635  C  CE1 . TYR A 1 347  ? -37.776  62.427  27.798  1.00 84.21  ? 347  TYR A CE1 1 
ATOM   2636  C  CE2 . TYR A 1 347  ? -38.142  61.104  25.807  1.00 86.43  ? 347  TYR A CE2 1 
ATOM   2637  C  CZ  . TYR A 1 347  ? -37.279  61.601  26.784  1.00 87.22  ? 347  TYR A CZ  1 
ATOM   2638  O  OH  . TYR A 1 347  ? -35.926  61.269  26.771  1.00 89.16  ? 347  TYR A OH  1 
ATOM   2639  N  N   . VAL A 1 348  ? -43.385  63.190  29.452  1.00 83.86  ? 348  VAL A N   1 
ATOM   2640  C  CA  . VAL A 1 348  ? -44.493  63.989  29.972  1.00 87.79  ? 348  VAL A CA  1 
ATOM   2641  C  C   . VAL A 1 348  ? -44.066  65.338  30.524  1.00 89.19  ? 348  VAL A C   1 
ATOM   2642  O  O   . VAL A 1 348  ? -43.153  65.423  31.346  1.00 90.26  ? 348  VAL A O   1 
ATOM   2643  C  CB  . VAL A 1 348  ? -45.284  63.251  31.062  1.00 91.24  ? 348  VAL A CB  1 
ATOM   2644  C  CG1 . VAL A 1 348  ? -46.246  64.218  31.751  1.00 91.42  ? 348  VAL A CG1 1 
ATOM   2645  C  CG2 . VAL A 1 348  ? -46.064  62.128  30.451  1.00 93.41  ? 348  VAL A CG2 1 
ATOM   2646  N  N   . LEU A 1 349  ? -44.730  66.396  30.080  1.00 87.78  ? 349  LEU A N   1 
ATOM   2647  C  CA  . LEU A 1 349  ? -44.449  67.691  30.650  1.00 88.39  ? 349  LEU A CA  1 
ATOM   2648  C  C   . LEU A 1 349  ? -44.995  67.716  32.079  1.00 83.98  ? 349  LEU A C   1 
ATOM   2649  O  O   . LEU A 1 349  ? -44.261  67.964  33.048  1.00 81.29  ? 349  LEU A O   1 
ATOM   2650  C  CB  . LEU A 1 349  ? -45.117  68.771  29.802  1.00 94.02  ? 349  LEU A CB  1 
ATOM   2651  C  CG  . LEU A 1 349  ? -44.623  70.225  29.908  1.00 96.31  ? 349  LEU A CG  1 
ATOM   2652  C  CD1 . LEU A 1 349  ? -45.634  71.111  30.642  1.00 96.45  ? 349  LEU A CD1 1 
ATOM   2653  C  CD2 . LEU A 1 349  ? -43.209  70.292  30.519  1.00 96.17  ? 349  LEU A CD2 1 
ATOM   2654  N  N   . SER A 1 350  ? -46.285  67.419  32.195  1.00 78.89  ? 350  SER A N   1 
ATOM   2655  C  CA  . SER A 1 350  ? -47.006  67.600  33.438  1.00 76.49  ? 350  SER A CA  1 
ATOM   2656  C  C   . SER A 1 350  ? -47.816  66.370  33.760  1.00 76.40  ? 350  SER A C   1 
ATOM   2657  O  O   . SER A 1 350  ? -48.548  65.853  32.938  1.00 78.84  ? 350  SER A O   1 
ATOM   2658  C  CB  . SER A 1 350  ? -47.944  68.790  33.323  1.00 76.59  ? 350  SER A CB  1 
ATOM   2659  O  OG  . SER A 1 350  ? -48.898  68.804  34.378  1.00 76.36  ? 350  SER A OG  1 
ATOM   2660  N  N   . PRO A 1 351  ? -47.705  65.895  34.986  1.00 74.37  ? 351  PRO A N   1 
ATOM   2661  C  CA  . PRO A 1 351  ? -48.253  64.566  35.205  1.00 75.11  ? 351  PRO A CA  1 
ATOM   2662  C  C   . PRO A 1 351  ? -49.755  64.562  35.367  1.00 77.09  ? 351  PRO A C   1 
ATOM   2663  O  O   . PRO A 1 351  ? -50.291  63.483  35.600  1.00 80.01  ? 351  PRO A O   1 
ATOM   2664  C  CB  . PRO A 1 351  ? -47.586  64.142  36.502  1.00 73.20  ? 351  PRO A CB  1 
ATOM   2665  C  CG  . PRO A 1 351  ? -46.420  65.121  36.672  1.00 71.82  ? 351  PRO A CG  1 
ATOM   2666  C  CD  . PRO A 1 351  ? -46.922  66.363  36.132  1.00 71.93  ? 351  PRO A CD  1 
ATOM   2667  N  N   . TYR A 1 352  ? -50.421  65.712  35.276  1.00 76.44  ? 352  TYR A N   1 
ATOM   2668  C  CA  . TYR A 1 352  ? -51.879  65.706  35.165  1.00 77.51  ? 352  TYR A CA  1 
ATOM   2669  C  C   . TYR A 1 352  ? -52.308  66.128  33.755  1.00 77.23  ? 352  TYR A C   1 
ATOM   2670  O  O   . TYR A 1 352  ? -51.502  66.650  33.002  1.00 74.93  ? 352  TYR A O   1 
ATOM   2671  C  CB  . TYR A 1 352  ? -52.539  66.607  36.219  1.00 79.42  ? 352  TYR A CB  1 
ATOM   2672  C  CG  . TYR A 1 352  ? -52.075  66.428  37.645  1.00 81.11  ? 352  TYR A CG  1 
ATOM   2673  C  CD1 . TYR A 1 352  ? -52.677  65.495  38.483  1.00 82.91  ? 352  TYR A CD1 1 
ATOM   2674  C  CD2 . TYR A 1 352  ? -51.063  67.212  38.167  1.00 82.15  ? 352  TYR A CD2 1 
ATOM   2675  C  CE1 . TYR A 1 352  ? -52.262  65.325  39.808  1.00 83.64  ? 352  TYR A CE1 1 
ATOM   2676  C  CE2 . TYR A 1 352  ? -50.649  67.059  39.477  1.00 84.16  ? 352  TYR A CE2 1 
ATOM   2677  C  CZ  . TYR A 1 352  ? -51.247  66.114  40.294  1.00 84.77  ? 352  TYR A CZ  1 
ATOM   2678  O  OH  . TYR A 1 352  ? -50.805  65.972  41.588  1.00 85.64  ? 352  TYR A OH  1 
ATOM   2679  N  N   . LYS A 1 353  ? -53.577  65.908  33.417  1.00 80.08  ? 353  LYS A N   1 
ATOM   2680  C  CA  . LYS A 1 353  ? -54.162  66.401  32.166  1.00 82.42  ? 353  LYS A CA  1 
ATOM   2681  C  C   . LYS A 1 353  ? -55.637  66.811  32.346  1.00 76.77  ? 353  LYS A C   1 
ATOM   2682  O  O   . LYS A 1 353  ? -56.521  65.979  32.635  1.00 72.23  ? 353  LYS A O   1 
ATOM   2683  C  CB  . LYS A 1 353  ? -54.006  65.352  31.062  1.00 89.36  ? 353  LYS A CB  1 
ATOM   2684  C  CG  . LYS A 1 353  ? -53.908  63.938  31.633  1.00 96.42  ? 353  LYS A CG  1 
ATOM   2685  C  CD  . LYS A 1 353  ? -53.086  62.971  30.766  1.00 102.81 ? 353  LYS A CD  1 
ATOM   2686  C  CE  . LYS A 1 353  ? -53.954  62.127  29.823  1.00 106.75 ? 353  LYS A CE  1 
ATOM   2687  N  NZ  . LYS A 1 353  ? -53.133  61.285  28.890  1.00 108.77 ? 353  LYS A NZ  1 
ATOM   2688  N  N   . LEU A 1 354  ? -55.883  68.108  32.190  1.00 75.76  ? 354  LEU A N   1 
ATOM   2689  C  CA  . LEU A 1 354  ? -57.225  68.661  32.308  1.00 76.34  ? 354  LEU A CA  1 
ATOM   2690  C  C   . LEU A 1 354  ? -58.017  68.482  31.031  1.00 75.70  ? 354  LEU A C   1 
ATOM   2691  O  O   . LEU A 1 354  ? -57.467  68.554  29.933  1.00 76.92  ? 354  LEU A O   1 
ATOM   2692  C  CB  . LEU A 1 354  ? -57.178  70.169  32.551  1.00 78.03  ? 354  LEU A CB  1 
ATOM   2693  C  CG  . LEU A 1 354  ? -56.097  70.920  33.319  1.00 76.50  ? 354  LEU A CG  1 
ATOM   2694  C  CD1 . LEU A 1 354  ? -56.214  70.479  34.731  1.00 77.94  ? 354  LEU A CD1 1 
ATOM   2695  C  CD2 . LEU A 1 354  ? -54.719  70.659  32.773  1.00 75.27  ? 354  LEU A CD2 1 
ATOM   2696  N  N   . ASN A 1 355  ? -59.320  68.322  31.180  1.00 74.89  ? 355  ASN A N   1 
ATOM   2697  C  CA  . ASN A 1 355  ? -60.208  68.331  30.049  1.00 77.46  ? 355  ASN A CA  1 
ATOM   2698  C  C   . ASN A 1 355  ? -61.588  68.625  30.539  1.00 76.71  ? 355  ASN A C   1 
ATOM   2699  O  O   . ASN A 1 355  ? -62.081  67.936  31.425  1.00 72.57  ? 355  ASN A O   1 
ATOM   2700  C  CB  . ASN A 1 355  ? -60.229  66.984  29.359  1.00 87.00  ? 355  ASN A CB  1 
ATOM   2701  C  CG  . ASN A 1 355  ? -60.560  65.852  30.297  1.00 92.45  ? 355  ASN A CG  1 
ATOM   2702  O  OD1 . ASN A 1 355  ? -59.669  65.293  30.956  1.00 94.30  ? 355  ASN A OD1 1 
ATOM   2703  N  ND2 . ASN A 1 355  ? -61.838  65.477  30.346  1.00 95.25  ? 355  ASN A ND2 1 
ATOM   2704  N  N   . LEU A 1 356  ? -62.203  69.658  29.975  1.00 76.03  ? 356  LEU A N   1 
ATOM   2705  C  CA  . LEU A 1 356  ? -63.541  70.073  30.361  1.00 74.57  ? 356  LEU A CA  1 
ATOM   2706  C  C   . LEU A 1 356  ? -64.448  68.856  30.308  1.00 76.80  ? 356  LEU A C   1 
ATOM   2707  O  O   . LEU A 1 356  ? -64.118  67.883  29.627  1.00 80.06  ? 356  LEU A O   1 
ATOM   2708  C  CB  . LEU A 1 356  ? -64.011  71.139  29.381  1.00 77.86  ? 356  LEU A CB  1 
ATOM   2709  C  CG  . LEU A 1 356  ? -63.186  72.425  29.424  1.00 76.18  ? 356  LEU A CG  1 
ATOM   2710  C  CD1 . LEU A 1 356  ? -63.817  73.539  28.588  1.00 76.74  ? 356  LEU A CD1 1 
ATOM   2711  C  CD2 . LEU A 1 356  ? -63.106  72.815  30.875  1.00 76.85  ? 356  LEU A CD2 1 
ATOM   2712  N  N   . VAL A 1 357  ? -65.573  68.891  31.019  1.00 78.13  ? 357  VAL A N   1 
ATOM   2713  C  CA  . VAL A 1 357  ? -66.464  67.737  31.073  1.00 80.68  ? 357  VAL A CA  1 
ATOM   2714  C  C   . VAL A 1 357  ? -67.904  68.138  30.939  1.00 87.42  ? 357  VAL A C   1 
ATOM   2715  O  O   . VAL A 1 357  ? -68.441  68.813  31.797  1.00 81.73  ? 357  VAL A O   1 
ATOM   2716  C  CB  . VAL A 1 357  ? -66.396  67.026  32.396  1.00 75.83  ? 357  VAL A CB  1 
ATOM   2717  C  CG1 . VAL A 1 357  ? -67.644  66.171  32.563  1.00 77.28  ? 357  VAL A CG1 1 
ATOM   2718  C  CG2 . VAL A 1 357  ? -65.140  66.191  32.470  1.00 74.92  ? 357  VAL A CG2 1 
ATOM   2719  N  N   . ALA A 1 358  ? -68.547  67.703  29.868  1.00 89.74  ? 358  ALA A N   1 
ATOM   2720  C  CA  . ALA A 1 358  ? -69.919  68.128  29.612  1.00 93.73  ? 358  ALA A CA  1 
ATOM   2721  C  C   . ALA A 1 358  ? -70.146  69.579  30.106  1.00 93.29  ? 358  ALA A C   1 
ATOM   2722  O  O   . ALA A 1 358  ? -70.996  69.873  30.952  1.00 89.52  ? 358  ALA A O   1 
ATOM   2723  C  CB  . ALA A 1 358  ? -70.923  67.128  30.189  1.00 97.56  ? 358  ALA A CB  1 
ATOM   2724  N  N   . THR A 1 359  ? -69.324  70.474  29.566  1.00 91.97  ? 359  THR A N   1 
ATOM   2725  C  CA  . THR A 1 359  ? -69.499  71.905  29.763  1.00 92.87  ? 359  THR A CA  1 
ATOM   2726  C  C   . THR A 1 359  ? -69.390  72.699  28.454  1.00 90.01  ? 359  THR A C   1 
ATOM   2727  O  O   . THR A 1 359  ? -68.290  73.154  28.078  1.00 85.68  ? 359  THR A O   1 
ATOM   2728  C  CB  . THR A 1 359  ? -68.518  72.457  30.787  1.00 94.85  ? 359  THR A CB  1 
ATOM   2729  O  OG1 . THR A 1 359  ? -67.181  72.238  30.330  1.00 95.37  ? 359  THR A OG1 1 
ATOM   2730  C  CG2 . THR A 1 359  ? -68.759  71.776  32.138  1.00 93.79  ? 359  THR A CG2 1 
ATOM   2731  N  N   . PRO A 1 360  ? -70.560  72.890  27.793  1.00 91.02  ? 360  PRO A N   1 
ATOM   2732  C  CA  . PRO A 1 360  ? -70.846  73.506  26.495  1.00 90.44  ? 360  PRO A CA  1 
ATOM   2733  C  C   . PRO A 1 360  ? -70.131  74.813  26.376  1.00 90.31  ? 360  PRO A C   1 
ATOM   2734  O  O   . PRO A 1 360  ? -70.029  75.524  27.369  1.00 83.27  ? 360  PRO A O   1 
ATOM   2735  C  CB  . PRO A 1 360  ? -72.335  73.767  26.572  1.00 92.14  ? 360  PRO A CB  1 
ATOM   2736  C  CG  . PRO A 1 360  ? -72.860  72.712  27.446  1.00 92.82  ? 360  PRO A CG  1 
ATOM   2737  C  CD  . PRO A 1 360  ? -71.802  72.443  28.457  1.00 91.58  ? 360  PRO A CD  1 
ATOM   2738  N  N   . LEU A 1 361  ? -69.657  75.131  25.181  1.00 92.29  ? 361  LEU A N   1 
ATOM   2739  C  CA  . LEU A 1 361  ? -68.766  76.272  25.021  1.00 94.40  ? 361  LEU A CA  1 
ATOM   2740  C  C   . LEU A 1 361  ? -69.403  77.546  24.500  1.00 103.84 ? 361  LEU A C   1 
ATOM   2741  O  O   . LEU A 1 361  ? -68.763  78.380  23.855  1.00 103.18 ? 361  LEU A O   1 
ATOM   2742  C  CB  . LEU A 1 361  ? -67.574  75.888  24.183  1.00 91.83  ? 361  LEU A CB  1 
ATOM   2743  C  CG  . LEU A 1 361  ? -66.474  75.480  25.155  1.00 89.02  ? 361  LEU A CG  1 
ATOM   2744  C  CD1 . LEU A 1 361  ? -66.634  74.040  25.690  1.00 85.77  ? 361  LEU A CD1 1 
ATOM   2745  C  CD2 . LEU A 1 361  ? -65.145  75.681  24.466  1.00 90.43  ? 361  LEU A CD2 1 
ATOM   2746  N  N   . PHE A 1 362  ? -70.676  77.684  24.828  1.00 111.36 ? 362  PHE A N   1 
ATOM   2747  C  CA  . PHE A 1 362  ? -71.475  78.808  24.404  1.00 118.52 ? 362  PHE A CA  1 
ATOM   2748  C  C   . PHE A 1 362  ? -72.209  79.320  25.604  1.00 110.62 ? 362  PHE A C   1 
ATOM   2749  O  O   . PHE A 1 362  ? -72.832  78.555  26.342  1.00 107.00 ? 362  PHE A O   1 
ATOM   2750  C  CB  . PHE A 1 362  ? -72.499  78.366  23.366  1.00 132.64 ? 362  PHE A CB  1 
ATOM   2751  C  CG  . PHE A 1 362  ? -71.889  77.784  22.143  1.00 143.99 ? 362  PHE A CG  1 
ATOM   2752  C  CD1 . PHE A 1 362  ? -72.261  76.535  21.696  1.00 147.68 ? 362  PHE A CD1 1 
ATOM   2753  C  CD2 . PHE A 1 362  ? -70.917  78.488  21.450  1.00 148.60 ? 362  PHE A CD2 1 
ATOM   2754  C  CE1 . PHE A 1 362  ? -71.691  76.012  20.568  1.00 152.07 ? 362  PHE A CE1 1 
ATOM   2755  C  CE2 . PHE A 1 362  ? -70.338  77.971  20.327  1.00 152.30 ? 362  PHE A CE2 1 
ATOM   2756  C  CZ  . PHE A 1 362  ? -70.723  76.730  19.882  1.00 153.72 ? 362  PHE A CZ  1 
ATOM   2757  N  N   . LEU A 1 363  ? -72.137  80.622  25.803  1.00 104.80 ? 363  LEU A N   1 
ATOM   2758  C  CA  . LEU A 1 363  ? -72.891  81.219  26.875  1.00 101.26 ? 363  LEU A CA  1 
ATOM   2759  C  C   . LEU A 1 363  ? -74.229  81.755  26.402  1.00 98.57  ? 363  LEU A C   1 
ATOM   2760  O  O   . LEU A 1 363  ? -74.308  82.483  25.437  1.00 97.75  ? 363  LEU A O   1 
ATOM   2761  C  CB  . LEU A 1 363  ? -72.070  82.296  27.584  1.00 97.90  ? 363  LEU A CB  1 
ATOM   2762  C  CG  . LEU A 1 363  ? -70.874  82.813  26.801  1.00 89.12  ? 363  LEU A CG  1 
ATOM   2763  C  CD1 . LEU A 1 363  ? -71.327  83.930  25.925  1.00 91.58  ? 363  LEU A CD1 1 
ATOM   2764  C  CD2 . LEU A 1 363  ? -69.836  83.307  27.745  1.00 87.41  ? 363  LEU A CD2 1 
ATOM   2765  N  N   . LYS A 1 364  ? -75.281  81.310  27.064  1.00 100.94 ? 364  LYS A N   1 
ATOM   2766  C  CA  . LYS A 1 364  ? -76.551  81.987  27.060  1.00 108.00 ? 364  LYS A CA  1 
ATOM   2767  C  C   . LYS A 1 364  ? -76.333  83.127  28.042  1.00 111.71 ? 364  LYS A C   1 
ATOM   2768  O  O   . LYS A 1 364  ? -75.633  82.924  29.044  1.00 108.94 ? 364  LYS A O   1 
ATOM   2769  C  CB  . LYS A 1 364  ? -77.625  81.049  27.596  1.00 110.65 ? 364  LYS A CB  1 
ATOM   2770  C  CG  . LYS A 1 364  ? -77.729  79.722  26.855  1.00 114.69 ? 364  LYS A CG  1 
ATOM   2771  C  CD  . LYS A 1 364  ? -76.546  78.773  27.123  1.00 114.86 ? 364  LYS A CD  1 
ATOM   2772  C  CE  . LYS A 1 364  ? -76.759  77.393  26.467  1.00 116.97 ? 364  LYS A CE  1 
ATOM   2773  N  NZ  . LYS A 1 364  ? -77.575  77.473  25.193  1.00 120.62 ? 364  LYS A NZ  1 
ATOM   2774  N  N   . PRO A 1 365  ? -76.893  84.334  27.764  1.00 117.29 ? 365  PRO A N   1 
ATOM   2775  C  CA  . PRO A 1 365  ? -76.675  85.459  28.679  1.00 119.11 ? 365  PRO A CA  1 
ATOM   2776  C  C   . PRO A 1 365  ? -77.724  85.524  29.791  1.00 123.42 ? 365  PRO A C   1 
ATOM   2777  O  O   . PRO A 1 365  ? -78.826  84.978  29.684  1.00 126.66 ? 365  PRO A O   1 
ATOM   2778  C  CB  . PRO A 1 365  ? -76.766  86.686  27.757  1.00 119.53 ? 365  PRO A CB  1 
ATOM   2779  C  CG  . PRO A 1 365  ? -76.976  86.166  26.391  1.00 118.92 ? 365  PRO A CG  1 
ATOM   2780  C  CD  . PRO A 1 365  ? -77.563  84.801  26.546  1.00 118.59 ? 365  PRO A CD  1 
ATOM   2781  N  N   . GLY A 1 366  ? -77.364  86.198  30.870  1.00 126.63 ? 366  GLY A N   1 
ATOM   2782  C  CA  . GLY A 1 366  ? -78.204  86.193  32.046  1.00 135.40 ? 366  GLY A CA  1 
ATOM   2783  C  C   . GLY A 1 366  ? -78.101  84.866  32.787  1.00 128.38 ? 366  GLY A C   1 
ATOM   2784  O  O   . GLY A 1 366  ? -78.368  84.781  33.996  1.00 128.91 ? 366  GLY A O   1 
ATOM   2785  N  N   . ILE A 1 367  ? -77.724  83.810  32.081  1.00 120.94 ? 367  ILE A N   1 
ATOM   2786  C  CA  . ILE A 1 367  ? -77.530  82.557  32.770  1.00 116.30 ? 367  ILE A CA  1 
ATOM   2787  C  C   . ILE A 1 367  ? -76.084  82.480  33.234  1.00 112.75 ? 367  ILE A C   1 
ATOM   2788  O  O   . ILE A 1 367  ? -75.203  83.021  32.582  1.00 112.61 ? 367  ILE A O   1 
ATOM   2789  C  CB  . ILE A 1 367  ? -77.980  81.381  31.912  1.00 116.99 ? 367  ILE A CB  1 
ATOM   2790  C  CG1 . ILE A 1 367  ? -79.504  81.274  31.960  1.00 117.90 ? 367  ILE A CG1 1 
ATOM   2791  C  CG2 . ILE A 1 367  ? -77.407  80.105  32.444  1.00 114.93 ? 367  ILE A CG2 1 
ATOM   2792  C  CD1 . ILE A 1 367  ? -80.081  80.403  30.910  1.00 118.50 ? 367  ILE A CD1 1 
ATOM   2793  N  N   . PRO A 1 368  ? -75.836  81.851  34.396  1.00 107.08 ? 368  PRO A N   1 
ATOM   2794  C  CA  . PRO A 1 368  ? -74.446  81.826  34.838  1.00 104.24 ? 368  PRO A CA  1 
ATOM   2795  C  C   . PRO A 1 368  ? -73.730  80.661  34.152  1.00 99.30  ? 368  PRO A C   1 
ATOM   2796  O  O   . PRO A 1 368  ? -74.259  79.542  34.110  1.00 101.30 ? 368  PRO A O   1 
ATOM   2797  C  CB  . PRO A 1 368  ? -74.571  81.564  36.345  1.00 100.82 ? 368  PRO A CB  1 
ATOM   2798  C  CG  . PRO A 1 368  ? -76.064  81.279  36.598  1.00 103.10 ? 368  PRO A CG  1 
ATOM   2799  C  CD  . PRO A 1 368  ? -76.681  81.038  35.285  1.00 106.00 ? 368  PRO A CD  1 
ATOM   2800  N  N   . TYR A 1 369  ? -72.550  80.921  33.605  1.00 95.87  ? 369  TYR A N   1 
ATOM   2801  C  CA  . TYR A 1 369  ? -71.820  79.914  32.855  1.00 100.00 ? 369  TYR A CA  1 
ATOM   2802  C  C   . TYR A 1 369  ? -71.049  79.041  33.832  1.00 96.47  ? 369  TYR A C   1 
ATOM   2803  O  O   . TYR A 1 369  ? -70.307  79.574  34.636  1.00 95.58  ? 369  TYR A O   1 
ATOM   2804  C  CB  . TYR A 1 369  ? -70.877  80.626  31.874  1.00 97.96  ? 369  TYR A CB  1 
ATOM   2805  C  CG  . TYR A 1 369  ? -70.124  79.721  30.935  1.00 101.27 ? 369  TYR A CG  1 
ATOM   2806  C  CD1 . TYR A 1 369  ? -70.755  78.656  30.294  1.00 106.22 ? 369  TYR A CD1 1 
ATOM   2807  C  CD2 . TYR A 1 369  ? -68.795  79.941  30.673  1.00 103.56 ? 369  TYR A CD2 1 
ATOM   2808  C  CE1 . TYR A 1 369  ? -70.068  77.823  29.443  1.00 105.95 ? 369  TYR A CE1 1 
ATOM   2809  C  CE2 . TYR A 1 369  ? -68.100  79.125  29.825  1.00 104.95 ? 369  TYR A CE2 1 
ATOM   2810  C  CZ  . TYR A 1 369  ? -68.738  78.066  29.211  1.00 107.52 ? 369  TYR A CZ  1 
ATOM   2811  O  OH  . TYR A 1 369  ? -68.034  77.248  28.359  1.00 110.16 ? 369  TYR A OH  1 
ATOM   2812  N  N   . PRO A 1 370  ? -71.267  77.710  33.794  1.00 81.03  ? 370  PRO A N   1 
ATOM   2813  C  CA  . PRO A 1 370  ? -70.617  76.557  34.470  1.00 79.48  ? 370  PRO A CA  1 
ATOM   2814  C  C   . PRO A 1 370  ? -69.361  76.051  33.767  1.00 87.75  ? 370  PRO A C   1 
ATOM   2815  O  O   . PRO A 1 370  ? -69.365  76.040  32.545  1.00 88.22  ? 370  PRO A O   1 
ATOM   2816  C  CB  . PRO A 1 370  ? -71.658  75.456  34.335  1.00 80.52  ? 370  PRO A CB  1 
ATOM   2817  C  CG  . PRO A 1 370  ? -72.925  76.154  33.899  1.00 85.27  ? 370  PRO A CG  1 
ATOM   2818  C  CD  . PRO A 1 370  ? -72.522  77.326  33.134  1.00 82.83  ? 370  PRO A CD  1 
ATOM   2819  N  N   . ILE A 1 371  ? -68.332  75.594  34.470  1.00 76.63  ? 371  ILE A N   1 
ATOM   2820  C  CA  . ILE A 1 371  ? -67.108  75.135  33.784  1.00 75.60  ? 371  ILE A CA  1 
ATOM   2821  C  C   . ILE A 1 371  ? -66.444  73.930  34.458  1.00 77.47  ? 371  ILE A C   1 
ATOM   2822  O  O   . ILE A 1 371  ? -65.281  74.034  34.807  1.00 75.77  ? 371  ILE A O   1 
ATOM   2823  C  CB  . ILE A 1 371  ? -65.956  76.253  33.668  1.00 76.86  ? 371  ILE A CB  1 
ATOM   2824  C  CG1 . ILE A 1 371  ? -66.300  77.468  32.787  1.00 76.13  ? 371  ILE A CG1 1 
ATOM   2825  C  CG2 . ILE A 1 371  ? -64.652  75.689  33.098  1.00 73.89  ? 371  ILE A CG2 1 
ATOM   2826  C  CD1 . ILE A 1 371  ? -65.181  78.506  32.776  1.00 75.61  ? 371  ILE A CD1 1 
ATOM   2827  N  N   . LYS A 1 372  ? -67.129  72.790  34.636  1.00 76.45  ? 372  LYS A N   1 
ATOM   2828  C  CA  . LYS A 1 372  ? -66.493  71.597  35.283  1.00 73.98  ? 372  LYS A CA  1 
ATOM   2829  C  C   . LYS A 1 372  ? -65.228  71.036  34.600  1.00 73.11  ? 372  LYS A C   1 
ATOM   2830  O  O   . LYS A 1 372  ? -65.358  70.228  33.700  1.00 79.26  ? 372  LYS A O   1 
ATOM   2831  C  CB  . LYS A 1 372  ? -67.484  70.422  35.403  1.00 74.99  ? 372  LYS A CB  1 
ATOM   2832  C  CG  . LYS A 1 372  ? -68.942  70.788  35.209  1.00 82.26  ? 372  LYS A CG  1 
ATOM   2833  C  CD  . LYS A 1 372  ? -69.819  69.552  34.890  1.00 85.67  ? 372  LYS A CD  1 
ATOM   2834  C  CE  . LYS A 1 372  ? -71.173  69.941  34.223  1.00 117.83 ? 372  LYS A CE  1 
ATOM   2835  N  NZ  . LYS A 1 372  ? -72.416  69.583  34.992  1.00 118.13 ? 372  LYS A NZ  1 
ATOM   2836  N  N   . VAL A 1 373  ? -64.020  71.412  35.025  1.00 71.92  ? 373  VAL A N   1 
ATOM   2837  C  CA  . VAL A 1 373  ? -62.810  70.799  34.448  1.00 83.54  ? 373  VAL A CA  1 
ATOM   2838  C  C   . VAL A 1 373  ? -62.552  69.442  35.106  1.00 79.06  ? 373  VAL A C   1 
ATOM   2839  O  O   . VAL A 1 373  ? -63.204  69.125  36.094  1.00 79.57  ? 373  VAL A O   1 
ATOM   2840  C  CB  . VAL A 1 373  ? -61.559  71.693  34.541  1.00 70.34  ? 373  VAL A CB  1 
ATOM   2841  C  CG1 . VAL A 1 373  ? -61.923  73.116  34.267  1.00 70.77  ? 373  VAL A CG1 1 
ATOM   2842  C  CG2 . VAL A 1 373  ? -60.920  71.591  35.876  1.00 69.44  ? 373  VAL A CG2 1 
ATOM   2843  N  N   . GLN A 1 374  ? -61.627  68.634  34.595  1.00 73.27  ? 374  GLN A N   1 
ATOM   2844  C  CA  . GLN A 1 374  ? -61.486  67.295  35.149  1.00 74.99  ? 374  GLN A CA  1 
ATOM   2845  C  C   . GLN A 1 374  ? -60.046  66.792  35.067  1.00 81.80  ? 374  GLN A C   1 
ATOM   2846  O  O   . GLN A 1 374  ? -59.533  66.577  33.976  1.00 87.80  ? 374  GLN A O   1 
ATOM   2847  C  CB  . GLN A 1 374  ? -62.429  66.363  34.420  1.00 74.37  ? 374  GLN A CB  1 
ATOM   2848  C  CG  . GLN A 1 374  ? -62.002  64.928  34.431  1.00 78.66  ? 374  GLN A CG  1 
ATOM   2849  C  CD  . GLN A 1 374  ? -63.054  64.023  33.786  1.00 85.52  ? 374  GLN A CD  1 
ATOM   2850  O  OE1 . GLN A 1 374  ? -62.965  63.675  32.597  1.00 87.12  ? 374  GLN A OE1 1 
ATOM   2851  N  NE2 . GLN A 1 374  ? -64.074  63.651  34.568  1.00 87.78  ? 374  GLN A NE2 1 
ATOM   2852  N  N   . VAL A 1 375  ? -59.378  66.612  36.207  1.00 81.32  ? 375  VAL A N   1 
ATOM   2853  C  CA  . VAL A 1 375  ? -57.949  66.266  36.194  1.00 78.51  ? 375  VAL A CA  1 
ATOM   2854  C  C   . VAL A 1 375  ? -57.710  64.776  36.073  1.00 82.11  ? 375  VAL A C   1 
ATOM   2855  O  O   . VAL A 1 375  ? -58.461  63.973  36.642  1.00 82.91  ? 375  VAL A O   1 
ATOM   2856  C  CB  . VAL A 1 375  ? -57.195  66.721  37.451  1.00 71.26  ? 375  VAL A CB  1 
ATOM   2857  C  CG1 . VAL A 1 375  ? -55.769  66.239  37.369  1.00 69.35  ? 375  VAL A CG1 1 
ATOM   2858  C  CG2 . VAL A 1 375  ? -57.227  68.215  37.592  1.00 68.55  ? 375  VAL A CG2 1 
ATOM   2859  N  N   . LYS A 1 376  ? -56.645  64.423  35.348  1.00 82.63  ? 376  LYS A N   1 
ATOM   2860  C  CA  . LYS A 1 376  ? -56.278  63.030  35.091  1.00 81.37  ? 376  LYS A CA  1 
ATOM   2861  C  C   . LYS A 1 376  ? -54.769  62.894  35.150  1.00 76.39  ? 376  LYS A C   1 
ATOM   2862  O  O   . LYS A 1 376  ? -54.047  63.861  34.926  1.00 71.89  ? 376  LYS A O   1 
ATOM   2863  C  CB  . LYS A 1 376  ? -56.790  62.574  33.720  1.00 83.90  ? 376  LYS A CB  1 
ATOM   2864  C  CG  . LYS A 1 376  ? -58.139  61.864  33.755  1.00 87.38  ? 376  LYS A CG  1 
ATOM   2865  C  CD  . LYS A 1 376  ? -58.838  61.876  32.407  1.00 89.23  ? 376  LYS A CD  1 
ATOM   2866  C  CE  . LYS A 1 376  ? -60.167  61.148  32.446  1.00 90.71  ? 376  LYS A CE  1 
ATOM   2867  N  NZ  . LYS A 1 376  ? -61.066  61.806  31.456  1.00 93.17  ? 376  LYS A NZ  1 
ATOM   2868  N  N   . ASP A 1 377  ? -54.288  61.702  35.474  1.00 78.95  ? 377  ASP A N   1 
ATOM   2869  C  CA  . ASP A 1 377  ? -52.852  61.480  35.546  1.00 82.60  ? 377  ASP A CA  1 
ATOM   2870  C  C   . ASP A 1 377  ? -52.342  60.874  34.292  1.00 88.29  ? 377  ASP A C   1 
ATOM   2871  O  O   . ASP A 1 377  ? -53.086  60.297  33.488  1.00 90.50  ? 377  ASP A O   1 
ATOM   2872  C  CB  . ASP A 1 377  ? -52.484  60.509  36.636  1.00 83.31  ? 377  ASP A CB  1 
ATOM   2873  C  CG  . ASP A 1 377  ? -53.296  59.272  36.570  1.00 87.28  ? 377  ASP A CG  1 
ATOM   2874  O  OD1 . ASP A 1 377  ? -54.336  59.306  35.898  1.00 88.99  ? 377  ASP A OD1 1 
ATOM   2875  O  OD2 . ASP A 1 377  ? -52.914  58.273  37.192  1.00 90.43  ? 377  ASP A OD2 1 
ATOM   2876  N  N   . SER A 1 378  ? -51.033  60.982  34.154  1.00 92.80  ? 378  SER A N   1 
ATOM   2877  C  CA  . SER A 1 378  ? -50.323  60.413  33.031  1.00 95.39  ? 378  SER A CA  1 
ATOM   2878  C  C   . SER A 1 378  ? -50.767  58.944  32.751  1.00 72.79  ? 378  SER A C   1 
ATOM   2879  O  O   . SER A 1 378  ? -50.235  58.293  31.866  1.00 73.69  ? 378  SER A O   1 
ATOM   2880  C  CB  . SER A 1 378  ? -48.797  60.588  33.268  1.00 97.80  ? 378  SER A CB  1 
ATOM   2881  O  OG  . SER A 1 378  ? -48.424  60.791  34.662  1.00 96.92  ? 378  SER A OG  1 
ATOM   2882  N  N   . LEU A 1 379  ? -51.763  58.450  33.490  1.00 75.30  ? 379  LEU A N   1 
ATOM   2883  C  CA  . LEU A 1 379  ? -52.332  57.120  33.261  1.00 80.52  ? 379  LEU A CA  1 
ATOM   2884  C  C   . LEU A 1 379  ? -53.820  57.178  33.041  1.00 88.48  ? 379  LEU A C   1 
ATOM   2885  O  O   . LEU A 1 379  ? -54.509  56.169  33.175  1.00 92.51  ? 379  LEU A O   1 
ATOM   2886  C  CB  . LEU A 1 379  ? -52.043  56.154  34.414  1.00 79.61  ? 379  LEU A CB  1 
ATOM   2887  C  CG  . LEU A 1 379  ? -50.873  55.215  34.116  1.00 80.78  ? 379  LEU A CG  1 
ATOM   2888  C  CD1 . LEU A 1 379  ? -50.229  54.588  35.364  1.00 80.91  ? 379  LEU A CD1 1 
ATOM   2889  C  CD2 . LEU A 1 379  ? -51.311  54.160  33.123  1.00 83.55  ? 379  LEU A CD2 1 
ATOM   2890  N  N   . ASP A 1 380  ? -54.314  58.361  32.715  1.00 91.47  ? 380  ASP A N   1 
ATOM   2891  C  CA  . ASP A 1 380  ? -55.735  58.547  32.489  1.00 96.71  ? 380  ASP A CA  1 
ATOM   2892  C  C   . ASP A 1 380  ? -56.711  57.960  33.524  1.00 99.46  ? 380  ASP A C   1 
ATOM   2893  O  O   . ASP A 1 380  ? -57.818  57.589  33.157  1.00 100.68 ? 380  ASP A O   1 
ATOM   2894  C  CB  . ASP A 1 380  ? -56.111  58.028  31.104  1.00 103.93 ? 380  ASP A CB  1 
ATOM   2895  C  CG  . ASP A 1 380  ? -55.557  58.889  29.989  1.00 110.35 ? 380  ASP A CG  1 
ATOM   2896  O  OD1 . ASP A 1 380  ? -56.147  59.951  29.667  1.00 110.29 ? 380  ASP A OD1 1 
ATOM   2897  O  OD2 . ASP A 1 380  ? -54.534  58.475  29.414  1.00 115.97 ? 380  ASP A OD2 1 
ATOM   2898  N  N   . GLN A 1 381  ? -56.326  57.843  34.793  1.00 101.03 ? 381  GLN A N   1 
ATOM   2899  C  CA  . GLN A 1 381  ? -57.356  57.706  35.835  1.00 102.74 ? 381  GLN A CA  1 
ATOM   2900  C  C   . GLN A 1 381  ? -57.710  59.091  36.373  1.00 98.72  ? 381  GLN A C   1 
ATOM   2901  O  O   . GLN A 1 381  ? -56.957  60.064  36.195  1.00 96.18  ? 381  GLN A O   1 
ATOM   2902  C  CB  . GLN A 1 381  ? -56.977  56.807  37.018  1.00 107.42 ? 381  GLN A CB  1 
ATOM   2903  C  CG  . GLN A 1 381  ? -56.526  55.422  36.683  1.00 113.80 ? 381  GLN A CG  1 
ATOM   2904  C  CD  . GLN A 1 381  ? -55.015  55.307  36.789  1.00 119.18 ? 381  GLN A CD  1 
ATOM   2905  O  OE1 . GLN A 1 381  ? -54.485  54.397  37.439  1.00 122.58 ? 381  GLN A OE1 1 
ATOM   2906  N  NE2 . GLN A 1 381  ? -54.311  56.252  36.173  1.00 119.22 ? 381  GLN A NE2 1 
ATOM   2907  N  N   . LEU A 1 382  ? -58.863  59.178  37.023  1.00 94.23  ? 382  LEU A N   1 
ATOM   2908  C  CA  . LEU A 1 382  ? -59.293  60.442  37.539  1.00 89.94  ? 382  LEU A CA  1 
ATOM   2909  C  C   . LEU A 1 382  ? -58.455  60.691  38.757  1.00 90.61  ? 382  LEU A C   1 
ATOM   2910  O  O   . LEU A 1 382  ? -58.089  59.744  39.431  1.00 94.95  ? 382  LEU A O   1 
ATOM   2911  C  CB  . LEU A 1 382  ? -60.766  60.350  37.856  1.00 89.65  ? 382  LEU A CB  1 
ATOM   2912  C  CG  . LEU A 1 382  ? -61.517  60.666  36.563  1.00 90.25  ? 382  LEU A CG  1 
ATOM   2913  C  CD1 . LEU A 1 382  ? -63.027  60.617  36.754  1.00 92.31  ? 382  LEU A CD1 1 
ATOM   2914  C  CD2 . LEU A 1 382  ? -61.071  62.038  36.032  1.00 87.59  ? 382  LEU A CD2 1 
ATOM   2915  N  N   . VAL A 1 383  ? -58.103  61.941  39.037  1.00 87.08  ? 383  VAL A N   1 
ATOM   2916  C  CA  . VAL A 1 383  ? -57.374  62.225  40.275  1.00 83.73  ? 383  VAL A CA  1 
ATOM   2917  C  C   . VAL A 1 383  ? -57.973  63.408  41.001  1.00 84.28  ? 383  VAL A C   1 
ATOM   2918  O  O   . VAL A 1 383  ? -58.112  64.495  40.453  1.00 84.25  ? 383  VAL A O   1 
ATOM   2919  C  CB  . VAL A 1 383  ? -55.866  62.372  40.046  1.00 78.35  ? 383  VAL A CB  1 
ATOM   2920  C  CG1 . VAL A 1 383  ? -55.571  62.147  38.609  1.00 79.76  ? 383  VAL A CG1 1 
ATOM   2921  C  CG2 . VAL A 1 383  ? -55.365  63.724  40.497  1.00 71.98  ? 383  VAL A CG2 1 
ATOM   2922  N  N   . GLY A 1 384  ? -58.377  63.161  42.238  1.00 86.15  ? 384  GLY A N   1 
ATOM   2923  C  CA  . GLY A 1 384  ? -59.072  64.168  43.007  1.00 86.81  ? 384  GLY A CA  1 
ATOM   2924  C  C   . GLY A 1 384  ? -58.135  64.913  43.924  1.00 88.68  ? 384  GLY A C   1 
ATOM   2925  O  O   . GLY A 1 384  ? -56.993  64.503  44.122  1.00 90.45  ? 384  GLY A O   1 
ATOM   2926  N  N   . GLY A 1 385  ? -58.619  66.016  44.480  1.00 88.91  ? 385  GLY A N   1 
ATOM   2927  C  CA  . GLY A 1 385  ? -57.859  66.783  45.447  1.00 88.40  ? 385  GLY A CA  1 
ATOM   2928  C  C   . GLY A 1 385  ? -56.729  67.578  44.821  1.00 86.67  ? 385  GLY A C   1 
ATOM   2929  O  O   . GLY A 1 385  ? -55.741  67.890  45.489  1.00 87.23  ? 385  GLY A O   1 
ATOM   2930  N  N   . VAL A 1 386  ? -56.845  67.888  43.534  1.00 84.18  ? 386  VAL A N   1 
ATOM   2931  C  CA  . VAL A 1 386  ? -55.883  68.791  42.923  1.00 81.54  ? 386  VAL A CA  1 
ATOM   2932  C  C   . VAL A 1 386  ? -56.502  70.171  42.915  1.00 75.77  ? 386  VAL A C   1 
ATOM   2933  O  O   . VAL A 1 386  ? -57.678  70.335  42.650  1.00 75.70  ? 386  VAL A O   1 
ATOM   2934  C  CB  . VAL A 1 386  ? -55.407  68.356  41.490  1.00 71.38  ? 386  VAL A CB  1 
ATOM   2935  C  CG1 . VAL A 1 386  ? -53.953  68.733  41.290  1.00 69.70  ? 386  VAL A CG1 1 
ATOM   2936  C  CG2 . VAL A 1 386  ? -55.533  66.874  41.295  1.00 72.20  ? 386  VAL A CG2 1 
ATOM   2937  N  N   . PRO A 1 387  ? -55.716  71.171  43.254  1.00 71.82  ? 387  PRO A N   1 
ATOM   2938  C  CA  . PRO A 1 387  ? -56.326  72.481  43.133  1.00 75.28  ? 387  PRO A CA  1 
ATOM   2939  C  C   . PRO A 1 387  ? -56.231  72.883  41.657  1.00 77.97  ? 387  PRO A C   1 
ATOM   2940  O  O   . PRO A 1 387  ? -55.267  72.509  40.993  1.00 79.67  ? 387  PRO A O   1 
ATOM   2941  C  CB  . PRO A 1 387  ? -55.429  73.361  44.028  1.00 75.69  ? 387  PRO A CB  1 
ATOM   2942  C  CG  . PRO A 1 387  ? -54.271  72.423  44.508  1.00 68.01  ? 387  PRO A CG  1 
ATOM   2943  C  CD  . PRO A 1 387  ? -54.300  71.245  43.630  1.00 68.45  ? 387  PRO A CD  1 
ATOM   2944  N  N   . VAL A 1 388  ? -57.202  73.642  41.162  1.00 78.42  ? 388  VAL A N   1 
ATOM   2945  C  CA  . VAL A 1 388  ? -57.252  74.036  39.752  1.00 77.81  ? 388  VAL A CA  1 
ATOM   2946  C  C   . VAL A 1 388  ? -57.672  75.524  39.587  1.00 80.68  ? 388  VAL A C   1 
ATOM   2947  O  O   . VAL A 1 388  ? -58.846  75.859  39.811  1.00 81.79  ? 388  VAL A O   1 
ATOM   2948  C  CB  . VAL A 1 388  ? -58.274  73.123  39.007  1.00 77.87  ? 388  VAL A CB  1 
ATOM   2949  C  CG1 . VAL A 1 388  ? -59.018  73.863  37.913  1.00 79.46  ? 388  VAL A CG1 1 
ATOM   2950  C  CG2 . VAL A 1 388  ? -57.603  71.894  38.459  1.00 76.46  ? 388  VAL A CG2 1 
ATOM   2951  N  N   . THR A 1 389  ? -56.753  76.425  39.212  1.00 79.54  ? 389  THR A N   1 
ATOM   2952  C  CA  . THR A 1 389  ? -57.157  77.837  38.983  1.00 81.04  ? 389  THR A CA  1 
ATOM   2953  C  C   . THR A 1 389  ? -57.886  78.063  37.652  1.00 83.04  ? 389  THR A C   1 
ATOM   2954  O  O   . THR A 1 389  ? -57.694  77.312  36.701  1.00 87.15  ? 389  THR A O   1 
ATOM   2955  C  CB  . THR A 1 389  ? -55.991  78.886  39.160  1.00 93.46  ? 389  THR A CB  1 
ATOM   2956  O  OG1 . THR A 1 389  ? -54.707  78.246  39.107  1.00 93.16  ? 389  THR A OG1 1 
ATOM   2957  C  CG2 . THR A 1 389  ? -56.121  79.626  40.491  1.00 93.21  ? 389  THR A CG2 1 
ATOM   2958  N  N   . LEU A 1 390  ? -58.727  79.085  37.578  1.00 79.34  ? 390  LEU A N   1 
ATOM   2959  C  CA  . LEU A 1 390  ? -59.468  79.321  36.352  1.00 77.57  ? 390  LEU A CA  1 
ATOM   2960  C  C   . LEU A 1 390  ? -59.468  80.797  35.984  1.00 82.81  ? 390  LEU A C   1 
ATOM   2961  O  O   . LEU A 1 390  ? -60.363  81.537  36.408  1.00 88.25  ? 390  LEU A O   1 
ATOM   2962  C  CB  . LEU A 1 390  ? -60.911  78.867  36.524  1.00 74.35  ? 390  LEU A CB  1 
ATOM   2963  C  CG  . LEU A 1 390  ? -61.794  79.451  35.427  1.00 76.37  ? 390  LEU A CG  1 
ATOM   2964  C  CD1 . LEU A 1 390  ? -61.690  78.587  34.236  1.00 80.77  ? 390  LEU A CD1 1 
ATOM   2965  C  CD2 . LEU A 1 390  ? -63.236  79.580  35.802  1.00 73.73  ? 390  LEU A CD2 1 
ATOM   2966  N  N   . ASN A 1 391  ? -58.473  81.246  35.224  1.00 81.09  ? 391  ASN A N   1 
ATOM   2967  C  CA  . ASN A 1 391  ? -58.441  82.637  34.807  1.00 85.19  ? 391  ASN A CA  1 
ATOM   2968  C  C   . ASN A 1 391  ? -59.286  82.776  33.578  1.00 89.32  ? 391  ASN A C   1 
ATOM   2969  O  O   . ASN A 1 391  ? -59.210  81.918  32.706  1.00 91.85  ? 391  ASN A O   1 
ATOM   2970  C  CB  . ASN A 1 391  ? -57.025  83.052  34.475  1.00 88.41  ? 391  ASN A CB  1 
ATOM   2971  C  CG  . ASN A 1 391  ? -56.225  83.401  35.697  1.00 90.93  ? 391  ASN A CG  1 
ATOM   2972  O  OD1 . ASN A 1 391  ? -55.869  82.535  36.502  1.00 89.74  ? 391  ASN A OD1 1 
ATOM   2973  N  ND2 . ASN A 1 391  ? -55.913  84.683  35.836  1.00 93.34  ? 391  ASN A ND2 1 
ATOM   2974  N  N   . ALA A 1 392  ? -60.083  83.840  33.482  1.00 90.40  ? 392  ALA A N   1 
ATOM   2975  C  CA  . ALA A 1 392  ? -60.984  83.990  32.328  1.00 90.84  ? 392  ALA A CA  1 
ATOM   2976  C  C   . ALA A 1 392  ? -61.071  85.421  31.884  1.00 89.86  ? 392  ALA A C   1 
ATOM   2977  O  O   . ALA A 1 392  ? -60.760  86.312  32.650  1.00 90.26  ? 392  ALA A O   1 
ATOM   2978  C  CB  . ALA A 1 392  ? -62.376  83.471  32.649  1.00 91.53  ? 392  ALA A CB  1 
ATOM   2979  N  N   . GLN A 1 393  ? -61.514  85.654  30.657  1.00 91.72  ? 393  GLN A N   1 
ATOM   2980  C  CA  . GLN A 1 393  ? -61.362  86.989  30.082  1.00 97.64  ? 393  GLN A CA  1 
ATOM   2981  C  C   . GLN A 1 393  ? -62.424  87.287  29.020  1.00 99.80  ? 393  GLN A C   1 
ATOM   2982  O  O   . GLN A 1 393  ? -62.850  86.410  28.258  1.00 97.71  ? 393  GLN A O   1 
ATOM   2983  C  CB  . GLN A 1 393  ? -59.917  87.204  29.572  1.00 98.90  ? 393  GLN A CB  1 
ATOM   2984  C  CG  . GLN A 1 393  ? -59.576  88.593  29.111  1.00 100.23 ? 393  GLN A CG  1 
ATOM   2985  C  CD  . GLN A 1 393  ? -60.171  88.904  27.760  1.00 101.75 ? 393  GLN A CD  1 
ATOM   2986  O  OE1 . GLN A 1 393  ? -60.531  90.048  27.479  1.00 103.30 ? 393  GLN A OE1 1 
ATOM   2987  N  NE2 . GLN A 1 393  ? -60.297  87.885  26.915  1.00 101.10 ? 393  GLN A NE2 1 
ATOM   2988  N  N   . THR A 1 394  ? -62.835  88.548  28.988  1.00 103.65 ? 394  THR A N   1 
ATOM   2989  C  CA  . THR A 1 394  ? -64.145  88.889  28.485  1.00 107.94 ? 394  THR A CA  1 
ATOM   2990  C  C   . THR A 1 394  ? -64.241  90.247  27.789  1.00 118.76 ? 394  THR A C   1 
ATOM   2991  O  O   . THR A 1 394  ? -63.606  91.213  28.213  1.00 122.49 ? 394  THR A O   1 
ATOM   2992  C  CB  . THR A 1 394  ? -65.132  88.810  29.657  1.00 101.99 ? 394  THR A CB  1 
ATOM   2993  O  OG1 . THR A 1 394  ? -65.685  87.494  29.687  1.00 99.48  ? 394  THR A OG1 1 
ATOM   2994  C  CG2 . THR A 1 394  ? -66.260  89.801  29.511  1.00 103.45 ? 394  THR A CG2 1 
ATOM   2995  N  N   . ILE A 1 395  ? -65.029  90.322  26.713  1.00 123.08 ? 395  ILE A N   1 
ATOM   2996  C  CA  . ILE A 1 395  ? -65.369  91.626  26.161  1.00 127.88 ? 395  ILE A CA  1 
ATOM   2997  C  C   . ILE A 1 395  ? -66.864  91.824  26.003  1.00 134.12 ? 395  ILE A C   1 
ATOM   2998  O  O   . ILE A 1 395  ? -67.625  90.870  25.806  1.00 135.02 ? 395  ILE A O   1 
ATOM   2999  C  CB  . ILE A 1 395  ? -64.733  91.894  24.817  1.00 128.21 ? 395  ILE A CB  1 
ATOM   3000  C  CG1 . ILE A 1 395  ? -65.447  91.085  23.742  1.00 127.67 ? 395  ILE A CG1 1 
ATOM   3001  C  CG2 . ILE A 1 395  ? -63.242  91.624  24.874  1.00 127.37 ? 395  ILE A CG2 1 
ATOM   3002  C  CD1 . ILE A 1 395  ? -65.779  91.915  22.527  1.00 130.25 ? 395  ILE A CD1 1 
ATOM   3003  N  N   . ASP A 1 396  ? -67.256  93.095  26.093  1.00 137.87 ? 396  ASP A N   1 
ATOM   3004  C  CA  . ASP A 1 396  ? -68.641  93.526  26.110  1.00 140.64 ? 396  ASP A CA  1 
ATOM   3005  C  C   . ASP A 1 396  ? -69.149  93.511  24.702  1.00 142.11 ? 396  ASP A C   1 
ATOM   3006  O  O   . ASP A 1 396  ? -68.365  93.473  23.765  1.00 143.01 ? 396  ASP A O   1 
ATOM   3007  C  CB  . ASP A 1 396  ? -68.724  94.952  26.646  1.00 145.39 ? 396  ASP A CB  1 
ATOM   3008  C  CG  . ASP A 1 396  ? -69.871  95.133  27.615  1.00 151.96 ? 396  ASP A CG  1 
ATOM   3009  O  OD1 . ASP A 1 396  ? -70.276  96.294  27.868  1.00 156.25 ? 396  ASP A OD1 1 
ATOM   3010  O  OD2 . ASP A 1 396  ? -70.368  94.104  28.135  1.00 152.29 ? 396  ASP A OD2 1 
ATOM   3011  N  N   . VAL A 1 397  ? -70.457  93.539  24.527  1.00 144.55 ? 397  VAL A N   1 
ATOM   3012  C  CA  . VAL A 1 397  ? -70.966  93.809  23.196  1.00 148.71 ? 397  VAL A CA  1 
ATOM   3013  C  C   . VAL A 1 397  ? -70.595  95.253  22.861  1.00 152.22 ? 397  VAL A C   1 
ATOM   3014  O  O   . VAL A 1 397  ? -70.484  95.636  21.701  1.00 153.36 ? 397  VAL A O   1 
ATOM   3015  C  CB  . VAL A 1 397  ? -72.486  93.587  23.086  1.00 150.77 ? 397  VAL A CB  1 
ATOM   3016  C  CG1 . VAL A 1 397  ? -73.239  94.758  23.686  1.00 152.18 ? 397  VAL A CG1 1 
ATOM   3017  C  CG2 . VAL A 1 397  ? -72.870  93.376  21.620  1.00 153.02 ? 397  VAL A CG2 1 
ATOM   3018  N  N   . ASN A 1 398  ? -70.379  96.033  23.911  1.00 153.50 ? 398  ASN A N   1 
ATOM   3019  C  CA  . ASN A 1 398  ? -69.967  97.423  23.817  1.00 156.16 ? 398  ASN A CA  1 
ATOM   3020  C  C   . ASN A 1 398  ? -68.500  97.532  23.436  1.00 154.37 ? 398  ASN A C   1 
ATOM   3021  O  O   . ASN A 1 398  ? -67.931  98.620  23.417  1.00 152.93 ? 398  ASN A O   1 
ATOM   3022  C  CB  . ASN A 1 398  ? -70.174  98.084  25.176  1.00 158.51 ? 398  ASN A CB  1 
ATOM   3023  C  CG  . ASN A 1 398  ? -70.592  99.526  25.068  1.00 163.77 ? 398  ASN A CG  1 
ATOM   3024  O  OD1 . ASN A 1 398  ? -70.931  100.006 23.988  1.00 167.90 ? 398  ASN A OD1 1 
ATOM   3025  N  ND2 . ASN A 1 398  ? -70.584  100.230 26.198  1.00 163.30 ? 398  ASN A ND2 1 
ATOM   3026  N  N   . GLN A 1 399  ? -67.883  96.389  23.169  1.00 153.49 ? 399  GLN A N   1 
ATOM   3027  C  CA  . GLN A 1 399  ? -66.480  96.341  22.764  1.00 154.60 ? 399  GLN A CA  1 
ATOM   3028  C  C   . GLN A 1 399  ? -65.485  96.741  23.860  1.00 153.98 ? 399  GLN A C   1 
ATOM   3029  O  O   . GLN A 1 399  ? -64.366  97.173  23.573  1.00 153.55 ? 399  GLN A O   1 
ATOM   3030  C  CB  . GLN A 1 399  ? -66.270  97.141  21.482  1.00 158.15 ? 399  GLN A CB  1 
ATOM   3031  C  CG  . GLN A 1 399  ? -66.810  96.417  20.275  1.00 160.29 ? 399  GLN A CG  1 
ATOM   3032  C  CD  . GLN A 1 399  ? -66.194  95.042  20.135  1.00 158.99 ? 399  GLN A CD  1 
ATOM   3033  O  OE1 . GLN A 1 399  ? -65.090  94.896  19.601  1.00 158.93 ? 399  GLN A OE1 1 
ATOM   3034  N  NE2 . GLN A 1 399  ? -66.906  94.021  20.611  1.00 157.48 ? 399  GLN A NE2 1 
ATOM   3035  N  N   . GLU A 1 400  ? -65.908  96.566  25.113  1.00 153.39 ? 400  GLU A N   1 
ATOM   3036  C  CA  . GLU A 1 400  ? -65.068  96.777  26.292  1.00 152.08 ? 400  GLU A CA  1 
ATOM   3037  C  C   . GLU A 1 400  ? -64.585  95.430  26.847  1.00 145.20 ? 400  GLU A C   1 
ATOM   3038  O  O   . GLU A 1 400  ? -65.309  94.448  26.752  1.00 143.39 ? 400  GLU A O   1 
ATOM   3039  C  CB  . GLU A 1 400  ? -65.891  97.488  27.358  1.00 155.01 ? 400  GLU A CB  1 
ATOM   3040  C  CG  . GLU A 1 400  ? -65.149  98.580  28.087  1.00 159.80 ? 400  GLU A CG  1 
ATOM   3041  C  CD  . GLU A 1 400  ? -66.093  99.560  28.737  1.00 166.08 ? 400  GLU A CD  1 
ATOM   3042  O  OE1 . GLU A 1 400  ? -65.966  100.776 28.462  1.00 168.72 ? 400  GLU A OE1 1 
ATOM   3043  O  OE2 . GLU A 1 400  ? -66.972  99.104  29.507  1.00 167.93 ? 400  GLU A OE2 1 
ATOM   3044  N  N   . THR A 1 401  ? -63.377  95.363  27.415  1.00 141.68 ? 401  THR A N   1 
ATOM   3045  C  CA  . THR A 1 401  ? -62.908  94.100  27.994  1.00 134.83 ? 401  THR A CA  1 
ATOM   3046  C  C   . THR A 1 401  ? -63.065  94.043  29.488  1.00 129.65 ? 401  THR A C   1 
ATOM   3047  O  O   . THR A 1 401  ? -63.507  94.984  30.132  1.00 132.60 ? 401  THR A O   1 
ATOM   3048  C  CB  . THR A 1 401  ? -61.414  93.841  27.826  1.00 133.78 ? 401  THR A CB  1 
ATOM   3049  O  OG1 . THR A 1 401  ? -60.693  94.740  28.678  1.00 133.65 ? 401  THR A OG1 1 
ATOM   3050  C  CG2 . THR A 1 401  ? -60.965  93.971  26.387  1.00 136.28 ? 401  THR A CG2 1 
ATOM   3051  N  N   . SER A 1 402  ? -62.619  92.921  30.032  1.00 123.13 ? 402  SER A N   1 
ATOM   3052  C  CA  . SER A 1 402  ? -62.650  92.671  31.460  1.00 116.54 ? 402  SER A CA  1 
ATOM   3053  C  C   . SER A 1 402  ? -61.669  91.547  31.796  1.00 109.23 ? 402  SER A C   1 
ATOM   3054  O  O   . SER A 1 402  ? -61.777  90.437  31.284  1.00 104.85 ? 402  SER A O   1 
ATOM   3055  C  CB  . SER A 1 402  ? -64.072  92.292  31.885  1.00 117.54 ? 402  SER A CB  1 
ATOM   3056  O  OG  . SER A 1 402  ? -64.568  91.240  31.068  1.00 117.40 ? 402  SER A OG  1 
ATOM   3057  N  N   . ASP A 1 403  ? -60.695  91.847  32.642  1.00 106.20 ? 403  ASP A N   1 
ATOM   3058  C  CA  . ASP A 1 403  ? -59.794  90.820  33.111  1.00 103.67 ? 403  ASP A CA  1 
ATOM   3059  C  C   . ASP A 1 403  ? -60.239  90.283  34.454  1.00 100.04 ? 403  ASP A C   1 
ATOM   3060  O  O   . ASP A 1 403  ? -59.808  90.739  35.523  1.00 101.02 ? 403  ASP A O   1 
ATOM   3061  C  CB  . ASP A 1 403  ? -58.384  91.333  33.202  1.00 107.43 ? 403  ASP A CB  1 
ATOM   3062  C  CG  . ASP A 1 403  ? -57.582  90.973  32.007  1.00 111.23 ? 403  ASP A CG  1 
ATOM   3063  O  OD1 . ASP A 1 403  ? -57.426  89.741  31.734  1.00 108.91 ? 403  ASP A OD1 1 
ATOM   3064  O  OD2 . ASP A 1 403  ? -57.109  91.940  31.358  1.00 115.31 ? 403  ASP A OD2 1 
ATOM   3065  N  N   . LEU A 1 404  ? -61.108  89.288  34.377  1.00 96.77  ? 404  LEU A N   1 
ATOM   3066  C  CA  . LEU A 1 404  ? -61.617  88.582  35.530  1.00 92.92  ? 404  LEU A CA  1 
ATOM   3067  C  C   . LEU A 1 404  ? -60.618  88.348  36.655  1.00 92.88  ? 404  LEU A C   1 
ATOM   3068  O  O   . LEU A 1 404  ? -59.389  88.346  36.473  1.00 94.25  ? 404  LEU A O   1 
ATOM   3069  C  CB  . LEU A 1 404  ? -62.177  87.245  35.065  1.00 86.58  ? 404  LEU A CB  1 
ATOM   3070  C  CG  . LEU A 1 404  ? -63.491  87.467  34.332  1.00 84.44  ? 404  LEU A CG  1 
ATOM   3071  C  CD1 . LEU A 1 404  ? -64.177  86.160  34.008  1.00 79.72  ? 404  LEU A CD1 1 
ATOM   3072  C  CD2 . LEU A 1 404  ? -64.359  88.295  35.221  1.00 81.39  ? 404  LEU A CD2 1 
ATOM   3073  N  N   . ASP A 1 405  ? -61.185  88.165  37.839  1.00 90.98  ? 405  ASP A N   1 
ATOM   3074  C  CA  . ASP A 1 405  ? -60.428  87.701  38.982  1.00 88.10  ? 405  ASP A CA  1 
ATOM   3075  C  C   . ASP A 1 405  ? -60.419  86.179  38.898  1.00 82.42  ? 405  ASP A C   1 
ATOM   3076  O  O   . ASP A 1 405  ? -61.405  85.556  38.477  1.00 81.43  ? 405  ASP A O   1 
ATOM   3077  C  CB  . ASP A 1 405  ? -61.017  88.244  40.299  1.00 93.01  ? 405  ASP A CB  1 
ATOM   3078  C  CG  . ASP A 1 405  ? -60.448  89.635  40.681  1.00 109.70 ? 405  ASP A CG  1 
ATOM   3079  O  OD1 . ASP A 1 405  ? -59.196  89.738  40.664  1.00 111.42 ? 405  ASP A OD1 1 
ATOM   3080  O  OD2 . ASP A 1 405  ? -61.218  90.596  41.010  1.00 108.67 ? 405  ASP A OD2 1 
ATOM   3081  N  N   . PRO A 1 406  ? -59.282  85.583  39.253  1.00 80.64  ? 406  PRO A N   1 
ATOM   3082  C  CA  . PRO A 1 406  ? -58.991  84.171  39.038  1.00 78.70  ? 406  PRO A CA  1 
ATOM   3083  C  C   . PRO A 1 406  ? -59.623  83.415  40.130  1.00 83.04  ? 406  PRO A C   1 
ATOM   3084  O  O   . PRO A 1 406  ? -59.565  83.848  41.283  1.00 87.66  ? 406  PRO A O   1 
ATOM   3085  C  CB  . PRO A 1 406  ? -57.478  84.089  39.216  1.00 77.69  ? 406  PRO A CB  1 
ATOM   3086  C  CG  . PRO A 1 406  ? -57.005  85.485  39.340  1.00 79.60  ? 406  PRO A CG  1 
ATOM   3087  C  CD  . PRO A 1 406  ? -58.153  86.277  39.868  1.00 80.01  ? 406  PRO A CD  1 
ATOM   3088  N  N   . SER A 1 407  ? -60.225  82.296  39.796  1.00 83.44  ? 407  SER A N   1 
ATOM   3089  C  CA  . SER A 1 407  ? -60.905  81.535  40.818  1.00 87.21  ? 407  SER A CA  1 
ATOM   3090  C  C   . SER A 1 407  ? -60.103  80.278  40.967  1.00 87.15  ? 407  SER A C   1 
ATOM   3091  O  O   . SER A 1 407  ? -59.284  79.964  40.092  1.00 87.86  ? 407  SER A O   1 
ATOM   3092  C  CB  . SER A 1 407  ? -62.283  81.225  40.316  1.00 90.36  ? 407  SER A CB  1 
ATOM   3093  O  OG  . SER A 1 407  ? -62.425  81.984  39.122  1.00 94.14  ? 407  SER A OG  1 
ATOM   3094  N  N   . LYS A 1 408  ? -60.295  79.574  42.078  1.00 85.29  ? 408  LYS A N   1 
ATOM   3095  C  CA  . LYS A 1 408  ? -59.607  78.307  42.283  1.00 80.54  ? 408  LYS A CA  1 
ATOM   3096  C  C   . LYS A 1 408  ? -60.552  77.412  42.998  1.00 76.30  ? 408  LYS A C   1 
ATOM   3097  O  O   . LYS A 1 408  ? -61.246  77.846  43.908  1.00 77.82  ? 408  LYS A O   1 
ATOM   3098  C  CB  . LYS A 1 408  ? -58.368  78.477  43.134  1.00 80.51  ? 408  LYS A CB  1 
ATOM   3099  C  CG  . LYS A 1 408  ? -57.685  77.179  43.442  1.00 83.52  ? 408  LYS A CG  1 
ATOM   3100  C  CD  . LYS A 1 408  ? -56.326  77.450  44.091  1.00 87.66  ? 408  LYS A CD  1 
ATOM   3101  C  CE  . LYS A 1 408  ? -55.731  78.802  43.640  1.00 89.17  ? 408  LYS A CE  1 
ATOM   3102  N  NZ  . LYS A 1 408  ? -54.256  78.905  43.888  1.00 89.51  ? 408  LYS A NZ  1 
ATOM   3103  N  N   . SER A 1 409  ? -60.623  76.171  42.566  1.00 72.45  ? 409  SER A N   1 
ATOM   3104  C  CA  . SER A 1 409  ? -61.413  75.212  43.308  1.00 75.15  ? 409  SER A CA  1 
ATOM   3105  C  C   . SER A 1 409  ? -60.528  74.022  43.417  1.00 71.95  ? 409  SER A C   1 
ATOM   3106  O  O   . SER A 1 409  ? -59.327  74.105  43.128  1.00 67.67  ? 409  SER A O   1 
ATOM   3107  C  CB  . SER A 1 409  ? -62.754  74.845  42.630  1.00 79.78  ? 409  SER A CB  1 
ATOM   3108  O  OG  . SER A 1 409  ? -63.467  73.802  43.324  1.00 70.30  ? 409  SER A OG  1 
ATOM   3109  N  N   . VAL A 1 410  ? -61.104  72.924  43.867  1.00 70.34  ? 410  VAL A N   1 
ATOM   3110  C  CA  . VAL A 1 410  ? -60.323  71.733  43.919  1.00 73.54  ? 410  VAL A CA  1 
ATOM   3111  C  C   . VAL A 1 410  ? -61.094  70.537  43.421  1.00 78.62  ? 410  VAL A C   1 
ATOM   3112  O  O   . VAL A 1 410  ? -62.324  70.496  43.467  1.00 80.81  ? 410  VAL A O   1 
ATOM   3113  C  CB  . VAL A 1 410  ? -59.820  71.494  45.276  1.00 73.87  ? 410  VAL A CB  1 
ATOM   3114  C  CG1 . VAL A 1 410  ? -58.984  70.228  45.255  1.00 76.18  ? 410  VAL A CG1 1 
ATOM   3115  C  CG2 . VAL A 1 410  ? -59.012  72.702  45.713  1.00 72.27  ? 410  VAL A CG2 1 
ATOM   3116  N  N   . THR A 1 411  ? -60.344  69.573  42.912  1.00 80.10  ? 411  THR A N   1 
ATOM   3117  C  CA  . THR A 1 411  ? -60.917  68.554  42.081  1.00 79.02  ? 411  THR A CA  1 
ATOM   3118  C  C   . THR A 1 411  ? -61.559  67.601  43.037  1.00 78.33  ? 411  THR A C   1 
ATOM   3119  O  O   . THR A 1 411  ? -60.915  67.201  43.981  1.00 74.59  ? 411  THR A O   1 
ATOM   3120  C  CB  . THR A 1 411  ? -59.807  67.918  41.221  1.00 80.11  ? 411  THR A CB  1 
ATOM   3121  O  OG1 . THR A 1 411  ? -60.372  67.040  40.252  1.00 84.06  ? 411  THR A OG1 1 
ATOM   3122  C  CG2 . THR A 1 411  ? -58.865  67.171  42.063  1.00 77.24  ? 411  THR A CG2 1 
ATOM   3123  N  N   . ARG A 1 412  ? -62.835  67.284  42.828  1.00 83.70  ? 412  ARG A N   1 
ATOM   3124  C  CA  . ARG A 1 412  ? -63.553  66.404  43.750  1.00 94.07  ? 412  ARG A CA  1 
ATOM   3125  C  C   . ARG A 1 412  ? -62.855  65.061  43.888  1.00 95.32  ? 412  ARG A C   1 
ATOM   3126  O  O   . ARG A 1 412  ? -62.016  64.740  43.062  1.00 95.84  ? 412  ARG A O   1 
ATOM   3127  C  CB  . ARG A 1 412  ? -64.998  66.196  43.320  1.00 104.67 ? 412  ARG A CB  1 
ATOM   3128  C  CG  . ARG A 1 412  ? -65.793  65.400  44.348  1.00 115.98 ? 412  ARG A CG  1 
ATOM   3129  C  CD  . ARG A 1 412  ? -67.250  65.256  43.954  1.00 126.00 ? 412  ARG A CD  1 
ATOM   3130  N  NE  . ARG A 1 412  ? -68.121  66.256  44.561  1.00 133.58 ? 412  ARG A NE  1 
ATOM   3131  C  CZ  . ARG A 1 412  ? -69.445  66.243  44.438  1.00 139.98 ? 412  ARG A CZ  1 
ATOM   3132  N  NH1 . ARG A 1 412  ? -70.035  65.284  43.729  1.00 142.06 ? 412  ARG A NH1 1 
ATOM   3133  N  NH2 . ARG A 1 412  ? -70.178  67.184  45.020  1.00 142.62 ? 412  ARG A NH2 1 
ATOM   3134  N  N   . VAL A 1 413  ? -63.185  64.287  44.922  1.00 96.77  ? 413  VAL A N   1 
ATOM   3135  C  CA  . VAL A 1 413  ? -62.472  63.039  45.206  1.00 98.19  ? 413  VAL A CA  1 
ATOM   3136  C  C   . VAL A 1 413  ? -63.032  61.828  44.470  1.00 99.75  ? 413  VAL A C   1 
ATOM   3137  O  O   . VAL A 1 413  ? -62.294  60.968  43.999  1.00 99.38  ? 413  VAL A O   1 
ATOM   3138  C  CB  . VAL A 1 413  ? -62.515  62.738  46.693  1.00 101.75 ? 413  VAL A CB  1 
ATOM   3139  C  CG1 . VAL A 1 413  ? -61.545  61.597  47.044  1.00 102.18 ? 413  VAL A CG1 1 
ATOM   3140  C  CG2 . VAL A 1 413  ? -62.240  64.014  47.501  1.00 101.24 ? 413  VAL A CG2 1 
ATOM   3141  N  N   . ASP A 1 414  ? -64.355  61.772  44.410  1.00 103.91 ? 414  ASP A N   1 
ATOM   3142  C  CA  . ASP A 1 414  ? -65.099  60.674  43.797  1.00 106.04 ? 414  ASP A CA  1 
ATOM   3143  C  C   . ASP A 1 414  ? -65.315  61.000  42.358  1.00 102.22 ? 414  ASP A C   1 
ATOM   3144  O  O   . ASP A 1 414  ? -65.721  60.151  41.579  1.00 102.94 ? 414  ASP A O   1 
ATOM   3145  C  CB  . ASP A 1 414  ? -66.502  60.607  44.390  1.00 111.83 ? 414  ASP A CB  1 
ATOM   3146  C  CG  . ASP A 1 414  ? -67.217  61.955  44.315  1.00 115.42 ? 414  ASP A CG  1 
ATOM   3147  O  OD1 . ASP A 1 414  ? -66.884  62.846  45.135  1.00 116.15 ? 414  ASP A OD1 1 
ATOM   3148  O  OD2 . ASP A 1 414  ? -68.092  62.133  43.437  1.00 116.65 ? 414  ASP A OD2 1 
ATOM   3149  N  N   . ASP A 1 415  ? -65.102  62.267  42.037  1.00 99.71  ? 415  ASP A N   1 
ATOM   3150  C  CA  . ASP A 1 415  ? -65.590  62.849  40.808  1.00 98.46  ? 415  ASP A CA  1 
ATOM   3151  C  C   . ASP A 1 415  ? -64.453  62.977  39.814  1.00 89.36  ? 415  ASP A C   1 
ATOM   3152  O  O   . ASP A 1 415  ? -64.625  62.721  38.621  1.00 86.49  ? 415  ASP A O   1 
ATOM   3153  C  CB  . ASP A 1 415  ? -66.172  64.224  41.132  1.00 105.84 ? 415  ASP A CB  1 
ATOM   3154  C  CG  . ASP A 1 415  ? -67.077  64.744  40.048  1.00 112.63 ? 415  ASP A CG  1 
ATOM   3155  O  OD1 . ASP A 1 415  ? -67.151  64.051  39.008  1.00 116.23 ? 415  ASP A OD1 1 
ATOM   3156  O  OD2 . ASP A 1 415  ? -67.700  65.832  40.223  1.00 113.60 ? 415  ASP A OD2 1 
ATOM   3157  N  N   . GLY A 1 416  ? -63.290  63.348  40.342  1.00 83.27  ? 416  GLY A N   1 
ATOM   3158  C  CA  . GLY A 1 416  ? -62.165  63.799  39.560  1.00 81.42  ? 416  GLY A CA  1 
ATOM   3159  C  C   . GLY A 1 416  ? -62.426  65.192  38.983  1.00 83.99  ? 416  GLY A C   1 
ATOM   3160  O  O   . GLY A 1 416  ? -61.597  65.741  38.255  1.00 86.01  ? 416  GLY A O   1 
ATOM   3161  N  N   . VAL A 1 417  ? -63.576  65.779  39.285  1.00 82.09  ? 417  VAL A N   1 
ATOM   3162  C  CA  . VAL A 1 417  ? -63.954  67.019  38.623  1.00 81.60  ? 417  VAL A CA  1 
ATOM   3163  C  C   . VAL A 1 417  ? -63.706  68.247  39.455  1.00 79.53  ? 417  VAL A C   1 
ATOM   3164  O  O   . VAL A 1 417  ? -64.006  68.277  40.639  1.00 79.34  ? 417  VAL A O   1 
ATOM   3165  C  CB  . VAL A 1 417  ? -65.439  67.017  38.307  1.00 86.57  ? 417  VAL A CB  1 
ATOM   3166  C  CG1 . VAL A 1 417  ? -65.925  68.443  38.084  1.00 86.85  ? 417  VAL A CG1 1 
ATOM   3167  C  CG2 . VAL A 1 417  ? -65.743  66.095  37.109  1.00 89.11  ? 417  VAL A CG2 1 
ATOM   3168  N  N   . ALA A 1 418  ? -63.180  69.281  38.840  1.00 79.91  ? 418  ALA A N   1 
ATOM   3169  C  CA  . ALA A 1 418  ? -63.081  70.547  39.529  1.00 82.20  ? 418  ALA A CA  1 
ATOM   3170  C  C   . ALA A 1 418  ? -64.066  71.528  38.910  1.00 83.11  ? 418  ALA A C   1 
ATOM   3171  O  O   . ALA A 1 418  ? -63.787  72.088  37.854  1.00 82.89  ? 418  ALA A O   1 
ATOM   3172  C  CB  . ALA A 1 418  ? -61.661  71.076  39.411  1.00 81.94  ? 418  ALA A CB  1 
ATOM   3173  N  N   . SER A 1 419  ? -65.209  71.743  39.554  1.00 84.68  ? 419  SER A N   1 
ATOM   3174  C  CA  . SER A 1 419  ? -66.306  72.513  38.936  1.00 87.27  ? 419  SER A CA  1 
ATOM   3175  C  C   . SER A 1 419  ? -66.242  74.018  39.194  1.00 84.00  ? 419  SER A C   1 
ATOM   3176  O  O   . SER A 1 419  ? -66.128  74.432  40.332  1.00 84.63  ? 419  SER A O   1 
ATOM   3177  C  CB  . SER A 1 419  ? -67.684  71.994  39.419  1.00 92.15  ? 419  SER A CB  1 
ATOM   3178  O  OG  . SER A 1 419  ? -67.650  70.636  39.891  1.00 93.43  ? 419  SER A OG  1 
ATOM   3179  N  N   . PHE A 1 420  ? -66.339  74.844  38.163  1.00 81.56  ? 420  PHE A N   1 
ATOM   3180  C  CA  . PHE A 1 420  ? -66.495  76.284  38.406  1.00 87.56  ? 420  PHE A CA  1 
ATOM   3181  C  C   . PHE A 1 420  ? -67.833  76.899  37.994  1.00 93.67  ? 420  PHE A C   1 
ATOM   3182  O  O   . PHE A 1 420  ? -68.726  76.213  37.486  1.00 100.48 ? 420  PHE A O   1 
ATOM   3183  C  CB  . PHE A 1 420  ? -65.442  77.061  37.681  1.00 86.03  ? 420  PHE A CB  1 
ATOM   3184  C  CG  . PHE A 1 420  ? -64.105  76.710  38.072  1.00 71.73  ? 420  PHE A CG  1 
ATOM   3185  C  CD1 . PHE A 1 420  ? -63.253  77.662  38.559  1.00 71.26  ? 420  PHE A CD1 1 
ATOM   3186  C  CD2 . PHE A 1 420  ? -63.688  75.429  37.961  1.00 71.10  ? 420  PHE A CD2 1 
ATOM   3187  C  CE1 . PHE A 1 420  ? -61.989  77.340  38.919  1.00 73.27  ? 420  PHE A CE1 1 
ATOM   3188  C  CE2 . PHE A 1 420  ? -62.429  75.098  38.307  1.00 75.69  ? 420  PHE A CE2 1 
ATOM   3189  C  CZ  . PHE A 1 420  ? -61.568  76.057  38.794  1.00 74.54  ? 420  PHE A CZ  1 
ATOM   3190  N  N   . VAL A 1 421  ? -67.950  78.209  38.221  1.00 90.87  ? 421  VAL A N   1 
ATOM   3191  C  CA  . VAL A 1 421  ? -69.032  79.012  37.657  1.00 87.09  ? 421  VAL A CA  1 
ATOM   3192  C  C   . VAL A 1 421  ? -68.700  80.466  37.808  1.00 87.31  ? 421  VAL A C   1 
ATOM   3193  O  O   . VAL A 1 421  ? -68.305  80.910  38.888  1.00 88.56  ? 421  VAL A O   1 
ATOM   3194  C  CB  . VAL A 1 421  ? -70.371  78.817  38.363  1.00 84.35  ? 421  VAL A CB  1 
ATOM   3195  C  CG1 . VAL A 1 421  ? -71.158  80.134  38.377  1.00 84.42  ? 421  VAL A CG1 1 
ATOM   3196  C  CG2 . VAL A 1 421  ? -71.159  77.708  37.711  1.00 82.70  ? 421  VAL A CG2 1 
ATOM   3197  N  N   . LEU A 1 422  ? -68.850  81.200  36.710  1.00 86.83  ? 422  LEU A N   1 
ATOM   3198  C  CA  . LEU A 1 422  ? -68.663  82.638  36.710  1.00 87.75  ? 422  LEU A CA  1 
ATOM   3199  C  C   . LEU A 1 422  ? -69.947  83.230  36.221  1.00 93.76  ? 422  LEU A C   1 
ATOM   3200  O  O   . LEU A 1 422  ? -70.612  82.650  35.362  1.00 94.12  ? 422  LEU A O   1 
ATOM   3201  C  CB  . LEU A 1 422  ? -67.474  83.099  35.854  1.00 86.30  ? 422  LEU A CB  1 
ATOM   3202  C  CG  . LEU A 1 422  ? -66.676  82.072  35.072  1.00 77.78  ? 422  LEU A CG  1 
ATOM   3203  C  CD1 . LEU A 1 422  ? -67.442  81.728  33.836  1.00 78.95  ? 422  LEU A CD1 1 
ATOM   3204  C  CD2 . LEU A 1 422  ? -65.321  82.645  34.752  1.00 77.15  ? 422  LEU A CD2 1 
ATOM   3205  N  N   . ASN A 1 423  ? -70.319  84.355  36.823  1.00 97.71  ? 423  ASN A N   1 
ATOM   3206  C  CA  . ASN A 1 423  ? -71.578  85.006  36.512  1.00 99.79  ? 423  ASN A CA  1 
ATOM   3207  C  C   . ASN A 1 423  ? -71.364  86.123  35.514  1.00 99.41  ? 423  ASN A C   1 
ATOM   3208  O  O   . ASN A 1 423  ? -70.669  87.091  35.782  1.00 97.18  ? 423  ASN A O   1 
ATOM   3209  C  CB  . ASN A 1 423  ? -72.274  85.445  37.797  1.00 99.97  ? 423  ASN A CB  1 
ATOM   3210  C  CG  . ASN A 1 423  ? -72.350  84.321  38.788  1.00 98.36  ? 423  ASN A CG  1 
ATOM   3211  O  OD1 . ASN A 1 423  ? -73.429  83.812  39.086  1.00 100.44 ? 423  ASN A OD1 1 
ATOM   3212  N  ND2 . ASN A 1 423  ? -71.188  83.864  39.246  1.00 95.21  ? 423  ASN A ND2 1 
ATOM   3213  N  N   . LEU A 1 424  ? -71.950  85.954  34.340  1.00 100.37 ? 424  LEU A N   1 
ATOM   3214  C  CA  . LEU A 1 424  ? -71.551  86.756  33.209  1.00 102.18 ? 424  LEU A CA  1 
ATOM   3215  C  C   . LEU A 1 424  ? -72.463  87.940  32.869  1.00 105.90 ? 424  LEU A C   1 
ATOM   3216  O  O   . LEU A 1 424  ? -73.682  87.790  32.669  1.00 106.77 ? 424  LEU A O   1 
ATOM   3217  C  CB  . LEU A 1 424  ? -71.257  85.859  32.012  1.00 100.75 ? 424  LEU A CB  1 
ATOM   3218  C  CG  . LEU A 1 424  ? -69.841  85.335  32.183  1.00 98.70  ? 424  LEU A CG  1 
ATOM   3219  C  CD1 . LEU A 1 424  ? -69.273  84.803  30.891  1.00 99.77  ? 424  LEU A CD1 1 
ATOM   3220  C  CD2 . LEU A 1 424  ? -68.956  86.440  32.703  1.00 98.01  ? 424  LEU A CD2 1 
ATOM   3221  N  N   . PRO A 1 425  ? -71.850  89.130  32.799  1.00 107.12 ? 425  PRO A N   1 
ATOM   3222  C  CA  . PRO A 1 425  ? -72.606  90.352  32.559  1.00 112.59 ? 425  PRO A CA  1 
ATOM   3223  C  C   . PRO A 1 425  ? -73.373  90.204  31.276  1.00 119.22 ? 425  PRO A C   1 
ATOM   3224  O  O   . PRO A 1 425  ? -72.752  90.223  30.232  1.00 123.85 ? 425  PRO A O   1 
ATOM   3225  C  CB  . PRO A 1 425  ? -71.512  91.390  32.386  1.00 111.12 ? 425  PRO A CB  1 
ATOM   3226  C  CG  . PRO A 1 425  ? -70.309  90.799  33.104  1.00 106.88 ? 425  PRO A CG  1 
ATOM   3227  C  CD  . PRO A 1 425  ? -70.395  89.366  32.859  1.00 103.88 ? 425  PRO A CD  1 
ATOM   3228  N  N   . SER A 1 426  ? -74.687  90.050  31.347  1.00 123.15 ? 426  SER A N   1 
ATOM   3229  C  CA  . SER A 1 426  ? -75.529  89.969  30.148  1.00 127.89 ? 426  SER A CA  1 
ATOM   3230  C  C   . SER A 1 426  ? -74.858  90.406  28.815  1.00 135.98 ? 426  SER A C   1 
ATOM   3231  O  O   . SER A 1 426  ? -74.804  89.629  27.851  1.00 133.87 ? 426  SER A O   1 
ATOM   3232  C  CB  . SER A 1 426  ? -76.841  90.739  30.391  1.00 133.21 ? 426  SER A CB  1 
ATOM   3233  O  OG  . SER A 1 426  ? -76.745  91.601  31.529  1.00 134.63 ? 426  SER A OG  1 
ATOM   3234  N  N   . GLY A 1 427  ? -74.335  91.629  28.771  1.00 138.08 ? 427  GLY A N   1 
ATOM   3235  C  CA  . GLY A 1 427  ? -73.630  92.114  27.595  1.00 139.65 ? 427  GLY A CA  1 
ATOM   3236  C  C   . GLY A 1 427  ? -72.305  91.435  27.252  1.00 135.79 ? 427  GLY A C   1 
ATOM   3237  O  O   . GLY A 1 427  ? -71.422  92.031  26.625  1.00 135.73 ? 427  GLY A O   1 
ATOM   3238  N  N   . VAL A 1 428  ? -72.147  90.185  27.660  1.00 130.71 ? 428  VAL A N   1 
ATOM   3239  C  CA  . VAL A 1 428  ? -70.926  89.468  27.345  1.00 125.55 ? 428  VAL A CA  1 
ATOM   3240  C  C   . VAL A 1 428  ? -71.139  88.672  26.075  1.00 123.58 ? 428  VAL A C   1 
ATOM   3241  O  O   . VAL A 1 428  ? -72.278  88.375  25.714  1.00 125.06 ? 428  VAL A O   1 
ATOM   3242  C  CB  . VAL A 1 428  ? -70.550  88.520  28.446  1.00 122.83 ? 428  VAL A CB  1 
ATOM   3243  C  CG1 . VAL A 1 428  ? -71.506  87.344  28.423  1.00 123.33 ? 428  VAL A CG1 1 
ATOM   3244  C  CG2 . VAL A 1 428  ? -69.106  88.070  28.275  1.00 120.63 ? 428  VAL A CG2 1 
ATOM   3245  N  N   . THR A 1 429  ? -70.031  88.263  25.458  1.00 120.05 ? 429  THR A N   1 
ATOM   3246  C  CA  . THR A 1 429  ? -69.972  87.956  24.031  1.00 119.30 ? 429  THR A CA  1 
ATOM   3247  C  C   . THR A 1 429  ? -69.121  86.715  23.709  1.00 111.09 ? 429  THR A C   1 
ATOM   3248  O  O   . THR A 1 429  ? -69.619  85.630  23.368  1.00 107.81 ? 429  THR A O   1 
ATOM   3249  C  CB  . THR A 1 429  ? -69.267  89.144  23.330  1.00 126.59 ? 429  THR A CB  1 
ATOM   3250  O  OG1 . THR A 1 429  ? -67.929  89.290  23.847  1.00 126.90 ? 429  THR A OG1 1 
ATOM   3251  C  CG2 . THR A 1 429  ? -70.003  90.432  23.625  1.00 130.07 ? 429  THR A CG2 1 
ATOM   3252  N  N   . VAL A 1 430  ? -67.812  86.946  23.747  1.00 107.54 ? 430  VAL A N   1 
ATOM   3253  C  CA  . VAL A 1 430  ? -66.800  85.929  23.779  1.00 102.41 ? 430  VAL A CA  1 
ATOM   3254  C  C   . VAL A 1 430  ? -66.215  86.047  25.172  1.00 103.20 ? 430  VAL A C   1 
ATOM   3255  O  O   . VAL A 1 430  ? -65.854  87.153  25.614  1.00 103.65 ? 430  VAL A O   1 
ATOM   3256  C  CB  . VAL A 1 430  ? -65.664  86.251  22.820  1.00 97.70  ? 430  VAL A CB  1 
ATOM   3257  C  CG1 . VAL A 1 430  ? -64.686  85.092  22.714  1.00 93.99  ? 430  VAL A CG1 1 
ATOM   3258  C  CG2 . VAL A 1 430  ? -66.201  86.566  21.500  1.00 99.40  ? 430  VAL A CG2 1 
ATOM   3259  N  N   . LEU A 1 431  ? -66.163  84.895  25.844  1.00 101.19 ? 431  LEU A N   1 
ATOM   3260  C  CA  . LEU A 1 431  ? -65.372  84.627  27.035  1.00 95.00  ? 431  LEU A CA  1 
ATOM   3261  C  C   . LEU A 1 431  ? -64.184  83.724  26.636  1.00 93.97  ? 431  LEU A C   1 
ATOM   3262  O  O   . LEU A 1 431  ? -64.365  82.709  25.954  1.00 83.51  ? 431  LEU A O   1 
ATOM   3263  C  CB  . LEU A 1 431  ? -66.286  83.921  28.034  1.00 89.07  ? 431  LEU A CB  1 
ATOM   3264  C  CG  . LEU A 1 431  ? -65.944  83.606  29.484  1.00 85.70  ? 431  LEU A CG  1 
ATOM   3265  C  CD1 . LEU A 1 431  ? -66.463  82.216  29.722  1.00 81.93  ? 431  LEU A CD1 1 
ATOM   3266  C  CD2 . LEU A 1 431  ? -64.456  83.672  29.763  1.00 84.40  ? 431  LEU A CD2 1 
ATOM   3267  N  N   . GLU A 1 432  ? -62.977  84.100  27.044  1.00 91.98  ? 432  GLU A N   1 
ATOM   3268  C  CA  . GLU A 1 432  ? -61.810  83.250  26.822  1.00 91.57  ? 432  GLU A CA  1 
ATOM   3269  C  C   . GLU A 1 432  ? -61.225  82.661  28.131  1.00 91.51  ? 432  GLU A C   1 
ATOM   3270  O  O   . GLU A 1 432  ? -60.714  83.404  28.964  1.00 94.61  ? 432  GLU A O   1 
ATOM   3271  C  CB  . GLU A 1 432  ? -60.720  84.057  26.121  1.00 92.67  ? 432  GLU A CB  1 
ATOM   3272  C  CG  . GLU A 1 432  ? -61.080  84.532  24.721  1.00 99.06  ? 432  GLU A CG  1 
ATOM   3273  C  CD  . GLU A 1 432  ? -60.769  83.509  23.629  1.00 102.15 ? 432  GLU A CD  1 
ATOM   3274  O  OE1 . GLU A 1 432  ? -60.220  82.409  23.924  1.00 97.31  ? 432  GLU A OE1 1 
ATOM   3275  O  OE2 . GLU A 1 432  ? -61.091  83.832  22.462  1.00 106.97 ? 432  GLU A OE2 1 
ATOM   3276  N  N   . PHE A 1 433  ? -61.253  81.345  28.337  1.00 87.43  ? 433  PHE A N   1 
ATOM   3277  C  CA  . PHE A 1 433  ? -60.611  80.837  29.558  1.00 84.10  ? 433  PHE A CA  1 
ATOM   3278  C  C   . PHE A 1 433  ? -59.389  79.906  29.456  1.00 87.61  ? 433  PHE A C   1 
ATOM   3279  O  O   . PHE A 1 433  ? -59.277  79.077  28.551  1.00 89.45  ? 433  PHE A O   1 
ATOM   3280  C  CB  . PHE A 1 433  ? -61.631  80.333  30.582  1.00 80.52  ? 433  PHE A CB  1 
ATOM   3281  C  CG  . PHE A 1 433  ? -62.510  79.220  30.101  1.00 80.31  ? 433  PHE A CG  1 
ATOM   3282  C  CD1 . PHE A 1 433  ? -63.651  79.491  29.353  1.00 80.68  ? 433  PHE A CD1 1 
ATOM   3283  C  CD2 . PHE A 1 433  ? -62.243  77.902  30.463  1.00 74.65  ? 433  PHE A CD2 1 
ATOM   3284  C  CE1 . PHE A 1 433  ? -64.497  78.457  28.930  1.00 79.97  ? 433  PHE A CE1 1 
ATOM   3285  C  CE2 . PHE A 1 433  ? -63.072  76.869  30.042  1.00 75.07  ? 433  PHE A CE2 1 
ATOM   3286  C  CZ  . PHE A 1 433  ? -64.205  77.151  29.260  1.00 76.65  ? 433  PHE A CZ  1 
ATOM   3287  N  N   . ASN A 1 434  ? -58.453  80.112  30.380  1.00 88.44  ? 434  ASN A N   1 
ATOM   3288  C  CA  . ASN A 1 434  ? -57.341  79.201  30.647  1.00 85.66  ? 434  ASN A CA  1 
ATOM   3289  C  C   . ASN A 1 434  ? -57.588  78.524  31.977  1.00 88.52  ? 434  ASN A C   1 
ATOM   3290  O  O   . ASN A 1 434  ? -58.154  79.128  32.897  1.00 91.02  ? 434  ASN A O   1 
ATOM   3291  C  CB  . ASN A 1 434  ? -56.053  79.976  30.792  1.00 83.08  ? 434  ASN A CB  1 
ATOM   3292  C  CG  . ASN A 1 434  ? -55.938  81.066  29.802  1.00 80.87  ? 434  ASN A CG  1 
ATOM   3293  O  OD1 . ASN A 1 434  ? -55.373  80.869  28.735  1.00 78.82  ? 434  ASN A OD1 1 
ATOM   3294  N  ND2 . ASN A 1 434  ? -56.448  82.243  30.148  1.00 82.20  ? 434  ASN A ND2 1 
ATOM   3295  N  N   . VAL A 1 435  ? -57.105  77.302  32.118  1.00 90.58  ? 435  VAL A N   1 
ATOM   3296  C  CA  . VAL A 1 435  ? -57.493  76.492  33.244  1.00 90.35  ? 435  VAL A CA  1 
ATOM   3297  C  C   . VAL A 1 435  ? -56.261  75.730  33.612  1.00 89.35  ? 435  VAL A C   1 
ATOM   3298  O  O   . VAL A 1 435  ? -55.667  75.078  32.756  1.00 89.09  ? 435  VAL A O   1 
ATOM   3299  C  CB  . VAL A 1 435  ? -58.577  75.504  32.808  1.00 70.16  ? 435  VAL A CB  1 
ATOM   3300  C  CG1 . VAL A 1 435  ? -58.400  74.203  33.451  1.00 69.41  ? 435  VAL A CG1 1 
ATOM   3301  C  CG2 . VAL A 1 435  ? -59.916  76.019  33.121  1.00 70.79  ? 435  VAL A CG2 1 
ATOM   3302  N  N   . LYS A 1 436  ? -55.838  75.799  34.864  1.00 78.64  ? 436  LYS A N   1 
ATOM   3303  C  CA  . LYS A 1 436  ? -54.696  74.984  35.212  1.00 75.84  ? 436  LYS A CA  1 
ATOM   3304  C  C   . LYS A 1 436  ? -54.739  74.330  36.571  1.00 79.15  ? 436  LYS A C   1 
ATOM   3305  O  O   . LYS A 1 436  ? -55.567  74.679  37.416  1.00 78.94  ? 436  LYS A O   1 
ATOM   3306  C  CB  . LYS A 1 436  ? -53.398  75.760  35.036  1.00 71.83  ? 436  LYS A CB  1 
ATOM   3307  C  CG  . LYS A 1 436  ? -53.078  76.773  36.103  1.00 67.84  ? 436  LYS A CG  1 
ATOM   3308  C  CD  . LYS A 1 436  ? -51.545  76.849  36.345  1.00 85.99  ? 436  LYS A CD  1 
ATOM   3309  C  CE  . LYS A 1 436  ? -51.023  78.248  36.832  1.00 90.70  ? 436  LYS A CE  1 
ATOM   3310  N  NZ  . LYS A 1 436  ? -50.419  79.181  35.794  1.00 89.62  ? 436  LYS A NZ  1 
ATOM   3311  N  N   . THR A 1 437  ? -53.849  73.348  36.746  1.00 82.09  ? 437  THR A N   1 
ATOM   3312  C  CA  . THR A 1 437  ? -53.572  72.752  38.046  1.00 88.48  ? 437  THR A CA  1 
ATOM   3313  C  C   . THR A 1 437  ? -52.622  73.612  38.839  1.00 83.76  ? 437  THR A C   1 
ATOM   3314  O  O   . THR A 1 437  ? -51.638  74.154  38.303  1.00 77.72  ? 437  THR A O   1 
ATOM   3315  C  CB  . THR A 1 437  ? -52.882  71.404  37.950  1.00 66.06  ? 437  THR A CB  1 
ATOM   3316  O  OG1 . THR A 1 437  ? -51.739  71.524  37.111  1.00 66.19  ? 437  THR A OG1 1 
ATOM   3317  C  CG2 . THR A 1 437  ? -53.810  70.379  37.426  1.00 66.37  ? 437  THR A CG2 1 
ATOM   3318  N  N   . ASP A 1 438  ? -52.915  73.729  40.127  1.00 87.72  ? 438  ASP A N   1 
ATOM   3319  C  CA  . ASP A 1 438  ? -51.966  74.375  41.007  1.00 95.34  ? 438  ASP A CA  1 
ATOM   3320  C  C   . ASP A 1 438  ? -51.294  73.452  42.037  1.00 94.76  ? 438  ASP A C   1 
ATOM   3321  O  O   . ASP A 1 438  ? -50.993  73.867  43.152  1.00 93.12  ? 438  ASP A O   1 
ATOM   3322  C  CB  . ASP A 1 438  ? -52.549  75.628  41.642  1.00 102.70 ? 438  ASP A CB  1 
ATOM   3323  C  CG  . ASP A 1 438  ? -51.677  76.823  41.402  1.00 109.76 ? 438  ASP A CG  1 
ATOM   3324  O  OD1 . ASP A 1 438  ? -50.730  76.693  40.569  1.00 111.09 ? 438  ASP A OD1 1 
ATOM   3325  O  OD2 . ASP A 1 438  ? -51.945  77.875  42.033  1.00 112.81 ? 438  ASP A OD2 1 
ATOM   3326  N  N   . ALA A 1 439  ? -51.033  72.216  41.635  1.00 96.06  ? 439  ALA A N   1 
ATOM   3327  C  CA  . ALA A 1 439  ? -50.067  71.394  42.335  1.00 99.26  ? 439  ALA A CA  1 
ATOM   3328  C  C   . ALA A 1 439  ? -49.088  72.291  43.060  1.00 101.77 ? 439  ALA A C   1 
ATOM   3329  O  O   . ALA A 1 439  ? -48.406  73.115  42.455  1.00 103.96 ? 439  ALA A O   1 
ATOM   3330  C  CB  . ALA A 1 439  ? -49.328  70.517  41.367  1.00 100.93 ? 439  ALA A CB  1 
ATOM   3331  N  N   . PRO A 1 440  ? -49.009  72.122  44.376  1.00 100.20 ? 440  PRO A N   1 
ATOM   3332  C  CA  . PRO A 1 440  ? -48.233  73.030  45.210  1.00 96.70  ? 440  PRO A CA  1 
ATOM   3333  C  C   . PRO A 1 440  ? -46.785  72.598  45.136  1.00 93.20  ? 440  PRO A C   1 
ATOM   3334  O  O   . PRO A 1 440  ? -45.885  73.409  45.353  1.00 93.41  ? 440  PRO A O   1 
ATOM   3335  C  CB  . PRO A 1 440  ? -48.779  72.747  46.607  1.00 96.96  ? 440  PRO A CB  1 
ATOM   3336  C  CG  . PRO A 1 440  ? -49.764  71.516  46.447  1.00 103.60 ? 440  PRO A CG  1 
ATOM   3337  C  CD  . PRO A 1 440  ? -49.459  70.938  45.128  1.00 102.40 ? 440  PRO A CD  1 
ATOM   3338  N  N   . ASP A 1 441  ? -46.598  71.319  44.819  1.00 91.01  ? 441  ASP A N   1 
ATOM   3339  C  CA  . ASP A 1 441  ? -45.312  70.675  44.679  1.00 92.97  ? 441  ASP A CA  1 
ATOM   3340  C  C   . ASP A 1 441  ? -44.969  70.472  43.208  1.00 89.32  ? 441  ASP A C   1 
ATOM   3341  O  O   . ASP A 1 441  ? -43.894  69.983  42.872  1.00 88.67  ? 441  ASP A O   1 
ATOM   3342  C  CB  . ASP A 1 441  ? -45.428  69.304  45.283  1.00 102.53 ? 441  ASP A CB  1 
ATOM   3343  C  CG  . ASP A 1 441  ? -46.576  68.520  44.669  1.00 110.24 ? 441  ASP A CG  1 
ATOM   3344  O  OD1 . ASP A 1 441  ? -46.454  67.276  44.536  1.00 115.80 ? 441  ASP A OD1 1 
ATOM   3345  O  OD2 . ASP A 1 441  ? -47.582  69.160  44.288  1.00 109.23 ? 441  ASP A OD2 1 
ATOM   3346  N  N   . LEU A 1 442  ? -45.888  70.791  42.309  1.00 86.92  ? 442  LEU A N   1 
ATOM   3347  C  CA  . LEU A 1 442  ? -45.483  70.893  40.903  1.00 83.16  ? 442  LEU A CA  1 
ATOM   3348  C  C   . LEU A 1 442  ? -44.879  72.261  40.574  1.00 85.18  ? 442  LEU A C   1 
ATOM   3349  O  O   . LEU A 1 442  ? -45.459  73.316  40.937  1.00 85.75  ? 442  LEU A O   1 
ATOM   3350  C  CB  . LEU A 1 442  ? -46.628  70.579  39.952  1.00 76.96  ? 442  LEU A CB  1 
ATOM   3351  C  CG  . LEU A 1 442  ? -46.491  69.135  39.525  1.00 72.28  ? 442  LEU A CG  1 
ATOM   3352  C  CD1 . LEU A 1 442  ? -47.360  68.860  38.313  1.00 71.22  ? 442  LEU A CD1 1 
ATOM   3353  C  CD2 . LEU A 1 442  ? -45.005  68.816  39.294  1.00 69.56  ? 442  LEU A CD2 1 
ATOM   3354  N  N   . PRO A 1 443  ? -43.721  72.255  39.881  1.00 81.92  ? 443  PRO A N   1 
ATOM   3355  C  CA  . PRO A 1 443  ? -43.066  73.511  39.546  1.00 84.44  ? 443  PRO A CA  1 
ATOM   3356  C  C   . PRO A 1 443  ? -43.889  74.146  38.440  1.00 92.33  ? 443  PRO A C   1 
ATOM   3357  O  O   . PRO A 1 443  ? -44.636  73.410  37.763  1.00 94.27  ? 443  PRO A O   1 
ATOM   3358  C  CB  . PRO A 1 443  ? -41.708  73.065  39.031  1.00 80.09  ? 443  PRO A CB  1 
ATOM   3359  C  CG  . PRO A 1 443  ? -41.684  71.610  39.166  1.00 79.16  ? 443  PRO A CG  1 
ATOM   3360  C  CD  . PRO A 1 443  ? -43.067  71.138  39.208  1.00 79.16  ? 443  PRO A CD  1 
ATOM   3361  N  N   . GLU A 1 444  ? -43.775  75.463  38.256  1.00 95.72  ? 444  GLU A N   1 
ATOM   3362  C  CA  . GLU A 1 444  ? -44.755  76.160  37.446  1.00 98.97  ? 444  GLU A CA  1 
ATOM   3363  C  C   . GLU A 1 444  ? -44.853  75.557  36.074  1.00 90.91  ? 444  GLU A C   1 
ATOM   3364  O  O   . GLU A 1 444  ? -45.924  75.165  35.643  1.00 85.54  ? 444  GLU A O   1 
ATOM   3365  C  CB  . GLU A 1 444  ? -44.465  77.645  37.365  1.00 112.63 ? 444  GLU A CB  1 
ATOM   3366  C  CG  . GLU A 1 444  ? -45.760  78.475  37.397  1.00 125.76 ? 444  GLU A CG  1 
ATOM   3367  C  CD  . GLU A 1 444  ? -46.629  78.317  36.135  1.00 135.62 ? 444  GLU A CD  1 
ATOM   3368  O  OE1 . GLU A 1 444  ? -46.191  77.612  35.195  1.00 138.66 ? 444  GLU A OE1 1 
ATOM   3369  O  OE2 . GLU A 1 444  ? -47.743  78.913  36.081  1.00 138.30 ? 444  GLU A OE2 1 
ATOM   3370  N  N   . GLU A 1 445  ? -43.709  75.468  35.409  1.00 91.80  ? 445  GLU A N   1 
ATOM   3371  C  CA  . GLU A 1 445  ? -43.592  74.836  34.088  1.00 92.51  ? 445  GLU A CA  1 
ATOM   3372  C  C   . GLU A 1 445  ? -44.486  73.619  33.943  1.00 86.34  ? 445  GLU A C   1 
ATOM   3373  O  O   . GLU A 1 445  ? -45.486  73.635  33.240  1.00 86.46  ? 445  GLU A O   1 
ATOM   3374  C  CB  . GLU A 1 445  ? -42.150  74.396  33.821  1.00 98.73  ? 445  GLU A CB  1 
ATOM   3375  C  CG  . GLU A 1 445  ? -41.173  75.522  33.553  1.00 106.85 ? 445  GLU A CG  1 
ATOM   3376  C  CD  . GLU A 1 445  ? -39.773  75.001  33.238  1.00 114.80 ? 445  GLU A CD  1 
ATOM   3377  O  OE1 . GLU A 1 445  ? -39.364  73.929  33.774  1.00 116.58 ? 445  GLU A OE1 1 
ATOM   3378  O  OE2 . GLU A 1 445  ? -39.079  75.667  32.440  1.00 118.22 ? 445  GLU A OE2 1 
ATOM   3379  N  N   . ASN A 1 446  ? -44.118  72.563  34.637  1.00 82.69  ? 446  ASN A N   1 
ATOM   3380  C  CA  . ASN A 1 446  ? -44.784  71.288  34.509  1.00 82.42  ? 446  ASN A CA  1 
ATOM   3381  C  C   . ASN A 1 446  ? -46.194  71.217  35.090  1.00 78.03  ? 446  ASN A C   1 
ATOM   3382  O  O   . ASN A 1 446  ? -46.792  70.167  35.143  1.00 76.83  ? 446  ASN A O   1 
ATOM   3383  C  CB  . ASN A 1 446  ? -43.872  70.252  35.112  1.00 86.84  ? 446  ASN A CB  1 
ATOM   3384  C  CG  . ASN A 1 446  ? -42.427  70.557  34.812  1.00 91.92  ? 446  ASN A CG  1 
ATOM   3385  O  OD1 . ASN A 1 446  ? -41.660  70.981  35.681  1.00 92.37  ? 446  ASN A OD1 1 
ATOM   3386  N  ND2 . ASN A 1 446  ? -42.052  70.375  33.557  1.00 95.75  ? 446  ASN A ND2 1 
ATOM   3387  N  N   . GLN A 1 447  ? -46.737  72.336  35.527  1.00 77.32  ? 447  GLN A N   1 
ATOM   3388  C  CA  . GLN A 1 447  ? -48.171  72.400  35.810  1.00 81.07  ? 447  GLN A CA  1 
ATOM   3389  C  C   . GLN A 1 447  ? -49.031  72.173  34.557  1.00 80.08  ? 447  GLN A C   1 
ATOM   3390  O  O   . GLN A 1 447  ? -48.725  72.692  33.471  1.00 77.95  ? 447  GLN A O   1 
ATOM   3391  C  CB  . GLN A 1 447  ? -48.497  73.789  36.346  1.00 83.34  ? 447  GLN A CB  1 
ATOM   3392  C  CG  . GLN A 1 447  ? -48.166  74.012  37.786  1.00 86.69  ? 447  GLN A CG  1 
ATOM   3393  C  CD  . GLN A 1 447  ? -48.691  72.902  38.611  1.00 88.70  ? 447  GLN A CD  1 
ATOM   3394  O  OE1 . GLN A 1 447  ? -49.589  72.169  38.189  1.00 88.42  ? 447  GLN A OE1 1 
ATOM   3395  N  NE2 . GLN A 1 447  ? -48.126  72.740  39.791  1.00 90.41  ? 447  GLN A NE2 1 
ATOM   3396  N  N   . ALA A 1 448  ? -50.139  71.466  34.699  1.00 67.05  ? 448  ALA A N   1 
ATOM   3397  C  CA  . ALA A 1 448  ? -50.925  71.159  33.522  1.00 67.53  ? 448  ALA A CA  1 
ATOM   3398  C  C   . ALA A 1 448  ? -51.974  72.206  33.109  1.00 77.87  ? 448  ALA A C   1 
ATOM   3399  O  O   . ALA A 1 448  ? -52.792  72.596  33.931  1.00 75.36  ? 448  ALA A O   1 
ATOM   3400  C  CB  . ALA A 1 448  ? -51.553  69.829  33.686  1.00 67.50  ? 448  ALA A CB  1 
ATOM   3401  N  N   . ARG A 1 449  ? -52.005  72.607  31.828  1.00 79.65  ? 449  ARG A N   1 
ATOM   3402  C  CA  . ARG A 1 449  ? -52.934  73.657  31.373  1.00 80.93  ? 449  ARG A CA  1 
ATOM   3403  C  C   . ARG A 1 449  ? -53.668  73.406  30.052  1.00 82.64  ? 449  ARG A C   1 
ATOM   3404  O  O   . ARG A 1 449  ? -53.244  72.612  29.218  1.00 82.53  ? 449  ARG A O   1 
ATOM   3405  C  CB  . ARG A 1 449  ? -52.177  74.947  31.234  1.00 81.75  ? 449  ARG A CB  1 
ATOM   3406  C  CG  . ARG A 1 449  ? -50.844  74.680  30.664  1.00 84.63  ? 449  ARG A CG  1 
ATOM   3407  C  CD  . ARG A 1 449  ? -50.009  75.884  30.822  1.00 89.76  ? 449  ARG A CD  1 
ATOM   3408  N  NE  . ARG A 1 449  ? -49.118  75.753  31.959  1.00 92.47  ? 449  ARG A NE  1 
ATOM   3409  C  CZ  . ARG A 1 449  ? -48.784  76.786  32.725  1.00 95.74  ? 449  ARG A CZ  1 
ATOM   3410  N  NH1 . ARG A 1 449  ? -49.307  78.008  32.493  1.00 97.00  ? 449  ARG A NH1 1 
ATOM   3411  N  NH2 . ARG A 1 449  ? -47.949  76.592  33.735  1.00 95.24  ? 449  ARG A NH2 1 
ATOM   3412  N  N   . GLU A 1 450  ? -54.775  74.119  29.879  1.00 85.27  ? 450  GLU A N   1 
ATOM   3413  C  CA  . GLU A 1 450  ? -55.654  73.989  28.728  1.00 86.97  ? 450  GLU A CA  1 
ATOM   3414  C  C   . GLU A 1 450  ? -56.379  75.291  28.627  1.00 86.38  ? 450  GLU A C   1 
ATOM   3415  O  O   . GLU A 1 450  ? -56.542  75.986  29.628  1.00 86.74  ? 450  GLU A O   1 
ATOM   3416  C  CB  . GLU A 1 450  ? -56.688  72.900  28.954  1.00 92.68  ? 450  GLU A CB  1 
ATOM   3417  C  CG  . GLU A 1 450  ? -56.177  71.521  28.639  1.00 99.31  ? 450  GLU A CG  1 
ATOM   3418  C  CD  . GLU A 1 450  ? -55.756  71.390  27.197  1.00 106.42 ? 450  GLU A CD  1 
ATOM   3419  O  OE1 . GLU A 1 450  ? -56.361  72.080  26.339  1.00 110.34 ? 450  GLU A OE1 1 
ATOM   3420  O  OE2 . GLU A 1 450  ? -54.817  70.604  26.925  1.00 107.42 ? 450  GLU A OE2 1 
ATOM   3421  N  N   . GLY A 1 451  ? -56.825  75.622  27.423  1.00 85.23  ? 451  GLY A N   1 
ATOM   3422  C  CA  . GLY A 1 451  ? -57.535  76.868  27.183  1.00 83.84  ? 451  GLY A CA  1 
ATOM   3423  C  C   . GLY A 1 451  ? -58.747  76.613  26.311  1.00 82.79  ? 451  GLY A C   1 
ATOM   3424  O  O   . GLY A 1 451  ? -58.783  75.641  25.540  1.00 85.69  ? 451  GLY A O   1 
ATOM   3425  N  N   . TYR A 1 452  ? -59.749  77.473  26.438  1.00 79.02  ? 452  TYR A N   1 
ATOM   3426  C  CA  . TYR A 1 452  ? -61.010  77.274  25.744  1.00 79.84  ? 452  TYR A CA  1 
ATOM   3427  C  C   . TYR A 1 452  ? -61.653  78.649  25.431  1.00 84.18  ? 452  TYR A C   1 
ATOM   3428  O  O   . TYR A 1 452  ? -61.195  79.672  25.941  1.00 84.06  ? 452  TYR A O   1 
ATOM   3429  C  CB  . TYR A 1 452  ? -61.926  76.403  26.602  1.00 78.56  ? 452  TYR A CB  1 
ATOM   3430  C  CG  . TYR A 1 452  ? -61.402  75.020  26.959  1.00 78.67  ? 452  TYR A CG  1 
ATOM   3431  C  CD1 . TYR A 1 452  ? -62.018  73.896  26.470  1.00 82.67  ? 452  TYR A CD1 1 
ATOM   3432  C  CD2 . TYR A 1 452  ? -60.320  74.833  27.812  1.00 78.15  ? 452  TYR A CD2 1 
ATOM   3433  C  CE1 . TYR A 1 452  ? -61.578  72.613  26.804  1.00 84.12  ? 452  TYR A CE1 1 
ATOM   3434  C  CE2 . TYR A 1 452  ? -59.858  73.542  28.145  1.00 78.99  ? 452  TYR A CE2 1 
ATOM   3435  C  CZ  . TYR A 1 452  ? -60.507  72.441  27.634  1.00 80.96  ? 452  TYR A CZ  1 
ATOM   3436  O  OH  . TYR A 1 452  ? -60.111  71.156  27.912  1.00 78.68  ? 452  TYR A OH  1 
ATOM   3437  N  N   . ARG A 1 453  ? -62.687  78.681  24.584  1.00 83.10  ? 453  ARG A N   1 
ATOM   3438  C  CA  . ARG A 1 453  ? -63.376  79.936  24.244  1.00 82.48  ? 453  ARG A CA  1 
ATOM   3439  C  C   . ARG A 1 453  ? -64.891  79.757  24.106  1.00 83.68  ? 453  ARG A C   1 
ATOM   3440  O  O   . ARG A 1 453  ? -65.348  78.800  23.499  1.00 84.13  ? 453  ARG A O   1 
ATOM   3441  C  CB  . ARG A 1 453  ? -62.818  80.513  22.942  1.00 84.05  ? 453  ARG A CB  1 
ATOM   3442  C  CG  . ARG A 1 453  ? -63.658  81.663  22.435  1.00 86.62  ? 453  ARG A CG  1 
ATOM   3443  C  CD  . ARG A 1 453  ? -63.591  81.858  20.948  1.00 90.28  ? 453  ARG A CD  1 
ATOM   3444  N  NE  . ARG A 1 453  ? -62.508  82.754  20.572  1.00 93.91  ? 453  ARG A NE  1 
ATOM   3445  C  CZ  . ARG A 1 453  ? -61.510  82.407  19.757  1.00 97.71  ? 453  ARG A CZ  1 
ATOM   3446  N  NH1 . ARG A 1 453  ? -61.480  81.176  19.234  1.00 98.23  ? 453  ARG A NH1 1 
ATOM   3447  N  NH2 . ARG A 1 453  ? -60.550  83.285  19.445  1.00 99.20  ? 453  ARG A NH2 1 
ATOM   3448  N  N   . ALA A 1 454  ? -65.676  80.681  24.648  1.00 84.39  ? 454  ALA A N   1 
ATOM   3449  C  CA  . ALA A 1 454  ? -67.124  80.494  24.641  1.00 91.16  ? 454  ALA A CA  1 
ATOM   3450  C  C   . ALA A 1 454  ? -67.812  81.692  24.064  1.00 96.45  ? 454  ALA A C   1 
ATOM   3451  O  O   . ALA A 1 454  ? -67.353  82.811  24.268  1.00 98.68  ? 454  ALA A O   1 
ATOM   3452  C  CB  . ALA A 1 454  ? -67.627  80.265  26.023  1.00 87.18  ? 454  ALA A CB  1 
ATOM   3453  N  N   . ILE A 1 455  ? -68.935  81.474  23.379  1.00 98.95  ? 455  ILE A N   1 
ATOM   3454  C  CA  . ILE A 1 455  ? -69.574  82.539  22.577  1.00 102.55 ? 455  ILE A CA  1 
ATOM   3455  C  C   . ILE A 1 455  ? -71.102  82.539  22.693  1.00 101.71 ? 455  ILE A C   1 
ATOM   3456  O  O   . ILE A 1 455  ? -71.731  81.484  22.793  1.00 100.91 ? 455  ILE A O   1 
ATOM   3457  C  CB  . ILE A 1 455  ? -69.274  82.333  21.138  1.00 93.58  ? 455  ILE A CB  1 
ATOM   3458  C  CG1 . ILE A 1 455  ? -67.845  82.730  20.863  1.00 92.83  ? 455  ILE A CG1 1 
ATOM   3459  C  CG2 . ILE A 1 455  ? -70.223  83.097  20.324  1.00 96.47  ? 455  ILE A CG2 1 
ATOM   3460  C  CD1 . ILE A 1 455  ? -67.114  81.636  20.085  1.00 95.89  ? 455  ILE A CD1 1 
ATOM   3461  N  N   . ALA A 1 456  ? -71.709  83.714  22.664  1.00 101.43 ? 456  ALA A N   1 
ATOM   3462  C  CA  . ALA A 1 456  ? -73.107  83.807  23.032  1.00 101.24 ? 456  ALA A CA  1 
ATOM   3463  C  C   . ALA A 1 456  ? -74.112  83.401  21.940  1.00 105.01 ? 456  ALA A C   1 
ATOM   3464  O  O   . ALA A 1 456  ? -73.978  83.793  20.769  1.00 105.99 ? 456  ALA A O   1 
ATOM   3465  C  CB  . ALA A 1 456  ? -73.388  85.196  23.547  1.00 102.28 ? 456  ALA A CB  1 
ATOM   3466  N  N   . TYR A 1 457  ? -75.098  82.590  22.338  1.00 105.63 ? 457  TYR A N   1 
ATOM   3467  C  CA  . TYR A 1 457  ? -76.263  82.291  21.515  1.00 110.08 ? 457  TYR A CA  1 
ATOM   3468  C  C   . TYR A 1 457  ? -76.868  83.619  21.187  1.00 113.92 ? 457  TYR A C   1 
ATOM   3469  O  O   . TYR A 1 457  ? -77.680  84.168  21.923  1.00 112.85 ? 457  TYR A O   1 
ATOM   3470  C  CB  . TYR A 1 457  ? -77.288  81.478  22.289  1.00 114.34 ? 457  TYR A CB  1 
ATOM   3471  C  CG  . TYR A 1 457  ? -78.495  80.965  21.507  1.00 122.09 ? 457  TYR A CG  1 
ATOM   3472  C  CD1 . TYR A 1 457  ? -79.179  79.825  21.930  1.00 124.78 ? 457  TYR A CD1 1 
ATOM   3473  C  CD2 . TYR A 1 457  ? -78.955  81.601  20.361  1.00 126.55 ? 457  TYR A CD2 1 
ATOM   3474  C  CE1 . TYR A 1 457  ? -80.281  79.331  21.238  1.00 127.50 ? 457  TYR A CE1 1 
ATOM   3475  C  CE2 . TYR A 1 457  ? -80.073  81.111  19.652  1.00 129.63 ? 457  TYR A CE2 1 
ATOM   3476  C  CZ  . TYR A 1 457  ? -80.725  79.971  20.104  1.00 129.08 ? 457  TYR A CZ  1 
ATOM   3477  O  OH  . TYR A 1 457  ? -81.816  79.470  19.428  1.00 130.47 ? 457  TYR A OH  1 
ATOM   3478  N  N   . SER A 1 458  ? -76.448  84.142  20.056  1.00 119.11 ? 458  SER A N   1 
ATOM   3479  C  CA  . SER A 1 458  ? -76.942  85.404  19.561  1.00 125.90 ? 458  SER A CA  1 
ATOM   3480  C  C   . SER A 1 458  ? -78.385  85.204  19.030  1.00 128.61 ? 458  SER A C   1 
ATOM   3481  O  O   . SER A 1 458  ? -78.634  84.322  18.202  1.00 125.82 ? 458  SER A O   1 
ATOM   3482  C  CB  . SER A 1 458  ? -75.969  85.865  18.468  1.00 128.74 ? 458  SER A CB  1 
ATOM   3483  O  OG  . SER A 1 458  ? -74.661  85.288  18.695  1.00 126.66 ? 458  SER A OG  1 
ATOM   3484  N  N   . SER A 1 459  ? -79.339  85.981  19.547  1.00 134.07 ? 459  SER A N   1 
ATOM   3485  C  CA  . SER A 1 459  ? -80.727  85.927  19.075  1.00 138.27 ? 459  SER A CA  1 
ATOM   3486  C  C   . SER A 1 459  ? -81.399  87.278  19.267  1.00 143.02 ? 459  SER A C   1 
ATOM   3487  O  O   . SER A 1 459  ? -81.497  87.771  20.375  1.00 141.30 ? 459  SER A O   1 
ATOM   3488  C  CB  . SER A 1 459  ? -81.512  84.829  19.786  1.00 136.05 ? 459  SER A CB  1 
ATOM   3489  O  OG  . SER A 1 459  ? -82.539  84.323  18.963  1.00 137.18 ? 459  SER A OG  1 
ATOM   3490  N  N   . LEU A 1 460  ? -81.856  87.868  18.169  1.00 153.16 ? 460  LEU A N   1 
ATOM   3491  C  CA  . LEU A 1 460  ? -82.328  89.248  18.170  1.00 163.87 ? 460  LEU A CA  1 
ATOM   3492  C  C   . LEU A 1 460  ? -83.629  89.399  18.942  1.00 170.64 ? 460  LEU A C   1 
ATOM   3493  O  O   . LEU A 1 460  ? -83.951  90.490  19.408  1.00 173.43 ? 460  LEU A O   1 
ATOM   3494  C  CB  . LEU A 1 460  ? -82.487  89.796  16.742  1.00 172.18 ? 460  LEU A CB  1 
ATOM   3495  C  CG  . LEU A 1 460  ? -82.342  91.323  16.568  1.00 179.23 ? 460  LEU A CG  1 
ATOM   3496  C  CD1 . LEU A 1 460  ? -80.880  91.713  16.348  1.00 178.20 ? 460  LEU A CD1 1 
ATOM   3497  C  CD2 . LEU A 1 460  ? -83.223  91.902  15.438  1.00 186.06 ? 460  LEU A CD2 1 
ATOM   3498  N  N   . SER A 1 461  ? -84.374  88.308  19.084  1.00 170.59 ? 461  SER A N   1 
ATOM   3499  C  CA  . SER A 1 461  ? -85.542  88.314  19.958  1.00 173.90 ? 461  SER A CA  1 
ATOM   3500  C  C   . SER A 1 461  ? -85.112  88.522  21.399  1.00 170.74 ? 461  SER A C   1 
ATOM   3501  O  O   . SER A 1 461  ? -85.942  88.545  22.300  1.00 170.63 ? 461  SER A O   1 
ATOM   3502  C  CB  . SER A 1 461  ? -86.328  87.011  19.839  1.00 175.88 ? 461  SER A CB  1 
ATOM   3503  O  OG  . SER A 1 461  ? -86.934  86.912  18.567  1.00 180.42 ? 461  SER A OG  1 
ATOM   3504  N  N   . GLN A 1 462  ? -83.806  88.667  21.604  1.00 167.32 ? 462  GLN A N   1 
ATOM   3505  C  CA  . GLN A 1 462  ? -83.240  88.766  22.939  1.00 161.99 ? 462  GLN A CA  1 
ATOM   3506  C  C   . GLN A 1 462  ? -83.549  87.491  23.689  1.00 154.34 ? 462  GLN A C   1 
ATOM   3507  O  O   . GLN A 1 462  ? -83.299  87.386  24.889  1.00 152.82 ? 462  GLN A O   1 
ATOM   3508  C  CB  . GLN A 1 462  ? -83.815  89.966  23.681  1.00 163.39 ? 462  GLN A CB  1 
ATOM   3509  C  CG  . GLN A 1 462  ? -83.019  91.229  23.502  1.00 163.60 ? 462  GLN A CG  1 
ATOM   3510  C  CD  . GLN A 1 462  ? -81.636  91.128  24.115  1.00 160.31 ? 462  GLN A CD  1 
ATOM   3511  O  OE1 . GLN A 1 462  ? -81.261  90.100  24.689  1.00 155.65 ? 462  GLN A OE1 1 
ATOM   3512  N  NE2 . GLN A 1 462  ? -80.865  92.201  23.992  1.00 161.93 ? 462  GLN A NE2 1 
ATOM   3513  N  N   . SER A 1 463  ? -84.100  86.528  22.958  1.00 150.49 ? 463  SER A N   1 
ATOM   3514  C  CA  . SER A 1 463  ? -84.588  85.288  23.530  1.00 145.52 ? 463  SER A CA  1 
ATOM   3515  C  C   . SER A 1 463  ? -83.494  84.233  23.547  1.00 138.17 ? 463  SER A C   1 
ATOM   3516  O  O   . SER A 1 463  ? -82.753  84.126  22.583  1.00 140.22 ? 463  SER A O   1 
ATOM   3517  C  CB  . SER A 1 463  ? -85.765  84.795  22.694  1.00 148.32 ? 463  SER A CB  1 
ATOM   3518  O  OG  . SER A 1 463  ? -86.064  83.443  22.983  1.00 148.05 ? 463  SER A OG  1 
ATOM   3519  N  N   . TYR A 1 464  ? -83.376  83.461  24.627  1.00 130.74 ? 464  TYR A N   1 
ATOM   3520  C  CA  . TYR A 1 464  ? -82.456  82.331  24.624  1.00 124.71 ? 464  TYR A CA  1 
ATOM   3521  C  C   . TYR A 1 464  ? -83.057  81.157  25.350  1.00 122.02 ? 464  TYR A C   1 
ATOM   3522  O  O   . TYR A 1 464  ? -84.198  81.228  25.810  1.00 121.84 ? 464  TYR A O   1 
ATOM   3523  C  CB  . TYR A 1 464  ? -81.125  82.682  25.261  1.00 122.81 ? 464  TYR A CB  1 
ATOM   3524  C  CG  . TYR A 1 464  ? -80.690  84.093  25.022  1.00 126.02 ? 464  TYR A CG  1 
ATOM   3525  C  CD1 . TYR A 1 464  ? -80.262  84.513  23.766  1.00 128.80 ? 464  TYR A CD1 1 
ATOM   3526  C  CD2 . TYR A 1 464  ? -80.686  85.006  26.053  1.00 126.62 ? 464  TYR A CD2 1 
ATOM   3527  C  CE1 . TYR A 1 464  ? -79.851  85.829  23.547  1.00 131.99 ? 464  TYR A CE1 1 
ATOM   3528  C  CE2 . TYR A 1 464  ? -80.281  86.309  25.856  1.00 130.40 ? 464  TYR A CE2 1 
ATOM   3529  C  CZ  . TYR A 1 464  ? -79.864  86.729  24.605  1.00 133.22 ? 464  TYR A CZ  1 
ATOM   3530  O  OH  . TYR A 1 464  ? -79.465  88.049  24.430  1.00 135.43 ? 464  TYR A OH  1 
ATOM   3531  N  N   . LEU A 1 465  ? -82.288  80.074  25.444  1.00 119.53 ? 465  LEU A N   1 
ATOM   3532  C  CA  . LEU A 1 465  ? -82.722  78.901  26.206  1.00 120.35 ? 465  LEU A CA  1 
ATOM   3533  C  C   . LEU A 1 465  ? -81.540  78.118  26.795  1.00 119.35 ? 465  LEU A C   1 
ATOM   3534  O  O   . LEU A 1 465  ? -80.473  78.048  26.165  1.00 120.04 ? 465  LEU A O   1 
ATOM   3535  C  CB  . LEU A 1 465  ? -83.611  77.985  25.359  1.00 122.34 ? 465  LEU A CB  1 
ATOM   3536  C  CG  . LEU A 1 465  ? -84.098  76.728  26.083  1.00 123.55 ? 465  LEU A CG  1 
ATOM   3537  C  CD1 . LEU A 1 465  ? -85.002  77.093  27.240  1.00 126.29 ? 465  LEU A CD1 1 
ATOM   3538  C  CD2 . LEU A 1 465  ? -84.799  75.756  25.150  1.00 125.09 ? 465  LEU A CD2 1 
ATOM   3539  N  N   . TYR A 1 466  ? -81.755  77.526  27.983  1.00 116.17 ? 466  TYR A N   1 
ATOM   3540  C  CA  . TYR A 1 466  ? -80.735  76.782  28.741  1.00 110.27 ? 466  TYR A CA  1 
ATOM   3541  C  C   . TYR A 1 466  ? -81.264  75.524  29.414  1.00 109.72 ? 466  TYR A C   1 
ATOM   3542  O  O   . TYR A 1 466  ? -82.030  75.612  30.372  1.00 112.94 ? 466  TYR A O   1 
ATOM   3543  C  CB  . TYR A 1 466  ? -80.204  77.634  29.884  1.00 107.27 ? 466  TYR A CB  1 
ATOM   3544  C  CG  . TYR A 1 466  ? -79.143  76.918  30.669  1.00 101.76 ? 466  TYR A CG  1 
ATOM   3545  C  CD1 . TYR A 1 466  ? -78.693  75.708  30.239  1.00 101.23 ? 466  TYR A CD1 1 
ATOM   3546  C  CD2 . TYR A 1 466  ? -78.559  77.459  31.797  1.00 98.44  ? 466  TYR A CD2 1 
ATOM   3547  C  CE1 . TYR A 1 466  ? -77.708  75.019  30.900  1.00 98.78  ? 466  TYR A CE1 1 
ATOM   3548  C  CE2 . TYR A 1 466  ? -77.544  76.781  32.465  1.00 96.55  ? 466  TYR A CE2 1 
ATOM   3549  C  CZ  . TYR A 1 466  ? -77.126  75.549  31.989  1.00 95.56  ? 466  TYR A CZ  1 
ATOM   3550  O  OH  . TYR A 1 466  ? -76.139  74.790  32.561  1.00 92.83  ? 466  TYR A OH  1 
ATOM   3551  N  N   . ILE A 1 467  ? -80.823  74.349  28.986  1.00 105.67 ? 467  ILE A N   1 
ATOM   3552  C  CA  . ILE A 1 467  ? -81.212  73.136  29.716  1.00 104.01 ? 467  ILE A CA  1 
ATOM   3553  C  C   . ILE A 1 467  ? -80.071  72.341  30.341  1.00 102.84 ? 467  ILE A C   1 
ATOM   3554  O  O   . ILE A 1 467  ? -78.990  72.223  29.786  1.00 101.62 ? 467  ILE A O   1 
ATOM   3555  C  CB  . ILE A 1 467  ? -82.035  72.206  28.841  1.00 102.84 ? 467  ILE A CB  1 
ATOM   3556  C  CG1 . ILE A 1 467  ? -81.129  71.531  27.812  1.00 99.61  ? 467  ILE A CG1 1 
ATOM   3557  C  CG2 . ILE A 1 467  ? -83.171  72.995  28.193  1.00 105.98 ? 467  ILE A CG2 1 
ATOM   3558  C  CD1 . ILE A 1 467  ? -81.801  70.394  27.077  1.00 99.44  ? 467  ILE A CD1 1 
ATOM   3559  N  N   . ASP A 1 468  ? -80.321  71.766  31.496  1.00 104.04 ? 468  ASP A N   1 
ATOM   3560  C  CA  . ASP A 1 468  ? -79.269  71.054  32.159  1.00 108.17 ? 468  ASP A CA  1 
ATOM   3561  C  C   . ASP A 1 468  ? -79.996  69.980  32.882  1.00 108.21 ? 468  ASP A C   1 
ATOM   3562  O  O   . ASP A 1 468  ? -81.181  69.808  32.668  1.00 108.02 ? 468  ASP A O   1 
ATOM   3563  C  CB  . ASP A 1 468  ? -78.548  71.979  33.136  1.00 114.83 ? 468  ASP A CB  1 
ATOM   3564  C  CG  . ASP A 1 468  ? -77.178  71.452  33.568  1.00 118.90 ? 468  ASP A CG  1 
ATOM   3565  O  OD1 . ASP A 1 468  ? -76.701  70.469  32.968  1.00 120.07 ? 468  ASP A OD1 1 
ATOM   3566  O  OD2 . ASP A 1 468  ? -76.572  72.026  34.510  1.00 120.18 ? 468  ASP A OD2 1 
ATOM   3567  N  N   . TRP A 1 469  ? -79.292  69.268  33.745  1.00 112.64 ? 469  TRP A N   1 
ATOM   3568  C  CA  . TRP A 1 469  ? -79.875  68.190  34.516  1.00 121.13 ? 469  TRP A CA  1 
ATOM   3569  C  C   . TRP A 1 469  ? -78.797  67.779  35.481  1.00 132.69 ? 469  TRP A C   1 
ATOM   3570  O  O   . TRP A 1 469  ? -77.625  67.982  35.166  1.00 131.88 ? 469  TRP A O   1 
ATOM   3571  C  CB  . TRP A 1 469  ? -80.160  67.023  33.584  1.00 119.24 ? 469  TRP A CB  1 
ATOM   3572  C  CG  . TRP A 1 469  ? -78.930  66.230  33.196  1.00 115.96 ? 469  TRP A CG  1 
ATOM   3573  C  CD1 . TRP A 1 469  ? -78.641  64.950  33.556  1.00 114.95 ? 469  TRP A CD1 1 
ATOM   3574  C  CD2 . TRP A 1 469  ? -77.841  66.663  32.377  1.00 115.26 ? 469  TRP A CD2 1 
ATOM   3575  N  NE1 . TRP A 1 469  ? -77.440  64.555  33.018  1.00 112.44 ? 469  TRP A NE1 1 
ATOM   3576  C  CE2 . TRP A 1 469  ? -76.930  65.592  32.287  1.00 113.26 ? 469  TRP A CE2 1 
ATOM   3577  C  CE3 . TRP A 1 469  ? -77.542  67.854  31.710  1.00 116.61 ? 469  TRP A CE3 1 
ATOM   3578  C  CZ2 . TRP A 1 469  ? -75.755  65.675  31.559  1.00 113.00 ? 469  TRP A CZ2 1 
ATOM   3579  C  CZ3 . TRP A 1 469  ? -76.357  67.933  30.978  1.00 115.09 ? 469  TRP A CZ3 1 
ATOM   3580  C  CH2 . TRP A 1 469  ? -75.488  66.852  30.909  1.00 113.21 ? 469  TRP A CH2 1 
ATOM   3581  N  N   . THR A 1 470  ? -79.130  67.195  36.634  1.00 144.33 ? 470  THR A N   1 
ATOM   3582  C  CA  . THR A 1 470  ? -78.037  66.541  37.380  1.00 154.13 ? 470  THR A CA  1 
ATOM   3583  C  C   . THR A 1 470  ? -78.253  65.097  37.802  1.00 169.02 ? 470  THR A C   1 
ATOM   3584  O  O   . THR A 1 470  ? -79.379  64.616  37.927  1.00 172.14 ? 470  THR A O   1 
ATOM   3585  C  CB  . THR A 1 470  ? -77.474  67.342  38.571  1.00 150.39 ? 470  THR A CB  1 
ATOM   3586  O  OG1 . THR A 1 470  ? -77.138  68.665  38.149  1.00 150.05 ? 470  THR A OG1 1 
ATOM   3587  C  CG2 . THR A 1 470  ? -76.210  66.677  39.073  1.00 145.34 ? 470  THR A CG2 1 
ATOM   3588  N  N   . ASP A 1 471  ? -77.120  64.432  37.999  1.00 181.91 ? 471  ASP A N   1 
ATOM   3589  C  CA  . ASP A 1 471  ? -77.020  63.030  38.362  1.00 198.38 ? 471  ASP A CA  1 
ATOM   3590  C  C   . ASP A 1 471  ? -75.561  62.882  38.826  1.00 209.57 ? 471  ASP A C   1 
ATOM   3591  O  O   . ASP A 1 471  ? -74.643  63.291  38.113  1.00 208.89 ? 471  ASP A O   1 
ATOM   3592  C  CB  . ASP A 1 471  ? -77.329  62.154  37.132  1.00 205.46 ? 471  ASP A CB  1 
ATOM   3593  C  CG  . ASP A 1 471  ? -77.441  60.654  37.460  1.00 213.72 ? 471  ASP A CG  1 
ATOM   3594  O  OD1 . ASP A 1 471  ? -78.562  60.101  37.460  1.00 218.09 ? 471  ASP A OD1 1 
ATOM   3595  O  OD2 . ASP A 1 471  ? -76.408  59.997  37.700  1.00 216.02 ? 471  ASP A OD2 1 
ATOM   3596  N  N   . ASN A 1 472  ? -75.346  62.335  40.024  1.00 219.92 ? 472  ASN A N   1 
ATOM   3597  C  CA  . ASN A 1 472  ? -74.008  62.298  40.630  1.00 228.16 ? 472  ASN A CA  1 
ATOM   3598  C  C   . ASN A 1 472  ? -72.973  61.323  40.037  1.00 234.16 ? 472  ASN A C   1 
ATOM   3599  O  O   . ASN A 1 472  ? -71.793  61.407  40.372  1.00 232.73 ? 472  ASN A O   1 
ATOM   3600  C  CB  . ASN A 1 472  ? -74.077  62.160  42.166  1.00 227.88 ? 472  ASN A CB  1 
ATOM   3601  C  CG  . ASN A 1 472  ? -75.261  61.325  42.647  1.00 226.46 ? 472  ASN A CG  1 
ATOM   3602  O  OD1 . ASN A 1 472  ? -76.084  60.875  41.857  1.00 225.87 ? 472  ASN A OD1 1 
ATOM   3603  N  ND2 . ASN A 1 472  ? -75.347  61.126  43.961  1.00 225.82 ? 472  ASN A ND2 1 
ATOM   3604  N  N   . HIS A 1 473  ? -73.398  60.414  39.160  1.00 243.31 ? 473  HIS A N   1 
ATOM   3605  C  CA  . HIS A 1 473  ? -72.468  59.448  38.556  1.00 250.75 ? 473  HIS A CA  1 
ATOM   3606  C  C   . HIS A 1 473  ? -72.195  59.618  37.063  1.00 236.73 ? 473  HIS A C   1 
ATOM   3607  O  O   . HIS A 1 473  ? -73.042  60.078  36.295  1.00 236.91 ? 473  HIS A O   1 
ATOM   3608  C  CB  . HIS A 1 473  ? -72.988  58.021  38.734  1.00 273.42 ? 473  HIS A CB  1 
ATOM   3609  C  CG  . HIS A 1 473  ? -74.152  57.902  39.749  1.00 295.97 ? 473  HIS A CG  1 
ATOM   3610  N  ND1 . HIS A 1 473  ? -75.134  56.940  39.646  1.00 305.71 ? 473  HIS A ND1 1 
ATOM   3611  C  CD2 . HIS A 1 473  ? -74.449  58.629  40.851  1.00 306.04 ? 473  HIS A CD2 1 
ATOM   3612  C  CE1 . HIS A 1 473  ? -75.987  57.080  40.643  1.00 322.03 ? 473  HIS A CE1 1 
ATOM   3613  N  NE2 . HIS A 1 473  ? -75.595  58.097  41.388  1.00 313.08 ? 473  HIS A NE2 1 
ATOM   3614  N  N   . LYS A 1 474  ? -70.998  59.196  36.673  1.00 223.93 ? 474  LYS A N   1 
ATOM   3615  C  CA  . LYS A 1 474  ? -70.449  59.496  35.360  1.00 212.39 ? 474  LYS A CA  1 
ATOM   3616  C  C   . LYS A 1 474  ? -71.212  58.871  34.197  1.00 200.58 ? 474  LYS A C   1 
ATOM   3617  O  O   . LYS A 1 474  ? -70.887  59.118  33.035  1.00 202.24 ? 474  LYS A O   1 
ATOM   3618  C  CB  . LYS A 1 474  ? -68.960  59.116  35.291  1.00 213.86 ? 474  LYS A CB  1 
ATOM   3619  C  CG  . LYS A 1 474  ? -68.622  57.726  35.810  1.00 215.61 ? 474  LYS A CG  1 
ATOM   3620  C  CD  . LYS A 1 474  ? -67.208  57.326  35.421  1.00 215.95 ? 474  LYS A CD  1 
ATOM   3621  C  CE  . LYS A 1 474  ? -67.062  57.245  33.908  1.00 216.67 ? 474  LYS A CE  1 
ATOM   3622  N  NZ  . LYS A 1 474  ? -65.736  56.709  33.495  1.00 215.98 ? 474  LYS A NZ  1 
ATOM   3623  N  N   . ALA A 1 475  ? -72.227  58.072  34.486  1.00 184.55 ? 475  ALA A N   1 
ATOM   3624  C  CA  . ALA A 1 475  ? -72.923  57.406  33.399  1.00 168.32 ? 475  ALA A CA  1 
ATOM   3625  C  C   . ALA A 1 475  ? -74.362  57.213  33.785  1.00 154.54 ? 475  ALA A C   1 
ATOM   3626  O  O   . ALA A 1 475  ? -74.651  56.812  34.906  1.00 152.16 ? 475  ALA A O   1 
ATOM   3627  C  CB  . ALA A 1 475  ? -72.270  56.074  33.086  1.00 167.68 ? 475  ALA A CB  1 
ATOM   3628  N  N   . LEU A 1 476  ? -75.267  57.513  32.865  1.00 142.16 ? 476  LEU A N   1 
ATOM   3629  C  CA  . LEU A 1 476  ? -76.677  57.339  33.145  1.00 131.37 ? 476  LEU A CA  1 
ATOM   3630  C  C   . LEU A 1 476  ? -77.021  55.892  32.892  1.00 126.92 ? 476  LEU A C   1 
ATOM   3631  O  O   . LEU A 1 476  ? -76.911  55.409  31.773  1.00 129.07 ? 476  LEU A O   1 
ATOM   3632  C  CB  . LEU A 1 476  ? -77.537  58.241  32.274  1.00 124.32 ? 476  LEU A CB  1 
ATOM   3633  C  CG  . LEU A 1 476  ? -76.977  59.625  32.013  1.00 116.76 ? 476  LEU A CG  1 
ATOM   3634  C  CD1 . LEU A 1 476  ? -78.015  60.503  31.380  1.00 115.81 ? 476  LEU A CD1 1 
ATOM   3635  C  CD2 . LEU A 1 476  ? -76.520  60.245  33.292  1.00 115.30 ? 476  LEU A CD2 1 
ATOM   3636  N  N   . LEU A 1 477  ? -77.426  55.190  33.936  1.00 120.57 ? 477  LEU A N   1 
ATOM   3637  C  CA  . LEU A 1 477  ? -77.810  53.807  33.777  1.00 116.05 ? 477  LEU A CA  1 
ATOM   3638  C  C   . LEU A 1 477  ? -79.123  53.783  33.048  1.00 110.13 ? 477  LEU A C   1 
ATOM   3639  O  O   . LEU A 1 477  ? -79.995  54.597  33.315  1.00 110.03 ? 477  LEU A O   1 
ATOM   3640  C  CB  . LEU A 1 477  ? -77.928  53.125  35.130  1.00 120.34 ? 477  LEU A CB  1 
ATOM   3641  C  CG  . LEU A 1 477  ? -76.731  53.416  36.044  1.00 124.53 ? 477  LEU A CG  1 
ATOM   3642  C  CD1 . LEU A 1 477  ? -77.056  53.085  37.501  1.00 128.34 ? 477  LEU A CD1 1 
ATOM   3643  C  CD2 . LEU A 1 477  ? -75.434  52.712  35.592  1.00 124.58 ? 477  LEU A CD2 1 
ATOM   3644  N  N   . VAL A 1 478  ? -79.238  52.872  32.096  1.00 107.50 ? 478  VAL A N   1 
ATOM   3645  C  CA  . VAL A 1 478  ? -80.474  52.673  31.376  1.00 110.20 ? 478  VAL A CA  1 
ATOM   3646  C  C   . VAL A 1 478  ? -81.456  52.168  32.390  1.00 111.91 ? 478  VAL A C   1 
ATOM   3647  O  O   . VAL A 1 478  ? -81.077  51.413  33.269  1.00 109.99 ? 478  VAL A O   1 
ATOM   3648  C  CB  . VAL A 1 478  ? -80.328  51.601  30.335  1.00 111.36 ? 478  VAL A CB  1 
ATOM   3649  C  CG1 . VAL A 1 478  ? -80.789  50.267  30.927  1.00 113.23 ? 478  VAL A CG1 1 
ATOM   3650  C  CG2 . VAL A 1 478  ? -81.134  51.964  29.106  1.00 113.13 ? 478  VAL A CG2 1 
ATOM   3651  N  N   . GLY A 1 479  ? -82.713  52.566  32.266  1.00 116.70 ? 479  GLY A N   1 
ATOM   3652  C  CA  . GLY A 1 479  ? -83.681  52.322  33.313  1.00 121.56 ? 479  GLY A CA  1 
ATOM   3653  C  C   . GLY A 1 479  ? -83.896  53.547  34.190  1.00 122.47 ? 479  GLY A C   1 
ATOM   3654  O  O   . GLY A 1 479  ? -84.973  53.718  34.760  1.00 127.13 ? 479  GLY A O   1 
ATOM   3655  N  N   . GLU A 1 480  ? -82.882  54.406  34.303  1.00 121.48 ? 480  GLU A N   1 
ATOM   3656  C  CA  . GLU A 1 480  ? -82.994  55.615  35.123  1.00 120.37 ? 480  GLU A CA  1 
ATOM   3657  C  C   . GLU A 1 480  ? -83.925  56.636  34.486  1.00 120.87 ? 480  GLU A C   1 
ATOM   3658  O  O   . GLU A 1 480  ? -84.486  56.390  33.428  1.00 121.19 ? 480  GLU A O   1 
ATOM   3659  C  CB  . GLU A 1 480  ? -81.624  56.225  35.432  1.00 121.31 ? 480  GLU A CB  1 
ATOM   3660  C  CG  . GLU A 1 480  ? -80.989  55.680  36.733  1.00 128.66 ? 480  GLU A CG  1 
ATOM   3661  C  CD  . GLU A 1 480  ? -79.738  56.469  37.180  1.00 135.70 ? 480  GLU A CD  1 
ATOM   3662  O  OE1 . GLU A 1 480  ? -79.261  56.312  38.334  1.00 136.87 ? 480  GLU A OE1 1 
ATOM   3663  O  OE2 . GLU A 1 480  ? -79.216  57.269  36.371  1.00 138.95 ? 480  GLU A OE2 1 
ATOM   3664  N  N   . HIS A 1 481  ? -84.110  57.773  35.145  1.00 122.70 ? 481  HIS A N   1 
ATOM   3665  C  CA  . HIS A 1 481  ? -85.052  58.777  34.667  1.00 126.28 ? 481  HIS A CA  1 
ATOM   3666  C  C   . HIS A 1 481  ? -84.431  60.143  34.813  1.00 121.56 ? 481  HIS A C   1 
ATOM   3667  O  O   . HIS A 1 481  ? -84.168  60.607  35.926  1.00 119.13 ? 481  HIS A O   1 
ATOM   3668  C  CB  . HIS A 1 481  ? -86.363  58.733  35.456  1.00 135.23 ? 481  HIS A CB  1 
ATOM   3669  C  CG  . HIS A 1 481  ? -87.351  57.723  34.953  1.00 142.64 ? 481  HIS A CG  1 
ATOM   3670  N  ND1 . HIS A 1 481  ? -88.421  58.063  34.149  1.00 147.21 ? 481  HIS A ND1 1 
ATOM   3671  C  CD2 . HIS A 1 481  ? -87.450  56.387  35.162  1.00 145.16 ? 481  HIS A CD2 1 
ATOM   3672  C  CE1 . HIS A 1 481  ? -89.128  56.980  33.876  1.00 149.93 ? 481  HIS A CE1 1 
ATOM   3673  N  NE2 . HIS A 1 481  ? -88.561  55.949  34.480  1.00 148.87 ? 481  HIS A NE2 1 
ATOM   3674  N  N   . LEU A 1 482  ? -84.223  60.787  33.673  1.00 120.42 ? 482  LEU A N   1 
ATOM   3675  C  CA  . LEU A 1 482  ? -83.480  62.035  33.605  1.00 119.42 ? 482  LEU A CA  1 
ATOM   3676  C  C   . LEU A 1 482  ? -84.336  63.277  33.864  1.00 121.67 ? 482  LEU A C   1 
ATOM   3677  O  O   . LEU A 1 482  ? -85.110  63.704  33.003  1.00 124.90 ? 482  LEU A O   1 
ATOM   3678  C  CB  . LEU A 1 482  ? -82.803  62.138  32.236  1.00 117.45 ? 482  LEU A CB  1 
ATOM   3679  C  CG  . LEU A 1 482  ? -81.546  63.003  32.155  1.00 113.86 ? 482  LEU A CG  1 
ATOM   3680  C  CD1 . LEU A 1 482  ? -80.694  62.633  30.938  1.00 110.58 ? 482  LEU A CD1 1 
ATOM   3681  C  CD2 . LEU A 1 482  ? -81.900  64.491  32.169  1.00 115.14 ? 482  LEU A CD2 1 
ATOM   3682  N  N   . ASN A 1 483  ? -84.197  63.868  35.045  1.00 120.02 ? 483  ASN A N   1 
ATOM   3683  C  CA  . ASN A 1 483  ? -84.874  65.132  35.299  1.00 120.02 ? 483  ASN A CA  1 
ATOM   3684  C  C   . ASN A 1 483  ? -84.006  66.273  34.802  1.00 117.25 ? 483  ASN A C   1 
ATOM   3685  O  O   . ASN A 1 483  ? -82.908  66.498  35.328  1.00 116.36 ? 483  ASN A O   1 
ATOM   3686  C  CB  . ASN A 1 483  ? -85.188  65.318  36.782  1.00 122.97 ? 483  ASN A CB  1 
ATOM   3687  C  CG  . ASN A 1 483  ? -86.289  66.338  37.016  1.00 127.03 ? 483  ASN A CG  1 
ATOM   3688  O  OD1 . ASN A 1 483  ? -87.403  66.189  36.512  1.00 129.02 ? 483  ASN A OD1 1 
ATOM   3689  N  ND2 . ASN A 1 483  ? -85.982  67.378  37.786  1.00 127.61 ? 483  ASN A ND2 1 
ATOM   3690  N  N   . ILE A 1 484  ? -84.519  67.006  33.815  1.00 114.25 ? 484  ILE A N   1 
ATOM   3691  C  CA  . ILE A 1 484  ? -83.724  67.970  33.061  1.00 109.16 ? 484  ILE A CA  1 
ATOM   3692  C  C   . ILE A 1 484  ? -84.380  69.349  33.004  1.00 106.63 ? 484  ILE A C   1 
ATOM   3693  O  O   . ILE A 1 484  ? -85.520  69.485  32.566  1.00 108.33 ? 484  ILE A O   1 
ATOM   3694  C  CB  . ILE A 1 484  ? -83.436  67.428  31.647  1.00 108.08 ? 484  ILE A CB  1 
ATOM   3695  C  CG1 . ILE A 1 484  ? -83.222  68.558  30.642  1.00 107.03 ? 484  ILE A CG1 1 
ATOM   3696  C  CG2 . ILE A 1 484  ? -84.565  66.555  31.186  1.00 109.53 ? 484  ILE A CG2 1 
ATOM   3697  C  CD1 . ILE A 1 484  ? -82.959  68.043  29.248  1.00 104.81 ? 484  ILE A CD1 1 
ATOM   3698  N  N   . ILE A 1 485  ? -83.631  70.366  33.430  1.00 102.10 ? 485  ILE A N   1 
ATOM   3699  C  CA  . ILE A 1 485  ? -84.195  71.672  33.779  1.00 102.76 ? 485  ILE A CA  1 
ATOM   3700  C  C   . ILE A 1 485  ? -84.232  72.737  32.690  1.00 106.45 ? 485  ILE A C   1 
ATOM   3701  O  O   . ILE A 1 485  ? -83.196  73.297  32.303  1.00 107.05 ? 485  ILE A O   1 
ATOM   3702  C  CB  . ILE A 1 485  ? -83.456  72.283  34.933  1.00 99.97  ? 485  ILE A CB  1 
ATOM   3703  C  CG1 . ILE A 1 485  ? -83.845  71.550  36.189  1.00 99.20  ? 485  ILE A CG1 1 
ATOM   3704  C  CG2 . ILE A 1 485  ? -83.851  73.736  35.060  1.00 102.40 ? 485  ILE A CG2 1 
ATOM   3705  C  CD1 . ILE A 1 485  ? -84.644  70.294  35.896  1.00 100.17 ? 485  ILE A CD1 1 
ATOM   3706  N  N   . VAL A 1 486  ? -85.446  73.056  32.254  1.00 106.64 ? 486  VAL A N   1 
ATOM   3707  C  CA  . VAL A 1 486  ? -85.649  73.922  31.115  1.00 106.20 ? 486  VAL A CA  1 
ATOM   3708  C  C   . VAL A 1 486  ? -85.823  75.338  31.589  1.00 106.88 ? 486  VAL A C   1 
ATOM   3709  O  O   . VAL A 1 486  ? -86.897  75.709  32.033  1.00 110.59 ? 486  VAL A O   1 
ATOM   3710  C  CB  . VAL A 1 486  ? -86.905  73.514  30.359  1.00 107.91 ? 486  VAL A CB  1 
ATOM   3711  C  CG1 . VAL A 1 486  ? -86.817  73.970  28.921  1.00 110.07 ? 486  VAL A CG1 1 
ATOM   3712  C  CG2 . VAL A 1 486  ? -87.102  72.001  30.429  1.00 105.09 ? 486  VAL A CG2 1 
ATOM   3713  N  N   . THR A 1 487  ? -84.758  76.124  31.508  1.00 107.55 ? 487  THR A N   1 
ATOM   3714  C  CA  . THR A 1 487  ? -84.805  77.537  31.890  1.00 108.36 ? 487  THR A CA  1 
ATOM   3715  C  C   . THR A 1 487  ? -84.718  78.441  30.651  1.00 110.23 ? 487  THR A C   1 
ATOM   3716  O  O   . THR A 1 487  ? -83.628  78.600  30.080  1.00 108.01 ? 487  THR A O   1 
ATOM   3717  C  CB  . THR A 1 487  ? -83.672  77.902  32.915  1.00 109.42 ? 487  THR A CB  1 
ATOM   3718  O  OG1 . THR A 1 487  ? -82.405  77.418  32.442  1.00 108.47 ? 487  THR A OG1 1 
ATOM   3719  C  CG2 . THR A 1 487  ? -83.952  77.284  34.292  1.00 107.25 ? 487  THR A CG2 1 
ATOM   3720  N  N   . PRO A 1 488  ? -85.865  79.029  30.233  1.00 114.73 ? 488  PRO A N   1 
ATOM   3721  C  CA  . PRO A 1 488  ? -86.008  79.888  29.048  1.00 118.52 ? 488  PRO A CA  1 
ATOM   3722  C  C   . PRO A 1 488  ? -85.501  81.299  29.253  1.00 125.46 ? 488  PRO A C   1 
ATOM   3723  O  O   . PRO A 1 488  ? -85.456  82.051  28.301  1.00 120.90 ? 488  PRO A O   1 
ATOM   3724  C  CB  . PRO A 1 488  ? -87.513  79.925  28.825  1.00 118.77 ? 488  PRO A CB  1 
ATOM   3725  C  CG  . PRO A 1 488  ? -88.085  78.889  29.711  1.00 117.81 ? 488  PRO A CG  1 
ATOM   3726  C  CD  . PRO A 1 488  ? -87.168  78.811  30.872  1.00 116.03 ? 488  PRO A CD  1 
ATOM   3727  N  N   . LYS A 1 489  ? -85.123  81.627  30.481  1.00 139.01 ? 489  LYS A N   1 
ATOM   3728  C  CA  . LYS A 1 489  ? -84.526  82.919  30.828  1.00 152.47 ? 489  LYS A CA  1 
ATOM   3729  C  C   . LYS A 1 489  ? -84.249  83.841  29.645  1.00 162.43 ? 489  LYS A C   1 
ATOM   3730  O  O   . LYS A 1 489  ? -83.737  83.423  28.610  1.00 163.18 ? 489  LYS A O   1 
ATOM   3731  C  CB  . LYS A 1 489  ? -83.227  82.722  31.633  1.00 152.88 ? 489  LYS A CB  1 
ATOM   3732  C  CG  . LYS A 1 489  ? -82.465  84.012  31.973  1.00 155.38 ? 489  LYS A CG  1 
ATOM   3733  C  CD  . LYS A 1 489  ? -81.885  83.937  33.392  1.00 156.84 ? 489  LYS A CD  1 
ATOM   3734  C  CE  . LYS A 1 489  ? -81.699  85.315  34.035  1.00 159.37 ? 489  LYS A CE  1 
ATOM   3735  N  NZ  . LYS A 1 489  ? -82.976  86.090  34.210  1.00 163.28 ? 489  LYS A NZ  1 
ATOM   3736  N  N   . SER A 1 490  ? -84.612  85.106  29.834  1.00 170.85 ? 490  SER A N   1 
ATOM   3737  C  CA  . SER A 1 490  ? -84.292  86.215  28.930  1.00 177.28 ? 490  SER A CA  1 
ATOM   3738  C  C   . SER A 1 490  ? -85.433  86.633  27.993  1.00 182.25 ? 490  SER A C   1 
ATOM   3739  O  O   . SER A 1 490  ? -85.978  87.730  28.149  1.00 185.99 ? 490  SER A O   1 
ATOM   3740  C  CB  . SER A 1 490  ? -82.977  85.961  28.190  1.00 178.86 ? 490  SER A CB  1 
ATOM   3741  O  OG  . SER A 1 490  ? -81.965  85.586  29.126  1.00 178.79 ? 490  SER A OG  1 
ATOM   3742  N  N   . PRO A 1 491  ? -85.825  85.754  27.050  1.00 181.59 ? 491  PRO A N   1 
ATOM   3743  C  CA  . PRO A 1 491  ? -86.867  86.103  26.086  1.00 179.76 ? 491  PRO A CA  1 
ATOM   3744  C  C   . PRO A 1 491  ? -87.720  87.221  26.598  1.00 171.03 ? 491  PRO A C   1 
ATOM   3745  O  O   . PRO A 1 491  ? -88.381  87.123  27.636  1.00 167.40 ? 491  PRO A O   1 
ATOM   3746  C  CB  . PRO A 1 491  ? -87.664  84.810  25.974  1.00 184.49 ? 491  PRO A CB  1 
ATOM   3747  C  CG  . PRO A 1 491  ? -86.584  83.749  26.081  1.00 184.33 ? 491  PRO A CG  1 
ATOM   3748  C  CD  . PRO A 1 491  ? -85.424  84.349  26.879  1.00 182.07 ? 491  PRO A CD  1 
ATOM   3749  N  N   . TYR A 1 492  ? -87.653  88.311  25.861  1.00 166.54 ? 492  TYR A N   1 
ATOM   3750  C  CA  . TYR A 1 492  ? -88.331  89.489  26.252  1.00 165.26 ? 492  TYR A CA  1 
ATOM   3751  C  C   . TYR A 1 492  ? -89.641  89.031  26.772  1.00 166.50 ? 492  TYR A C   1 
ATOM   3752  O  O   . TYR A 1 492  ? -90.189  89.678  27.638  1.00 169.48 ? 492  TYR A O   1 
ATOM   3753  C  CB  . TYR A 1 492  ? -88.518  90.419  25.067  1.00 166.68 ? 492  TYR A CB  1 
ATOM   3754  C  CG  . TYR A 1 492  ? -89.544  90.008  24.000  1.00 166.35 ? 492  TYR A CG  1 
ATOM   3755  C  CD1 . TYR A 1 492  ? -90.056  90.961  23.104  1.00 167.55 ? 492  TYR A CD1 1 
ATOM   3756  C  CD2 . TYR A 1 492  ? -89.993  88.693  23.876  1.00 163.53 ? 492  TYR A CD2 1 
ATOM   3757  C  CE1 . TYR A 1 492  ? -90.974  90.617  22.127  1.00 168.30 ? 492  TYR A CE1 1 
ATOM   3758  C  CE2 . TYR A 1 492  ? -90.920  88.344  22.894  1.00 164.43 ? 492  TYR A CE2 1 
ATOM   3759  C  CZ  . TYR A 1 492  ? -91.399  89.313  22.024  1.00 167.54 ? 492  TYR A CZ  1 
ATOM   3760  O  OH  . TYR A 1 492  ? -92.309  88.979  21.052  1.00 170.89 ? 492  TYR A OH  1 
ATOM   3761  N  N   . ILE A 1 493  ? -90.156  87.906  26.287  1.00 167.52 ? 493  ILE A N   1 
ATOM   3762  C  CA  . ILE A 1 493  ? -91.378  87.412  26.911  1.00 172.89 ? 493  ILE A CA  1 
ATOM   3763  C  C   . ILE A 1 493  ? -91.569  85.897  27.130  1.00 175.63 ? 493  ILE A C   1 
ATOM   3764  O  O   . ILE A 1 493  ? -90.793  85.068  26.664  1.00 175.42 ? 493  ILE A O   1 
ATOM   3765  C  CB  . ILE A 1 493  ? -92.667  88.161  26.405  1.00 244.52 ? 493  ILE A CB  1 
ATOM   3766  C  CG1 . ILE A 1 493  ? -93.006  89.345  27.336  1.00 245.60 ? 493  ILE A CG1 1 
ATOM   3767  C  CG2 . ILE A 1 493  ? -93.861  87.233  26.331  1.00 246.06 ? 493  ILE A CG2 1 
ATOM   3768  C  CD1 . ILE A 1 493  ? -94.255  90.159  26.938  1.00 249.46 ? 493  ILE A CD1 1 
ATOM   3769  N  N   . ASP A 1 494  ? -92.607  85.607  27.917  1.00 178.24 ? 494  ASP A N   1 
ATOM   3770  C  CA  . ASP A 1 494  ? -92.966  84.310  28.480  1.00 177.23 ? 494  ASP A CA  1 
ATOM   3771  C  C   . ASP A 1 494  ? -94.160  83.644  27.790  1.00 180.23 ? 494  ASP A C   1 
ATOM   3772  O  O   . ASP A 1 494  ? -94.751  82.722  28.351  1.00 180.41 ? 494  ASP A O   1 
ATOM   3773  C  CB  . ASP A 1 494  ? -93.363  84.514  29.952  1.00 177.84 ? 494  ASP A CB  1 
ATOM   3774  C  CG  . ASP A 1 494  ? -94.612  85.444  30.130  1.00 174.54 ? 494  ASP A CG  1 
ATOM   3775  O  OD1 . ASP A 1 494  ? -94.716  86.484  29.437  1.00 174.78 ? 494  ASP A OD1 1 
ATOM   3776  O  OD2 . ASP A 1 494  ? -95.476  85.136  30.984  1.00 175.32 ? 494  ASP A OD2 1 
ATOM   3777  N  N   . LYS A 1 495  ? -94.546  84.115  26.606  1.00 182.31 ? 495  LYS A N   1 
ATOM   3778  C  CA  . LYS A 1 495  ? -95.740  83.581  25.939  1.00 183.30 ? 495  LYS A CA  1 
ATOM   3779  C  C   . LYS A 1 495  ? -95.515  82.197  25.335  1.00 177.39 ? 495  LYS A C   1 
ATOM   3780  O  O   . LYS A 1 495  ? -96.010  81.870  24.249  1.00 177.29 ? 495  LYS A O   1 
ATOM   3781  C  CB  . LYS A 1 495  ? -96.294  84.561  24.898  1.00 188.87 ? 495  LYS A CB  1 
ATOM   3782  C  CG  . LYS A 1 495  ? -97.113  85.716  25.493  1.00 192.55 ? 495  LYS A CG  1 
ATOM   3783  C  CD  . LYS A 1 495  ? -97.864  85.290  26.763  1.00 192.16 ? 495  LYS A CD  1 
ATOM   3784  C  CE  . LYS A 1 495  ? -96.995  85.446  28.010  1.00 187.69 ? 495  LYS A CE  1 
ATOM   3785  N  NZ  . LYS A 1 495  ? -97.019  84.241  28.881  1.00 184.39 ? 495  LYS A NZ  1 
ATOM   3786  N  N   . ILE A 1 496  ? -94.766  81.385  26.065  1.00 171.30 ? 496  ILE A N   1 
ATOM   3787  C  CA  . ILE A 1 496  ? -94.426  80.055  25.615  1.00 167.80 ? 496  ILE A CA  1 
ATOM   3788  C  C   . ILE A 1 496  ? -95.617  79.104  25.725  1.00 171.64 ? 496  ILE A C   1 
ATOM   3789  O  O   . ILE A 1 496  ? -96.238  78.971  26.776  1.00 172.00 ? 496  ILE A O   1 
ATOM   3790  C  CB  . ILE A 1 496  ? -93.218  79.496  26.394  1.00 160.35 ? 496  ILE A CB  1 
ATOM   3791  C  CG1 . ILE A 1 496  ? -92.117  80.557  26.544  1.00 153.62 ? 496  ILE A CG1 1 
ATOM   3792  C  CG2 . ILE A 1 496  ? -92.674  78.268  25.700  1.00 161.90 ? 496  ILE A CG2 1 
ATOM   3793  C  CD1 . ILE A 1 496  ? -92.158  81.368  27.861  1.00 150.22 ? 496  ILE A CD1 1 
ATOM   3794  N  N   . THR A 1 497  ? -95.931  78.451  24.616  1.00 176.70 ? 497  THR A N   1 
ATOM   3795  C  CA  . THR A 1 497  ? -96.983  77.452  24.584  1.00 182.65 ? 497  THR A CA  1 
ATOM   3796  C  C   . THR A 1 497  ? -96.475  76.115  25.120  1.00 181.30 ? 497  THR A C   1 
ATOM   3797  O  O   . THR A 1 497  ? -96.854  75.685  26.203  1.00 182.27 ? 497  THR A O   1 
ATOM   3798  C  CB  . THR A 1 497  ? -97.497  77.262  23.149  1.00 189.93 ? 497  THR A CB  1 
ATOM   3799  O  OG1 . THR A 1 497  ? -98.312  76.086  23.082  1.00 192.19 ? 497  THR A OG1 1 
ATOM   3800  C  CG2 . THR A 1 497  ? -96.320  77.125  22.163  1.00 189.42 ? 497  THR A CG2 1 
ATOM   3801  N  N   . HIS A 1 498  ? -95.600  75.475  24.352  1.00 178.85 ? 498  HIS A N   1 
ATOM   3802  C  CA  . HIS A 1 498  ? -95.081  74.151  24.674  1.00 174.73 ? 498  HIS A CA  1 
ATOM   3803  C  C   . HIS A 1 498  ? -93.560  74.127  24.555  1.00 167.48 ? 498  HIS A C   1 
ATOM   3804  O  O   . HIS A 1 498  ? -92.991  74.780  23.669  1.00 167.61 ? 498  HIS A O   1 
ATOM   3805  C  CB  . HIS A 1 498  ? -95.622  73.105  23.693  1.00 179.50 ? 498  HIS A CB  1 
ATOM   3806  C  CG  . HIS A 1 498  ? -97.082  72.810  23.844  1.00 186.44 ? 498  HIS A CG  1 
ATOM   3807  N  ND1 . HIS A 1 498  ? -98.028  73.285  22.966  1.00 191.07 ? 498  HIS A ND1 1 
ATOM   3808  C  CD2 . HIS A 1 498  ? -97.749  72.061  24.753  1.00 187.63 ? 498  HIS A CD2 1 
ATOM   3809  C  CE1 . HIS A 1 498  ? -99.222  72.852  23.335  1.00 194.41 ? 498  HIS A CE1 1 
ATOM   3810  N  NE2 . HIS A 1 498  ? -99.080  72.108  24.415  1.00 192.35 ? 498  HIS A NE2 1 
ATOM   3811  N  N   . TYR A 1 499  ? -92.911  73.375  25.444  1.00 156.75 ? 499  TYR A N   1 
ATOM   3812  C  CA  . TYR A 1 499  ? -91.521  73.001  25.250  1.00 146.55 ? 499  TYR A CA  1 
ATOM   3813  C  C   . TYR A 1 499  ? -91.508  71.729  24.433  1.00 140.89 ? 499  TYR A C   1 
ATOM   3814  O  O   . TYR A 1 499  ? -92.305  70.828  24.693  1.00 139.79 ? 499  TYR A O   1 
ATOM   3815  C  CB  . TYR A 1 499  ? -90.842  72.735  26.581  1.00 142.44 ? 499  TYR A CB  1 
ATOM   3816  C  CG  . TYR A 1 499  ? -90.752  73.939  27.466  1.00 141.81 ? 499  TYR A CG  1 
ATOM   3817  C  CD1 . TYR A 1 499  ? -89.790  74.915  27.258  1.00 140.40 ? 499  TYR A CD1 1 
ATOM   3818  C  CD2 . TYR A 1 499  ? -91.631  74.102  28.517  1.00 144.50 ? 499  TYR A CD2 1 
ATOM   3819  C  CE1 . TYR A 1 499  ? -89.710  76.034  28.087  1.00 140.74 ? 499  TYR A CE1 1 
ATOM   3820  C  CE2 . TYR A 1 499  ? -91.559  75.203  29.356  1.00 144.78 ? 499  TYR A CE2 1 
ATOM   3821  C  CZ  . TYR A 1 499  ? -90.605  76.172  29.141  1.00 142.94 ? 499  TYR A CZ  1 
ATOM   3822  O  OH  . TYR A 1 499  ? -90.570  77.261  29.993  1.00 142.26 ? 499  TYR A OH  1 
ATOM   3823  N  N   . ASN A 1 500  ? -90.602  71.654  23.457  1.00 137.53 ? 500  ASN A N   1 
ATOM   3824  C  CA  . ASN A 1 500  ? -90.437  70.453  22.634  1.00 135.21 ? 500  ASN A CA  1 
ATOM   3825  C  C   . ASN A 1 500  ? -88.987  69.938  22.610  1.00 127.70 ? 500  ASN A C   1 
ATOM   3826  O  O   . ASN A 1 500  ? -88.043  70.683  22.339  1.00 127.15 ? 500  ASN A O   1 
ATOM   3827  C  CB  . ASN A 1 500  ? -90.904  70.706  21.196  1.00 138.20 ? 500  ASN A CB  1 
ATOM   3828  C  CG  . ASN A 1 500  ? -91.985  71.770  21.099  1.00 142.24 ? 500  ASN A CG  1 
ATOM   3829  O  OD1 . ASN A 1 500  ? -93.041  71.664  21.728  1.00 144.49 ? 500  ASN A OD1 1 
ATOM   3830  N  ND2 . ASN A 1 500  ? -91.732  72.797  20.287  1.00 142.85 ? 500  ASN A ND2 1 
ATOM   3831  N  N   . TYR A 1 501  ? -88.809  68.657  22.893  1.00 124.02 ? 501  TYR A N   1 
ATOM   3832  C  CA  . TYR A 1 501  ? -87.484  68.074  22.842  1.00 119.56 ? 501  TYR A CA  1 
ATOM   3833  C  C   . TYR A 1 501  ? -87.328  67.145  21.648  1.00 119.32 ? 501  TYR A C   1 
ATOM   3834  O  O   . TYR A 1 501  ? -88.254  66.955  20.852  1.00 120.70 ? 501  TYR A O   1 
ATOM   3835  C  CB  . TYR A 1 501  ? -87.205  67.292  24.108  1.00 120.63 ? 501  TYR A CB  1 
ATOM   3836  C  CG  . TYR A 1 501  ? -88.088  66.081  24.251  1.00 124.94 ? 501  TYR A CG  1 
ATOM   3837  C  CD1 . TYR A 1 501  ? -87.629  64.812  23.934  1.00 125.49 ? 501  TYR A CD1 1 
ATOM   3838  C  CD2 . TYR A 1 501  ? -89.384  66.211  24.691  1.00 128.92 ? 501  TYR A CD2 1 
ATOM   3839  C  CE1 . TYR A 1 501  ? -88.452  63.699  24.069  1.00 128.35 ? 501  TYR A CE1 1 
ATOM   3840  C  CE2 . TYR A 1 501  ? -90.211  65.120  24.829  1.00 131.91 ? 501  TYR A CE2 1 
ATOM   3841  C  CZ  . TYR A 1 501  ? -89.750  63.867  24.517  1.00 131.81 ? 501  TYR A CZ  1 
ATOM   3842  O  OH  . TYR A 1 501  ? -90.605  62.793  24.657  1.00 134.22 ? 501  TYR A OH  1 
ATOM   3843  N  N   . LEU A 1 502  ? -86.155  66.530  21.566  1.00 116.55 ? 502  LEU A N   1 
ATOM   3844  C  CA  . LEU A 1 502  ? -85.744  65.804  20.374  1.00 114.45 ? 502  LEU A CA  1 
ATOM   3845  C  C   . LEU A 1 502  ? -84.427  65.060  20.684  1.00 113.27 ? 502  LEU A C   1 
ATOM   3846  O  O   . LEU A 1 502  ? -83.392  65.688  20.907  1.00 110.26 ? 502  LEU A O   1 
ATOM   3847  C  CB  . LEU A 1 502  ? -85.566  66.822  19.239  1.00 111.17 ? 502  LEU A CB  1 
ATOM   3848  C  CG  . LEU A 1 502  ? -85.560  66.363  17.784  1.00 109.18 ? 502  LEU A CG  1 
ATOM   3849  C  CD1 . LEU A 1 502  ? -86.715  65.393  17.466  1.00 108.73 ? 502  LEU A CD1 1 
ATOM   3850  C  CD2 . LEU A 1 502  ? -85.579  67.615  16.922  1.00 109.30 ? 502  LEU A CD2 1 
ATOM   3851  N  N   . ILE A 1 503  ? -84.472  63.727  20.707  1.00 112.26 ? 503  ILE A N   1 
ATOM   3852  C  CA  . ILE A 1 503  ? -83.332  62.933  21.165  1.00 111.07 ? 503  ILE A CA  1 
ATOM   3853  C  C   . ILE A 1 503  ? -82.823  62.000  20.079  1.00 111.09 ? 503  ILE A C   1 
ATOM   3854  O  O   . ILE A 1 503  ? -83.558  61.124  19.621  1.00 112.34 ? 503  ILE A O   1 
ATOM   3855  C  CB  . ILE A 1 503  ? -83.678  62.077  22.411  1.00 110.48 ? 503  ILE A CB  1 
ATOM   3856  C  CG1 . ILE A 1 503  ? -84.315  62.930  23.514  1.00 111.52 ? 503  ILE A CG1 1 
ATOM   3857  C  CG2 . ILE A 1 503  ? -82.438  61.381  22.939  1.00 107.82 ? 503  ILE A CG2 1 
ATOM   3858  C  CD1 . ILE A 1 503  ? -84.774  62.145  24.749  1.00 109.92 ? 503  ILE A CD1 1 
ATOM   3859  N  N   . LEU A 1 504  ? -81.559  62.205  19.687  1.00 112.30 ? 504  LEU A N   1 
ATOM   3860  C  CA  . LEU A 1 504  ? -80.871  61.395  18.669  1.00 112.81 ? 504  LEU A CA  1 
ATOM   3861  C  C   . LEU A 1 504  ? -79.944  60.388  19.335  1.00 115.46 ? 504  LEU A C   1 
ATOM   3862  O  O   . LEU A 1 504  ? -79.643  60.514  20.521  1.00 116.43 ? 504  LEU A O   1 
ATOM   3863  C  CB  . LEU A 1 504  ? -80.026  62.265  17.735  1.00 107.70 ? 504  LEU A CB  1 
ATOM   3864  C  CG  . LEU A 1 504  ? -80.627  63.368  16.878  1.00 106.62 ? 504  LEU A CG  1 
ATOM   3865  C  CD1 . LEU A 1 504  ? -81.956  63.830  17.424  1.00 107.70 ? 504  LEU A CD1 1 
ATOM   3866  C  CD2 . LEU A 1 504  ? -79.658  64.533  16.803  1.00 98.16  ? 504  LEU A CD2 1 
ATOM   3867  N  N   . SER A 1 505  ? -79.469  59.411  18.565  1.00 119.56 ? 505  SER A N   1 
ATOM   3868  C  CA  . SER A 1 505  ? -78.492  58.439  19.064  1.00 119.46 ? 505  SER A CA  1 
ATOM   3869  C  C   . SER A 1 505  ? -78.012  57.470  17.988  1.00 122.59 ? 505  SER A C   1 
ATOM   3870  O  O   . SER A 1 505  ? -78.809  56.752  17.372  1.00 122.66 ? 505  SER A O   1 
ATOM   3871  C  CB  . SER A 1 505  ? -79.054  57.643  20.236  1.00 118.69 ? 505  SER A CB  1 
ATOM   3872  O  OG  . SER A 1 505  ? -78.083  56.721  20.687  1.00 116.73 ? 505  SER A OG  1 
ATOM   3873  N  N   . LYS A 1 506  ? -76.701  57.423  17.796  1.00 124.38 ? 506  LYS A N   1 
ATOM   3874  C  CA  . LYS A 1 506  ? -76.165  56.700  16.668  1.00 125.98 ? 506  LYS A CA  1 
ATOM   3875  C  C   . LYS A 1 506  ? -76.814  57.283  15.447  1.00 130.37 ? 506  LYS A C   1 
ATOM   3876  O  O   . LYS A 1 506  ? -77.565  56.600  14.758  1.00 133.23 ? 506  LYS A O   1 
ATOM   3877  C  CB  . LYS A 1 506  ? -76.482  55.219  16.760  1.00 125.22 ? 506  LYS A CB  1 
ATOM   3878  C  CG  . LYS A 1 506  ? -75.573  54.490  17.703  1.00 121.14 ? 506  LYS A CG  1 
ATOM   3879  C  CD  . LYS A 1 506  ? -76.239  53.241  18.205  1.00 119.81 ? 506  LYS A CD  1 
ATOM   3880  C  CE  . LYS A 1 506  ? -77.643  53.549  18.705  1.00 120.46 ? 506  LYS A CE  1 
ATOM   3881  N  NZ  . LYS A 1 506  ? -77.643  54.166  20.049  1.00 118.84 ? 506  LYS A NZ  1 
ATOM   3882  N  N   . GLY A 1 507  ? -76.567  58.575  15.235  1.00 130.27 ? 507  GLY A N   1 
ATOM   3883  C  CA  . GLY A 1 507  ? -76.947  59.274  14.015  1.00 133.62 ? 507  GLY A CA  1 
ATOM   3884  C  C   . GLY A 1 507  ? -78.432  59.414  13.706  1.00 138.66 ? 507  GLY A C   1 
ATOM   3885  O  O   . GLY A 1 507  ? -78.806  59.944  12.643  1.00 139.69 ? 507  GLY A O   1 
ATOM   3886  N  N   . LYS A 1 508  ? -79.271  58.956  14.639  1.00 138.58 ? 508  LYS A N   1 
ATOM   3887  C  CA  . LYS A 1 508  ? -80.720  58.882  14.426  1.00 140.68 ? 508  LYS A CA  1 
ATOM   3888  C  C   . LYS A 1 508  ? -81.544  59.440  15.581  1.00 135.49 ? 508  LYS A C   1 
ATOM   3889  O  O   . LYS A 1 508  ? -81.309  59.120  16.735  1.00 133.02 ? 508  LYS A O   1 
ATOM   3890  C  CB  . LYS A 1 508  ? -81.167  57.435  14.139  1.00 142.77 ? 508  LYS A CB  1 
ATOM   3891  C  CG  . LYS A 1 508  ? -81.268  57.109  12.652  1.00 145.91 ? 508  LYS A CG  1 
ATOM   3892  C  CD  . LYS A 1 508  ? -81.280  55.615  12.376  1.00 146.13 ? 508  LYS A CD  1 
ATOM   3893  C  CE  . LYS A 1 508  ? -80.649  55.339  11.014  1.00 147.20 ? 508  LYS A CE  1 
ATOM   3894  N  NZ  . LYS A 1 508  ? -80.313  53.907  10.798  1.00 146.42 ? 508  LYS A NZ  1 
ATOM   3895  N  N   . ILE A 1 509  ? -82.513  60.279  15.246  1.00 133.26 ? 509  ILE A N   1 
ATOM   3896  C  CA  . ILE A 1 509  ? -83.552  60.677  16.172  1.00 129.21 ? 509  ILE A CA  1 
ATOM   3897  C  C   . ILE A 1 509  ? -84.362  59.457  16.575  1.00 127.03 ? 509  ILE A C   1 
ATOM   3898  O  O   . ILE A 1 509  ? -84.771  58.681  15.718  1.00 128.68 ? 509  ILE A O   1 
ATOM   3899  C  CB  . ILE A 1 509  ? -84.497  61.630  15.479  1.00 129.03 ? 509  ILE A CB  1 
ATOM   3900  C  CG1 . ILE A 1 509  ? -83.689  62.744  14.820  1.00 127.44 ? 509  ILE A CG1 1 
ATOM   3901  C  CG2 . ILE A 1 509  ? -85.541  62.152  16.455  1.00 130.66 ? 509  ILE A CG2 1 
ATOM   3902  C  CD1 . ILE A 1 509  ? -84.510  63.679  13.967  1.00 129.07 ? 509  ILE A CD1 1 
ATOM   3903  N  N   . ILE A 1 510  ? -84.617  59.294  17.869  1.00 124.67 ? 510  ILE A N   1 
ATOM   3904  C  CA  . ILE A 1 510  ? -85.333  58.113  18.353  1.00 124.33 ? 510  ILE A CA  1 
ATOM   3905  C  C   . ILE A 1 510  ? -86.470  58.465  19.311  1.00 126.02 ? 510  ILE A C   1 
ATOM   3906  O  O   . ILE A 1 510  ? -87.371  57.661  19.552  1.00 125.33 ? 510  ILE A O   1 
ATOM   3907  C  CB  . ILE A 1 510  ? -84.377  57.086  19.016  1.00 130.89 ? 510  ILE A CB  1 
ATOM   3908  C  CG1 . ILE A 1 510  ? -83.167  57.787  19.640  1.00 128.25 ? 510  ILE A CG1 1 
ATOM   3909  C  CG2 . ILE A 1 510  ? -83.902  56.043  18.013  1.00 130.76 ? 510  ILE A CG2 1 
ATOM   3910  C  CD1 . ILE A 1 510  ? -82.213  56.833  20.346  1.00 125.40 ? 510  ILE A CD1 1 
ATOM   3911  N  N   . HIS A 1 511  ? -86.424  59.672  19.851  1.00 129.04 ? 511  HIS A N   1 
ATOM   3912  C  CA  . HIS A 1 511  ? -87.510  60.149  20.677  1.00 135.01 ? 511  HIS A CA  1 
ATOM   3913  C  C   . HIS A 1 511  ? -87.751  61.606  20.358  1.00 138.31 ? 511  HIS A C   1 
ATOM   3914  O  O   . HIS A 1 511  ? -86.879  62.288  19.825  1.00 138.12 ? 511  HIS A O   1 
ATOM   3915  C  CB  . HIS A 1 511  ? -87.172  59.996  22.156  1.00 136.68 ? 511  HIS A CB  1 
ATOM   3916  C  CG  . HIS A 1 511  ? -86.648  58.642  22.521  1.00 137.45 ? 511  HIS A CG  1 
ATOM   3917  N  ND1 . HIS A 1 511  ? -87.447  57.522  22.565  1.00 139.42 ? 511  HIS A ND1 1 
ATOM   3918  C  CD2 . HIS A 1 511  ? -85.406  58.233  22.874  1.00 135.63 ? 511  HIS A CD2 1 
ATOM   3919  C  CE1 . HIS A 1 511  ? -86.721  56.478  22.921  1.00 137.41 ? 511  HIS A CE1 1 
ATOM   3920  N  NE2 . HIS A 1 511  ? -85.479  56.882  23.115  1.00 135.10 ? 511  HIS A NE2 1 
ATOM   3921  N  N   . PHE A 1 512  ? -88.946  62.074  20.684  1.00 143.27 ? 512  PHE A N   1 
ATOM   3922  C  CA  . PHE A 1 512  ? -89.324  63.458  20.462  1.00 147.48 ? 512  PHE A CA  1 
ATOM   3923  C  C   . PHE A 1 512  ? -90.691  63.639  21.098  1.00 147.45 ? 512  PHE A C   1 
ATOM   3924  O  O   . PHE A 1 512  ? -91.466  62.688  21.197  1.00 145.90 ? 512  PHE A O   1 
ATOM   3925  C  CB  . PHE A 1 512  ? -89.389  63.756  18.967  1.00 155.02 ? 512  PHE A CB  1 
ATOM   3926  C  CG  . PHE A 1 512  ? -90.477  63.008  18.256  1.00 162.07 ? 512  PHE A CG  1 
ATOM   3927  C  CD1 . PHE A 1 512  ? -91.426  63.679  17.506  1.00 166.10 ? 512  PHE A CD1 1 
ATOM   3928  C  CD2 . PHE A 1 512  ? -90.566  61.627  18.367  1.00 162.44 ? 512  PHE A CD2 1 
ATOM   3929  C  CE1 . PHE A 1 512  ? -92.426  62.982  16.867  1.00 169.37 ? 512  PHE A CE1 1 
ATOM   3930  C  CE2 . PHE A 1 512  ? -91.568  60.926  17.732  1.00 165.18 ? 512  PHE A CE2 1 
ATOM   3931  C  CZ  . PHE A 1 512  ? -92.498  61.600  16.984  1.00 168.46 ? 512  PHE A CZ  1 
ATOM   3932  N  N   . GLY A 1 513  ? -90.992  64.850  21.543  1.00 148.17 ? 513  GLY A N   1 
ATOM   3933  C  CA  . GLY A 1 513  ? -92.221  65.054  22.283  1.00 151.16 ? 513  GLY A CA  1 
ATOM   3934  C  C   . GLY A 1 513  ? -92.484  66.475  22.741  1.00 152.41 ? 513  GLY A C   1 
ATOM   3935  O  O   . GLY A 1 513  ? -91.802  67.425  22.332  1.00 150.43 ? 513  GLY A O   1 
ATOM   3936  N  N   . THR A 1 514  ? -93.486  66.622  23.603  1.00 154.72 ? 514  THR A N   1 
ATOM   3937  C  CA  . THR A 1 514  ? -93.894  67.947  24.035  1.00 157.28 ? 514  THR A CA  1 
ATOM   3938  C  C   . THR A 1 514  ? -94.488  67.963  25.441  1.00 155.82 ? 514  THR A C   1 
ATOM   3939  O  O   . THR A 1 514  ? -95.360  67.165  25.765  1.00 156.91 ? 514  THR A O   1 
ATOM   3940  C  CB  . THR A 1 514  ? -94.859  68.581  23.008  1.00 162.09 ? 514  THR A CB  1 
ATOM   3941  O  OG1 . THR A 1 514  ? -94.098  69.174  21.948  1.00 162.29 ? 514  THR A OG1 1 
ATOM   3942  C  CG2 . THR A 1 514  ? -95.717  69.652  23.647  1.00 165.15 ? 514  THR A CG2 1 
ATOM   3943  N  N   . ARG A 1 515  ? -93.975  68.861  26.277  1.00 155.53 ? 515  ARG A N   1 
ATOM   3944  C  CA  . ARG A 1 515  ? -94.577  69.130  27.573  1.00 159.31 ? 515  ARG A CA  1 
ATOM   3945  C  C   . ARG A 1 515  ? -95.245  70.487  27.520  1.00 159.95 ? 515  ARG A C   1 
ATOM   3946  O  O   . ARG A 1 515  ? -94.675  71.433  26.971  1.00 159.58 ? 515  ARG A O   1 
ATOM   3947  C  CB  . ARG A 1 515  ? -93.523  69.135  28.675  1.00 161.69 ? 515  ARG A CB  1 
ATOM   3948  C  CG  . ARG A 1 515  ? -92.651  67.917  28.665  1.00 163.94 ? 515  ARG A CG  1 
ATOM   3949  C  CD  . ARG A 1 515  ? -93.487  66.676  28.469  1.00 169.81 ? 515  ARG A CD  1 
ATOM   3950  N  NE  . ARG A 1 515  ? -92.652  65.491  28.462  1.00 171.64 ? 515  ARG A NE  1 
ATOM   3951  C  CZ  . ARG A 1 515  ? -91.946  65.089  29.511  1.00 174.02 ? 515  ARG A CZ  1 
ATOM   3952  N  NH1 . ARG A 1 515  ? -91.978  65.784  30.648  1.00 175.22 ? 515  ARG A NH1 1 
ATOM   3953  N  NH2 . ARG A 1 515  ? -91.199  63.997  29.421  1.00 173.73 ? 515  ARG A NH2 1 
ATOM   3954  N  N   . GLU A 1 516  ? -96.445  70.591  28.085  1.00 160.44 ? 516  GLU A N   1 
ATOM   3955  C  CA  . GLU A 1 516  ? -97.106  71.882  28.132  1.00 160.08 ? 516  GLU A CA  1 
ATOM   3956  C  C   . GLU A 1 516  ? -96.340  72.761  29.103  1.00 155.86 ? 516  GLU A C   1 
ATOM   3957  O  O   . GLU A 1 516  ? -95.852  72.274  30.114  1.00 151.79 ? 516  GLU A O   1 
ATOM   3958  C  CB  . GLU A 1 516  ? -98.580  71.751  28.527  1.00 164.68 ? 516  GLU A CB  1 
ATOM   3959  C  CG  . GLU A 1 516  ? -99.286  73.106  28.651  1.00 168.44 ? 516  GLU A CG  1 
ATOM   3960  C  CD  . GLU A 1 516  ? -100.663 73.161  27.992  1.00 173.11 ? 516  GLU A CD  1 
ATOM   3961  O  OE1 . GLU A 1 516  ? -101.502 73.952  28.464  1.00 175.20 ? 516  GLU A OE1 1 
ATOM   3962  O  OE2 . GLU A 1 516  ? -100.903 72.442  26.997  1.00 175.01 ? 516  GLU A OE2 1 
ATOM   3963  N  N   . LYS A 1 517  ? -96.201  74.043  28.779  1.00 156.41 ? 517  LYS A N   1 
ATOM   3964  C  CA  . LYS A 1 517  ? -95.473  74.971  29.641  1.00 156.21 ? 517  LYS A CA  1 
ATOM   3965  C  C   . LYS A 1 517  ? -96.307  75.441  30.823  1.00 163.88 ? 517  LYS A C   1 
ATOM   3966  O  O   . LYS A 1 517  ? -97.449  75.857  30.660  1.00 169.22 ? 517  LYS A O   1 
ATOM   3967  C  CB  . LYS A 1 517  ? -94.980  76.188  28.857  1.00 152.65 ? 517  LYS A CB  1 
ATOM   3968  C  CG  . LYS A 1 517  ? -93.937  77.017  29.619  1.00 148.01 ? 517  LYS A CG  1 
ATOM   3969  C  CD  . LYS A 1 517  ? -94.452  78.335  30.193  1.00 147.56 ? 517  LYS A CD  1 
ATOM   3970  C  CE  . LYS A 1 517  ? -93.284  79.168  30.734  1.00 143.83 ? 517  LYS A CE  1 
ATOM   3971  N  NZ  . LYS A 1 517  ? -93.400  80.630  30.436  1.00 144.63 ? 517  LYS A NZ  1 
ATOM   3972  N  N   . PHE A 1 518  ? -95.723  75.400  32.014  1.00 165.16 ? 518  PHE A N   1 
ATOM   3973  C  CA  . PHE A 1 518  ? -96.431  75.822  33.208  1.00 171.08 ? 518  PHE A CA  1 
ATOM   3974  C  C   . PHE A 1 518  ? -96.707  77.317  33.221  1.00 175.54 ? 518  PHE A C   1 
ATOM   3975  O  O   . PHE A 1 518  ? -95.825  78.123  33.533  1.00 171.81 ? 518  PHE A O   1 
ATOM   3976  C  CB  . PHE A 1 518  ? -95.674  75.378  34.448  1.00 171.95 ? 518  PHE A CB  1 
ATOM   3977  C  CG  . PHE A 1 518  ? -95.843  73.925  34.745  1.00 176.02 ? 518  PHE A CG  1 
ATOM   3978  C  CD1 . PHE A 1 518  ? -96.926  73.232  34.222  1.00 179.68 ? 518  PHE A CD1 1 
ATOM   3979  C  CD2 . PHE A 1 518  ? -94.947  73.254  35.561  1.00 175.98 ? 518  PHE A CD2 1 
ATOM   3980  C  CE1 . PHE A 1 518  ? -97.107  71.897  34.492  1.00 180.75 ? 518  PHE A CE1 1 
ATOM   3981  C  CE2 . PHE A 1 518  ? -95.121  71.912  35.841  1.00 177.07 ? 518  PHE A CE2 1 
ATOM   3982  C  CZ  . PHE A 1 518  ? -96.204  71.232  35.303  1.00 179.22 ? 518  PHE A CZ  1 
ATOM   3983  N  N   . SER A 1 519  ? -97.956  77.650  32.899  1.00 183.83 ? 519  SER A N   1 
ATOM   3984  C  CA  . SER A 1 519  ? -98.390  79.010  32.614  1.00 190.36 ? 519  SER A CA  1 
ATOM   3985  C  C   . SER A 1 519  ? -97.761  80.024  33.542  1.00 192.63 ? 519  SER A C   1 
ATOM   3986  O  O   . SER A 1 519  ? -97.202  81.027  33.107  1.00 195.40 ? 519  SER A O   1 
ATOM   3987  C  CB  . SER A 1 519  ? -99.908  79.094  32.725  1.00 193.13 ? 519  SER A CB  1 
ATOM   3988  O  OG  . SER A 1 519  ? -100.512 77.912  32.235  1.00 193.03 ? 519  SER A OG  1 
ATOM   3989  N  N   . ASP A 1 520  ? -97.865  79.754  34.831  1.00 192.75 ? 520  ASP A N   1 
ATOM   3990  C  CA  . ASP A 1 520  ? -97.254  80.610  35.825  1.00 194.65 ? 520  ASP A CA  1 
ATOM   3991  C  C   . ASP A 1 520  ? -95.734  80.663  35.650  1.00 189.22 ? 520  ASP A C   1 
ATOM   3992  O  O   . ASP A 1 520  ? -95.233  81.374  34.773  1.00 189.28 ? 520  ASP A O   1 
ATOM   3993  C  CB  . ASP A 1 520  ? -97.628  80.152  37.241  1.00 203.06 ? 520  ASP A CB  1 
ATOM   3994  C  CG  . ASP A 1 520  ? -97.455  78.650  37.447  1.00 211.81 ? 520  ASP A CG  1 
ATOM   3995  O  OD1 . ASP A 1 520  ? -97.071  77.949  36.484  1.00 214.19 ? 520  ASP A OD1 1 
ATOM   3996  O  OD2 . ASP A 1 520  ? -97.705  78.178  38.581  1.00 215.54 ? 520  ASP A OD2 1 
ATOM   3997  N  N   . ALA A 1 521  ? -95.013  79.877  36.455  1.00 183.98 ? 521  ALA A N   1 
ATOM   3998  C  CA  . ALA A 1 521  ? -93.570  80.057  36.653  1.00 174.79 ? 521  ALA A CA  1 
ATOM   3999  C  C   . ALA A 1 521  ? -92.690  79.887  35.414  1.00 161.21 ? 521  ALA A C   1 
ATOM   4000  O  O   . ALA A 1 521  ? -93.139  79.420  34.362  1.00 160.06 ? 521  ALA A O   1 
ATOM   4001  C  CB  . ALA A 1 521  ? -93.064  79.186  37.821  1.00 175.46 ? 521  ALA A CB  1 
ATOM   4002  N  N   . SER A 1 522  ? -91.433  80.292  35.581  1.00 149.74 ? 522  SER A N   1 
ATOM   4003  C  CA  . SER A 1 522  ? -90.412  80.208  34.546  1.00 140.83 ? 522  SER A CA  1 
ATOM   4004  C  C   . SER A 1 522  ? -90.115  78.767  34.080  1.00 133.95 ? 522  SER A C   1 
ATOM   4005  O  O   . SER A 1 522  ? -90.709  78.252  33.120  1.00 135.28 ? 522  SER A O   1 
ATOM   4006  C  CB  . SER A 1 522  ? -89.117  80.873  35.052  1.00 137.54 ? 522  SER A CB  1 
ATOM   4007  O  OG  . SER A 1 522  ? -88.116  80.928  34.036  1.00 135.65 ? 522  SER A OG  1 
ATOM   4008  N  N   . TYR A 1 523  ? -89.189  78.122  34.779  1.00 125.32 ? 523  TYR A N   1 
ATOM   4009  C  CA  . TYR A 1 523  ? -88.680  76.821  34.380  1.00 117.23 ? 523  TYR A CA  1 
ATOM   4010  C  C   . TYR A 1 523  ? -89.484  75.681  34.915  1.00 113.72 ? 523  TYR A C   1 
ATOM   4011  O  O   . TYR A 1 523  ? -90.006  75.737  36.022  1.00 112.43 ? 523  TYR A O   1 
ATOM   4012  C  CB  . TYR A 1 523  ? -87.267  76.643  34.927  1.00 114.38 ? 523  TYR A CB  1 
ATOM   4013  C  CG  . TYR A 1 523  ? -87.143  76.823  36.444  1.00 112.83 ? 523  TYR A CG  1 
ATOM   4014  C  CD1 . TYR A 1 523  ? -87.370  75.767  37.321  1.00 112.02 ? 523  TYR A CD1 1 
ATOM   4015  C  CD2 . TYR A 1 523  ? -86.778  78.046  36.991  1.00 111.04 ? 523  TYR A CD2 1 
ATOM   4016  C  CE1 . TYR A 1 523  ? -87.243  75.930  38.682  1.00 110.55 ? 523  TYR A CE1 1 
ATOM   4017  C  CE2 . TYR A 1 523  ? -86.650  78.211  38.342  1.00 108.95 ? 523  TYR A CE2 1 
ATOM   4018  C  CZ  . TYR A 1 523  ? -86.886  77.154  39.177  1.00 109.61 ? 523  TYR A CZ  1 
ATOM   4019  O  OH  . TYR A 1 523  ? -86.752  77.328  40.523  1.00 110.86 ? 523  TYR A OH  1 
ATOM   4020  N  N   . GLN A 1 524  ? -89.519  74.602  34.163  1.00 114.16 ? 524  GLN A N   1 
ATOM   4021  C  CA  . GLN A 1 524  ? -89.927  73.352  34.766  1.00 117.66 ? 524  GLN A CA  1 
ATOM   4022  C  C   . GLN A 1 524  ? -88.972  72.205  34.446  1.00 118.65 ? 524  GLN A C   1 
ATOM   4023  O  O   . GLN A 1 524  ? -87.869  72.410  33.925  1.00 117.68 ? 524  GLN A O   1 
ATOM   4024  C  CB  . GLN A 1 524  ? -91.334  72.996  34.348  1.00 120.38 ? 524  GLN A CB  1 
ATOM   4025  C  CG  . GLN A 1 524  ? -91.467  72.729  32.897  1.00 120.73 ? 524  GLN A CG  1 
ATOM   4026  C  CD  . GLN A 1 524  ? -92.764  73.237  32.390  1.00 125.19 ? 524  GLN A CD  1 
ATOM   4027  O  OE1 . GLN A 1 524  ? -93.143  74.376  32.680  1.00 126.60 ? 524  GLN A OE1 1 
ATOM   4028  N  NE2 . GLN A 1 524  ? -93.483  72.397  31.642  1.00 127.22 ? 524  GLN A NE2 1 
ATOM   4029  N  N   . SER A 1 525  ? -89.385  70.999  34.811  1.00 119.98 ? 525  SER A N   1 
ATOM   4030  C  CA  . SER A 1 525  ? -88.566  69.831  34.581  1.00 118.83 ? 525  SER A CA  1 
ATOM   4031  C  C   . SER A 1 525  ? -89.217  69.041  33.463  1.00 120.40 ? 525  SER A C   1 
ATOM   4032  O  O   . SER A 1 525  ? -90.440  69.044  33.336  1.00 120.15 ? 525  SER A O   1 
ATOM   4033  C  CB  . SER A 1 525  ? -88.474  68.977  35.856  1.00 121.61 ? 525  SER A CB  1 
ATOM   4034  O  OG  . SER A 1 525  ? -88.322  69.760  37.046  1.00 122.60 ? 525  SER A OG  1 
ATOM   4035  N  N   . ILE A 1 526  ? -88.393  68.402  32.633  1.00 120.54 ? 526  ILE A N   1 
ATOM   4036  C  CA  . ILE A 1 526  ? -88.867  67.432  31.645  1.00 117.66 ? 526  ILE A CA  1 
ATOM   4037  C  C   . ILE A 1 526  ? -88.296  66.080  32.023  1.00 114.48 ? 526  ILE A C   1 
ATOM   4038  O  O   . ILE A 1 526  ? -87.088  65.913  32.112  1.00 106.57 ? 526  ILE A O   1 
ATOM   4039  C  CB  . ILE A 1 526  ? -88.413  67.767  30.200  1.00 111.25 ? 526  ILE A CB  1 
ATOM   4040  C  CG1 . ILE A 1 526  ? -88.707  69.223  29.830  1.00 106.70 ? 526  ILE A CG1 1 
ATOM   4041  C  CG2 . ILE A 1 526  ? -89.102  66.859  29.211  1.00 112.37 ? 526  ILE A CG2 1 
ATOM   4042  C  CD1 . ILE A 1 526  ? -88.571  69.527  28.352  1.00 107.07 ? 526  ILE A CD1 1 
ATOM   4043  N  N   . ASN A 1 527  ? -89.144  65.101  32.257  1.00 116.36 ? 527  ASN A N   1 
ATOM   4044  C  CA  . ASN A 1 527  ? -88.584  63.845  32.685  1.00 120.83 ? 527  ASN A CA  1 
ATOM   4045  C  C   . ASN A 1 527  ? -88.537  62.744  31.637  1.00 125.59 ? 527  ASN A C   1 
ATOM   4046  O  O   . ASN A 1 527  ? -89.521  62.053  31.391  1.00 128.65 ? 527  ASN A O   1 
ATOM   4047  C  CB  . ASN A 1 527  ? -89.276  63.357  33.930  1.00 123.65 ? 527  ASN A CB  1 
ATOM   4048  C  CG  . ASN A 1 527  ? -88.421  62.411  34.705  1.00 123.81 ? 527  ASN A CG  1 
ATOM   4049  O  OD1 . ASN A 1 527  ? -88.121  61.305  34.251  1.00 122.51 ? 527  ASN A OD1 1 
ATOM   4050  N  ND2 . ASN A 1 527  ? -87.999  62.841  35.883  1.00 125.82 ? 527  ASN A ND2 1 
ATOM   4051  N  N   . ILE A 1 528  ? -87.370  62.566  31.039  1.00 127.11 ? 528  ILE A N   1 
ATOM   4052  C  CA  . ILE A 1 528  ? -87.181  61.528  30.044  1.00 129.42 ? 528  ILE A CA  1 
ATOM   4053  C  C   . ILE A 1 528  ? -86.600  60.273  30.660  1.00 129.88 ? 528  ILE A C   1 
ATOM   4054  O  O   . ILE A 1 528  ? -85.533  60.304  31.267  1.00 128.10 ? 528  ILE A O   1 
ATOM   4055  C  CB  . ILE A 1 528  ? -86.212  61.983  28.947  1.00 132.26 ? 528  ILE A CB  1 
ATOM   4056  C  CG1 . ILE A 1 528  ? -86.558  63.391  28.489  1.00 134.09 ? 528  ILE A CG1 1 
ATOM   4057  C  CG2 . ILE A 1 528  ? -86.200  61.001  27.783  1.00 133.34 ? 528  ILE A CG2 1 
ATOM   4058  C  CD1 . ILE A 1 528  ? -85.917  64.437  29.332  1.00 133.88 ? 528  ILE A CD1 1 
ATOM   4059  N  N   . PRO A 1 529  ? -87.303  59.154  30.512  1.00 130.32 ? 529  PRO A N   1 
ATOM   4060  C  CA  . PRO A 1 529  ? -86.654  57.870  30.756  1.00 131.02 ? 529  PRO A CA  1 
ATOM   4061  C  C   . PRO A 1 529  ? -85.376  57.748  29.902  1.00 129.68 ? 529  PRO A C   1 
ATOM   4062  O  O   . PRO A 1 529  ? -85.346  58.237  28.767  1.00 131.87 ? 529  PRO A O   1 
ATOM   4063  C  CB  . PRO A 1 529  ? -87.708  56.872  30.273  1.00 131.57 ? 529  PRO A CB  1 
ATOM   4064  C  CG  . PRO A 1 529  ? -88.999  57.561  30.497  1.00 134.15 ? 529  PRO A CG  1 
ATOM   4065  C  CD  . PRO A 1 529  ? -88.747  59.020  30.269  1.00 133.56 ? 529  PRO A CD  1 
ATOM   4066  N  N   . VAL A 1 530  ? -84.325  57.132  30.430  1.00 127.28 ? 530  VAL A N   1 
ATOM   4067  C  CA  . VAL A 1 530  ? -83.214  56.740  29.574  1.00 124.41 ? 530  VAL A CA  1 
ATOM   4068  C  C   . VAL A 1 530  ? -83.571  55.363  29.006  1.00 123.27 ? 530  VAL A C   1 
ATOM   4069  O  O   . VAL A 1 530  ? -83.814  54.427  29.759  1.00 122.79 ? 530  VAL A O   1 
ATOM   4070  C  CB  . VAL A 1 530  ? -81.841  56.728  30.340  1.00 98.86  ? 530  VAL A CB  1 
ATOM   4071  C  CG1 . VAL A 1 530  ? -81.580  55.396  30.958  1.00 97.61  ? 530  VAL A CG1 1 
ATOM   4072  C  CG2 . VAL A 1 530  ? -80.688  57.062  29.413  1.00 97.59  ? 530  VAL A CG2 1 
ATOM   4073  N  N   . THR A 1 531  ? -83.659  55.251  27.682  1.00 123.22 ? 531  THR A N   1 
ATOM   4074  C  CA  . THR A 1 531  ? -83.988  53.966  27.058  1.00 124.86 ? 531  THR A CA  1 
ATOM   4075  C  C   . THR A 1 531  ? -82.806  53.252  26.437  1.00 123.79 ? 531  THR A C   1 
ATOM   4076  O  O   . THR A 1 531  ? -81.839  53.872  25.989  1.00 121.82 ? 531  THR A O   1 
ATOM   4077  C  CB  . THR A 1 531  ? -85.034  54.076  25.940  1.00 127.69 ? 531  THR A CB  1 
ATOM   4078  O  OG1 . THR A 1 531  ? -85.469  52.759  25.573  1.00 128.39 ? 531  THR A OG1 1 
ATOM   4079  C  CG2 . THR A 1 531  ? -84.424  54.726  24.715  1.00 127.93 ? 531  THR A CG2 1 
ATOM   4080  N  N   . GLN A 1 532  ? -82.941  51.935  26.365  1.00 126.02 ? 532  GLN A N   1 
ATOM   4081  C  CA  . GLN A 1 532  ? -81.929  51.075  25.790  1.00 127.14 ? 532  GLN A CA  1 
ATOM   4082  C  C   . GLN A 1 532  ? -81.536  51.520  24.379  1.00 128.27 ? 532  GLN A C   1 
ATOM   4083  O  O   . GLN A 1 532  ? -80.467  51.173  23.891  1.00 127.94 ? 532  GLN A O   1 
ATOM   4084  C  CB  . GLN A 1 532  ? -82.437  49.636  25.784  1.00 128.82 ? 532  GLN A CB  1 
ATOM   4085  C  CG  . GLN A 1 532  ? -81.508  48.654  25.105  1.00 128.84 ? 532  GLN A CG  1 
ATOM   4086  C  CD  . GLN A 1 532  ? -80.290  48.296  25.938  1.00 126.52 ? 532  GLN A CD  1 
ATOM   4087  O  OE1 . GLN A 1 532  ? -80.253  48.537  27.148  1.00 126.39 ? 532  GLN A OE1 1 
ATOM   4088  N  NE2 . GLN A 1 532  ? -79.285  47.705  25.287  1.00 124.01 ? 532  GLN A NE2 1 
ATOM   4089  N  N   . ASN A 1 533  ? -82.389  52.296  23.722  1.00 131.00 ? 533  ASN A N   1 
ATOM   4090  C  CA  . ASN A 1 533  ? -82.036  52.811  22.404  1.00 131.39 ? 533  ASN A CA  1 
ATOM   4091  C  C   . ASN A 1 533  ? -81.006  53.925  22.472  1.00 128.85 ? 533  ASN A C   1 
ATOM   4092  O  O   . ASN A 1 533  ? -80.392  54.262  21.457  1.00 129.27 ? 533  ASN A O   1 
ATOM   4093  C  CB  . ASN A 1 533  ? -83.269  53.306  21.659  1.00 136.10 ? 533  ASN A CB  1 
ATOM   4094  C  CG  . ASN A 1 533  ? -84.275  52.220  21.440  1.00 140.70 ? 533  ASN A CG  1 
ATOM   4095  O  OD1 . ASN A 1 533  ? -85.400  52.298  21.934  1.00 144.09 ? 533  ASN A OD1 1 
ATOM   4096  N  ND2 . ASN A 1 533  ? -83.876  51.179  20.720  1.00 140.61 ? 533  ASN A ND2 1 
ATOM   4097  N  N   . MET A 1 534  ? -80.833  54.506  23.656  1.00 124.74 ? 534  MET A N   1 
ATOM   4098  C  CA  . MET A 1 534  ? -79.904  55.610  23.840  1.00 120.11 ? 534  MET A CA  1 
ATOM   4099  C  C   . MET A 1 534  ? -78.501  55.090  24.156  1.00 116.15 ? 534  MET A C   1 
ATOM   4100  O  O   . MET A 1 534  ? -77.559  55.861  24.310  1.00 113.66 ? 534  MET A O   1 
ATOM   4101  C  CB  . MET A 1 534  ? -80.413  56.509  24.958  1.00 119.52 ? 534  MET A CB  1 
ATOM   4102  C  CG  . MET A 1 534  ? -81.910  56.684  24.931  1.00 121.21 ? 534  MET A CG  1 
ATOM   4103  S  SD  . MET A 1 534  ? -82.618  57.505  26.383  1.00 117.99 ? 534  MET A SD  1 
ATOM   4104  C  CE  . MET A 1 534  ? -82.029  59.166  26.150  1.00 93.09  ? 534  MET A CE  1 
ATOM   4105  N  N   . VAL A 1 535  ? -78.375  53.767  24.184  1.00 114.24 ? 535  VAL A N   1 
ATOM   4106  C  CA  . VAL A 1 535  ? -77.292  53.063  24.879  1.00 112.19 ? 535  VAL A CA  1 
ATOM   4107  C  C   . VAL A 1 535  ? -75.830  53.486  24.751  1.00 110.54 ? 535  VAL A C   1 
ATOM   4108  O  O   . VAL A 1 535  ? -75.087  53.376  25.713  1.00 110.90 ? 535  VAL A O   1 
ATOM   4109  C  CB  . VAL A 1 535  ? -77.338  51.563  24.598  1.00 112.71 ? 535  VAL A CB  1 
ATOM   4110  C  CG1 . VAL A 1 535  ? -78.116  50.849  25.701  1.00 113.78 ? 535  VAL A CG1 1 
ATOM   4111  C  CG2 . VAL A 1 535  ? -77.881  51.290  23.172  1.00 117.84 ? 535  VAL A CG2 1 
ATOM   4112  N  N   . PRO A 1 536  ? -75.368  53.879  23.569  1.00 109.47 ? 536  PRO A N   1 
ATOM   4113  C  CA  . PRO A 1 536  ? -73.947  54.232  23.728  1.00 105.63 ? 536  PRO A CA  1 
ATOM   4114  C  C   . PRO A 1 536  ? -73.778  55.661  24.235  1.00 101.30 ? 536  PRO A C   1 
ATOM   4115  O  O   . PRO A 1 536  ? -72.880  55.980  25.014  1.00 100.50 ? 536  PRO A O   1 
ATOM   4116  C  CB  . PRO A 1 536  ? -73.382  54.078  22.314  1.00 108.60 ? 536  PRO A CB  1 
ATOM   4117  C  CG  . PRO A 1 536  ? -74.362  53.150  21.613  1.00 112.12 ? 536  PRO A CG  1 
ATOM   4118  C  CD  . PRO A 1 536  ? -75.704  53.455  22.201  1.00 112.34 ? 536  PRO A CD  1 
ATOM   4119  N  N   . SER A 1 537  ? -74.679  56.509  23.767  1.00 98.83  ? 537  SER A N   1 
ATOM   4120  C  CA  . SER A 1 537  ? -74.765  57.910  24.138  1.00 96.30  ? 537  SER A CA  1 
ATOM   4121  C  C   . SER A 1 537  ? -75.971  58.385  23.334  1.00 99.36  ? 537  SER A C   1 
ATOM   4122  O  O   . SER A 1 537  ? -76.651  57.572  22.696  1.00 102.13 ? 537  SER A O   1 
ATOM   4123  C  CB  . SER A 1 537  ? -73.487  58.692  23.758  1.00 91.80  ? 537  SER A CB  1 
ATOM   4124  O  OG  . SER A 1 537  ? -73.502  59.154  22.397  1.00 91.30  ? 537  SER A OG  1 
ATOM   4125  N  N   . SER A 1 538  ? -76.237  59.687  23.365  1.00 96.87  ? 538  SER A N   1 
ATOM   4126  C  CA  . SER A 1 538  ? -77.350  60.285  22.642  1.00 93.33  ? 538  SER A CA  1 
ATOM   4127  C  C   . SER A 1 538  ? -77.132  61.783  22.718  1.00 93.07  ? 538  SER A C   1 
ATOM   4128  O  O   . SER A 1 538  ? -76.259  62.236  23.450  1.00 92.05  ? 538  SER A O   1 
ATOM   4129  C  CB  . SER A 1 538  ? -78.675  59.948  23.334  1.00 93.01  ? 538  SER A CB  1 
ATOM   4130  O  OG  . SER A 1 538  ? -78.934  58.553  23.358  1.00 89.78  ? 538  SER A OG  1 
ATOM   4131  N  N   . ARG A 1 539  ? -77.911  62.565  21.981  1.00 90.68  ? 539  ARG A N   1 
ATOM   4132  C  CA  . ARG A 1 539  ? -78.029  63.978  22.310  1.00 91.23  ? 539  ARG A CA  1 
ATOM   4133  C  C   . ARG A 1 539  ? -79.480  64.350  22.346  1.00 93.26  ? 539  ARG A C   1 
ATOM   4134  O  O   . ARG A 1 539  ? -80.305  63.749  21.664  1.00 94.55  ? 539  ARG A O   1 
ATOM   4135  C  CB  . ARG A 1 539  ? -77.340  64.878  21.304  1.00 91.50  ? 539  ARG A CB  1 
ATOM   4136  C  CG  . ARG A 1 539  ? -76.113  64.315  20.693  1.00 90.22  ? 539  ARG A CG  1 
ATOM   4137  C  CD  . ARG A 1 539  ? -75.580  65.356  19.777  1.00 95.97  ? 539  ARG A CD  1 
ATOM   4138  N  NE  . ARG A 1 539  ? -74.442  66.016  20.369  1.00 98.62  ? 539  ARG A NE  1 
ATOM   4139  C  CZ  . ARG A 1 539  ? -73.212  65.540  20.252  1.00 100.52 ? 539  ARG A CZ  1 
ATOM   4140  N  NH1 . ARG A 1 539  ? -73.012  64.424  19.565  1.00 101.78 ? 539  ARG A NH1 1 
ATOM   4141  N  NH2 . ARG A 1 539  ? -72.189  66.172  20.804  1.00 102.66 ? 539  ARG A NH2 1 
ATOM   4142  N  N   . LEU A 1 540  ? -79.794  65.346  23.156  1.00 94.69  ? 540  LEU A N   1 
ATOM   4143  C  CA  . LEU A 1 540  ? -81.104  65.947  23.068  1.00 98.64  ? 540  LEU A CA  1 
ATOM   4144  C  C   . LEU A 1 540  ? -81.015  67.459  22.919  1.00 99.54  ? 540  LEU A C   1 
ATOM   4145  O  O   . LEU A 1 540  ? -80.022  68.099  23.292  1.00 95.28  ? 540  LEU A O   1 
ATOM   4146  C  CB  . LEU A 1 540  ? -82.051  65.514  24.205  1.00 102.84 ? 540  LEU A CB  1 
ATOM   4147  C  CG  . LEU A 1 540  ? -81.993  65.978  25.669  1.00 106.20 ? 540  LEU A CG  1 
ATOM   4148  C  CD1 . LEU A 1 540  ? -81.667  67.456  25.811  1.00 108.41 ? 540  LEU A CD1 1 
ATOM   4149  C  CD2 . LEU A 1 540  ? -83.326  65.652  26.368  1.00 108.06 ? 540  LEU A CD2 1 
ATOM   4150  N  N   . LEU A 1 541  ? -82.071  68.002  22.332  1.00 101.74 ? 541  LEU A N   1 
ATOM   4151  C  CA  . LEU A 1 541  ? -82.159  69.404  22.021  1.00 103.31 ? 541  LEU A CA  1 
ATOM   4152  C  C   . LEU A 1 541  ? -83.616  69.763  22.282  1.00 109.81 ? 541  LEU A C   1 
ATOM   4153  O  O   . LEU A 1 541  ? -84.528  68.960  22.078  1.00 110.85 ? 541  LEU A O   1 
ATOM   4154  C  CB  . LEU A 1 541  ? -81.721  69.645  20.581  1.00 101.41 ? 541  LEU A CB  1 
ATOM   4155  C  CG  . LEU A 1 541  ? -82.243  70.800  19.752  1.00 106.35 ? 541  LEU A CG  1 
ATOM   4156  C  CD1 . LEU A 1 541  ? -81.162  71.289  18.793  1.00 102.65 ? 541  LEU A CD1 1 
ATOM   4157  C  CD2 . LEU A 1 541  ? -83.523  70.360  19.010  1.00 108.28 ? 541  LEU A CD2 1 
ATOM   4158  N  N   . VAL A 1 542  ? -83.824  70.967  22.782  1.00 114.08 ? 542  VAL A N   1 
ATOM   4159  C  CA  . VAL A 1 542  ? -85.109  71.353  23.303  1.00 119.35 ? 542  VAL A CA  1 
ATOM   4160  C  C   . VAL A 1 542  ? -85.380  72.738  22.791  1.00 126.41 ? 542  VAL A C   1 
ATOM   4161  O  O   . VAL A 1 542  ? -84.520  73.610  22.881  1.00 125.67 ? 542  VAL A O   1 
ATOM   4162  C  CB  . VAL A 1 542  ? -85.061  71.371  24.837  1.00 116.89 ? 542  VAL A CB  1 
ATOM   4163  C  CG1 . VAL A 1 542  ? -86.043  72.374  25.406  1.00 118.12 ? 542  VAL A CG1 1 
ATOM   4164  C  CG2 . VAL A 1 542  ? -85.313  69.987  25.380  1.00 115.86 ? 542  VAL A CG2 1 
ATOM   4165  N  N   . TYR A 1 543  ? -86.578  72.931  22.249  1.00 133.50 ? 543  TYR A N   1 
ATOM   4166  C  CA  . TYR A 1 543  ? -86.967  74.226  21.720  1.00 139.10 ? 543  TYR A CA  1 
ATOM   4167  C  C   . TYR A 1 543  ? -88.395  74.643  22.045  1.00 143.05 ? 543  TYR A C   1 
ATOM   4168  O  O   . TYR A 1 543  ? -89.317  73.829  22.004  1.00 144.28 ? 543  TYR A O   1 
ATOM   4169  C  CB  . TYR A 1 543  ? -86.781  74.258  20.213  1.00 141.80 ? 543  TYR A CB  1 
ATOM   4170  C  CG  . TYR A 1 543  ? -87.630  73.280  19.431  1.00 145.18 ? 543  TYR A CG  1 
ATOM   4171  C  CD1 . TYR A 1 543  ? -87.192  71.984  19.215  1.00 145.38 ? 543  TYR A CD1 1 
ATOM   4172  C  CD2 . TYR A 1 543  ? -88.845  73.662  18.860  1.00 148.25 ? 543  TYR A CD2 1 
ATOM   4173  C  CE1 . TYR A 1 543  ? -87.944  71.082  18.465  1.00 147.03 ? 543  TYR A CE1 1 
ATOM   4174  C  CE2 . TYR A 1 543  ? -89.608  72.761  18.108  1.00 149.72 ? 543  TYR A CE2 1 
ATOM   4175  C  CZ  . TYR A 1 543  ? -89.147  71.469  17.912  1.00 148.09 ? 543  TYR A CZ  1 
ATOM   4176  O  OH  . TYR A 1 543  ? -89.862  70.546  17.170  1.00 147.44 ? 543  TYR A OH  1 
ATOM   4177  N  N   . TYR A 1 544  ? -88.557  75.921  22.381  1.00 144.92 ? 544  TYR A N   1 
ATOM   4178  C  CA  . TYR A 1 544  ? -89.867  76.563  22.386  1.00 148.71 ? 544  TYR A CA  1 
ATOM   4179  C  C   . TYR A 1 544  ? -89.952  77.473  21.163  1.00 150.52 ? 544  TYR A C   1 
ATOM   4180  O  O   . TYR A 1 544  ? -88.926  77.996  20.698  1.00 149.87 ? 544  TYR A O   1 
ATOM   4181  C  CB  . TYR A 1 544  ? -90.097  77.363  23.675  1.00 149.27 ? 544  TYR A CB  1 
ATOM   4182  C  CG  . TYR A 1 544  ? -89.120  78.497  23.881  1.00 148.44 ? 544  TYR A CG  1 
ATOM   4183  C  CD1 . TYR A 1 544  ? -87.761  78.273  23.783  1.00 145.58 ? 544  TYR A CD1 1 
ATOM   4184  C  CD2 . TYR A 1 544  ? -89.556  79.785  24.188  1.00 149.09 ? 544  TYR A CD2 1 
ATOM   4185  C  CE1 . TYR A 1 544  ? -86.866  79.283  23.970  1.00 144.83 ? 544  TYR A CE1 1 
ATOM   4186  C  CE2 . TYR A 1 544  ? -88.658  80.809  24.379  1.00 147.87 ? 544  TYR A CE2 1 
ATOM   4187  C  CZ  . TYR A 1 544  ? -87.314  80.546  24.263  1.00 146.13 ? 544  TYR A CZ  1 
ATOM   4188  O  OH  . TYR A 1 544  ? -86.381  81.525  24.442  1.00 145.65 ? 544  TYR A OH  1 
ATOM   4189  N  N   . ILE A 1 545  ? -91.165  77.640  20.635  1.00 150.68 ? 545  ILE A N   1 
ATOM   4190  C  CA  . ILE A 1 545  ? -91.379  78.516  19.491  1.00 151.40 ? 545  ILE A CA  1 
ATOM   4191  C  C   . ILE A 1 545  ? -91.925  79.859  19.977  1.00 153.86 ? 545  ILE A C   1 
ATOM   4192  O  O   . ILE A 1 545  ? -93.035  79.922  20.494  1.00 153.72 ? 545  ILE A O   1 
ATOM   4193  C  CB  . ILE A 1 545  ? -92.332  77.884  18.446  1.00 149.14 ? 545  ILE A CB  1 
ATOM   4194  C  CG1 . ILE A 1 545  ? -92.149  76.364  18.355  1.00 145.30 ? 545  ILE A CG1 1 
ATOM   4195  C  CG2 . ILE A 1 545  ? -92.095  78.496  17.077  1.00 152.73 ? 545  ILE A CG2 1 
ATOM   4196  C  CD1 . ILE A 1 545  ? -93.090  75.669  17.327  1.00 136.75 ? 545  ILE A CD1 1 
ATOM   4197  N  N   . VAL A 1 546  ? -91.131  80.919  19.809  1.00 158.78 ? 546  VAL A N   1 
ATOM   4198  C  CA  . VAL A 1 546  ? -91.412  82.256  20.365  1.00 165.50 ? 546  VAL A CA  1 
ATOM   4199  C  C   . VAL A 1 546  ? -91.957  83.277  19.369  1.00 179.18 ? 546  VAL A C   1 
ATOM   4200  O  O   . VAL A 1 546  ? -91.277  83.649  18.418  1.00 180.21 ? 546  VAL A O   1 
ATOM   4201  C  CB  . VAL A 1 546  ? -90.141  82.869  20.975  1.00 157.48 ? 546  VAL A CB  1 
ATOM   4202  C  CG1 . VAL A 1 546  ? -90.039  84.357  20.658  1.00 157.54 ? 546  VAL A CG1 1 
ATOM   4203  C  CG2 . VAL A 1 546  ? -90.107  82.635  22.459  1.00 154.42 ? 546  VAL A CG2 1 
ATOM   4204  N  N   . THR A 1 547  ? -93.166  83.765  19.606  1.00 193.21 ? 547  THR A N   1 
ATOM   4205  C  CA  . THR A 1 547  ? -93.772  84.718  18.686  1.00 209.18 ? 547  THR A CA  1 
ATOM   4206  C  C   . THR A 1 547  ? -93.353  86.168  18.941  1.00 224.22 ? 547  THR A C   1 
ATOM   4207  O  O   . THR A 1 547  ? -94.135  86.967  19.460  1.00 227.33 ? 547  THR A O   1 
ATOM   4208  C  CB  . THR A 1 547  ? -95.308  84.614  18.708  1.00 211.51 ? 547  THR A CB  1 
ATOM   4209  O  OG1 . THR A 1 547  ? -95.689  83.243  18.538  1.00 209.92 ? 547  THR A OG1 1 
ATOM   4210  C  CG2 . THR A 1 547  ? -95.936  85.459  17.598  1.00 215.24 ? 547  THR A CG2 1 
ATOM   4211  N  N   . GLY A 1 548  ? -92.124  86.510  18.566  1.00 236.18 ? 548  GLY A N   1 
ATOM   4212  C  CA  . GLY A 1 548  ? -91.741  87.908  18.508  1.00 251.08 ? 548  GLY A CA  1 
ATOM   4213  C  C   . GLY A 1 548  ? -92.708  88.586  17.555  1.00 270.02 ? 548  GLY A C   1 
ATOM   4214  O  O   . GLY A 1 548  ? -93.136  87.974  16.576  1.00 273.66 ? 548  GLY A O   1 
ATOM   4215  N  N   . GLU A 1 549  ? -93.070  89.837  17.829  1.00 283.10 ? 549  GLU A N   1 
ATOM   4216  C  CA  . GLU A 1 549  ? -94.044  90.541  16.990  1.00 297.09 ? 549  GLU A CA  1 
ATOM   4217  C  C   . GLU A 1 549  ? -93.610  90.637  15.522  1.00 299.07 ? 549  GLU A C   1 
ATOM   4218  O  O   . GLU A 1 549  ? -94.436  90.549  14.613  1.00 302.24 ? 549  GLU A O   1 
ATOM   4219  C  CB  . GLU A 1 549  ? -94.358  91.936  17.552  1.00 307.51 ? 549  GLU A CB  1 
ATOM   4220  C  CG  . GLU A 1 549  ? -93.185  92.904  17.558  1.00 313.74 ? 549  GLU A CG  1 
ATOM   4221  C  CD  . GLU A 1 549  ? -92.181  92.602  18.655  1.00 315.68 ? 549  GLU A CD  1 
ATOM   4222  O  OE1 . GLU A 1 549  ? -92.480  91.758  19.526  1.00 316.12 ? 549  GLU A OE1 1 
ATOM   4223  O  OE2 . GLU A 1 549  ? -91.092  93.211  18.648  1.00 316.47 ? 549  GLU A OE2 1 
ATOM   4224  N  N   . GLN A 1 550  ? -92.310  90.804  15.302  1.00 295.41 ? 550  GLN A N   1 
ATOM   4225  C  CA  . GLN A 1 550  ? -91.756  90.963  13.960  1.00 293.51 ? 550  GLN A CA  1 
ATOM   4226  C  C   . GLN A 1 550  ? -91.712  89.665  13.148  1.00 284.62 ? 550  GLN A C   1 
ATOM   4227  O  O   . GLN A 1 550  ? -92.081  89.651  11.975  1.00 288.31 ? 550  GLN A O   1 
ATOM   4228  C  CB  . GLN A 1 550  ? -90.359  91.598  14.030  1.00 295.36 ? 550  GLN A CB  1 
ATOM   4229  C  CG  . GLN A 1 550  ? -89.268  90.717  14.650  1.00 293.49 ? 550  GLN A CG  1 
ATOM   4230  C  CD  . GLN A 1 550  ? -89.279  90.706  16.178  1.00 292.57 ? 550  GLN A CD  1 
ATOM   4231  O  OE1 . GLN A 1 550  ? -90.049  91.424  16.814  1.00 294.84 ? 550  GLN A OE1 1 
ATOM   4232  N  NE2 . GLN A 1 550  ? -88.413  89.887  16.768  1.00 288.72 ? 550  GLN A NE2 1 
ATOM   4233  N  N   . THR A 1 551  ? -91.270  88.579  13.777  1.00 271.47 ? 551  THR A N   1 
ATOM   4234  C  CA  . THR A 1 551  ? -91.028  87.313  13.081  1.00 261.24 ? 551  THR A CA  1 
ATOM   4235  C  C   . THR A 1 551  ? -90.937  86.126  14.043  1.00 246.36 ? 551  THR A C   1 
ATOM   4236  O  O   . THR A 1 551  ? -90.378  86.243  15.136  1.00 243.41 ? 551  THR A O   1 
ATOM   4237  C  CB  . THR A 1 551  ? -89.712  87.366  12.283  1.00 261.81 ? 551  THR A CB  1 
ATOM   4238  O  OG1 . THR A 1 551  ? -89.795  88.389  11.285  1.00 266.61 ? 551  THR A OG1 1 
ATOM   4239  C  CG2 . THR A 1 551  ? -89.431  86.029  11.619  1.00 260.93 ? 551  THR A CG2 1 
ATOM   4240  N  N   . ALA A 1 552  ? -91.471  84.981  13.629  1.00 234.83 ? 552  ALA A N   1 
ATOM   4241  C  CA  . ALA A 1 552  ? -91.469  83.792  14.478  1.00 220.50 ? 552  ALA A CA  1 
ATOM   4242  C  C   . ALA A 1 552  ? -90.053  83.288  14.770  1.00 204.65 ? 552  ALA A C   1 
ATOM   4243  O  O   . ALA A 1 552  ? -89.297  83.008  13.837  1.00 203.12 ? 552  ALA A O   1 
ATOM   4244  C  CB  . ALA A 1 552  ? -92.296  82.691  13.835  1.00 221.66 ? 552  ALA A CB  1 
ATOM   4245  N  N   . GLU A 1 553  ? -89.708  83.176  16.063  1.00 192.77 ? 553  GLU A N   1 
ATOM   4246  C  CA  . GLU A 1 553  ? -88.411  82.622  16.526  1.00 177.79 ? 553  GLU A CA  1 
ATOM   4247  C  C   . GLU A 1 553  ? -88.430  81.206  17.097  1.00 167.84 ? 553  GLU A C   1 
ATOM   4248  O  O   . GLU A 1 553  ? -89.064  80.939  18.113  1.00 165.50 ? 553  GLU A O   1 
ATOM   4249  C  CB  . GLU A 1 553  ? -87.723  83.531  17.556  1.00 171.45 ? 553  GLU A CB  1 
ATOM   4250  C  CG  . GLU A 1 553  ? -86.405  84.115  17.072  1.00 167.30 ? 553  GLU A CG  1 
ATOM   4251  C  CD  . GLU A 1 553  ? -85.503  84.536  18.207  1.00 162.50 ? 553  GLU A CD  1 
ATOM   4252  O  OE1 . GLU A 1 553  ? -85.584  83.916  19.279  1.00 160.71 ? 553  GLU A OE1 1 
ATOM   4253  O  OE2 . GLU A 1 553  ? -84.714  85.487  18.031  1.00 161.05 ? 553  GLU A OE2 1 
ATOM   4254  N  N   . LEU A 1 554  ? -87.713  80.308  16.433  1.00 163.49 ? 554  LEU A N   1 
ATOM   4255  C  CA  . LEU A 1 554  ? -87.371  79.034  17.027  1.00 157.88 ? 554  LEU A CA  1 
ATOM   4256  C  C   . LEU A 1 554  ? -86.174  79.315  17.884  1.00 153.20 ? 554  LEU A C   1 
ATOM   4257  O  O   . LEU A 1 554  ? -85.297  80.101  17.516  1.00 153.15 ? 554  LEU A O   1 
ATOM   4258  C  CB  . LEU A 1 554  ? -86.986  78.001  15.975  1.00 157.78 ? 554  LEU A CB  1 
ATOM   4259  C  CG  . LEU A 1 554  ? -88.085  77.249  15.227  1.00 161.14 ? 554  LEU A CG  1 
ATOM   4260  C  CD1 . LEU A 1 554  ? -87.600  75.855  14.804  1.00 159.49 ? 554  LEU A CD1 1 
ATOM   4261  C  CD2 . LEU A 1 554  ? -89.308  77.141  16.103  1.00 162.55 ? 554  LEU A CD2 1 
ATOM   4262  N  N   . VAL A 1 555  ? -86.135  78.673  19.034  1.00 150.16 ? 555  VAL A N   1 
ATOM   4263  C  CA  . VAL A 1 555  ? -85.021  78.864  19.932  1.00 145.73 ? 555  VAL A CA  1 
ATOM   4264  C  C   . VAL A 1 555  ? -84.811  77.567  20.691  1.00 138.97 ? 555  VAL A C   1 
ATOM   4265  O  O   . VAL A 1 555  ? -85.771  76.898  21.066  1.00 138.19 ? 555  VAL A O   1 
ATOM   4266  C  CB  . VAL A 1 555  ? -85.278  80.056  20.873  1.00 148.06 ? 555  VAL A CB  1 
ATOM   4267  C  CG1 . VAL A 1 555  ? -84.331  80.023  22.038  1.00 146.76 ? 555  VAL A CG1 1 
ATOM   4268  C  CG2 . VAL A 1 555  ? -85.103  81.348  20.113  1.00 149.68 ? 555  VAL A CG2 1 
ATOM   4269  N  N   . SER A 1 556  ? -83.558  77.184  20.877  1.00 132.48 ? 556  SER A N   1 
ATOM   4270  C  CA  . SER A 1 556  ? -83.296  75.944  21.566  1.00 129.66 ? 556  SER A CA  1 
ATOM   4271  C  C   . SER A 1 556  ? -81.833  75.840  21.967  1.00 128.81 ? 556  SER A C   1 
ATOM   4272  O  O   . SER A 1 556  ? -80.972  76.511  21.385  1.00 131.45 ? 556  SER A O   1 
ATOM   4273  C  CB  . SER A 1 556  ? -83.678  74.765  20.677  1.00 128.44 ? 556  SER A CB  1 
ATOM   4274  O  OG  . SER A 1 556  ? -82.632  74.481  19.775  1.00 127.76 ? 556  SER A OG  1 
ATOM   4275  N  N   . ASP A 1 557  ? -81.580  75.002  22.974  1.00 122.20 ? 557  ASP A N   1 
ATOM   4276  C  CA  . ASP A 1 557  ? -80.241  74.617  23.394  1.00 114.07 ? 557  ASP A CA  1 
ATOM   4277  C  C   . ASP A 1 557  ? -80.242  73.091  23.370  1.00 108.61 ? 557  ASP A C   1 
ATOM   4278  O  O   . ASP A 1 557  ? -81.258  72.483  23.059  1.00 106.89 ? 557  ASP A O   1 
ATOM   4279  C  CB  . ASP A 1 557  ? -79.943  75.184  24.787  1.00 114.46 ? 557  ASP A CB  1 
ATOM   4280  C  CG  . ASP A 1 557  ? -78.737  74.522  25.472  1.00 113.91 ? 557  ASP A CG  1 
ATOM   4281  O  OD1 . ASP A 1 557  ? -77.598  74.650  24.975  1.00 114.97 ? 557  ASP A OD1 1 
ATOM   4282  O  OD2 . ASP A 1 557  ? -78.925  73.899  26.538  1.00 111.84 ? 557  ASP A OD2 1 
ATOM   4283  N  N   . SER A 1 558  ? -79.106  72.476  23.673  1.00 107.34 ? 558  SER A N   1 
ATOM   4284  C  CA  . SER A 1 558  ? -78.943  71.027  23.545  1.00 107.09 ? 558  SER A CA  1 
ATOM   4285  C  C   . SER A 1 558  ? -77.735  70.524  24.358  1.00 104.54 ? 558  SER A C   1 
ATOM   4286  O  O   . SER A 1 558  ? -76.831  71.303  24.671  1.00 102.50 ? 558  SER A O   1 
ATOM   4287  C  CB  . SER A 1 558  ? -78.788  70.655  22.067  1.00 108.43 ? 558  SER A CB  1 
ATOM   4288  O  OG  . SER A 1 558  ? -77.631  71.270  21.497  1.00 108.38 ? 558  SER A OG  1 
ATOM   4289  N  N   . VAL A 1 559  ? -77.721  69.229  24.692  1.00 104.42 ? 559  VAL A N   1 
ATOM   4290  C  CA  . VAL A 1 559  ? -76.698  68.653  25.584  1.00 100.90 ? 559  VAL A CA  1 
ATOM   4291  C  C   . VAL A 1 559  ? -76.328  67.211  25.208  1.00 102.60 ? 559  VAL A C   1 
ATOM   4292  O  O   . VAL A 1 559  ? -77.193  66.411  24.853  1.00 106.98 ? 559  VAL A O   1 
ATOM   4293  C  CB  . VAL A 1 559  ? -77.167  68.640  27.059  1.00 94.68  ? 559  VAL A CB  1 
ATOM   4294  C  CG1 . VAL A 1 559  ? -77.587  70.025  27.494  1.00 90.82  ? 559  VAL A CG1 1 
ATOM   4295  C  CG2 . VAL A 1 559  ? -78.299  67.656  27.249  1.00 90.65  ? 559  VAL A CG2 1 
ATOM   4296  N  N   . TRP A 1 560  ? -75.047  66.870  25.287  1.00 98.40  ? 560  TRP A N   1 
ATOM   4297  C  CA  . TRP A 1 560  ? -74.620  65.536  24.906  1.00 97.35  ? 560  TRP A CA  1 
ATOM   4298  C  C   . TRP A 1 560  ? -74.778  64.629  26.090  1.00 92.93  ? 560  TRP A C   1 
ATOM   4299  O  O   . TRP A 1 560  ? -74.280  64.944  27.157  1.00 92.85  ? 560  TRP A O   1 
ATOM   4300  C  CB  . TRP A 1 560  ? -73.162  65.552  24.442  1.00 102.66 ? 560  TRP A CB  1 
ATOM   4301  C  CG  . TRP A 1 560  ? -72.645  64.194  24.133  1.00 108.11 ? 560  TRP A CG  1 
ATOM   4302  C  CD1 . TRP A 1 560  ? -72.945  63.433  23.050  1.00 112.44 ? 560  TRP A CD1 1 
ATOM   4303  C  CD2 . TRP A 1 560  ? -71.751  63.423  24.931  1.00 109.41 ? 560  TRP A CD2 1 
ATOM   4304  N  NE1 . TRP A 1 560  ? -72.290  62.224  23.120  1.00 112.66 ? 560  TRP A NE1 1 
ATOM   4305  C  CE2 . TRP A 1 560  ? -71.552  62.196  24.273  1.00 110.28 ? 560  TRP A CE2 1 
ATOM   4306  C  CE3 . TRP A 1 560  ? -71.108  63.647  26.148  1.00 110.50 ? 560  TRP A CE3 1 
ATOM   4307  C  CZ2 . TRP A 1 560  ? -70.738  61.201  24.785  1.00 109.64 ? 560  TRP A CZ2 1 
ATOM   4308  C  CZ3 . TRP A 1 560  ? -70.297  62.656  26.656  1.00 110.49 ? 560  TRP A CZ3 1 
ATOM   4309  C  CH2 . TRP A 1 560  ? -70.114  61.449  25.973  1.00 109.25 ? 560  TRP A CH2 1 
ATOM   4310  N  N   . LEU A 1 561  ? -75.454  63.500  25.924  1.00 93.51  ? 561  LEU A N   1 
ATOM   4311  C  CA  . LEU A 1 561  ? -75.716  62.613  27.065  1.00 95.54  ? 561  LEU A CA  1 
ATOM   4312  C  C   . LEU A 1 561  ? -74.943  61.306  27.090  1.00 99.04  ? 561  LEU A C   1 
ATOM   4313  O  O   . LEU A 1 561  ? -75.405  60.325  26.513  1.00 103.20 ? 561  LEU A O   1 
ATOM   4314  C  CB  . LEU A 1 561  ? -77.190  62.238  27.078  1.00 95.37  ? 561  LEU A CB  1 
ATOM   4315  C  CG  . LEU A 1 561  ? -78.156  63.411  27.205  1.00 95.81  ? 561  LEU A CG  1 
ATOM   4316  C  CD1 . LEU A 1 561  ? -79.550  62.878  27.318  1.00 95.11  ? 561  LEU A CD1 1 
ATOM   4317  C  CD2 . LEU A 1 561  ? -77.802  64.212  28.435  1.00 95.22  ? 561  LEU A CD2 1 
ATOM   4318  N  N   . ASN A 1 562  ? -73.804  61.248  27.777  1.00 96.52  ? 562  ASN A N   1 
ATOM   4319  C  CA  . ASN A 1 562  ? -73.054  59.981  27.820  1.00 96.13  ? 562  ASN A CA  1 
ATOM   4320  C  C   . ASN A 1 562  ? -73.735  58.972  28.713  1.00 98.93  ? 562  ASN A C   1 
ATOM   4321  O  O   . ASN A 1 562  ? -73.998  59.251  29.882  1.00 99.60  ? 562  ASN A O   1 
ATOM   4322  C  CB  . ASN A 1 562  ? -71.595  60.161  28.274  1.00 91.26  ? 562  ASN A CB  1 
ATOM   4323  C  CG  . ASN A 1 562  ? -70.818  58.816  28.383  1.00 118.52 ? 562  ASN A CG  1 
ATOM   4324  O  OD1 . ASN A 1 562  ? -71.239  57.757  27.872  1.00 117.71 ? 562  ASN A OD1 1 
ATOM   4325  N  ND2 . ASN A 1 562  ? -69.667  58.875  29.050  1.00 117.52 ? 562  ASN A ND2 1 
ATOM   4326  N  N   . ILE A 1 563  ? -74.009  57.791  28.185  1.00 98.56  ? 563  ILE A N   1 
ATOM   4327  C  CA  . ILE A 1 563  ? -74.699  56.855  29.015  1.00 98.83  ? 563  ILE A CA  1 
ATOM   4328  C  C   . ILE A 1 563  ? -73.987  55.520  29.027  1.00 101.62 ? 563  ILE A C   1 
ATOM   4329  O  O   . ILE A 1 563  ? -73.016  55.312  28.290  1.00 101.90 ? 563  ILE A O   1 
ATOM   4330  C  CB  . ILE A 1 563  ? -76.179  56.771  28.630  1.00 98.42  ? 563  ILE A CB  1 
ATOM   4331  C  CG1 . ILE A 1 563  ? -76.501  55.472  27.920  1.00 99.24  ? 563  ILE A CG1 1 
ATOM   4332  C  CG2 . ILE A 1 563  ? -76.567  57.949  27.777  1.00 96.99  ? 563  ILE A CG2 1 
ATOM   4333  C  CD1 . ILE A 1 563  ? -77.957  55.106  28.037  1.00 101.66 ? 563  ILE A CD1 1 
ATOM   4334  N  N   . GLU A 1 564  ? -74.457  54.647  29.914  1.00 104.80 ? 564  GLU A N   1 
ATOM   4335  C  CA  . GLU A 1 564  ? -73.792  53.396  30.247  1.00 106.28 ? 564  GLU A CA  1 
ATOM   4336  C  C   . GLU A 1 564  ? -73.657  52.457  29.070  1.00 110.24 ? 564  GLU A C   1 
ATOM   4337  O  O   . GLU A 1 564  ? -74.599  52.263  28.318  1.00 112.85 ? 564  GLU A O   1 
ATOM   4338  C  CB  . GLU A 1 564  ? -74.554  52.685  31.366  1.00 107.90 ? 564  GLU A CB  1 
ATOM   4339  C  CG  . GLU A 1 564  ? -75.989  52.253  31.024  1.00 111.50 ? 564  GLU A CG  1 
ATOM   4340  C  CD  . GLU A 1 564  ? -76.454  51.081  31.895  1.00 115.11 ? 564  GLU A CD  1 
ATOM   4341  O  OE1 . GLU A 1 564  ? -77.677  50.949  32.183  1.00 117.50 ? 564  GLU A OE1 1 
ATOM   4342  O  OE2 . GLU A 1 564  ? -75.572  50.284  32.297  1.00 114.99 ? 564  GLU A OE2 1 
ATOM   4343  N  N   . GLU A 1 565  ? -72.492  51.850  28.920  1.00 111.76 ? 565  GLU A N   1 
ATOM   4344  C  CA  . GLU A 1 565  ? -72.322  50.833  27.891  1.00 117.34 ? 565  GLU A CA  1 
ATOM   4345  C  C   . GLU A 1 565  ? -73.048  49.525  28.210  1.00 116.87 ? 565  GLU A C   1 
ATOM   4346  O  O   . GLU A 1 565  ? -72.464  48.451  28.144  1.00 114.42 ? 565  GLU A O   1 
ATOM   4347  C  CB  . GLU A 1 565  ? -70.847  50.555  27.650  1.00 122.51 ? 565  GLU A CB  1 
ATOM   4348  C  CG  . GLU A 1 565  ? -70.149  51.654  26.894  1.00 127.81 ? 565  GLU A CG  1 
ATOM   4349  C  CD  . GLU A 1 565  ? -68.655  51.457  26.873  1.00 130.86 ? 565  GLU A CD  1 
ATOM   4350  O  OE1 . GLU A 1 565  ? -68.163  50.526  27.572  1.00 130.94 ? 565  GLU A OE1 1 
ATOM   4351  O  OE2 . GLU A 1 565  ? -67.982  52.240  26.158  1.00 131.94 ? 565  GLU A OE2 1 
ATOM   4352  N  N   . LYS A 1 566  ? -74.318  49.618  28.567  1.00 119.51 ? 566  LYS A N   1 
ATOM   4353  C  CA  . LYS A 1 566  ? -75.149  48.434  28.640  1.00 122.15 ? 566  LYS A CA  1 
ATOM   4354  C  C   . LYS A 1 566  ? -75.275  47.858  27.246  1.00 124.52 ? 566  LYS A C   1 
ATOM   4355  O  O   . LYS A 1 566  ? -75.544  48.588  26.297  1.00 124.27 ? 566  LYS A O   1 
ATOM   4356  C  CB  . LYS A 1 566  ? -76.539  48.780  29.157  1.00 123.15 ? 566  LYS A CB  1 
ATOM   4357  C  CG  . LYS A 1 566  ? -77.480  47.598  29.193  1.00 124.12 ? 566  LYS A CG  1 
ATOM   4358  C  CD  . LYS A 1 566  ? -78.438  47.711  30.362  1.00 126.34 ? 566  LYS A CD  1 
ATOM   4359  C  CE  . LYS A 1 566  ? -79.428  46.565  30.358  1.00 129.14 ? 566  LYS A CE  1 
ATOM   4360  N  NZ  . LYS A 1 566  ? -80.264  46.541  29.112  1.00 130.90 ? 566  LYS A NZ  1 
ATOM   4361  N  N   . CYS A 1 567  ? -75.077  46.548  27.131  1.00 146.80 ? 567  CYS A N   1 
ATOM   4362  C  CA  . CYS A 1 567  ? -75.246  45.822  25.869  1.00 147.62 ? 567  CYS A CA  1 
ATOM   4363  C  C   . CYS A 1 567  ? -76.735  45.692  25.497  1.00 148.83 ? 567  CYS A C   1 
ATOM   4364  O  O   . CYS A 1 567  ? -77.600  46.109  26.254  1.00 149.39 ? 567  CYS A O   1 
ATOM   4365  C  CB  . CYS A 1 567  ? -74.607  44.421  25.973  1.00 148.01 ? 567  CYS A CB  1 
ATOM   4366  S  SG  . CYS A 1 567  ? -72.778  44.318  25.933  1.00 211.80 ? 567  CYS A SG  1 
ATOM   4367  N  N   . GLY A 1 568  ? -77.027  45.132  24.327  1.00 147.41 ? 568  GLY A N   1 
ATOM   4368  C  CA  . GLY A 1 568  ? -78.385  44.738  23.991  1.00 148.60 ? 568  GLY A CA  1 
ATOM   4369  C  C   . GLY A 1 568  ? -78.619  43.270  24.330  1.00 148.53 ? 568  GLY A C   1 
ATOM   4370  O  O   . GLY A 1 568  ? -79.655  42.903  24.886  1.00 149.30 ? 568  GLY A O   1 
ATOM   4371  N  N   . ASN A 1 569  ? -77.651  42.427  23.975  1.00 149.95 ? 569  ASN A N   1 
ATOM   4372  C  CA  . ASN A 1 569  ? -77.664  41.013  24.341  1.00 149.55 ? 569  ASN A CA  1 
ATOM   4373  C  C   . ASN A 1 569  ? -76.529  40.662  25.292  1.00 147.31 ? 569  ASN A C   1 
ATOM   4374  O  O   . ASN A 1 569  ? -75.393  40.479  24.872  1.00 148.34 ? 569  ASN A O   1 
ATOM   4375  C  CB  . ASN A 1 569  ? -77.561  40.149  23.091  1.00 150.32 ? 569  ASN A CB  1 
ATOM   4376  C  CG  . ASN A 1 569  ? -78.866  39.493  22.738  1.00 151.88 ? 569  ASN A CG  1 
ATOM   4377  O  OD1 . ASN A 1 569  ? -79.842  39.578  23.489  1.00 152.76 ? 569  ASN A OD1 1 
ATOM   4378  N  ND2 . ASN A 1 569  ? -78.894  38.819  21.596  1.00 151.65 ? 569  ASN A ND2 1 
ATOM   4379  N  N   . GLN A 1 570  ? -76.821  40.584  26.580  1.00 145.30 ? 570  GLN A N   1 
ATOM   4380  C  CA  . GLN A 1 570  ? -75.759  40.273  27.521  1.00 143.88 ? 570  GLN A CA  1 
ATOM   4381  C  C   . GLN A 1 570  ? -75.291  38.870  27.192  1.00 147.13 ? 570  GLN A C   1 
ATOM   4382  O  O   . GLN A 1 570  ? -75.955  37.888  27.511  1.00 147.05 ? 570  GLN A O   1 
ATOM   4383  C  CB  . GLN A 1 570  ? -76.214  40.383  28.991  1.00 140.37 ? 570  GLN A CB  1 
ATOM   4384  C  CG  . GLN A 1 570  ? -76.042  41.778  29.652  1.00 176.02 ? 570  GLN A CG  1 
ATOM   4385  C  CD  . GLN A 1 570  ? -77.318  42.645  29.637  1.00 174.98 ? 570  GLN A CD  1 
ATOM   4386  O  OE1 . GLN A 1 570  ? -78.027  42.712  28.633  1.00 173.82 ? 570  GLN A OE1 1 
ATOM   4387  N  NE2 . GLN A 1 570  ? -77.603  43.314  30.758  1.00 174.85 ? 570  GLN A NE2 1 
ATOM   4388  N  N   . LEU A 1 571  ? -74.166  38.780  26.503  1.00 151.87 ? 571  LEU A N   1 
ATOM   4389  C  CA  . LEU A 1 571  ? -73.511  37.502  26.323  1.00 152.26 ? 571  LEU A CA  1 
ATOM   4390  C  C   . LEU A 1 571  ? -72.461  37.335  27.403  1.00 155.81 ? 571  LEU A C   1 
ATOM   4391  O  O   . LEU A 1 571  ? -71.621  38.208  27.601  1.00 157.52 ? 571  LEU A O   1 
ATOM   4392  C  CB  . LEU A 1 571  ? -72.851  37.441  24.963  1.00 144.56 ? 571  LEU A CB  1 
ATOM   4393  C  CG  . LEU A 1 571  ? -71.538  36.673  24.956  1.00 137.17 ? 571  LEU A CG  1 
ATOM   4394  C  CD1 . LEU A 1 571  ? -71.676  35.290  25.582  1.00 130.39 ? 571  LEU A CD1 1 
ATOM   4395  C  CD2 . LEU A 1 571  ? -71.038  36.587  23.528  1.00 131.51 ? 571  LEU A CD2 1 
ATOM   4396  N  N   . GLN A 1 572  ? -72.494  36.209  28.098  1.00 154.46 ? 572  GLN A N   1 
ATOM   4397  C  CA  . GLN A 1 572  ? -71.499  35.967  29.126  1.00 156.69 ? 572  GLN A CA  1 
ATOM   4398  C  C   . GLN A 1 572  ? -71.017  34.537  29.072  1.00 152.24 ? 572  GLN A C   1 
ATOM   4399  O  O   . GLN A 1 572  ? -71.797  33.596  29.199  1.00 149.90 ? 572  GLN A O   1 
ATOM   4400  C  CB  . GLN A 1 572  ? -72.044  36.300  30.521  1.00 167.74 ? 572  GLN A CB  1 
ATOM   4401  C  CG  . GLN A 1 572  ? -70.991  36.287  31.642  1.00 178.40 ? 572  GLN A CG  1 
ATOM   4402  C  CD  . GLN A 1 572  ? -69.710  37.054  31.301  1.00 187.07 ? 572  GLN A CD  1 
ATOM   4403  O  OE1 . GLN A 1 572  ? -69.729  38.062  30.584  1.00 189.62 ? 572  GLN A OE1 1 
ATOM   4404  N  NE2 . GLN A 1 572  ? -68.587  36.572  31.825  1.00 190.79 ? 572  GLN A NE2 1 
ATOM   4405  N  N   . VAL A 1 573  ? -69.712  34.390  28.894  1.00 148.49 ? 573  VAL A N   1 
ATOM   4406  C  CA  . VAL A 1 573  ? -69.075  33.089  28.808  1.00 144.63 ? 573  VAL A CA  1 
ATOM   4407  C  C   . VAL A 1 573  ? -68.421  32.645  30.146  1.00 146.85 ? 573  VAL A C   1 
ATOM   4408  O  O   . VAL A 1 573  ? -67.845  33.466  30.864  1.00 148.39 ? 573  VAL A O   1 
ATOM   4409  C  CB  . VAL A 1 573  ? -68.088  33.125  27.646  1.00 134.92 ? 573  VAL A CB  1 
ATOM   4410  C  CG1 . VAL A 1 573  ? -68.817  32.840  26.379  1.00 131.89 ? 573  VAL A CG1 1 
ATOM   4411  C  CG2 . VAL A 1 573  ? -67.476  34.511  27.544  1.00 131.25 ? 573  VAL A CG2 1 
ATOM   4412  N  N   . HIS A 1 574  ? -68.526  31.357  30.483  1.00 146.52 ? 574  HIS A N   1 
ATOM   4413  C  CA  . HIS A 1 574  ? -67.936  30.830  31.717  1.00 147.88 ? 574  HIS A CA  1 
ATOM   4414  C  C   . HIS A 1 574  ? -67.336  29.438  31.570  1.00 151.53 ? 574  HIS A C   1 
ATOM   4415  O  O   . HIS A 1 574  ? -67.860  28.608  30.839  1.00 149.91 ? 574  HIS A O   1 
ATOM   4416  C  CB  . HIS A 1 574  ? -68.980  30.810  32.827  1.00 150.85 ? 574  HIS A CB  1 
ATOM   4417  C  CG  . HIS A 1 574  ? -69.447  32.171  33.220  1.00 154.64 ? 574  HIS A CG  1 
ATOM   4418  N  ND1 . HIS A 1 574  ? -68.575  33.177  33.581  1.00 155.76 ? 574  HIS A ND1 1 
ATOM   4419  C  CD2 . HIS A 1 574  ? -70.690  32.704  33.296  1.00 156.24 ? 574  HIS A CD2 1 
ATOM   4420  C  CE1 . HIS A 1 574  ? -69.259  34.271  33.863  1.00 156.54 ? 574  HIS A CE1 1 
ATOM   4421  N  NE2 . HIS A 1 574  ? -70.545  34.012  33.699  1.00 157.07 ? 574  HIS A NE2 1 
ATOM   4422  N  N   . LEU A 1 575  ? -66.234  29.189  32.272  1.00 157.41 ? 575  LEU A N   1 
ATOM   4423  C  CA  . LEU A 1 575  ? -65.618  27.861  32.298  1.00 165.35 ? 575  LEU A CA  1 
ATOM   4424  C  C   . LEU A 1 575  ? -66.190  26.985  33.416  1.00 176.48 ? 575  LEU A C   1 
ATOM   4425  O  O   . LEU A 1 575  ? -66.457  27.479  34.510  1.00 181.15 ? 575  LEU A O   1 
ATOM   4426  C  CB  . LEU A 1 575  ? -64.100  27.969  32.438  1.00 160.61 ? 575  LEU A CB  1 
ATOM   4427  C  CG  . LEU A 1 575  ? -63.347  28.412  31.184  1.00 153.97 ? 575  LEU A CG  1 
ATOM   4428  C  CD1 . LEU A 1 575  ? -61.839  28.346  31.379  1.00 151.76 ? 575  LEU A CD1 1 
ATOM   4429  C  CD2 . LEU A 1 575  ? -63.765  27.555  30.009  1.00 153.21 ? 575  LEU A CD2 1 
ATOM   4430  N  N   . SER A 1 576  ? -66.365  25.688  33.144  1.00 182.99 ? 576  SER A N   1 
ATOM   4431  C  CA  . SER A 1 576  ? -67.024  24.767  34.089  1.00 191.19 ? 576  SER A CA  1 
ATOM   4432  C  C   . SER A 1 576  ? -66.302  24.655  35.430  1.00 193.73 ? 576  SER A C   1 
ATOM   4433  O  O   . SER A 1 576  ? -66.871  24.989  36.474  1.00 194.12 ? 576  SER A O   1 
ATOM   4434  C  CB  . SER A 1 576  ? -67.231  23.373  33.475  1.00 196.00 ? 576  SER A CB  1 
ATOM   4435  O  OG  . SER A 1 576  ? -68.531  23.237  32.913  1.00 199.40 ? 576  SER A OG  1 
ATOM   4436  N  N   . PRO A 1 577  ? -65.060  24.156  35.417  1.00 199.61 ? 577  PRO A N   1 
ATOM   4437  C  CA  . PRO A 1 577  ? -64.290  24.348  36.642  1.00 201.20 ? 577  PRO A CA  1 
ATOM   4438  C  C   . PRO A 1 577  ? -63.838  25.811  36.702  1.00 200.07 ? 577  PRO A C   1 
ATOM   4439  O  O   . PRO A 1 577  ? -62.931  26.178  35.964  1.00 200.91 ? 577  PRO A O   1 
ATOM   4440  C  CB  . PRO A 1 577  ? -63.090  23.417  36.439  1.00 204.35 ? 577  PRO A CB  1 
ATOM   4441  C  CG  . PRO A 1 577  ? -63.488  22.483  35.336  1.00 204.39 ? 577  PRO A CG  1 
ATOM   4442  C  CD  . PRO A 1 577  ? -64.361  23.289  34.456  1.00 201.01 ? 577  PRO A CD  1 
ATOM   4443  N  N   . ASP A 1 578  ? -64.457  26.640  37.540  1.00 195.74 ? 578  ASP A N   1 
ATOM   4444  C  CA  . ASP A 1 578  ? -64.101  28.059  37.552  1.00 191.83 ? 578  ASP A CA  1 
ATOM   4445  C  C   . ASP A 1 578  ? -62.706  28.271  38.142  1.00 189.27 ? 578  ASP A C   1 
ATOM   4446  O  O   . ASP A 1 578  ? -62.281  29.406  38.315  1.00 186.28 ? 578  ASP A O   1 
ATOM   4447  C  CB  . ASP A 1 578  ? -65.155  28.911  38.290  1.00 194.16 ? 578  ASP A CB  1 
ATOM   4448  C  CG  . ASP A 1 578  ? -65.165  30.392  37.838  1.00 196.44 ? 578  ASP A CG  1 
ATOM   4449  O  OD1 . ASP A 1 578  ? -64.160  30.879  37.276  1.00 196.48 ? 578  ASP A OD1 1 
ATOM   4450  O  OD2 . ASP A 1 578  ? -66.189  31.078  38.055  1.00 197.63 ? 578  ASP A OD2 1 
ATOM   4451  N  N   . ALA A 1 579  ? -61.990  27.188  38.440  1.00 190.43 ? 579  ALA A N   1 
ATOM   4452  C  CA  . ALA A 1 579  ? -60.649  27.311  39.014  1.00 190.34 ? 579  ALA A CA  1 
ATOM   4453  C  C   . ALA A 1 579  ? -59.735  28.174  38.140  1.00 184.95 ? 579  ALA A C   1 
ATOM   4454  O  O   . ALA A 1 579  ? -59.895  28.233  36.923  1.00 185.26 ? 579  ALA A O   1 
ATOM   4455  C  CB  . ALA A 1 579  ? -60.034  25.947  39.276  1.00 193.19 ? 579  ALA A CB  1 
ATOM   4456  N  N   . ASP A 1 580  ? -58.788  28.854  38.780  1.00 181.37 ? 580  ASP A N   1 
ATOM   4457  C  CA  . ASP A 1 580  ? -57.966  29.868  38.119  1.00 178.95 ? 580  ASP A CA  1 
ATOM   4458  C  C   . ASP A 1 580  ? -56.673  29.285  37.586  1.00 176.76 ? 580  ASP A C   1 
ATOM   4459  O  O   . ASP A 1 580  ? -55.712  30.007  37.321  1.00 176.33 ? 580  ASP A O   1 
ATOM   4460  C  CB  . ASP A 1 580  ? -57.648  31.010  39.083  1.00 183.81 ? 580  ASP A CB  1 
ATOM   4461  C  CG  . ASP A 1 580  ? -56.814  30.553  40.267  1.00 192.00 ? 580  ASP A CG  1 
ATOM   4462  O  OD1 . ASP A 1 580  ? -56.082  29.541  40.124  1.00 195.28 ? 580  ASP A OD1 1 
ATOM   4463  O  OD2 . ASP A 1 580  ? -56.890  31.207  41.336  1.00 195.07 ? 580  ASP A OD2 1 
ATOM   4464  N  N   . ALA A 1 581  ? -56.647  27.967  37.469  1.00 176.28 ? 581  ALA A N   1 
ATOM   4465  C  CA  . ALA A 1 581  ? -55.524  27.280  36.861  1.00 174.03 ? 581  ALA A CA  1 
ATOM   4466  C  C   . ALA A 1 581  ? -55.993  25.888  36.452  1.00 172.59 ? 581  ALA A C   1 
ATOM   4467  O  O   . ALA A 1 581  ? -56.746  25.247  37.186  1.00 173.05 ? 581  ALA A O   1 
ATOM   4468  C  CB  . ALA A 1 581  ? -54.371  27.204  37.831  1.00 176.69 ? 581  ALA A CB  1 
ATOM   4469  N  N   . TYR A 1 582  ? -55.564  25.428  35.277  1.00 166.82 ? 582  TYR A N   1 
ATOM   4470  C  CA  . TYR A 1 582  ? -56.022  24.149  34.745  1.00 162.83 ? 582  TYR A CA  1 
ATOM   4471  C  C   . TYR A 1 582  ? -54.870  23.237  34.394  1.00 159.29 ? 582  TYR A C   1 
ATOM   4472  O  O   . TYR A 1 582  ? -53.743  23.674  34.161  1.00 159.69 ? 582  TYR A O   1 
ATOM   4473  C  CB  . TYR A 1 582  ? -56.869  24.334  33.482  1.00 159.55 ? 582  TYR A CB  1 
ATOM   4474  C  CG  . TYR A 1 582  ? -58.187  25.043  33.676  1.00 157.35 ? 582  TYR A CG  1 
ATOM   4475  C  CD1 . TYR A 1 582  ? -59.342  24.338  33.997  1.00 157.81 ? 582  TYR A CD1 1 
ATOM   4476  C  CD2 . TYR A 1 582  ? -58.282  26.421  33.514  1.00 155.05 ? 582  TYR A CD2 1 
ATOM   4477  C  CE1 . TYR A 1 582  ? -60.556  24.995  34.167  1.00 157.15 ? 582  TYR A CE1 1 
ATOM   4478  C  CE2 . TYR A 1 582  ? -59.484  27.084  33.683  1.00 154.22 ? 582  TYR A CE2 1 
ATOM   4479  C  CZ  . TYR A 1 582  ? -60.617  26.373  34.008  1.00 155.42 ? 582  TYR A CZ  1 
ATOM   4480  O  OH  . TYR A 1 582  ? -61.804  27.054  34.172  1.00 154.87 ? 582  TYR A OH  1 
ATOM   4481  N  N   . SER A 1 583  ? -55.187  21.955  34.338  1.00 158.71 ? 583  SER A N   1 
ATOM   4482  C  CA  . SER A 1 583  ? -54.235  20.929  33.963  1.00 157.34 ? 583  SER A CA  1 
ATOM   4483  C  C   . SER A 1 583  ? -54.060  20.875  32.446  1.00 155.19 ? 583  SER A C   1 
ATOM   4484  O  O   . SER A 1 583  ? -55.040  20.931  31.706  1.00 150.06 ? 583  SER A O   1 
ATOM   4485  C  CB  . SER A 1 583  ? -54.738  19.585  34.472  1.00 163.69 ? 583  SER A CB  1 
ATOM   4486  O  OG  . SER A 1 583  ? -56.117  19.447  34.173  1.00 165.44 ? 583  SER A OG  1 
ATOM   4487  N  N   . PRO A 1 584  ? -52.804  20.744  31.983  1.00 153.60 ? 584  PRO A N   1 
ATOM   4488  C  CA  . PRO A 1 584  ? -52.497  20.722  30.551  1.00 153.55 ? 584  PRO A CA  1 
ATOM   4489  C  C   . PRO A 1 584  ? -53.122  19.528  29.866  1.00 150.08 ? 584  PRO A C   1 
ATOM   4490  O  O   . PRO A 1 584  ? -52.387  18.662  29.431  1.00 151.69 ? 584  PRO A O   1 
ATOM   4491  C  CB  . PRO A 1 584  ? -50.971  20.573  30.516  1.00 153.68 ? 584  PRO A CB  1 
ATOM   4492  C  CG  . PRO A 1 584  ? -50.496  20.943  31.879  1.00 156.05 ? 584  PRO A CG  1 
ATOM   4493  C  CD  . PRO A 1 584  ? -51.596  20.557  32.809  1.00 157.70 ? 584  PRO A CD  1 
ATOM   4494  N  N   . GLY A 1 585  ? -54.441  19.463  29.783  1.00 149.96 ? 585  GLY A N   1 
ATOM   4495  C  CA  . GLY A 1 585  ? -55.072  18.387  29.054  1.00 151.38 ? 585  GLY A CA  1 
ATOM   4496  C  C   . GLY A 1 585  ? -56.478  18.178  29.538  1.00 152.51 ? 585  GLY A C   1 
ATOM   4497  O  O   . GLY A 1 585  ? -57.233  17.387  28.981  1.00 152.99 ? 585  GLY A O   1 
ATOM   4498  N  N   . GLN A 1 586  ? -56.836  18.901  30.587  1.00 154.38 ? 586  GLN A N   1 
ATOM   4499  C  CA  . GLN A 1 586  ? -58.148  18.739  31.186  1.00 157.67 ? 586  GLN A CA  1 
ATOM   4500  C  C   . GLN A 1 586  ? -59.265  18.892  30.176  1.00 159.00 ? 586  GLN A C   1 
ATOM   4501  O  O   . GLN A 1 586  ? -59.273  19.811  29.362  1.00 157.23 ? 586  GLN A O   1 
ATOM   4502  C  CB  . GLN A 1 586  ? -58.364  19.734  32.319  1.00 156.95 ? 586  GLN A CB  1 
ATOM   4503  C  CG  . GLN A 1 586  ? -59.628  19.474  33.096  1.00 159.52 ? 586  GLN A CG  1 
ATOM   4504  C  CD  . GLN A 1 586  ? -59.763  20.382  34.298  1.00 162.33 ? 586  GLN A CD  1 
ATOM   4505  O  OE1 . GLN A 1 586  ? -58.888  21.208  34.576  1.00 162.40 ? 586  GLN A OE1 1 
ATOM   4506  N  NE2 . GLN A 1 586  ? -60.868  20.237  35.022  1.00 164.40 ? 586  GLN A NE2 1 
ATOM   4507  N  N   . THR A 1 587  ? -60.198  17.958  30.233  1.00 164.47 ? 587  THR A N   1 
ATOM   4508  C  CA  . THR A 1 587  ? -61.464  18.103  29.557  1.00 169.04 ? 587  THR A CA  1 
ATOM   4509  C  C   . THR A 1 587  ? -62.220  19.121  30.393  1.00 170.63 ? 587  THR A C   1 
ATOM   4510  O  O   . THR A 1 587  ? -62.153  19.067  31.619  1.00 169.03 ? 587  THR A O   1 
ATOM   4511  C  CB  . THR A 1 587  ? -62.208  16.762  29.558  1.00 173.98 ? 587  THR A CB  1 
ATOM   4512  O  OG1 . THR A 1 587  ? -62.223  16.237  30.890  1.00 176.59 ? 587  THR A OG1 1 
ATOM   4513  C  CG2 . THR A 1 587  ? -61.501  15.750  28.650  1.00 176.04 ? 587  THR A CG2 1 
ATOM   4514  N  N   . VAL A 1 588  ? -62.920  20.052  29.746  1.00 173.60 ? 588  VAL A N   1 
ATOM   4515  C  CA  . VAL A 1 588  ? -63.624  21.122  30.462  1.00 174.73 ? 588  VAL A CA  1 
ATOM   4516  C  C   . VAL A 1 588  ? -64.709  21.808  29.648  1.00 173.70 ? 588  VAL A C   1 
ATOM   4517  O  O   . VAL A 1 588  ? -64.479  22.257  28.535  1.00 174.99 ? 588  VAL A O   1 
ATOM   4518  C  CB  . VAL A 1 588  ? -62.667  22.219  30.949  1.00 174.32 ? 588  VAL A CB  1 
ATOM   4519  C  CG1 . VAL A 1 588  ? -61.713  22.629  29.843  1.00 172.66 ? 588  VAL A CG1 1 
ATOM   4520  C  CG2 . VAL A 1 588  ? -63.462  23.412  31.422  1.00 173.16 ? 588  VAL A CG2 1 
ATOM   4521  N  N   . SER A 1 589  ? -65.886  21.922  30.239  1.00 171.75 ? 589  SER A N   1 
ATOM   4522  C  CA  . SER A 1 589  ? -67.042  22.467  29.549  1.00 171.63 ? 589  SER A CA  1 
ATOM   4523  C  C   . SER A 1 589  ? -67.105  24.003  29.620  1.00 167.99 ? 589  SER A C   1 
ATOM   4524  O  O   . SER A 1 589  ? -66.999  24.579  30.698  1.00 166.55 ? 589  SER A O   1 
ATOM   4525  C  CB  . SER A 1 589  ? -68.307  21.860  30.162  1.00 176.71 ? 589  SER A CB  1 
ATOM   4526  O  OG  . SER A 1 589  ? -68.036  20.579  30.727  1.00 181.10 ? 589  SER A OG  1 
ATOM   4527  N  N   . LEU A 1 590  ? -67.275  24.663  28.476  1.00 165.77 ? 590  LEU A N   1 
ATOM   4528  C  CA  . LEU A 1 590  ? -67.480  26.114  28.449  1.00 160.85 ? 590  LEU A CA  1 
ATOM   4529  C  C   . LEU A 1 590  ? -68.946  26.445  28.201  1.00 159.04 ? 590  LEU A C   1 
ATOM   4530  O  O   . LEU A 1 590  ? -69.612  25.754  27.431  1.00 161.94 ? 590  LEU A O   1 
ATOM   4531  C  CB  . LEU A 1 590  ? -66.608  26.762  27.379  1.00 155.19 ? 590  LEU A CB  1 
ATOM   4532  C  CG  . LEU A 1 590  ? -67.139  28.076  26.809  1.00 147.19 ? 590  LEU A CG  1 
ATOM   4533  C  CD1 . LEU A 1 590  ? -67.098  29.151  27.857  1.00 144.27 ? 590  LEU A CD1 1 
ATOM   4534  C  CD2 . LEU A 1 590  ? -66.355  28.509  25.578  1.00 143.46 ? 590  LEU A CD2 1 
ATOM   4535  N  N   . ASN A 1 591  ? -69.444  27.493  28.857  1.00 154.91 ? 591  ASN A N   1 
ATOM   4536  C  CA  . ASN A 1 591  ? -70.850  27.920  28.740  1.00 152.59 ? 591  ASN A CA  1 
ATOM   4537  C  C   . ASN A 1 591  ? -71.073  29.269  28.023  1.00 149.79 ? 591  ASN A C   1 
ATOM   4538  O  O   . ASN A 1 591  ? -70.355  30.234  28.269  1.00 148.84 ? 591  ASN A O   1 
ATOM   4539  C  CB  . ASN A 1 591  ? -71.508  27.980  30.134  1.00 153.73 ? 591  ASN A CB  1 
ATOM   4540  C  CG  . ASN A 1 591  ? -71.863  26.607  30.683  1.00 157.88 ? 591  ASN A CG  1 
ATOM   4541  O  OD1 . ASN A 1 591  ? -72.744  25.925  30.158  1.00 159.68 ? 591  ASN A OD1 1 
ATOM   4542  N  ND2 . ASN A 1 591  ? -71.190  26.206  31.759  1.00 159.53 ? 591  ASN A ND2 1 
ATOM   4543  N  N   . MET A 1 592  ? -72.072  29.337  27.147  1.00 148.64 ? 592  MET A N   1 
ATOM   4544  C  CA  . MET A 1 592  ? -72.511  30.615  26.597  1.00 145.28 ? 592  MET A CA  1 
ATOM   4545  C  C   . MET A 1 592  ? -73.749  31.105  27.348  1.00 146.80 ? 592  MET A C   1 
ATOM   4546  O  O   . MET A 1 592  ? -74.407  30.320  28.029  1.00 147.70 ? 592  MET A O   1 
ATOM   4547  C  CB  . MET A 1 592  ? -72.803  30.496  25.104  1.00 144.15 ? 592  MET A CB  1 
ATOM   4548  C  CG  . MET A 1 592  ? -71.666  30.936  24.180  1.00 141.93 ? 592  MET A CG  1 
ATOM   4549  S  SD  . MET A 1 592  ? -70.524  29.609  23.778  1.00 162.71 ? 592  MET A SD  1 
ATOM   4550  C  CE  . MET A 1 592  ? -71.675  28.243  23.849  1.00 151.20 ? 592  MET A CE  1 
ATOM   4551  N  N   . ALA A 1 593  ? -74.064  32.395  27.225  1.00 146.60 ? 593  ALA A N   1 
ATOM   4552  C  CA  . ALA A 1 593  ? -75.192  32.998  27.949  1.00 149.54 ? 593  ALA A CA  1 
ATOM   4553  C  C   . ALA A 1 593  ? -75.763  34.241  27.254  1.00 152.88 ? 593  ALA A C   1 
ATOM   4554  O  O   . ALA A 1 593  ? -75.011  35.088  26.767  1.00 150.73 ? 593  ALA A O   1 
ATOM   4555  C  CB  . ALA A 1 593  ? -74.787  33.335  29.390  1.00 147.82 ? 593  ALA A CB  1 
ATOM   4556  N  N   . THR A 1 594  ? -77.093  34.342  27.219  1.00 159.16 ? 594  THR A N   1 
ATOM   4557  C  CA  . THR A 1 594  ? -77.769  35.506  26.643  1.00 163.68 ? 594  THR A CA  1 
ATOM   4558  C  C   . THR A 1 594  ? -79.205  35.652  27.106  1.00 168.12 ? 594  THR A C   1 
ATOM   4559  O  O   . THR A 1 594  ? -79.905  34.666  27.328  1.00 171.44 ? 594  THR A O   1 
ATOM   4560  C  CB  . THR A 1 594  ? -77.863  35.431  25.123  1.00 164.66 ? 594  THR A CB  1 
ATOM   4561  O  OG1 . THR A 1 594  ? -76.876  34.532  24.617  1.00 164.52 ? 594  THR A OG1 1 
ATOM   4562  C  CG2 . THR A 1 594  ? -77.695  36.819  24.515  1.00 163.51 ? 594  THR A CG2 1 
ATOM   4563  N  N   . GLY A 1 595  ? -79.648  36.899  27.205  1.00 171.71 ? 595  GLY A N   1 
ATOM   4564  C  CA  . GLY A 1 595  ? -81.020  37.199  27.569  1.00 176.57 ? 595  GLY A CA  1 
ATOM   4565  C  C   . GLY A 1 595  ? -81.944  37.088  26.375  1.00 184.10 ? 595  GLY A C   1 
ATOM   4566  O  O   . GLY A 1 595  ? -83.154  37.271  26.480  1.00 184.07 ? 595  GLY A O   1 
ATOM   4567  N  N   . MET A 1 596  ? -81.365  36.786  25.225  1.00 187.36 ? 596  MET A N   1 
ATOM   4568  C  CA  . MET A 1 596  ? -82.135  36.653  24.008  1.00 191.75 ? 596  MET A CA  1 
ATOM   4569  C  C   . MET A 1 596  ? -81.313  35.824  23.053  1.00 191.68 ? 596  MET A C   1 
ATOM   4570  O  O   . MET A 1 596  ? -80.096  35.971  22.987  1.00 192.90 ? 596  MET A O   1 
ATOM   4571  C  CB  . MET A 1 596  ? -82.423  38.027  23.400  1.00 191.96 ? 596  MET A CB  1 
ATOM   4572  C  CG  . MET A 1 596  ? -83.557  38.784  24.066  1.00 192.51 ? 596  MET A CG  1 
ATOM   4573  S  SD  . MET A 1 596  ? -85.167  38.056  23.718  1.00 218.02 ? 596  MET A SD  1 
ATOM   4574  C  CE  . MET A 1 596  ? -85.408  38.595  22.030  1.00 168.71 ? 596  MET A CE  1 
ATOM   4575  N  N   . ASP A 1 597  ? -81.979  34.939  22.325  1.00 189.99 ? 597  ASP A N   1 
ATOM   4576  C  CA  . ASP A 1 597  ? -81.312  34.119  21.322  1.00 188.58 ? 597  ASP A CA  1 
ATOM   4577  C  C   . ASP A 1 597  ? -80.264  34.953  20.587  1.00 180.33 ? 597  ASP A C   1 
ATOM   4578  O  O   . ASP A 1 597  ? -80.530  36.101  20.220  1.00 177.63 ? 597  ASP A O   1 
ATOM   4579  C  CB  . ASP A 1 597  ? -82.348  33.586  20.332  1.00 195.57 ? 597  ASP A CB  1 
ATOM   4580  C  CG  . ASP A 1 597  ? -83.511  32.893  21.024  1.00 203.79 ? 597  ASP A CG  1 
ATOM   4581  O  OD1 . ASP A 1 597  ? -83.249  32.018  21.878  1.00 206.65 ? 597  ASP A OD1 1 
ATOM   4582  O  OD2 . ASP A 1 597  ? -84.680  33.218  20.711  1.00 206.47 ? 597  ASP A OD2 1 
ATOM   4583  N  N   . SER A 1 598  ? -79.081  34.381  20.364  1.00 175.55 ? 598  SER A N   1 
ATOM   4584  C  CA  . SER A 1 598  ? -77.977  35.151  19.791  1.00 167.59 ? 598  SER A CA  1 
ATOM   4585  C  C   . SER A 1 598  ? -76.889  34.345  19.080  1.00 158.81 ? 598  SER A C   1 
ATOM   4586  O  O   . SER A 1 598  ? -76.717  33.147  19.311  1.00 158.50 ? 598  SER A O   1 
ATOM   4587  C  CB  . SER A 1 598  ? -77.333  36.028  20.869  1.00 165.55 ? 598  SER A CB  1 
ATOM   4588  O  OG  . SER A 1 598  ? -76.359  36.892  20.311  1.00 163.23 ? 598  SER A OG  1 
ATOM   4589  N  N   . TRP A 1 599  ? -76.162  35.032  18.203  1.00 151.47 ? 599  TRP A N   1 
ATOM   4590  C  CA  . TRP A 1 599  ? -74.938  34.487  17.620  1.00 146.49 ? 599  TRP A CA  1 
ATOM   4591  C  C   . TRP A 1 599  ? -73.733  34.809  18.507  1.00 141.71 ? 599  TRP A C   1 
ATOM   4592  O  O   . TRP A 1 599  ? -73.625  35.908  19.046  1.00 142.22 ? 599  TRP A O   1 
ATOM   4593  C  CB  . TRP A 1 599  ? -74.738  34.989  16.180  1.00 148.19 ? 599  TRP A CB  1 
ATOM   4594  C  CG  . TRP A 1 599  ? -75.769  34.403  15.254  1.00 154.09 ? 599  TRP A CG  1 
ATOM   4595  C  CD1 . TRP A 1 599  ? -76.755  35.067  14.588  1.00 156.71 ? 599  TRP A CD1 1 
ATOM   4596  C  CD2 . TRP A 1 599  ? -75.945  33.017  14.943  1.00 156.79 ? 599  TRP A CD2 1 
ATOM   4597  N  NE1 . TRP A 1 599  ? -77.525  34.182  13.867  1.00 158.16 ? 599  TRP A NE1 1 
ATOM   4598  C  CE2 . TRP A 1 599  ? -77.044  32.916  14.072  1.00 157.68 ? 599  TRP A CE2 1 
ATOM   4599  C  CE3 . TRP A 1 599  ? -75.273  31.852  15.310  1.00 157.68 ? 599  TRP A CE3 1 
ATOM   4600  C  CZ2 . TRP A 1 599  ? -77.482  31.709  13.573  1.00 157.87 ? 599  TRP A CZ2 1 
ATOM   4601  C  CZ3 . TRP A 1 599  ? -75.705  30.661  14.805  1.00 158.03 ? 599  TRP A CZ3 1 
ATOM   4602  C  CH2 . TRP A 1 599  ? -76.799  30.595  13.949  1.00 158.10 ? 599  TRP A CH2 1 
ATOM   4603  N  N   . VAL A 1 600  ? -72.850  33.830  18.677  1.00 135.97 ? 600  VAL A N   1 
ATOM   4604  C  CA  . VAL A 1 600  ? -71.659  33.967  19.498  1.00 129.33 ? 600  VAL A CA  1 
ATOM   4605  C  C   . VAL A 1 600  ? -70.505  34.063  18.527  1.00 125.87 ? 600  VAL A C   1 
ATOM   4606  O  O   . VAL A 1 600  ? -70.739  34.148  17.337  1.00 126.92 ? 600  VAL A O   1 
ATOM   4607  C  CB  . VAL A 1 600  ? -71.490  32.716  20.372  1.00 128.81 ? 600  VAL A CB  1 
ATOM   4608  C  CG1 . VAL A 1 600  ? -70.405  32.911  21.404  1.00 128.20 ? 600  VAL A CG1 1 
ATOM   4609  C  CG2 . VAL A 1 600  ? -72.793  32.394  21.057  1.00 128.40 ? 600  VAL A CG2 1 
ATOM   4610  N  N   . ALA A 1 601  ? -69.270  34.064  19.017  1.00 122.01 ? 601  ALA A N   1 
ATOM   4611  C  CA  . ALA A 1 601  ? -68.095  33.851  18.163  1.00 120.71 ? 601  ALA A CA  1 
ATOM   4612  C  C   . ALA A 1 601  ? -66.808  33.727  18.979  1.00 120.81 ? 601  ALA A C   1 
ATOM   4613  O  O   . ALA A 1 601  ? -66.079  34.703  19.173  1.00 122.07 ? 601  ALA A O   1 
ATOM   4614  C  CB  . ALA A 1 601  ? -67.962  34.950  17.118  1.00 118.77 ? 601  ALA A CB  1 
ATOM   4615  N  N   . LEU A 1 602  ? -66.528  32.511  19.436  1.00 120.34 ? 602  LEU A N   1 
ATOM   4616  C  CA  . LEU A 1 602  ? -65.392  32.255  20.309  1.00 119.53 ? 602  LEU A CA  1 
ATOM   4617  C  C   . LEU A 1 602  ? -64.027  32.461  19.633  1.00 121.67 ? 602  LEU A C   1 
ATOM   4618  O  O   . LEU A 1 602  ? -63.921  32.707  18.430  1.00 121.95 ? 602  LEU A O   1 
ATOM   4619  C  CB  . LEU A 1 602  ? -65.483  30.856  20.932  1.00 117.76 ? 602  LEU A CB  1 
ATOM   4620  C  CG  . LEU A 1 602  ? -66.883  30.461  21.412  1.00 116.29 ? 602  LEU A CG  1 
ATOM   4621  C  CD1 . LEU A 1 602  ? -66.882  29.181  22.288  1.00 114.18 ? 602  LEU A CD1 1 
ATOM   4622  C  CD2 . LEU A 1 602  ? -67.557  31.631  22.125  1.00 113.78 ? 602  LEU A CD2 1 
ATOM   4623  N  N   . ALA A 1 603  ? -62.985  32.368  20.448  1.00 121.66 ? 603  ALA A N   1 
ATOM   4624  C  CA  . ALA A 1 603  ? -61.604  32.541  20.026  1.00 116.87 ? 603  ALA A CA  1 
ATOM   4625  C  C   . ALA A 1 603  ? -60.800  32.332  21.297  1.00 115.38 ? 603  ALA A C   1 
ATOM   4626  O  O   . ALA A 1 603  ? -61.264  32.641  22.389  1.00 113.75 ? 603  ALA A O   1 
ATOM   4627  C  CB  . ALA A 1 603  ? -61.371  33.929  19.444  1.00 114.90 ? 603  ALA A CB  1 
ATOM   4628  N  N   . ALA A 1 604  ? -59.614  31.764  21.161  1.00 113.67 ? 604  ALA A N   1 
ATOM   4629  C  CA  . ALA A 1 604  ? -58.775  31.481  22.310  1.00 113.15 ? 604  ALA A CA  1 
ATOM   4630  C  C   . ALA A 1 604  ? -57.360  31.799  21.898  1.00 112.89 ? 604  ALA A C   1 
ATOM   4631  O  O   . ALA A 1 604  ? -56.693  31.007  21.257  1.00 114.39 ? 604  ALA A O   1 
ATOM   4632  C  CB  . ALA A 1 604  ? -58.905  30.027  22.741  1.00 111.60 ? 604  ALA A CB  1 
ATOM   4633  N  N   . VAL A 1 605  ? -56.923  32.994  22.249  1.00 112.86 ? 605  VAL A N   1 
ATOM   4634  C  CA  . VAL A 1 605  ? -55.617  33.477  21.871  1.00 114.32 ? 605  VAL A CA  1 
ATOM   4635  C  C   . VAL A 1 605  ? -54.637  33.194  22.980  1.00 116.75 ? 605  VAL A C   1 
ATOM   4636  O  O   . VAL A 1 605  ? -54.998  33.257  24.154  1.00 118.01 ? 605  VAL A O   1 
ATOM   4637  C  CB  . VAL A 1 605  ? -55.672  34.980  21.703  1.00 112.37 ? 605  VAL A CB  1 
ATOM   4638  C  CG1 . VAL A 1 605  ? -54.282  35.544  21.555  1.00 112.88 ? 605  VAL A CG1 1 
ATOM   4639  C  CG2 . VAL A 1 605  ? -56.568  35.341  20.528  1.00 112.45 ? 605  VAL A CG2 1 
ATOM   4640  N  N   . ASP A 1 606  ? -53.394  32.879  22.639  1.00 119.58 ? 606  ASP A N   1 
ATOM   4641  C  CA  . ASP A 1 606  ? -52.381  32.892  23.676  1.00 120.68 ? 606  ASP A CA  1 
ATOM   4642  C  C   . ASP A 1 606  ? -52.359  34.320  24.141  1.00 119.02 ? 606  ASP A C   1 
ATOM   4643  O  O   . ASP A 1 606  ? -51.815  35.191  23.464  1.00 120.16 ? 606  ASP A O   1 
ATOM   4644  C  CB  . ASP A 1 606  ? -50.996  32.525  23.156  1.00 123.58 ? 606  ASP A CB  1 
ATOM   4645  C  CG  . ASP A 1 606  ? -49.902  32.887  24.139  1.00 123.26 ? 606  ASP A CG  1 
ATOM   4646  O  OD1 . ASP A 1 606  ? -50.267  33.385  25.217  1.00 123.89 ? 606  ASP A OD1 1 
ATOM   4647  O  OD2 . ASP A 1 606  ? -48.698  32.682  23.853  1.00 122.89 ? 606  ASP A OD2 1 
ATOM   4648  N  N   . SER A 1 607  ? -52.957  34.554  25.300  1.00 110.78 ? 607  SER A N   1 
ATOM   4649  C  CA  . SER A 1 607  ? -53.034  35.886  25.879  1.00 112.31 ? 607  SER A CA  1 
ATOM   4650  C  C   . SER A 1 607  ? -51.728  36.700  25.821  1.00 110.64 ? 607  SER A C   1 
ATOM   4651  O  O   . SER A 1 607  ? -51.741  37.910  26.054  1.00 109.77 ? 607  SER A O   1 
ATOM   4652  C  CB  . SER A 1 607  ? -53.410  35.770  27.352  1.00 119.07 ? 607  SER A CB  1 
ATOM   4653  O  OG  . SER A 1 607  ? -52.216  35.580  28.135  1.00 122.49 ? 607  SER A OG  1 
ATOM   4654  N  N   . ALA A 1 608  ? -50.606  36.052  25.545  1.00 109.28 ? 608  ALA A N   1 
ATOM   4655  C  CA  . ALA A 1 608  ? -49.321  36.720  25.672  1.00 107.59 ? 608  ALA A CA  1 
ATOM   4656  C  C   . ALA A 1 608  ? -48.990  37.756  24.589  1.00 103.21 ? 608  ALA A C   1 
ATOM   4657  O  O   . ALA A 1 608  ? -48.116  38.597  24.789  1.00 102.29 ? 608  ALA A O   1 
ATOM   4658  C  CB  . ALA A 1 608  ? -48.223  35.704  25.758  1.00 111.17 ? 608  ALA A CB  1 
ATOM   4659  N  N   . VAL A 1 609  ? -49.658  37.702  23.447  1.00 100.44 ? 609  VAL A N   1 
ATOM   4660  C  CA  . VAL A 1 609  ? -49.379  38.669  22.396  1.00 96.11  ? 609  VAL A CA  1 
ATOM   4661  C  C   . VAL A 1 609  ? -49.482  40.098  22.929  1.00 96.22  ? 609  VAL A C   1 
ATOM   4662  O  O   . VAL A 1 609  ? -48.456  40.771  23.095  1.00 96.05  ? 609  VAL A O   1 
ATOM   4663  C  CB  . VAL A 1 609  ? -50.321  38.453  21.229  1.00 92.53  ? 609  VAL A CB  1 
ATOM   4664  C  CG1 . VAL A 1 609  ? -49.936  37.189  20.561  1.00 95.09  ? 609  VAL A CG1 1 
ATOM   4665  C  CG2 . VAL A 1 609  ? -51.727  38.325  21.706  1.00 91.69  ? 609  VAL A CG2 1 
ATOM   4666  N  N   . TYR A 1 610  ? -50.710  40.537  23.215  1.00 94.32  ? 610  TYR A N   1 
ATOM   4667  C  CA  . TYR A 1 610  ? -50.964  41.789  23.901  1.00 92.48  ? 610  TYR A CA  1 
ATOM   4668  C  C   . TYR A 1 610  ? -50.037  41.963  25.136  1.00 150.05 ? 610  TYR A C   1 
ATOM   4669  O  O   . TYR A 1 610  ? -49.082  42.754  25.132  1.00 144.22 ? 610  TYR A O   1 
ATOM   4670  C  CB  . TYR A 1 610  ? -52.419  41.799  24.375  1.00 90.46  ? 610  TYR A CB  1 
ATOM   4671  C  CG  . TYR A 1 610  ? -53.404  40.989  23.577  1.00 92.65  ? 610  TYR A CG  1 
ATOM   4672  C  CD1 . TYR A 1 610  ? -54.193  41.590  22.627  1.00 94.10  ? 610  TYR A CD1 1 
ATOM   4673  C  CD2 . TYR A 1 610  ? -53.582  39.638  23.800  1.00 90.96  ? 610  TYR A CD2 1 
ATOM   4674  C  CE1 . TYR A 1 610  ? -55.128  40.855  21.865  1.00 97.45  ? 610  TYR A CE1 1 
ATOM   4675  C  CE2 . TYR A 1 610  ? -54.522  38.882  23.045  1.00 94.65  ? 610  TYR A CE2 1 
ATOM   4676  C  CZ  . TYR A 1 610  ? -55.295  39.508  22.066  1.00 96.80  ? 610  TYR A CZ  1 
ATOM   4677  O  OH  . TYR A 1 610  ? -56.240  38.852  21.277  1.00 93.93  ? 610  TYR A OH  1 
ATOM   4678  N  N   . GLY A 1 611  ? -50.356  41.219  26.193  1.00 157.06 ? 611  GLY A N   1 
ATOM   4679  C  CA  . GLY A 1 611  ? -49.516  41.096  27.368  1.00 164.51 ? 611  GLY A CA  1 
ATOM   4680  C  C   . GLY A 1 611  ? -48.903  42.361  27.934  1.00 172.08 ? 611  GLY A C   1 
ATOM   4681  O  O   . GLY A 1 611  ? -49.566  43.088  28.676  1.00 173.89 ? 611  GLY A O   1 
ATOM   4682  N  N   . VAL A 1 612  ? -47.638  42.617  27.587  1.00 178.95 ? 612  VAL A N   1 
ATOM   4683  C  CA  . VAL A 1 612  ? -46.829  43.665  28.236  1.00 186.83 ? 612  VAL A CA  1 
ATOM   4684  C  C   . VAL A 1 612  ? -47.597  44.976  28.337  1.00 196.97 ? 612  VAL A C   1 
ATOM   4685  O  O   . VAL A 1 612  ? -47.907  45.597  27.319  1.00 197.64 ? 612  VAL A O   1 
ATOM   4686  C  CB  . VAL A 1 612  ? -45.471  43.914  27.509  1.00 267.35 ? 612  VAL A CB  1 
ATOM   4687  C  CG1 . VAL A 1 612  ? -44.443  42.841  27.872  1.00 268.81 ? 612  VAL A CG1 1 
ATOM   4688  C  CG2 . VAL A 1 612  ? -45.664  44.008  25.999  1.00 266.72 ? 612  VAL A CG2 1 
ATOM   4689  N  N   . GLN A 1 613  ? -47.888  45.395  29.567  1.00 208.81 ? 613  GLN A N   1 
ATOM   4690  C  CA  . GLN A 1 613  ? -48.850  46.471  29.817  1.00 218.50 ? 613  GLN A CA  1 
ATOM   4691  C  C   . GLN A 1 613  ? -49.931  46.511  28.743  1.00 227.16 ? 613  GLN A C   1 
ATOM   4692  O  O   . GLN A 1 613  ? -49.821  47.250  27.761  1.00 225.40 ? 613  GLN A O   1 
ATOM   4693  C  CB  . GLN A 1 613  ? -48.182  47.856  29.971  1.00 219.39 ? 613  GLN A CB  1 
ATOM   4694  C  CG  . GLN A 1 613  ? -49.195  49.039  30.031  1.00 216.71 ? 613  GLN A CG  1 
ATOM   4695  C  CD  . GLN A 1 613  ? -48.701  50.269  30.810  1.00 215.30 ? 613  GLN A CD  1 
ATOM   4696  O  OE1 . GLN A 1 613  ? -48.126  50.154  31.894  1.00 215.63 ? 613  GLN A OE1 1 
ATOM   4697  N  NE2 . GLN A 1 613  ? -48.959  51.451  30.263  1.00 213.66 ? 613  GLN A NE2 1 
ATOM   4698  N  N   . ARG A 1 614  ? -50.969  45.702  28.922  1.00 235.66 ? 614  ARG A N   1 
ATOM   4699  C  CA  . ARG A 1 614  ? -52.116  45.777  28.037  1.00 241.15 ? 614  ARG A CA  1 
ATOM   4700  C  C   . ARG A 1 614  ? -52.823  47.083  28.339  1.00 245.39 ? 614  ARG A C   1 
ATOM   4701  O  O   . ARG A 1 614  ? -53.713  47.129  29.186  1.00 247.58 ? 614  ARG A O   1 
ATOM   4702  C  CB  . ARG A 1 614  ? -53.052  44.597  28.265  1.00 242.48 ? 614  ARG A CB  1 
ATOM   4703  C  CG  . ARG A 1 614  ? -54.030  44.353  27.137  1.00 240.74 ? 614  ARG A CG  1 
ATOM   4704  C  CD  . ARG A 1 614  ? -54.144  42.868  26.916  1.00 241.10 ? 614  ARG A CD  1 
ATOM   4705  N  NE  . ARG A 1 614  ? -55.493  42.456  26.570  1.00 241.73 ? 614  ARG A NE  1 
ATOM   4706  C  CZ  . ARG A 1 614  ? -56.007  41.284  26.910  1.00 244.01 ? 614  ARG A CZ  1 
ATOM   4707  N  NH1 . ARG A 1 614  ? -55.279  40.422  27.610  1.00 245.05 ? 614  ARG A NH1 1 
ATOM   4708  N  NH2 . ARG A 1 614  ? -57.247  40.982  26.565  1.00 245.70 ? 614  ARG A NH2 1 
ATOM   4709  N  N   . GLY A 1 615  ? -52.412  48.142  27.646  1.00 245.29 ? 615  GLY A N   1 
ATOM   4710  C  CA  . GLY A 1 615  ? -52.888  49.483  27.925  1.00 247.02 ? 615  GLY A CA  1 
ATOM   4711  C  C   . GLY A 1 615  ? -54.338  49.482  28.349  1.00 251.36 ? 615  GLY A C   1 
ATOM   4712  O  O   . GLY A 1 615  ? -55.178  48.843  27.709  1.00 253.03 ? 615  GLY A O   1 
ATOM   4713  N  N   . ALA A 1 616  ? -54.628  50.193  29.435  1.00 253.76 ? 616  ALA A N   1 
ATOM   4714  C  CA  . ALA A 1 616  ? -55.974  50.219  29.986  1.00 256.48 ? 616  ALA A CA  1 
ATOM   4715  C  C   . ALA A 1 616  ? -57.018  50.438  28.890  1.00 256.63 ? 616  ALA A C   1 
ATOM   4716  O  O   . ALA A 1 616  ? -57.883  49.587  28.682  1.00 258.73 ? 616  ALA A O   1 
ATOM   4717  C  CB  . ALA A 1 616  ? -56.088  51.280  31.075  1.00 256.65 ? 616  ALA A CB  1 
ATOM   4718  N  N   . LYS A 1 617  ? -56.912  51.560  28.178  1.00 253.66 ? 617  LYS A N   1 
ATOM   4719  C  CA  . LYS A 1 617  ? -57.890  51.927  27.151  1.00 251.41 ? 617  LYS A CA  1 
ATOM   4720  C  C   . LYS A 1 617  ? -59.240  51.344  27.519  1.00 248.63 ? 617  LYS A C   1 
ATOM   4721  O  O   . LYS A 1 617  ? -59.903  51.856  28.412  1.00 250.14 ? 617  LYS A O   1 
ATOM   4722  C  CB  . LYS A 1 617  ? -57.462  51.440  25.763  1.00 252.62 ? 617  LYS A CB  1 
ATOM   4723  C  CG  . LYS A 1 617  ? -58.268  52.047  24.609  1.00 253.60 ? 617  LYS A CG  1 
ATOM   4724  C  CD  . LYS A 1 617  ? -58.201  53.571  24.635  1.00 253.15 ? 617  LYS A CD  1 
ATOM   4725  C  CE  . LYS A 1 617  ? -58.810  54.199  23.391  1.00 253.62 ? 617  LYS A CE  1 
ATOM   4726  N  NZ  . LYS A 1 617  ? -58.742  55.688  23.443  1.00 252.81 ? 617  LYS A NZ  1 
ATOM   4727  N  N   . LYS A 1 618  ? -59.619  50.260  26.841  1.00 244.00 ? 618  LYS A N   1 
ATOM   4728  C  CA  . LYS A 1 618  ? -60.792  49.449  27.185  1.00 240.53 ? 618  LYS A CA  1 
ATOM   4729  C  C   . LYS A 1 618  ? -60.874  48.218  26.265  1.00 229.49 ? 618  LYS A C   1 
ATOM   4730  O  O   . LYS A 1 618  ? -60.259  48.196  25.195  1.00 225.70 ? 618  LYS A O   1 
ATOM   4731  C  CB  . LYS A 1 618  ? -62.088  50.259  27.070  1.00 247.05 ? 618  LYS A CB  1 
ATOM   4732  C  CG  . LYS A 1 618  ? -62.295  51.381  28.089  1.00 251.54 ? 618  LYS A CG  1 
ATOM   4733  C  CD  . LYS A 1 618  ? -62.602  50.891  29.497  1.00 255.91 ? 618  LYS A CD  1 
ATOM   4734  C  CE  . LYS A 1 618  ? -63.024  52.050  30.413  1.00 256.43 ? 618  LYS A CE  1 
ATOM   4735  N  NZ  . LYS A 1 618  ? -62.038  53.173  30.464  1.00 254.27 ? 618  LYS A NZ  1 
ATOM   4736  N  N   . PRO A 1 619  ? -61.622  47.181  26.687  1.00 224.40 ? 619  PRO A N   1 
ATOM   4737  C  CA  . PRO A 1 619  ? -61.885  46.002  25.848  1.00 220.18 ? 619  PRO A CA  1 
ATOM   4738  C  C   . PRO A 1 619  ? -63.111  46.151  24.924  1.00 215.65 ? 619  PRO A C   1 
ATOM   4739  O  O   . PRO A 1 619  ? -62.928  46.210  23.708  1.00 214.38 ? 619  PRO A O   1 
ATOM   4740  C  CB  . PRO A 1 619  ? -62.119  44.886  26.876  1.00 224.04 ? 619  PRO A CB  1 
ATOM   4741  C  CG  . PRO A 1 619  ? -61.798  45.497  28.240  1.00 224.52 ? 619  PRO A CG  1 
ATOM   4742  C  CD  . PRO A 1 619  ? -62.031  46.956  28.082  1.00 223.75 ? 619  PRO A CD  1 
ATOM   4743  N  N   . LEU A 1 620  ? -64.321  46.204  25.500  1.00 212.55 ? 620  LEU A N   1 
ATOM   4744  C  CA  . LEU A 1 620  ? -65.601  46.389  24.772  1.00 208.79 ? 620  LEU A CA  1 
ATOM   4745  C  C   . LEU A 1 620  ? -65.886  47.843  24.361  1.00 207.12 ? 620  LEU A C   1 
ATOM   4746  O  O   . LEU A 1 620  ? -66.745  48.104  23.520  1.00 208.82 ? 620  LEU A O   1 
ATOM   4747  C  CB  . LEU A 1 620  ? -66.777  45.857  25.611  1.00 206.32 ? 620  LEU A CB  1 
ATOM   4748  C  CG  . LEU A 1 620  ? -68.204  46.264  25.236  1.00 204.72 ? 620  LEU A CG  1 
ATOM   4749  C  CD1 . LEU A 1 620  ? -68.662  45.507  24.010  1.00 205.91 ? 620  LEU A CD1 1 
ATOM   4750  C  CD2 . LEU A 1 620  ? -69.176  46.030  26.382  1.00 205.70 ? 620  LEU A CD2 1 
ATOM   4751  N  N   . GLU A 1 621  ? -65.179  48.782  24.986  1.00 204.91 ? 621  GLU A N   1 
ATOM   4752  C  CA  . GLU A 1 621  ? -65.224  50.196  24.617  1.00 203.72 ? 621  GLU A CA  1 
ATOM   4753  C  C   . GLU A 1 621  ? -64.404  50.425  23.335  1.00 197.49 ? 621  GLU A C   1 
ATOM   4754  O  O   . GLU A 1 621  ? -64.644  51.385  22.603  1.00 196.97 ? 621  GLU A O   1 
ATOM   4755  C  CB  . GLU A 1 621  ? -64.740  51.065  25.800  1.00 208.16 ? 621  GLU A CB  1 
ATOM   4756  C  CG  . GLU A 1 621  ? -64.496  52.566  25.538  1.00 212.01 ? 621  GLU A CG  1 
ATOM   4757  C  CD  . GLU A 1 621  ? -63.959  53.315  26.773  1.00 214.38 ? 621  GLU A CD  1 
ATOM   4758  O  OE1 . GLU A 1 621  ? -64.560  53.182  27.863  1.00 216.48 ? 621  GLU A OE1 1 
ATOM   4759  O  OE2 . GLU A 1 621  ? -62.935  54.033  26.659  1.00 213.30 ? 621  GLU A OE2 1 
ATOM   4760  N  N   . ARG A 1 622  ? -63.454  49.529  23.057  1.00 192.18 ? 622  ARG A N   1 
ATOM   4761  C  CA  . ARG A 1 622  ? -62.714  49.559  21.796  1.00 184.98 ? 622  ARG A CA  1 
ATOM   4762  C  C   . ARG A 1 622  ? -63.729  49.676  20.665  1.00 179.71 ? 622  ARG A C   1 
ATOM   4763  O  O   . ARG A 1 622  ? -63.659  50.602  19.859  1.00 178.95 ? 622  ARG A O   1 
ATOM   4764  C  CB  . ARG A 1 622  ? -61.844  48.299  21.630  1.00 185.95 ? 622  ARG A CB  1 
ATOM   4765  C  CG  . ARG A 1 622  ? -60.725  48.392  20.573  1.00 184.66 ? 622  ARG A CG  1 
ATOM   4766  C  CD  . ARG A 1 622  ? -59.875  47.095  20.488  1.00 168.58 ? 622  ARG A CD  1 
ATOM   4767  N  NE  . ARG A 1 622  ? -60.633  45.926  20.012  1.00 171.66 ? 622  ARG A NE  1 
ATOM   4768  C  CZ  . ARG A 1 622  ? -60.129  44.700  19.849  1.00 171.97 ? 622  ARG A CZ  1 
ATOM   4769  N  NH1 . ARG A 1 622  ? -58.853  44.468  20.125  1.00 170.97 ? 622  ARG A NH1 1 
ATOM   4770  N  NH2 . ARG A 1 622  ? -60.901  43.702  19.413  1.00 172.99 ? 622  ARG A NH2 1 
ATOM   4771  N  N   . VAL A 1 623  ? -64.697  48.763  20.625  1.00 175.08 ? 623  VAL A N   1 
ATOM   4772  C  CA  . VAL A 1 623  ? -65.744  48.832  19.603  1.00 172.14 ? 623  VAL A CA  1 
ATOM   4773  C  C   . VAL A 1 623  ? -66.699  50.019  19.799  1.00 167.51 ? 623  VAL A C   1 
ATOM   4774  O  O   . VAL A 1 623  ? -66.915  50.799  18.874  1.00 166.72 ? 623  VAL A O   1 
ATOM   4775  C  CB  . VAL A 1 623  ? -66.529  47.496  19.447  1.00 131.14 ? 623  VAL A CB  1 
ATOM   4776  C  CG1 . VAL A 1 623  ? -68.027  47.753  19.421  1.00 132.24 ? 623  VAL A CG1 1 
ATOM   4777  C  CG2 . VAL A 1 623  ? -66.054  46.711  18.187  1.00 129.02 ? 623  VAL A CG2 1 
ATOM   4778  N  N   . PHE A 1 624  ? -67.255  50.178  20.994  1.00 163.83 ? 624  PHE A N   1 
ATOM   4779  C  CA  . PHE A 1 624  ? -68.181  51.284  21.216  1.00 159.52 ? 624  PHE A CA  1 
ATOM   4780  C  C   . PHE A 1 624  ? -67.622  52.627  20.775  1.00 161.76 ? 624  PHE A C   1 
ATOM   4781  O  O   . PHE A 1 624  ? -68.349  53.462  20.245  1.00 162.83 ? 624  PHE A O   1 
ATOM   4782  C  CB  . PHE A 1 624  ? -68.623  51.371  22.674  1.00 150.07 ? 624  PHE A CB  1 
ATOM   4783  C  CG  . PHE A 1 624  ? -70.004  50.857  22.908  1.00 142.10 ? 624  PHE A CG  1 
ATOM   4784  C  CD1 . PHE A 1 624  ? -70.263  49.964  23.930  1.00 139.42 ? 624  PHE A CD1 1 
ATOM   4785  C  CD2 . PHE A 1 624  ? -71.042  51.252  22.089  1.00 138.41 ? 624  PHE A CD2 1 
ATOM   4786  C  CE1 . PHE A 1 624  ? -71.532  49.484  24.140  1.00 139.51 ? 624  PHE A CE1 1 
ATOM   4787  C  CE2 . PHE A 1 624  ? -72.305  50.772  22.292  1.00 138.25 ? 624  PHE A CE2 1 
ATOM   4788  C  CZ  . PHE A 1 624  ? -72.553  49.886  23.320  1.00 139.50 ? 624  PHE A CZ  1 
ATOM   4789  N  N   . GLN A 1 625  ? -66.332  52.842  21.006  1.00 163.80 ? 625  GLN A N   1 
ATOM   4790  C  CA  . GLN A 1 625  ? -65.722  54.118  20.657  1.00 167.56 ? 625  GLN A CA  1 
ATOM   4791  C  C   . GLN A 1 625  ? -65.922  54.346  19.176  1.00 166.47 ? 625  GLN A C   1 
ATOM   4792  O  O   . GLN A 1 625  ? -66.600  55.285  18.763  1.00 167.19 ? 625  GLN A O   1 
ATOM   4793  C  CB  . GLN A 1 625  ? -64.228  54.138  20.995  1.00 174.25 ? 625  GLN A CB  1 
ATOM   4794  C  CG  . GLN A 1 625  ? -63.918  54.348  22.475  1.00 182.28 ? 625  GLN A CG  1 
ATOM   4795  C  CD  . GLN A 1 625  ? -62.464  54.728  22.718  1.00 188.43 ? 625  GLN A CD  1 
ATOM   4796  O  OE1 . GLN A 1 625  ? -62.045  55.840  22.399  1.00 190.42 ? 625  GLN A OE1 1 
ATOM   4797  N  NE2 . GLN A 1 625  ? -61.692  53.805  23.292  1.00 190.79 ? 625  GLN A NE2 1 
ATOM   4798  N  N   . PHE A 1 626  ? -65.338  53.453  18.389  1.00 163.41 ? 626  PHE A N   1 
ATOM   4799  C  CA  . PHE A 1 626  ? -65.477  53.462  16.948  1.00 161.88 ? 626  PHE A CA  1 
ATOM   4800  C  C   . PHE A 1 626  ? -66.951  53.540  16.520  1.00 154.17 ? 626  PHE A C   1 
ATOM   4801  O  O   . PHE A 1 626  ? -67.393  54.530  15.937  1.00 150.93 ? 626  PHE A O   1 
ATOM   4802  C  CB  . PHE A 1 626  ? -64.787  52.213  16.382  1.00 167.76 ? 626  PHE A CB  1 
ATOM   4803  C  CG  . PHE A 1 626  ? -65.124  51.917  14.948  1.00 175.16 ? 626  PHE A CG  1 
ATOM   4804  C  CD1 . PHE A 1 626  ? -64.241  52.246  13.932  1.00 177.21 ? 626  PHE A CD1 1 
ATOM   4805  C  CD2 . PHE A 1 626  ? -66.320  51.296  14.612  1.00 179.49 ? 626  PHE A CD2 1 
ATOM   4806  C  CE1 . PHE A 1 626  ? -64.554  51.969  12.603  1.00 179.98 ? 626  PHE A CE1 1 
ATOM   4807  C  CE2 . PHE A 1 626  ? -66.638  51.019  13.292  1.00 182.45 ? 626  PHE A CE2 1 
ATOM   4808  C  CZ  . PHE A 1 626  ? -65.755  51.353  12.286  1.00 182.46 ? 626  PHE A CZ  1 
ATOM   4809  N  N   . LEU A 1 627  ? -67.710  52.505  16.853  1.00 150.34 ? 627  LEU A N   1 
ATOM   4810  C  CA  . LEU A 1 627  ? -69.058  52.314  16.332  1.00 147.12 ? 627  LEU A CA  1 
ATOM   4811  C  C   . LEU A 1 627  ? -70.037  53.455  16.613  1.00 146.46 ? 627  LEU A C   1 
ATOM   4812  O  O   . LEU A 1 627  ? -71.217  53.358  16.300  1.00 151.57 ? 627  LEU A O   1 
ATOM   4813  C  CB  . LEU A 1 627  ? -69.599  50.973  16.829  1.00 143.14 ? 627  LEU A CB  1 
ATOM   4814  C  CG  . LEU A 1 627  ? -71.081  50.731  17.074  1.00 140.64 ? 627  LEU A CG  1 
ATOM   4815  C  CD1 . LEU A 1 627  ? -71.370  49.257  16.985  1.00 141.41 ? 627  LEU A CD1 1 
ATOM   4816  C  CD2 . LEU A 1 627  ? -71.453  51.247  18.437  1.00 138.97 ? 627  LEU A CD2 1 
ATOM   4817  N  N   . GLU A 1 628  ? -69.550  54.544  17.188  1.00 143.02 ? 628  GLU A N   1 
ATOM   4818  C  CA  . GLU A 1 628  ? -70.403  55.698  17.441  1.00 142.46 ? 628  GLU A CA  1 
ATOM   4819  C  C   . GLU A 1 628  ? -69.683  56.953  17.004  1.00 139.90 ? 628  GLU A C   1 
ATOM   4820  O  O   . GLU A 1 628  ? -69.692  57.974  17.690  1.00 139.66 ? 628  GLU A O   1 
ATOM   4821  C  CB  . GLU A 1 628  ? -70.864  55.786  18.909  1.00 146.33 ? 628  GLU A CB  1 
ATOM   4822  C  CG  . GLU A 1 628  ? -69.833  56.324  19.934  1.00 174.36 ? 628  GLU A CG  1 
ATOM   4823  C  CD  . GLU A 1 628  ? -70.503  56.982  21.151  1.00 177.43 ? 628  GLU A CD  1 
ATOM   4824  O  OE1 . GLU A 1 628  ? -71.364  57.880  20.946  1.00 180.02 ? 628  GLU A OE1 1 
ATOM   4825  O  OE2 . GLU A 1 628  ? -70.161  56.611  22.304  1.00 176.61 ? 628  GLU A OE2 1 
ATOM   4826  N  N   . LYS A 1 629  ? -69.015  56.851  15.864  1.00 136.90 ? 629  LYS A N   1 
ATOM   4827  C  CA  . LYS A 1 629  ? -68.587  58.043  15.149  1.00 133.89 ? 629  LYS A CA  1 
ATOM   4828  C  C   . LYS A 1 629  ? -69.613  58.293  14.029  1.00 132.43 ? 629  LYS A C   1 
ATOM   4829  O  O   . LYS A 1 629  ? -69.467  59.160  13.163  1.00 127.88 ? 629  LYS A O   1 
ATOM   4830  C  CB  . LYS A 1 629  ? -67.146  57.896  14.663  1.00 133.09 ? 629  LYS A CB  1 
ATOM   4831  C  CG  . LYS A 1 629  ? -66.182  57.491  15.788  1.00 131.61 ? 629  LYS A CG  1 
ATOM   4832  C  CD  . LYS A 1 629  ? -66.551  58.140  17.156  1.00 155.83 ? 629  LYS A CD  1 
ATOM   4833  C  CE  . LYS A 1 629  ? -65.503  57.859  18.266  1.00 139.82 ? 629  LYS A CE  1 
ATOM   4834  N  NZ  . LYS A 1 629  ? -65.945  58.302  19.629  1.00 138.66 ? 629  LYS A NZ  1 
ATOM   4835  N  N   . SER A 1 630  ? -70.672  57.501  14.081  1.00 133.40 ? 630  SER A N   1 
ATOM   4836  C  CA  . SER A 1 630  ? -71.842  57.741  13.287  1.00 135.11 ? 630  SER A CA  1 
ATOM   4837  C  C   . SER A 1 630  ? -72.681  58.768  14.014  1.00 137.70 ? 630  SER A C   1 
ATOM   4838  O  O   . SER A 1 630  ? -73.780  59.091  13.590  1.00 143.94 ? 630  SER A O   1 
ATOM   4839  C  CB  . SER A 1 630  ? -72.620  56.454  13.144  1.00 133.70 ? 630  SER A CB  1 
ATOM   4840  O  OG  . SER A 1 630  ? -72.856  55.897  14.408  1.00 130.90 ? 630  SER A OG  1 
ATOM   4841  N  N   . ASP A 1 631  ? -72.178  59.249  15.143  1.00 135.38 ? 631  ASP A N   1 
ATOM   4842  C  CA  . ASP A 1 631  ? -72.776  60.405  15.808  1.00 136.72 ? 631  ASP A CA  1 
ATOM   4843  C  C   . ASP A 1 631  ? -72.415  61.598  14.944  1.00 136.83 ? 631  ASP A C   1 
ATOM   4844  O  O   . ASP A 1 631  ? -71.272  62.070  14.949  1.00 133.90 ? 631  ASP A O   1 
ATOM   4845  C  CB  . ASP A 1 631  ? -72.265  60.573  17.261  1.00 140.99 ? 631  ASP A CB  1 
ATOM   4846  C  CG  . ASP A 1 631  ? -73.061  61.621  18.069  1.00 154.39 ? 631  ASP A CG  1 
ATOM   4847  O  OD1 . ASP A 1 631  ? -72.755  62.824  17.919  1.00 156.90 ? 631  ASP A OD1 1 
ATOM   4848  O  OD2 . ASP A 1 631  ? -73.962  61.242  18.867  1.00 159.50 ? 631  ASP A OD2 1 
ATOM   4849  N  N   . LEU A 1 632  ? -73.403  62.058  14.183  1.00 138.74 ? 632  LEU A N   1 
ATOM   4850  C  CA  . LEU A 1 632  ? -73.227  63.139  13.232  1.00 138.54 ? 632  LEU A CA  1 
ATOM   4851  C  C   . LEU A 1 632  ? -72.859  64.435  13.957  1.00 135.93 ? 632  LEU A C   1 
ATOM   4852  O  O   . LEU A 1 632  ? -71.967  65.161  13.517  1.00 135.41 ? 632  LEU A O   1 
ATOM   4853  C  CB  . LEU A 1 632  ? -74.511  63.316  12.419  1.00 142.59 ? 632  LEU A CB  1 
ATOM   4854  C  CG  . LEU A 1 632  ? -75.272  62.027  12.071  1.00 143.54 ? 632  LEU A CG  1 
ATOM   4855  C  CD1 . LEU A 1 632  ? -76.741  62.291  11.680  1.00 144.26 ? 632  LEU A CD1 1 
ATOM   4856  C  CD2 . LEU A 1 632  ? -74.534  61.232  10.989  1.00 143.46 ? 632  LEU A CD2 1 
ATOM   4857  N  N   . GLY A 1 633  ? -73.536  64.696  15.080  1.00 130.14 ? 633  GLY A N   1 
ATOM   4858  C  CA  . GLY A 1 633  ? -73.353  65.906  15.877  1.00 125.38 ? 633  GLY A CA  1 
ATOM   4859  C  C   . GLY A 1 633  ? -71.939  66.266  16.315  1.00 117.68 ? 633  GLY A C   1 
ATOM   4860  O  O   . GLY A 1 633  ? -70.969  65.919  15.673  1.00 116.66 ? 633  GLY A O   1 
ATOM   4861  N  N   . CYS A 1 634  ? -71.826  66.986  17.417  1.00 117.52 ? 634  CYS A N   1 
ATOM   4862  C  CA  . CYS A 1 634  ? -70.536  67.436  17.897  1.00 117.00 ? 634  CYS A CA  1 
ATOM   4863  C  C   . CYS A 1 634  ? -70.682  68.328  19.141  1.00 119.00 ? 634  CYS A C   1 
ATOM   4864  O  O   . CYS A 1 634  ? -71.731  68.952  19.356  1.00 124.56 ? 634  CYS A O   1 
ATOM   4865  C  CB  . CYS A 1 634  ? -69.814  68.193  16.788  1.00 117.14 ? 634  CYS A CB  1 
ATOM   4866  S  SG  . CYS A 1 634  ? -68.091  68.554  17.158  1.00 151.88 ? 634  CYS A SG  1 
ATOM   4867  N  N   . GLY A 1 635  ? -69.631  68.393  19.958  1.00 115.82 ? 635  GLY A N   1 
ATOM   4868  C  CA  . GLY A 1 635  ? -69.631  69.255  21.136  1.00 114.10 ? 635  GLY A CA  1 
ATOM   4869  C  C   . GLY A 1 635  ? -70.311  68.729  22.402  1.00 115.58 ? 635  GLY A C   1 
ATOM   4870  O  O   . GLY A 1 635  ? -70.830  67.608  22.426  1.00 115.10 ? 635  GLY A O   1 
ATOM   4871  N  N   . ALA A 1 636  ? -70.291  69.537  23.465  1.00 117.50 ? 636  ALA A N   1 
ATOM   4872  C  CA  . ALA A 1 636  ? -70.909  69.177  24.736  1.00 118.39 ? 636  ALA A CA  1 
ATOM   4873  C  C   . ALA A 1 636  ? -72.380  69.469  24.638  1.00 118.38 ? 636  ALA A C   1 
ATOM   4874  O  O   . ALA A 1 636  ? -73.191  68.962  25.409  1.00 119.94 ? 636  ALA A O   1 
ATOM   4875  C  CB  . ALA A 1 636  ? -70.299  69.968  25.849  1.00 121.57 ? 636  ALA A CB  1 
ATOM   4876  N  N   . GLY A 1 637  ? -72.701  70.314  23.670  1.00 117.08 ? 637  GLY A N   1 
ATOM   4877  C  CA  . GLY A 1 637  ? -74.071  70.635  23.338  1.00 120.46 ? 637  GLY A CA  1 
ATOM   4878  C  C   . GLY A 1 637  ? -74.170  72.071  22.858  1.00 126.48 ? 637  GLY A C   1 
ATOM   4879  O  O   . GLY A 1 637  ? -73.144  72.768  22.741  1.00 122.98 ? 637  GLY A O   1 
ATOM   4880  N  N   . GLY A 1 638  ? -75.402  72.491  22.564  1.00 131.34 ? 638  GLY A N   1 
ATOM   4881  C  CA  . GLY A 1 638  ? -75.742  73.886  22.380  1.00 133.90 ? 638  GLY A CA  1 
ATOM   4882  C  C   . GLY A 1 638  ? -75.030  74.576  21.249  1.00 131.69 ? 638  GLY A C   1 
ATOM   4883  O  O   . GLY A 1 638  ? -73.812  74.543  21.145  1.00 134.31 ? 638  GLY A O   1 
ATOM   4884  N  N   . GLY A 1 639  ? -75.815  75.215  20.396  1.00 128.57 ? 639  GLY A N   1 
ATOM   4885  C  CA  . GLY A 1 639  ? -75.281  75.957  19.271  1.00 125.25 ? 639  GLY A CA  1 
ATOM   4886  C  C   . GLY A 1 639  ? -74.931  77.419  19.526  1.00 126.21 ? 639  GLY A C   1 
ATOM   4887  O  O   . GLY A 1 639  ? -74.216  77.750  20.481  1.00 121.85 ? 639  GLY A O   1 
ATOM   4888  N  N   . LEU A 1 640  ? -75.470  78.291  18.670  1.00 131.04 ? 640  LEU A N   1 
ATOM   4889  C  CA  . LEU A 1 640  ? -74.988  79.660  18.505  1.00 131.38 ? 640  LEU A CA  1 
ATOM   4890  C  C   . LEU A 1 640  ? -76.063  80.478  17.777  1.00 131.88 ? 640  LEU A C   1 
ATOM   4891  O  O   . LEU A 1 640  ? -76.173  81.694  17.940  1.00 131.66 ? 640  LEU A O   1 
ATOM   4892  C  CB  . LEU A 1 640  ? -73.689  79.590  17.706  1.00 129.01 ? 640  LEU A CB  1 
ATOM   4893  C  CG  . LEU A 1 640  ? -72.824  80.765  17.310  1.00 99.99  ? 640  LEU A CG  1 
ATOM   4894  C  CD1 . LEU A 1 640  ? -73.234  82.052  18.050  1.00 100.37 ? 640  LEU A CD1 1 
ATOM   4895  C  CD2 . LEU A 1 640  ? -71.367  80.346  17.519  1.00 98.29  ? 640  LEU A CD2 1 
ATOM   4896  N  N   . ASN A 1 641  ? -76.840  79.756  16.975  1.00 132.06 ? 641  ASN A N   1 
ATOM   4897  C  CA  . ASN A 1 641  ? -78.091  80.183  16.380  1.00 133.01 ? 641  ASN A CA  1 
ATOM   4898  C  C   . ASN A 1 641  ? -78.945  78.968  16.610  1.00 135.15 ? 641  ASN A C   1 
ATOM   4899  O  O   . ASN A 1 641  ? -78.410  77.889  16.830  1.00 135.35 ? 641  ASN A O   1 
ATOM   4900  C  CB  . ASN A 1 641  ? -77.973  80.320  14.864  1.00 135.88 ? 641  ASN A CB  1 
ATOM   4901  C  CG  . ASN A 1 641  ? -76.657  80.926  14.417  1.00 138.18 ? 641  ASN A CG  1 
ATOM   4902  O  OD1 . ASN A 1 641  ? -76.282  82.009  14.871  1.00 139.02 ? 641  ASN A OD1 1 
ATOM   4903  N  ND2 . ASN A 1 641  ? -75.957  80.241  13.492  1.00 139.24 ? 641  ASN A ND2 1 
ATOM   4904  N  N   . ASN A 1 642  ? -80.261  79.106  16.532  1.00 139.14 ? 642  ASN A N   1 
ATOM   4905  C  CA  . ASN A 1 642  ? -81.124  77.930  16.584  1.00 140.69 ? 642  ASN A CA  1 
ATOM   4906  C  C   . ASN A 1 642  ? -80.688  76.994  15.462  1.00 138.39 ? 642  ASN A C   1 
ATOM   4907  O  O   . ASN A 1 642  ? -80.881  75.771  15.510  1.00 134.54 ? 642  ASN A O   1 
ATOM   4908  C  CB  . ASN A 1 642  ? -82.593  78.332  16.425  1.00 148.37 ? 642  ASN A CB  1 
ATOM   4909  C  CG  . ASN A 1 642  ? -83.522  77.138  16.374  1.00 153.95 ? 642  ASN A CG  1 
ATOM   4910  O  OD1 . ASN A 1 642  ? -84.466  77.101  15.591  1.00 158.50 ? 642  ASN A OD1 1 
ATOM   4911  N  ND2 . ASN A 1 642  ? -83.248  76.146  17.202  1.00 153.85 ? 642  ASN A ND2 1 
ATOM   4912  N  N   . ALA A 1 643  ? -80.090  77.590  14.442  1.00 140.18 ? 643  ALA A N   1 
ATOM   4913  C  CA  . ALA A 1 643  ? -79.457  76.800  13.419  1.00 140.83 ? 643  ALA A CA  1 
ATOM   4914  C  C   . ALA A 1 643  ? -78.342  76.015  14.078  1.00 133.20 ? 643  ALA A C   1 
ATOM   4915  O  O   . ALA A 1 643  ? -78.535  74.856  14.437  1.00 129.38 ? 643  ALA A O   1 
ATOM   4916  C  CB  . ALA A 1 643  ? -78.918  77.692  12.323  1.00 146.32 ? 643  ALA A CB  1 
ATOM   4917  N  N   . ASN A 1 644  ? -77.195  76.670  14.257  1.00 129.78 ? 644  ASN A N   1 
ATOM   4918  C  CA  . ASN A 1 644  ? -76.024  76.054  14.878  1.00 127.33 ? 644  ASN A CA  1 
ATOM   4919  C  C   . ASN A 1 644  ? -76.461  74.981  15.871  1.00 128.97 ? 644  ASN A C   1 
ATOM   4920  O  O   . ASN A 1 644  ? -76.172  73.807  15.659  1.00 131.87 ? 644  ASN A O   1 
ATOM   4921  C  CB  . ASN A 1 644  ? -75.153  77.117  15.573  1.00 123.58 ? 644  ASN A CB  1 
ATOM   4922  C  CG  . ASN A 1 644  ? -73.661  76.741  15.628  1.00 121.04 ? 644  ASN A CG  1 
ATOM   4923  O  OD1 . ASN A 1 644  ? -72.814  77.505  16.125  1.00 118.86 ? 644  ASN A OD1 1 
ATOM   4924  N  ND2 . ASN A 1 644  ? -73.338  75.566  15.108  1.00 121.61 ? 644  ASN A ND2 1 
ATOM   4925  N  N   . VAL A 1 645  ? -77.183  75.382  16.925  1.00 129.19 ? 645  VAL A N   1 
ATOM   4926  C  CA  . VAL A 1 645  ? -77.750  74.450  17.921  1.00 128.93 ? 645  VAL A CA  1 
ATOM   4927  C  C   . VAL A 1 645  ? -78.278  73.153  17.300  1.00 130.42 ? 645  VAL A C   1 
ATOM   4928  O  O   . VAL A 1 645  ? -77.898  72.059  17.713  1.00 128.86 ? 645  VAL A O   1 
ATOM   4929  C  CB  . VAL A 1 645  ? -78.943  75.068  18.685  1.00 132.26 ? 645  VAL A CB  1 
ATOM   4930  C  CG1 . VAL A 1 645  ? -79.542  74.042  19.628  1.00 133.20 ? 645  VAL A CG1 1 
ATOM   4931  C  CG2 . VAL A 1 645  ? -78.534  76.313  19.433  1.00 130.92 ? 645  VAL A CG2 1 
ATOM   4932  N  N   . PHE A 1 646  ? -79.171  73.289  16.321  1.00 131.54 ? 646  PHE A N   1 
ATOM   4933  C  CA  . PHE A 1 646  ? -79.679  72.150  15.580  1.00 130.05 ? 646  PHE A CA  1 
ATOM   4934  C  C   . PHE A 1 646  ? -78.583  71.458  14.782  1.00 131.11 ? 646  PHE A C   1 
ATOM   4935  O  O   . PHE A 1 646  ? -78.603  70.237  14.636  1.00 130.80 ? 646  PHE A O   1 
ATOM   4936  C  CB  . PHE A 1 646  ? -80.787  72.597  14.641  1.00 129.93 ? 646  PHE A CB  1 
ATOM   4937  C  CG  . PHE A 1 646  ? -82.157  72.322  15.163  1.00 127.30 ? 646  PHE A CG  1 
ATOM   4938  C  CD1 . PHE A 1 646  ? -82.973  73.352  15.567  1.00 125.06 ? 646  PHE A CD1 1 
ATOM   4939  C  CD2 . PHE A 1 646  ? -82.624  71.022  15.267  1.00 125.32 ? 646  PHE A CD2 1 
ATOM   4940  C  CE1 . PHE A 1 646  ? -84.229  73.090  16.056  1.00 125.21 ? 646  PHE A CE1 1 
ATOM   4941  C  CE2 . PHE A 1 646  ? -83.884  70.755  15.758  1.00 125.09 ? 646  PHE A CE2 1 
ATOM   4942  C  CZ  . PHE A 1 646  ? -84.682  71.785  16.153  1.00 125.22 ? 646  PHE A CZ  1 
ATOM   4943  N  N   . HIS A 1 647  ? -77.637  72.245  14.265  1.00 130.31 ? 647  HIS A N   1 
ATOM   4944  C  CA  . HIS A 1 647  ? -76.525  71.723  13.464  1.00 131.53 ? 647  HIS A CA  1 
ATOM   4945  C  C   . HIS A 1 647  ? -75.682  70.726  14.259  1.00 120.46 ? 647  HIS A C   1 
ATOM   4946  O  O   . HIS A 1 647  ? -75.775  69.525  14.070  1.00 117.85 ? 647  HIS A O   1 
ATOM   4947  C  CB  . HIS A 1 647  ? -75.642  72.874  12.944  1.00 140.92 ? 647  HIS A CB  1 
ATOM   4948  C  CG  . HIS A 1 647  ? -74.837  72.525  11.724  1.00 152.09 ? 647  HIS A CG  1 
ATOM   4949  N  ND1 . HIS A 1 647  ? -74.187  71.315  11.573  1.00 155.35 ? 647  HIS A ND1 1 
ATOM   4950  C  CD2 . HIS A 1 647  ? -74.564  73.237  10.603  1.00 158.38 ? 647  HIS A CD2 1 
ATOM   4951  C  CE1 . HIS A 1 647  ? -73.564  71.288  10.406  1.00 157.63 ? 647  HIS A CE1 1 
ATOM   4952  N  NE2 . HIS A 1 647  ? -73.773  72.443  9.800   1.00 159.91 ? 647  HIS A NE2 1 
ATOM   4953  N  N   . LEU A 1 648  ? -74.861  71.246  15.155  1.00 115.35 ? 648  LEU A N   1 
ATOM   4954  C  CA  . LEU A 1 648  ? -74.065  70.430  16.062  1.00 111.62 ? 648  LEU A CA  1 
ATOM   4955  C  C   . LEU A 1 648  ? -74.841  69.263  16.683  1.00 109.71 ? 648  LEU A C   1 
ATOM   4956  O  O   . LEU A 1 648  ? -74.266  68.277  17.133  1.00 108.97 ? 648  LEU A O   1 
ATOM   4957  C  CB  . LEU A 1 648  ? -73.488  71.322  17.157  1.00 107.53 ? 648  LEU A CB  1 
ATOM   4958  C  CG  . LEU A 1 648  ? -72.380  72.243  16.656  1.00 103.98 ? 648  LEU A CG  1 
ATOM   4959  C  CD1 . LEU A 1 648  ? -72.348  73.542  17.432  1.00 102.40 ? 648  LEU A CD1 1 
ATOM   4960  C  CD2 . LEU A 1 648  ? -71.064  71.526  16.769  1.00 101.68 ? 648  LEU A CD2 1 
ATOM   4961  N  N   . ALA A 1 649  ? -76.154  69.374  16.714  1.00 111.16 ? 649  ALA A N   1 
ATOM   4962  C  CA  . ALA A 1 649  ? -76.973  68.271  17.170  1.00 109.89 ? 649  ALA A CA  1 
ATOM   4963  C  C   . ALA A 1 649  ? -76.812  67.093  16.243  1.00 107.66 ? 649  ALA A C   1 
ATOM   4964  O  O   . ALA A 1 649  ? -77.102  65.971  16.610  1.00 106.00 ? 649  ALA A O   1 
ATOM   4965  C  CB  . ALA A 1 649  ? -78.422  68.687  17.173  1.00 115.13 ? 649  ALA A CB  1 
ATOM   4966  N  N   . GLY A 1 650  ? -76.361  67.362  15.028  1.00 108.96 ? 650  GLY A N   1 
ATOM   4967  C  CA  . GLY A 1 650  ? -76.323  66.353  13.981  1.00 111.11 ? 650  GLY A CA  1 
ATOM   4968  C  C   . GLY A 1 650  ? -77.461  66.484  12.976  1.00 114.95 ? 650  GLY A C   1 
ATOM   4969  O  O   . GLY A 1 650  ? -77.611  65.681  12.033  1.00 113.93 ? 650  GLY A O   1 
ATOM   4970  N  N   . LEU A 1 651  ? -78.262  67.520  13.181  1.00 116.47 ? 651  LEU A N   1 
ATOM   4971  C  CA  . LEU A 1 651  ? -79.474  67.709  12.413  1.00 121.95 ? 651  LEU A CA  1 
ATOM   4972  C  C   . LEU A 1 651  ? -79.407  68.882  11.452  1.00 124.25 ? 651  LEU A C   1 
ATOM   4973  O  O   . LEU A 1 651  ? -78.683  69.851  11.670  1.00 122.85 ? 651  LEU A O   1 
ATOM   4974  C  CB  . LEU A 1 651  ? -80.640  67.949  13.374  1.00 122.23 ? 651  LEU A CB  1 
ATOM   4975  C  CG  . LEU A 1 651  ? -81.086  66.761  14.229  1.00 121.24 ? 651  LEU A CG  1 
ATOM   4976  C  CD1 . LEU A 1 651  ? -82.100  67.213  15.242  1.00 121.63 ? 651  LEU A CD1 1 
ATOM   4977  C  CD2 . LEU A 1 651  ? -81.668  65.666  13.371  1.00 123.47 ? 651  LEU A CD2 1 
ATOM   4978  N  N   . THR A 1 652  ? -80.182  68.787  10.382  1.00 127.17 ? 652  THR A N   1 
ATOM   4979  C  CA  . THR A 1 652  ? -80.748  69.994  9.803   1.00 127.37 ? 652  THR A CA  1 
ATOM   4980  C  C   . THR A 1 652  ? -82.261  69.810  9.656   1.00 126.42 ? 652  THR A C   1 
ATOM   4981  O  O   . THR A 1 652  ? -82.774  68.709  9.458   1.00 125.52 ? 652  THR A O   1 
ATOM   4982  C  CB  . THR A 1 652  ? -79.996  70.535  8.562   1.00 126.05 ? 652  THR A CB  1 
ATOM   4983  O  OG1 . THR A 1 652  ? -80.109  71.964  8.545   1.00 126.24 ? 652  THR A OG1 1 
ATOM   4984  C  CG2 . THR A 1 652  ? -80.534  69.948  7.272   1.00 128.72 ? 652  THR A CG2 1 
ATOM   4985  N  N   . PHE A 1 653  ? -82.973  70.896  9.863   1.00 128.65 ? 653  PHE A N   1 
ATOM   4986  C  CA  . PHE A 1 653  ? -84.384  70.781  10.116  1.00 134.27 ? 653  PHE A CA  1 
ATOM   4987  C  C   . PHE A 1 653  ? -85.173  71.497  9.062   1.00 140.28 ? 653  PHE A C   1 
ATOM   4988  O  O   . PHE A 1 653  ? -84.614  72.191  8.222   1.00 137.78 ? 653  PHE A O   1 
ATOM   4989  C  CB  . PHE A 1 653  ? -84.716  71.347  11.482  1.00 136.25 ? 653  PHE A CB  1 
ATOM   4990  C  CG  . PHE A 1 653  ? -84.321  72.792  11.659  1.00 139.60 ? 653  PHE A CG  1 
ATOM   4991  C  CD1 . PHE A 1 653  ? -85.282  73.761  11.914  1.00 142.93 ? 653  PHE A CD1 1 
ATOM   4992  C  CD2 . PHE A 1 653  ? -82.991  73.182  11.594  1.00 138.20 ? 653  PHE A CD2 1 
ATOM   4993  C  CE1 . PHE A 1 653  ? -84.918  75.089  12.104  1.00 142.66 ? 653  PHE A CE1 1 
ATOM   4994  C  CE2 . PHE A 1 653  ? -82.622  74.510  11.779  1.00 137.96 ? 653  PHE A CE2 1 
ATOM   4995  C  CZ  . PHE A 1 653  ? -83.583  75.462  12.036  1.00 139.97 ? 653  PHE A CZ  1 
ATOM   4996  N  N   . LEU A 1 654  ? -86.487  71.357  9.153   1.00 149.11 ? 654  LEU A N   1 
ATOM   4997  C  CA  . LEU A 1 654  ? -87.371  71.701  8.069   1.00 157.76 ? 654  LEU A CA  1 
ATOM   4998  C  C   . LEU A 1 654  ? -88.550  72.492  8.582   1.00 169.79 ? 654  LEU A C   1 
ATOM   4999  O  O   . LEU A 1 654  ? -89.622  71.928  8.761   1.00 176.57 ? 654  LEU A O   1 
ATOM   5000  C  CB  . LEU A 1 654  ? -87.906  70.415  7.500   1.00 154.96 ? 654  LEU A CB  1 
ATOM   5001  C  CG  . LEU A 1 654  ? -88.199  70.571  6.042   1.00 155.37 ? 654  LEU A CG  1 
ATOM   5002  C  CD1 . LEU A 1 654  ? -87.333  71.700  5.511   1.00 153.37 ? 654  LEU A CD1 1 
ATOM   5003  C  CD2 . LEU A 1 654  ? -87.847  69.260  5.423   1.00 155.66 ? 654  LEU A CD2 1 
ATOM   5004  N  N   . THR A 1 655  ? -88.366  73.799  8.781   1.00 173.25 ? 655  THR A N   1 
ATOM   5005  C  CA  . THR A 1 655  ? -89.311  74.625  9.553   1.00 178.64 ? 655  THR A CA  1 
ATOM   5006  C  C   . THR A 1 655  ? -89.419  76.058  9.042   1.00 187.48 ? 655  THR A C   1 
ATOM   5007  O  O   . THR A 1 655  ? -88.543  76.889  9.286   1.00 183.55 ? 655  THR A O   1 
ATOM   5008  C  CB  . THR A 1 655  ? -88.872  74.729  11.045  1.00 201.87 ? 655  THR A CB  1 
ATOM   5009  O  OG1 . THR A 1 655  ? -89.007  73.459  11.698  1.00 199.52 ? 655  THR A OG1 1 
ATOM   5010  C  CG2 . THR A 1 655  ? -89.699  75.774  11.779  1.00 202.89 ? 655  THR A CG2 1 
ATOM   5011  N  N   . ASN A 1 656  ? -90.501  76.374  8.356   1.00 200.70 ? 656  ASN A N   1 
ATOM   5012  C  CA  . ASN A 1 656  ? -90.587  77.719  7.831   1.00 212.22 ? 656  ASN A CA  1 
ATOM   5013  C  C   . ASN A 1 656  ? -90.937  78.731  8.903   1.00 212.66 ? 656  ASN A C   1 
ATOM   5014  O  O   . ASN A 1 656  ? -92.066  78.798  9.400   1.00 215.78 ? 656  ASN A O   1 
ATOM   5015  C  CB  . ASN A 1 656  ? -91.463  77.815  6.578   1.00 220.60 ? 656  ASN A CB  1 
ATOM   5016  C  CG  . ASN A 1 656  ? -90.693  77.469  5.296   1.00 219.99 ? 656  ASN A CG  1 
ATOM   5017  O  OD1 . ASN A 1 656  ? -91.288  77.254  4.239   1.00 222.99 ? 656  ASN A OD1 1 
ATOM   5018  N  ND2 . ASN A 1 656  ? -89.365  77.415  5.394   1.00 215.27 ? 656  ASN A ND2 1 
ATOM   5019  N  N   . ALA A 1 657  ? -89.906  79.495  9.242   1.00 209.58 ? 657  ALA A N   1 
ATOM   5020  C  CA  . ALA A 1 657  ? -89.914  80.496  10.291  1.00 207.11 ? 657  ALA A CA  1 
ATOM   5021  C  C   . ALA A 1 657  ? -88.463  80.919  10.442  1.00 203.53 ? 657  ALA A C   1 
ATOM   5022  O  O   . ALA A 1 657  ? -88.061  82.004  10.004  1.00 203.79 ? 657  ALA A O   1 
ATOM   5023  C  CB  . ALA A 1 657  ? -90.419  79.899  11.601  1.00 204.27 ? 657  ALA A CB  1 
ATOM   5024  N  N   . ASN A 1 658  ? -87.675  80.035  11.048  1.00 199.84 ? 658  ASN A N   1 
ATOM   5025  C  CA  . ASN A 1 658  ? -86.239  80.238  11.159  1.00 195.88 ? 658  ASN A CA  1 
ATOM   5026  C  C   . ASN A 1 658  ? -85.456  79.624  10.012  1.00 193.47 ? 658  ASN A C   1 
ATOM   5027  O  O   . ASN A 1 658  ? -85.814  78.567  9.495   1.00 193.67 ? 658  ASN A O   1 
ATOM   5028  C  CB  . ASN A 1 658  ? -85.723  79.689  12.483  1.00 190.94 ? 658  ASN A CB  1 
ATOM   5029  C  CG  . ASN A 1 658  ? -85.759  80.714  13.575  1.00 186.72 ? 658  ASN A CG  1 
ATOM   5030  O  OD1 . ASN A 1 658  ? -85.128  80.550  14.620  1.00 183.04 ? 658  ASN A OD1 1 
ATOM   5031  N  ND2 . ASN A 1 658  ? -86.492  81.795  13.339  1.00 187.23 ? 658  ASN A ND2 1 
ATOM   5032  N  N   . ALA A 1 659  ? -84.381  80.295  9.624   1.00 191.09 ? 659  ALA A N   1 
ATOM   5033  C  CA  . ALA A 1 659  ? -83.500  79.761  8.609   1.00 190.56 ? 659  ALA A CA  1 
ATOM   5034  C  C   . ALA A 1 659  ? -82.972  78.419  9.082   1.00 187.46 ? 659  ALA A C   1 
ATOM   5035  O  O   . ALA A 1 659  ? -82.122  78.364  9.973   1.00 186.35 ? 659  ALA A O   1 
ATOM   5036  C  CB  . ALA A 1 659  ? -82.355  80.717  8.362   1.00 189.96 ? 659  ALA A CB  1 
ATOM   5037  N  N   . ASP A 1 660  ? -83.476  77.333  8.496   1.00 187.98 ? 660  ASP A N   1 
ATOM   5038  C  CA  . ASP A 1 660  ? -83.013  75.987  8.873   1.00 184.96 ? 660  ASP A CA  1 
ATOM   5039  C  C   . ASP A 1 660  ? -81.579  75.702  8.412   1.00 181.37 ? 660  ASP A C   1 
ATOM   5040  O  O   . ASP A 1 660  ? -81.080  74.578  8.538   1.00 176.93 ? 660  ASP A O   1 
ATOM   5041  C  CB  . ASP A 1 660  ? -83.998  74.885  8.427   1.00 189.51 ? 660  ASP A CB  1 
ATOM   5042  C  CG  . ASP A 1 660  ? -84.406  74.998  6.964   1.00 196.72 ? 660  ASP A CG  1 
ATOM   5043  O  OD1 . ASP A 1 660  ? -83.508  75.132  6.104   1.00 197.78 ? 660  ASP A OD1 1 
ATOM   5044  O  OD2 . ASP A 1 660  ? -85.624  74.922  6.670   1.00 200.62 ? 660  ASP A OD2 1 
ATOM   5045  N  N   . ASP A 1 661  ? -80.934  76.760  7.923   1.00 181.75 ? 661  ASP A N   1 
ATOM   5046  C  CA  . ASP A 1 661  ? -79.635  76.710  7.263   1.00 179.00 ? 661  ASP A CA  1 
ATOM   5047  C  C   . ASP A 1 661  ? -78.525  75.985  8.042   1.00 178.45 ? 661  ASP A C   1 
ATOM   5048  O  O   . ASP A 1 661  ? -78.716  75.554  9.184   1.00 177.67 ? 661  ASP A O   1 
ATOM   5049  C  CB  . ASP A 1 661  ? -79.198  78.128  6.903   1.00 173.24 ? 661  ASP A CB  1 
ATOM   5050  C  CG  . ASP A 1 661  ? -78.331  78.749  7.966   1.00 161.81 ? 661  ASP A CG  1 
ATOM   5051  O  OD1 . ASP A 1 661  ? -78.849  79.509  8.814   1.00 156.60 ? 661  ASP A OD1 1 
ATOM   5052  O  OD2 . ASP A 1 661  ? -77.120  78.458  7.951   1.00 158.43 ? 661  ASP A OD2 1 
ATOM   5053  N  N   . SER A 1 662  ? -77.365  75.859  7.403   1.00 178.97 ? 662  SER A N   1 
ATOM   5054  C  CA  . SER A 1 662  ? -76.278  75.027  7.909   1.00 179.17 ? 662  SER A CA  1 
ATOM   5055  C  C   . SER A 1 662  ? -74.958  75.484  7.298   1.00 182.54 ? 662  SER A C   1 
ATOM   5056  O  O   . SER A 1 662  ? -74.277  74.729  6.588   1.00 178.89 ? 662  SER A O   1 
ATOM   5057  C  CB  . SER A 1 662  ? -76.535  73.542  7.587   1.00 181.25 ? 662  SER A CB  1 
ATOM   5058  O  OG  . SER A 1 662  ? -76.117  73.186  6.267   1.00 183.46 ? 662  SER A OG  1 
ATOM   5059  N  N   . GLN A 1 663  ? -74.608  76.729  7.601   1.00 189.23 ? 663  GLN A N   1 
ATOM   5060  C  CA  . GLN A 1 663  ? -73.488  77.418  6.966   1.00 195.65 ? 663  GLN A CA  1 
ATOM   5061  C  C   . GLN A 1 663  ? -72.501  76.540  6.193   1.00 205.14 ? 663  GLN A C   1 
ATOM   5062  O  O   . GLN A 1 663  ? -71.649  75.880  6.774   1.00 202.47 ? 663  GLN A O   1 
ATOM   5063  C  CB  . GLN A 1 663  ? -72.761  78.285  7.990   1.00 188.42 ? 663  GLN A CB  1 
ATOM   5064  C  CG  . GLN A 1 663  ? -73.693  79.261  8.664   1.00 182.99 ? 663  GLN A CG  1 
ATOM   5065  C  CD  . GLN A 1 663  ? -74.577  79.996  7.670   1.00 180.88 ? 663  GLN A CD  1 
ATOM   5066  O  OE1 . GLN A 1 663  ? -74.258  80.074  6.488   1.00 180.84 ? 663  GLN A OE1 1 
ATOM   5067  N  NE2 . GLN A 1 663  ? -75.689  80.549  8.150   1.00 179.90 ? 663  GLN A NE2 1 
ATOM   5068  N  N   . GLU A 1 664  ? -72.662  76.554  4.871   1.00 217.12 ? 664  GLU A N   1 
ATOM   5069  C  CA  . GLU A 1 664  ? -71.759  75.941  3.879   1.00 228.56 ? 664  GLU A CA  1 
ATOM   5070  C  C   . GLU A 1 664  ? -71.016  74.660  4.264   1.00 235.28 ? 664  GLU A C   1 
ATOM   5071  O  O   . GLU A 1 664  ? -70.455  74.561  5.349   1.00 232.35 ? 664  GLU A O   1 
ATOM   5072  C  CB  . GLU A 1 664  ? -70.769  76.982  3.318   1.00 231.14 ? 664  GLU A CB  1 
ATOM   5073  C  CG  . GLU A 1 664  ? -69.929  77.722  4.354   1.00 231.64 ? 664  GLU A CG  1 
ATOM   5074  C  CD  . GLU A 1 664  ? -68.972  78.719  3.722   1.00 236.49 ? 664  GLU A CD  1 
ATOM   5075  O  OE1 . GLU A 1 664  ? -68.106  78.294  2.930   1.00 238.40 ? 664  GLU A OE1 1 
ATOM   5076  O  OE2 . GLU A 1 664  ? -69.082  79.927  4.021   1.00 238.55 ? 664  GLU A OE2 1 
ATOM   5077  N  N   . ASN A 1 665  ? -70.998  73.686  3.356   1.00 246.52 ? 665  ASN A N   1 
ATOM   5078  C  CA  . ASN A 1 665  ? -70.189  72.505  3.582   1.00 252.74 ? 665  ASN A CA  1 
ATOM   5079  C  C   . ASN A 1 665  ? -70.632  71.915  4.918   1.00 256.79 ? 665  ASN A C   1 
ATOM   5080  O  O   . ASN A 1 665  ? -71.785  72.106  5.310   1.00 259.68 ? 665  ASN A O   1 
ATOM   5081  C  CB  . ASN A 1 665  ? -68.721  72.933  3.597   1.00 252.31 ? 665  ASN A CB  1 
ATOM   5082  C  CG  . ASN A 1 665  ? -67.765  71.772  3.688   1.00 249.48 ? 665  ASN A CG  1 
ATOM   5083  O  OD1 . ASN A 1 665  ? -67.384  71.360  4.781   1.00 246.41 ? 665  ASN A OD1 1 
ATOM   5084  N  ND2 . ASN A 1 665  ? -67.339  71.258  2.539   1.00 250.77 ? 665  ASN A ND2 1 
ATOM   5085  N  N   . ASP A 1 666  ? -69.747  71.210  5.625   1.00 258.34 ? 666  ASP A N   1 
ATOM   5086  C  CA  . ASP A 1 666  ? -70.070  70.792  6.999   1.00 259.54 ? 666  ASP A CA  1 
ATOM   5087  C  C   . ASP A 1 666  ? -68.925  70.379  7.944   1.00 252.26 ? 666  ASP A C   1 
ATOM   5088  O  O   . ASP A 1 666  ? -68.371  69.288  7.842   1.00 250.01 ? 666  ASP A O   1 
ATOM   5089  C  CB  . ASP A 1 666  ? -71.190  69.734  7.017   1.00 269.27 ? 666  ASP A CB  1 
ATOM   5090  C  CG  . ASP A 1 666  ? -70.757  68.396  6.434   1.00 277.53 ? 666  ASP A CG  1 
ATOM   5091  O  OD1 . ASP A 1 666  ? -69.805  68.362  5.626   1.00 280.36 ? 666  ASP A OD1 1 
ATOM   5092  O  OD2 . ASP A 1 666  ? -71.383  67.371  6.779   1.00 280.27 ? 666  ASP A OD2 1 
ATOM   5093  N  N   . GLU A 1 667  ? -68.575  71.300  8.837   1.00 246.67 ? 667  GLU A N   1 
ATOM   5094  C  CA  . GLU A 1 667  ? -68.009  71.004  10.156  1.00 239.12 ? 667  GLU A CA  1 
ATOM   5095  C  C   . GLU A 1 667  ? -67.248  69.698  10.362  1.00 237.36 ? 667  GLU A C   1 
ATOM   5096  O  O   . GLU A 1 667  ? -67.769  68.800  11.021  1.00 237.27 ? 667  GLU A O   1 
ATOM   5097  C  CB  . GLU A 1 667  ? -69.164  70.981  11.152  1.00 231.51 ? 667  GLU A CB  1 
ATOM   5098  C  CG  . GLU A 1 667  ? -70.468  71.480  10.560  1.00 226.76 ? 667  GLU A CG  1 
ATOM   5099  C  CD  . GLU A 1 667  ? -70.422  72.957  10.270  1.00 222.03 ? 667  GLU A CD  1 
ATOM   5100  O  OE1 . GLU A 1 667  ? -69.310  73.494  10.105  1.00 219.31 ? 667  GLU A OE1 1 
ATOM   5101  O  OE2 . GLU A 1 667  ? -71.493  73.588  10.214  1.00 221.63 ? 667  GLU A OE2 1 
ATOM   5102  N  N   . PRO A 1 668  ? -66.011  69.590  9.848   1.00 235.52 ? 668  PRO A N   1 
ATOM   5103  C  CA  . PRO A 1 668  ? -65.239  68.358  10.089  1.00 233.48 ? 668  PRO A CA  1 
ATOM   5104  C  C   . PRO A 1 668  ? -64.920  68.071  11.574  1.00 230.84 ? 668  PRO A C   1 
ATOM   5105  O  O   . PRO A 1 668  ? -63.858  67.514  11.864  1.00 229.13 ? 668  PRO A O   1 
ATOM   5106  C  CB  . PRO A 1 668  ? -63.952  68.590  9.288   1.00 232.69 ? 668  PRO A CB  1 
ATOM   5107  C  CG  . PRO A 1 668  ? -64.338  69.574  8.226   1.00 235.10 ? 668  PRO A CG  1 
ATOM   5108  C  CD  . PRO A 1 668  ? -65.359  70.472  8.864   1.00 236.01 ? 668  PRO A CD  1 
ATOM   5109  N  N   . CYS A 1 669  ? -65.840  68.428  12.475  1.00 232.23 ? 669  CYS A N   1 
ATOM   5110  C  CA  . CYS A 1 669  ? -65.682  68.275  13.928  1.00 230.93 ? 669  CYS A CA  1 
ATOM   5111  C  C   . CYS A 1 669  ? -64.674  67.207  14.350  1.00 229.72 ? 669  CYS A C   1 
ATOM   5112  O  O   . CYS A 1 669  ? -64.553  66.159  13.712  1.00 229.92 ? 669  CYS A O   1 
ATOM   5113  C  CB  . CYS A 1 669  ? -67.040  67.999  14.590  1.00 231.82 ? 669  CYS A CB  1 
ATOM   5114  S  SG  . CYS A 1 669  ? -66.954  67.176  16.211  1.00 279.99 ? 669  CYS A SG  1 
ATOM   5115  N  N   . LYS A 1 670  ? -63.968  67.480  15.444  1.00 227.99 ? 670  LYS A N   1 
ATOM   5116  C  CA  . LYS A 1 670  ? -62.888  66.619  15.903  1.00 225.28 ? 670  LYS A CA  1 
ATOM   5117  C  C   . LYS A 1 670  ? -62.611  66.826  17.392  1.00 220.71 ? 670  LYS A C   1 
ATOM   5118  O  O   . LYS A 1 670  ? -61.943  67.784  17.778  1.00 219.56 ? 670  LYS A O   1 
ATOM   5119  C  CB  . LYS A 1 670  ? -61.622  66.908  15.090  1.00 226.69 ? 670  LYS A CB  1 
ATOM   5120  C  CG  . LYS A 1 670  ? -60.414  66.090  15.494  1.00 226.42 ? 670  LYS A CG  1 
ATOM   5121  C  CD  . LYS A 1 670  ? -60.665  64.606  15.285  1.00 227.26 ? 670  LYS A CD  1 
ATOM   5122  C  CE  . LYS A 1 670  ? -59.507  63.752  15.803  1.00 226.35 ? 670  LYS A CE  1 
ATOM   5123  N  NZ  . LYS A 1 670  ? -58.256  63.920  15.013  1.00 226.65 ? 670  LYS A NZ  1 
ATOM   5124  N  N   . GLU A 1 671  ? -63.148  65.935  18.221  1.00 218.77 ? 671  GLU A N   1 
ATOM   5125  C  CA  . GLU A 1 671  ? -62.814  65.876  19.652  1.00 214.29 ? 671  GLU A CA  1 
ATOM   5126  C  C   . GLU A 1 671  ? -63.057  67.150  20.502  1.00 193.47 ? 671  GLU A C   1 
ATOM   5127  O  O   . GLU A 1 671  ? -62.185  67.547  21.284  1.00 194.99 ? 671  GLU A O   1 
ATOM   5128  C  CB  . GLU A 1 671  ? -61.369  65.385  19.842  1.00 213.05 ? 671  GLU A CB  1 
ATOM   5129  C  CG  . GLU A 1 671  ? -61.078  64.004  19.238  1.00 211.26 ? 671  GLU A CG  1 
ATOM   5130  C  CD  . GLU A 1 671  ? -59.663  63.510  19.536  1.00 208.31 ? 671  GLU A CD  1 
ATOM   5131  O  OE1 . GLU A 1 671  ? -58.912  64.223  20.239  1.00 206.64 ? 671  GLU A OE1 1 
ATOM   5132  O  OE2 . GLU A 1 671  ? -59.304  62.406  19.068  1.00 207.57 ? 671  GLU A OE2 1 
ATOM   5133  N  N   . ILE A 1 672  ? -64.231  67.776  20.346  1.00 186.93 ? 672  ILE A N   1 
ATOM   5134  C  CA  . ILE A 1 672  ? -64.681  68.892  21.215  1.00 178.85 ? 672  ILE A CA  1 
ATOM   5135  C  C   . ILE A 1 672  ? -65.814  68.460  22.178  1.00 171.24 ? 672  ILE A C   1 
ATOM   5136  O  O   . ILE A 1 672  ? -66.093  69.132  23.173  1.00 169.22 ? 672  ILE A O   1 
ATOM   5137  C  CB  . ILE A 1 672  ? -65.143  70.158  20.389  1.00 198.40 ? 672  ILE A CB  1 
ATOM   5138  C  CG1 . ILE A 1 672  ? -64.855  71.471  21.133  1.00 196.83 ? 672  ILE A CG1 1 
ATOM   5139  C  CG2 . ILE A 1 672  ? -66.623  70.068  20.008  1.00 199.98 ? 672  ILE A CG2 1 
ATOM   5140  C  CD1 . ILE A 1 672  ? -65.448  72.708  20.456  1.00 198.01 ? 672  ILE A CD1 1 
ATOM   5141  N  N   . LEU A 1 673  ? -66.460  67.336  21.878  1.00 164.82 ? 673  LEU A N   1 
ATOM   5142  C  CA  . LEU A 1 673  ? -67.597  66.896  22.670  1.00 156.37 ? 673  LEU A CA  1 
ATOM   5143  C  C   . LEU A 1 673  ? -67.202  66.715  24.116  1.00 153.47 ? 673  LEU A C   1 
ATOM   5144  O  O   . LEU A 1 673  ? -67.955  66.138  24.886  1.00 152.88 ? 673  LEU A O   1 
ATOM   5145  C  CB  . LEU A 1 673  ? -68.169  65.590  22.130  1.00 149.55 ? 673  LEU A CB  1 
ATOM   5146  C  CG  . LEU A 1 673  ? -67.805  64.286  22.828  1.00 140.13 ? 673  LEU A CG  1 
ATOM   5147  C  CD1 . LEU A 1 673  ? -69.011  63.385  22.745  1.00 138.32 ? 673  LEU A CD1 1 
ATOM   5148  C  CD2 . LEU A 1 673  ? -66.552  63.616  22.248  1.00 136.43 ? 673  LEU A CD2 1 
ATOM   5149  N  N   . LEU A 1 679  ? -16.490  56.380  21.017  1.00 238.75 ? 679  LEU A N   1 
ATOM   5150  C  CA  . LEU A 1 679  ? -15.505  56.065  19.987  1.00 237.52 ? 679  LEU A CA  1 
ATOM   5151  C  C   . LEU A 1 679  ? -16.168  55.616  18.685  1.00 236.75 ? 679  LEU A C   1 
ATOM   5152  O  O   . LEU A 1 679  ? -15.578  55.732  17.612  1.00 236.45 ? 679  LEU A O   1 
ATOM   5153  C  CB  . LEU A 1 679  ? -14.518  55.012  20.493  1.00 236.26 ? 679  LEU A CB  1 
ATOM   5154  C  CG  . LEU A 1 679  ? -13.577  55.487  21.606  1.00 236.42 ? 679  LEU A CG  1 
ATOM   5155  C  CD1 . LEU A 1 679  ? -13.108  54.325  22.474  1.00 236.07 ? 679  LEU A CD1 1 
ATOM   5156  C  CD2 . LEU A 1 679  ? -12.391  56.269  21.034  1.00 236.58 ? 679  LEU A CD2 1 
ATOM   5157  N  N   . GLN A 1 680  ? -17.392  55.099  18.787  1.00 236.94 ? 680  GLN A N   1 
ATOM   5158  C  CA  . GLN A 1 680  ? -18.204  54.798  17.608  1.00 236.30 ? 680  GLN A CA  1 
ATOM   5159  C  C   . GLN A 1 680  ? -18.976  56.050  17.175  1.00 234.53 ? 680  GLN A C   1 
ATOM   5160  O  O   . GLN A 1 680  ? -19.533  56.101  16.080  1.00 233.83 ? 680  GLN A O   1 
ATOM   5161  C  CB  . GLN A 1 680  ? -19.160  53.621  17.871  1.00 238.51 ? 680  GLN A CB  1 
ATOM   5162  C  CG  . GLN A 1 680  ? -20.638  53.991  18.054  1.00 240.89 ? 680  GLN A CG  1 
ATOM   5163  C  CD  . GLN A 1 680  ? -20.928  54.717  19.357  1.00 243.45 ? 680  GLN A CD  1 
ATOM   5164  O  OE1 . GLN A 1 680  ? -20.063  54.846  20.217  1.00 244.82 ? 680  GLN A OE1 1 
ATOM   5165  N  NE2 . GLN A 1 680  ? -22.157  55.198  19.503  1.00 244.18 ? 680  GLN A NE2 1 
ATOM   5166  N  N   . LYS A 1 681  ? -18.998  57.058  18.046  1.00 232.94 ? 681  LYS A N   1 
ATOM   5167  C  CA  . LYS A 1 681  ? -19.635  58.338  17.747  1.00 229.84 ? 681  LYS A CA  1 
ATOM   5168  C  C   . LYS A 1 681  ? -18.791  59.122  16.746  1.00 229.81 ? 681  LYS A C   1 
ATOM   5169  O  O   . LYS A 1 681  ? -19.315  59.940  15.985  1.00 230.01 ? 681  LYS A O   1 
ATOM   5170  C  CB  . LYS A 1 681  ? -19.798  59.160  19.028  1.00 227.67 ? 681  LYS A CB  1 
ATOM   5171  C  CG  . LYS A 1 681  ? -19.993  58.330  20.291  1.00 224.38 ? 681  LYS A CG  1 
ATOM   5172  C  CD  . LYS A 1 681  ? -19.583  59.111  21.528  1.00 223.00 ? 681  LYS A CD  1 
ATOM   5173  C  CE  . LYS A 1 681  ? -19.410  58.190  22.715  1.00 221.74 ? 681  LYS A CE  1 
ATOM   5174  N  NZ  . LYS A 1 681  ? -18.884  58.924  23.889  1.00 223.15 ? 681  LYS A NZ  1 
ATOM   5175  N  N   . LYS A 1 682  ? -17.481  58.866  16.772  1.00 229.74 ? 682  LYS A N   1 
ATOM   5176  C  CA  . LYS A 1 682  ? -16.504  59.498  15.876  1.00 229.98 ? 682  LYS A CA  1 
ATOM   5177  C  C   . LYS A 1 682  ? -16.722  59.105  14.417  1.00 232.26 ? 682  LYS A C   1 
ATOM   5178  O  O   . LYS A 1 682  ? -16.361  59.841  13.498  1.00 230.94 ? 682  LYS A O   1 
ATOM   5179  C  CB  . LYS A 1 682  ? -15.075  59.135  16.308  1.00 227.67 ? 682  LYS A CB  1 
ATOM   5180  C  CG  . LYS A 1 682  ? -14.027  59.199  15.192  1.00 225.24 ? 682  LYS A CG  1 
ATOM   5181  C  CD  . LYS A 1 682  ? -13.700  60.633  14.783  1.00 224.27 ? 682  LYS A CD  1 
ATOM   5182  C  CE  . LYS A 1 682  ? -12.702  60.676  13.629  1.00 222.18 ? 682  LYS A CE  1 
ATOM   5183  N  NZ  . LYS A 1 682  ? -12.353  62.069  13.222  1.00 221.91 ? 682  LYS A NZ  1 
ATOM   5184  N  N   . ILE A 1 683  ? -17.298  57.927  14.209  1.00 236.33 ? 683  ILE A N   1 
ATOM   5185  C  CA  . ILE A 1 683  ? -17.696  57.518  12.872  1.00 239.94 ? 683  ILE A CA  1 
ATOM   5186  C  C   . ILE A 1 683  ? -19.096  58.075  12.574  1.00 244.00 ? 683  ILE A C   1 
ATOM   5187  O  O   . ILE A 1 683  ? -19.358  58.524  11.459  1.00 245.82 ? 683  ILE A O   1 
ATOM   5188  C  CB  . ILE A 1 683  ? -17.664  55.973  12.693  1.00 200.91 ? 683  ILE A CB  1 
ATOM   5189  C  CG1 . ILE A 1 683  ? -16.520  55.353  13.494  1.00 198.89 ? 683  ILE A CG1 1 
ATOM   5190  C  CG2 . ILE A 1 683  ? -17.512  55.607  11.232  1.00 201.21 ? 683  ILE A CG2 1 
ATOM   5191  C  CD1 . ILE A 1 683  ? -16.616  53.857  13.644  1.00 196.07 ? 683  ILE A CD1 1 
ATOM   5192  N  N   . GLU A 1 684  ? -19.973  58.075  13.585  1.00 245.97 ? 684  GLU A N   1 
ATOM   5193  C  CA  . GLU A 1 684  ? -21.392  58.437  13.408  1.00 247.77 ? 684  GLU A CA  1 
ATOM   5194  C  C   . GLU A 1 684  ? -21.620  59.896  13.008  1.00 245.33 ? 684  GLU A C   1 
ATOM   5195  O  O   . GLU A 1 684  ? -22.726  60.288  12.636  1.00 244.61 ? 684  GLU A O   1 
ATOM   5196  C  CB  . GLU A 1 684  ? -22.238  58.063  14.645  1.00 253.11 ? 684  GLU A CB  1 
ATOM   5197  C  CG  . GLU A 1 684  ? -22.610  56.567  14.722  1.00 257.00 ? 684  GLU A CG  1 
ATOM   5198  C  CD  . GLU A 1 684  ? -23.811  56.262  15.619  1.00 260.91 ? 684  GLU A CD  1 
ATOM   5199  O  OE1 . GLU A 1 684  ? -24.419  57.203  16.177  1.00 262.94 ? 684  GLU A OE1 1 
ATOM   5200  O  OE2 . GLU A 1 684  ? -24.148  55.064  15.759  1.00 261.57 ? 684  GLU A OE2 1 
ATOM   5201  N  N   . GLU A 1 685  ? -20.562  60.690  13.082  1.00 244.20 ? 685  GLU A N   1 
ATOM   5202  C  CA  . GLU A 1 685  ? -20.603  62.064  12.620  1.00 243.09 ? 685  GLU A CA  1 
ATOM   5203  C  C   . GLU A 1 685  ? -20.481  62.098  11.101  1.00 238.58 ? 685  GLU A C   1 
ATOM   5204  O  O   . GLU A 1 685  ? -20.967  63.018  10.448  1.00 239.06 ? 685  GLU A O   1 
ATOM   5205  C  CB  . GLU A 1 685  ? -19.450  62.834  13.246  1.00 245.50 ? 685  GLU A CB  1 
ATOM   5206  C  CG  . GLU A 1 685  ? -18.105  62.202  12.954  1.00 245.69 ? 685  GLU A CG  1 
ATOM   5207  C  CD  . GLU A 1 685  ? -17.034  62.637  13.924  1.00 247.45 ? 685  GLU A CD  1 
ATOM   5208  O  OE1 . GLU A 1 685  ? -17.384  63.246  14.960  1.00 248.70 ? 685  GLU A OE1 1 
ATOM   5209  O  OE2 . GLU A 1 685  ? -15.845  62.365  13.649  1.00 247.52 ? 685  GLU A OE2 1 
ATOM   5210  N  N   . ILE A 1 686  ? -19.824  61.083  10.551  1.00 233.64 ? 686  ILE A N   1 
ATOM   5211  C  CA  . ILE A 1 686  ? -19.594  60.981  9.109   1.00 229.54 ? 686  ILE A CA  1 
ATOM   5212  C  C   . ILE A 1 686  ? -20.843  60.520  8.320   1.00 225.26 ? 686  ILE A C   1 
ATOM   5213  O  O   . ILE A 1 686  ? -20.732  59.957  7.224   1.00 225.47 ? 686  ILE A O   1 
ATOM   5214  C  CB  . ILE A 1 686  ? -18.369  60.081  8.806   1.00 228.81 ? 686  ILE A CB  1 
ATOM   5215  C  CG1 . ILE A 1 686  ? -17.236  60.385  9.791   1.00 228.97 ? 686  ILE A CG1 1 
ATOM   5216  C  CG2 . ILE A 1 686  ? -17.892  60.270  7.374   1.00 228.91 ? 686  ILE A CG2 1 
ATOM   5217  C  CD1 . ILE A 1 686  ? -16.718  61.809  9.717   1.00 229.63 ? 686  ILE A CD1 1 
ATOM   5218  N  N   . ALA A 1 687  ? -22.025  60.747  8.903   1.00 220.22 ? 687  ALA A N   1 
ATOM   5219  C  CA  . ALA A 1 687  ? -23.290  60.711  8.167   1.00 213.80 ? 687  ALA A CA  1 
ATOM   5220  C  C   . ALA A 1 687  ? -23.351  62.024  7.409   1.00 209.27 ? 687  ALA A C   1 
ATOM   5221  O  O   . ALA A 1 687  ? -24.326  62.337  6.720   1.00 207.51 ? 687  ALA A O   1 
ATOM   5222  C  CB  . ALA A 1 687  ? -24.470  60.590  9.122   1.00 213.33 ? 687  ALA A CB  1 
ATOM   5223  N  N   . ALA A 1 688  ? -22.275  62.789  7.582   1.00 207.39 ? 688  ALA A N   1 
ATOM   5224  C  CA  . ALA A 1 688  ? -22.059  64.063  6.918   1.00 204.41 ? 688  ALA A CA  1 
ATOM   5225  C  C   . ALA A 1 688  ? -21.963  63.891  5.411   1.00 201.32 ? 688  ALA A C   1 
ATOM   5226  O  O   . ALA A 1 688  ? -21.950  64.870  4.666   1.00 199.92 ? 688  ALA A O   1 
ATOM   5227  C  CB  . ALA A 1 688  ? -20.796  64.720  7.455   1.00 205.00 ? 688  ALA A CB  1 
ATOM   5228  N  N   . LYS A 1 689  ? -21.863  62.646  4.962   1.00 198.67 ? 689  LYS A N   1 
ATOM   5229  C  CA  . LYS A 1 689  ? -21.945  62.375  3.533   1.00 199.13 ? 689  LYS A CA  1 
ATOM   5230  C  C   . LYS A 1 689  ? -23.279  61.754  3.150   1.00 205.05 ? 689  LYS A C   1 
ATOM   5231  O  O   . LYS A 1 689  ? -23.348  60.900  2.270   1.00 205.91 ? 689  LYS A O   1 
ATOM   5232  C  CB  . LYS A 1 689  ? -20.758  61.552  3.011   1.00 191.69 ? 689  LYS A CB  1 
ATOM   5233  C  CG  . LYS A 1 689  ? -20.547  60.190  3.635   1.00 185.32 ? 689  LYS A CG  1 
ATOM   5234  C  CD  . LYS A 1 689  ? -19.276  59.585  3.060   1.00 180.39 ? 689  LYS A CD  1 
ATOM   5235  C  CE  . LYS A 1 689  ? -18.091  60.533  3.232   1.00 177.49 ? 689  LYS A CE  1 
ATOM   5236  N  NZ  . LYS A 1 689  ? -17.006  60.338  2.230   1.00 175.00 ? 689  LYS A NZ  1 
ATOM   5237  N  N   . TYR A 1 690  ? -24.336  62.183  3.830   1.00 212.54 ? 690  TYR A N   1 
ATOM   5238  C  CA  . TYR A 1 690  ? -25.679  61.872  3.376   1.00 220.29 ? 690  TYR A CA  1 
ATOM   5239  C  C   . TYR A 1 690  ? -25.924  62.538  2.012   1.00 223.11 ? 690  TYR A C   1 
ATOM   5240  O  O   . TYR A 1 690  ? -25.522  63.679  1.771   1.00 223.14 ? 690  TYR A O   1 
ATOM   5241  C  CB  . TYR A 1 690  ? -26.729  62.296  4.409   1.00 227.39 ? 690  TYR A CB  1 
ATOM   5242  C  CG  . TYR A 1 690  ? -28.102  62.498  3.812   1.00 235.12 ? 690  TYR A CG  1 
ATOM   5243  C  CD1 . TYR A 1 690  ? -28.837  61.417  3.323   1.00 237.25 ? 690  TYR A CD1 1 
ATOM   5244  C  CD2 . TYR A 1 690  ? -28.659  63.772  3.723   1.00 239.20 ? 690  TYR A CD2 1 
ATOM   5245  C  CE1 . TYR A 1 690  ? -30.089  61.601  2.764   1.00 240.42 ? 690  TYR A CE1 1 
ATOM   5246  C  CE2 . TYR A 1 690  ? -29.910  63.967  3.169   1.00 242.33 ? 690  TYR A CE2 1 
ATOM   5247  C  CZ  . TYR A 1 690  ? -30.621  62.880  2.690   1.00 242.97 ? 690  TYR A CZ  1 
ATOM   5248  O  OH  . TYR A 1 690  ? -31.868  63.080  2.138   1.00 245.12 ? 690  TYR A OH  1 
ATOM   5249  N  N   . LYS A 1 691  ? -26.575  61.794  1.124   1.00 226.35 ? 691  LYS A N   1 
ATOM   5250  C  CA  . LYS A 1 691  ? -26.847  62.214  -0.246  1.00 228.30 ? 691  LYS A CA  1 
ATOM   5251  C  C   . LYS A 1 691  ? -27.671  61.079  -0.828  1.00 229.92 ? 691  LYS A C   1 
ATOM   5252  O  O   . LYS A 1 691  ? -27.900  60.987  -2.037  1.00 230.53 ? 691  LYS A O   1 
ATOM   5253  C  CB  . LYS A 1 691  ? -25.548  62.414  -1.033  1.00 227.87 ? 691  LYS A CB  1 
ATOM   5254  C  CG  . LYS A 1 691  ? -24.557  61.256  -0.924  1.00 224.87 ? 691  LYS A CG  1 
ATOM   5255  C  CD  . LYS A 1 691  ? -23.217  61.599  -1.565  1.00 222.98 ? 691  LYS A CD  1 
ATOM   5256  C  CE  . LYS A 1 691  ? -22.137  60.604  -1.175  1.00 220.52 ? 691  LYS A CE  1 
ATOM   5257  N  NZ  . LYS A 1 691  ? -20.808  61.050  -1.662  1.00 219.86 ? 691  LYS A NZ  1 
ATOM   5258  N  N   . HIS A 1 692  ? -28.094  60.212  0.087   1.00 228.30 ? 692  HIS A N   1 
ATOM   5259  C  CA  . HIS A 1 692  ? -28.906  59.040  -0.194  1.00 227.82 ? 692  HIS A CA  1 
ATOM   5260  C  C   . HIS A 1 692  ? -28.814  58.120  1.021   1.00 221.69 ? 692  HIS A C   1 
ATOM   5261  O  O   . HIS A 1 692  ? -27.802  58.098  1.721   1.00 218.98 ? 692  HIS A O   1 
ATOM   5262  C  CB  . HIS A 1 692  ? -28.422  58.323  -1.456  1.00 232.48 ? 692  HIS A CB  1 
ATOM   5263  C  CG  . HIS A 1 692  ? -29.424  57.369  -2.029  1.00 238.47 ? 692  HIS A CG  1 
ATOM   5264  N  ND1 . HIS A 1 692  ? -30.690  57.760  -2.409  1.00 242.60 ? 692  HIS A ND1 1 
ATOM   5265  C  CD2 . HIS A 1 692  ? -29.343  56.044  -2.297  1.00 240.54 ? 692  HIS A CD2 1 
ATOM   5266  C  CE1 . HIS A 1 692  ? -31.348  56.715  -2.879  1.00 244.37 ? 692  HIS A CE1 1 
ATOM   5267  N  NE2 . HIS A 1 692  ? -30.553  55.661  -2.823  1.00 243.07 ? 692  HIS A NE2 1 
ATOM   5268  N  N   . SER A 1 693  ? -29.875  57.373  1.287   1.00 218.45 ? 693  SER A N   1 
ATOM   5269  C  CA  . SER A 1 693  ? -29.861  56.435  2.398   1.00 213.05 ? 693  SER A CA  1 
ATOM   5270  C  C   . SER A 1 693  ? -28.703  55.468  2.232   1.00 205.23 ? 693  SER A C   1 
ATOM   5271  O  O   . SER A 1 693  ? -27.860  55.338  3.118   1.00 203.90 ? 693  SER A O   1 
ATOM   5272  C  CB  . SER A 1 693  ? -31.177  55.654  2.452   1.00 214.18 ? 693  SER A CB  1 
ATOM   5273  O  OG  . SER A 1 693  ? -31.067  54.499  3.271   1.00 212.89 ? 693  SER A OG  1 
ATOM   5274  N  N   . VAL A 1 694  ? -28.672  54.823  1.065   1.00 199.68 ? 694  VAL A N   1 
ATOM   5275  C  CA  . VAL A 1 694  ? -27.786  53.689  0.771   1.00 193.97 ? 694  VAL A CA  1 
ATOM   5276  C  C   . VAL A 1 694  ? -26.305  53.988  1.059   1.00 189.28 ? 694  VAL A C   1 
ATOM   5277  O  O   . VAL A 1 694  ? -25.506  53.072  1.271   1.00 188.15 ? 694  VAL A O   1 
ATOM   5278  C  CB  . VAL A 1 694  ? -27.990  53.141  -0.698  1.00 188.13 ? 694  VAL A CB  1 
ATOM   5279  C  CG1 . VAL A 1 694  ? -27.253  51.830  -0.902  1.00 186.83 ? 694  VAL A CG1 1 
ATOM   5280  C  CG2 . VAL A 1 694  ? -29.471  52.942  -1.020  1.00 189.20 ? 694  VAL A CG2 1 
ATOM   5281  N  N   . VAL A 1 695  ? -25.934  55.263  1.080   1.00 186.17 ? 695  VAL A N   1 
ATOM   5282  C  CA  . VAL A 1 695  ? -24.575  55.605  1.467   1.00 182.59 ? 695  VAL A CA  1 
ATOM   5283  C  C   . VAL A 1 695  ? -24.458  55.558  2.988   1.00 179.86 ? 695  VAL A C   1 
ATOM   5284  O  O   . VAL A 1 695  ? -23.418  55.159  3.515   1.00 178.24 ? 695  VAL A O   1 
ATOM   5285  C  CB  . VAL A 1 695  ? -24.119  56.964  0.895   1.00 183.75 ? 695  VAL A CB  1 
ATOM   5286  C  CG1 . VAL A 1 695  ? -22.672  57.249  1.259   1.00 182.63 ? 695  VAL A CG1 1 
ATOM   5287  C  CG2 . VAL A 1 695  ? -24.267  56.965  -0.609  1.00 184.09 ? 695  VAL A CG2 1 
ATOM   5288  N  N   . LYS A 1 696  ? -25.522  55.940  3.696   1.00 179.38 ? 696  LYS A N   1 
ATOM   5289  C  CA  . LYS A 1 696  ? -25.517  55.806  5.150   1.00 177.80 ? 696  LYS A CA  1 
ATOM   5290  C  C   . LYS A 1 696  ? -25.147  54.375  5.499   1.00 176.52 ? 696  LYS A C   1 
ATOM   5291  O  O   . LYS A 1 696  ? -24.093  54.110  6.088   1.00 175.89 ? 696  LYS A O   1 
ATOM   5292  C  CB  . LYS A 1 696  ? -26.877  56.141  5.757   1.00 178.78 ? 696  LYS A CB  1 
ATOM   5293  C  CG  . LYS A 1 696  ? -27.040  55.641  7.210   1.00 179.12 ? 696  LYS A CG  1 
ATOM   5294  C  CD  . LYS A 1 696  ? -25.948  56.196  8.166   1.00 174.27 ? 696  LYS A CD  1 
ATOM   5295  C  CE  . LYS A 1 696  ? -26.163  55.766  9.639   1.00 173.22 ? 696  LYS A CE  1 
ATOM   5296  N  NZ  . LYS A 1 696  ? -25.103  56.248  10.601  1.00 171.43 ? 696  LYS A NZ  1 
ATOM   5297  N  N   . LYS A 1 697  ? -26.027  53.456  5.114   1.00 175.14 ? 697  LYS A N   1 
ATOM   5298  C  CA  . LYS A 1 697  ? -25.775  52.029  5.252   1.00 173.23 ? 697  LYS A CA  1 
ATOM   5299  C  C   . LYS A 1 697  ? -24.367  51.701  4.747   1.00 171.13 ? 697  LYS A C   1 
ATOM   5300  O  O   . LYS A 1 697  ? -23.661  50.881  5.336   1.00 171.19 ? 697  LYS A O   1 
ATOM   5301  C  CB  . LYS A 1 697  ? -26.845  51.235  4.489   1.00 173.70 ? 697  LYS A CB  1 
ATOM   5302  C  CG  . LYS A 1 697  ? -26.605  49.743  4.384   1.00 174.30 ? 697  LYS A CG  1 
ATOM   5303  C  CD  . LYS A 1 697  ? -26.892  49.007  5.676   1.00 175.42 ? 697  LYS A CD  1 
ATOM   5304  C  CE  . LYS A 1 697  ? -26.727  47.509  5.463   1.00 175.94 ? 697  LYS A CE  1 
ATOM   5305  N  NZ  . LYS A 1 697  ? -26.740  46.710  6.722   1.00 176.39 ? 697  LYS A NZ  1 
ATOM   5306  N  N   . CYS A 1 698  ? -23.949  52.366  3.674   1.00 168.78 ? 698  CYS A N   1 
ATOM   5307  C  CA  . CYS A 1 698  ? -22.609  52.160  3.143   1.00 167.05 ? 698  CYS A CA  1 
ATOM   5308  C  C   . CYS A 1 698  ? -21.530  52.379  4.212   1.00 164.89 ? 698  CYS A C   1 
ATOM   5309  O  O   . CYS A 1 698  ? -20.724  51.491  4.467   1.00 162.05 ? 698  CYS A O   1 
ATOM   5310  C  CB  . CYS A 1 698  ? -22.359  53.043  1.912   1.00 166.86 ? 698  CYS A CB  1 
ATOM   5311  S  SG  . CYS A 1 698  ? -22.901  52.352  0.309   1.00 199.58 ? 698  CYS A SG  1 
ATOM   5312  N  N   . CYS A 1 699  ? -21.506  53.540  4.852   1.00 168.85 ? 699  CYS A N   1 
ATOM   5313  C  CA  . CYS A 1 699  ? -20.497  53.752  5.876   1.00 172.18 ? 699  CYS A CA  1 
ATOM   5314  C  C   . CYS A 1 699  ? -20.794  52.931  7.113   1.00 175.56 ? 699  CYS A C   1 
ATOM   5315  O  O   . CYS A 1 699  ? -19.909  52.290  7.674   1.00 174.93 ? 699  CYS A O   1 
ATOM   5316  C  CB  . CYS A 1 699  ? -20.410  55.214  6.267   1.00 174.46 ? 699  CYS A CB  1 
ATOM   5317  S  SG  . CYS A 1 699  ? -19.546  55.461  7.825   1.00 173.60 ? 699  CYS A SG  1 
ATOM   5318  N  N   . TYR A 1 700  ? -22.052  52.965  7.531   1.00 180.18 ? 700  TYR A N   1 
ATOM   5319  C  CA  . TYR A 1 700  ? -22.480  52.317  8.764   1.00 187.59 ? 700  TYR A CA  1 
ATOM   5320  C  C   . TYR A 1 700  ? -21.975  50.869  8.826   1.00 190.58 ? 700  TYR A C   1 
ATOM   5321  O  O   . TYR A 1 700  ? -21.055  50.558  9.593   1.00 190.91 ? 700  TYR A O   1 
ATOM   5322  C  CB  . TYR A 1 700  ? -24.008  52.380  8.868   1.00 194.40 ? 700  TYR A CB  1 
ATOM   5323  C  CG  . TYR A 1 700  ? -24.561  52.390  10.278  1.00 202.31 ? 700  TYR A CG  1 
ATOM   5324  C  CD1 . TYR A 1 700  ? -25.085  51.233  10.844  1.00 206.03 ? 700  TYR A CD1 1 
ATOM   5325  C  CD2 . TYR A 1 700  ? -24.573  53.556  11.035  1.00 206.03 ? 700  TYR A CD2 1 
ATOM   5326  C  CE1 . TYR A 1 700  ? -25.595  51.235  12.122  1.00 209.14 ? 700  TYR A CE1 1 
ATOM   5327  C  CE2 . TYR A 1 700  ? -25.085  53.569  12.314  1.00 209.33 ? 700  TYR A CE2 1 
ATOM   5328  C  CZ  . TYR A 1 700  ? -25.596  52.403  12.854  1.00 210.76 ? 700  TYR A CZ  1 
ATOM   5329  O  OH  . TYR A 1 700  ? -26.108  52.398  14.134  1.00 212.36 ? 700  TYR A OH  1 
ATOM   5330  N  N   . ASP A 1 701  ? -22.568  49.994  8.009   1.00 192.35 ? 701  ASP A N   1 
ATOM   5331  C  CA  . ASP A 1 701  ? -22.104  48.605  7.889   1.00 193.45 ? 701  ASP A CA  1 
ATOM   5332  C  C   . ASP A 1 701  ? -20.754  48.576  7.177   1.00 191.17 ? 701  ASP A C   1 
ATOM   5333  O  O   . ASP A 1 701  ? -20.132  47.522  7.007   1.00 191.73 ? 701  ASP A O   1 
ATOM   5334  C  CB  . ASP A 1 701  ? -23.152  47.695  7.203   1.00 194.84 ? 701  ASP A CB  1 
ATOM   5335  C  CG  . ASP A 1 701  ? -23.190  47.845  5.684   1.00 195.27 ? 701  ASP A CG  1 
ATOM   5336  O  OD1 . ASP A 1 701  ? -22.356  48.579  5.117   1.00 195.43 ? 701  ASP A OD1 1 
ATOM   5337  O  OD2 . ASP A 1 701  ? -24.063  47.211  5.053   1.00 195.32 ? 701  ASP A OD2 1 
ATOM   5338  N  N   . GLY A 1 702  ? -20.319  49.764  6.768   1.00 188.22 ? 702  GLY A N   1 
ATOM   5339  C  CA  . GLY A 1 702  ? -19.037  49.941  6.128   1.00 183.88 ? 702  GLY A CA  1 
ATOM   5340  C  C   . GLY A 1 702  ? -17.890  49.689  7.077   1.00 180.44 ? 702  GLY A C   1 
ATOM   5341  O  O   . GLY A 1 702  ? -16.931  48.999  6.740   1.00 178.73 ? 702  GLY A O   1 
ATOM   5342  N  N   . ALA A 1 703  ? -17.979  50.253  8.273   1.00 177.55 ? 703  ALA A N   1 
ATOM   5343  C  CA  . ALA A 1 703  ? -16.924  50.051  9.244   1.00 174.94 ? 703  ALA A CA  1 
ATOM   5344  C  C   . ALA A 1 703  ? -17.117  48.708  9.899   1.00 171.35 ? 703  ALA A C   1 
ATOM   5345  O  O   . ALA A 1 703  ? -16.156  48.066  10.316  1.00 171.62 ? 703  ALA A O   1 
ATOM   5346  C  CB  . ALA A 1 703  ? -16.949  51.143  10.276  1.00 176.51 ? 703  ALA A CB  1 
ATOM   5347  N  N   . CYS A 1 704  ? -18.371  48.270  9.926   1.00 166.61 ? 704  CYS A N   1 
ATOM   5348  C  CA  . CYS A 1 704  ? -18.808  47.244  10.861  1.00 164.48 ? 704  CYS A CA  1 
ATOM   5349  C  C   . CYS A 1 704  ? -17.625  46.594  11.572  1.00 164.32 ? 704  CYS A C   1 
ATOM   5350  O  O   . CYS A 1 704  ? -17.204  47.088  12.608  1.00 164.80 ? 704  CYS A O   1 
ATOM   5351  C  CB  . CYS A 1 704  ? -19.715  46.208  10.195  1.00 162.65 ? 704  CYS A CB  1 
ATOM   5352  S  SG  . CYS A 1 704  ? -20.901  45.433  11.338  1.00 138.42 ? 704  CYS A SG  1 
ATOM   5353  N  N   . VAL A 1 705  ? -17.060  45.526  11.015  1.00 164.49 ? 705  VAL A N   1 
ATOM   5354  C  CA  . VAL A 1 705  ? -15.999  44.796  11.705  1.00 165.22 ? 705  VAL A CA  1 
ATOM   5355  C  C   . VAL A 1 705  ? -15.383  43.719  10.868  1.00 167.22 ? 705  VAL A C   1 
ATOM   5356  O  O   . VAL A 1 705  ? -15.738  42.554  11.039  1.00 169.47 ? 705  VAL A O   1 
ATOM   5357  C  CB  . VAL A 1 705  ? -16.557  44.013  12.902  1.00 162.94 ? 705  VAL A CB  1 
ATOM   5358  C  CG1 . VAL A 1 705  ? -16.439  44.811  14.171  1.00 164.17 ? 705  VAL A CG1 1 
ATOM   5359  C  CG2 . VAL A 1 705  ? -17.996  43.562  12.640  1.00 161.40 ? 705  VAL A CG2 1 
ATOM   5360  N  N   . ASN A 1 706  ? -14.442  44.049  9.994   1.00 168.50 ? 706  ASN A N   1 
ATOM   5361  C  CA  . ASN A 1 706  ? -13.910  42.979  9.155   1.00 169.68 ? 706  ASN A CA  1 
ATOM   5362  C  C   . ASN A 1 706  ? -12.408  42.934  9.049   1.00 167.63 ? 706  ASN A C   1 
ATOM   5363  O  O   . ASN A 1 706  ? -11.790  43.660  8.273   1.00 167.73 ? 706  ASN A O   1 
ATOM   5364  C  CB  . ASN A 1 706  ? -14.551  42.971  7.770   1.00 172.60 ? 706  ASN A CB  1 
ATOM   5365  C  CG  . ASN A 1 706  ? -14.786  41.573  7.257   1.00 175.10 ? 706  ASN A CG  1 
ATOM   5366  O  OD1 . ASN A 1 706  ? -14.158  40.618  7.720   1.00 176.13 ? 706  ASN A OD1 1 
ATOM   5367  N  ND2 . ASN A 1 706  ? -15.706  41.439  6.308   1.00 176.17 ? 706  ASN A ND2 1 
ATOM   5368  N  N   . ASN A 1 707  ? -11.835  42.044  9.840   1.00 166.41 ? 707  ASN A N   1 
ATOM   5369  C  CA  . ASN A 1 707  ? -10.395  41.984  9.986   1.00 165.11 ? 707  ASN A CA  1 
ATOM   5370  C  C   . ASN A 1 707  ? -9.702   40.919  9.139   1.00 161.00 ? 707  ASN A C   1 
ATOM   5371  O  O   . ASN A 1 707  ? -8.480   40.781  9.188   1.00 158.17 ? 707  ASN A O   1 
ATOM   5372  C  CB  . ASN A 1 707  ? -9.980   41.891  11.471  1.00 168.02 ? 707  ASN A CB  1 
ATOM   5373  C  CG  . ASN A 1 707  ? -10.960  41.096  12.333  1.00 168.49 ? 707  ASN A CG  1 
ATOM   5374  O  OD1 . ASN A 1 707  ? -12.072  40.761  11.915  1.00 167.80 ? 707  ASN A OD1 1 
ATOM   5375  N  ND2 . ASN A 1 707  ? -10.540  40.802  13.559  1.00 169.14 ? 707  ASN A ND2 1 
ATOM   5376  N  N   . ASP A 1 708  ? -10.472  40.172  8.359   1.00 159.13 ? 708  ASP A N   1 
ATOM   5377  C  CA  . ASP A 1 708  ? -9.871   39.136  7.536   1.00 155.53 ? 708  ASP A CA  1 
ATOM   5378  C  C   . ASP A 1 708  ? -9.537   39.617  6.134   1.00 154.66 ? 708  ASP A C   1 
ATOM   5379  O  O   . ASP A 1 708  ? -8.879   38.919  5.362   1.00 152.92 ? 708  ASP A O   1 
ATOM   5380  C  CB  . ASP A 1 708  ? -10.742  37.890  7.514   1.00 149.93 ? 708  ASP A CB  1 
ATOM   5381  C  CG  . ASP A 1 708  ? -10.402  36.945  8.632   1.00 142.53 ? 708  ASP A CG  1 
ATOM   5382  O  OD1 . ASP A 1 708  ? -9.359   37.180  9.276   1.00 138.52 ? 708  ASP A OD1 1 
ATOM   5383  O  OD2 . ASP A 1 708  ? -11.159  35.975  8.857   1.00 139.44 ? 708  ASP A OD2 1 
ATOM   5384  N  N   . GLU A 1 709  ? -9.983   40.825  5.817   1.00 154.83 ? 709  GLU A N   1 
ATOM   5385  C  CA  . GLU A 1 709  ? -9.602   41.459  4.568   1.00 156.69 ? 709  GLU A CA  1 
ATOM   5386  C  C   . GLU A 1 709  ? -9.479   42.974  4.722   1.00 158.34 ? 709  GLU A C   1 
ATOM   5387  O  O   . GLU A 1 709  ? -10.104  43.565  5.604   1.00 161.85 ? 709  GLU A O   1 
ATOM   5388  C  CB  . GLU A 1 709  ? -10.562  41.075  3.426   1.00 158.18 ? 709  GLU A CB  1 
ATOM   5389  C  CG  . GLU A 1 709  ? -12.056  40.934  3.790   1.00 159.16 ? 709  GLU A CG  1 
ATOM   5390  C  CD  . GLU A 1 709  ? -12.856  40.184  2.713   1.00 158.74 ? 709  GLU A CD  1 
ATOM   5391  O  OE1 . GLU A 1 709  ? -12.366  40.114  1.558   1.00 157.88 ? 709  GLU A OE1 1 
ATOM   5392  O  OE2 . GLU A 1 709  ? -13.962  39.669  3.025   1.00 158.46 ? 709  GLU A OE2 1 
ATOM   5393  N  N   . THR A 1 710  ? -8.660   43.584  3.866   1.00 156.99 ? 710  THR A N   1 
ATOM   5394  C  CA  . THR A 1 710  ? -8.416   45.029  3.879   1.00 158.97 ? 710  THR A CA  1 
ATOM   5395  C  C   . THR A 1 710  ? -9.702   45.830  3.722   1.00 162.58 ? 710  THR A C   1 
ATOM   5396  O  O   . THR A 1 710  ? -10.762  45.269  3.463   1.00 162.15 ? 710  THR A O   1 
ATOM   5397  C  CB  . THR A 1 710  ? -7.447   45.458  2.738   1.00 179.67 ? 710  THR A CB  1 
ATOM   5398  O  OG1 . THR A 1 710  ? -8.184   45.725  1.537   1.00 179.26 ? 710  THR A OG1 1 
ATOM   5399  C  CG2 . THR A 1 710  ? -6.399   44.386  2.472   1.00 179.70 ? 710  THR A CG2 1 
ATOM   5400  N  N   . CYS A 1 711  ? -9.623   47.144  3.875   1.00 166.56 ? 711  CYS A N   1 
ATOM   5401  C  CA  . CYS A 1 711  ? -10.793  47.942  3.575   1.00 170.17 ? 711  CYS A CA  1 
ATOM   5402  C  C   . CYS A 1 711  ? -11.091  47.861  2.095   1.00 170.39 ? 711  CYS A C   1 
ATOM   5403  O  O   . CYS A 1 711  ? -12.201  47.521  1.704   1.00 172.10 ? 711  CYS A O   1 
ATOM   5404  C  CB  . CYS A 1 711  ? -10.642  49.385  4.030   1.00 172.80 ? 711  CYS A CB  1 
ATOM   5405  S  SG  . CYS A 1 711  ? -11.588  49.724  5.524   1.00 172.14 ? 711  CYS A SG  1 
ATOM   5406  N  N   . GLU A 1 712  ? -10.094  48.131  1.266   1.00 169.55 ? 712  GLU A N   1 
ATOM   5407  C  CA  . GLU A 1 712  ? -10.324  48.119  -0.173  1.00 169.34 ? 712  GLU A CA  1 
ATOM   5408  C  C   . GLU A 1 712  ? -10.484  46.715  -0.790  1.00 164.10 ? 712  GLU A C   1 
ATOM   5409  O  O   . GLU A 1 712  ? -10.820  46.594  -1.965  1.00 162.25 ? 712  GLU A O   1 
ATOM   5410  C  CB  . GLU A 1 712  ? -9.275   48.963  -0.911  1.00 176.16 ? 712  GLU A CB  1 
ATOM   5411  C  CG  . GLU A 1 712  ? -7.845   48.475  -0.781  1.00 182.72 ? 712  GLU A CG  1 
ATOM   5412  C  CD  . GLU A 1 712  ? -6.866   49.365  -1.524  1.00 187.97 ? 712  GLU A CD  1 
ATOM   5413  O  OE1 . GLU A 1 712  ? -7.029   50.607  -1.463  1.00 190.29 ? 712  GLU A OE1 1 
ATOM   5414  O  OE2 . GLU A 1 712  ? -5.939   48.821  -2.164  1.00 189.32 ? 712  GLU A OE2 1 
ATOM   5415  N  N   . GLN A 1 713  ? -10.256  45.662  -0.009  1.00 161.57 ? 713  GLN A N   1 
ATOM   5416  C  CA  . GLN A 1 713  ? -10.599  44.314  -0.459  1.00 158.53 ? 713  GLN A CA  1 
ATOM   5417  C  C   . GLN A 1 713  ? -12.102  44.178  -0.387  1.00 154.93 ? 713  GLN A C   1 
ATOM   5418  O  O   . GLN A 1 713  ? -12.744  43.640  -1.286  1.00 155.42 ? 713  GLN A O   1 
ATOM   5419  C  CB  . GLN A 1 713  ? -9.933   43.240  0.403   1.00 158.70 ? 713  GLN A CB  1 
ATOM   5420  C  CG  . GLN A 1 713  ? -8.513   42.923  -0.017  1.00 158.89 ? 713  GLN A CG  1 
ATOM   5421  C  CD  . GLN A 1 713  ? -7.725   42.151  1.030   1.00 158.78 ? 713  GLN A CD  1 
ATOM   5422  O  OE1 . GLN A 1 713  ? -8.167   41.972  2.160   1.00 158.83 ? 713  GLN A OE1 1 
ATOM   5423  N  NE2 . GLN A 1 713  ? -6.535   41.705  0.655   1.00 158.65 ? 713  GLN A NE2 1 
ATOM   5424  N  N   . ARG A 1 714  ? -12.659  44.689  0.700   1.00 150.45 ? 714  ARG A N   1 
ATOM   5425  C  CA  . ARG A 1 714  ? -14.101  44.718  0.874   1.00 147.53 ? 714  ARG A CA  1 
ATOM   5426  C  C   . ARG A 1 714  ? -14.749  45.666  -0.138  1.00 143.21 ? 714  ARG A C   1 
ATOM   5427  O  O   . ARG A 1 714  ? -15.757  45.332  -0.745  1.00 141.44 ? 714  ARG A O   1 
ATOM   5428  C  CB  . ARG A 1 714  ? -14.456  45.122  2.315   1.00 149.31 ? 714  ARG A CB  1 
ATOM   5429  C  CG  . ARG A 1 714  ? -14.076  44.089  3.373   1.00 151.63 ? 714  ARG A CG  1 
ATOM   5430  C  CD  . ARG A 1 714  ? -13.907  44.723  4.739   1.00 155.01 ? 714  ARG A CD  1 
ATOM   5431  N  NE  . ARG A 1 714  ? -15.172  45.216  5.266   1.00 158.78 ? 714  ARG A NE  1 
ATOM   5432  C  CZ  . ARG A 1 714  ? -15.298  45.904  6.402   1.00 162.47 ? 714  ARG A CZ  1 
ATOM   5433  N  NH1 . ARG A 1 714  ? -14.235  46.197  7.156   1.00 163.06 ? 714  ARG A NH1 1 
ATOM   5434  N  NH2 . ARG A 1 714  ? -16.500  46.304  6.795   1.00 163.86 ? 714  ARG A NH2 1 
ATOM   5435  N  N   . ALA A 1 715  ? -14.160  46.845  -0.322  1.00 141.59 ? 715  ALA A N   1 
ATOM   5436  C  CA  . ALA A 1 715  ? -14.718  47.841  -1.232  1.00 139.08 ? 715  ALA A CA  1 
ATOM   5437  C  C   . ALA A 1 715  ? -14.827  47.260  -2.622  1.00 136.89 ? 715  ALA A C   1 
ATOM   5438  O  O   . ALA A 1 715  ? -15.748  47.569  -3.370  1.00 138.33 ? 715  ALA A O   1 
ATOM   5439  C  CB  . ALA A 1 715  ? -13.866  49.094  -1.258  1.00 135.43 ? 715  ALA A CB  1 
ATOM   5440  N  N   . ALA A 1 716  ? -13.874  46.415  -2.970  1.00 137.92 ? 716  ALA A N   1 
ATOM   5441  C  CA  . ALA A 1 716  ? -13.911  45.769  -4.266  1.00 139.86 ? 716  ALA A CA  1 
ATOM   5442  C  C   . ALA A 1 716  ? -15.282  45.139  -4.494  1.00 140.34 ? 716  ALA A C   1 
ATOM   5443  O  O   . ALA A 1 716  ? -15.954  45.413  -5.488  1.00 140.62 ? 716  ALA A O   1 
ATOM   5444  C  CB  . ALA A 1 716  ? -12.819  44.717  -4.358  1.00 139.99 ? 716  ALA A CB  1 
ATOM   5445  N  N   . ARG A 1 717  ? -15.699  44.313  -3.543  1.00 143.09 ? 717  ARG A N   1 
ATOM   5446  C  CA  . ARG A 1 717  ? -16.927  43.531  -3.660  1.00 145.33 ? 717  ARG A CA  1 
ATOM   5447  C  C   . ARG A 1 717  ? -18.162  44.416  -3.693  1.00 144.98 ? 717  ARG A C   1 
ATOM   5448  O  O   . ARG A 1 717  ? -19.275  43.914  -3.792  1.00 144.46 ? 717  ARG A O   1 
ATOM   5449  C  CB  . ARG A 1 717  ? -17.030  42.557  -2.480  1.00 148.58 ? 717  ARG A CB  1 
ATOM   5450  C  CG  . ARG A 1 717  ? -17.762  41.258  -2.761  1.00 151.49 ? 717  ARG A CG  1 
ATOM   5451  C  CD  . ARG A 1 717  ? -17.674  40.329  -1.546  1.00 152.78 ? 717  ARG A CD  1 
ATOM   5452  N  NE  . ARG A 1 717  ? -16.329  40.280  -0.969  1.00 151.67 ? 717  ARG A NE  1 
ATOM   5453  C  CZ  . ARG A 1 717  ? -15.963  40.894  0.151   1.00 149.58 ? 717  ARG A CZ  1 
ATOM   5454  N  NH1 . ARG A 1 717  ? -16.830  41.605  0.840   1.00 148.47 ? 717  ARG A NH1 1 
ATOM   5455  N  NH2 . ARG A 1 717  ? -14.721  40.792  0.583   1.00 149.54 ? 717  ARG A NH2 1 
ATOM   5456  N  N   . ILE A 1 718  ? -17.961  45.728  -3.585  1.00 146.93 ? 718  ILE A N   1 
ATOM   5457  C  CA  . ILE A 1 718  ? -19.077  46.669  -3.553  1.00 149.97 ? 718  ILE A CA  1 
ATOM   5458  C  C   . ILE A 1 718  ? -19.621  46.892  -4.937  1.00 155.28 ? 718  ILE A C   1 
ATOM   5459  O  O   . ILE A 1 718  ? -18.865  47.136  -5.875  1.00 153.44 ? 718  ILE A O   1 
ATOM   5460  C  CB  . ILE A 1 718  ? -18.679  48.033  -2.992  1.00 147.24 ? 718  ILE A CB  1 
ATOM   5461  C  CG1 . ILE A 1 718  ? -18.586  47.959  -1.480  1.00 148.58 ? 718  ILE A CG1 1 
ATOM   5462  C  CG2 . ILE A 1 718  ? -19.703  49.094  -3.372  1.00 146.44 ? 718  ILE A CG2 1 
ATOM   5463  C  CD1 . ILE A 1 718  ? -18.325  49.290  -0.862  1.00 149.78 ? 718  ILE A CD1 1 
ATOM   5464  N  N   . SER A 1 719  ? -20.937  46.805  -5.063  1.00 161.51 ? 719  SER A N   1 
ATOM   5465  C  CA  . SER A 1 719  ? -21.566  47.082  -6.329  1.00 165.74 ? 719  SER A CA  1 
ATOM   5466  C  C   . SER A 1 719  ? -22.372  48.361  -6.272  1.00 174.80 ? 719  SER A C   1 
ATOM   5467  O  O   . SER A 1 719  ? -22.259  49.212  -7.145  1.00 176.90 ? 719  SER A O   1 
ATOM   5468  C  CB  . SER A 1 719  ? -22.469  45.941  -6.714  1.00 161.66 ? 719  SER A CB  1 
ATOM   5469  O  OG  . SER A 1 719  ? -22.842  46.117  -8.055  1.00 160.55 ? 719  SER A OG  1 
ATOM   5470  N  N   . LEU A 1 720  ? -23.158  48.494  -5.210  1.00 181.77 ? 720  LEU A N   1 
ATOM   5471  C  CA  . LEU A 1 720  ? -24.186  49.538  -5.081  1.00 190.59 ? 720  LEU A CA  1 
ATOM   5472  C  C   . LEU A 1 720  ? -23.899  50.882  -5.766  1.00 197.21 ? 720  LEU A C   1 
ATOM   5473  O  O   . LEU A 1 720  ? -24.828  51.569  -6.192  1.00 197.11 ? 720  LEU A O   1 
ATOM   5474  C  CB  . LEU A 1 720  ? -24.550  49.762  -3.600  1.00 194.86 ? 720  LEU A CB  1 
ATOM   5475  C  CG  . LEU A 1 720  ? -25.172  48.574  -2.842  1.00 201.42 ? 720  LEU A CG  1 
ATOM   5476  C  CD1 . LEU A 1 720  ? -25.569  48.951  -1.421  1.00 203.43 ? 720  LEU A CD1 1 
ATOM   5477  C  CD2 . LEU A 1 720  ? -26.374  48.020  -3.592  1.00 205.22 ? 720  LEU A CD2 1 
ATOM   5478  N  N   . GLY A 1 721  ? -22.631  51.263  -5.868  1.00 204.00 ? 721  GLY A N   1 
ATOM   5479  C  CA  . GLY A 1 721  ? -22.283  52.481  -6.573  1.00 210.86 ? 721  GLY A CA  1 
ATOM   5480  C  C   . GLY A 1 721  ? -21.063  53.187  -6.023  1.00 213.98 ? 721  GLY A C   1 
ATOM   5481  O  O   . GLY A 1 721  ? -21.032  53.535  -4.839  1.00 215.48 ? 721  GLY A O   1 
ATOM   5482  N  N   . PRO A 1 722  ? -20.049  53.404  -6.883  1.00 213.54 ? 722  PRO A N   1 
ATOM   5483  C  CA  . PRO A 1 722  ? -18.839  54.155  -6.520  1.00 211.05 ? 722  PRO A CA  1 
ATOM   5484  C  C   . PRO A 1 722  ? -19.158  55.450  -5.762  1.00 208.27 ? 722  PRO A C   1 
ATOM   5485  O  O   . PRO A 1 722  ? -18.266  56.146  -5.281  1.00 206.54 ? 722  PRO A O   1 
ATOM   5486  C  CB  . PRO A 1 722  ? -18.204  54.448  -7.881  1.00 212.10 ? 722  PRO A CB  1 
ATOM   5487  C  CG  . PRO A 1 722  ? -18.586  53.240  -8.725  1.00 211.57 ? 722  PRO A CG  1 
ATOM   5488  C  CD  . PRO A 1 722  ? -19.954  52.814  -8.237  1.00 212.67 ? 722  PRO A CD  1 
ATOM   5489  N  N   . ARG A 1 723  ? -20.446  55.749  -5.664  1.00 206.02 ? 723  ARG A N   1 
ATOM   5490  C  CA  . ARG A 1 723  ? -20.943  56.880  -4.908  1.00 203.65 ? 723  ARG A CA  1 
ATOM   5491  C  C   . ARG A 1 723  ? -20.699  56.682  -3.410  1.00 201.51 ? 723  ARG A C   1 
ATOM   5492  O  O   . ARG A 1 723  ? -20.473  57.642  -2.666  1.00 202.71 ? 723  ARG A O   1 
ATOM   5493  C  CB  . ARG A 1 723  ? -22.440  57.026  -5.175  1.00 201.12 ? 723  ARG A CB  1 
ATOM   5494  C  CG  . ARG A 1 723  ? -22.883  56.528  -6.559  1.00 197.07 ? 723  ARG A CG  1 
ATOM   5495  C  CD  . ARG A 1 723  ? -24.385  56.711  -6.739  1.00 194.26 ? 723  ARG A CD  1 
ATOM   5496  N  NE  . ARG A 1 723  ? -24.853  56.460  -8.098  1.00 192.01 ? 723  ARG A NE  1 
ATOM   5497  C  CZ  . ARG A 1 723  ? -25.463  55.342  -8.480  1.00 190.92 ? 723  ARG A CZ  1 
ATOM   5498  N  NH1 . ARG A 1 723  ? -25.667  54.366  -7.606  1.00 190.07 ? 723  ARG A NH1 1 
ATOM   5499  N  NH2 . ARG A 1 723  ? -25.868  55.195  -9.736  1.00 191.23 ? 723  ARG A NH2 1 
ATOM   5500  N  N   . CYS A 1 724  ? -20.758  55.427  -2.972  1.00 198.08 ? 724  CYS A N   1 
ATOM   5501  C  CA  . CYS A 1 724  ? -20.625  55.099  -1.556  1.00 195.28 ? 724  CYS A CA  1 
ATOM   5502  C  C   . CYS A 1 724  ? -19.336  54.339  -1.225  1.00 194.28 ? 724  CYS A C   1 
ATOM   5503  O  O   . CYS A 1 724  ? -19.023  54.109  -0.058  1.00 192.73 ? 724  CYS A O   1 
ATOM   5504  C  CB  . CYS A 1 724  ? -21.853  54.319  -1.064  1.00 193.80 ? 724  CYS A CB  1 
ATOM   5505  S  SG  . CYS A 1 724  ? -21.867  52.545  -1.430  1.00 160.95 ? 724  CYS A SG  1 
ATOM   5506  N  N   . ILE A 1 725  ? -18.585  53.950  -2.246  1.00 194.98 ? 725  ILE A N   1 
ATOM   5507  C  CA  . ILE A 1 725  ? -17.328  53.262  -2.003  1.00 194.12 ? 725  ILE A CA  1 
ATOM   5508  C  C   . ILE A 1 725  ? -16.427  54.063  -1.082  1.00 195.58 ? 725  ILE A C   1 
ATOM   5509  O  O   . ILE A 1 725  ? -15.750  53.493  -0.231  1.00 196.03 ? 725  ILE A O   1 
ATOM   5510  C  CB  . ILE A 1 725  ? -16.575  52.997  -3.294  1.00 192.26 ? 725  ILE A CB  1 
ATOM   5511  C  CG1 . ILE A 1 725  ? -17.334  51.958  -4.113  1.00 191.10 ? 725  ILE A CG1 1 
ATOM   5512  C  CG2 . ILE A 1 725  ? -15.160  52.525  -2.983  1.00 191.38 ? 725  ILE A CG2 1 
ATOM   5513  C  CD1 . ILE A 1 725  ? -16.654  51.583  -5.405  1.00 190.69 ? 725  ILE A CD1 1 
ATOM   5514  N  N   . LYS A 1 726  ? -16.416  55.383  -1.269  1.00 196.62 ? 726  LYS A N   1 
ATOM   5515  C  CA  . LYS A 1 726  ? -15.666  56.286  -0.399  1.00 197.62 ? 726  LYS A CA  1 
ATOM   5516  C  C   . LYS A 1 726  ? -16.254  56.221  0.994   1.00 191.59 ? 726  LYS A C   1 
ATOM   5517  O  O   . LYS A 1 726  ? -15.536  56.038  1.974   1.00 188.79 ? 726  LYS A O   1 
ATOM   5518  C  CB  . LYS A 1 726  ? -15.726  57.735  -0.902  1.00 206.21 ? 726  LYS A CB  1 
ATOM   5519  C  CG  . LYS A 1 726  ? -14.574  58.165  -1.817  1.00 214.02 ? 726  LYS A CG  1 
ATOM   5520  C  CD  . LYS A 1 726  ? -14.420  59.693  -1.845  1.00 220.71 ? 726  LYS A CD  1 
ATOM   5521  C  CE  . LYS A 1 726  ? -13.364  60.151  -2.851  1.00 224.25 ? 726  LYS A CE  1 
ATOM   5522  N  NZ  . LYS A 1 726  ? -13.220  61.641  -2.893  1.00 226.41 ? 726  LYS A NZ  1 
ATOM   5523  N  N   . ALA A 1 727  ? -17.572  56.366  1.071   1.00 188.46 ? 727  ALA A N   1 
ATOM   5524  C  CA  . ALA A 1 727  ? -18.269  56.292  2.344   1.00 186.12 ? 727  ALA A CA  1 
ATOM   5525  C  C   . ALA A 1 727  ? -17.917  55.000  3.076   1.00 179.57 ? 727  ALA A C   1 
ATOM   5526  O  O   . ALA A 1 727  ? -18.005  54.919  4.301   1.00 178.73 ? 727  ALA A O   1 
ATOM   5527  C  CB  . ALA A 1 727  ? -19.758  56.390  2.124   1.00 187.21 ? 727  ALA A CB  1 
ATOM   5528  N  N   . PHE A 1 728  ? -17.515  53.992  2.310   1.00 175.18 ? 728  PHE A N   1 
ATOM   5529  C  CA  . PHE A 1 728  ? -17.149  52.691  2.863   1.00 169.58 ? 728  PHE A CA  1 
ATOM   5530  C  C   . PHE A 1 728  ? -15.690  52.653  3.353   1.00 172.33 ? 728  PHE A C   1 
ATOM   5531  O  O   . PHE A 1 728  ? -15.431  52.374  4.528   1.00 174.32 ? 728  PHE A O   1 
ATOM   5532  C  CB  . PHE A 1 728  ? -17.414  51.592  1.827   1.00 159.73 ? 728  PHE A CB  1 
ATOM   5533  C  CG  . PHE A 1 728  ? -17.197  50.200  2.345   1.00 152.17 ? 728  PHE A CG  1 
ATOM   5534  C  CD1 . PHE A 1 728  ? -17.964  49.703  3.373   1.00 149.87 ? 728  PHE A CD1 1 
ATOM   5535  C  CD2 . PHE A 1 728  ? -16.234  49.382  1.789   1.00 149.27 ? 728  PHE A CD2 1 
ATOM   5536  C  CE1 . PHE A 1 728  ? -17.768  48.419  3.843   1.00 148.49 ? 728  PHE A CE1 1 
ATOM   5537  C  CE2 . PHE A 1 728  ? -16.035  48.100  2.258   1.00 147.54 ? 728  PHE A CE2 1 
ATOM   5538  C  CZ  . PHE A 1 728  ? -16.803  47.620  3.286   1.00 147.67 ? 728  PHE A CZ  1 
ATOM   5539  N  N   . THR A 1 729  ? -14.746  52.941  2.453   1.00 173.92 ? 729  THR A N   1 
ATOM   5540  C  CA  . THR A 1 729  ? -13.316  52.932  2.787   1.00 173.72 ? 729  THR A CA  1 
ATOM   5541  C  C   . THR A 1 729  ? -12.985  54.002  3.825   1.00 175.89 ? 729  THR A C   1 
ATOM   5542  O  O   . THR A 1 729  ? -12.163  53.788  4.716   1.00 175.70 ? 729  THR A O   1 
ATOM   5543  C  CB  . THR A 1 729  ? -12.403  53.087  1.523   1.00 200.96 ? 729  THR A CB  1 
ATOM   5544  O  OG1 . THR A 1 729  ? -13.192  53.494  0.399   1.00 200.73 ? 729  THR A OG1 1 
ATOM   5545  C  CG2 . THR A 1 729  ? -11.710  51.771  1.172   1.00 200.45 ? 729  THR A CG2 1 
ATOM   5546  N  N   . GLU A 1 730  ? -13.639  55.150  3.716   1.00 177.69 ? 730  GLU A N   1 
ATOM   5547  C  CA  . GLU A 1 730  ? -13.451  56.207  4.692   1.00 180.98 ? 730  GLU A CA  1 
ATOM   5548  C  C   . GLU A 1 730  ? -13.764  55.673  6.073   1.00 182.24 ? 730  GLU A C   1 
ATOM   5549  O  O   . GLU A 1 730  ? -12.866  55.402  6.870   1.00 182.24 ? 730  GLU A O   1 
ATOM   5550  C  CB  . GLU A 1 730  ? -14.370  57.391  4.385   1.00 182.38 ? 730  GLU A CB  1 
ATOM   5551  C  CG  . GLU A 1 730  ? -13.884  58.291  3.252   1.00 181.98 ? 730  GLU A CG  1 
ATOM   5552  C  CD  . GLU A 1 730  ? -13.086  59.477  3.758   1.00 181.23 ? 730  GLU A CD  1 
ATOM   5553  O  OE1 . GLU A 1 730  ? -13.507  60.075  4.777   1.00 180.13 ? 730  GLU A OE1 1 
ATOM   5554  O  OE2 . GLU A 1 730  ? -12.050  59.806  3.135   1.00 181.17 ? 730  GLU A OE2 1 
ATOM   5555  N  N   . CYS A 1 731  ? -15.053  55.506  6.332   1.00 182.51 ? 731  CYS A N   1 
ATOM   5556  C  CA  . CYS A 1 731  ? -15.529  55.139  7.652   1.00 184.81 ? 731  CYS A CA  1 
ATOM   5557  C  C   . CYS A 1 731  ? -14.882  53.846  8.126   1.00 186.72 ? 731  CYS A C   1 
ATOM   5558  O  O   . CYS A 1 731  ? -14.734  53.626  9.327   1.00 187.64 ? 731  CYS A O   1 
ATOM   5559  C  CB  . CYS A 1 731  ? -17.057  55.014  7.655   1.00 183.92 ? 731  CYS A CB  1 
ATOM   5560  S  SG  . CYS A 1 731  ? -17.950  56.522  7.171   1.00 231.90 ? 731  CYS A SG  1 
ATOM   5561  N  N   . CYS A 1 732  ? -14.489  52.995  7.184   1.00 188.20 ? 732  CYS A N   1 
ATOM   5562  C  CA  . CYS A 1 732  ? -13.891  51.720  7.549   1.00 189.42 ? 732  CYS A CA  1 
ATOM   5563  C  C   . CYS A 1 732  ? -12.522  51.924  8.176   1.00 190.45 ? 732  CYS A C   1 
ATOM   5564  O  O   . CYS A 1 732  ? -12.249  51.404  9.260   1.00 191.78 ? 732  CYS A O   1 
ATOM   5565  C  CB  . CYS A 1 732  ? -13.780  50.790  6.349   1.00 188.33 ? 732  CYS A CB  1 
ATOM   5566  S  SG  . CYS A 1 732  ? -13.086  49.202  6.799   1.00 181.10 ? 732  CYS A SG  1 
ATOM   5567  N  N   . VAL A 1 733  ? -11.662  52.681  7.497   1.00 190.79 ? 733  VAL A N   1 
ATOM   5568  C  CA  . VAL A 1 733  ? -10.332  52.964  8.030   1.00 189.83 ? 733  VAL A CA  1 
ATOM   5569  C  C   . VAL A 1 733  ? -10.484  53.632  9.393   1.00 188.67 ? 733  VAL A C   1 
ATOM   5570  O  O   . VAL A 1 733  ? -9.901   53.190  10.381  1.00 187.56 ? 733  VAL A O   1 
ATOM   5571  C  CB  . VAL A 1 733  ? -9.481   53.835  7.072   1.00 189.31 ? 733  VAL A CB  1 
ATOM   5572  C  CG1 . VAL A 1 733  ? -8.258   54.378  7.794   1.00 191.21 ? 733  VAL A CG1 1 
ATOM   5573  C  CG2 . VAL A 1 733  ? -9.058   53.033  5.846   1.00 187.59 ? 733  VAL A CG2 1 
ATOM   5574  N  N   . VAL A 1 734  ? -11.308  54.671  9.443   1.00 189.00 ? 734  VAL A N   1 
ATOM   5575  C  CA  . VAL A 1 734  ? -11.598  55.358  10.691  1.00 190.27 ? 734  VAL A CA  1 
ATOM   5576  C  C   . VAL A 1 734  ? -11.818  54.375  11.840  1.00 191.68 ? 734  VAL A C   1 
ATOM   5577  O  O   . VAL A 1 734  ? -11.241  54.528  12.918  1.00 194.38 ? 734  VAL A O   1 
ATOM   5578  C  CB  . VAL A 1 734  ? -12.832  56.269  10.541  1.00 189.51 ? 734  VAL A CB  1 
ATOM   5579  C  CG1 . VAL A 1 734  ? -13.304  56.785  11.899  1.00 189.48 ? 734  VAL A CG1 1 
ATOM   5580  C  CG2 . VAL A 1 734  ? -12.522  57.416  9.593   1.00 189.51 ? 734  VAL A CG2 1 
ATOM   5581  N  N   . ALA A 1 735  ? -12.642  53.361  11.601  1.00 189.60 ? 735  ALA A N   1 
ATOM   5582  C  CA  . ALA A 1 735  ? -12.983  52.398  12.644  1.00 189.24 ? 735  ALA A CA  1 
ATOM   5583  C  C   . ALA A 1 735  ? -11.934  51.298  12.789  1.00 189.72 ? 735  ALA A C   1 
ATOM   5584  O  O   . ALA A 1 735  ? -11.974  50.518  13.737  1.00 189.97 ? 735  ALA A O   1 
ATOM   5585  C  CB  . ALA A 1 735  ? -14.360  51.790  12.388  1.00 187.84 ? 735  ALA A CB  1 
ATOM   5586  N  N   . SER A 1 736  ? -10.999  51.226  11.851  1.00 189.76 ? 736  SER A N   1 
ATOM   5587  C  CA  . SER A 1 736  ? -9.974   50.191  11.905  1.00 190.80 ? 736  SER A CA  1 
ATOM   5588  C  C   . SER A 1 736  ? -8.761   50.605  12.733  1.00 192.10 ? 736  SER A C   1 
ATOM   5589  O  O   . SER A 1 736  ? -8.214   49.804  13.499  1.00 193.04 ? 736  SER A O   1 
ATOM   5590  C  CB  . SER A 1 736  ? -9.547   49.794  10.498  1.00 189.81 ? 736  SER A CB  1 
ATOM   5591  O  OG  . SER A 1 736  ? -10.619  49.174  9.815   1.00 188.83 ? 736  SER A OG  1 
ATOM   5592  N  N   . GLN A 1 737  ? -8.340   51.856  12.564  1.00 192.61 ? 737  GLN A N   1 
ATOM   5593  C  CA  . GLN A 1 737  ? -7.248   52.418  13.351  1.00 192.69 ? 737  GLN A CA  1 
ATOM   5594  C  C   . GLN A 1 737  ? -7.737   52.578  14.785  1.00 193.29 ? 737  GLN A C   1 
ATOM   5595  O  O   . GLN A 1 737  ? -6.976   52.430  15.740  1.00 192.45 ? 737  GLN A O   1 
ATOM   5596  C  CB  . GLN A 1 737  ? -6.807   53.774  12.775  1.00 192.36 ? 737  GLN A CB  1 
ATOM   5597  C  CG  . GLN A 1 737  ? -7.152   53.983  11.284  1.00 191.28 ? 737  GLN A CG  1 
ATOM   5598  C  CD  . GLN A 1 737  ? -6.100   53.449  10.316  1.00 191.26 ? 737  GLN A CD  1 
ATOM   5599  O  OE1 . GLN A 1 737  ? -5.026   54.031  10.182  1.00 192.94 ? 737  GLN A OE1 1 
ATOM   5600  N  NE2 . GLN A 1 737  ? -6.420   52.358  9.615   1.00 189.29 ? 737  GLN A NE2 1 
ATOM   5601  N  N   . LEU A 1 738  ? -9.025   52.863  14.923  1.00 195.92 ? 738  LEU A N   1 
ATOM   5602  C  CA  . LEU A 1 738  ? -9.622   53.061  16.229  1.00 200.08 ? 738  LEU A CA  1 
ATOM   5603  C  C   . LEU A 1 738  ? -9.541   51.808  17.092  1.00 206.37 ? 738  LEU A C   1 
ATOM   5604  O  O   . LEU A 1 738  ? -9.438   51.904  18.311  1.00 208.67 ? 738  LEU A O   1 
ATOM   5605  C  CB  . LEU A 1 738  ? -11.079  53.507  16.099  1.00 197.35 ? 738  LEU A CB  1 
ATOM   5606  C  CG  . LEU A 1 738  ? -11.744  53.972  17.400  1.00 195.28 ? 738  LEU A CG  1 
ATOM   5607  C  CD1 . LEU A 1 738  ? -11.473  55.456  17.651  1.00 195.27 ? 738  LEU A CD1 1 
ATOM   5608  C  CD2 . LEU A 1 738  ? -13.238  53.695  17.371  1.00 193.02 ? 738  LEU A CD2 1 
ATOM   5609  N  N   . ARG A 1 739  ? -9.592   50.631  16.482  1.00 210.07 ? 739  ARG A N   1 
ATOM   5610  C  CA  . ARG A 1 739  ? -9.586   49.415  17.290  1.00 217.04 ? 739  ARG A CA  1 
ATOM   5611  C  C   . ARG A 1 739  ? -8.194   49.122  17.835  1.00 219.32 ? 739  ARG A C   1 
ATOM   5612  O  O   . ARG A 1 739  ? -8.026   48.284  18.720  1.00 219.95 ? 739  ARG A O   1 
ATOM   5613  C  CB  . ARG A 1 739  ? -10.165  48.214  16.532  1.00 222.36 ? 739  ARG A CB  1 
ATOM   5614  C  CG  . ARG A 1 739  ? -9.351   47.732  15.359  1.00 228.73 ? 739  ARG A CG  1 
ATOM   5615  C  CD  . ARG A 1 739  ? -10.053  46.560  14.704  1.00 234.58 ? 739  ARG A CD  1 
ATOM   5616  N  NE  . ARG A 1 739  ? -9.329   46.079  13.534  1.00 240.07 ? 739  ARG A NE  1 
ATOM   5617  C  CZ  . ARG A 1 739  ? -9.709   45.047  12.785  1.00 242.88 ? 739  ARG A CZ  1 
ATOM   5618  N  NH1 . ARG A 1 739  ? -10.818  44.374  13.078  1.00 243.41 ? 739  ARG A NH1 1 
ATOM   5619  N  NH2 . ARG A 1 739  ? -8.976   44.688  11.738  1.00 243.67 ? 739  ARG A NH2 1 
ATOM   5620  N  N   . ALA A 1 740  ? -7.201   49.830  17.308  1.00 220.01 ? 740  ALA A N   1 
ATOM   5621  C  CA  . ALA A 1 740  ? -5.838   49.711  17.806  1.00 221.97 ? 740  ALA A CA  1 
ATOM   5622  C  C   . ALA A 1 740  ? -5.676   50.502  19.098  1.00 222.12 ? 740  ALA A C   1 
ATOM   5623  O  O   . ALA A 1 740  ? -4.721   50.294  19.847  1.00 226.08 ? 740  ALA A O   1 
ATOM   5624  C  CB  . ALA A 1 740  ? -4.850   50.196  16.762  1.00 222.26 ? 740  ALA A CB  1 
ATOM   5625  N  N   . ASN A 1 741  ? -6.626   51.400  19.353  1.00 217.36 ? 741  ASN A N   1 
ATOM   5626  C  CA  . ASN A 1 741  ? -6.521   52.375  20.442  1.00 214.37 ? 741  ASN A CA  1 
ATOM   5627  C  C   . ASN A 1 741  ? -7.460   52.190  21.643  1.00 224.25 ? 741  ASN A C   1 
ATOM   5628  O  O   . ASN A 1 741  ? -7.113   52.572  22.761  1.00 226.46 ? 741  ASN A O   1 
ATOM   5629  C  CB  . ASN A 1 741  ? -6.625   53.801  19.885  1.00 201.86 ? 741  ASN A CB  1 
ATOM   5630  C  CG  . ASN A 1 741  ? -5.342   54.245  19.186  1.00 193.24 ? 741  ASN A CG  1 
ATOM   5631  O  OD1 . ASN A 1 741  ? -5.352   54.650  18.017  1.00 189.93 ? 741  ASN A OD1 1 
ATOM   5632  N  ND2 . ASN A 1 741  ? -4.217   54.135  19.899  1.00 189.34 ? 741  ASN A ND2 1 
ATOM   5633  N  N   . ILE A 1 742  ? -8.644   51.625  21.419  1.00 233.43 ? 742  ILE A N   1 
ATOM   5634  C  CA  . ILE A 1 742  ? -9.564   51.337  22.522  1.00 242.40 ? 742  ILE A CA  1 
ATOM   5635  C  C   . ILE A 1 742  ? -8.976   50.221  23.372  1.00 247.41 ? 742  ILE A C   1 
ATOM   5636  O  O   . ILE A 1 742  ? -9.375   50.014  24.520  1.00 248.36 ? 742  ILE A O   1 
ATOM   5637  C  CB  . ILE A 1 742  ? -10.956  50.886  22.021  1.00 243.57 ? 742  ILE A CB  1 
ATOM   5638  C  CG1 . ILE A 1 742  ? -11.439  51.778  20.874  1.00 243.33 ? 742  ILE A CG1 1 
ATOM   5639  C  CG2 . ILE A 1 742  ? -11.960  50.881  23.168  1.00 244.42 ? 742  ILE A CG2 1 
ATOM   5640  C  CD1 . ILE A 1 742  ? -12.744  51.327  20.259  1.00 241.99 ? 742  ILE A CD1 1 
ATOM   5641  N  N   . SER A 1 743  ? -8.012   49.514  22.786  1.00 250.34 ? 743  SER A N   1 
ATOM   5642  C  CA  . SER A 1 743  ? -7.400   48.344  23.401  1.00 252.58 ? 743  SER A CA  1 
ATOM   5643  C  C   . SER A 1 743  ? -5.991   48.118  22.855  1.00 253.01 ? 743  SER A C   1 
ATOM   5644  O  O   . SER A 1 743  ? -5.757   48.208  21.648  1.00 251.32 ? 743  SER A O   1 
ATOM   5645  C  CB  . SER A 1 743  ? -8.263   47.107  23.142  1.00 252.47 ? 743  SER A CB  1 
ATOM   5646  O  OG  . SER A 1 743  ? -8.513   46.946  21.755  1.00 251.16 ? 743  SER A OG  1 
ATOM   5647  N  N   . LEU A 1 749  ? -5.393   39.720  28.007  1.00 243.63 ? 749  LEU A N   1 
ATOM   5648  C  CA  . LEU A 1 749  ? -6.281   38.893  27.194  1.00 242.01 ? 749  LEU A CA  1 
ATOM   5649  C  C   . LEU A 1 749  ? -6.311   39.400  25.759  1.00 241.96 ? 749  LEU A C   1 
ATOM   5650  O  O   . LEU A 1 749  ? -5.627   40.366  25.422  1.00 242.52 ? 749  LEU A O   1 
ATOM   5651  C  CB  . LEU A 1 749  ? -7.698   38.882  27.775  1.00 239.62 ? 749  LEU A CB  1 
ATOM   5652  C  CG  . LEU A 1 749  ? -8.609   37.726  27.360  1.00 236.49 ? 749  LEU A CG  1 
ATOM   5653  C  CD1 . LEU A 1 749  ? -8.003   36.406  27.805  1.00 237.10 ? 749  LEU A CD1 1 
ATOM   5654  C  CD2 . LEU A 1 749  ? -10.002  37.905  27.941  1.00 235.39 ? 749  LEU A CD2 1 
ATOM   5655  N  N   . GLY A 1 750  ? -7.118   38.755  24.923  1.00 242.12 ? 750  GLY A N   1 
ATOM   5656  C  CA  . GLY A 1 750  ? -7.177   39.083  23.510  1.00 242.91 ? 750  GLY A CA  1 
ATOM   5657  C  C   . GLY A 1 750  ? -8.594   39.331  23.037  1.00 244.00 ? 750  GLY A C   1 
ATOM   5658  O  O   . GLY A 1 750  ? -8.925   39.057  21.881  1.00 242.23 ? 750  GLY A O   1 
ATOM   5659  N  N   . ARG A 1 751  ? -9.431   39.841  23.942  1.00 248.27 ? 751  ARG A N   1 
ATOM   5660  C  CA  . ARG A 1 751  ? -10.825  40.163  23.623  1.00 248.74 ? 751  ARG A CA  1 
ATOM   5661  C  C   . ARG A 1 751  ? -11.020  41.622  23.155  1.00 255.73 ? 751  ARG A C   1 
ATOM   5662  O  O   . ARG A 1 751  ? -11.001  42.553  23.967  1.00 256.93 ? 751  ARG A O   1 
ATOM   5663  C  CB  . ARG A 1 751  ? -11.760  39.836  24.809  1.00 242.61 ? 751  ARG A CB  1 
ATOM   5664  C  CG  . ARG A 1 751  ? -11.795  38.352  25.234  1.00 235.72 ? 751  ARG A CG  1 
ATOM   5665  C  CD  . ARG A 1 751  ? -12.246  37.401  24.107  1.00 227.14 ? 751  ARG A CD  1 
ATOM   5666  N  NE  . ARG A 1 751  ? -11.985  35.990  24.417  1.00 221.15 ? 751  ARG A NE  1 
ATOM   5667  C  CZ  . ARG A 1 751  ? -10.998  35.268  23.888  1.00 215.76 ? 751  ARG A CZ  1 
ATOM   5668  N  NH1 . ARG A 1 751  ? -10.171  35.815  23.006  1.00 213.71 ? 751  ARG A NH1 1 
ATOM   5669  N  NH2 . ARG A 1 751  ? -10.837  33.995  24.233  1.00 214.18 ? 751  ARG A NH2 1 
ATOM   5670  N  N   . LEU A 1 752  ? -11.203  41.800  21.842  1.00 259.64 ? 752  LEU A N   1 
ATOM   5671  C  CA  . LEU A 1 752  ? -11.597  43.088  21.250  1.00 263.43 ? 752  LEU A CA  1 
ATOM   5672  C  C   . LEU A 1 752  ? -12.573  42.898  20.081  1.00 261.57 ? 752  LEU A C   1 
ATOM   5673  O  O   . LEU A 1 752  ? -12.333  42.096  19.175  1.00 261.73 ? 752  LEU A O   1 
ATOM   5674  C  CB  . LEU A 1 752  ? -10.386  43.902  20.780  1.00 268.40 ? 752  LEU A CB  1 
ATOM   5675  C  CG  . LEU A 1 752  ? -10.755  45.201  20.049  1.00 271.61 ? 752  LEU A CG  1 
ATOM   5676  C  CD1 . LEU A 1 752  ? -11.259  46.270  21.023  1.00 273.63 ? 752  LEU A CD1 1 
ATOM   5677  C  CD2 . LEU A 1 752  ? -9.585   45.719  19.232  1.00 273.11 ? 752  LEU A CD2 1 
ATOM   5678  N  N   . HIS A 1 753  ? -13.668  43.657  20.111  1.00 258.17 ? 753  HIS A N   1 
ATOM   5679  C  CA  . HIS A 1 753  ? -14.745  43.530  19.136  1.00 253.19 ? 753  HIS A CA  1 
ATOM   5680  C  C   . HIS A 1 753  ? -15.473  44.863  19.001  1.00 242.44 ? 753  HIS A C   1 
ATOM   5681  O  O   . HIS A 1 753  ? -16.337  45.190  19.810  1.00 240.66 ? 753  HIS A O   1 
ATOM   5682  C  CB  . HIS A 1 753  ? -15.754  42.473  19.591  1.00 259.33 ? 753  HIS A CB  1 
ATOM   5683  C  CG  . HIS A 1 753  ? -15.243  41.565  20.672  1.00 266.16 ? 753  HIS A CG  1 
ATOM   5684  N  ND1 . HIS A 1 753  ? -15.376  41.853  22.012  1.00 269.80 ? 753  HIS A ND1 1 
ATOM   5685  C  CD2 . HIS A 1 753  ? -14.610  40.369  20.602  1.00 268.52 ? 753  HIS A CD2 1 
ATOM   5686  C  CE1 . HIS A 1 753  ? -14.842  40.874  22.726  1.00 271.75 ? 753  HIS A CE1 1 
ATOM   5687  N  NE2 . HIS A 1 753  ? -14.371  39.965  21.895  1.00 271.03 ? 753  HIS A NE2 1 
ATOM   5688  N  N   . MET A 1 754  ? -15.130  45.634  17.980  1.00 234.35 ? 754  MET A N   1 
ATOM   5689  C  CA  . MET A 1 754  ? -15.787  46.910  17.764  1.00 226.09 ? 754  MET A CA  1 
ATOM   5690  C  C   . MET A 1 754  ? -17.260  46.662  17.539  1.00 220.21 ? 754  MET A C   1 
ATOM   5691  O  O   . MET A 1 754  ? -17.688  45.512  17.504  1.00 219.97 ? 754  MET A O   1 
ATOM   5692  C  CB  . MET A 1 754  ? -15.204  47.574  16.533  1.00 222.54 ? 754  MET A CB  1 
ATOM   5693  C  CG  . MET A 1 754  ? -13.712  47.397  16.414  1.00 221.09 ? 754  MET A CG  1 
ATOM   5694  S  SD  . MET A 1 754  ? -13.205  47.660  14.718  1.00 196.36 ? 754  MET A SD  1 
ATOM   5695  C  CE  . MET A 1 754  ? -14.592  48.637  14.122  1.00 133.42 ? 754  MET A CE  1 
ATOM   5696  N  N   . LYS A 1 755  ? -18.032  47.736  17.392  1.00 216.03 ? 755  LYS A N   1 
ATOM   5697  C  CA  . LYS A 1 755  ? -19.425  47.643  16.941  1.00 212.88 ? 755  LYS A CA  1 
ATOM   5698  C  C   . LYS A 1 755  ? -20.073  49.015  16.743  1.00 215.33 ? 755  LYS A C   1 
ATOM   5699  O  O   . LYS A 1 755  ? -19.507  50.051  17.102  1.00 213.97 ? 755  LYS A O   1 
ATOM   5700  C  CB  . LYS A 1 755  ? -20.298  46.809  17.901  1.00 209.95 ? 755  LYS A CB  1 
ATOM   5701  C  CG  . LYS A 1 755  ? -20.324  45.286  17.672  1.00 207.04 ? 755  LYS A CG  1 
ATOM   5702  C  CD  . LYS A 1 755  ? -20.317  44.898  16.196  1.00 204.58 ? 755  LYS A CD  1 
ATOM   5703  C  CE  . LYS A 1 755  ? -21.666  45.091  15.529  1.00 203.28 ? 755  LYS A CE  1 
ATOM   5704  N  NZ  . LYS A 1 755  ? -21.619  44.602  14.119  1.00 201.63 ? 755  LYS A NZ  1 
ATOM   5705  N  N   . THR A 1 756  ? -21.263  48.988  16.148  1.00 219.49 ? 756  THR A N   1 
ATOM   5706  C  CA  . THR A 1 756  ? -22.175  50.127  16.091  1.00 224.09 ? 756  THR A CA  1 
ATOM   5707  C  C   . THR A 1 756  ? -23.558  49.587  15.732  1.00 230.40 ? 756  THR A C   1 
ATOM   5708  O  O   . THR A 1 756  ? -23.941  49.547  14.561  1.00 231.29 ? 756  THR A O   1 
ATOM   5709  C  CB  . THR A 1 756  ? -21.730  51.193  15.074  1.00 221.62 ? 756  THR A CB  1 
ATOM   5710  O  OG1 . THR A 1 756  ? -20.459  51.726  15.465  1.00 221.03 ? 756  THR A OG1 1 
ATOM   5711  C  CG2 . THR A 1 756  ? -22.743  52.329  15.018  1.00 220.99 ? 756  THR A CG2 1 
ATOM   5712  N  N   . LEU A 1 757  ? -24.296  49.167  16.756  1.00 235.86 ? 757  LEU A N   1 
ATOM   5713  C  CA  . LEU A 1 757  ? -25.555  48.445  16.579  1.00 242.34 ? 757  LEU A CA  1 
ATOM   5714  C  C   . LEU A 1 757  ? -26.561  49.186  15.699  1.00 246.08 ? 757  LEU A C   1 
ATOM   5715  O  O   . LEU A 1 757  ? -26.612  50.414  15.679  1.00 244.35 ? 757  LEU A O   1 
ATOM   5716  C  CB  . LEU A 1 757  ? -26.183  48.112  17.949  1.00 246.89 ? 757  LEU A CB  1 
ATOM   5717  C  CG  . LEU A 1 757  ? -27.518  47.342  18.021  1.00 251.49 ? 757  LEU A CG  1 
ATOM   5718  C  CD1 . LEU A 1 757  ? -27.345  45.885  17.602  1.00 252.20 ? 757  LEU A CD1 1 
ATOM   5719  C  CD2 . LEU A 1 757  ? -28.160  47.428  19.414  1.00 253.61 ? 757  LEU A CD2 1 
ATOM   5720  N  N   . LEU A 1 758  ? -27.344  48.409  14.962  1.00 251.89 ? 758  LEU A N   1 
ATOM   5721  C  CA  . LEU A 1 758  ? -28.508  48.901  14.248  1.00 256.63 ? 758  LEU A CA  1 
ATOM   5722  C  C   . LEU A 1 758  ? -29.144  47.684  13.621  1.00 269.72 ? 758  LEU A C   1 
ATOM   5723  O  O   . LEU A 1 758  ? -28.700  47.233  12.566  1.00 269.88 ? 758  LEU A O   1 
ATOM   5724  C  CB  . LEU A 1 758  ? -28.119  49.880  13.153  1.00 246.23 ? 758  LEU A CB  1 
ATOM   5725  C  CG  . LEU A 1 758  ? -29.161  50.934  12.772  1.00 236.25 ? 758  LEU A CG  1 
ATOM   5726  C  CD1 . LEU A 1 758  ? -28.852  51.491  11.395  1.00 232.33 ? 758  LEU A CD1 1 
ATOM   5727  C  CD2 . LEU A 1 758  ? -30.576  50.382  12.818  1.00 233.06 ? 758  LEU A CD2 1 
ATOM   5728  N  N   . PRO A 1 759  ? -30.177  47.132  14.281  1.00 281.49 ? 759  PRO A N   1 
ATOM   5729  C  CA  . PRO A 1 759  ? -30.893  45.949  13.787  1.00 289.46 ? 759  PRO A CA  1 
ATOM   5730  C  C   . PRO A 1 759  ? -31.383  46.123  12.349  1.00 296.69 ? 759  PRO A C   1 
ATOM   5731  O  O   . PRO A 1 759  ? -32.061  45.239  11.825  1.00 300.13 ? 759  PRO A O   1 
ATOM   5732  C  CB  . PRO A 1 759  ? -32.084  45.837  14.746  1.00 288.59 ? 759  PRO A CB  1 
ATOM   5733  C  CG  . PRO A 1 759  ? -31.590  46.442  16.019  1.00 286.82 ? 759  PRO A CG  1 
ATOM   5734  C  CD  . PRO A 1 759  ? -30.667  47.562  15.604  1.00 284.22 ? 759  PRO A CD  1 
ATOM   5735  N  N   . VAL A 1 760  ? -31.032  47.251  11.732  1.00 297.26 ? 760  VAL A N   1 
ATOM   5736  C  CA  . VAL A 1 760  ? -31.410  47.564  10.354  1.00 302.45 ? 760  VAL A CA  1 
ATOM   5737  C  C   . VAL A 1 760  ? -32.920  47.791  10.237  1.00 291.78 ? 760  VAL A C   1 
ATOM   5738  O  O   . VAL A 1 760  ? -33.474  47.833  9.136   1.00 292.88 ? 760  VAL A O   1 
ATOM   5739  C  CB  . VAL A 1 760  ? -30.934  46.476  9.361   1.00 321.68 ? 760  VAL A CB  1 
ATOM   5740  C  CG1 . VAL A 1 760  ? -30.970  47.000  7.933   1.00 328.96 ? 760  VAL A CG1 1 
ATOM   5741  C  CG2 . VAL A 1 760  ? -29.525  46.018  9.711   1.00 327.36 ? 760  VAL A CG2 1 
ATOM   5742  N  N   . SER A 1 761  ? -33.573  47.941  11.388  1.00 279.19 ? 761  SER A N   1 
ATOM   5743  C  CA  . SER A 1 761  ? -35.010  48.190  11.450  1.00 264.69 ? 761  SER A CA  1 
ATOM   5744  C  C   . SER A 1 761  ? -35.843  46.937  11.153  1.00 247.68 ? 761  SER A C   1 
ATOM   5745  O  O   . SER A 1 761  ? -36.980  47.048  10.703  1.00 245.77 ? 761  SER A O   1 
ATOM   5746  C  CB  . SER A 1 761  ? -35.399  49.337  10.505  1.00 268.41 ? 761  SER A CB  1 
ATOM   5747  O  OG  . SER A 1 761  ? -36.741  49.744  10.703  1.00 267.02 ? 761  SER A OG  1 
ATOM   5748  N  N   . LYS A 1 762  ? -35.279  45.755  11.406  1.00 230.55 ? 762  LYS A N   1 
ATOM   5749  C  CA  . LYS A 1 762  ? -35.989  44.492  11.179  1.00 210.69 ? 762  LYS A CA  1 
ATOM   5750  C  C   . LYS A 1 762  ? -36.780  44.044  12.397  1.00 199.94 ? 762  LYS A C   1 
ATOM   5751  O  O   . LYS A 1 762  ? -36.245  43.976  13.503  1.00 199.97 ? 762  LYS A O   1 
ATOM   5752  C  CB  . LYS A 1 762  ? -35.027  43.369  10.792  1.00 201.69 ? 762  LYS A CB  1 
ATOM   5753  C  CG  . LYS A 1 762  ? -34.371  43.501  9.429   1.00 193.22 ? 762  LYS A CG  1 
ATOM   5754  C  CD  . LYS A 1 762  ? -33.315  42.414  9.251   1.00 185.00 ? 762  LYS A CD  1 
ATOM   5755  C  CE  . LYS A 1 762  ? -32.397  42.700  8.079   1.00 180.89 ? 762  LYS A CE  1 
ATOM   5756  N  NZ  . LYS A 1 762  ? -31.546  41.521  7.795   1.00 178.61 ? 762  LYS A NZ  1 
ATOM   5757  N  N   . PRO A 1 763  ? -38.066  43.723  12.193  1.00 186.93 ? 763  PRO A N   1 
ATOM   5758  C  CA  . PRO A 1 763  ? -38.896  43.198  13.278  1.00 178.85 ? 763  PRO A CA  1 
ATOM   5759  C  C   . PRO A 1 763  ? -38.557  41.751  13.604  1.00 170.21 ? 763  PRO A C   1 
ATOM   5760  O  O   . PRO A 1 763  ? -39.153  40.848  13.010  1.00 170.31 ? 763  PRO A O   1 
ATOM   5761  C  CB  . PRO A 1 763  ? -40.329  43.276  12.705  1.00 176.53 ? 763  PRO A CB  1 
ATOM   5762  C  CG  . PRO A 1 763  ? -40.249  44.229  11.568  1.00 179.23 ? 763  PRO A CG  1 
ATOM   5763  C  CD  . PRO A 1 763  ? -38.872  44.029  11.001  1.00 184.39 ? 763  PRO A CD  1 
ATOM   5764  N  N   . GLU A 1 764  ? -37.615  41.532  14.521  1.00 162.51 ? 764  GLU A N   1 
ATOM   5765  C  CA  . GLU A 1 764  ? -37.380  40.193  15.059  1.00 152.98 ? 764  GLU A CA  1 
ATOM   5766  C  C   . GLU A 1 764  ? -38.173  40.065  16.334  1.00 142.90 ? 764  GLU A C   1 
ATOM   5767  O  O   . GLU A 1 764  ? -38.623  41.065  16.872  1.00 141.63 ? 764  GLU A O   1 
ATOM   5768  C  CB  . GLU A 1 764  ? -35.902  39.953  15.331  1.00 154.25 ? 764  GLU A CB  1 
ATOM   5769  C  CG  . GLU A 1 764  ? -35.195  41.151  15.894  1.00 155.34 ? 764  GLU A CG  1 
ATOM   5770  C  CD  . GLU A 1 764  ? -33.697  41.072  15.679  1.00 157.92 ? 764  GLU A CD  1 
ATOM   5771  O  OE1 . GLU A 1 764  ? -33.161  39.940  15.630  1.00 157.57 ? 764  GLU A OE1 1 
ATOM   5772  O  OE2 . GLU A 1 764  ? -33.061  42.142  15.552  1.00 159.72 ? 764  GLU A OE2 1 
ATOM   5773  N  N   . ILE A 1 765  ? -38.345  38.843  16.819  1.00 135.03 ? 765  ILE A N   1 
ATOM   5774  C  CA  . ILE A 1 765  ? -39.195  38.631  17.979  1.00 128.88 ? 765  ILE A CA  1 
ATOM   5775  C  C   . ILE A 1 765  ? -38.916  37.299  18.678  1.00 128.30 ? 765  ILE A C   1 
ATOM   5776  O  O   . ILE A 1 765  ? -39.403  36.267  18.238  1.00 130.33 ? 765  ILE A O   1 
ATOM   5777  C  CB  . ILE A 1 765  ? -40.676  38.708  17.558  1.00 122.65 ? 765  ILE A CB  1 
ATOM   5778  C  CG1 . ILE A 1 765  ? -41.600  38.706  18.775  1.00 120.81 ? 765  ILE A CG1 1 
ATOM   5779  C  CG2 . ILE A 1 765  ? -41.015  37.561  16.654  1.00 121.35 ? 765  ILE A CG2 1 
ATOM   5780  C  CD1 . ILE A 1 765  ? -42.872  39.483  18.562  1.00 119.00 ? 765  ILE A CD1 1 
ATOM   5781  N  N   . ARG A 1 766  ? -38.160  37.323  19.779  1.00 126.03 ? 766  ARG A N   1 
ATOM   5782  C  CA  . ARG A 1 766  ? -37.628  36.085  20.362  1.00 123.86 ? 766  ARG A CA  1 
ATOM   5783  C  C   . ARG A 1 766  ? -38.615  35.226  21.159  1.00 124.85 ? 766  ARG A C   1 
ATOM   5784  O  O   . ARG A 1 766  ? -38.205  34.418  21.988  1.00 124.72 ? 766  ARG A O   1 
ATOM   5785  C  CB  . ARG A 1 766  ? -36.400  36.371  21.219  1.00 121.54 ? 766  ARG A CB  1 
ATOM   5786  C  CG  . ARG A 1 766  ? -35.548  37.476  20.702  1.00 120.62 ? 766  ARG A CG  1 
ATOM   5787  C  CD  . ARG A 1 766  ? -34.498  36.973  19.784  1.00 121.76 ? 766  ARG A CD  1 
ATOM   5788  N  NE  . ARG A 1 766  ? -33.686  38.084  19.311  1.00 125.66 ? 766  ARG A NE  1 
ATOM   5789  C  CZ  . ARG A 1 766  ? -32.405  37.984  18.960  1.00 130.92 ? 766  ARG A CZ  1 
ATOM   5790  N  NH1 . ARG A 1 766  ? -31.771  36.819  19.039  1.00 134.26 ? 766  ARG A NH1 1 
ATOM   5791  N  NH2 . ARG A 1 766  ? -31.743  39.048  18.537  1.00 131.85 ? 766  ARG A NH2 1 
ATOM   5792  N  N   . SER A 1 767  ? -39.908  35.381  20.917  1.00 127.02 ? 767  SER A N   1 
ATOM   5793  C  CA  . SER A 1 767  ? -40.880  34.530  21.594  1.00 130.94 ? 767  SER A CA  1 
ATOM   5794  C  C   . SER A 1 767  ? -42.010  34.125  20.660  1.00 132.27 ? 767  SER A C   1 
ATOM   5795  O  O   . SER A 1 767  ? -42.556  34.948  19.928  1.00 132.02 ? 767  SER A O   1 
ATOM   5796  C  CB  . SER A 1 767  ? -41.434  35.207  22.859  1.00 133.72 ? 767  SER A CB  1 
ATOM   5797  O  OG  . SER A 1 767  ? -42.317  36.288  22.576  1.00 134.08 ? 767  SER A OG  1 
ATOM   5798  N  N   . TYR A 1 768  ? -42.355  32.847  20.684  1.00 133.98 ? 768  TYR A N   1 
ATOM   5799  C  CA  . TYR A 1 768  ? -43.358  32.321  19.773  1.00 136.77 ? 768  TYR A CA  1 
ATOM   5800  C  C   . TYR A 1 768  ? -44.722  32.477  20.398  1.00 129.96 ? 768  TYR A C   1 
ATOM   5801  O  O   . TYR A 1 768  ? -44.837  32.528  21.621  1.00 130.64 ? 768  TYR A O   1 
ATOM   5802  C  CB  . TYR A 1 768  ? -43.073  30.839  19.481  1.00 146.42 ? 768  TYR A CB  1 
ATOM   5803  C  CG  . TYR A 1 768  ? -44.071  30.150  18.563  1.00 152.84 ? 768  TYR A CG  1 
ATOM   5804  C  CD1 . TYR A 1 768  ? -43.876  30.125  17.190  1.00 157.52 ? 768  TYR A CD1 1 
ATOM   5805  C  CD2 . TYR A 1 768  ? -45.185  29.505  19.078  1.00 155.32 ? 768  TYR A CD2 1 
ATOM   5806  C  CE1 . TYR A 1 768  ? -44.772  29.499  16.352  1.00 160.25 ? 768  TYR A CE1 1 
ATOM   5807  C  CE2 . TYR A 1 768  ? -46.084  28.876  18.254  1.00 158.24 ? 768  TYR A CE2 1 
ATOM   5808  C  CZ  . TYR A 1 768  ? -45.878  28.874  16.889  1.00 161.08 ? 768  TYR A CZ  1 
ATOM   5809  O  OH  . TYR A 1 768  ? -46.787  28.249  16.060  1.00 162.59 ? 768  TYR A OH  1 
ATOM   5810  N  N   . PHE A 1 769  ? -45.756  32.532  19.564  1.00 123.64 ? 769  PHE A N   1 
ATOM   5811  C  CA  . PHE A 1 769  ? -47.126  32.543  20.061  1.00 118.75 ? 769  PHE A CA  1 
ATOM   5812  C  C   . PHE A 1 769  ? -47.948  31.543  19.292  1.00 117.79 ? 769  PHE A C   1 
ATOM   5813  O  O   . PHE A 1 769  ? -48.174  31.745  18.112  1.00 119.41 ? 769  PHE A O   1 
ATOM   5814  C  CB  . PHE A 1 769  ? -47.773  33.908  19.862  1.00 115.92 ? 769  PHE A CB  1 
ATOM   5815  C  CG  . PHE A 1 769  ? -47.047  35.034  20.525  1.00 113.56 ? 769  PHE A CG  1 
ATOM   5816  C  CD1 . PHE A 1 769  ? -47.075  35.189  21.887  1.00 112.52 ? 769  PHE A CD1 1 
ATOM   5817  C  CD2 . PHE A 1 769  ? -46.347  35.953  19.765  1.00 111.59 ? 769  PHE A CD2 1 
ATOM   5818  C  CE1 . PHE A 1 769  ? -46.401  36.229  22.462  1.00 113.37 ? 769  PHE A CE1 1 
ATOM   5819  C  CE2 . PHE A 1 769  ? -45.683  36.993  20.331  1.00 107.29 ? 769  PHE A CE2 1 
ATOM   5820  C  CZ  . PHE A 1 769  ? -45.702  37.132  21.672  1.00 112.57 ? 769  PHE A CZ  1 
ATOM   5821  N  N   . PRO A 1 770  ? -48.439  30.501  19.975  1.00 117.96 ? 770  PRO A N   1 
ATOM   5822  C  CA  . PRO A 1 770  ? -49.148  29.315  19.483  1.00 121.72 ? 770  PRO A CA  1 
ATOM   5823  C  C   . PRO A 1 770  ? -50.373  29.632  18.656  1.00 126.67 ? 770  PRO A C   1 
ATOM   5824  O  O   . PRO A 1 770  ? -51.088  30.600  18.943  1.00 128.04 ? 770  PRO A O   1 
ATOM   5825  C  CB  . PRO A 1 770  ? -49.610  28.641  20.760  1.00 120.83 ? 770  PRO A CB  1 
ATOM   5826  C  CG  . PRO A 1 770  ? -48.688  29.118  21.793  1.00 120.58 ? 770  PRO A CG  1 
ATOM   5827  C  CD  . PRO A 1 770  ? -48.339  30.507  21.437  1.00 118.78 ? 770  PRO A CD  1 
ATOM   5828  N  N   . GLU A 1 771  ? -50.635  28.806  17.650  1.00 129.32 ? 771  GLU A N   1 
ATOM   5829  C  CA  . GLU A 1 771  ? -51.841  28.995  16.874  1.00 133.04 ? 771  GLU A CA  1 
ATOM   5830  C  C   . GLU A 1 771  ? -53.026  29.039  17.842  1.00 129.85 ? 771  GLU A C   1 
ATOM   5831  O  O   . GLU A 1 771  ? -53.025  28.314  18.842  1.00 128.64 ? 771  GLU A O   1 
ATOM   5832  C  CB  . GLU A 1 771  ? -52.014  27.854  15.872  1.00 140.86 ? 771  GLU A CB  1 
ATOM   5833  C  CG  . GLU A 1 771  ? -53.263  27.985  14.978  1.00 147.36 ? 771  GLU A CG  1 
ATOM   5834  C  CD  . GLU A 1 771  ? -53.395  26.867  13.952  1.00 153.30 ? 771  GLU A CD  1 
ATOM   5835  O  OE1 . GLU A 1 771  ? -53.652  27.175  12.764  1.00 154.38 ? 771  GLU A OE1 1 
ATOM   5836  O  OE2 . GLU A 1 771  ? -53.237  25.687  14.337  1.00 156.13 ? 771  GLU A OE2 1 
ATOM   5837  N  N   . SER A 1 772  ? -54.012  29.894  17.542  1.00 128.85 ? 772  SER A N   1 
ATOM   5838  C  CA  . SER A 1 772  ? -55.237  30.052  18.350  1.00 126.21 ? 772  SER A CA  1 
ATOM   5839  C  C   . SER A 1 772  ? -56.280  28.956  18.095  1.00 122.95 ? 772  SER A C   1 
ATOM   5840  O  O   . SER A 1 772  ? -56.114  28.141  17.197  1.00 123.40 ? 772  SER A O   1 
ATOM   5841  C  CB  . SER A 1 772  ? -55.872  31.444  18.145  1.00 125.99 ? 772  SER A CB  1 
ATOM   5842  O  OG  . SER A 1 772  ? -55.077  32.497  18.670  1.00 125.87 ? 772  SER A OG  1 
ATOM   5843  N  N   . TRP A 1 773  ? -57.365  28.962  18.868  1.00 120.64 ? 773  TRP A N   1 
ATOM   5844  C  CA  . TRP A 1 773  ? -58.375  27.904  18.783  1.00 122.71 ? 773  TRP A CA  1 
ATOM   5845  C  C   . TRP A 1 773  ? -59.728  28.260  19.398  1.00 126.61 ? 773  TRP A C   1 
ATOM   5846  O  O   . TRP A 1 773  ? -59.881  29.317  19.994  1.00 129.38 ? 773  TRP A O   1 
ATOM   5847  C  CB  . TRP A 1 773  ? -57.856  26.666  19.467  1.00 122.64 ? 773  TRP A CB  1 
ATOM   5848  C  CG  . TRP A 1 773  ? -57.469  26.902  20.883  1.00 122.50 ? 773  TRP A CG  1 
ATOM   5849  C  CD1 . TRP A 1 773  ? -56.361  27.561  21.336  1.00 122.66 ? 773  TRP A CD1 1 
ATOM   5850  C  CD2 . TRP A 1 773  ? -58.175  26.460  22.044  1.00 123.95 ? 773  TRP A CD2 1 
ATOM   5851  N  NE1 . TRP A 1 773  ? -56.337  27.562  22.708  1.00 122.51 ? 773  TRP A NE1 1 
ATOM   5852  C  CE2 . TRP A 1 773  ? -57.440  26.891  23.166  1.00 123.29 ? 773  TRP A CE2 1 
ATOM   5853  C  CE3 . TRP A 1 773  ? -59.357  25.739  22.245  1.00 123.99 ? 773  TRP A CE3 1 
ATOM   5854  C  CZ2 . TRP A 1 773  ? -57.850  26.625  24.467  1.00 124.09 ? 773  TRP A CZ2 1 
ATOM   5855  C  CZ3 . TRP A 1 773  ? -59.761  25.476  23.536  1.00 124.38 ? 773  TRP A CZ3 1 
ATOM   5856  C  CH2 . TRP A 1 773  ? -59.010  25.913  24.630  1.00 124.56 ? 773  TRP A CH2 1 
ATOM   5857  N  N   . LEU A 1 774  ? -60.701  27.361  19.282  1.00 128.57 ? 774  LEU A N   1 
ATOM   5858  C  CA  . LEU A 1 774  ? -62.089  27.687  19.635  1.00 129.92 ? 774  LEU A CA  1 
ATOM   5859  C  C   . LEU A 1 774  ? -62.653  28.811  18.761  1.00 127.51 ? 774  LEU A C   1 
ATOM   5860  O  O   . LEU A 1 774  ? -63.534  29.566  19.196  1.00 124.63 ? 774  LEU A O   1 
ATOM   5861  C  CB  . LEU A 1 774  ? -62.249  28.025  21.120  1.00 132.46 ? 774  LEU A CB  1 
ATOM   5862  C  CG  . LEU A 1 774  ? -63.024  26.968  21.906  1.00 137.13 ? 774  LEU A CG  1 
ATOM   5863  C  CD1 . LEU A 1 774  ? -63.441  27.449  23.287  1.00 137.34 ? 774  LEU A CD1 1 
ATOM   5864  C  CD2 . LEU A 1 774  ? -64.244  26.600  21.105  1.00 139.25 ? 774  LEU A CD2 1 
ATOM   5865  N  N   . TRP A 1 775  ? -62.136  28.878  17.527  1.00 127.36 ? 775  TRP A N   1 
ATOM   5866  C  CA  . TRP A 1 775  ? -62.469  29.894  16.529  1.00 124.75 ? 775  TRP A CA  1 
ATOM   5867  C  C   . TRP A 1 775  ? -63.795  29.608  15.816  1.00 126.58 ? 775  TRP A C   1 
ATOM   5868  O  O   . TRP A 1 775  ? -64.035  30.118  14.725  1.00 125.68 ? 775  TRP A O   1 
ATOM   5869  C  CB  . TRP A 1 775  ? -61.319  30.006  15.524  1.00 122.25 ? 775  TRP A CB  1 
ATOM   5870  C  CG  . TRP A 1 775  ? -61.433  31.125  14.533  1.00 122.00 ? 775  TRP A CG  1 
ATOM   5871  C  CD1 . TRP A 1 775  ? -61.840  31.019  13.244  1.00 124.74 ? 775  TRP A CD1 1 
ATOM   5872  C  CD2 . TRP A 1 775  ? -61.103  32.510  14.730  1.00 121.22 ? 775  TRP A CD2 1 
ATOM   5873  N  NE1 . TRP A 1 775  ? -61.807  32.249  12.622  1.00 124.15 ? 775  TRP A NE1 1 
ATOM   5874  C  CE2 . TRP A 1 775  ? -61.353  33.179  13.514  1.00 121.43 ? 775  TRP A CE2 1 
ATOM   5875  C  CE3 . TRP A 1 775  ? -60.639  33.250  15.817  1.00 120.35 ? 775  TRP A CE3 1 
ATOM   5876  C  CZ2 . TRP A 1 775  ? -61.154  34.544  13.355  1.00 119.99 ? 775  TRP A CZ2 1 
ATOM   5877  C  CZ3 . TRP A 1 775  ? -60.435  34.603  15.654  1.00 119.52 ? 775  TRP A CZ3 1 
ATOM   5878  C  CH2 . TRP A 1 775  ? -60.690  35.235  14.432  1.00 119.54 ? 775  TRP A CH2 1 
ATOM   5879  N  N   . GLU A 1 776  ? -64.653  28.812  16.456  1.00 129.97 ? 776  GLU A N   1 
ATOM   5880  C  CA  . GLU A 1 776  ? -65.976  28.457  15.931  1.00 134.48 ? 776  GLU A CA  1 
ATOM   5881  C  C   . GLU A 1 776  ? -67.065  29.500  16.195  1.00 134.45 ? 776  GLU A C   1 
ATOM   5882  O  O   . GLU A 1 776  ? -67.006  30.193  17.191  1.00 132.96 ? 776  GLU A O   1 
ATOM   5883  C  CB  . GLU A 1 776  ? -66.421  27.121  16.526  1.00 140.41 ? 776  GLU A CB  1 
ATOM   5884  C  CG  . GLU A 1 776  ? -65.812  26.788  17.879  1.00 144.89 ? 776  GLU A CG  1 
ATOM   5885  C  CD  . GLU A 1 776  ? -65.877  25.292  18.185  1.00 151.77 ? 776  GLU A CD  1 
ATOM   5886  O  OE1 . GLU A 1 776  ? -64.964  24.762  18.866  1.00 152.83 ? 776  GLU A OE1 1 
ATOM   5887  O  OE2 . GLU A 1 776  ? -66.841  24.638  17.723  1.00 155.69 ? 776  GLU A OE2 1 
ATOM   5888  N  N   . VAL A 1 777  ? -68.048  29.618  15.300  1.00 135.84 ? 777  VAL A N   1 
ATOM   5889  C  CA  . VAL A 1 777  ? -69.287  30.356  15.586  1.00 134.25 ? 777  VAL A CA  1 
ATOM   5890  C  C   . VAL A 1 777  ? -70.260  29.384  16.243  1.00 143.43 ? 777  VAL A C   1 
ATOM   5891  O  O   . VAL A 1 777  ? -70.026  28.182  16.219  1.00 146.74 ? 777  VAL A O   1 
ATOM   5892  C  CB  . VAL A 1 777  ? -69.919  30.929  14.312  1.00 125.79 ? 777  VAL A CB  1 
ATOM   5893  C  CG1 . VAL A 1 777  ? -71.406  31.207  14.513  1.00 120.39 ? 777  VAL A CG1 1 
ATOM   5894  C  CG2 . VAL A 1 777  ? -69.175  32.180  13.870  1.00 121.53 ? 777  VAL A CG2 1 
ATOM   5895  N  N   . HIS A 1 778  ? -71.338  29.880  16.835  1.00 148.69 ? 778  HIS A N   1 
ATOM   5896  C  CA  . HIS A 1 778  ? -72.310  28.994  17.458  1.00 156.16 ? 778  HIS A CA  1 
ATOM   5897  C  C   . HIS A 1 778  ? -73.650  29.682  17.529  1.00 168.27 ? 778  HIS A C   1 
ATOM   5898  O  O   . HIS A 1 778  ? -73.714  30.908  17.516  1.00 167.11 ? 778  HIS A O   1 
ATOM   5899  C  CB  . HIS A 1 778  ? -71.889  28.652  18.884  1.00 153.74 ? 778  HIS A CB  1 
ATOM   5900  C  CG  . HIS A 1 778  ? -70.963  27.476  19.001  1.00 152.44 ? 778  HIS A CG  1 
ATOM   5901  N  ND1 . HIS A 1 778  ? -71.375  26.250  19.484  1.00 153.06 ? 778  HIS A ND1 1 
ATOM   5902  C  CD2 . HIS A 1 778  ? -69.637  27.352  18.752  1.00 150.85 ? 778  HIS A CD2 1 
ATOM   5903  C  CE1 . HIS A 1 778  ? -70.349  25.418  19.503  1.00 152.72 ? 778  HIS A CE1 1 
ATOM   5904  N  NE2 . HIS A 1 778  ? -69.282  26.063  19.066  1.00 151.33 ? 778  HIS A NE2 1 
ATOM   5905  N  N   . LEU A 1 779  ? -74.719  28.896  17.619  1.00 180.83 ? 779  LEU A N   1 
ATOM   5906  C  CA  . LEU A 1 779  ? -76.056  29.452  17.815  1.00 191.71 ? 779  LEU A CA  1 
ATOM   5907  C  C   . LEU A 1 779  ? -76.573  29.233  19.219  1.00 199.71 ? 779  LEU A C   1 
ATOM   5908  O  O   . LEU A 1 779  ? -77.179  28.200  19.502  1.00 203.12 ? 779  LEU A O   1 
ATOM   5909  C  CB  . LEU A 1 779  ? -77.056  28.818  16.868  1.00 194.90 ? 779  LEU A CB  1 
ATOM   5910  C  CG  . LEU A 1 779  ? -78.418  29.416  17.184  1.00 195.96 ? 779  LEU A CG  1 
ATOM   5911  C  CD1 . LEU A 1 779  ? -78.445  30.849  16.690  1.00 195.30 ? 779  LEU A CD1 1 
ATOM   5912  C  CD2 . LEU A 1 779  ? -79.531  28.605  16.566  1.00 198.32 ? 779  LEU A CD2 1 
ATOM   5913  N  N   . VAL A 1 780  ? -76.373  30.210  20.092  1.00 203.57 ? 780  VAL A N   1 
ATOM   5914  C  CA  . VAL A 1 780  ? -76.757  30.025  21.483  1.00 210.08 ? 780  VAL A CA  1 
ATOM   5915  C  C   . VAL A 1 780  ? -78.075  30.696  21.853  1.00 208.26 ? 780  VAL A C   1 
ATOM   5916  O  O   . VAL A 1 780  ? -78.148  31.915  22.014  1.00 205.67 ? 780  VAL A O   1 
ATOM   5917  C  CB  . VAL A 1 780  ? -75.653  30.483  22.440  1.00 215.33 ? 780  VAL A CB  1 
ATOM   5918  C  CG1 . VAL A 1 780  ? -76.116  30.345  23.883  1.00 220.96 ? 780  VAL A CG1 1 
ATOM   5919  C  CG2 . VAL A 1 780  ? -74.395  29.670  22.195  1.00 218.97 ? 780  VAL A CG2 1 
ATOM   5920  N  N   . PRO A 1 781  ? -79.127  29.889  21.983  1.00 211.34 ? 781  PRO A N   1 
ATOM   5921  C  CA  . PRO A 1 781  ? -80.413  30.388  22.450  1.00 211.48 ? 781  PRO A CA  1 
ATOM   5922  C  C   . PRO A 1 781  ? -80.361  30.453  23.954  1.00 211.11 ? 781  PRO A C   1 
ATOM   5923  O  O   . PRO A 1 781  ? -80.702  29.476  24.606  1.00 213.56 ? 781  PRO A O   1 
ATOM   5924  C  CB  . PRO A 1 781  ? -81.385  29.291  22.018  1.00 215.45 ? 781  PRO A CB  1 
ATOM   5925  C  CG  . PRO A 1 781  ? -80.600  28.400  21.083  1.00 216.65 ? 781  PRO A CG  1 
ATOM   5926  C  CD  . PRO A 1 781  ? -79.206  28.486  21.565  1.00 214.60 ? 781  PRO A CD  1 
ATOM   5927  N  N   . ARG A 1 782  ? -79.911  31.578  24.492  1.00 208.67 ? 782  ARG A N   1 
ATOM   5928  C  CA  . ARG A 1 782  ? -79.903  31.797  25.938  1.00 209.28 ? 782  ARG A CA  1 
ATOM   5929  C  C   . ARG A 1 782  ? -79.021  30.815  26.717  1.00 205.83 ? 782  ARG A C   1 
ATOM   5930  O  O   . ARG A 1 782  ? -78.785  31.014  27.907  1.00 206.24 ? 782  ARG A O   1 
ATOM   5931  C  CB  . ARG A 1 782  ? -81.333  31.776  26.502  1.00 216.20 ? 782  ARG A CB  1 
ATOM   5932  C  CG  . ARG A 1 782  ? -82.286  32.799  25.880  1.00 222.47 ? 782  ARG A CG  1 
ATOM   5933  C  CD  . ARG A 1 782  ? -83.642  32.823  26.598  1.00 230.07 ? 782  ARG A CD  1 
ATOM   5934  N  NE  . ARG A 1 782  ? -84.387  31.573  26.450  1.00 236.73 ? 782  ARG A NE  1 
ATOM   5935  C  CZ  . ARG A 1 782  ? -85.569  31.327  27.013  1.00 241.67 ? 782  ARG A CZ  1 
ATOM   5936  N  NH1 . ARG A 1 782  ? -86.155  32.244  27.772  1.00 242.86 ? 782  ARG A NH1 1 
ATOM   5937  N  NH2 . ARG A 1 782  ? -86.169  30.159  26.818  1.00 244.40 ? 782  ARG A NH2 1 
ATOM   5938  N  N   . ARG A 1 783  ? -78.540  29.767  26.052  1.00 201.94 ? 783  ARG A N   1 
ATOM   5939  C  CA  . ARG A 1 783  ? -77.709  28.744  26.693  1.00 198.86 ? 783  ARG A CA  1 
ATOM   5940  C  C   . ARG A 1 783  ? -77.064  27.842  25.656  1.00 194.19 ? 783  ARG A C   1 
ATOM   5941  O  O   . ARG A 1 783  ? -77.628  27.606  24.592  1.00 194.64 ? 783  ARG A O   1 
ATOM   5942  C  CB  . ARG A 1 783  ? -78.543  27.854  27.621  1.00 202.08 ? 783  ARG A CB  1 
ATOM   5943  C  CG  . ARG A 1 783  ? -78.803  28.389  29.012  1.00 203.10 ? 783  ARG A CG  1 
ATOM   5944  C  CD  . ARG A 1 783  ? -79.993  27.675  29.630  1.00 206.29 ? 783  ARG A CD  1 
ATOM   5945  N  NE  . ARG A 1 783  ? -80.844  28.613  30.358  1.00 207.86 ? 783  ARG A NE  1 
ATOM   5946  C  CZ  . ARG A 1 783  ? -82.138  28.423  30.604  1.00 209.65 ? 783  ARG A CZ  1 
ATOM   5947  N  NH1 . ARG A 1 783  ? -82.738  27.318  30.176  1.00 211.13 ? 783  ARG A NH1 1 
ATOM   5948  N  NH2 . ARG A 1 783  ? -82.832  29.340  31.275  1.00 209.21 ? 783  ARG A NH2 1 
ATOM   5949  N  N   . LYS A 1 784  ? -75.882  27.336  25.979  1.00 189.35 ? 784  LYS A N   1 
ATOM   5950  C  CA  . LYS A 1 784  ? -75.240  26.271  25.218  1.00 185.68 ? 784  LYS A CA  1 
ATOM   5951  C  C   . LYS A 1 784  ? -73.915  25.984  25.888  1.00 183.05 ? 784  LYS A C   1 
ATOM   5952  O  O   . LYS A 1 784  ? -73.208  26.902  26.286  1.00 182.26 ? 784  LYS A O   1 
ATOM   5953  C  CB  . LYS A 1 784  ? -75.015  26.648  23.748  1.00 183.41 ? 784  LYS A CB  1 
ATOM   5954  C  CG  . LYS A 1 784  ? -74.521  25.471  22.873  1.00 182.80 ? 784  LYS A CG  1 
ATOM   5955  C  CD  . LYS A 1 784  ? -74.428  25.815  21.367  1.00 180.00 ? 784  LYS A CD  1 
ATOM   5956  C  CE  . LYS A 1 784  ? -74.049  24.590  20.509  1.00 178.82 ? 784  LYS A CE  1 
ATOM   5957  N  NZ  . LYS A 1 784  ? -73.960  24.885  19.042  1.00 176.58 ? 784  LYS A NZ  1 
ATOM   5958  N  N   . GLN A 1 785  ? -73.579  24.707  26.005  1.00 181.35 ? 785  GLN A N   1 
ATOM   5959  C  CA  . GLN A 1 785  ? -72.390  24.285  26.725  1.00 178.58 ? 785  GLN A CA  1 
ATOM   5960  C  C   . GLN A 1 785  ? -71.656  23.258  25.892  1.00 175.81 ? 785  GLN A C   1 
ATOM   5961  O  O   . GLN A 1 785  ? -72.272  22.339  25.372  1.00 175.56 ? 785  GLN A O   1 
ATOM   5962  C  CB  . GLN A 1 785  ? -72.798  23.666  28.051  1.00 181.38 ? 785  GLN A CB  1 
ATOM   5963  C  CG  . GLN A 1 785  ? -71.684  22.939  28.754  1.00 184.23 ? 785  GLN A CG  1 
ATOM   5964  C  CD  . GLN A 1 785  ? -72.190  22.172  29.948  1.00 188.75 ? 785  GLN A CD  1 
ATOM   5965  O  OE1 . GLN A 1 785  ? -73.270  21.585  29.902  1.00 191.30 ? 785  GLN A OE1 1 
ATOM   5966  N  NE2 . GLN A 1 785  ? -71.417  22.172  31.029  1.00 189.56 ? 785  GLN A NE2 1 
ATOM   5967  N  N   . LEU A 1 786  ? -70.344  23.392  25.764  1.00 174.10 ? 786  LEU A N   1 
ATOM   5968  C  CA  . LEU A 1 786  ? -69.648  22.579  24.776  1.00 174.64 ? 786  LEU A CA  1 
ATOM   5969  C  C   . LEU A 1 786  ? -68.264  22.143  25.208  1.00 176.79 ? 786  LEU A C   1 
ATOM   5970  O  O   . LEU A 1 786  ? -67.266  22.707  24.774  1.00 177.49 ? 786  LEU A O   1 
ATOM   5971  C  CB  . LEU A 1 786  ? -69.571  23.311  23.433  1.00 170.63 ? 786  LEU A CB  1 
ATOM   5972  C  CG  . LEU A 1 786  ? -69.144  24.777  23.455  1.00 165.50 ? 786  LEU A CG  1 
ATOM   5973  C  CD1 . LEU A 1 786  ? -68.980  25.337  22.057  1.00 162.88 ? 786  LEU A CD1 1 
ATOM   5974  C  CD2 . LEU A 1 786  ? -70.154  25.588  24.214  1.00 163.99 ? 786  LEU A CD2 1 
ATOM   5975  N  N   . GLN A 1 787  ? -68.217  21.098  26.026  1.00 177.94 ? 787  GLN A N   1 
ATOM   5976  C  CA  . GLN A 1 787  ? -66.962  20.599  26.570  1.00 177.97 ? 787  GLN A CA  1 
ATOM   5977  C  C   . GLN A 1 787  ? -65.872  20.376  25.514  1.00 173.53 ? 787  GLN A C   1 
ATOM   5978  O  O   . GLN A 1 787  ? -66.135  20.376  24.307  1.00 172.32 ? 787  GLN A O   1 
ATOM   5979  C  CB  . GLN A 1 787  ? -67.202  19.327  27.394  1.00 184.27 ? 787  GLN A CB  1 
ATOM   5980  C  CG  . GLN A 1 787  ? -67.936  18.220  26.654  1.00 190.72 ? 787  GLN A CG  1 
ATOM   5981  C  CD  . GLN A 1 787  ? -68.425  17.130  27.587  1.00 197.63 ? 787  GLN A CD  1 
ATOM   5982  O  OE1 . GLN A 1 787  ? -68.488  15.958  27.213  1.00 201.16 ? 787  GLN A OE1 1 
ATOM   5983  N  NE2 . GLN A 1 787  ? -68.770  17.511  28.813  1.00 199.07 ? 787  GLN A NE2 1 
ATOM   5984  N  N   . PHE A 1 788  ? -64.648  20.212  26.012  1.00 170.63 ? 788  PHE A N   1 
ATOM   5985  C  CA  . PHE A 1 788  ? -63.443  19.943  25.227  1.00 165.98 ? 788  PHE A CA  1 
ATOM   5986  C  C   . PHE A 1 788  ? -62.262  19.988  26.206  1.00 163.00 ? 788  PHE A C   1 
ATOM   5987  O  O   . PHE A 1 788  ? -62.340  20.677  27.218  1.00 164.79 ? 788  PHE A O   1 
ATOM   5988  C  CB  . PHE A 1 788  ? -63.277  20.971  24.100  1.00 161.59 ? 788  PHE A CB  1 
ATOM   5989  C  CG  . PHE A 1 788  ? -63.211  22.410  24.572  1.00 157.09 ? 788  PHE A CG  1 
ATOM   5990  C  CD1 . PHE A 1 788  ? -62.015  22.963  25.009  1.00 155.07 ? 788  PHE A CD1 1 
ATOM   5991  C  CD2 . PHE A 1 788  ? -64.331  23.220  24.547  1.00 154.39 ? 788  PHE A CD2 1 
ATOM   5992  C  CE1 . PHE A 1 788  ? -61.946  24.282  25.429  1.00 151.65 ? 788  PHE A CE1 1 
ATOM   5993  C  CE2 . PHE A 1 788  ? -64.260  24.546  24.968  1.00 151.27 ? 788  PHE A CE2 1 
ATOM   5994  C  CZ  . PHE A 1 788  ? -63.073  25.070  25.405  1.00 149.95 ? 788  PHE A CZ  1 
ATOM   5995  N  N   . ALA A 1 789  ? -61.188  19.249  25.954  1.00 158.13 ? 789  ALA A N   1 
ATOM   5996  C  CA  . ALA A 1 789  ? -60.011  19.395  26.810  1.00 153.01 ? 789  ALA A CA  1 
ATOM   5997  C  C   . ALA A 1 789  ? -59.038  20.378  26.179  1.00 148.68 ? 789  ALA A C   1 
ATOM   5998  O  O   . ALA A 1 789  ? -58.798  20.331  24.975  1.00 147.45 ? 789  ALA A O   1 
ATOM   5999  C  CB  . ALA A 1 789  ? -59.342  18.058  27.055  1.00 155.11 ? 789  ALA A CB  1 
ATOM   6000  N  N   . LEU A 1 790  ? -58.489  21.287  26.969  1.00 146.06 ? 790  LEU A N   1 
ATOM   6001  C  CA  . LEU A 1 790  ? -57.630  22.311  26.388  1.00 144.82 ? 790  LEU A CA  1 
ATOM   6002  C  C   . LEU A 1 790  ? -56.229  21.777  26.076  1.00 147.44 ? 790  LEU A C   1 
ATOM   6003  O  O   . LEU A 1 790  ? -55.798  20.777  26.649  1.00 146.38 ? 790  LEU A O   1 
ATOM   6004  C  CB  . LEU A 1 790  ? -57.634  23.600  27.226  1.00 140.85 ? 790  LEU A CB  1 
ATOM   6005  C  CG  . LEU A 1 790  ? -58.444  23.606  28.527  1.00 138.35 ? 790  LEU A CG  1 
ATOM   6006  C  CD1 . LEU A 1 790  ? -57.640  23.039  29.683  1.00 139.23 ? 790  LEU A CD1 1 
ATOM   6007  C  CD2 . LEU A 1 790  ? -58.903  24.999  28.871  1.00 134.54 ? 790  LEU A CD2 1 
ATOM   6008  N  N   . PRO A 1 791  ? -55.522  22.448  25.156  1.00 153.44 ? 791  PRO A N   1 
ATOM   6009  C  CA  . PRO A 1 791  ? -54.329  21.906  24.502  1.00 160.22 ? 791  PRO A CA  1 
ATOM   6010  C  C   . PRO A 1 791  ? -53.191  21.686  25.463  1.00 168.80 ? 791  PRO A C   1 
ATOM   6011  O  O   . PRO A 1 791  ? -52.954  22.523  26.328  1.00 171.94 ? 791  PRO A O   1 
ATOM   6012  C  CB  . PRO A 1 791  ? -53.917  23.017  23.533  1.00 157.20 ? 791  PRO A CB  1 
ATOM   6013  C  CG  . PRO A 1 791  ? -55.039  23.996  23.526  1.00 154.26 ? 791  PRO A CG  1 
ATOM   6014  C  CD  . PRO A 1 791  ? -55.727  23.864  24.825  1.00 152.60 ? 791  PRO A CD  1 
ATOM   6015  N  N   . ASP A 1 792  ? -52.479  20.582  25.294  1.00 175.11 ? 792  ASP A N   1 
ATOM   6016  C  CA  . ASP A 1 792  ? -51.260  20.349  26.048  1.00 181.97 ? 792  ASP A CA  1 
ATOM   6017  C  C   . ASP A 1 792  ? -50.285  21.481  25.740  1.00 176.19 ? 792  ASP A C   1 
ATOM   6018  O  O   . ASP A 1 792  ? -49.561  21.408  24.751  1.00 174.78 ? 792  ASP A O   1 
ATOM   6019  C  CB  . ASP A 1 792  ? -50.652  18.993  25.641  1.00 197.50 ? 792  ASP A CB  1 
ATOM   6020  C  CG  . ASP A 1 792  ? -49.453  18.579  26.511  1.00 216.31 ? 792  ASP A CG  1 
ATOM   6021  O  OD1 . ASP A 1 792  ? -48.854  19.449  27.187  1.00 223.93 ? 792  ASP A OD1 1 
ATOM   6022  O  OD2 . ASP A 1 792  ? -49.109  17.371  26.508  1.00 226.79 ? 792  ASP A OD2 1 
ATOM   6023  N  N   . SER A 1 793  ? -50.263  22.527  26.564  1.00 171.92 ? 793  SER A N   1 
ATOM   6024  C  CA  . SER A 1 793  ? -49.279  23.596  26.379  1.00 165.45 ? 793  SER A CA  1 
ATOM   6025  C  C   . SER A 1 793  ? -49.317  24.698  27.417  1.00 158.17 ? 793  SER A C   1 
ATOM   6026  O  O   . SER A 1 793  ? -50.376  25.244  27.724  1.00 157.56 ? 793  SER A O   1 
ATOM   6027  C  CB  . SER A 1 793  ? -49.411  24.245  25.008  1.00 163.49 ? 793  SER A CB  1 
ATOM   6028  O  OG  . SER A 1 793  ? -48.555  25.365  24.923  1.00 160.65 ? 793  SER A OG  1 
ATOM   6029  N  N   . LEU A 1 794  ? -48.135  25.036  27.923  1.00 151.32 ? 794  LEU A N   1 
ATOM   6030  C  CA  . LEU A 1 794  ? -47.947  26.146  28.845  1.00 144.77 ? 794  LEU A CA  1 
ATOM   6031  C  C   . LEU A 1 794  ? -48.349  27.446  28.180  1.00 142.71 ? 794  LEU A C   1 
ATOM   6032  O  O   . LEU A 1 794  ? -47.505  28.099  27.573  1.00 145.33 ? 794  LEU A O   1 
ATOM   6033  C  CB  . LEU A 1 794  ? -46.463  26.281  29.198  1.00 143.69 ? 794  LEU A CB  1 
ATOM   6034  C  CG  . LEU A 1 794  ? -45.751  25.458  30.279  1.00 145.80 ? 794  LEU A CG  1 
ATOM   6035  C  CD1 . LEU A 1 794  ? -46.278  24.025  30.347  1.00 147.12 ? 794  LEU A CD1 1 
ATOM   6036  C  CD2 . LEU A 1 794  ? -44.215  25.505  30.082  1.00 146.89 ? 794  LEU A CD2 1 
ATOM   6037  N  N   . THR A 1 795  ? -49.614  27.844  28.316  1.00 139.56 ? 795  THR A N   1 
ATOM   6038  C  CA  . THR A 1 795  ? -50.105  29.108  27.743  1.00 134.18 ? 795  THR A CA  1 
ATOM   6039  C  C   . THR A 1 795  ? -51.285  29.675  28.550  1.00 131.03 ? 795  THR A C   1 
ATOM   6040  O  O   . THR A 1 795  ? -52.138  28.919  29.009  1.00 127.95 ? 795  THR A O   1 
ATOM   6041  C  CB  . THR A 1 795  ? -50.522  28.929  26.256  1.00 190.34 ? 795  THR A CB  1 
ATOM   6042  O  OG1 . THR A 1 795  ? -50.941  27.575  26.032  1.00 191.24 ? 795  THR A OG1 1 
ATOM   6043  C  CG2 . THR A 1 795  ? -49.358  29.244  25.326  1.00 190.20 ? 795  THR A CG2 1 
ATOM   6044  N  N   . THR A 1 796  ? -51.329  30.990  28.754  1.00 129.32 ? 796  THR A N   1 
ATOM   6045  C  CA  . THR A 1 796  ? -52.520  31.583  29.359  1.00 128.26 ? 796  THR A CA  1 
ATOM   6046  C  C   . THR A 1 796  ? -53.532  31.910  28.284  1.00 131.11 ? 796  THR A C   1 
ATOM   6047  O  O   . THR A 1 796  ? -53.468  32.959  27.641  1.00 132.30 ? 796  THR A O   1 
ATOM   6048  C  CB  . THR A 1 796  ? -52.242  32.852  30.116  1.00 125.25 ? 796  THR A CB  1 
ATOM   6049  O  OG1 . THR A 1 796  ? -51.353  32.570  31.192  1.00 126.42 ? 796  THR A OG1 1 
ATOM   6050  C  CG2 . THR A 1 796  ? -53.544  33.384  30.687  1.00 122.77 ? 796  THR A CG2 1 
ATOM   6051  N  N   . TRP A 1 797  ? -54.472  30.998  28.089  1.00 131.08 ? 797  TRP A N   1 
ATOM   6052  C  CA  . TRP A 1 797  ? -55.449  31.144  27.026  1.00 128.44 ? 797  TRP A CA  1 
ATOM   6053  C  C   . TRP A 1 797  ? -56.454  32.218  27.385  1.00 122.69 ? 797  TRP A C   1 
ATOM   6054  O  O   . TRP A 1 797  ? -57.352  31.979  28.195  1.00 122.14 ? 797  TRP A O   1 
ATOM   6055  C  CB  . TRP A 1 797  ? -56.203  29.830  26.816  1.00 132.39 ? 797  TRP A CB  1 
ATOM   6056  C  CG  . TRP A 1 797  ? -55.399  28.719  26.224  1.00 138.40 ? 797  TRP A CG  1 
ATOM   6057  C  CD1 . TRP A 1 797  ? -55.284  27.446  26.704  1.00 142.22 ? 797  TRP A CD1 1 
ATOM   6058  C  CD2 . TRP A 1 797  ? -54.610  28.772  25.035  1.00 141.41 ? 797  TRP A CD2 1 
ATOM   6059  N  NE1 . TRP A 1 797  ? -54.470  26.705  25.890  1.00 145.53 ? 797  TRP A NE1 1 
ATOM   6060  C  CE2 . TRP A 1 797  ? -54.043  27.497  24.855  1.00 145.29 ? 797  TRP A CE2 1 
ATOM   6061  C  CE3 . TRP A 1 797  ? -54.324  29.774  24.107  1.00 141.75 ? 797  TRP A CE3 1 
ATOM   6062  C  CZ2 . TRP A 1 797  ? -53.210  27.199  23.782  1.00 146.58 ? 797  TRP A CZ2 1 
ATOM   6063  C  CZ3 . TRP A 1 797  ? -53.504  29.479  23.053  1.00 143.41 ? 797  TRP A CZ3 1 
ATOM   6064  C  CH2 . TRP A 1 797  ? -52.954  28.202  22.894  1.00 145.60 ? 797  TRP A CH2 1 
ATOM   6065  N  N   . GLU A 1 798  ? -56.326  33.400  26.799  1.00 118.14 ? 798  GLU A N   1 
ATOM   6066  C  CA  . GLU A 1 798  ? -57.412  34.342  26.962  1.00 116.08 ? 798  GLU A CA  1 
ATOM   6067  C  C   . GLU A 1 798  ? -58.497  33.981  25.975  1.00 114.98 ? 798  GLU A C   1 
ATOM   6068  O  O   . GLU A 1 798  ? -58.334  34.166  24.785  1.00 114.02 ? 798  GLU A O   1 
ATOM   6069  C  CB  . GLU A 1 798  ? -56.972  35.768  26.722  1.00 115.69 ? 798  GLU A CB  1 
ATOM   6070  C  CG  . GLU A 1 798  ? -58.161  36.663  26.536  1.00 116.08 ? 798  GLU A CG  1 
ATOM   6071  C  CD  . GLU A 1 798  ? -57.766  38.095  26.453  1.00 118.16 ? 798  GLU A CD  1 
ATOM   6072  O  OE1 . GLU A 1 798  ? -56.602  38.409  26.783  1.00 119.74 ? 798  GLU A OE1 1 
ATOM   6073  O  OE2 . GLU A 1 798  ? -58.619  38.908  26.057  1.00 118.75 ? 798  GLU A OE2 1 
ATOM   6074  N  N   . ILE A 1 799  ? -59.608  33.457  26.456  1.00 115.87 ? 799  ILE A N   1 
ATOM   6075  C  CA  . ILE A 1 799  ? -60.651  33.032  25.544  1.00 117.96 ? 799  ILE A CA  1 
ATOM   6076  C  C   . ILE A 1 799  ? -61.802  34.046  25.496  1.00 118.77 ? 799  ILE A C   1 
ATOM   6077  O  O   . ILE A 1 799  ? -62.732  34.009  26.294  1.00 119.81 ? 799  ILE A O   1 
ATOM   6078  C  CB  . ILE A 1 799  ? -61.056  31.553  25.831  1.00 100.47 ? 799  ILE A CB  1 
ATOM   6079  C  CG1 . ILE A 1 799  ? -62.448  31.202  25.335  1.00 99.95  ? 799  ILE A CG1 1 
ATOM   6080  C  CG2 . ILE A 1 799  ? -61.006  31.258  27.302  1.00 102.57 ? 799  ILE A CG2 1 
ATOM   6081  C  CD1 . ILE A 1 799  ? -62.923  29.873  25.929  1.00 100.48 ? 799  ILE A CD1 1 
ATOM   6082  N  N   . GLN A 1 800  ? -61.680  34.982  24.560  1.00 121.73 ? 800  GLN A N   1 
ATOM   6083  C  CA  . GLN A 1 800  ? -62.695  35.995  24.289  1.00 122.73 ? 800  GLN A CA  1 
ATOM   6084  C  C   . GLN A 1 800  ? -63.857  35.413  23.464  1.00 123.24 ? 800  GLN A C   1 
ATOM   6085  O  O   . GLN A 1 800  ? -63.768  34.299  22.943  1.00 123.71 ? 800  GLN A O   1 
ATOM   6086  C  CB  . GLN A 1 800  ? -62.051  37.196  23.578  1.00 124.01 ? 800  GLN A CB  1 
ATOM   6087  C  CG  . GLN A 1 800  ? -61.372  36.861  22.229  1.00 125.80 ? 800  GLN A CG  1 
ATOM   6088  C  CD  . GLN A 1 800  ? -59.947  37.419  22.102  1.00 126.73 ? 800  GLN A CD  1 
ATOM   6089  O  OE1 . GLN A 1 800  ? -59.218  37.475  23.084  1.00 128.15 ? 800  GLN A OE1 1 
ATOM   6090  N  NE2 . GLN A 1 800  ? -59.549  37.814  20.891  1.00 125.72 ? 800  GLN A NE2 1 
ATOM   6091  N  N   . GLY A 1 801  ? -64.952  36.160  23.360  1.00 123.40 ? 801  GLY A N   1 
ATOM   6092  C  CA  . GLY A 1 801  ? -66.124  35.695  22.633  1.00 123.43 ? 801  GLY A CA  1 
ATOM   6093  C  C   . GLY A 1 801  ? -67.186  36.768  22.412  1.00 124.67 ? 801  GLY A C   1 
ATOM   6094  O  O   . GLY A 1 801  ? -68.060  36.972  23.242  1.00 122.54 ? 801  GLY A O   1 
ATOM   6095  N  N   . ILE A 1 802  ? -67.102  37.452  21.280  1.00 125.35 ? 802  ILE A N   1 
ATOM   6096  C  CA  . ILE A 1 802  ? -68.079  38.446  20.881  1.00 125.65 ? 802  ILE A CA  1 
ATOM   6097  C  C   . ILE A 1 802  ? -69.376  37.753  20.472  1.00 126.40 ? 802  ILE A C   1 
ATOM   6098  O  O   . ILE A 1 802  ? -69.375  36.569  20.130  1.00 130.58 ? 802  ILE A O   1 
ATOM   6099  C  CB  . ILE A 1 802  ? -67.508  39.254  19.704  1.00 127.85 ? 802  ILE A CB  1 
ATOM   6100  C  CG1 . ILE A 1 802  ? -68.513  39.399  18.565  1.00 127.67 ? 802  ILE A CG1 1 
ATOM   6101  C  CG2 . ILE A 1 802  ? -66.292  38.552  19.123  1.00 127.95 ? 802  ILE A CG2 1 
ATOM   6102  C  CD1 . ILE A 1 802  ? -69.140  40.763  18.457  1.00 127.96 ? 802  ILE A CD1 1 
ATOM   6103  N  N   . GLY A 1 803  ? -70.486  38.487  20.505  1.00 123.23 ? 803  GLY A N   1 
ATOM   6104  C  CA  . GLY A 1 803  ? -71.746  37.988  19.963  1.00 121.70 ? 803  GLY A CA  1 
ATOM   6105  C  C   . GLY A 1 803  ? -72.502  39.029  19.138  1.00 125.26 ? 803  GLY A C   1 
ATOM   6106  O  O   . GLY A 1 803  ? -72.395  40.227  19.391  1.00 122.63 ? 803  GLY A O   1 
ATOM   6107  N  N   . ILE A 1 804  ? -73.259  38.597  18.135  1.00 127.49 ? 804  ILE A N   1 
ATOM   6108  C  CA  . ILE A 1 804  ? -74.103  39.544  17.428  1.00 127.69 ? 804  ILE A CA  1 
ATOM   6109  C  C   . ILE A 1 804  ? -75.451  38.965  17.116  1.00 129.79 ? 804  ILE A C   1 
ATOM   6110  O  O   . ILE A 1 804  ? -75.573  37.807  16.724  1.00 126.13 ? 804  ILE A O   1 
ATOM   6111  C  CB  . ILE A 1 804  ? -73.462  40.119  16.171  1.00 121.49 ? 804  ILE A CB  1 
ATOM   6112  C  CG1 . ILE A 1 804  ? -73.080  39.027  15.207  1.00 118.71 ? 804  ILE A CG1 1 
ATOM   6113  C  CG2 . ILE A 1 804  ? -72.207  40.884  16.511  1.00 117.06 ? 804  ILE A CG2 1 
ATOM   6114  C  CD1 . ILE A 1 804  ? -72.100  39.536  14.176  1.00 117.45 ? 804  ILE A CD1 1 
ATOM   6115  N  N   . SER A 1 805  ? -76.455  39.806  17.342  1.00 136.45 ? 805  SER A N   1 
ATOM   6116  C  CA  . SER A 1 805  ? -77.858  39.490  17.130  1.00 144.36 ? 805  SER A CA  1 
ATOM   6117  C  C   . SER A 1 805  ? -78.641  40.771  16.886  1.00 146.13 ? 805  SER A C   1 
ATOM   6118  O  O   . SER A 1 805  ? -78.057  41.818  16.643  1.00 147.36 ? 805  SER A O   1 
ATOM   6119  C  CB  . SER A 1 805  ? -78.445  38.698  18.305  1.00 142.91 ? 805  SER A CB  1 
ATOM   6120  O  OG  . SER A 1 805  ? -78.312  37.295  18.084  1.00 144.18 ? 805  SER A OG  1 
ATOM   6121  N  N   . ASN A 1 806  ? -79.964  40.680  16.940  1.00 155.34 ? 806  ASN A N   1 
ATOM   6122  C  CA  . ASN A 1 806  ? -80.818  41.768  16.475  1.00 163.31 ? 806  ASN A CA  1 
ATOM   6123  C  C   . ASN A 1 806  ? -80.781  43.007  17.365  1.00 165.91 ? 806  ASN A C   1 
ATOM   6124  O  O   . ASN A 1 806  ? -81.439  44.011  17.101  1.00 166.35 ? 806  ASN A O   1 
ATOM   6125  C  CB  . ASN A 1 806  ? -82.248  41.272  16.261  1.00 169.81 ? 806  ASN A CB  1 
ATOM   6126  C  CG  . ASN A 1 806  ? -82.359  40.338  15.072  1.00 176.19 ? 806  ASN A CG  1 
ATOM   6127  O  OD1 . ASN A 1 806  ? -82.655  39.155  15.225  1.00 178.78 ? 806  ASN A OD1 1 
ATOM   6128  N  ND2 . ASN A 1 806  ? -82.091  40.860  13.879  1.00 178.82 ? 806  ASN A ND2 1 
ATOM   6129  N  N   . THR A 1 807  ? -79.998  42.934  18.424  1.00 167.70 ? 807  THR A N   1 
ATOM   6130  C  CA  . THR A 1 807  ? -79.802  44.088  19.274  1.00 166.92 ? 807  THR A CA  1 
ATOM   6131  C  C   . THR A 1 807  ? -78.584  44.900  18.793  1.00 161.29 ? 807  THR A C   1 
ATOM   6132  O  O   . THR A 1 807  ? -78.549  46.128  18.913  1.00 164.19 ? 807  THR A O   1 
ATOM   6133  C  CB  . THR A 1 807  ? -79.645  43.626  20.728  1.00 169.12 ? 807  THR A CB  1 
ATOM   6134  O  OG1 . THR A 1 807  ? -78.652  42.591  20.794  1.00 169.84 ? 807  THR A OG1 1 
ATOM   6135  C  CG2 . THR A 1 807  ? -80.968  43.055  21.231  1.00 170.14 ? 807  THR A CG2 1 
ATOM   6136  N  N   . GLY A 1 808  ? -77.603  44.192  18.230  1.00 153.47 ? 808  GLY A N   1 
ATOM   6137  C  CA  . GLY A 1 808  ? -76.312  44.760  17.846  1.00 146.37 ? 808  GLY A CA  1 
ATOM   6138  C  C   . GLY A 1 808  ? -75.100  43.876  18.190  1.00 143.47 ? 808  GLY A C   1 
ATOM   6139  O  O   . GLY A 1 808  ? -75.216  42.653  18.324  1.00 141.39 ? 808  GLY A O   1 
ATOM   6140  N  N   . ILE A 1 809  ? -73.930  44.499  18.335  1.00 141.65 ? 809  ILE A N   1 
ATOM   6141  C  CA  . ILE A 1 809  ? -72.699  43.805  18.711  1.00 138.22 ? 809  ILE A CA  1 
ATOM   6142  C  C   . ILE A 1 809  ? -72.385  43.933  20.195  1.00 138.25 ? 809  ILE A C   1 
ATOM   6143  O  O   . ILE A 1 809  ? -72.367  45.047  20.710  1.00 140.83 ? 809  ILE A O   1 
ATOM   6144  C  CB  . ILE A 1 809  ? -71.517  44.420  17.978  1.00 135.00 ? 809  ILE A CB  1 
ATOM   6145  C  CG1 . ILE A 1 809  ? -70.211  43.983  18.626  1.00 132.11 ? 809  ILE A CG1 1 
ATOM   6146  C  CG2 . ILE A 1 809  ? -71.593  45.939  18.025  1.00 133.36 ? 809  ILE A CG2 1 
ATOM   6147  C  CD1 . ILE A 1 809  ? -69.016  44.764  18.116  1.00 130.99 ? 809  ILE A CD1 1 
ATOM   6148  N  N   . CYS A 1 810  ? -72.100  42.812  20.870  1.00 136.00 ? 810  CYS A N   1 
ATOM   6149  C  CA  . CYS A 1 810  ? -71.750  42.802  22.315  1.00 133.66 ? 810  CYS A CA  1 
ATOM   6150  C  C   . CYS A 1 810  ? -70.612  41.832  22.695  1.00 133.72 ? 810  CYS A C   1 
ATOM   6151  O  O   . CYS A 1 810  ? -70.850  40.657  23.024  1.00 132.65 ? 810  CYS A O   1 
ATOM   6152  C  CB  . CYS A 1 810  ? -72.981  42.510  23.205  1.00 131.74 ? 810  CYS A CB  1 
ATOM   6153  S  SG  . CYS A 1 810  ? -72.678  42.499  25.022  1.00 162.95 ? 810  CYS A SG  1 
ATOM   6154  N  N   . VAL A 1 811  ? -69.385  42.346  22.662  1.00 134.79 ? 811  VAL A N   1 
ATOM   6155  C  CA  . VAL A 1 811  ? -68.232  41.643  23.193  1.00 134.31 ? 811  VAL A CA  1 
ATOM   6156  C  C   . VAL A 1 811  ? -68.422  41.342  24.666  1.00 134.76 ? 811  VAL A C   1 
ATOM   6157  O  O   . VAL A 1 811  ? -68.865  42.193  25.434  1.00 135.52 ? 811  VAL A O   1 
ATOM   6158  C  CB  . VAL A 1 811  ? -67.005  42.519  23.130  1.00 134.69 ? 811  VAL A CB  1 
ATOM   6159  C  CG1 . VAL A 1 811  ? -65.794  41.719  23.579  1.00 135.60 ? 811  VAL A CG1 1 
ATOM   6160  C  CG2 . VAL A 1 811  ? -66.831  43.089  21.742  1.00 133.34 ? 811  VAL A CG2 1 
ATOM   6161  N  N   . ALA A 1 812  ? -68.064  40.140  25.077  1.00 134.11 ? 812  ALA A N   1 
ATOM   6162  C  CA  . ALA A 1 812  ? -68.240  39.792  26.473  1.00 132.97 ? 812  ALA A CA  1 
ATOM   6163  C  C   . ALA A 1 812  ? -66.955  39.951  27.242  1.00 131.77 ? 812  ALA A C   1 
ATOM   6164  O  O   . ALA A 1 812  ? -65.869  40.063  26.664  1.00 131.28 ? 812  ALA A O   1 
ATOM   6165  C  CB  . ALA A 1 812  ? -68.764  38.382  26.626  1.00 135.50 ? 812  ALA A CB  1 
ATOM   6166  N  N   . ASP A 1 813  ? -67.101  39.954  28.559  1.00 128.64 ? 813  ASP A N   1 
ATOM   6167  C  CA  . ASP A 1 813  ? -65.964  40.034  29.429  1.00 126.80 ? 813  ASP A CA  1 
ATOM   6168  C  C   . ASP A 1 813  ? -65.199  38.750  29.163  1.00 122.54 ? 813  ASP A C   1 
ATOM   6169  O  O   . ASP A 1 813  ? -65.775  37.657  29.159  1.00 120.49 ? 813  ASP A O   1 
ATOM   6170  C  CB  . ASP A 1 813  ? -66.422  40.198  30.879  1.00 131.34 ? 813  ASP A CB  1 
ATOM   6171  C  CG  . ASP A 1 813  ? -67.245  41.487  31.092  1.00 134.47 ? 813  ASP A CG  1 
ATOM   6172  O  OD1 . ASP A 1 813  ? -66.661  42.605  31.019  1.00 134.71 ? 813  ASP A OD1 1 
ATOM   6173  O  OD2 . ASP A 1 813  ? -68.477  41.376  31.327  1.00 135.81 ? 813  ASP A OD2 1 
ATOM   6174  N  N   . THR A 1 814  ? -63.911  38.916  28.869  1.00 120.56 ? 814  THR A N   1 
ATOM   6175  C  CA  . THR A 1 814  ? -63.006  37.832  28.500  1.00 119.29 ? 814  THR A CA  1 
ATOM   6176  C  C   . THR A 1 814  ? -63.046  36.718  29.523  1.00 118.79 ? 814  THR A C   1 
ATOM   6177  O  O   . THR A 1 814  ? -63.730  36.835  30.515  1.00 119.19 ? 814  THR A O   1 
ATOM   6178  C  CB  . THR A 1 814  ? -61.587  38.364  28.460  1.00 117.09 ? 814  THR A CB  1 
ATOM   6179  O  OG1 . THR A 1 814  ? -60.683  37.292  28.707  1.00 117.40 ? 814  THR A OG1 1 
ATOM   6180  C  CG2 . THR A 1 814  ? -61.400  39.411  29.544  1.00 117.22 ? 814  THR A CG2 1 
ATOM   6181  N  N   . VAL A 1 815  ? -62.316  35.638  29.300  1.00 120.59 ? 815  VAL A N   1 
ATOM   6182  C  CA  . VAL A 1 815  ? -62.122  34.660  30.365  1.00 123.71 ? 815  VAL A CA  1 
ATOM   6183  C  C   . VAL A 1 815  ? -60.786  33.931  30.255  1.00 124.96 ? 815  VAL A C   1 
ATOM   6184  O  O   . VAL A 1 815  ? -60.691  32.890  29.612  1.00 128.31 ? 815  VAL A O   1 
ATOM   6185  C  CB  . VAL A 1 815  ? -63.277  33.639  30.461  1.00 126.14 ? 815  VAL A CB  1 
ATOM   6186  C  CG1 . VAL A 1 815  ? -62.844  32.409  31.266  1.00 126.94 ? 815  VAL A CG1 1 
ATOM   6187  C  CG2 . VAL A 1 815  ? -64.530  34.272  31.082  1.00 126.18 ? 815  VAL A CG2 1 
ATOM   6188  N  N   . LYS A 1 816  ? -59.755  34.487  30.897  1.00 125.58 ? 816  LYS A N   1 
ATOM   6189  C  CA  . LYS A 1 816  ? -58.412  33.890  30.888  1.00 128.57 ? 816  LYS A CA  1 
ATOM   6190  C  C   . LYS A 1 816  ? -58.522  32.459  31.403  1.00 132.73 ? 816  LYS A C   1 
ATOM   6191  O  O   . LYS A 1 816  ? -59.354  32.165  32.260  1.00 131.18 ? 816  LYS A O   1 
ATOM   6192  C  CB  . LYS A 1 816  ? -57.399  34.706  31.735  1.00 153.06 ? 816  LYS A CB  1 
ATOM   6193  C  CG  . LYS A 1 816  ? -56.887  36.050  31.118  1.00 170.16 ? 816  LYS A CG  1 
ATOM   6194  C  CD  . LYS A 1 816  ? -57.903  37.197  31.302  1.00 168.57 ? 816  LYS A CD  1 
ATOM   6195  C  CE  . LYS A 1 816  ? -57.414  38.561  30.808  1.00 165.58 ? 816  LYS A CE  1 
ATOM   6196  N  NZ  . LYS A 1 816  ? -58.436  39.622  31.093  1.00 163.25 ? 816  LYS A NZ  1 
ATOM   6197  N  N   . ALA A 1 817  ? -57.693  31.570  30.872  1.00 138.33 ? 817  ALA A N   1 
ATOM   6198  C  CA  . ALA A 1 817  ? -57.733  30.179  31.278  1.00 145.71 ? 817  ALA A CA  1 
ATOM   6199  C  C   . ALA A 1 817  ? -56.359  29.538  31.149  1.00 146.55 ? 817  ALA A C   1 
ATOM   6200  O  O   . ALA A 1 817  ? -56.184  28.570  30.415  1.00 147.78 ? 817  ALA A O   1 
ATOM   6201  C  CB  . ALA A 1 817  ? -58.765  29.420  30.466  1.00 149.49 ? 817  ALA A CB  1 
ATOM   6202  N  N   . LYS A 1 818  ? -55.385  30.089  31.867  1.00 144.85 ? 818  LYS A N   1 
ATOM   6203  C  CA  . LYS A 1 818  ? -54.035  29.538  31.861  1.00 145.91 ? 818  LYS A CA  1 
ATOM   6204  C  C   . LYS A 1 818  ? -54.068  28.077  32.266  1.00 144.41 ? 818  LYS A C   1 
ATOM   6205  O  O   . LYS A 1 818  ? -54.668  27.711  33.275  1.00 142.35 ? 818  LYS A O   1 
ATOM   6206  C  CB  . LYS A 1 818  ? -53.092  30.311  32.801  1.00 149.66 ? 818  LYS A CB  1 
ATOM   6207  C  CG  . LYS A 1 818  ? -53.009  29.780  34.248  1.00 155.70 ? 818  LYS A CG  1 
ATOM   6208  C  CD  . LYS A 1 818  ? -51.847  30.407  35.031  1.00 161.30 ? 818  LYS A CD  1 
ATOM   6209  C  CE  . LYS A 1 818  ? -51.973  30.151  36.534  1.00 166.35 ? 818  LYS A CE  1 
ATOM   6210  N  NZ  . LYS A 1 818  ? -51.023  30.960  37.362  1.00 168.12 ? 818  LYS A NZ  1 
ATOM   6211  N  N   . VAL A 1 819  ? -53.440  27.243  31.451  1.00 145.76 ? 819  VAL A N   1 
ATOM   6212  C  CA  . VAL A 1 819  ? -53.198  25.866  31.817  1.00 146.69 ? 819  VAL A CA  1 
ATOM   6213  C  C   . VAL A 1 819  ? -51.730  25.770  32.129  1.00 147.93 ? 819  VAL A C   1 
ATOM   6214  O  O   . VAL A 1 819  ? -50.946  26.625  31.718  1.00 147.56 ? 819  VAL A O   1 
ATOM   6215  C  CB  . VAL A 1 819  ? -53.558  24.905  30.686  1.00 145.25 ? 819  VAL A CB  1 
ATOM   6216  C  CG1 . VAL A 1 819  ? -55.060  24.822  30.536  1.00 144.48 ? 819  VAL A CG1 1 
ATOM   6217  C  CG2 . VAL A 1 819  ? -52.915  25.354  29.378  1.00 143.35 ? 819  VAL A CG2 1 
ATOM   6218  N  N   . PHE A 1 820  ? -51.353  24.736  32.862  1.00 152.30 ? 820  PHE A N   1 
ATOM   6219  C  CA  . PHE A 1 820  ? -49.958  24.576  33.212  1.00 157.78 ? 820  PHE A CA  1 
ATOM   6220  C  C   . PHE A 1 820  ? -49.687  23.425  34.188  1.00 159.38 ? 820  PHE A C   1 
ATOM   6221  O  O   . PHE A 1 820  ? -50.433  23.219  35.145  1.00 157.08 ? 820  PHE A O   1 
ATOM   6222  C  CB  . PHE A 1 820  ? -49.427  25.890  33.773  1.00 166.15 ? 820  PHE A CB  1 
ATOM   6223  C  CG  . PHE A 1 820  ? -48.239  25.719  34.628  1.00 178.99 ? 820  PHE A CG  1 
ATOM   6224  C  CD1 . PHE A 1 820  ? -48.358  25.761  36.000  1.00 185.74 ? 820  PHE A CD1 1 
ATOM   6225  C  CD2 . PHE A 1 820  ? -47.002  25.473  34.063  1.00 184.64 ? 820  PHE A CD2 1 
ATOM   6226  C  CE1 . PHE A 1 820  ? -47.256  25.583  36.794  1.00 191.04 ? 820  PHE A CE1 1 
ATOM   6227  C  CE2 . PHE A 1 820  ? -45.896  25.295  34.842  1.00 189.18 ? 820  PHE A CE2 1 
ATOM   6228  C  CZ  . PHE A 1 820  ? -46.018  25.345  36.211  1.00 191.93 ? 820  PHE A CZ  1 
ATOM   6229  N  N   . LYS A 1 821  ? -48.615  22.680  33.926  1.00 163.20 ? 821  LYS A N   1 
ATOM   6230  C  CA  . LYS A 1 821  ? -48.189  21.577  34.779  1.00 166.99 ? 821  LYS A CA  1 
ATOM   6231  C  C   . LYS A 1 821  ? -47.072  22.034  35.716  1.00 168.81 ? 821  LYS A C   1 
ATOM   6232  O  O   . LYS A 1 821  ? -46.147  22.725  35.302  1.00 170.22 ? 821  LYS A O   1 
ATOM   6233  C  CB  . LYS A 1 821  ? -47.718  20.399  33.926  1.00 166.25 ? 821  LYS A CB  1 
ATOM   6234  C  CG  . LYS A 1 821  ? -47.216  19.188  34.698  1.00 164.50 ? 821  LYS A CG  1 
ATOM   6235  C  CD  . LYS A 1 821  ? -48.185  18.004  34.609  1.00 162.53 ? 821  LYS A CD  1 
ATOM   6236  C  CE  . LYS A 1 821  ? -47.468  16.665  34.899  1.00 163.14 ? 821  LYS A CE  1 
ATOM   6237  N  NZ  . LYS A 1 821  ? -48.356  15.448  34.888  1.00 163.82 ? 821  LYS A NZ  1 
ATOM   6238  N  N   . ASP A 1 822  ? -47.167  21.611  36.974  1.00 159.16 ? 822  ASP A N   1 
ATOM   6239  C  CA  . ASP A 1 822  ? -46.365  22.131  38.088  1.00 159.10 ? 822  ASP A CA  1 
ATOM   6240  C  C   . ASP A 1 822  ? -44.868  21.934  37.919  1.00 156.76 ? 822  ASP A C   1 
ATOM   6241  O  O   . ASP A 1 822  ? -44.095  22.898  37.933  1.00 152.71 ? 822  ASP A O   1 
ATOM   6242  C  CB  . ASP A 1 822  ? -46.792  21.450  39.389  1.00 165.34 ? 822  ASP A CB  1 
ATOM   6243  C  CG  . ASP A 1 822  ? -48.039  22.073  40.005  1.00 174.96 ? 822  ASP A CG  1 
ATOM   6244  O  OD1 . ASP A 1 822  ? -48.860  22.687  39.272  1.00 178.82 ? 822  ASP A OD1 1 
ATOM   6245  O  OD2 . ASP A 1 822  ? -48.196  21.932  41.242  1.00 178.43 ? 822  ASP A OD2 1 
ATOM   6246  N  N   . VAL A 1 823  ? -44.472  20.666  37.812  1.00 160.01 ? 823  VAL A N   1 
ATOM   6247  C  CA  . VAL A 1 823  ? -43.099  20.290  37.502  1.00 159.55 ? 823  VAL A CA  1 
ATOM   6248  C  C   . VAL A 1 823  ? -43.088  19.358  36.310  1.00 163.10 ? 823  VAL A C   1 
ATOM   6249  O  O   . VAL A 1 823  ? -43.907  18.437  36.215  1.00 167.53 ? 823  VAL A O   1 
ATOM   6250  C  CB  . VAL A 1 823  ? -42.401  19.577  38.657  1.00 154.85 ? 823  VAL A CB  1 
ATOM   6251  C  CG1 . VAL A 1 823  ? -41.108  18.956  38.174  1.00 151.28 ? 823  VAL A CG1 1 
ATOM   6252  C  CG2 . VAL A 1 823  ? -42.128  20.546  39.777  1.00 153.77 ? 823  VAL A CG2 1 
ATOM   6253  N  N   . PHE A 1 824  ? -42.144  19.602  35.405  1.00 162.01 ? 824  PHE A N   1 
ATOM   6254  C  CA  . PHE A 1 824  ? -42.026  18.826  34.177  1.00 160.58 ? 824  PHE A CA  1 
ATOM   6255  C  C   . PHE A 1 824  ? -40.592  18.861  33.633  1.00 154.73 ? 824  PHE A C   1 
ATOM   6256  O  O   . PHE A 1 824  ? -39.880  19.854  33.771  1.00 151.63 ? 824  PHE A O   1 
ATOM   6257  C  CB  . PHE A 1 824  ? -43.016  19.344  33.129  1.00 164.18 ? 824  PHE A CB  1 
ATOM   6258  C  CG  . PHE A 1 824  ? -42.677  20.699  32.599  1.00 167.21 ? 824  PHE A CG  1 
ATOM   6259  C  CD1 . PHE A 1 824  ? -42.076  20.839  31.364  1.00 169.94 ? 824  PHE A CD1 1 
ATOM   6260  C  CD2 . PHE A 1 824  ? -42.955  21.829  33.334  1.00 169.06 ? 824  PHE A CD2 1 
ATOM   6261  C  CE1 . PHE A 1 824  ? -41.761  22.085  30.872  1.00 171.16 ? 824  PHE A CE1 1 
ATOM   6262  C  CE2 . PHE A 1 824  ? -42.643  23.078  32.850  1.00 170.40 ? 824  PHE A CE2 1 
ATOM   6263  C  CZ  . PHE A 1 824  ? -42.046  23.207  31.619  1.00 171.12 ? 824  PHE A CZ  1 
ATOM   6264  N  N   . LEU A 1 825  ? -40.162  17.762  33.030  1.00 152.23 ? 825  LEU A N   1 
ATOM   6265  C  CA  . LEU A 1 825  ? -38.843  17.721  32.436  1.00 145.68 ? 825  LEU A CA  1 
ATOM   6266  C  C   . LEU A 1 825  ? -38.883  17.785  30.912  1.00 146.57 ? 825  LEU A C   1 
ATOM   6267  O  O   . LEU A 1 825  ? -39.788  17.241  30.266  1.00 148.49 ? 825  LEU A O   1 
ATOM   6268  C  CB  . LEU A 1 825  ? -38.100  16.468  32.872  1.00 139.04 ? 825  LEU A CB  1 
ATOM   6269  C  CG  . LEU A 1 825  ? -36.987  16.152  31.882  1.00 130.72 ? 825  LEU A CG  1 
ATOM   6270  C  CD1 . LEU A 1 825  ? -35.782  17.044  32.132  1.00 125.45 ? 825  LEU A CD1 1 
ATOM   6271  C  CD2 . LEU A 1 825  ? -36.620  14.690  31.936  1.00 128.85 ? 825  LEU A CD2 1 
ATOM   6272  N  N   . GLU A 1 826  ? -37.876  18.448  30.355  1.00 143.76 ? 826  GLU A N   1 
ATOM   6273  C  CA  . GLU A 1 826  ? -37.616  18.434  28.927  1.00 143.98 ? 826  GLU A CA  1 
ATOM   6274  C  C   . GLU A 1 826  ? -36.188  17.927  28.719  1.00 142.02 ? 826  GLU A C   1 
ATOM   6275  O  O   . GLU A 1 826  ? -35.285  18.238  29.509  1.00 138.67 ? 826  GLU A O   1 
ATOM   6276  C  CB  . GLU A 1 826  ? -37.732  19.846  28.366  1.00 145.34 ? 826  GLU A CB  1 
ATOM   6277  C  CG  . GLU A 1 826  ? -36.690  20.798  28.940  1.00 146.80 ? 826  GLU A CG  1 
ATOM   6278  C  CD  . GLU A 1 826  ? -36.643  22.129  28.227  1.00 150.19 ? 826  GLU A CD  1 
ATOM   6279  O  OE1 . GLU A 1 826  ? -35.539  22.725  28.191  1.00 149.78 ? 826  GLU A OE1 1 
ATOM   6280  O  OE2 . GLU A 1 826  ? -37.699  22.569  27.707  1.00 152.51 ? 826  GLU A OE2 1 
ATOM   6281  N  N   . MET A 1 827  ? -35.991  17.132  27.669  1.00 143.39 ? 827  MET A N   1 
ATOM   6282  C  CA  . MET A 1 827  ? -34.665  16.663  27.294  1.00 141.02 ? 827  MET A CA  1 
ATOM   6283  C  C   . MET A 1 827  ? -34.314  17.247  25.946  1.00 138.66 ? 827  MET A C   1 
ATOM   6284  O  O   . MET A 1 827  ? -35.140  17.245  25.044  1.00 141.87 ? 827  MET A O   1 
ATOM   6285  C  CB  . MET A 1 827  ? -34.686  15.160  27.146  1.00 142.36 ? 827  MET A CB  1 
ATOM   6286  C  CG  . MET A 1 827  ? -35.117  14.429  28.372  1.00 142.21 ? 827  MET A CG  1 
ATOM   6287  S  SD  . MET A 1 827  ? -33.750  14.436  29.498  1.00 128.70 ? 827  MET A SD  1 
ATOM   6288  C  CE  . MET A 1 827  ? -32.376  14.079  28.409  1.00 97.89  ? 827  MET A CE  1 
ATOM   6289  N  N   . ASN A 1 828  ? -33.094  17.737  25.790  1.00 134.94 ? 828  ASN A N   1 
ATOM   6290  C  CA  . ASN A 1 828  ? -32.687  18.235  24.488  1.00 133.88 ? 828  ASN A CA  1 
ATOM   6291  C  C   . ASN A 1 828  ? -31.960  17.185  23.624  1.00 128.47 ? 828  ASN A C   1 
ATOM   6292  O  O   . ASN A 1 828  ? -30.740  16.999  23.751  1.00 126.57 ? 828  ASN A O   1 
ATOM   6293  C  CB  . ASN A 1 828  ? -31.846  19.506  24.620  1.00 140.42 ? 828  ASN A CB  1 
ATOM   6294  C  CG  . ASN A 1 828  ? -31.915  20.363  23.369  1.00 149.29 ? 828  ASN A CG  1 
ATOM   6295  O  OD1 . ASN A 1 828  ? -32.997  20.786  22.965  1.00 153.72 ? 828  ASN A OD1 1 
ATOM   6296  N  ND2 . ASN A 1 828  ? -30.765  20.616  22.743  1.00 151.82 ? 828  ASN A ND2 1 
ATOM   6297  N  N   . ILE A 1 829  ? -32.708  16.503  22.750  1.00 122.92 ? 829  ILE A N   1 
ATOM   6298  C  CA  . ILE A 1 829  ? -32.129  15.550  21.810  1.00 114.50 ? 829  ILE A CA  1 
ATOM   6299  C  C   . ILE A 1 829  ? -31.667  16.342  20.602  1.00 108.73 ? 829  ILE A C   1 
ATOM   6300  O  O   . ILE A 1 829  ? -32.250  17.383  20.281  1.00 110.57 ? 829  ILE A O   1 
ATOM   6301  C  CB  . ILE A 1 829  ? -33.169  14.512  21.381  1.00 112.64 ? 829  ILE A CB  1 
ATOM   6302  C  CG1 . ILE A 1 829  ? -33.983  14.063  22.588  1.00 110.31 ? 829  ILE A CG1 1 
ATOM   6303  C  CG2 . ILE A 1 829  ? -32.504  13.307  20.764  1.00 111.34 ? 829  ILE A CG2 1 
ATOM   6304  C  CD1 . ILE A 1 829  ? -33.184  13.297  23.587  1.00 108.27 ? 829  ILE A CD1 1 
ATOM   6305  N  N   . PRO A 1 830  ? -30.603  15.874  19.940  1.00 103.24 ? 830  PRO A N   1 
ATOM   6306  C  CA  . PRO A 1 830  ? -30.024  16.537  18.777  1.00 107.45 ? 830  PRO A CA  1 
ATOM   6307  C  C   . PRO A 1 830  ? -30.816  16.146  17.572  1.00 123.77 ? 830  PRO A C   1 
ATOM   6308  O  O   . PRO A 1 830  ? -31.669  15.257  17.645  1.00 136.52 ? 830  PRO A O   1 
ATOM   6309  C  CB  . PRO A 1 830  ? -28.656  15.872  18.634  1.00 98.72  ? 830  PRO A CB  1 
ATOM   6310  C  CG  . PRO A 1 830  ? -28.578  14.886  19.704  1.00 94.47  ? 830  PRO A CG  1 
ATOM   6311  C  CD  . PRO A 1 830  ? -29.930  14.609  20.196  1.00 96.56  ? 830  PRO A CD  1 
ATOM   6312  N  N   . TYR A 1 831  ? -30.541  16.780  16.449  1.00 125.64 ? 831  TYR A N   1 
ATOM   6313  C  CA  . TYR A 1 831  ? -31.084  16.243  15.238  1.00 127.94 ? 831  TYR A CA  1 
ATOM   6314  C  C   . TYR A 1 831  ? -30.485  14.856  15.160  1.00 124.48 ? 831  TYR A C   1 
ATOM   6315  O  O   . TYR A 1 831  ? -31.142  13.862  15.440  1.00 126.12 ? 831  TYR A O   1 
ATOM   6316  C  CB  . TYR A 1 831  ? -30.640  17.080  14.057  1.00 132.18 ? 831  TYR A CB  1 
ATOM   6317  C  CG  . TYR A 1 831  ? -31.275  16.701  12.739  1.00 137.90 ? 831  TYR A CG  1 
ATOM   6318  C  CD1 . TYR A 1 831  ? -30.515  16.656  11.578  1.00 138.61 ? 831  TYR A CD1 1 
ATOM   6319  C  CD2 . TYR A 1 831  ? -32.624  16.398  12.652  1.00 140.13 ? 831  TYR A CD2 1 
ATOM   6320  C  CE1 . TYR A 1 831  ? -31.071  16.331  10.378  1.00 141.58 ? 831  TYR A CE1 1 
ATOM   6321  C  CE2 . TYR A 1 831  ? -33.187  16.063  11.448  1.00 143.31 ? 831  TYR A CE2 1 
ATOM   6322  C  CZ  . TYR A 1 831  ? -32.401  16.034  10.312  1.00 144.13 ? 831  TYR A CZ  1 
ATOM   6323  O  OH  . TYR A 1 831  ? -32.929  15.703  9.086   1.00 147.26 ? 831  TYR A OH  1 
ATOM   6324  N  N   . SER A 1 832  ? -29.211  14.776  14.841  1.00 120.96 ? 832  SER A N   1 
ATOM   6325  C  CA  . SER A 1 832  ? -28.706  13.480  14.484  1.00 124.06 ? 832  SER A CA  1 
ATOM   6326  C  C   . SER A 1 832  ? -27.359  13.224  15.083  1.00 121.16 ? 832  SER A C   1 
ATOM   6327  O  O   . SER A 1 832  ? -26.618  14.161  15.367  1.00 120.02 ? 832  SER A O   1 
ATOM   6328  C  CB  . SER A 1 832  ? -28.619  13.374  12.968  1.00 128.25 ? 832  SER A CB  1 
ATOM   6329  O  OG  . SER A 1 832  ? -27.750  14.369  12.460  1.00 129.64 ? 832  SER A OG  1 
ATOM   6330  N  N   . VAL A 1 833  ? -27.052  11.935  15.243  1.00 120.46 ? 833  VAL A N   1 
ATOM   6331  C  CA  . VAL A 1 833  ? -25.777  11.472  15.769  1.00 116.86 ? 833  VAL A CA  1 
ATOM   6332  C  C   . VAL A 1 833  ? -25.235  10.366  14.895  1.00 114.79 ? 833  VAL A C   1 
ATOM   6333  O  O   . VAL A 1 833  ? -25.990  9.509   14.456  1.00 115.88 ? 833  VAL A O   1 
ATOM   6334  C  CB  . VAL A 1 833  ? -25.953  10.823  17.133  1.00 115.87 ? 833  VAL A CB  1 
ATOM   6335  C  CG1 . VAL A 1 833  ? -24.744  11.112  17.999  1.00 113.95 ? 833  VAL A CG1 1 
ATOM   6336  C  CG2 . VAL A 1 833  ? -27.214  11.311  17.791  1.00 116.99 ? 833  VAL A CG2 1 
ATOM   6337  N  N   . VAL A 1 834  ? -23.927  10.368  14.668  1.00 113.43 ? 834  VAL A N   1 
ATOM   6338  C  CA  . VAL A 1 834  ? -23.266  9.266   13.978  1.00 113.87 ? 834  VAL A CA  1 
ATOM   6339  C  C   . VAL A 1 834  ? -23.115  8.018   14.853  1.00 117.07 ? 834  VAL A C   1 
ATOM   6340  O  O   . VAL A 1 834  ? -22.997  8.110   16.076  1.00 116.20 ? 834  VAL A O   1 
ATOM   6341  C  CB  . VAL A 1 834  ? -21.881  9.695   13.496  1.00 111.73 ? 834  VAL A CB  1 
ATOM   6342  C  CG1 . VAL A 1 834  ? -21.055  8.488   13.086  1.00 112.25 ? 834  VAL A CG1 1 
ATOM   6343  C  CG2 . VAL A 1 834  ? -22.014  10.694  12.367  1.00 110.99 ? 834  VAL A CG2 1 
ATOM   6344  N  N   . ARG A 1 835  ? -23.129  6.848   14.221  1.00 121.73 ? 835  ARG A N   1 
ATOM   6345  C  CA  . ARG A 1 835  ? -22.919  5.586   14.928  1.00 126.48 ? 835  ARG A CA  1 
ATOM   6346  C  C   . ARG A 1 835  ? -21.556  5.569   15.607  1.00 125.15 ? 835  ARG A C   1 
ATOM   6347  O  O   . ARG A 1 835  ? -20.538  5.877   14.985  1.00 124.66 ? 835  ARG A O   1 
ATOM   6348  C  CB  . ARG A 1 835  ? -23.063  4.389   13.968  1.00 130.71 ? 835  ARG A CB  1 
ATOM   6349  C  CG  . ARG A 1 835  ? -22.117  3.211   14.248  1.00 133.26 ? 835  ARG A CG  1 
ATOM   6350  C  CD  . ARG A 1 835  ? -22.631  1.887   13.669  1.00 137.66 ? 835  ARG A CD  1 
ATOM   6351  N  NE  . ARG A 1 835  ? -22.300  1.580   12.272  1.00 138.71 ? 835  ARG A NE  1 
ATOM   6352  C  CZ  . ARG A 1 835  ? -21.518  2.300   11.469  1.00 137.34 ? 835  ARG A CZ  1 
ATOM   6353  N  NH1 . ARG A 1 835  ? -20.943  3.432   11.873  1.00 134.40 ? 835  ARG A NH1 1 
ATOM   6354  N  NH2 . ARG A 1 835  ? -21.312  1.875   10.232  1.00 138.18 ? 835  ARG A NH2 1 
ATOM   6355  N  N   . GLY A 1 836  ? -21.549  5.224   16.890  1.00 126.93 ? 836  GLY A N   1 
ATOM   6356  C  CA  . GLY A 1 836  ? -20.310  5.087   17.641  1.00 126.95 ? 836  GLY A CA  1 
ATOM   6357  C  C   . GLY A 1 836  ? -19.623  6.393   17.998  1.00 126.52 ? 836  GLY A C   1 
ATOM   6358  O  O   . GLY A 1 836  ? -18.414  6.417   18.247  1.00 123.96 ? 836  GLY A O   1 
ATOM   6359  N  N   . GLU A 1 837  ? -20.402  7.474   17.972  1.00 126.67 ? 837  GLU A N   1 
ATOM   6360  C  CA  . GLU A 1 837  ? -20.023  8.785   18.478  1.00 125.96 ? 837  GLU A CA  1 
ATOM   6361  C  C   . GLU A 1 837  ? -20.636  8.741   19.873  1.00 129.39 ? 837  GLU A C   1 
ATOM   6362  O  O   . GLU A 1 837  ? -21.774  8.285   20.001  1.00 131.12 ? 837  GLU A O   1 
ATOM   6363  C  CB  . GLU A 1 837  ? -20.728  9.866   17.638  1.00 124.88 ? 837  GLU A CB  1 
ATOM   6364  C  CG  . GLU A 1 837  ? -19.827  10.910  16.928  1.00 112.60 ? 837  GLU A CG  1 
ATOM   6365  C  CD  . GLU A 1 837  ? -20.564  11.726  15.836  1.00 108.73 ? 837  GLU A CD  1 
ATOM   6366  O  OE1 . GLU A 1 837  ? -21.816  11.786  15.879  1.00 109.59 ? 837  GLU A OE1 1 
ATOM   6367  O  OE2 . GLU A 1 837  ? -19.898  12.309  14.937  1.00 104.93 ? 837  GLU A OE2 1 
ATOM   6368  N  N   . GLN A 1 838  ? -19.907  9.166   20.914  1.00 130.08 ? 838  GLN A N   1 
ATOM   6369  C  CA  . GLN A 1 838  ? -20.443  9.171   22.297  1.00 130.19 ? 838  GLN A CA  1 
ATOM   6370  C  C   . GLN A 1 838  ? -21.117  10.511  22.659  1.00 129.12 ? 838  GLN A C   1 
ATOM   6371  O  O   . GLN A 1 838  ? -20.466  11.534  22.796  1.00 125.05 ? 838  GLN A O   1 
ATOM   6372  C  CB  . GLN A 1 838  ? -19.347  8.806   23.307  1.00 130.53 ? 838  GLN A CB  1 
ATOM   6373  C  CG  . GLN A 1 838  ? -19.746  8.918   24.775  1.00 135.27 ? 838  GLN A CG  1 
ATOM   6374  C  CD  . GLN A 1 838  ? -18.522  9.062   25.711  1.00 143.54 ? 838  GLN A CD  1 
ATOM   6375  O  OE1 . GLN A 1 838  ? -17.963  8.054   26.182  1.00 146.53 ? 838  GLN A OE1 1 
ATOM   6376  N  NE2 . GLN A 1 838  ? -18.103  10.322  25.982  1.00 143.62 ? 838  GLN A NE2 1 
ATOM   6377  N  N   . ILE A 1 839  ? -22.434  10.496  22.809  1.00 131.28 ? 839  ILE A N   1 
ATOM   6378  C  CA  . ILE A 1 839  ? -23.204  11.732  22.847  1.00 131.77 ? 839  ILE A CA  1 
ATOM   6379  C  C   . ILE A 1 839  ? -23.654  12.141  24.259  1.00 134.16 ? 839  ILE A C   1 
ATOM   6380  O  O   . ILE A 1 839  ? -24.014  11.289  25.067  1.00 136.50 ? 839  ILE A O   1 
ATOM   6381  C  CB  . ILE A 1 839  ? -24.441  11.589  21.937  1.00 133.46 ? 839  ILE A CB  1 
ATOM   6382  C  CG1 . ILE A 1 839  ? -25.050  12.950  21.596  1.00 133.00 ? 839  ILE A CG1 1 
ATOM   6383  C  CG2 . ILE A 1 839  ? -25.462  10.706  22.587  1.00 134.25 ? 839  ILE A CG2 1 
ATOM   6384  C  CD1 . ILE A 1 839  ? -24.295  13.712  20.527  1.00 132.61 ? 839  ILE A CD1 1 
ATOM   6385  N  N   . GLN A 1 840  ? -23.636  13.443  24.558  1.00 132.56 ? 840  GLN A N   1 
ATOM   6386  C  CA  . GLN A 1 840  ? -24.147  13.935  25.839  1.00 132.01 ? 840  GLN A CA  1 
ATOM   6387  C  C   . GLN A 1 840  ? -25.547  14.537  25.753  1.00 126.48 ? 840  GLN A C   1 
ATOM   6388  O  O   . GLN A 1 840  ? -25.739  15.621  25.218  1.00 124.44 ? 840  GLN A O   1 
ATOM   6389  C  CB  . GLN A 1 840  ? -23.197  14.942  26.459  1.00 136.84 ? 840  GLN A CB  1 
ATOM   6390  C  CG  . GLN A 1 840  ? -23.049  14.718  27.946  1.00 145.09 ? 840  GLN A CG  1 
ATOM   6391  C  CD  . GLN A 1 840  ? -23.258  15.985  28.749  1.00 151.49 ? 840  GLN A CD  1 
ATOM   6392  O  OE1 . GLN A 1 840  ? -22.708  16.140  29.845  1.00 154.27 ? 840  GLN A OE1 1 
ATOM   6393  N  NE2 . GLN A 1 840  ? -24.049  16.906  28.206  1.00 152.57 ? 840  GLN A NE2 1 
ATOM   6394  N  N   . LEU A 1 841  ? -26.512  13.823  26.315  1.00 124.61 ? 841  LEU A N   1 
ATOM   6395  C  CA  . LEU A 1 841  ? -27.919  14.166  26.188  1.00 121.70 ? 841  LEU A CA  1 
ATOM   6396  C  C   . LEU A 1 841  ? -28.452  15.012  27.334  1.00 119.22 ? 841  LEU A C   1 
ATOM   6397  O  O   . LEU A 1 841  ? -28.882  14.480  28.356  1.00 117.63 ? 841  LEU A O   1 
ATOM   6398  C  CB  . LEU A 1 841  ? -28.732  12.881  26.113  1.00 120.72 ? 841  LEU A CB  1 
ATOM   6399  C  CG  . LEU A 1 841  ? -28.987  12.377  24.705  1.00 116.70 ? 841  LEU A CG  1 
ATOM   6400  C  CD1 . LEU A 1 841  ? -29.988  11.227  24.730  1.00 116.69 ? 841  LEU A CD1 1 
ATOM   6401  C  CD2 . LEU A 1 841  ? -29.505  13.544  23.894  1.00 114.68 ? 841  LEU A CD2 1 
ATOM   6402  N  N   . LYS A 1 842  ? -28.472  16.326  27.152  1.00 118.75 ? 842  LYS A N   1 
ATOM   6403  C  CA  . LYS A 1 842  ? -28.923  17.198  28.223  1.00 119.24 ? 842  LYS A CA  1 
ATOM   6404  C  C   . LYS A 1 842  ? -30.429  17.418  28.285  1.00 122.28 ? 842  LYS A C   1 
ATOM   6405  O  O   . LYS A 1 842  ? -31.212  16.796  27.569  1.00 122.87 ? 842  LYS A O   1 
ATOM   6406  C  CB  . LYS A 1 842  ? -28.213  18.542  28.178  1.00 117.57 ? 842  LYS A CB  1 
ATOM   6407  C  CG  . LYS A 1 842  ? -26.713  18.434  28.253  1.00 116.66 ? 842  LYS A CG  1 
ATOM   6408  C  CD  . LYS A 1 842  ? -26.100  19.809  28.173  1.00 116.84 ? 842  LYS A CD  1 
ATOM   6409  C  CE  . LYS A 1 842  ? -24.656  19.760  27.728  1.00 117.47 ? 842  LYS A CE  1 
ATOM   6410  N  NZ  . LYS A 1 842  ? -24.191  21.162  27.533  1.00 119.14 ? 842  LYS A NZ  1 
ATOM   6411  N  N   . GLY A 1 843  ? -30.806  18.318  29.186  1.00 123.82 ? 843  GLY A N   1 
ATOM   6412  C  CA  . GLY A 1 843  ? -32.194  18.603  29.501  1.00 127.88 ? 843  GLY A CA  1 
ATOM   6413  C  C   . GLY A 1 843  ? -32.244  19.384  30.797  1.00 129.40 ? 843  GLY A C   1 
ATOM   6414  O  O   . GLY A 1 843  ? -31.263  19.412  31.545  1.00 129.02 ? 843  GLY A O   1 
ATOM   6415  N  N   . THR A 1 844  ? -33.372  20.026  31.066  1.00 136.13 ? 844  THR A N   1 
ATOM   6416  C  CA  . THR A 1 844  ? -33.532  20.741  32.334  1.00 139.07 ? 844  THR A CA  1 
ATOM   6417  C  C   . THR A 1 844  ? -34.914  20.374  32.960  1.00 138.05 ? 844  THR A C   1 
ATOM   6418  O  O   . THR A 1 844  ? -35.868  20.072  32.231  1.00 138.28 ? 844  THR A O   1 
ATOM   6419  C  CB  . THR A 1 844  ? -33.160  22.302  32.203  1.00 120.49 ? 844  THR A CB  1 
ATOM   6420  O  OG1 . THR A 1 844  ? -34.293  23.110  31.833  1.00 120.86 ? 844  THR A OG1 1 
ATOM   6421  C  CG2 . THR A 1 844  ? -32.014  22.525  31.167  1.00 112.91 ? 844  THR A CG2 1 
ATOM   6422  N  N   . VAL A 1 845  ? -35.001  20.287  34.291  1.00 138.54 ? 845  VAL A N   1 
ATOM   6423  C  CA  . VAL A 1 845  ? -36.251  19.833  34.928  1.00 140.82 ? 845  VAL A CA  1 
ATOM   6424  C  C   . VAL A 1 845  ? -36.958  20.949  35.669  1.00 140.23 ? 845  VAL A C   1 
ATOM   6425  O  O   . VAL A 1 845  ? -36.387  21.592  36.541  1.00 137.52 ? 845  VAL A O   1 
ATOM   6426  C  CB  . VAL A 1 845  ? -36.073  18.592  35.856  1.00 105.54 ? 845  VAL A CB  1 
ATOM   6427  C  CG1 . VAL A 1 845  ? -35.046  18.849  36.950  1.00 103.92 ? 845  VAL A CG1 1 
ATOM   6428  C  CG2 . VAL A 1 845  ? -37.421  18.166  36.434  1.00 106.35 ? 845  VAL A CG2 1 
ATOM   6429  N  N   . TYR A 1 846  ? -38.212  21.171  35.311  1.00 142.58 ? 846  TYR A N   1 
ATOM   6430  C  CA  . TYR A 1 846  ? -38.875  22.406  35.695  1.00 143.23 ? 846  TYR A CA  1 
ATOM   6431  C  C   . TYR A 1 846  ? -39.686  22.324  36.975  1.00 150.06 ? 846  TYR A C   1 
ATOM   6432  O  O   . TYR A 1 846  ? -40.642  21.558  37.087  1.00 150.60 ? 846  TYR A O   1 
ATOM   6433  C  CB  . TYR A 1 846  ? -39.638  23.037  34.507  1.00 137.75 ? 846  TYR A CB  1 
ATOM   6434  C  CG  . TYR A 1 846  ? -38.670  23.562  33.459  1.00 130.77 ? 846  TYR A CG  1 
ATOM   6435  C  CD1 . TYR A 1 846  ? -38.885  23.390  32.103  1.00 128.93 ? 846  TYR A CD1 1 
ATOM   6436  C  CD2 . TYR A 1 846  ? -37.499  24.183  33.850  1.00 127.26 ? 846  TYR A CD2 1 
ATOM   6437  C  CE1 . TYR A 1 846  ? -37.955  23.861  31.175  1.00 125.87 ? 846  TYR A CE1 1 
ATOM   6438  C  CE2 . TYR A 1 846  ? -36.581  24.648  32.937  1.00 123.69 ? 846  TYR A CE2 1 
ATOM   6439  C  CZ  . TYR A 1 846  ? -36.803  24.488  31.613  1.00 122.98 ? 846  TYR A CZ  1 
ATOM   6440  O  OH  . TYR A 1 846  ? -35.843  24.963  30.753  1.00 120.82 ? 846  TYR A OH  1 
ATOM   6441  N  N   . ASN A 1 847  ? -39.231  23.108  37.952  1.00 157.76 ? 847  ASN A N   1 
ATOM   6442  C  CA  . ASN A 1 847  ? -39.962  23.359  39.190  1.00 165.96 ? 847  ASN A CA  1 
ATOM   6443  C  C   . ASN A 1 847  ? -40.609  24.725  39.116  1.00 169.09 ? 847  ASN A C   1 
ATOM   6444  O  O   . ASN A 1 847  ? -39.948  25.742  38.896  1.00 165.43 ? 847  ASN A O   1 
ATOM   6445  C  CB  . ASN A 1 847  ? -39.056  23.273  40.429  1.00 168.83 ? 847  ASN A CB  1 
ATOM   6446  C  CG  . ASN A 1 847  ? -39.829  22.926  41.705  1.00 174.10 ? 847  ASN A CG  1 
ATOM   6447  O  OD1 . ASN A 1 847  ? -40.921  23.447  41.954  1.00 176.72 ? 847  ASN A OD1 1 
ATOM   6448  N  ND2 . ASN A 1 847  ? -39.259  22.039  42.515  1.00 174.97 ? 847  ASN A ND2 1 
ATOM   6449  N  N   . TYR A 1 848  ? -41.914  24.722  39.323  1.00 175.97 ? 848  TYR A N   1 
ATOM   6450  C  CA  . TYR A 1 848  ? -42.717  25.903  39.183  1.00 180.43 ? 848  TYR A CA  1 
ATOM   6451  C  C   . TYR A 1 848  ? -43.631  26.008  40.392  1.00 183.85 ? 848  TYR A C   1 
ATOM   6452  O  O   . TYR A 1 848  ? -44.339  26.992  40.581  1.00 184.20 ? 848  TYR A O   1 
ATOM   6453  C  CB  . TYR A 1 848  ? -43.487  25.830  37.872  1.00 182.38 ? 848  TYR A CB  1 
ATOM   6454  C  CG  . TYR A 1 848  ? -42.714  26.403  36.695  1.00 180.84 ? 848  TYR A CG  1 
ATOM   6455  C  CD1 . TYR A 1 848  ? -41.452  26.961  36.879  1.00 178.31 ? 848  TYR A CD1 1 
ATOM   6456  C  CD2 . TYR A 1 848  ? -43.269  26.439  35.415  1.00 180.78 ? 848  TYR A CD2 1 
ATOM   6457  C  CE1 . TYR A 1 848  ? -40.756  27.508  35.824  1.00 177.03 ? 848  TYR A CE1 1 
ATOM   6458  C  CE2 . TYR A 1 848  ? -42.585  26.985  34.359  1.00 179.44 ? 848  TYR A CE2 1 
ATOM   6459  C  CZ  . TYR A 1 848  ? -41.329  27.516  34.573  1.00 178.65 ? 848  TYR A CZ  1 
ATOM   6460  O  OH  . TYR A 1 848  ? -40.638  28.061  33.528  1.00 179.98 ? 848  TYR A OH  1 
ATOM   6461  N  N   . ARG A 1 849  ? -43.593  24.970  41.217  1.00 186.83 ? 849  ARG A N   1 
ATOM   6462  C  CA  . ARG A 1 849  ? -44.196  25.014  42.537  1.00 190.56 ? 849  ARG A CA  1 
ATOM   6463  C  C   . ARG A 1 849  ? -43.452  26.106  43.320  1.00 189.35 ? 849  ARG A C   1 
ATOM   6464  O  O   . ARG A 1 849  ? -42.266  26.352  43.071  1.00 186.50 ? 849  ARG A O   1 
ATOM   6465  C  CB  . ARG A 1 849  ? -44.085  23.629  43.198  1.00 195.26 ? 849  ARG A CB  1 
ATOM   6466  C  CG  . ARG A 1 849  ? -44.633  23.509  44.616  1.00 201.36 ? 849  ARG A CG  1 
ATOM   6467  C  CD  . ARG A 1 849  ? -46.104  23.902  44.732  1.00 208.12 ? 849  ARG A CD  1 
ATOM   6468  N  NE  . ARG A 1 849  ? -46.635  23.639  46.073  1.00 212.58 ? 849  ARG A NE  1 
ATOM   6469  C  CZ  . ARG A 1 849  ? -47.764  24.155  46.559  1.00 215.66 ? 849  ARG A CZ  1 
ATOM   6470  N  NH1 . ARG A 1 849  ? -48.495  24.979  45.818  1.00 216.98 ? 849  ARG A NH1 1 
ATOM   6471  N  NH2 . ARG A 1 849  ? -48.164  23.850  47.790  1.00 216.32 ? 849  ARG A NH2 1 
ATOM   6472  N  N   . THR A 1 850  ? -44.152  26.781  44.233  1.00 190.66 ? 850  THR A N   1 
ATOM   6473  C  CA  . THR A 1 850  ? -43.584  27.908  44.985  1.00 188.83 ? 850  THR A CA  1 
ATOM   6474  C  C   . THR A 1 850  ? -42.417  27.491  45.870  1.00 188.10 ? 850  THR A C   1 
ATOM   6475  O  O   . THR A 1 850  ? -41.468  28.256  46.068  1.00 188.84 ? 850  THR A O   1 
ATOM   6476  C  CB  . THR A 1 850  ? -44.646  28.600  45.859  1.00 187.52 ? 850  THR A CB  1 
ATOM   6477  O  OG1 . THR A 1 850  ? -45.407  27.613  46.563  1.00 187.76 ? 850  THR A OG1 1 
ATOM   6478  C  CG2 . THR A 1 850  ? -45.579  29.422  45.000  1.00 187.66 ? 850  THR A CG2 1 
ATOM   6479  N  N   . SER A 1 851  ? -42.513  26.281  46.414  1.00 188.34 ? 851  SER A N   1 
ATOM   6480  C  CA  . SER A 1 851  ? -41.426  25.664  47.172  1.00 188.67 ? 851  SER A CA  1 
ATOM   6481  C  C   . SER A 1 851  ? -40.572  24.746  46.283  1.00 189.50 ? 851  SER A C   1 
ATOM   6482  O  O   . SER A 1 851  ? -40.924  24.469  45.132  1.00 187.79 ? 851  SER A O   1 
ATOM   6483  C  CB  . SER A 1 851  ? -41.982  24.885  48.374  1.00 191.45 ? 851  SER A CB  1 
ATOM   6484  O  OG  . SER A 1 851  ? -42.906  23.884  47.970  1.00 195.03 ? 851  SER A OG  1 
ATOM   6485  N  N   . GLY A 1 852  ? -39.443  24.288  46.815  1.00 191.59 ? 852  GLY A N   1 
ATOM   6486  C  CA  . GLY A 1 852  ? -38.593  23.363  46.092  1.00 190.44 ? 852  GLY A CA  1 
ATOM   6487  C  C   . GLY A 1 852  ? -39.111  21.949  46.240  1.00 186.40 ? 852  GLY A C   1 
ATOM   6488  O  O   . GLY A 1 852  ? -40.133  21.724  46.892  1.00 187.86 ? 852  GLY A O   1 
ATOM   6489  N  N   . MET A 1 853  ? -38.411  20.993  45.635  1.00 180.53 ? 853  MET A N   1 
ATOM   6490  C  CA  . MET A 1 853  ? -38.729  19.580  45.843  1.00 176.66 ? 853  MET A CA  1 
ATOM   6491  C  C   . MET A 1 853  ? -37.633  18.612  45.394  1.00 171.93 ? 853  MET A C   1 
ATOM   6492  O  O   . MET A 1 853  ? -36.603  19.013  44.860  1.00 169.45 ? 853  MET A O   1 
ATOM   6493  C  CB  . MET A 1 853  ? -40.062  19.217  45.184  1.00 178.85 ? 853  MET A CB  1 
ATOM   6494  C  CG  . MET A 1 853  ? -40.040  19.202  43.674  1.00 179.61 ? 853  MET A CG  1 
ATOM   6495  S  SD  . MET A 1 853  ? -41.718  19.135  43.034  1.00 207.75 ? 853  MET A SD  1 
ATOM   6496  C  CE  . MET A 1 853  ? -42.308  20.776  43.470  1.00 217.54 ? 853  MET A CE  1 
ATOM   6497  N  N   . GLN A 1 854  ? -37.862  17.331  45.642  1.00 170.78 ? 854  GLN A N   1 
ATOM   6498  C  CA  . GLN A 1 854  ? -36.919  16.307  45.244  1.00 168.75 ? 854  GLN A CA  1 
ATOM   6499  C  C   . GLN A 1 854  ? -37.416  15.611  43.989  1.00 167.81 ? 854  GLN A C   1 
ATOM   6500  O  O   . GLN A 1 854  ? -38.596  15.264  43.903  1.00 168.96 ? 854  GLN A O   1 
ATOM   6501  C  CB  . GLN A 1 854  ? -36.757  15.296  46.374  1.00 169.88 ? 854  GLN A CB  1 
ATOM   6502  C  CG  . GLN A 1 854  ? -36.549  15.944  47.726  1.00 169.41 ? 854  GLN A CG  1 
ATOM   6503  C  CD  . GLN A 1 854  ? -36.253  14.939  48.831  1.00 170.12 ? 854  GLN A CD  1 
ATOM   6504  O  OE1 . GLN A 1 854  ? -36.380  13.723  48.642  1.00 170.79 ? 854  GLN A OE1 1 
ATOM   6505  N  NE2 . GLN A 1 854  ? -35.857  15.448  49.999  1.00 169.42 ? 854  GLN A NE2 1 
ATOM   6506  N  N   . PHE A 1 855  ? -36.526  15.432  43.009  1.00 164.69 ? 855  PHE A N   1 
ATOM   6507  C  CA  . PHE A 1 855  ? -36.812  14.578  41.846  1.00 162.18 ? 855  PHE A CA  1 
ATOM   6508  C  C   . PHE A 1 855  ? -35.912  13.346  41.749  1.00 163.41 ? 855  PHE A C   1 
ATOM   6509  O  O   . PHE A 1 855  ? -35.301  12.939  42.734  1.00 164.48 ? 855  PHE A O   1 
ATOM   6510  C  CB  . PHE A 1 855  ? -36.805  15.363  40.531  1.00 157.25 ? 855  PHE A CB  1 
ATOM   6511  C  CG  . PHE A 1 855  ? -35.498  16.036  40.205  1.00 150.98 ? 855  PHE A CG  1 
ATOM   6512  C  CD1 . PHE A 1 855  ? -34.576  15.422  39.385  1.00 149.14 ? 855  PHE A CD1 1 
ATOM   6513  C  CD2 . PHE A 1 855  ? -35.219  17.311  40.667  1.00 147.72 ? 855  PHE A CD2 1 
ATOM   6514  C  CE1 . PHE A 1 855  ? -33.382  16.056  39.058  1.00 146.74 ? 855  PHE A CE1 1 
ATOM   6515  C  CE2 . PHE A 1 855  ? -34.026  17.946  40.334  1.00 145.20 ? 855  PHE A CE2 1 
ATOM   6516  C  CZ  . PHE A 1 855  ? -33.110  17.319  39.531  1.00 144.54 ? 855  PHE A CZ  1 
ATOM   6517  N  N   . CYS A 1 856  ? -35.848  12.751  40.561  1.00 163.26 ? 856  CYS A N   1 
ATOM   6518  C  CA  . CYS A 1 856  ? -35.034  11.555  40.324  1.00 164.25 ? 856  CYS A CA  1 
ATOM   6519  C  C   . CYS A 1 856  ? -35.228  11.079  38.889  1.00 167.10 ? 856  CYS A C   1 
ATOM   6520  O  O   . CYS A 1 856  ? -36.007  10.157  38.651  1.00 168.66 ? 856  CYS A O   1 
ATOM   6521  C  CB  . CYS A 1 856  ? -35.435  10.433  41.299  1.00 165.33 ? 856  CYS A CB  1 
ATOM   6522  S  SG  . CYS A 1 856  ? -34.680  8.779   41.042  1.00 203.42 ? 856  CYS A SG  1 
ATOM   6523  N  N   . VAL A 1 857  ? -34.533  11.697  37.933  1.00 166.91 ? 857  VAL A N   1 
ATOM   6524  C  CA  . VAL A 1 857  ? -34.745  11.377  36.515  1.00 166.72 ? 857  VAL A CA  1 
ATOM   6525  C  C   . VAL A 1 857  ? -33.930  10.179  36.061  1.00 167.68 ? 857  VAL A C   1 
ATOM   6526  O  O   . VAL A 1 857  ? -32.727  10.116  36.299  1.00 167.74 ? 857  VAL A O   1 
ATOM   6527  C  CB  . VAL A 1 857  ? -34.390  12.548  35.607  1.00 163.63 ? 857  VAL A CB  1 
ATOM   6528  C  CG1 . VAL A 1 857  ? -35.362  13.688  35.821  1.00 163.25 ? 857  VAL A CG1 1 
ATOM   6529  C  CG2 . VAL A 1 857  ? -32.981  12.985  35.882  1.00 161.06 ? 857  VAL A CG2 1 
ATOM   6530  N  N   . LYS A 1 858  ? -34.583  9.236   35.392  1.00 168.73 ? 858  LYS A N   1 
ATOM   6531  C  CA  . LYS A 1 858  ? -33.894  8.043   34.917  1.00 170.03 ? 858  LYS A CA  1 
ATOM   6532  C  C   . LYS A 1 858  ? -34.224  7.757   33.451  1.00 168.68 ? 858  LYS A C   1 
ATOM   6533  O  O   . LYS A 1 858  ? -35.371  7.881   33.024  1.00 170.18 ? 858  LYS A O   1 
ATOM   6534  C  CB  . LYS A 1 858  ? -34.196  6.830   35.814  1.00 175.69 ? 858  LYS A CB  1 
ATOM   6535  C  CG  . LYS A 1 858  ? -35.676  6.498   35.973  1.00 182.13 ? 858  LYS A CG  1 
ATOM   6536  C  CD  . LYS A 1 858  ? -35.897  5.251   36.836  1.00 187.03 ? 858  LYS A CD  1 
ATOM   6537  C  CE  . LYS A 1 858  ? -37.363  4.803   36.799  1.00 191.60 ? 858  LYS A CE  1 
ATOM   6538  N  NZ  . LYS A 1 858  ? -37.664  3.704   37.770  1.00 193.69 ? 858  LYS A NZ  1 
ATOM   6539  N  N   . MET A 1 859  ? -33.197  7.394   32.686  1.00 164.98 ? 859  MET A N   1 
ATOM   6540  C  CA  . MET A 1 859  ? -33.322  7.129   31.256  1.00 161.63 ? 859  MET A CA  1 
ATOM   6541  C  C   . MET A 1 859  ? -33.379  5.640   30.942  1.00 161.57 ? 859  MET A C   1 
ATOM   6542  O  O   . MET A 1 859  ? -32.723  4.830   31.583  1.00 161.30 ? 859  MET A O   1 
ATOM   6543  C  CB  . MET A 1 859  ? -32.168  7.787   30.514  1.00 158.15 ? 859  MET A CB  1 
ATOM   6544  C  CG  . MET A 1 859  ? -31.455  6.891   29.547  1.00 157.86 ? 859  MET A CG  1 
ATOM   6545  S  SD  . MET A 1 859  ? -29.914  7.659   29.021  1.00 118.00 ? 859  MET A SD  1 
ATOM   6546  C  CE  . MET A 1 859  ? -30.545  8.806   27.790  1.00 190.60 ? 859  MET A CE  1 
ATOM   6547  N  N   . SER A 1 860  ? -34.168  5.288   29.940  1.00 163.20 ? 860  SER A N   1 
ATOM   6548  C  CA  . SER A 1 860  ? -34.425  3.895   29.619  1.00 165.98 ? 860  SER A CA  1 
ATOM   6549  C  C   . SER A 1 860  ? -33.449  3.269   28.616  1.00 166.49 ? 860  SER A C   1 
ATOM   6550  O  O   . SER A 1 860  ? -33.392  3.669   27.450  1.00 167.01 ? 860  SER A O   1 
ATOM   6551  C  CB  . SER A 1 860  ? -35.850  3.753   29.103  1.00 169.01 ? 860  SER A CB  1 
ATOM   6552  O  OG  . SER A 1 860  ? -35.912  2.759   28.098  1.00 172.12 ? 860  SER A OG  1 
ATOM   6553  N  N   . ALA A 1 861  ? -32.709  2.260   29.075  1.00 166.42 ? 861  ALA A N   1 
ATOM   6554  C  CA  . ALA A 1 861  ? -31.774  1.512   28.229  1.00 164.16 ? 861  ALA A CA  1 
ATOM   6555  C  C   . ALA A 1 861  ? -32.473  0.810   27.058  1.00 163.70 ? 861  ALA A C   1 
ATOM   6556  O  O   . ALA A 1 861  ? -33.062  -0.257  27.223  1.00 162.95 ? 861  ALA A O   1 
ATOM   6557  C  CB  . ALA A 1 861  ? -30.988  0.493   29.075  1.00 163.66 ? 861  ALA A CB  1 
ATOM   6558  N  N   . VAL A 1 862  ? -32.404  1.408   25.876  1.00 163.00 ? 862  VAL A N   1 
ATOM   6559  C  CA  . VAL A 1 862  ? -32.991  0.778   24.707  1.00 164.98 ? 862  VAL A CA  1 
ATOM   6560  C  C   . VAL A 1 862  ? -31.960  0.010   23.900  1.00 164.24 ? 862  VAL A C   1 
ATOM   6561  O  O   . VAL A 1 862  ? -30.860  0.501   23.663  1.00 164.27 ? 862  VAL A O   1 
ATOM   6562  C  CB  . VAL A 1 862  ? -33.678  1.784   23.805  1.00 166.62 ? 862  VAL A CB  1 
ATOM   6563  C  CG1 . VAL A 1 862  ? -34.228  1.072   22.582  1.00 168.78 ? 862  VAL A CG1 1 
ATOM   6564  C  CG2 . VAL A 1 862  ? -34.787  2.484   24.564  1.00 166.53 ? 862  VAL A CG2 1 
ATOM   6565  N  N   . GLU A 1 863  ? -32.360  -1.176  23.445  1.00 162.31 ? 863  GLU A N   1 
ATOM   6566  C  CA  . GLU A 1 863  ? -31.445  -2.207  22.947  1.00 159.97 ? 863  GLU A CA  1 
ATOM   6567  C  C   . GLU A 1 863  ? -30.087  -1.743  22.404  1.00 154.17 ? 863  GLU A C   1 
ATOM   6568  O  O   . GLU A 1 863  ? -29.044  -2.242  22.827  1.00 151.45 ? 863  GLU A O   1 
ATOM   6569  C  CB  . GLU A 1 863  ? -32.149  -3.096  21.906  1.00 167.79 ? 863  GLU A CB  1 
ATOM   6570  C  CG  . GLU A 1 863  ? -32.714  -4.439  22.433  1.00 180.47 ? 863  GLU A CG  1 
ATOM   6571  C  CD  . GLU A 1 863  ? -31.703  -5.603  22.401  1.00 185.43 ? 863  GLU A CD  1 
ATOM   6572  O  OE1 . GLU A 1 863  ? -30.566  -5.436  22.913  1.00 184.45 ? 863  GLU A OE1 1 
ATOM   6573  O  OE2 . GLU A 1 863  ? -32.061  -6.690  21.875  1.00 188.29 ? 863  GLU A OE2 1 
ATOM   6574  N  N   . GLY A 1 864  ? -30.094  -0.806  21.466  1.00 151.85 ? 864  GLY A N   1 
ATOM   6575  C  CA  . GLY A 1 864  ? -28.893  -0.521  20.700  1.00 150.48 ? 864  GLY A CA  1 
ATOM   6576  C  C   . GLY A 1 864  ? -27.998  0.564   21.251  1.00 145.49 ? 864  GLY A C   1 
ATOM   6577  O  O   . GLY A 1 864  ? -27.053  1.010   20.593  1.00 145.49 ? 864  GLY A O   1 
ATOM   6578  N  N   . ILE A 1 865  ? -28.281  0.981   22.476  1.00 143.12 ? 865  ILE A N   1 
ATOM   6579  C  CA  . ILE A 1 865  ? -27.620  2.150   23.032  1.00 137.66 ? 865  ILE A CA  1 
ATOM   6580  C  C   . ILE A 1 865  ? -26.901  1.881   24.338  1.00 137.23 ? 865  ILE A C   1 
ATOM   6581  O  O   . ILE A 1 865  ? -27.503  1.437   25.316  1.00 136.55 ? 865  ILE A O   1 
ATOM   6582  C  CB  . ILE A 1 865  ? -28.619  3.277   23.275  1.00 133.88 ? 865  ILE A CB  1 
ATOM   6583  C  CG1 . ILE A 1 865  ? -29.571  3.409   22.085  1.00 133.86 ? 865  ILE A CG1 1 
ATOM   6584  C  CG2 . ILE A 1 865  ? -27.877  4.563   23.525  1.00 131.28 ? 865  ILE A CG2 1 
ATOM   6585  C  CD1 . ILE A 1 865  ? -30.497  4.589   22.192  1.00 133.15 ? 865  ILE A CD1 1 
ATOM   6586  N  N   . CYS A 1 866  ? -25.605  2.170   24.338  1.00 140.30 ? 866  CYS A N   1 
ATOM   6587  C  CA  . CYS A 1 866  ? -24.776  1.996   25.517  1.00 144.87 ? 866  CYS A CA  1 
ATOM   6588  C  C   . CYS A 1 866  ? -25.101  3.025   26.578  1.00 152.14 ? 866  CYS A C   1 
ATOM   6589  O  O   . CYS A 1 866  ? -25.659  4.080   26.284  1.00 148.01 ? 866  CYS A O   1 
ATOM   6590  C  CB  . CYS A 1 866  ? -23.298  2.096   25.160  1.00 142.28 ? 866  CYS A CB  1 
ATOM   6591  S  SG  . CYS A 1 866  ? -22.557  0.506   24.844  1.00 146.62 ? 866  CYS A SG  1 
ATOM   6592  N  N   . THR A 1 867  ? -24.726  2.704   27.810  1.00 164.09 ? 867  THR A N   1 
ATOM   6593  C  CA  . THR A 1 867  ? -25.020  3.550   28.954  1.00 173.82 ? 867  THR A CA  1 
ATOM   6594  C  C   . THR A 1 867  ? -24.319  3.057   30.217  1.00 185.51 ? 867  THR A C   1 
ATOM   6595  O  O   . THR A 1 867  ? -23.753  1.963   30.249  1.00 186.21 ? 867  THR A O   1 
ATOM   6596  C  CB  . THR A 1 867  ? -26.552  3.677   29.207  1.00 163.35 ? 867  THR A CB  1 
ATOM   6597  O  OG1 . THR A 1 867  ? -27.268  2.754   28.372  1.00 163.97 ? 867  THR A OG1 1 
ATOM   6598  C  CG2 . THR A 1 867  ? -27.036  5.087   28.903  1.00 161.62 ? 867  THR A CG2 1 
ATOM   6599  N  N   . SER A 1 868  ? -24.376  3.883   31.255  1.00 194.81 ? 868  SER A N   1 
ATOM   6600  C  CA  . SER A 1 868  ? -23.638  3.647   32.490  1.00 207.33 ? 868  SER A CA  1 
ATOM   6601  C  C   . SER A 1 868  ? -24.310  2.654   33.449  1.00 221.80 ? 868  SER A C   1 
ATOM   6602  O  O   . SER A 1 868  ? -23.667  2.159   34.375  1.00 221.48 ? 868  SER A O   1 
ATOM   6603  C  CB  . SER A 1 868  ? -23.376  4.979   33.202  1.00 206.28 ? 868  SER A CB  1 
ATOM   6604  O  OG  . SER A 1 868  ? -22.923  5.964   32.285  1.00 205.94 ? 868  SER A OG  1 
ATOM   6605  N  N   . GLU A 1 869  ? -25.598  2.379   33.246  1.00 236.20 ? 869  GLU A N   1 
ATOM   6606  C  CA  . GLU A 1 869  ? -26.299  1.373   34.052  1.00 249.64 ? 869  GLU A CA  1 
ATOM   6607  C  C   . GLU A 1 869  ? -26.045  -0.023  33.475  1.00 258.05 ? 869  GLU A C   1 
ATOM   6608  O  O   . GLU A 1 869  ? -25.813  -0.170  32.273  1.00 258.81 ? 869  GLU A O   1 
ATOM   6609  C  CB  . GLU A 1 869  ? -27.803  1.681   34.138  1.00 252.58 ? 869  GLU A CB  1 
ATOM   6610  C  CG  . GLU A 1 869  ? -28.606  0.775   35.085  1.00 254.76 ? 869  GLU A CG  1 
ATOM   6611  C  CD  . GLU A 1 869  ? -29.122  -0.497  34.414  1.00 256.22 ? 869  GLU A CD  1 
ATOM   6612  O  OE1 . GLU A 1 869  ? -29.168  -0.540  33.168  1.00 256.54 ? 869  GLU A OE1 1 
ATOM   6613  O  OE2 . GLU A 1 869  ? -29.490  -1.454  35.130  1.00 256.84 ? 869  GLU A OE2 1 
ATOM   6614  N  N   . SER A 1 870  ? -26.081  -1.041  34.332  1.00 264.96 ? 870  SER A N   1 
ATOM   6615  C  CA  . SER A 1 870  ? -25.747  -2.406  33.923  1.00 270.29 ? 870  SER A CA  1 
ATOM   6616  C  C   . SER A 1 870  ? -26.634  -2.905  32.785  1.00 273.49 ? 870  SER A C   1 
ATOM   6617  O  O   . SER A 1 870  ? -27.858  -2.801  32.846  1.00 275.46 ? 870  SER A O   1 
ATOM   6618  C  CB  . SER A 1 870  ? -25.826  -3.364  35.115  1.00 273.30 ? 870  SER A CB  1 
ATOM   6619  O  OG  . SER A 1 870  ? -27.138  -3.407  35.644  1.00 275.85 ? 870  SER A OG  1 
ATOM   6620  N  N   . LYS A 1 882  ? -31.151  4.195   36.880  1.00 222.88 ? 882  LYS A N   1 
ATOM   6621  C  CA  . LYS A 1 882  ? -30.815  4.288   38.305  1.00 223.57 ? 882  LYS A CA  1 
ATOM   6622  C  C   . LYS A 1 882  ? -31.422  5.535   38.955  1.00 220.33 ? 882  LYS A C   1 
ATOM   6623  O  O   . LYS A 1 882  ? -31.462  6.595   38.337  1.00 219.11 ? 882  LYS A O   1 
ATOM   6624  C  CB  . LYS A 1 882  ? -29.291  4.256   38.514  1.00 224.41 ? 882  LYS A CB  1 
ATOM   6625  C  CG  . LYS A 1 882  ? -28.526  5.483   38.007  1.00 224.40 ? 882  LYS A CG  1 
ATOM   6626  C  CD  . LYS A 1 882  ? -27.005  5.353   38.215  1.00 224.49 ? 882  LYS A CD  1 
ATOM   6627  C  CE  . LYS A 1 882  ? -26.384  4.276   37.315  1.00 226.31 ? 882  LYS A CE  1 
ATOM   6628  N  NZ  . LYS A 1 882  ? -24.890  4.168   37.420  1.00 225.17 ? 882  LYS A NZ  1 
ATOM   6629  N  N   . CYS A 1 883  ? -31.889  5.410   40.198  1.00 219.33 ? 883  CYS A N   1 
ATOM   6630  C  CA  . CYS A 1 883  ? -32.567  6.526   40.869  1.00 216.84 ? 883  CYS A CA  1 
ATOM   6631  C  C   . CYS A 1 883  ? -31.645  7.532   41.572  1.00 212.14 ? 883  CYS A C   1 
ATOM   6632  O  O   . CYS A 1 883  ? -31.568  7.565   42.804  1.00 212.18 ? 883  CYS A O   1 
ATOM   6633  C  CB  . CYS A 1 883  ? -33.618  6.026   41.859  1.00 218.27 ? 883  CYS A CB  1 
ATOM   6634  S  SG  . CYS A 1 883  ? -34.614  7.377   42.520  1.00 271.76 ? 883  CYS A SG  1 
ATOM   6635  N  N   . VAL A 1 884  ? -30.977  8.365   40.777  1.00 209.11 ? 884  VAL A N   1 
ATOM   6636  C  CA  . VAL A 1 884  ? -30.136  9.447   41.288  1.00 205.86 ? 884  VAL A CA  1 
ATOM   6637  C  C   . VAL A 1 884  ? -30.999  10.642  41.715  1.00 206.80 ? 884  VAL A C   1 
ATOM   6638  O  O   . VAL A 1 884  ? -31.229  11.570  40.930  1.00 205.78 ? 884  VAL A O   1 
ATOM   6639  C  CB  . VAL A 1 884  ? -29.098  9.897   40.221  1.00 168.94 ? 884  VAL A CB  1 
ATOM   6640  C  CG1 . VAL A 1 884  ? -28.138  8.758   39.888  1.00 168.81 ? 884  VAL A CG1 1 
ATOM   6641  C  CG2 . VAL A 1 884  ? -29.790  10.385  38.948  1.00 169.53 ? 884  VAL A CG2 1 
ATOM   6642  N  N   . ARG A 1 885  ? -31.478  10.624  42.959  1.00 207.29 ? 885  ARG A N   1 
ATOM   6643  C  CA  . ARG A 1 885  ? -32.447  11.632  43.398  1.00 206.61 ? 885  ARG A CA  1 
ATOM   6644  C  C   . ARG A 1 885  ? -31.827  12.944  43.857  1.00 203.70 ? 885  ARG A C   1 
ATOM   6645  O  O   . ARG A 1 885  ? -31.039  13.003  44.797  1.00 202.02 ? 885  ARG A O   1 
ATOM   6646  C  CB  . ARG A 1 885  ? -33.411  11.084  44.450  1.00 207.79 ? 885  ARG A CB  1 
ATOM   6647  C  CG  . ARG A 1 885  ? -32.749  10.577  45.690  1.00 207.37 ? 885  ARG A CG  1 
ATOM   6648  C  CD  . ARG A 1 885  ? -33.768  10.371  46.791  1.00 208.83 ? 885  ARG A CD  1 
ATOM   6649  N  NE  . ARG A 1 885  ? -34.878  9.521   46.362  1.00 211.14 ? 885  ARG A NE  1 
ATOM   6650  C  CZ  . ARG A 1 885  ? -35.983  9.334   47.077  1.00 213.27 ? 885  ARG A CZ  1 
ATOM   6651  N  NH1 . ARG A 1 885  ? -36.122  9.946   48.250  1.00 213.54 ? 885  ARG A NH1 1 
ATOM   6652  N  NH2 . ARG A 1 885  ? -36.950  8.546   46.622  1.00 214.83 ? 885  ARG A NH2 1 
ATOM   6653  N  N   . GLN A 1 886  ? -32.223  14.000  43.169  1.00 202.70 ? 886  GLN A N   1 
ATOM   6654  C  CA  . GLN A 1 886  ? -31.649  15.310  43.353  1.00 202.75 ? 886  GLN A CA  1 
ATOM   6655  C  C   . GLN A 1 886  ? -32.642  16.231  44.046  1.00 198.69 ? 886  GLN A C   1 
ATOM   6656  O  O   . GLN A 1 886  ? -33.712  15.794  44.466  1.00 200.12 ? 886  GLN A O   1 
ATOM   6657  C  CB  . GLN A 1 886  ? -31.303  15.874  41.987  1.00 208.22 ? 886  GLN A CB  1 
ATOM   6658  C  CG  . GLN A 1 886  ? -30.304  16.984  42.025  1.00 213.29 ? 886  GLN A CG  1 
ATOM   6659  C  CD  . GLN A 1 886  ? -28.886  16.473  42.067  1.00 217.23 ? 886  GLN A CD  1 
ATOM   6660  O  OE1 . GLN A 1 886  ? -27.931  17.255  41.976  1.00 218.84 ? 886  GLN A OE1 1 
ATOM   6661  N  NE2 . GLN A 1 886  ? -28.734  15.155  42.186  1.00 218.21 ? 886  GLN A NE2 1 
ATOM   6662  N  N   . LYS A 1 887  ? -32.297  17.512  44.143  1.00 195.05 ? 887  LYS A N   1 
ATOM   6663  C  CA  . LYS A 1 887  ? -33.173  18.496  44.767  1.00 193.60 ? 887  LYS A CA  1 
ATOM   6664  C  C   . LYS A 1 887  ? -33.292  19.727  43.877  1.00 189.94 ? 887  LYS A C   1 
ATOM   6665  O  O   . LYS A 1 887  ? -32.283  20.347  43.550  1.00 185.46 ? 887  LYS A O   1 
ATOM   6666  C  CB  . LYS A 1 887  ? -32.628  18.919  46.140  1.00 193.88 ? 887  LYS A CB  1 
ATOM   6667  C  CG  . LYS A 1 887  ? -32.066  17.798  47.020  1.00 195.11 ? 887  LYS A CG  1 
ATOM   6668  C  CD  . LYS A 1 887  ? -30.604  17.496  46.686  1.00 194.81 ? 887  LYS A CD  1 
ATOM   6669  C  CE  . LYS A 1 887  ? -30.015  16.385  47.565  1.00 195.25 ? 887  LYS A CE  1 
ATOM   6670  N  NZ  . LYS A 1 887  ? -29.685  16.843  48.943  1.00 194.45 ? 887  LYS A NZ  1 
ATOM   6671  N  N   . VAL A 1 888  ? -34.517  20.076  43.483  1.00 192.44 ? 888  VAL A N   1 
ATOM   6672  C  CA  . VAL A 1 888  ? -34.761  21.282  42.687  1.00 191.82 ? 888  VAL A CA  1 
ATOM   6673  C  C   . VAL A 1 888  ? -35.226  22.438  43.523  1.00 194.90 ? 888  VAL A C   1 
ATOM   6674  O  O   . VAL A 1 888  ? -36.319  22.398  44.084  1.00 198.81 ? 888  VAL A O   1 
ATOM   6675  C  CB  . VAL A 1 888  ? -35.877  21.089  41.666  1.00 189.05 ? 888  VAL A CB  1 
ATOM   6676  C  CG1 . VAL A 1 888  ? -35.304  20.841  40.283  1.00 187.78 ? 888  VAL A CG1 1 
ATOM   6677  C  CG2 . VAL A 1 888  ? -36.818  19.984  42.121  1.00 188.99 ? 888  VAL A CG2 1 
ATOM   6678  N  N   . GLU A 1 889  ? -34.419  23.488  43.570  1.00 195.36 ? 889  GLU A N   1 
ATOM   6679  C  CA  . GLU A 1 889  ? -34.802  24.699  44.283  1.00 200.41 ? 889  GLU A CA  1 
ATOM   6680  C  C   . GLU A 1 889  ? -36.100  25.286  43.692  1.00 198.48 ? 889  GLU A C   1 
ATOM   6681  O  O   . GLU A 1 889  ? -36.312  25.257  42.477  1.00 194.95 ? 889  GLU A O   1 
ATOM   6682  C  CB  . GLU A 1 889  ? -33.648  25.714  44.286  1.00 210.14 ? 889  GLU A CB  1 
ATOM   6683  C  CG  . GLU A 1 889  ? -33.176  26.177  42.897  1.00 220.98 ? 889  GLU A CG  1 
ATOM   6684  C  CD  . GLU A 1 889  ? -32.294  25.166  42.160  1.00 229.76 ? 889  GLU A CD  1 
ATOM   6685  O  OE1 . GLU A 1 889  ? -31.960  24.108  42.743  1.00 233.22 ? 889  GLU A OE1 1 
ATOM   6686  O  OE2 . GLU A 1 889  ? -31.931  25.443  40.991  1.00 232.19 ? 889  GLU A OE2 1 
ATOM   6687  N  N   . GLY A 1 890  ? -36.967  25.800  44.562  1.00 198.67 ? 890  GLY A N   1 
ATOM   6688  C  CA  . GLY A 1 890  ? -38.298  26.232  44.169  1.00 196.88 ? 890  GLY A CA  1 
ATOM   6689  C  C   . GLY A 1 890  ? -38.327  27.276  43.074  1.00 188.60 ? 890  GLY A C   1 
ATOM   6690  O  O   . GLY A 1 890  ? -37.473  28.155  43.026  1.00 186.74 ? 890  GLY A O   1 
ATOM   6691  N  N   . SER A 1 891  ? -39.319  27.170  42.195  1.00 183.71 ? 891  SER A N   1 
ATOM   6692  C  CA  . SER A 1 891  ? -39.494  28.110  41.085  1.00 178.38 ? 891  SER A CA  1 
ATOM   6693  C  C   . SER A 1 891  ? -38.260  28.233  40.204  1.00 175.16 ? 891  SER A C   1 
ATOM   6694  O  O   . SER A 1 891  ? -37.950  29.323  39.707  1.00 175.40 ? 891  SER A O   1 
ATOM   6695  C  CB  . SER A 1 891  ? -39.881  29.487  41.601  1.00 175.50 ? 891  SER A CB  1 
ATOM   6696  O  OG  . SER A 1 891  ? -41.036  29.393  42.402  1.00 176.97 ? 891  SER A OG  1 
ATOM   6697  N  N   . SER A 1 892  ? -37.574  27.108  40.007  1.00 173.28 ? 892  SER A N   1 
ATOM   6698  C  CA  . SER A 1 892  ? -36.322  27.073  39.255  1.00 170.49 ? 892  SER A CA  1 
ATOM   6699  C  C   . SER A 1 892  ? -36.230  25.799  38.437  1.00 170.06 ? 892  SER A C   1 
ATOM   6700  O  O   . SER A 1 892  ? -37.253  25.236  38.049  1.00 169.07 ? 892  SER A O   1 
ATOM   6701  C  CB  . SER A 1 892  ? -35.119  27.141  40.198  1.00 169.30 ? 892  SER A CB  1 
ATOM   6702  O  OG  . SER A 1 892  ? -35.086  28.361  40.914  1.00 169.06 ? 892  SER A OG  1 
ATOM   6703  N  N   . SER A 1 893  ? -35.000  25.350  38.189  1.00 170.63 ? 893  SER A N   1 
ATOM   6704  C  CA  . SER A 1 893  ? -34.760  24.145  37.405  1.00 171.18 ? 893  SER A CA  1 
ATOM   6705  C  C   . SER A 1 893  ? -33.366  23.562  37.586  1.00 171.99 ? 893  SER A C   1 
ATOM   6706  O  O   . SER A 1 893  ? -32.381  24.290  37.601  1.00 171.58 ? 893  SER A O   1 
ATOM   6707  C  CB  . SER A 1 893  ? -34.944  24.441  35.930  1.00 170.37 ? 893  SER A CB  1 
ATOM   6708  O  OG  . SER A 1 893  ? -34.736  23.261  35.180  1.00 169.82 ? 893  SER A OG  1 
ATOM   6709  N  N   . HIS A 1 894  ? -33.287  22.238  37.690  1.00 174.97 ? 894  HIS A N   1 
ATOM   6710  C  CA  . HIS A 1 894  ? -31.999  21.558  37.828  1.00 183.71 ? 894  HIS A CA  1 
ATOM   6711  C  C   . HIS A 1 894  ? -31.574  20.832  36.570  1.00 167.51 ? 894  HIS A C   1 
ATOM   6712  O  O   . HIS A 1 894  ? -32.240  19.897  36.138  1.00 165.69 ? 894  HIS A O   1 
ATOM   6713  C  CB  . HIS A 1 894  ? -32.045  20.554  38.980  1.00 221.77 ? 894  HIS A CB  1 
ATOM   6714  C  CG  . HIS A 1 894  ? -30.835  19.586  39.014  1.00 268.77 ? 894  HIS A CG  1 
ATOM   6715  N  ND1 . HIS A 1 894  ? -30.826  18.432  39.767  1.00 295.25 ? 894  HIS A ND1 1 
ATOM   6716  C  CD2 . HIS A 1 894  ? -29.638  19.636  38.385  1.00 288.89 ? 894  HIS A CD2 1 
ATOM   6717  C  CE1 . HIS A 1 894  ? -29.673  17.812  39.601  1.00 317.11 ? 894  HIS A CE1 1 
ATOM   6718  N  NE2 . HIS A 1 894  ? -28.935  18.521  38.767  1.00 305.03 ? 894  HIS A NE2 1 
ATOM   6719  N  N   . LEU A 1 895  ? -30.446  21.248  36.007  1.00 157.35 ? 895  LEU A N   1 
ATOM   6720  C  CA  . LEU A 1 895  ? -29.885  20.583  34.845  1.00 151.18 ? 895  LEU A CA  1 
ATOM   6721  C  C   . LEU A 1 895  ? -29.855  19.098  35.029  1.00 142.22 ? 895  LEU A C   1 
ATOM   6722  O  O   . LEU A 1 895  ? -29.632  18.601  36.129  1.00 142.17 ? 895  LEU A O   1 
ATOM   6723  C  CB  . LEU A 1 895  ? -28.464  21.048  34.614  1.00 152.74 ? 895  LEU A CB  1 
ATOM   6724  C  CG  . LEU A 1 895  ? -28.338  21.933  33.392  1.00 155.24 ? 895  LEU A CG  1 
ATOM   6725  C  CD1 . LEU A 1 895  ? -27.405  23.079  33.714  1.00 154.90 ? 895  LEU A CD1 1 
ATOM   6726  C  CD2 . LEU A 1 895  ? -27.881  21.112  32.178  1.00 155.19 ? 895  LEU A CD2 1 
ATOM   6727  N  N   . VAL A 1 896  ? -30.073  18.391  33.935  1.00 133.78 ? 896  VAL A N   1 
ATOM   6728  C  CA  . VAL A 1 896  ? -29.952  16.959  33.941  1.00 125.46 ? 896  VAL A CA  1 
ATOM   6729  C  C   . VAL A 1 896  ? -29.072  16.666  32.762  1.00 123.36 ? 896  VAL A C   1 
ATOM   6730  O  O   . VAL A 1 896  ? -28.924  17.506  31.871  1.00 123.77 ? 896  VAL A O   1 
ATOM   6731  C  CB  . VAL A 1 896  ? -31.292  16.274  33.709  1.00 121.66 ? 896  VAL A CB  1 
ATOM   6732  C  CG1 . VAL A 1 896  ? -31.188  14.834  34.077  1.00 121.67 ? 896  VAL A CG1 1 
ATOM   6733  C  CG2 . VAL A 1 896  ? -32.372  16.918  34.520  1.00 119.44 ? 896  VAL A CG2 1 
ATOM   6734  N  N   . THR A 1 897  ? -28.466  15.487  32.767  1.00 120.81 ? 897  THR A N   1 
ATOM   6735  C  CA  . THR A 1 897  ? -27.718  15.016  31.618  1.00 117.15 ? 897  THR A CA  1 
ATOM   6736  C  C   . THR A 1 897  ? -27.548  13.516  31.686  1.00 118.55 ? 897  THR A C   1 
ATOM   6737  O  O   . THR A 1 897  ? -27.674  12.896  32.748  1.00 119.50 ? 897  THR A O   1 
ATOM   6738  C  CB  . THR A 1 897  ? -26.302  15.564  31.583  1.00 112.93 ? 897  THR A CB  1 
ATOM   6739  O  OG1 . THR A 1 897  ? -25.383  14.466  31.684  1.00 113.22 ? 897  THR A OG1 1 
ATOM   6740  C  CG2 . THR A 1 897  ? -26.073  16.524  32.726  1.00 111.34 ? 897  THR A CG2 1 
ATOM   6741  N  N   . PHE A 1 898  ? -27.237  12.953  30.527  1.00 118.92 ? 898  PHE A N   1 
ATOM   6742  C  CA  . PHE A 1 898  ? -26.911  11.548  30.382  1.00 118.16 ? 898  PHE A CA  1 
ATOM   6743  C  C   . PHE A 1 898  ? -25.926  11.453  29.238  1.00 117.25 ? 898  PHE A C   1 
ATOM   6744  O  O   . PHE A 1 898  ? -26.003  12.214  28.271  1.00 115.40 ? 898  PHE A O   1 
ATOM   6745  C  CB  . PHE A 1 898  ? -28.147  10.719  30.014  1.00 119.15 ? 898  PHE A CB  1 
ATOM   6746  C  CG  . PHE A 1 898  ? -29.274  10.827  30.998  1.00 118.62 ? 898  PHE A CG  1 
ATOM   6747  C  CD1 . PHE A 1 898  ? -29.607  9.759   31.803  1.00 118.72 ? 898  PHE A CD1 1 
ATOM   6748  C  CD2 . PHE A 1 898  ? -30.011  11.994  31.104  1.00 118.04 ? 898  PHE A CD2 1 
ATOM   6749  C  CE1 . PHE A 1 898  ? -30.640  9.854   32.697  1.00 119.64 ? 898  PHE A CE1 1 
ATOM   6750  C  CE2 . PHE A 1 898  ? -31.044  12.092  31.999  1.00 118.72 ? 898  PHE A CE2 1 
ATOM   6751  C  CZ  . PHE A 1 898  ? -31.360  11.019  32.796  1.00 119.83 ? 898  PHE A CZ  1 
ATOM   6752  N  N   . THR A 1 899  ? -24.997  10.521  29.344  1.00 115.92 ? 899  THR A N   1 
ATOM   6753  C  CA  . THR A 1 899  ? -24.160  10.204  28.214  1.00 113.31 ? 899  THR A CA  1 
ATOM   6754  C  C   . THR A 1 899  ? -24.643  8.856   27.652  1.00 110.91 ? 899  THR A C   1 
ATOM   6755  O  O   . THR A 1 899  ? -25.017  7.970   28.420  1.00 109.79 ? 899  THR A O   1 
ATOM   6756  C  CB  . THR A 1 899  ? -22.655  10.275  28.609  1.00 114.49 ? 899  THR A CB  1 
ATOM   6757  O  OG1 . THR A 1 899  ? -22.366  9.316   29.636  1.00 116.17 ? 899  THR A OG1 1 
ATOM   6758  C  CG2 . THR A 1 899  ? -22.312  11.679  29.130  1.00 109.79 ? 899  THR A CG2 1 
ATOM   6759  N  N   . VAL A 1 900  ? -24.718  8.764   26.317  1.00 111.83 ? 900  VAL A N   1 
ATOM   6760  C  CA  . VAL A 1 900  ? -25.094  7.546   25.560  1.00 111.64 ? 900  VAL A CA  1 
ATOM   6761  C  C   . VAL A 1 900  ? -24.185  7.361   24.356  1.00 108.76 ? 900  VAL A C   1 
ATOM   6762  O  O   . VAL A 1 900  ? -23.300  8.165   24.091  1.00 107.71 ? 900  VAL A O   1 
ATOM   6763  C  CB  . VAL A 1 900  ? -26.556  7.566   24.982  1.00 96.50  ? 900  VAL A CB  1 
ATOM   6764  C  CG1 . VAL A 1 900  ? -27.550  6.940   25.942  1.00 98.07  ? 900  VAL A CG1 1 
ATOM   6765  C  CG2 . VAL A 1 900  ? -26.989  8.954   24.593  1.00 95.90  ? 900  VAL A CG2 1 
ATOM   6766  N  N   . LEU A 1 901  ? -24.407  6.303   23.607  1.00 110.57 ? 901  LEU A N   1 
ATOM   6767  C  CA  . LEU A 1 901  ? -23.564  6.079   22.449  1.00 115.46 ? 901  LEU A CA  1 
ATOM   6768  C  C   . LEU A 1 901  ? -24.083  4.911   21.608  1.00 122.00 ? 901  LEU A C   1 
ATOM   6769  O  O   . LEU A 1 901  ? -23.912  3.740   21.981  1.00 125.24 ? 901  LEU A O   1 
ATOM   6770  C  CB  . LEU A 1 901  ? -22.112  5.882   22.896  1.00 112.91 ? 901  LEU A CB  1 
ATOM   6771  C  CG  . LEU A 1 901  ? -21.180  5.030   22.042  1.00 113.66 ? 901  LEU A CG  1 
ATOM   6772  C  CD1 . LEU A 1 901  ? -19.811  5.661   21.971  1.00 111.07 ? 901  LEU A CD1 1 
ATOM   6773  C  CD2 . LEU A 1 901  ? -21.112  3.635   22.630  1.00 115.01 ? 901  LEU A CD2 1 
ATOM   6774  N  N   . PRO A 1 902  ? -24.733  5.231   20.468  1.00 124.55 ? 902  PRO A N   1 
ATOM   6775  C  CA  . PRO A 1 902  ? -25.465  4.202   19.740  1.00 127.12 ? 902  PRO A CA  1 
ATOM   6776  C  C   . PRO A 1 902  ? -24.547  3.497   18.754  1.00 130.31 ? 902  PRO A C   1 
ATOM   6777  O  O   . PRO A 1 902  ? -23.661  4.139   18.179  1.00 129.26 ? 902  PRO A O   1 
ATOM   6778  C  CB  . PRO A 1 902  ? -26.534  5.016   19.003  1.00 128.65 ? 902  PRO A CB  1 
ATOM   6779  C  CG  . PRO A 1 902  ? -26.310  6.498   19.422  1.00 120.39 ? 902  PRO A CG  1 
ATOM   6780  C  CD  . PRO A 1 902  ? -24.893  6.544   19.824  1.00 120.01 ? 902  PRO A CD  1 
ATOM   6781  N  N   . LEU A 1 903  ? -24.733  2.190   18.591  1.00 134.15 ? 903  LEU A N   1 
ATOM   6782  C  CA  . LEU A 1 903  ? -24.005  1.426   17.573  1.00 137.03 ? 903  LEU A CA  1 
ATOM   6783  C  C   . LEU A 1 903  ? -24.978  1.015   16.463  1.00 140.50 ? 903  LEU A C   1 
ATOM   6784  O  O   . LEU A 1 903  ? -24.609  0.836   15.302  1.00 142.32 ? 903  LEU A O   1 
ATOM   6785  C  CB  . LEU A 1 903  ? -23.318  0.182   18.180  1.00 136.62 ? 903  LEU A CB  1 
ATOM   6786  C  CG  . LEU A 1 903  ? -22.573  0.233   19.527  1.00 135.14 ? 903  LEU A CG  1 
ATOM   6787  C  CD1 . LEU A 1 903  ? -21.448  1.265   19.528  1.00 132.92 ? 903  LEU A CD1 1 
ATOM   6788  C  CD2 . LEU A 1 903  ? -23.520  0.464   20.707  1.00 134.63 ? 903  LEU A CD2 1 
ATOM   6789  N  N   . GLU A 1 904  ? -26.234  0.856   16.837  1.00 141.52 ? 904  GLU A N   1 
ATOM   6790  C  CA  . GLU A 1 904  ? -27.246  0.527   15.864  1.00 147.81 ? 904  GLU A CA  1 
ATOM   6791  C  C   . GLU A 1 904  ? -27.780  1.791   15.180  1.00 144.85 ? 904  GLU A C   1 
ATOM   6792  O  O   . GLU A 1 904  ? -28.290  2.721   15.847  1.00 142.16 ? 904  GLU A O   1 
ATOM   6793  C  CB  . GLU A 1 904  ? -28.351  -0.296  16.519  1.00 155.00 ? 904  GLU A CB  1 
ATOM   6794  C  CG  . GLU A 1 904  ? -27.819  -1.565  17.180  1.00 161.19 ? 904  GLU A CG  1 
ATOM   6795  C  CD  . GLU A 1 904  ? -28.854  -2.674  17.229  1.00 169.76 ? 904  GLU A CD  1 
ATOM   6796  O  OE1 . GLU A 1 904  ? -30.059  -2.378  17.022  1.00 172.75 ? 904  GLU A OE1 1 
ATOM   6797  O  OE2 . GLU A 1 904  ? -28.456  -3.839  17.474  1.00 172.25 ? 904  GLU A OE2 1 
ATOM   6798  N  N   . ILE A 1 905  ? -27.640  1.811   13.848  1.00 143.01 ? 905  ILE A N   1 
ATOM   6799  C  CA  . ILE A 1 905  ? -27.981  2.974   13.030  1.00 134.55 ? 905  ILE A CA  1 
ATOM   6800  C  C   . ILE A 1 905  ? -29.472  3.130   12.993  1.00 130.22 ? 905  ILE A C   1 
ATOM   6801  O  O   . ILE A 1 905  ? -30.176  2.156   13.204  1.00 123.33 ? 905  ILE A O   1 
ATOM   6802  C  CB  . ILE A 1 905  ? -27.419  2.849   11.591  1.00 119.74 ? 905  ILE A CB  1 
ATOM   6803  C  CG1 . ILE A 1 905  ? -25.988  2.269   11.644  1.00 117.75 ? 905  ILE A CG1 1 
ATOM   6804  C  CG2 . ILE A 1 905  ? -27.457  4.201   10.873  1.00 113.75 ? 905  ILE A CG2 1 
ATOM   6805  C  CD1 . ILE A 1 905  ? -24.939  3.088   10.882  1.00 114.77 ? 905  ILE A CD1 1 
ATOM   6806  N  N   . GLY A 1 906  ? -29.926  4.365   12.782  1.00 139.59 ? 906  GLY A N   1 
ATOM   6807  C  CA  . GLY A 1 906  ? -31.338  4.703   12.676  1.00 146.94 ? 906  GLY A CA  1 
ATOM   6808  C  C   . GLY A 1 906  ? -32.152  4.543   13.945  1.00 150.54 ? 906  GLY A C   1 
ATOM   6809  O  O   . GLY A 1 906  ? -33.052  5.330   14.217  1.00 150.02 ? 906  GLY A O   1 
ATOM   6810  N  N   . LEU A 1 907  ? -31.803  3.516   14.717  1.00 155.52 ? 907  LEU A N   1 
ATOM   6811  C  CA  . LEU A 1 907  ? -32.450  3.164   15.985  1.00 159.12 ? 907  LEU A CA  1 
ATOM   6812  C  C   . LEU A 1 907  ? -32.830  4.368   16.811  1.00 160.34 ? 907  LEU A C   1 
ATOM   6813  O  O   . LEU A 1 907  ? -32.108  5.357   16.866  1.00 157.95 ? 907  LEU A O   1 
ATOM   6814  C  CB  . LEU A 1 907  ? -31.519  2.295   16.825  1.00 160.85 ? 907  LEU A CB  1 
ATOM   6815  C  CG  . LEU A 1 907  ? -32.033  2.067   18.238  1.00 166.97 ? 907  LEU A CG  1 
ATOM   6816  C  CD1 . LEU A 1 907  ? -33.443  1.468   18.227  1.00 170.50 ? 907  LEU A CD1 1 
ATOM   6817  C  CD2 . LEU A 1 907  ? -31.062  1.168   18.937  1.00 170.37 ? 907  LEU A CD2 1 
ATOM   6818  N  N   . HIS A 1 908  ? -33.953  4.279   17.494  1.00 165.34 ? 908  HIS A N   1 
ATOM   6819  C  CA  . HIS A 1 908  ? -34.461  5.463   18.134  1.00 168.07 ? 908  HIS A CA  1 
ATOM   6820  C  C   . HIS A 1 908  ? -35.011  5.085   19.486  1.00 168.43 ? 908  HIS A C   1 
ATOM   6821  O  O   . HIS A 1 908  ? -34.738  3.995   19.991  1.00 170.50 ? 908  HIS A O   1 
ATOM   6822  C  CB  . HIS A 1 908  ? -35.575  6.082   17.280  1.00 171.25 ? 908  HIS A CB  1 
ATOM   6823  C  CG  . HIS A 1 908  ? -35.454  5.815   15.802  1.00 168.46 ? 908  HIS A CG  1 
ATOM   6824  N  ND1 . HIS A 1 908  ? -35.247  4.554   15.282  1.00 166.97 ? 908  HIS A ND1 1 
ATOM   6825  C  CD2 . HIS A 1 908  ? -35.565  6.648   14.737  1.00 165.78 ? 908  HIS A CD2 1 
ATOM   6826  C  CE1 . HIS A 1 908  ? -35.214  4.627   13.965  1.00 166.35 ? 908  HIS A CE1 1 
ATOM   6827  N  NE2 . HIS A 1 908  ? -35.398  5.887   13.609  1.00 165.34 ? 908  HIS A NE2 1 
ATOM   6828  N  N   . ASN A 1 909  ? -35.789  5.996   20.058  1.00 165.44 ? 909  ASN A N   1 
ATOM   6829  C  CA  . ASN A 1 909  ? -36.524  5.742   21.292  1.00 164.87 ? 909  ASN A CA  1 
ATOM   6830  C  C   . ASN A 1 909  ? -35.674  5.654   22.562  1.00 158.96 ? 909  ASN A C   1 
ATOM   6831  O  O   . ASN A 1 909  ? -34.792  4.807   22.690  1.00 156.53 ? 909  ASN A O   1 
ATOM   6832  C  CB  . ASN A 1 909  ? -37.404  4.492   21.163  1.00 171.84 ? 909  ASN A CB  1 
ATOM   6833  C  CG  . ASN A 1 909  ? -38.060  4.112   22.476  1.00 177.61 ? 909  ASN A CG  1 
ATOM   6834  O  OD1 . ASN A 1 909  ? -38.061  2.949   22.881  1.00 180.09 ? 909  ASN A OD1 1 
ATOM   6835  N  ND2 . ASN A 1 909  ? -38.610  5.105   23.158  1.00 178.98 ? 909  ASN A ND2 1 
ATOM   6836  N  N   . ILE A 1 910  ? -35.978  6.546   23.497  1.00 153.77 ? 910  ILE A N   1 
ATOM   6837  C  CA  . ILE A 1 910  ? -35.410  6.534   24.826  1.00 146.64 ? 910  ILE A CA  1 
ATOM   6838  C  C   . ILE A 1 910  ? -36.508  7.082   25.730  1.00 148.65 ? 910  ILE A C   1 
ATOM   6839  O  O   . ILE A 1 910  ? -36.994  8.195   25.515  1.00 153.33 ? 910  ILE A O   1 
ATOM   6840  C  CB  . ILE A 1 910  ? -34.161  7.418   24.903  1.00 136.74 ? 910  ILE A CB  1 
ATOM   6841  C  CG1 . ILE A 1 910  ? -33.018  6.806   24.101  1.00 131.64 ? 910  ILE A CG1 1 
ATOM   6842  C  CG2 . ILE A 1 910  ? -33.737  7.597   26.329  1.00 133.71 ? 910  ILE A CG2 1 
ATOM   6843  C  CD1 . ILE A 1 910  ? -31.695  7.522   24.268  1.00 127.35 ? 910  ILE A CD1 1 
ATOM   6844  N  N   . ASN A 1 911  ? -36.954  6.276   26.692  1.00 144.31 ? 911  ASN A N   1 
ATOM   6845  C  CA  . ASN A 1 911  ? -37.943  6.728   27.666  1.00 140.62 ? 911  ASN A CA  1 
ATOM   6846  C  C   . ASN A 1 911  ? -37.191  7.544   28.728  1.00 140.30 ? 911  ASN A C   1 
ATOM   6847  O  O   . ASN A 1 911  ? -36.067  7.195   29.084  1.00 138.39 ? 911  ASN A O   1 
ATOM   6848  C  CB  . ASN A 1 911  ? -38.696  5.545   28.321  1.00 139.22 ? 911  ASN A CB  1 
ATOM   6849  C  CG  . ASN A 1 911  ? -39.561  4.711   27.316  1.00 136.71 ? 911  ASN A CG  1 
ATOM   6850  O  OD1 . ASN A 1 911  ? -39.059  3.779   26.661  1.00 137.82 ? 911  ASN A OD1 1 
ATOM   6851  N  ND2 . ASN A 1 911  ? -40.875  5.005   27.256  1.00 137.76 ? 911  ASN A ND2 1 
ATOM   6852  N  N   . PHE A 1 912  ? -37.785  8.632   29.216  1.00 142.57 ? 912  PHE A N   1 
ATOM   6853  C  CA  . PHE A 1 912  ? -37.207  9.398   30.316  1.00 140.49 ? 912  PHE A CA  1 
ATOM   6854  C  C   . PHE A 1 912  ? -38.256  9.492   31.399  1.00 144.99 ? 912  PHE A C   1 
ATOM   6855  O  O   . PHE A 1 912  ? -39.432  9.641   31.105  1.00 147.80 ? 912  PHE A O   1 
ATOM   6856  C  CB  . PHE A 1 912  ? -36.785  10.802  29.870  1.00 134.62 ? 912  PHE A CB  1 
ATOM   6857  C  CG  . PHE A 1 912  ? -35.471  10.837  29.152  1.00 127.62 ? 912  PHE A CG  1 
ATOM   6858  C  CD1 . PHE A 1 912  ? -34.318  10.428  29.772  1.00 124.43 ? 912  PHE A CD1 1 
ATOM   6859  C  CD2 . PHE A 1 912  ? -35.383  11.264  27.854  1.00 125.48 ? 912  PHE A CD2 1 
ATOM   6860  C  CE1 . PHE A 1 912  ? -33.101  10.447  29.107  1.00 120.96 ? 912  PHE A CE1 1 
ATOM   6861  C  CE2 . PHE A 1 912  ? -34.159  11.282  27.193  1.00 122.02 ? 912  PHE A CE2 1 
ATOM   6862  C  CZ  . PHE A 1 912  ? -33.027  10.875  27.823  1.00 119.35 ? 912  PHE A CZ  1 
ATOM   6863  N  N   . SER A 1 913  ? -37.835  9.397   32.651  1.00 146.31 ? 913  SER A N   1 
ATOM   6864  C  CA  . SER A 1 913  ? -38.768  9.358   33.771  1.00 150.47 ? 913  SER A CA  1 
ATOM   6865  C  C   . SER A 1 913  ? -38.266  10.273  34.888  1.00 154.78 ? 913  SER A C   1 
ATOM   6866  O  O   . SER A 1 913  ? -37.060  10.483  35.020  1.00 152.36 ? 913  SER A O   1 
ATOM   6867  C  CB  . SER A 1 913  ? -38.891  7.909   34.281  1.00 150.66 ? 913  SER A CB  1 
ATOM   6868  O  OG  . SER A 1 913  ? -39.719  7.790   35.432  1.00 150.59 ? 913  SER A OG  1 
ATOM   6869  N  N   . LEU A 1 914  ? -39.175  10.830  35.683  1.00 160.06 ? 914  LEU A N   1 
ATOM   6870  C  CA  . LEU A 1 914  ? -38.762  11.476  36.928  1.00 163.48 ? 914  LEU A CA  1 
ATOM   6871  C  C   . LEU A 1 914  ? -39.715  11.181  38.087  1.00 173.73 ? 914  LEU A C   1 
ATOM   6872  O  O   . LEU A 1 914  ? -40.880  10.828  37.877  1.00 177.14 ? 914  LEU A O   1 
ATOM   6873  C  CB  . LEU A 1 914  ? -38.529  12.980  36.763  1.00 155.36 ? 914  LEU A CB  1 
ATOM   6874  C  CG  . LEU A 1 914  ? -39.593  13.880  36.154  1.00 149.42 ? 914  LEU A CG  1 
ATOM   6875  C  CD1 . LEU A 1 914  ? -41.002  13.470  36.550  1.00 148.95 ? 914  LEU A CD1 1 
ATOM   6876  C  CD2 . LEU A 1 914  ? -39.300  15.301  36.581  1.00 145.66 ? 914  LEU A CD2 1 
ATOM   6877  N  N   . GLU A 1 915  ? -39.208  11.325  39.309  1.00 179.74 ? 915  GLU A N   1 
ATOM   6878  C  CA  . GLU A 1 915  ? -39.961  10.940  40.498  1.00 188.55 ? 915  GLU A CA  1 
ATOM   6879  C  C   . GLU A 1 915  ? -40.040  12.056  41.538  1.00 192.27 ? 915  GLU A C   1 
ATOM   6880  O  O   . GLU A 1 915  ? -39.027  12.578  42.001  1.00 189.05 ? 915  GLU A O   1 
ATOM   6881  C  CB  . GLU A 1 915  ? -39.374  9.666   41.126  1.00 191.03 ? 915  GLU A CB  1 
ATOM   6882  C  CG  . GLU A 1 915  ? -39.733  8.359   40.402  1.00 196.11 ? 915  GLU A CG  1 
ATOM   6883  C  CD  . GLU A 1 915  ? -38.634  7.856   39.474  1.00 198.57 ? 915  GLU A CD  1 
ATOM   6884  O  OE1 . GLU A 1 915  ? -37.440  8.019   39.809  1.00 197.59 ? 915  GLU A OE1 1 
ATOM   6885  O  OE2 . GLU A 1 915  ? -38.968  7.283   38.413  1.00 201.22 ? 915  GLU A OE2 1 
ATOM   6886  N  N   . THR A 1 916  ? -41.270  12.399  41.900  1.00 202.15 ? 916  THR A N   1 
ATOM   6887  C  CA  . THR A 1 916  ? -41.544  13.397  42.917  1.00 209.02 ? 916  THR A CA  1 
ATOM   6888  C  C   . THR A 1 916  ? -42.608  12.839  43.847  1.00 219.90 ? 916  THR A C   1 
ATOM   6889  O  O   . THR A 1 916  ? -43.469  12.070  43.426  1.00 221.81 ? 916  THR A O   1 
ATOM   6890  C  CB  . THR A 1 916  ? -42.040  14.720  42.301  1.00 206.58 ? 916  THR A CB  1 
ATOM   6891  O  OG1 . THR A 1 916  ? -41.015  15.267  41.466  1.00 203.97 ? 916  THR A OG1 1 
ATOM   6892  C  CG2 . THR A 1 916  ? -42.382  15.735  43.384  1.00 205.16 ? 916  THR A CG2 1 
ATOM   6893  N  N   . TRP A 1 917  ? -42.528  13.234  45.114  1.00 228.49 ? 917  TRP A N   1 
ATOM   6894  C  CA  . TRP A 1 917  ? -43.424  12.763  46.164  1.00 237.85 ? 917  TRP A CA  1 
ATOM   6895  C  C   . TRP A 1 917  ? -44.835  12.497  45.649  1.00 243.98 ? 917  TRP A C   1 
ATOM   6896  O  O   . TRP A 1 917  ? -45.408  11.436  45.901  1.00 243.92 ? 917  TRP A O   1 
ATOM   6897  C  CB  . TRP A 1 917  ? -43.473  13.804  47.283  1.00 242.09 ? 917  TRP A CB  1 
ATOM   6898  C  CG  . TRP A 1 917  ? -43.654  13.242  48.660  1.00 247.56 ? 917  TRP A CG  1 
ATOM   6899  C  CD1 . TRP A 1 917  ? -44.790  13.278  49.416  1.00 250.04 ? 917  TRP A CD1 1 
ATOM   6900  C  CD2 . TRP A 1 917  ? -42.662  12.577  49.457  1.00 249.11 ? 917  TRP A CD2 1 
ATOM   6901  N  NE1 . TRP A 1 917  ? -44.570  12.672  50.630  1.00 251.46 ? 917  TRP A NE1 1 
ATOM   6902  C  CE2 . TRP A 1 917  ? -43.273  12.233  50.679  1.00 250.77 ? 917  TRP A CE2 1 
ATOM   6903  C  CE3 . TRP A 1 917  ? -41.320  12.234  49.253  1.00 249.35 ? 917  TRP A CE3 1 
ATOM   6904  C  CZ2 . TRP A 1 917  ? -42.588  11.565  51.692  1.00 250.86 ? 917  TRP A CZ2 1 
ATOM   6905  C  CZ3 . TRP A 1 917  ? -40.643  11.571  50.260  1.00 249.22 ? 917  TRP A CZ3 1 
ATOM   6906  C  CH2 . TRP A 1 917  ? -41.278  11.243  51.464  1.00 250.08 ? 917  TRP A CH2 1 
ATOM   6907  N  N   . PHE A 1 918  ? -45.393  13.467  44.932  1.00 248.19 ? 918  PHE A N   1 
ATOM   6908  C  CA  . PHE A 1 918  ? -46.751  13.332  44.423  1.00 253.63 ? 918  PHE A CA  1 
ATOM   6909  C  C   . PHE A 1 918  ? -46.827  13.206  42.904  1.00 247.58 ? 918  PHE A C   1 
ATOM   6910  O  O   . PHE A 1 918  ? -47.907  13.311  42.329  1.00 249.44 ? 918  PHE A O   1 
ATOM   6911  C  CB  . PHE A 1 918  ? -47.636  14.479  44.915  1.00 261.66 ? 918  PHE A CB  1 
ATOM   6912  C  CG  . PHE A 1 918  ? -47.209  15.829  44.430  1.00 265.09 ? 918  PHE A CG  1 
ATOM   6913  C  CD1 . PHE A 1 918  ? -47.730  16.353  43.264  1.00 268.02 ? 918  PHE A CD1 1 
ATOM   6914  C  CD2 . PHE A 1 918  ? -46.296  16.582  45.148  1.00 265.17 ? 918  PHE A CD2 1 
ATOM   6915  C  CE1 . PHE A 1 918  ? -47.345  17.599  42.817  1.00 267.67 ? 918  PHE A CE1 1 
ATOM   6916  C  CE2 . PHE A 1 918  ? -45.906  17.831  44.706  1.00 264.77 ? 918  PHE A CE2 1 
ATOM   6917  C  CZ  . PHE A 1 918  ? -46.431  18.340  43.538  1.00 265.96 ? 918  PHE A CZ  1 
ATOM   6918  N  N   . GLY A 1 919  ? -45.691  12.969  42.257  1.00 238.94 ? 919  GLY A N   1 
ATOM   6919  C  CA  . GLY A 1 919  ? -45.685  12.801  40.815  1.00 231.94 ? 919  GLY A CA  1 
ATOM   6920  C  C   . GLY A 1 919  ? -44.581  11.920  40.257  1.00 225.07 ? 919  GLY A C   1 
ATOM   6921  O  O   . GLY A 1 919  ? -43.422  12.045  40.642  1.00 222.35 ? 919  GLY A O   1 
ATOM   6922  N  N   . LYS A 1 920  ? -44.956  11.029  39.341  1.00 220.00 ? 920  LYS A N   1 
ATOM   6923  C  CA  . LYS A 1 920  ? -44.009  10.220  38.574  1.00 212.81 ? 920  LYS A CA  1 
ATOM   6924  C  C   . LYS A 1 920  ? -44.427  10.206  37.105  1.00 207.26 ? 920  LYS A C   1 
ATOM   6925  O  O   . LYS A 1 920  ? -45.467  9.658   36.743  1.00 210.74 ? 920  LYS A O   1 
ATOM   6926  C  CB  . LYS A 1 920  ? -43.937  8.794   39.114  1.00 211.92 ? 920  LYS A CB  1 
ATOM   6927  C  CG  . LYS A 1 920  ? -43.015  7.887   38.316  1.00 209.28 ? 920  LYS A CG  1 
ATOM   6928  C  CD  . LYS A 1 920  ? -42.679  6.622   39.087  1.00 207.65 ? 920  LYS A CD  1 
ATOM   6929  C  CE  . LYS A 1 920  ? -41.596  5.817   38.389  1.00 205.08 ? 920  LYS A CE  1 
ATOM   6930  N  NZ  . LYS A 1 920  ? -41.044  4.758   39.280  1.00 204.49 ? 920  LYS A NZ  1 
ATOM   6931  N  N   . GLU A 1 921  ? -43.594  10.793  36.255  1.00 198.29 ? 921  GLU A N   1 
ATOM   6932  C  CA  . GLU A 1 921  ? -44.005  11.149  34.903  1.00 191.78 ? 921  GLU A CA  1 
ATOM   6933  C  C   . GLU A 1 921  ? -43.038  10.580  33.867  1.00 182.42 ? 921  GLU A C   1 
ATOM   6934  O  O   . GLU A 1 921  ? -41.821  10.569  34.091  1.00 179.54 ? 921  GLU A O   1 
ATOM   6935  C  CB  . GLU A 1 921  ? -44.036  12.676  34.793  1.00 194.20 ? 921  GLU A CB  1 
ATOM   6936  C  CG  . GLU A 1 921  ? -44.627  13.226  33.510  1.00 198.92 ? 921  GLU A CG  1 
ATOM   6937  C  CD  . GLU A 1 921  ? -46.113  13.489  33.618  1.00 204.54 ? 921  GLU A CD  1 
ATOM   6938  O  OE1 . GLU A 1 921  ? -46.783  12.806  34.422  1.00 207.59 ? 921  GLU A OE1 1 
ATOM   6939  O  OE2 . GLU A 1 921  ? -46.608  14.379  32.896  1.00 205.87 ? 921  GLU A OE2 1 
ATOM   6940  N  N   . ILE A 1 922  ? -43.567  10.123  32.728  1.00 175.11 ? 922  ILE A N   1 
ATOM   6941  C  CA  . ILE A 1 922  ? -42.707  9.561   31.677  1.00 165.48 ? 922  ILE A CA  1 
ATOM   6942  C  C   . ILE A 1 922  ? -42.783  10.259  30.325  1.00 158.18 ? 922  ILE A C   1 
ATOM   6943  O  O   . ILE A 1 922  ? -43.843  10.358  29.709  1.00 157.97 ? 922  ILE A O   1 
ATOM   6944  C  CB  . ILE A 1 922  ? -42.930  8.065   31.440  1.00 163.98 ? 922  ILE A CB  1 
ATOM   6945  C  CG1 . ILE A 1 922  ? -42.217  7.236   32.511  1.00 161.78 ? 922  ILE A CG1 1 
ATOM   6946  C  CG2 . ILE A 1 922  ? -42.351  7.691   30.108  1.00 164.10 ? 922  ILE A CG2 1 
ATOM   6947  C  CD1 . ILE A 1 922  ? -41.882  5.818   32.086  1.00 161.20 ? 922  ILE A CD1 1 
ATOM   6948  N  N   . LEU A 1 923  ? -41.619  10.714  29.878  1.00 152.30 ? 923  LEU A N   1 
ATOM   6949  C  CA  . LEU A 1 923  ? -41.454  11.429  28.626  1.00 150.23 ? 923  LEU A CA  1 
ATOM   6950  C  C   . LEU A 1 923  ? -40.674  10.561  27.651  1.00 149.33 ? 923  LEU A C   1 
ATOM   6951  O  O   . LEU A 1 923  ? -39.574  10.106  27.983  1.00 149.83 ? 923  LEU A O   1 
ATOM   6952  C  CB  . LEU A 1 923  ? -40.707  12.744  28.893  1.00 146.85 ? 923  LEU A CB  1 
ATOM   6953  C  CG  . LEU A 1 923  ? -39.854  13.451  27.830  1.00 144.57 ? 923  LEU A CG  1 
ATOM   6954  C  CD1 . LEU A 1 923  ? -40.607  13.635  26.513  1.00 146.39 ? 923  LEU A CD1 1 
ATOM   6955  C  CD2 . LEU A 1 923  ? -39.337  14.801  28.343  1.00 142.16 ? 923  LEU A CD2 1 
ATOM   6956  N  N   . VAL A 1 924  ? -41.240  10.320  26.461  1.00 149.10 ? 924  VAL A N   1 
ATOM   6957  C  CA  . VAL A 1 924  ? -40.513  9.591   25.407  1.00 145.82 ? 924  VAL A CA  1 
ATOM   6958  C  C   . VAL A 1 924  ? -39.996  10.481  24.273  1.00 139.15 ? 924  VAL A C   1 
ATOM   6959  O  O   . VAL A 1 924  ? -40.609  11.491  23.912  1.00 136.78 ? 924  VAL A O   1 
ATOM   6960  C  CB  . VAL A 1 924  ? -41.292  8.397   24.799  1.00 147.29 ? 924  VAL A CB  1 
ATOM   6961  C  CG1 . VAL A 1 924  ? -40.298  7.384   24.276  1.00 147.49 ? 924  VAL A CG1 1 
ATOM   6962  C  CG2 . VAL A 1 924  ? -42.183  7.743   25.830  1.00 149.36 ? 924  VAL A CG2 1 
ATOM   6963  N  N   . LYS A 1 925  ? -38.876  10.045  23.706  1.00 136.16 ? 925  LYS A N   1 
ATOM   6964  C  CA  . LYS A 1 925  ? -38.033  10.835  22.832  1.00 130.98 ? 925  LYS A CA  1 
ATOM   6965  C  C   . LYS A 1 925  ? -37.505  9.829   21.796  1.00 129.04 ? 925  LYS A C   1 
ATOM   6966  O  O   . LYS A 1 925  ? -37.556  8.627   22.057  1.00 134.41 ? 925  LYS A O   1 
ATOM   6967  C  CB  . LYS A 1 925  ? -36.888  11.377  23.686  1.00 126.34 ? 925  LYS A CB  1 
ATOM   6968  C  CG  . LYS A 1 925  ? -36.507  12.772  23.396  1.00 122.93 ? 925  LYS A CG  1 
ATOM   6969  C  CD  . LYS A 1 925  ? -37.602  13.694  23.801  1.00 123.42 ? 925  LYS A CD  1 
ATOM   6970  C  CE  . LYS A 1 925  ? -37.419  15.053  23.160  1.00 123.04 ? 925  LYS A CE  1 
ATOM   6971  N  NZ  . LYS A 1 925  ? -38.361  16.063  23.727  1.00 124.28 ? 925  LYS A NZ  1 
ATOM   6972  N  N   . THR A 1 926  ? -37.008  10.277  20.637  1.00 121.18 ? 926  THR A N   1 
ATOM   6973  C  CA  . THR A 1 926  ? -36.434  9.332   19.644  1.00 115.48 ? 926  THR A CA  1 
ATOM   6974  C  C   . THR A 1 926  ? -35.172  9.832   18.911  1.00 111.57 ? 926  THR A C   1 
ATOM   6975  O  O   . THR A 1 926  ? -35.130  10.962  18.421  1.00 110.63 ? 926  THR A O   1 
ATOM   6976  C  CB  . THR A 1 926  ? -37.487  8.882   18.596  1.00 144.75 ? 926  THR A CB  1 
ATOM   6977  O  OG1 . THR A 1 926  ? -38.476  9.917   18.435  1.00 145.21 ? 926  THR A OG1 1 
ATOM   6978  C  CG2 . THR A 1 926  ? -38.171  7.559   19.026  1.00 143.49 ? 926  THR A CG2 1 
ATOM   6979  N  N   . LEU A 1 927  ? -34.159  8.972   18.822  1.00 109.60 ? 927  LEU A N   1 
ATOM   6980  C  CA  . LEU A 1 927  ? -32.796  9.404   18.481  1.00 109.46 ? 927  LEU A CA  1 
ATOM   6981  C  C   . LEU A 1 927  ? -32.329  9.026   17.066  1.00 110.43 ? 927  LEU A C   1 
ATOM   6982  O  O   . LEU A 1 927  ? -32.021  7.868   16.796  1.00 111.68 ? 927  LEU A O   1 
ATOM   6983  C  CB  . LEU A 1 927  ? -31.809  8.840   19.520  1.00 109.93 ? 927  LEU A CB  1 
ATOM   6984  C  CG  . LEU A 1 927  ? -30.450  9.479   19.833  1.00 107.59 ? 927  LEU A CG  1 
ATOM   6985  C  CD1 . LEU A 1 927  ? -29.570  8.546   20.684  1.00 106.01 ? 927  LEU A CD1 1 
ATOM   6986  C  CD2 . LEU A 1 927  ? -29.719  9.852   18.569  1.00 107.24 ? 927  LEU A CD2 1 
ATOM   6987  N  N   . ARG A 1 928  ? -32.239  10.015  16.178  1.00 109.57 ? 928  ARG A N   1 
ATOM   6988  C  CA  . ARG A 1 928  ? -31.723  9.799   14.825  1.00 109.54 ? 928  ARG A CA  1 
ATOM   6989  C  C   . ARG A 1 928  ? -30.231  9.452   14.859  1.00 109.63 ? 928  ARG A C   1 
ATOM   6990  O  O   . ARG A 1 928  ? -29.394  10.269  15.262  1.00 108.72 ? 928  ARG A O   1 
ATOM   6991  C  CB  . ARG A 1 928  ? -32.000  11.023  13.921  1.00 110.09 ? 928  ARG A CB  1 
ATOM   6992  C  CG  . ARG A 1 928  ? -33.360  10.983  13.186  1.00 116.02 ? 928  ARG A CG  1 
ATOM   6993  C  CD  . ARG A 1 928  ? -34.026  12.360  13.011  1.00 122.69 ? 928  ARG A CD  1 
ATOM   6994  N  NE  . ARG A 1 928  ? -34.162  13.071  14.291  1.00 130.15 ? 928  ARG A NE  1 
ATOM   6995  C  CZ  . ARG A 1 928  ? -35.311  13.441  14.881  1.00 134.43 ? 928  ARG A CZ  1 
ATOM   6996  N  NH1 . ARG A 1 928  ? -36.502  13.186  14.305  1.00 137.31 ? 928  ARG A NH1 1 
ATOM   6997  N  NH2 . ARG A 1 928  ? -35.258  14.090  16.057  1.00 131.74 ? 928  ARG A NH2 1 
ATOM   6998  N  N   . VAL A 1 929  ? -29.901  8.224   14.465  1.00 110.88 ? 929  VAL A N   1 
ATOM   6999  C  CA  . VAL A 1 929  ? -28.504  7.805   14.340  1.00 109.76 ? 929  VAL A CA  1 
ATOM   7000  C  C   . VAL A 1 929  ? -28.176  7.579   12.856  1.00 110.00 ? 929  VAL A C   1 
ATOM   7001  O  O   . VAL A 1 929  ? -29.042  7.147   12.099  1.00 109.73 ? 929  VAL A O   1 
ATOM   7002  C  CB  . VAL A 1 929  ? -28.233  6.530   15.179  1.00 113.03 ? 929  VAL A CB  1 
ATOM   7003  C  CG1 . VAL A 1 929  ? -26.805  6.042   15.006  1.00 111.85 ? 929  VAL A CG1 1 
ATOM   7004  C  CG2 . VAL A 1 929  ? -28.538  6.804   16.637  1.00 111.77 ? 929  VAL A CG2 1 
ATOM   7005  N  N   . VAL A 1 930  ? -26.934  7.856   12.458  1.00 109.61 ? 930  VAL A N   1 
ATOM   7006  C  CA  . VAL A 1 930  ? -26.547  7.980   11.051  1.00 112.76 ? 930  VAL A CA  1 
ATOM   7007  C  C   . VAL A 1 930  ? -25.220  7.295   10.798  1.00 117.01 ? 930  VAL A C   1 
ATOM   7008  O  O   . VAL A 1 930  ? -24.617  6.760   11.718  1.00 119.89 ? 930  VAL A O   1 
ATOM   7009  C  CB  . VAL A 1 930  ? -26.319  9.456   10.703  1.00 113.61 ? 930  VAL A CB  1 
ATOM   7010  C  CG1 . VAL A 1 930  ? -25.944  9.616   9.247   1.00 114.34 ? 930  VAL A CG1 1 
ATOM   7011  C  CG2 . VAL A 1 930  ? -27.552  10.285  11.058  1.00 114.49 ? 930  VAL A CG2 1 
ATOM   7012  N  N   . PRO A 1 931  ? -24.775  7.254   9.538   1.00 118.57 ? 931  PRO A N   1 
ATOM   7013  C  CA  . PRO A 1 931  ? -23.388  6.885   9.202   1.00 121.00 ? 931  PRO A CA  1 
ATOM   7014  C  C   . PRO A 1 931  ? -22.497  8.058   8.697   1.00 116.87 ? 931  PRO A C   1 
ATOM   7015  O  O   . PRO A 1 931  ? -22.593  9.120   9.275   1.00 118.11 ? 931  PRO A O   1 
ATOM   7016  C  CB  . PRO A 1 931  ? -23.572  5.798   8.137   1.00 119.71 ? 931  PRO A CB  1 
ATOM   7017  C  CG  . PRO A 1 931  ? -25.092  5.497   8.135   1.00 117.33 ? 931  PRO A CG  1 
ATOM   7018  C  CD  . PRO A 1 931  ? -25.707  6.785   8.510   1.00 116.14 ? 931  PRO A CD  1 
ATOM   7019  N  N   . GLU A 1 932  ? -21.670  7.885   7.659   1.00 115.63 ? 932  GLU A N   1 
ATOM   7020  C  CA  . GLU A 1 932  ? -20.611  8.860   7.346   1.00 116.56 ? 932  GLU A CA  1 
ATOM   7021  C  C   . GLU A 1 932  ? -20.225  9.101   5.851   1.00 112.29 ? 932  GLU A C   1 
ATOM   7022  O  O   . GLU A 1 932  ? -19.435  8.337   5.312   1.00 108.67 ? 932  GLU A O   1 
ATOM   7023  C  CB  . GLU A 1 932  ? -19.358  8.391   8.079   1.00 120.06 ? 932  GLU A CB  1 
ATOM   7024  C  CG  . GLU A 1 932  ? -19.596  7.856   9.489   1.00 122.69 ? 932  GLU A CG  1 
ATOM   7025  C  CD  . GLU A 1 932  ? -20.061  6.418   9.528   1.00 122.65 ? 932  GLU A CD  1 
ATOM   7026  O  OE1 . GLU A 1 932  ? -20.830  6.030   8.638   1.00 121.18 ? 932  GLU A OE1 1 
ATOM   7027  O  OE2 . GLU A 1 932  ? -19.664  5.676   10.454  1.00 124.16 ? 932  GLU A OE2 1 
ATOM   7028  N  N   . GLY A 1 933  ? -20.733  10.178  5.221   1.00 115.48 ? 933  GLY A N   1 
ATOM   7029  C  CA  . GLY A 1 933  ? -20.494  10.528  3.803   1.00 116.15 ? 933  GLY A CA  1 
ATOM   7030  C  C   . GLY A 1 933  ? -21.445  9.949   2.749   1.00 113.57 ? 933  GLY A C   1 
ATOM   7031  O  O   . GLY A 1 933  ? -21.228  8.844   2.256   1.00 110.85 ? 933  GLY A O   1 
ATOM   7032  N  N   . VAL A 1 934  ? -22.490  10.689  2.380   1.00 117.05 ? 934  VAL A N   1 
ATOM   7033  C  CA  . VAL A 1 934  ? -23.681  10.059  1.734   1.00 121.75 ? 934  VAL A CA  1 
ATOM   7034  C  C   . VAL A 1 934  ? -24.023  10.304  0.269   1.00 119.01 ? 934  VAL A C   1 
ATOM   7035  O  O   . VAL A 1 934  ? -24.650  11.297  -0.095  1.00 117.07 ? 934  VAL A O   1 
ATOM   7036  C  CB  . VAL A 1 934  ? -25.006  10.389  2.457   1.00 128.46 ? 934  VAL A CB  1 
ATOM   7037  C  CG1 . VAL A 1 934  ? -26.229  9.886   1.611   1.00 92.45  ? 934  VAL A CG1 1 
ATOM   7038  C  CG2 . VAL A 1 934  ? -24.987  9.815   3.874   1.00 133.33 ? 934  VAL A CG2 1 
ATOM   7039  N  N   . LYS A 1 935  ? -23.694  9.325   -0.547  1.00 119.88 ? 935  LYS A N   1 
ATOM   7040  C  CA  . LYS A 1 935  ? -23.957  9.385   -1.958  1.00 120.74 ? 935  LYS A CA  1 
ATOM   7041  C  C   . LYS A 1 935  ? -25.199  8.511   -2.279  1.00 123.12 ? 935  LYS A C   1 
ATOM   7042  O  O   . LYS A 1 935  ? -25.419  7.472   -1.650  1.00 121.64 ? 935  LYS A O   1 
ATOM   7043  C  CB  . LYS A 1 935  ? -22.681  8.940   -2.697  1.00 122.42 ? 935  LYS A CB  1 
ATOM   7044  C  CG  . LYS A 1 935  ? -21.609  10.042  -2.913  1.00 92.61  ? 935  LYS A CG  1 
ATOM   7045  C  CD  . LYS A 1 935  ? -21.972  11.333  -2.201  1.00 100.08 ? 935  LYS A CD  1 
ATOM   7046  C  CE  . LYS A 1 935  ? -21.651  12.579  -3.032  1.00 103.21 ? 935  LYS A CE  1 
ATOM   7047  N  NZ  . LYS A 1 935  ? -20.327  13.196  -2.726  1.00 107.39 ? 935  LYS A NZ  1 
ATOM   7048  N  N   . ARG A 1 936  ? -26.036  8.946   -3.220  1.00 124.33 ? 936  ARG A N   1 
ATOM   7049  C  CA  . ARG A 1 936  ? -27.125  8.092   -3.683  1.00 125.32 ? 936  ARG A CA  1 
ATOM   7050  C  C   . ARG A 1 936  ? -27.116  8.022   -5.208  1.00 127.20 ? 936  ARG A C   1 
ATOM   7051  O  O   . ARG A 1 936  ? -27.112  9.041   -5.888  1.00 130.37 ? 936  ARG A O   1 
ATOM   7052  C  CB  . ARG A 1 936  ? -28.475  8.534   -3.119  1.00 124.57 ? 936  ARG A CB  1 
ATOM   7053  C  CG  . ARG A 1 936  ? -29.163  9.660   -3.851  1.00 125.73 ? 936  ARG A CG  1 
ATOM   7054  C  CD  . ARG A 1 936  ? -29.974  10.498  -2.870  1.00 130.12 ? 936  ARG A CD  1 
ATOM   7055  N  NE  . ARG A 1 936  ? -31.363  10.668  -3.293  1.00 133.53 ? 936  ARG A NE  1 
ATOM   7056  C  CZ  . ARG A 1 936  ? -32.326  11.194  -2.534  1.00 136.55 ? 936  ARG A CZ  1 
ATOM   7057  N  NH1 . ARG A 1 936  ? -32.051  11.613  -1.302  1.00 137.41 ? 936  ARG A NH1 1 
ATOM   7058  N  NH2 . ARG A 1 936  ? -33.569  11.301  -3.007  1.00 136.67 ? 936  ARG A NH2 1 
ATOM   7059  N  N   . GLU A 1 937  ? -27.052  6.792   -5.714  1.00 128.45 ? 937  GLU A N   1 
ATOM   7060  C  CA  . GLU A 1 937  ? -26.952  6.486   -7.137  1.00 136.65 ? 937  GLU A CA  1 
ATOM   7061  C  C   . GLU A 1 937  ? -28.221  5.799   -7.644  1.00 140.03 ? 937  GLU A C   1 
ATOM   7062  O  O   . GLU A 1 937  ? -28.519  4.657   -7.294  1.00 133.97 ? 937  GLU A O   1 
ATOM   7063  C  CB  . GLU A 1 937  ? -25.696  5.638   -7.425  1.00 149.40 ? 937  GLU A CB  1 
ATOM   7064  C  CG  . GLU A 1 937  ? -25.413  4.453   -6.449  1.00 198.72 ? 937  GLU A CG  1 
ATOM   7065  C  CD  . GLU A 1 937  ? -23.921  3.993   -6.417  1.00 211.04 ? 937  GLU A CD  1 
ATOM   7066  O  OE1 . GLU A 1 937  ? -23.099  4.653   -5.717  1.00 211.87 ? 937  GLU A OE1 1 
ATOM   7067  O  OE2 . GLU A 1 937  ? -23.587  2.956   -7.064  1.00 210.74 ? 937  GLU A OE2 1 
ATOM   7068  N  N   . SER A 1 938  ? -28.942  6.507   -8.502  1.00 148.24 ? 938  SER A N   1 
ATOM   7069  C  CA  . SER A 1 938  ? -30.315  6.194   -8.837  1.00 151.39 ? 938  SER A CA  1 
ATOM   7070  C  C   . SER A 1 938  ? -30.476  5.722   -10.262 1.00 161.90 ? 938  SER A C   1 
ATOM   7071  O  O   . SER A 1 938  ? -31.530  5.210   -10.638 1.00 168.80 ? 938  SER A O   1 
ATOM   7072  C  CB  . SER A 1 938  ? -31.070  7.486   -8.753  1.00 128.99 ? 938  SER A CB  1 
ATOM   7073  O  OG  . SER A 1 938  ? -30.965  8.097   -10.014 1.00 115.91 ? 938  SER A OG  1 
ATOM   7074  N  N   . TYR A 1 939  ? -29.437  5.935   -11.059 1.00 173.36 ? 939  TYR A N   1 
ATOM   7075  C  CA  . TYR A 1 939  ? -29.523  5.823   -12.517 1.00 182.98 ? 939  TYR A CA  1 
ATOM   7076  C  C   . TYR A 1 939  ? -30.333  4.628   -13.056 1.00 170.07 ? 939  TYR A C   1 
ATOM   7077  O  O   . TYR A 1 939  ? -30.635  4.549   -14.259 1.00 162.43 ? 939  TYR A O   1 
ATOM   7078  C  CB  . TYR A 1 939  ? -28.126  5.934   -13.177 1.00 214.23 ? 939  TYR A CB  1 
ATOM   7079  C  CG  . TYR A 1 939  ? -27.145  4.789   -12.952 1.00 231.20 ? 939  TYR A CG  1 
ATOM   7080  C  CD1 . TYR A 1 939  ? -27.300  3.569   -13.612 1.00 236.55 ? 939  TYR A CD1 1 
ATOM   7081  C  CD2 . TYR A 1 939  ? -26.033  4.951   -12.126 1.00 238.32 ? 939  TYR A CD2 1 
ATOM   7082  C  CE1 . TYR A 1 939  ? -26.400  2.535   -13.427 1.00 239.23 ? 939  TYR A CE1 1 
ATOM   7083  C  CE2 . TYR A 1 939  ? -25.128  3.923   -11.935 1.00 241.10 ? 939  TYR A CE2 1 
ATOM   7084  C  CZ  . TYR A 1 939  ? -25.318  2.717   -12.588 1.00 241.36 ? 939  TYR A CZ  1 
ATOM   7085  O  OH  . TYR A 1 939  ? -24.426  1.685   -12.411 1.00 242.85 ? 939  TYR A OH  1 
ATOM   7086  N  N   . SER A 1 940  ? -30.692  3.711   -12.164 1.00 161.72 ? 940  SER A N   1 
ATOM   7087  C  CA  . SER A 1 940  ? -31.504  2.570   -12.544 1.00 155.22 ? 940  SER A CA  1 
ATOM   7088  C  C   . SER A 1 940  ? -32.944  3.011   -12.691 1.00 144.40 ? 940  SER A C   1 
ATOM   7089  O  O   . SER A 1 940  ? -33.431  3.871   -11.949 1.00 144.06 ? 940  SER A O   1 
ATOM   7090  C  CB  . SER A 1 940  ? -31.424  1.493   -11.483 1.00 157.85 ? 940  SER A CB  1 
ATOM   7091  O  OG  . SER A 1 940  ? -31.906  2.026   -10.270 1.00 158.30 ? 940  SER A OG  1 
ATOM   7092  N  N   . GLY A 1 941  ? -33.610  2.395   -13.660 1.00 133.83 ? 941  GLY A N   1 
ATOM   7093  C  CA  . GLY A 1 941  ? -34.995  2.672   -13.990 1.00 124.82 ? 941  GLY A CA  1 
ATOM   7094  C  C   . GLY A 1 941  ? -35.326  1.893   -15.248 1.00 118.40 ? 941  GLY A C   1 
ATOM   7095  O  O   . GLY A 1 941  ? -34.418  1.327   -15.864 1.00 117.60 ? 941  GLY A O   1 
ATOM   7096  N  N   . VAL A 1 942  ? -36.611  1.837   -15.614 1.00 113.35 ? 942  VAL A N   1 
ATOM   7097  C  CA  . VAL A 1 942  ? -37.061  1.263   -16.898 1.00 105.13 ? 942  VAL A CA  1 
ATOM   7098  C  C   . VAL A 1 942  ? -38.277  1.991   -17.381 1.00 100.31 ? 942  VAL A C   1 
ATOM   7099  O  O   . VAL A 1 942  ? -38.978  2.624   -16.592 1.00 102.24 ? 942  VAL A O   1 
ATOM   7100  C  CB  . VAL A 1 942  ? -37.606  -0.126  -16.764 1.00 102.68 ? 942  VAL A CB  1 
ATOM   7101  C  CG1 . VAL A 1 942  ? -37.548  -0.793  -18.095 1.00 103.09 ? 942  VAL A CG1 1 
ATOM   7102  C  CG2 . VAL A 1 942  ? -36.830  -0.886  -15.777 1.00 103.60 ? 942  VAL A CG2 1 
ATOM   7103  N  N   . THR A 1 943  ? -38.568  1.899   -18.667 1.00 93.37  ? 943  THR A N   1 
ATOM   7104  C  CA  . THR A 1 943  ? -39.944  2.186   -19.032 1.00 88.96  ? 943  THR A CA  1 
ATOM   7105  C  C   . THR A 1 943  ? -40.670  0.910   -19.411 1.00 88.34  ? 943  THR A C   1 
ATOM   7106  O  O   . THR A 1 943  ? -40.360  0.278   -20.429 1.00 89.68  ? 943  THR A O   1 
ATOM   7107  C  CB  . THR A 1 943  ? -40.120  3.265   -20.096 1.00 84.92  ? 943  THR A CB  1 
ATOM   7108  O  OG1 . THR A 1 943  ? -39.711  4.529   -19.551 1.00 85.52  ? 943  THR A OG1 1 
ATOM   7109  C  CG2 . THR A 1 943  ? -41.581  3.335   -20.441 1.00 81.35  ? 943  THR A CG2 1 
ATOM   7110  N  N   . LEU A 1 944  ? -41.606  0.506   -18.561 1.00 84.95  ? 944  LEU A N   1 
ATOM   7111  C  CA  . LEU A 1 944  ? -42.364  -0.695  -18.816 1.00 82.58  ? 944  LEU A CA  1 
ATOM   7112  C  C   . LEU A 1 944  ? -43.247  -0.386  -20.000 1.00 86.30  ? 944  LEU A C   1 
ATOM   7113  O  O   . LEU A 1 944  ? -44.053  0.569   -19.945 1.00 87.52  ? 944  LEU A O   1 
ATOM   7114  C  CB  . LEU A 1 944  ? -43.183  -1.079  -17.586 1.00 80.10  ? 944  LEU A CB  1 
ATOM   7115  C  CG  . LEU A 1 944  ? -42.310  -1.798  -16.566 1.00 78.44  ? 944  LEU A CG  1 
ATOM   7116  C  CD1 . LEU A 1 944  ? -43.107  -2.567  -15.525 1.00 78.15  ? 944  LEU A CD1 1 
ATOM   7117  C  CD2 . LEU A 1 944  ? -41.445  -2.725  -17.343 1.00 76.70  ? 944  LEU A CD2 1 
ATOM   7118  N  N   . ASP A 1 945  ? -43.066  -1.165  -21.075 1.00 86.14  ? 945  ASP A N   1 
ATOM   7119  C  CA  . ASP A 1 945  ? -43.801  -0.973  -22.341 1.00 85.25  ? 945  ASP A CA  1 
ATOM   7120  C  C   . ASP A 1 945  ? -44.165  -2.306  -22.880 1.00 82.69  ? 945  ASP A C   1 
ATOM   7121  O  O   . ASP A 1 945  ? -43.402  -2.907  -23.613 1.00 83.86  ? 945  ASP A O   1 
ATOM   7122  C  CB  . ASP A 1 945  ? -42.924  -0.331  -23.422 1.00 86.55  ? 945  ASP A CB  1 
ATOM   7123  C  CG  . ASP A 1 945  ? -43.740  0.357   -24.487 1.00 85.90  ? 945  ASP A CG  1 
ATOM   7124  O  OD1 . ASP A 1 945  ? -44.928  -0.026  -24.619 1.00 85.85  ? 945  ASP A OD1 1 
ATOM   7125  O  OD2 . ASP A 1 945  ? -43.190  1.277   -25.148 1.00 84.41  ? 945  ASP A OD2 1 
ATOM   7126  N  N   . PRO A 1 946  ? -45.345  -2.770  -22.572 1.00 80.03  ? 946  PRO A N   1 
ATOM   7127  C  CA  . PRO A 1 946  ? -45.550  -4.198  -22.814 1.00 81.20  ? 946  PRO A CA  1 
ATOM   7128  C  C   . PRO A 1 946  ? -45.877  -4.408  -24.285 1.00 81.94  ? 946  PRO A C   1 
ATOM   7129  O  O   . PRO A 1 946  ? -45.782  -5.502  -24.855 1.00 81.64  ? 946  PRO A O   1 
ATOM   7130  C  CB  . PRO A 1 946  ? -46.772  -4.492  -21.959 1.00 80.80  ? 946  PRO A CB  1 
ATOM   7131  C  CG  . PRO A 1 946  ? -47.388  -3.081  -21.622 1.00 80.19  ? 946  PRO A CG  1 
ATOM   7132  C  CD  . PRO A 1 946  ? -46.584  -2.042  -22.303 1.00 78.55  ? 946  PRO A CD  1 
ATOM   7133  N  N   . ARG A 1 947  ? -46.274  -3.288  -24.878 1.00 83.13  ? 947  ARG A N   1 
ATOM   7134  C  CA  . ARG A 1 947  ? -46.935  -3.226  -26.161 1.00 83.46  ? 947  ARG A CA  1 
ATOM   7135  C  C   . ARG A 1 947  ? -45.949  -2.598  -27.118 1.00 82.68  ? 947  ARG A C   1 
ATOM   7136  O  O   . ARG A 1 947  ? -46.336  -2.058  -28.141 1.00 85.45  ? 947  ARG A O   1 
ATOM   7137  C  CB  . ARG A 1 947  ? -48.178  -2.315  -26.058 1.00 84.81  ? 947  ARG A CB  1 
ATOM   7138  C  CG  . ARG A 1 947  ? -49.411  -2.904  -25.360 1.00 85.60  ? 947  ARG A CG  1 
ATOM   7139  C  CD  . ARG A 1 947  ? -50.311  -3.697  -26.318 1.00 85.57  ? 947  ARG A CD  1 
ATOM   7140  N  NE  . ARG A 1 947  ? -51.587  -3.034  -26.582 1.00 86.19  ? 947  ARG A NE  1 
ATOM   7141  C  CZ  . ARG A 1 947  ? -52.768  -3.487  -26.150 1.00 89.49  ? 947  ARG A CZ  1 
ATOM   7142  N  NH1 . ARG A 1 947  ? -52.852  -4.607  -25.423 1.00 90.06  ? 947  ARG A NH1 1 
ATOM   7143  N  NH2 . ARG A 1 947  ? -53.884  -2.826  -26.441 1.00 91.37  ? 947  ARG A NH2 1 
ATOM   7144  N  N   . GLY A 1 948  ? -44.673  -2.613  -26.765 1.00 81.22  ? 948  GLY A N   1 
ATOM   7145  C  CA  . GLY A 1 948  ? -43.643  -2.086  -27.648 1.00 79.90  ? 948  GLY A CA  1 
ATOM   7146  C  C   . GLY A 1 948  ? -43.809  -0.685  -28.263 1.00 77.74  ? 948  GLY A C   1 
ATOM   7147  O  O   . GLY A 1 948  ? -42.921  -0.232  -28.991 1.00 76.66  ? 948  GLY A O   1 
ATOM   7148  N  N   . ILE A 1 949  ? -44.919  0.004   -27.986 1.00 76.51  ? 949  ILE A N   1 
ATOM   7149  C  CA  . ILE A 1 949  ? -45.138  1.387   -28.434 1.00 76.96  ? 949  ILE A CA  1 
ATOM   7150  C  C   . ILE A 1 949  ? -43.896  2.224   -28.704 1.00 77.08  ? 949  ILE A C   1 
ATOM   7151  O  O   . ILE A 1 949  ? -43.854  3.024   -29.632 1.00 72.36  ? 949  ILE A O   1 
ATOM   7152  C  CB  . ILE A 1 949  ? -45.844  2.154   -27.340 1.00 72.06  ? 949  ILE A CB  1 
ATOM   7153  C  CG1 . ILE A 1 949  ? -47.002  1.331   -26.810 1.00 85.84  ? 949  ILE A CG1 1 
ATOM   7154  C  CG2 . ILE A 1 949  ? -46.298  3.523   -27.832 1.00 71.94  ? 949  ILE A CG2 1 
ATOM   7155  C  CD1 . ILE A 1 949  ? -48.191  1.386   -27.701 1.00 84.77  ? 949  ILE A CD1 1 
ATOM   7156  N  N   . TYR A 1 950  ? -42.897  2.053   -27.847 1.00 79.83  ? 950  TYR A N   1 
ATOM   7157  C  CA  . TYR A 1 950  ? -41.785  2.995   -27.758 1.00 83.26  ? 950  TYR A CA  1 
ATOM   7158  C  C   . TYR A 1 950  ? -40.519  2.581   -28.483 1.00 83.73  ? 950  TYR A C   1 
ATOM   7159  O  O   . TYR A 1 950  ? -39.536  3.322   -28.509 1.00 85.92  ? 950  TYR A O   1 
ATOM   7160  C  CB  . TYR A 1 950  ? -41.580  3.515   -26.302 1.00 74.82  ? 950  TYR A CB  1 
ATOM   7161  C  CG  . TYR A 1 950  ? -42.530  4.664   -26.112 1.00 74.21  ? 950  TYR A CG  1 
ATOM   7162  C  CD1 . TYR A 1 950  ? -42.119  5.994   -26.308 1.00 70.38  ? 950  TYR A CD1 1 
ATOM   7163  C  CD2 . TYR A 1 950  ? -43.876  4.415   -25.894 1.00 73.73  ? 950  TYR A CD2 1 
ATOM   7164  C  CE1 . TYR A 1 950  ? -43.030  7.052   -26.222 1.00 70.72  ? 950  TYR A CE1 1 
ATOM   7165  C  CE2 . TYR A 1 950  ? -44.788  5.448   -25.808 1.00 75.90  ? 950  TYR A CE2 1 
ATOM   7166  C  CZ  . TYR A 1 950  ? -44.373  6.766   -25.967 1.00 76.68  ? 950  TYR A CZ  1 
ATOM   7167  O  OH  . TYR A 1 950  ? -45.336  7.755   -25.855 1.00 76.46  ? 950  TYR A OH  1 
ATOM   7168  N  N   . GLY A 1 951  ? -40.565  1.411   -29.095 1.00 83.38  ? 951  GLY A N   1 
ATOM   7169  C  CA  . GLY A 1 951  ? -39.490  1.005   -29.975 1.00 86.68  ? 951  GLY A CA  1 
ATOM   7170  C  C   . GLY A 1 951  ? -39.072  -0.424  -29.731 1.00 89.81  ? 951  GLY A C   1 
ATOM   7171  O  O   . GLY A 1 951  ? -38.354  -1.025  -30.538 1.00 91.16  ? 951  GLY A O   1 
ATOM   7172  N  N   . THR A 1 952  ? -39.515  -0.963  -28.601 1.00 90.20  ? 952  THR A N   1 
ATOM   7173  C  CA  . THR A 1 952  ? -39.325  -2.375  -28.308 1.00 88.19  ? 952  THR A CA  1 
ATOM   7174  C  C   . THR A 1 952  ? -40.146  -2.769  -27.106 1.00 86.24  ? 952  THR A C   1 
ATOM   7175  O  O   . THR A 1 952  ? -40.780  -1.917  -26.450 1.00 85.36  ? 952  THR A O   1 
ATOM   7176  C  CB  . THR A 1 952  ? -37.895  -2.675  -27.966 1.00 87.50  ? 952  THR A CB  1 
ATOM   7177  O  OG1 . THR A 1 952  ? -37.858  -3.850  -27.149 1.00 89.70  ? 952  THR A OG1 1 
ATOM   7178  C  CG2 . THR A 1 952  ? -37.293  -1.515  -27.196 1.00 85.55  ? 952  THR A CG2 1 
ATOM   7179  N  N   . ILE A 1 953  ? -40.107  -4.054  -26.793 1.00 84.22  ? 953  ILE A N   1 
ATOM   7180  C  CA  . ILE A 1 953  ? -40.928  -4.546  -25.719 1.00 87.12  ? 953  ILE A CA  1 
ATOM   7181  C  C   . ILE A 1 953  ? -40.181  -4.673  -24.362 1.00 96.79  ? 953  ILE A C   1 
ATOM   7182  O  O   . ILE A 1 953  ? -39.216  -5.443  -24.213 1.00 99.29  ? 953  ILE A O   1 
ATOM   7183  C  CB  . ILE A 1 953  ? -41.692  -5.796  -26.218 1.00 89.98  ? 953  ILE A CB  1 
ATOM   7184  C  CG1 . ILE A 1 953  ? -41.257  -7.107  -25.570 1.00 89.87  ? 953  ILE A CG1 1 
ATOM   7185  C  CG2 . ILE A 1 953  ? -41.540  -5.892  -27.709 1.00 93.64  ? 953  ILE A CG2 1 
ATOM   7186  C  CD1 . ILE A 1 953  ? -42.284  -8.220  -25.845 1.00 89.17  ? 953  ILE A CD1 1 
ATOM   7187  N  N   . SER A 1 954  ? -40.617  -3.839  -23.408 1.00 93.52  ? 954  SER A N   1 
ATOM   7188  C  CA  . SER A 1 954  ? -40.058  -3.768  -22.065 1.00 87.90  ? 954  SER A CA  1 
ATOM   7189  C  C   . SER A 1 954  ? -40.960  -4.539  -21.140 1.00 86.26  ? 954  SER A C   1 
ATOM   7190  O  O   . SER A 1 954  ? -41.943  -3.985  -20.685 1.00 87.51  ? 954  SER A O   1 
ATOM   7191  C  CB  . SER A 1 954  ? -40.005  -2.314  -21.580 1.00 82.81  ? 954  SER A CB  1 
ATOM   7192  O  OG  . SER A 1 954  ? -38.717  -1.986  -21.091 1.00 81.20  ? 954  SER A OG  1 
ATOM   7193  N  N   . ARG A 1 955  ? -40.668  -5.807  -20.869 1.00 85.05  ? 955  ARG A N   1 
ATOM   7194  C  CA  . ARG A 1 955  ? -41.410  -6.490  -19.818 1.00 85.20  ? 955  ARG A CA  1 
ATOM   7195  C  C   . ARG A 1 955  ? -40.487  -7.040  -18.758 1.00 88.90  ? 955  ARG A C   1 
ATOM   7196  O  O   . ARG A 1 955  ? -40.853  -7.964  -18.020 1.00 91.57  ? 955  ARG A O   1 
ATOM   7197  C  CB  . ARG A 1 955  ? -42.241  -7.616  -20.361 1.00 84.81  ? 955  ARG A CB  1 
ATOM   7198  C  CG  . ARG A 1 955  ? -43.321  -7.159  -21.284 1.00 85.27  ? 955  ARG A CG  1 
ATOM   7199  C  CD  . ARG A 1 955  ? -43.600  -8.332  -22.182 1.00 84.09  ? 955  ARG A CD  1 
ATOM   7200  N  NE  . ARG A 1 955  ? -44.630  -8.166  -23.183 1.00 80.17  ? 955  ARG A NE  1 
ATOM   7201  C  CZ  . ARG A 1 955  ? -44.811  -9.089  -24.097 1.00 79.06  ? 955  ARG A CZ  1 
ATOM   7202  N  NH1 . ARG A 1 955  ? -44.023  -10.148 -24.091 1.00 79.74  ? 955  ARG A NH1 1 
ATOM   7203  N  NH2 . ARG A 1 955  ? -45.752  -8.959  -24.998 1.00 83.33  ? 955  ARG A NH2 1 
ATOM   7204  N  N   . ARG A 1 956  ? -39.285  -6.479  -18.690 1.00 86.37  ? 956  ARG A N   1 
ATOM   7205  C  CA  . ARG A 1 956  ? -38.358  -6.822  -17.642 1.00 86.56  ? 956  ARG A CA  1 
ATOM   7206  C  C   . ARG A 1 956  ? -37.236  -5.850  -17.643 1.00 92.51  ? 956  ARG A C   1 
ATOM   7207  O  O   . ARG A 1 956  ? -36.843  -5.354  -18.695 1.00 91.55  ? 956  ARG A O   1 
ATOM   7208  C  CB  . ARG A 1 956  ? -37.813  -8.235  -17.786 1.00 84.47  ? 956  ARG A CB  1 
ATOM   7209  C  CG  . ARG A 1 956  ? -38.437  -9.145  -16.778 1.00 85.87  ? 956  ARG A CG  1 
ATOM   7210  C  CD  . ARG A 1 956  ? -38.066  -10.585 -16.972 1.00 89.42  ? 956  ARG A CD  1 
ATOM   7211  N  NE  . ARG A 1 956  ? -36.697  -10.845 -16.556 1.00 91.87  ? 956  ARG A NE  1 
ATOM   7212  C  CZ  . ARG A 1 956  ? -36.305  -11.970 -15.966 1.00 94.52  ? 956  ARG A CZ  1 
ATOM   7213  N  NH1 . ARG A 1 956  ? -37.201  -12.936 -15.704 1.00 95.26  ? 956  ARG A NH1 1 
ATOM   7214  N  NH2 . ARG A 1 956  ? -35.018  -12.118 -15.628 1.00 95.15  ? 956  ARG A NH2 1 
ATOM   7215  N  N   . LYS A 1 957  ? -36.790  -5.533  -16.424 1.00 98.85  ? 957  LYS A N   1 
ATOM   7216  C  CA  . LYS A 1 957  ? -35.472  -4.975  -16.134 1.00 100.28 ? 957  LYS A CA  1 
ATOM   7217  C  C   . LYS A 1 957  ? -35.076  -5.582  -14.827 1.00 98.22  ? 957  LYS A C   1 
ATOM   7218  O  O   . LYS A 1 957  ? -35.910  -5.714  -13.938 1.00 95.16  ? 957  LYS A O   1 
ATOM   7219  C  CB  . LYS A 1 957  ? -35.471  -3.463  -15.977 1.00 101.54 ? 957  LYS A CB  1 
ATOM   7220  C  CG  . LYS A 1 957  ? -34.092  -2.930  -15.660 1.00 106.50 ? 957  LYS A CG  1 
ATOM   7221  C  CD  . LYS A 1 957  ? -33.630  -1.881  -16.662 1.00 110.83 ? 957  LYS A CD  1 
ATOM   7222  C  CE  . LYS A 1 957  ? -32.096  -1.857  -16.786 1.00 115.44 ? 957  LYS A CE  1 
ATOM   7223  N  NZ  . LYS A 1 957  ? -31.345  -1.483  -15.523 1.00 118.41 ? 957  LYS A NZ  1 
ATOM   7224  N  N   . GLU A 1 958  ? -33.817  -5.994  -14.746 1.00 102.66 ? 958  GLU A N   1 
ATOM   7225  C  CA  . GLU A 1 958  ? -33.221  -6.449  -13.507 1.00 108.27 ? 958  GLU A CA  1 
ATOM   7226  C  C   . GLU A 1 958  ? -32.356  -5.321  -12.955 1.00 109.57 ? 958  GLU A C   1 
ATOM   7227  O  O   . GLU A 1 958  ? -31.497  -4.805  -13.666 1.00 110.29 ? 958  GLU A O   1 
ATOM   7228  C  CB  . GLU A 1 958  ? -32.356  -7.671  -13.779 1.00 114.58 ? 958  GLU A CB  1 
ATOM   7229  C  CG  . GLU A 1 958  ? -32.188  -8.617  -12.596 1.00 121.75 ? 958  GLU A CG  1 
ATOM   7230  C  CD  . GLU A 1 958  ? -31.329  -9.836  -12.941 1.00 128.36 ? 958  GLU A CD  1 
ATOM   7231  O  OE1 . GLU A 1 958  ? -31.853  -10.795 -13.578 1.00 130.52 ? 958  GLU A OE1 1 
ATOM   7232  O  OE2 . GLU A 1 958  ? -30.128  -9.830  -12.564 1.00 130.39 ? 958  GLU A OE2 1 
ATOM   7233  N  N   . PHE A 1 959  ? -32.609  -4.903  -11.715 1.00 108.47 ? 959  PHE A N   1 
ATOM   7234  C  CA  . PHE A 1 959  ? -31.661  -4.068  -10.978 1.00 109.93 ? 959  PHE A CA  1 
ATOM   7235  C  C   . PHE A 1 959  ? -31.015  -4.980  -9.950  1.00 115.49 ? 959  PHE A C   1 
ATOM   7236  O  O   . PHE A 1 959  ? -31.738  -5.658  -9.203  1.00 117.22 ? 959  PHE A O   1 
ATOM   7237  C  CB  . PHE A 1 959  ? -32.350  -2.918  -10.254 1.00 103.64 ? 959  PHE A CB  1 
ATOM   7238  C  CG  . PHE A 1 959  ? -33.532  -2.405  -10.960 1.00 99.09  ? 959  PHE A CG  1 
ATOM   7239  C  CD1 . PHE A 1 959  ? -33.582  -1.103  -11.389 1.00 98.37  ? 959  PHE A CD1 1 
ATOM   7240  C  CD2 . PHE A 1 959  ? -34.603  -3.230  -11.210 1.00 96.46  ? 959  PHE A CD2 1 
ATOM   7241  C  CE1 . PHE A 1 959  ? -34.702  -0.628  -12.051 1.00 96.78  ? 959  PHE A CE1 1 
ATOM   7242  C  CE2 . PHE A 1 959  ? -35.707  -2.770  -11.871 1.00 95.17  ? 959  PHE A CE2 1 
ATOM   7243  C  CZ  . PHE A 1 959  ? -35.759  -1.463  -12.284 1.00 95.31  ? 959  PHE A CZ  1 
ATOM   7244  N  N   . PRO A 1 960  ? -29.667  -5.020  -9.916  1.00 118.18 ? 960  PRO A N   1 
ATOM   7245  C  CA  . PRO A 1 960  ? -29.030  -5.985  -9.034  1.00 124.19 ? 960  PRO A CA  1 
ATOM   7246  C  C   . PRO A 1 960  ? -28.375  -5.288  -7.854  1.00 132.61 ? 960  PRO A C   1 
ATOM   7247  O  O   . PRO A 1 960  ? -28.578  -4.093  -7.632  1.00 132.55 ? 960  PRO A O   1 
ATOM   7248  C  CB  . PRO A 1 960  ? -27.961  -6.589  -9.942  1.00 123.91 ? 960  PRO A CB  1 
ATOM   7249  C  CG  . PRO A 1 960  ? -27.990  -5.744  -11.256 1.00 110.58 ? 960  PRO A CG  1 
ATOM   7250  C  CD  . PRO A 1 960  ? -28.696  -4.499  -10.887 1.00 112.89 ? 960  PRO A CD  1 
ATOM   7251  N  N   . TYR A 1 961  ? -27.606  -6.053  -7.096  1.00 139.84 ? 961  TYR A N   1 
ATOM   7252  C  CA  . TYR A 1 961  ? -26.666  -5.506  -6.144  1.00 147.64 ? 961  TYR A CA  1 
ATOM   7253  C  C   . TYR A 1 961  ? -25.409  -5.006  -6.828  1.00 151.20 ? 961  TYR A C   1 
ATOM   7254  O  O   . TYR A 1 961  ? -24.776  -5.729  -7.605  1.00 152.98 ? 961  TYR A O   1 
ATOM   7255  C  CB  . TYR A 1 961  ? -26.219  -6.611  -5.216  1.00 152.75 ? 961  TYR A CB  1 
ATOM   7256  C  CG  . TYR A 1 961  ? -26.775  -6.518  -3.843  1.00 156.75 ? 961  TYR A CG  1 
ATOM   7257  C  CD1 . TYR A 1 961  ? -25.934  -6.390  -2.745  1.00 159.15 ? 961  TYR A CD1 1 
ATOM   7258  C  CD2 . TYR A 1 961  ? -28.134  -6.561  -3.637  1.00 157.76 ? 961  TYR A CD2 1 
ATOM   7259  C  CE1 . TYR A 1 961  ? -26.429  -6.311  -1.484  1.00 160.74 ? 961  TYR A CE1 1 
ATOM   7260  C  CE2 . TYR A 1 961  ? -28.646  -6.481  -2.382  1.00 160.11 ? 961  TYR A CE2 1 
ATOM   7261  C  CZ  . TYR A 1 961  ? -27.788  -6.356  -1.306  1.00 161.95 ? 961  TYR A CZ  1 
ATOM   7262  O  OH  . TYR A 1 961  ? -28.301  -6.252  -0.044  1.00 164.50 ? 961  TYR A OH  1 
ATOM   7263  N  N   . ARG A 1 962  ? -25.022  -3.781  -6.509  1.00 154.18 ? 962  ARG A N   1 
ATOM   7264  C  CA  . ARG A 1 962  ? -23.658  -3.352  -6.774  1.00 159.26 ? 962  ARG A CA  1 
ATOM   7265  C  C   . ARG A 1 962  ? -23.167  -2.593  -5.548  1.00 156.72 ? 962  ARG A C   1 
ATOM   7266  O  O   . ARG A 1 962  ? -23.605  -1.467  -5.265  1.00 153.85 ? 962  ARG A O   1 
ATOM   7267  C  CB  . ARG A 1 962  ? -23.526  -2.531  -8.069  1.00 167.94 ? 962  ARG A CB  1 
ATOM   7268  C  CG  . ARG A 1 962  ? -22.153  -1.858  -8.247  1.00 178.61 ? 962  ARG A CG  1 
ATOM   7269  C  CD  . ARG A 1 962  ? -21.572  -1.985  -9.666  1.00 186.69 ? 962  ARG A CD  1 
ATOM   7270  N  NE  . ARG A 1 962  ? -21.995  -0.925  -10.582 1.00 191.89 ? 962  ARG A NE  1 
ATOM   7271  C  CZ  . ARG A 1 962  ? -21.255  -0.468  -11.590 1.00 196.02 ? 962  ARG A CZ  1 
ATOM   7272  N  NH1 . ARG A 1 962  ? -20.043  -0.962  -11.805 1.00 198.37 ? 962  ARG A NH1 1 
ATOM   7273  N  NH2 . ARG A 1 962  ? -21.720  0.494   -12.377 1.00 196.37 ? 962  ARG A NH2 1 
ATOM   7274  N  N   . ILE A 1 963  ? -22.288  -3.260  -4.800  1.00 154.02 ? 963  ILE A N   1 
ATOM   7275  C  CA  . ILE A 1 963  ? -21.684  -2.693  -3.615  1.00 147.85 ? 963  ILE A CA  1 
ATOM   7276  C  C   . ILE A 1 963  ? -20.405  -2.028  -4.023  1.00 148.66 ? 963  ILE A C   1 
ATOM   7277  O  O   . ILE A 1 963  ? -19.510  -2.664  -4.562  1.00 149.12 ? 963  ILE A O   1 
ATOM   7278  C  CB  . ILE A 1 963  ? -21.351  -3.751  -2.618  1.00 138.96 ? 963  ILE A CB  1 
ATOM   7279  C  CG1 . ILE A 1 963  ? -22.440  -4.804  -2.603  1.00 133.31 ? 963  ILE A CG1 1 
ATOM   7280  C  CG2 . ILE A 1 963  ? -21.240  -3.131  -1.272  1.00 139.17 ? 963  ILE A CG2 1 
ATOM   7281  C  CD1 . ILE A 1 963  ? -22.151  -5.903  -1.680  1.00 132.22 ? 963  ILE A CD1 1 
ATOM   7282  N  N   . PRO A 1 964  ? -20.339  -0.719  -3.805  1.00 151.18 ? 964  PRO A N   1 
ATOM   7283  C  CA  . PRO A 1 964  ? -19.191  0.122   -4.160  1.00 154.20 ? 964  PRO A CA  1 
ATOM   7284  C  C   . PRO A 1 964  ? -18.090  -0.089  -3.140  1.00 159.91 ? 964  PRO A C   1 
ATOM   7285  O  O   . PRO A 1 964  ? -18.372  -0.042  -1.947  1.00 160.73 ? 964  PRO A O   1 
ATOM   7286  C  CB  . PRO A 1 964  ? -19.758  1.546   -4.062  1.00 153.52 ? 964  PRO A CB  1 
ATOM   7287  C  CG  . PRO A 1 964  ? -21.297  1.370   -4.021  1.00 148.31 ? 964  PRO A CG  1 
ATOM   7288  C  CD  . PRO A 1 964  ? -21.494  0.064   -3.335  1.00 148.17 ? 964  PRO A CD  1 
ATOM   7289  N  N   . LEU A 1 965  ? -16.862  -0.331  -3.572  1.00 164.11 ? 965  LEU A N   1 
ATOM   7290  C  CA  . LEU A 1 965  ? -15.854  -0.747  -2.600  1.00 172.00 ? 965  LEU A CA  1 
ATOM   7291  C  C   . LEU A 1 965  ? -15.482  0.374   -1.606  1.00 175.85 ? 965  LEU A C   1 
ATOM   7292  O  O   . LEU A 1 965  ? -14.489  0.274   -0.876  1.00 178.85 ? 965  LEU A O   1 
ATOM   7293  C  CB  . LEU A 1 965  ? -14.627  -1.397  -3.275  1.00 175.78 ? 965  LEU A CB  1 
ATOM   7294  C  CG  . LEU A 1 965  ? -14.837  -2.754  -3.995  1.00 189.59 ? 965  LEU A CG  1 
ATOM   7295  C  CD1 . LEU A 1 965  ? -13.567  -3.248  -4.695  1.00 191.72 ? 965  LEU A CD1 1 
ATOM   7296  C  CD2 . LEU A 1 965  ? -15.386  -3.848  -3.077  1.00 189.99 ? 965  LEU A CD2 1 
ATOM   7297  N  N   . ASP A 1 966  ? -16.300  1.426   -1.573  1.00 174.45 ? 966  ASP A N   1 
ATOM   7298  C  CA  . ASP A 1 966  ? -16.132  2.513   -0.610  1.00 172.99 ? 966  ASP A CA  1 
ATOM   7299  C  C   . ASP A 1 966  ? -17.212  2.493   0.455   1.00 164.51 ? 966  ASP A C   1 
ATOM   7300  O  O   . ASP A 1 966  ? -17.330  3.427   1.239   1.00 164.97 ? 966  ASP A O   1 
ATOM   7301  C  CB  . ASP A 1 966  ? -16.145  3.868   -1.317  1.00 176.22 ? 966  ASP A CB  1 
ATOM   7302  C  CG  . ASP A 1 966  ? -14.852  4.153   -2.048  1.00 179.74 ? 966  ASP A CG  1 
ATOM   7303  O  OD1 . ASP A 1 966  ? -13.772  3.882   -1.476  1.00 181.85 ? 966  ASP A OD1 1 
ATOM   7304  O  OD2 . ASP A 1 966  ? -14.915  4.645   -3.195  1.00 179.60 ? 966  ASP A OD2 1 
ATOM   7305  N  N   . LEU A 1 967  ? -18.004  1.431   0.477   1.00 155.49 ? 967  LEU A N   1 
ATOM   7306  C  CA  . LEU A 1 967  ? -19.140  1.370   1.381   1.00 149.35 ? 967  LEU A CA  1 
ATOM   7307  C  C   . LEU A 1 967  ? -18.701  1.351   2.832   1.00 146.33 ? 967  LEU A C   1 
ATOM   7308  O  O   . LEU A 1 967  ? -17.808  0.581   3.201   1.00 148.37 ? 967  LEU A O   1 
ATOM   7309  C  CB  . LEU A 1 967  ? -20.001  0.140   1.085   1.00 148.25 ? 967  LEU A CB  1 
ATOM   7310  C  CG  . LEU A 1 967  ? -21.189  -0.075  2.031   1.00 149.34 ? 967  LEU A CG  1 
ATOM   7311  C  CD1 . LEU A 1 967  ? -22.038  1.191   2.166   1.00 149.62 ? 967  LEU A CD1 1 
ATOM   7312  C  CD2 . LEU A 1 967  ? -22.036  -1.256  1.585   1.00 148.39 ? 967  LEU A CD2 1 
ATOM   7313  N  N   . VAL A 1 968  ? -19.340  2.187   3.651   1.00 141.60 ? 968  VAL A N   1 
ATOM   7314  C  CA  . VAL A 1 968  ? -19.103  2.198   5.094   1.00 137.72 ? 968  VAL A CA  1 
ATOM   7315  C  C   . VAL A 1 968  ? -19.542  0.888   5.773   1.00 137.40 ? 968  VAL A C   1 
ATOM   7316  O  O   . VAL A 1 968  ? -20.714  0.529   5.746   1.00 135.00 ? 968  VAL A O   1 
ATOM   7317  C  CB  . VAL A 1 968  ? -19.806  3.392   5.763   1.00 133.80 ? 968  VAL A CB  1 
ATOM   7318  C  CG1 . VAL A 1 968  ? -19.147  4.684   5.353   1.00 131.76 ? 968  VAL A CG1 1 
ATOM   7319  C  CG2 . VAL A 1 968  ? -21.254  3.416   5.376   1.00 132.34 ? 968  VAL A CG2 1 
ATOM   7320  N  N   . PRO A 1 969  ? -18.585  0.164   6.371   1.00 139.42 ? 969  PRO A N   1 
ATOM   7321  C  CA  . PRO A 1 969  ? -18.797  -1.106  7.063   1.00 142.15 ? 969  PRO A CA  1 
ATOM   7322  C  C   . PRO A 1 969  ? -20.048  -1.168  7.934   1.00 146.88 ? 969  PRO A C   1 
ATOM   7323  O  O   . PRO A 1 969  ? -20.459  -0.177  8.523   1.00 147.49 ? 969  PRO A O   1 
ATOM   7324  C  CB  . PRO A 1 969  ? -17.561  -1.202  7.949   1.00 143.40 ? 969  PRO A CB  1 
ATOM   7325  C  CG  . PRO A 1 969  ? -16.492  -0.538  7.153   1.00 142.61 ? 969  PRO A CG  1 
ATOM   7326  C  CD  . PRO A 1 969  ? -17.156  0.528   6.336   1.00 140.81 ? 969  PRO A CD  1 
ATOM   7327  N  N   . LYS A 1 970  ? -20.620  -2.362  8.021   1.00 152.92 ? 970  LYS A N   1 
ATOM   7328  C  CA  . LYS A 1 970  ? -21.836  -2.623  8.792   1.00 160.67 ? 970  LYS A CA  1 
ATOM   7329  C  C   . LYS A 1 970  ? -22.931  -1.602  8.572   1.00 162.56 ? 970  LYS A C   1 
ATOM   7330  O  O   . LYS A 1 970  ? -23.582  -1.179  9.521   1.00 162.42 ? 970  LYS A O   1 
ATOM   7331  C  CB  . LYS A 1 970  ? -21.548  -2.780  10.286  1.00 168.68 ? 970  LYS A CB  1 
ATOM   7332  C  CG  . LYS A 1 970  ? -21.138  -4.198  10.691  1.00 177.22 ? 970  LYS A CG  1 
ATOM   7333  C  CD  . LYS A 1 970  ? -21.376  -4.443  12.184  1.00 185.19 ? 970  LYS A CD  1 
ATOM   7334  C  CE  . LYS A 1 970  ? -20.750  -5.754  12.672  1.00 190.20 ? 970  LYS A CE  1 
ATOM   7335  N  NZ  . LYS A 1 970  ? -20.864  -5.890  14.159  1.00 193.14 ? 970  LYS A NZ  1 
ATOM   7336  N  N   . THR A 1 971  ? -23.122  -1.219  7.312   1.00 165.25 ? 971  THR A N   1 
ATOM   7337  C  CA  . THR A 1 971  ? -24.237  -0.370  6.905   1.00 167.26 ? 971  THR A CA  1 
ATOM   7338  C  C   . THR A 1 971  ? -24.869  -0.944  5.664   1.00 165.14 ? 971  THR A C   1 
ATOM   7339  O  O   . THR A 1 971  ? -24.202  -1.138  4.651   1.00 166.71 ? 971  THR A O   1 
ATOM   7340  C  CB  . THR A 1 971  ? -23.800  1.058   6.570   1.00 169.67 ? 971  THR A CB  1 
ATOM   7341  O  OG1 . THR A 1 971  ? -23.501  1.169   5.171   1.00 167.45 ? 971  THR A OG1 1 
ATOM   7342  C  CG2 . THR A 1 971  ? -22.601  1.449   7.409   1.00 173.74 ? 971  THR A CG2 1 
ATOM   7343  N  N   . GLU A 1 972  ? -26.164  -1.214  5.757   1.00 162.38 ? 972  GLU A N   1 
ATOM   7344  C  CA  . GLU A 1 972  ? -26.916  -1.856  4.689   1.00 158.64 ? 972  GLU A CA  1 
ATOM   7345  C  C   . GLU A 1 972  ? -27.146  -0.895  3.531   1.00 148.19 ? 972  GLU A C   1 
ATOM   7346  O  O   . GLU A 1 972  ? -27.089  0.320   3.709   1.00 144.33 ? 972  GLU A O   1 
ATOM   7347  C  CB  . GLU A 1 972  ? -28.249  -2.363  5.240   1.00 167.05 ? 972  GLU A CB  1 
ATOM   7348  C  CG  . GLU A 1 972  ? -28.723  -1.538  6.434   1.00 176.08 ? 972  GLU A CG  1 
ATOM   7349  C  CD  . GLU A 1 972  ? -30.087  -1.955  6.966   1.00 182.51 ? 972  GLU A CD  1 
ATOM   7350  O  OE1 . GLU A 1 972  ? -30.919  -2.464  6.172   1.00 183.20 ? 972  GLU A OE1 1 
ATOM   7351  O  OE2 . GLU A 1 972  ? -30.324  -1.752  8.184   1.00 186.05 ? 972  GLU A OE2 1 
ATOM   7352  N  N   . ILE A 1 973  ? -27.386  -1.443  2.343   1.00 141.35 ? 973  ILE A N   1 
ATOM   7353  C  CA  . ILE A 1 973  ? -27.657  -0.614  1.186   1.00 133.31 ? 973  ILE A CA  1 
ATOM   7354  C  C   . ILE A 1 973  ? -29.140  -0.439  1.009   1.00 136.49 ? 973  ILE A C   1 
ATOM   7355  O  O   . ILE A 1 973  ? -29.857  -1.398  0.694   1.00 138.59 ? 973  ILE A O   1 
ATOM   7356  C  CB  . ILE A 1 973  ? -27.153  -1.220  -0.089  1.00 120.81 ? 973  ILE A CB  1 
ATOM   7357  C  CG1 . ILE A 1 973  ? -25.684  -1.553  0.034   1.00 118.83 ? 973  ILE A CG1 1 
ATOM   7358  C  CG2 . ILE A 1 973  ? -27.346  -0.234  -1.199  1.00 116.11 ? 973  ILE A CG2 1 
ATOM   7359  C  CD1 . ILE A 1 973  ? -25.194  -2.385  -1.089  1.00 117.44 ? 973  ILE A CD1 1 
ATOM   7360  N  N   . LYS A 1 974  ? -29.582  0.800   1.210   1.00 135.50 ? 974  LYS A N   1 
ATOM   7361  C  CA  . LYS A 1 974  ? -30.971  1.198   1.024   1.00 133.22 ? 974  LYS A CA  1 
ATOM   7362  C  C   . LYS A 1 974  ? -31.206  1.525   -0.459  1.00 126.04 ? 974  LYS A C   1 
ATOM   7363  O  O   . LYS A 1 974  ? -30.317  2.050   -1.131  1.00 125.40 ? 974  LYS A O   1 
ATOM   7364  C  CB  . LYS A 1 974  ? -31.290  2.399   1.939   1.00 137.90 ? 974  LYS A CB  1 
ATOM   7365  C  CG  . LYS A 1 974  ? -32.756  2.833   2.016   1.00 143.51 ? 974  LYS A CG  1 
ATOM   7366  C  CD  . LYS A 1 974  ? -32.931  4.009   2.989   1.00 151.29 ? 974  LYS A CD  1 
ATOM   7367  C  CE  . LYS A 1 974  ? -34.178  4.868   2.666   1.00 154.59 ? 974  LYS A CE  1 
ATOM   7368  N  NZ  . LYS A 1 974  ? -34.424  6.027   3.606   1.00 156.21 ? 974  LYS A NZ  1 
ATOM   7369  N  N   . ARG A 1 975  ? -32.385  1.172   -0.971  1.00 120.61 ? 975  ARG A N   1 
ATOM   7370  C  CA  . ARG A 1 975  ? -32.810  1.581   -2.310  1.00 114.54 ? 975  ARG A CA  1 
ATOM   7371  C  C   . ARG A 1 975  ? -34.304  1.422   -2.481  1.00 109.18 ? 975  ARG A C   1 
ATOM   7372  O  O   . ARG A 1 975  ? -34.895  0.426   -2.057  1.00 110.05 ? 975  ARG A O   1 
ATOM   7373  C  CB  . ARG A 1 975  ? -32.089  0.785   -3.382  1.00 112.14 ? 975  ARG A CB  1 
ATOM   7374  C  CG  . ARG A 1 975  ? -32.250  -0.671  -3.222  1.00 110.53 ? 975  ARG A CG  1 
ATOM   7375  C  CD  . ARG A 1 975  ? -31.073  -1.380  -3.798  1.00 109.19 ? 975  ARG A CD  1 
ATOM   7376  N  NE  . ARG A 1 975  ? -31.285  -2.808  -3.649  1.00 109.13 ? 975  ARG A NE  1 
ATOM   7377  C  CZ  . ARG A 1 975  ? -31.357  -3.668  -4.659  1.00 107.34 ? 975  ARG A CZ  1 
ATOM   7378  N  NH1 . ARG A 1 975  ? -31.194  -3.252  -5.911  1.00 105.24 ? 975  ARG A NH1 1 
ATOM   7379  N  NH2 . ARG A 1 975  ? -31.567  -4.954  -4.408  1.00 107.74 ? 975  ARG A NH2 1 
ATOM   7380  N  N   . ILE A 1 976  ? -34.901  2.419   -3.116  1.00 104.14 ? 976  ILE A N   1 
ATOM   7381  C  CA  . ILE A 1 976  ? -36.340  2.503   -3.240  1.00 99.78  ? 976  ILE A CA  1 
ATOM   7382  C  C   . ILE A 1 976  ? -36.799  2.290   -4.661  1.00 96.49  ? 976  ILE A C   1 
ATOM   7383  O  O   . ILE A 1 976  ? -36.143  2.732   -5.597  1.00 98.12  ? 976  ILE A O   1 
ATOM   7384  C  CB  . ILE A 1 976  ? -36.766  3.879   -2.883  1.00 99.72  ? 976  ILE A CB  1 
ATOM   7385  C  CG1 . ILE A 1 976  ? -35.901  4.338   -1.735  1.00 104.22 ? 976  ILE A CG1 1 
ATOM   7386  C  CG2 . ILE A 1 976  ? -38.264  3.928   -2.578  1.00 98.19  ? 976  ILE A CG2 1 
ATOM   7387  C  CD1 . ILE A 1 976  ? -35.435  5.744   -1.918  1.00 107.96 ? 976  ILE A CD1 1 
ATOM   7388  N  N   . LEU A 1 977  ? -37.954  1.648   -4.804  1.00 89.52  ? 977  LEU A N   1 
ATOM   7389  C  CA  . LEU A 1 977  ? -38.537  1.340   -6.088  1.00 82.44  ? 977  LEU A CA  1 
ATOM   7390  C  C   . LEU A 1 977  ? -39.839  2.100   -6.270  1.00 81.56  ? 977  LEU A C   1 
ATOM   7391  O  O   . LEU A 1 977  ? -40.739  1.912   -5.478  1.00 83.58  ? 977  LEU A O   1 
ATOM   7392  C  CB  . LEU A 1 977  ? -38.849  -0.139  -6.095  1.00 80.76  ? 977  LEU A CB  1 
ATOM   7393  C  CG  . LEU A 1 977  ? -39.285  -0.692  -7.441  1.00 81.42  ? 977  LEU A CG  1 
ATOM   7394  C  CD1 . LEU A 1 977  ? -38.240  -1.651  -7.987  1.00 80.32  ? 977  LEU A CD1 1 
ATOM   7395  C  CD2 . LEU A 1 977  ? -40.588  -1.409  -7.216  1.00 84.85  ? 977  LEU A CD2 1 
ATOM   7396  N  N   . SER A 1 978  ? -39.968  2.921   -7.311  1.00 81.76  ? 978  SER A N   1 
ATOM   7397  C  CA  . SER A 1 978  ? -41.198  3.697   -7.522  1.00 87.23  ? 978  SER A CA  1 
ATOM   7398  C  C   . SER A 1 978  ? -41.890  3.479   -8.889  1.00 95.79  ? 978  SER A C   1 
ATOM   7399  O  O   . SER A 1 978  ? -41.641  4.209   -9.868  1.00 100.45 ? 978  SER A O   1 
ATOM   7400  C  CB  . SER A 1 978  ? -40.922  5.179   -7.333  1.00 86.51  ? 978  SER A CB  1 
ATOM   7401  O  OG  . SER A 1 978  ? -42.105  5.906   -7.557  1.00 79.10  ? 978  SER A OG  1 
ATOM   7402  N  N   . VAL A 1 979  ? -42.788  2.494   -8.922  1.00 96.53  ? 979  VAL A N   1 
ATOM   7403  C  CA  . VAL A 1 979  ? -43.486  2.038   -10.129 1.00 92.91  ? 979  VAL A CA  1 
ATOM   7404  C  C   . VAL A 1 979  ? -44.792  2.785   -10.385 1.00 92.60  ? 979  VAL A C   1 
ATOM   7405  O  O   . VAL A 1 979  ? -45.695  2.712   -9.565  1.00 95.57  ? 979  VAL A O   1 
ATOM   7406  C  CB  . VAL A 1 979  ? -43.881  0.592   -9.902  1.00 90.56  ? 979  VAL A CB  1 
ATOM   7407  C  CG1 . VAL A 1 979  ? -44.401  -0.019  -11.154 1.00 88.20  ? 979  VAL A CG1 1 
ATOM   7408  C  CG2 . VAL A 1 979  ? -42.699  -0.172  -9.370  1.00 90.94  ? 979  VAL A CG2 1 
ATOM   7409  N  N   . LYS A 1 980  ? -44.933  3.490   -11.502 1.00 90.89  ? 980  LYS A N   1 
ATOM   7410  C  CA  . LYS A 1 980  ? -46.242  4.113   -11.784 1.00 93.07  ? 980  LYS A CA  1 
ATOM   7411  C  C   . LYS A 1 980  ? -46.710  4.174   -13.241 1.00 91.76  ? 980  LYS A C   1 
ATOM   7412  O  O   . LYS A 1 980  ? -45.921  4.268   -14.170 1.00 92.44  ? 980  LYS A O   1 
ATOM   7413  C  CB  . LYS A 1 980  ? -46.370  5.515   -11.166 1.00 94.72  ? 980  LYS A CB  1 
ATOM   7414  C  CG  . LYS A 1 980  ? -45.068  6.170   -10.798 1.00 95.53  ? 980  LYS A CG  1 
ATOM   7415  C  CD  . LYS A 1 980  ? -44.790  5.973   -9.325  1.00 94.78  ? 980  LYS A CD  1 
ATOM   7416  C  CE  . LYS A 1 980  ? -45.803  6.667   -8.451  1.00 92.33  ? 980  LYS A CE  1 
ATOM   7417  N  NZ  . LYS A 1 980  ? -45.501  6.270   -7.070  1.00 91.80  ? 980  LYS A NZ  1 
ATOM   7418  N  N   . GLY A 1 981  ? -48.019  4.133   -13.430 1.00 91.21  ? 981  GLY A N   1 
ATOM   7419  C  CA  . GLY A 1 981  ? -48.552  4.266   -14.763 1.00 88.67  ? 981  GLY A CA  1 
ATOM   7420  C  C   . GLY A 1 981  ? -48.391  5.705   -15.178 1.00 86.82  ? 981  GLY A C   1 
ATOM   7421  O  O   . GLY A 1 981  ? -48.340  6.583   -14.326 1.00 87.91  ? 981  GLY A O   1 
ATOM   7422  N  N   . LEU A 1 982  ? -48.297  5.925   -16.483 1.00 83.41  ? 982  LEU A N   1 
ATOM   7423  C  CA  . LEU A 1 982  ? -48.217  7.256   -17.099 1.00 82.69  ? 982  LEU A CA  1 
ATOM   7424  C  C   . LEU A 1 982  ? -46.841  7.923   -17.075 1.00 86.30  ? 982  LEU A C   1 
ATOM   7425  O  O   . LEU A 1 982  ? -46.109  7.871   -16.070 1.00 85.91  ? 982  LEU A O   1 
ATOM   7426  C  CB  . LEU A 1 982  ? -49.292  8.205   -16.574 1.00 80.07  ? 982  LEU A CB  1 
ATOM   7427  C  CG  . LEU A 1 982  ? -50.711  7.652   -16.574 1.00 78.53  ? 982  LEU A CG  1 
ATOM   7428  C  CD1 . LEU A 1 982  ? -51.666  8.647   -17.210 1.00 79.21  ? 982  LEU A CD1 1 
ATOM   7429  C  CD2 . LEU A 1 982  ? -50.751  6.377   -17.337 1.00 78.05  ? 982  LEU A CD2 1 
ATOM   7430  N  N   . LEU A 1 983  ? -46.503  8.543   -18.206 1.00 89.61  ? 983  LEU A N   1 
ATOM   7431  C  CA  . LEU A 1 983  ? -45.220  9.205   -18.360 1.00 91.81  ? 983  LEU A CA  1 
ATOM   7432  C  C   . LEU A 1 983  ? -45.219  10.365  -17.407 1.00 99.31  ? 983  LEU A C   1 
ATOM   7433  O  O   . LEU A 1 983  ? -44.178  10.844  -16.982 1.00 98.93  ? 983  LEU A O   1 
ATOM   7434  C  CB  . LEU A 1 983  ? -45.053  9.701   -19.783 1.00 88.43  ? 983  LEU A CB  1 
ATOM   7435  C  CG  . LEU A 1 983  ? -44.489  8.673   -20.765 1.00 87.72  ? 983  LEU A CG  1 
ATOM   7436  C  CD1 . LEU A 1 983  ? -44.486  7.262   -20.214 1.00 85.78  ? 983  LEU A CD1 1 
ATOM   7437  C  CD2 . LEU A 1 983  ? -45.251  8.718   -22.081 1.00 89.90  ? 983  LEU A CD2 1 
ATOM   7438  N  N   . VAL A 1 984  ? -46.426  10.791  -17.062 1.00 77.08  ? 984  VAL A N   1 
ATOM   7439  C  CA  . VAL A 1 984  ? -46.654  11.947  -16.214 1.00 79.69  ? 984  VAL A CA  1 
ATOM   7440  C  C   . VAL A 1 984  ? -47.146  11.491  -14.813 1.00 92.46  ? 984  VAL A C   1 
ATOM   7441  O  O   . VAL A 1 984  ? -47.851  12.202  -14.105 1.00 92.74  ? 984  VAL A O   1 
ATOM   7442  C  CB  . VAL A 1 984  ? -47.654  12.867  -16.926 1.00 80.05  ? 984  VAL A CB  1 
ATOM   7443  C  CG1 . VAL A 1 984  ? -49.062  12.494  -16.522 1.00 80.76  ? 984  VAL A CG1 1 
ATOM   7444  C  CG2 . VAL A 1 984  ? -47.351  14.341  -16.667 1.00 79.07  ? 984  VAL A CG2 1 
ATOM   7445  N  N   . GLY A 1 985  ? -46.752  10.280  -14.429 1.00 93.00  ? 985  GLY A N   1 
ATOM   7446  C  CA  . GLY A 1 985  ? -47.147  9.698   -13.151 1.00 93.07  ? 985  GLY A CA  1 
ATOM   7447  C  C   . GLY A 1 985  ? -46.283  9.972   -11.916 1.00 92.37  ? 985  GLY A C   1 
ATOM   7448  O  O   . GLY A 1 985  ? -46.805  9.980   -10.802 1.00 96.51  ? 985  GLY A O   1 
ATOM   7449  N  N   . GLU A 1 986  ? -44.973  10.155  -12.071 1.00 91.27  ? 986  GLU A N   1 
ATOM   7450  C  CA  . GLU A 1 986  ? -44.224  10.628  -10.934 1.00 89.77  ? 986  GLU A CA  1 
ATOM   7451  C  C   . GLU A 1 986  ? -44.795  11.980  -10.663 1.00 88.28  ? 986  GLU A C   1 
ATOM   7452  O  O   . GLU A 1 986  ? -45.252  12.249  -9.567  1.00 91.27  ? 986  GLU A O   1 
ATOM   7453  C  CB  . GLU A 1 986  ? -42.746  10.761  -11.226 1.00 90.40  ? 986  GLU A CB  1 
ATOM   7454  C  CG  . GLU A 1 986  ? -41.868  10.367  -10.047 1.00 93.15  ? 986  GLU A CG  1 
ATOM   7455  C  CD  . GLU A 1 986  ? -42.009  8.891   -9.734  1.00 96.78  ? 986  GLU A CD  1 
ATOM   7456  O  OE1 . GLU A 1 986  ? -41.034  8.107   -9.858  1.00 96.67  ? 986  GLU A OE1 1 
ATOM   7457  O  OE2 . GLU A 1 986  ? -43.135  8.506   -9.373  1.00 99.51  ? 986  GLU A OE2 1 
ATOM   7458  N  N   . ILE A 1 987  ? -44.826  12.833  -11.678 1.00 85.39  ? 987  ILE A N   1 
ATOM   7459  C  CA  . ILE A 1 987  ? -45.205  14.215  -11.432 1.00 83.99  ? 987  ILE A CA  1 
ATOM   7460  C  C   . ILE A 1 987  ? -46.583  14.317  -10.867 1.00 87.99  ? 987  ILE A C   1 
ATOM   7461  O  O   . ILE A 1 987  ? -46.967  15.366  -10.384 1.00 88.91  ? 987  ILE A O   1 
ATOM   7462  C  CB  . ILE A 1 987  ? -45.242  15.063  -12.675 1.00 80.91  ? 987  ILE A CB  1 
ATOM   7463  C  CG1 . ILE A 1 987  ? -44.306  14.501  -13.733 1.00 85.65  ? 987  ILE A CG1 1 
ATOM   7464  C  CG2 . ILE A 1 987  ? -44.927  16.511  -12.307 1.00 75.85  ? 987  ILE A CG2 1 
ATOM   7465  C  CD1 . ILE A 1 987  ? -43.927  15.537  -14.776 1.00 89.32  ? 987  ILE A CD1 1 
ATOM   7466  N  N   . LEU A 1 988  ? -47.348  13.241  -10.971 1.00 90.86  ? 988  LEU A N   1 
ATOM   7467  C  CA  . LEU A 1 988  ? -48.676  13.228  -10.386 1.00 92.91  ? 988  LEU A CA  1 
ATOM   7468  C  C   . LEU A 1 988  ? -48.616  12.753  -8.962  1.00 95.72  ? 988  LEU A C   1 
ATOM   7469  O  O   . LEU A 1 988  ? -49.225  13.364  -8.106  1.00 98.72  ? 988  LEU A O   1 
ATOM   7470  C  CB  . LEU A 1 988  ? -49.623  12.335  -11.168 1.00 94.22  ? 988  LEU A CB  1 
ATOM   7471  C  CG  . LEU A 1 988  ? -50.276  12.979  -12.382 1.00 93.93  ? 988  LEU A CG  1 
ATOM   7472  C  CD1 . LEU A 1 988  ? -51.066  11.916  -13.109 1.00 95.73  ? 988  LEU A CD1 1 
ATOM   7473  C  CD2 . LEU A 1 988  ? -51.152  14.157  -11.979 1.00 91.40  ? 988  LEU A CD2 1 
ATOM   7474  N  N   . SER A 1 989  ? -47.893  11.664  -8.704  1.00 95.09  ? 989  SER A N   1 
ATOM   7475  C  CA  . SER A 1 989  ? -47.781  11.128  -7.349  1.00 95.03  ? 989  SER A CA  1 
ATOM   7476  C  C   . SER A 1 989  ? -47.151  12.160  -6.422  1.00 92.09  ? 989  SER A C   1 
ATOM   7477  O  O   . SER A 1 989  ? -47.507  12.265  -5.251  1.00 91.49  ? 989  SER A O   1 
ATOM   7478  C  CB  . SER A 1 989  ? -46.982  9.826   -7.331  1.00 98.20  ? 989  SER A CB  1 
ATOM   7479  O  OG  . SER A 1 989  ? -46.877  9.333   -6.012  1.00 101.69 ? 989  SER A OG  1 
ATOM   7480  N  N   . ALA A 1 990  ? -46.235  12.954  -6.952  1.00 89.93  ? 990  ALA A N   1 
ATOM   7481  C  CA  . ALA A 1 990  ? -45.595  13.953  -6.121  1.00 90.92  ? 990  ALA A CA  1 
ATOM   7482  C  C   . ALA A 1 990  ? -46.570  15.044  -5.650  1.00 90.98  ? 990  ALA A C   1 
ATOM   7483  O  O   . ALA A 1 990  ? -46.403  15.626  -4.584  1.00 94.76  ? 990  ALA A O   1 
ATOM   7484  C  CB  . ALA A 1 990  ? -44.375  14.557  -6.823  1.00 90.61  ? 990  ALA A CB  1 
ATOM   7485  N  N   . VAL A 1 991  ? -47.597  15.338  -6.413  1.00 86.61  ? 991  VAL A N   1 
ATOM   7486  C  CA  . VAL A 1 991  ? -48.452  16.422  -5.988  1.00 87.92  ? 991  VAL A CA  1 
ATOM   7487  C  C   . VAL A 1 991  ? -49.691  15.881  -5.279  1.00 91.22  ? 991  VAL A C   1 
ATOM   7488  O  O   . VAL A 1 991  ? -50.419  16.608  -4.607  1.00 93.11  ? 991  VAL A O   1 
ATOM   7489  C  CB  . VAL A 1 991  ? -48.718  17.423  -7.175  1.00 63.27  ? 991  VAL A CB  1 
ATOM   7490  C  CG1 . VAL A 1 991  ? -49.873  18.397  -6.899  1.00 63.10  ? 991  VAL A CG1 1 
ATOM   7491  C  CG2 . VAL A 1 991  ? -47.458  18.197  -7.480  1.00 63.29  ? 991  VAL A CG2 1 
ATOM   7492  N  N   . LEU A 1 992  ? -49.914  14.587  -5.383  1.00 93.15  ? 992  LEU A N   1 
ATOM   7493  C  CA  . LEU A 1 992  ? -51.097  14.050  -4.755  1.00 100.01 ? 992  LEU A CA  1 
ATOM   7494  C  C   . LEU A 1 992  ? -50.734  12.882  -3.876  1.00 117.00 ? 992  LEU A C   1 
ATOM   7495  O  O   . LEU A 1 992  ? -51.357  11.828  -3.980  1.00 123.05 ? 992  LEU A O   1 
ATOM   7496  C  CB  . LEU A 1 992  ? -52.132  13.599  -5.783  1.00 92.41  ? 992  LEU A CB  1 
ATOM   7497  C  CG  . LEU A 1 992  ? -52.323  14.450  -7.030  1.00 86.19  ? 992  LEU A CG  1 
ATOM   7498  C  CD1 . LEU A 1 992  ? -52.940  13.600  -8.088  1.00 83.80  ? 992  LEU A CD1 1 
ATOM   7499  C  CD2 . LEU A 1 992  ? -53.195  15.635  -6.744  1.00 86.45  ? 992  LEU A CD2 1 
ATOM   7500  N  N   . SER A 1 993  ? -49.731  13.059  -3.017  1.00 126.47 ? 993  SER A N   1 
ATOM   7501  C  CA  . SER A 1 993  ? -49.373  12.045  -2.027  1.00 136.03 ? 993  SER A CA  1 
ATOM   7502  C  C   . SER A 1 993  ? -48.833  12.745  -0.804  1.00 145.69 ? 993  SER A C   1 
ATOM   7503  O  O   . SER A 1 993  ? -48.887  12.231  0.310   1.00 148.64 ? 993  SER A O   1 
ATOM   7504  C  CB  . SER A 1 993  ? -48.325  11.090  -2.591  1.00 134.91 ? 993  SER A CB  1 
ATOM   7505  O  OG  . SER A 1 993  ? -48.877  10.250  -3.598  1.00 134.18 ? 993  SER A OG  1 
ATOM   7506  N  N   . GLN A 1 994  ? -48.296  13.930  -1.043  1.00 153.05 ? 994  GLN A N   1 
ATOM   7507  C  CA  . GLN A 1 994  ? -47.836  14.806  0.009   1.00 161.50 ? 994  GLN A CA  1 
ATOM   7508  C  C   . GLN A 1 994  ? -48.701  16.051  -0.033  1.00 162.70 ? 994  GLN A C   1 
ATOM   7509  O  O   . GLN A 1 994  ? -49.040  16.520  -1.114  1.00 159.19 ? 994  GLN A O   1 
ATOM   7510  C  CB  . GLN A 1 994  ? -46.387  15.196  -0.252  1.00 165.92 ? 994  GLN A CB  1 
ATOM   7511  C  CG  . GLN A 1 994  ? -46.199  15.860  -1.601  1.00 168.40 ? 994  GLN A CG  1 
ATOM   7512  C  CD  . GLN A 1 994  ? -45.569  17.234  -1.483  1.00 171.15 ? 994  GLN A CD  1 
ATOM   7513  O  OE1 . GLN A 1 994  ? -44.772  17.485  -0.573  1.00 173.69 ? 994  GLN A OE1 1 
ATOM   7514  N  NE2 . GLN A 1 994  ? -45.926  18.138  -2.402  1.00 169.65 ? 994  GLN A NE2 1 
ATOM   7515  N  N   . GLU A 1 995  ? -49.071  16.581  1.130   1.00 169.62 ? 995  GLU A N   1 
ATOM   7516  C  CA  . GLU A 1 995  ? -49.776  17.864  1.184   1.00 174.60 ? 995  GLU A CA  1 
ATOM   7517  C  C   . GLU A 1 995  ? -48.771  18.997  1.133   1.00 174.60 ? 995  GLU A C   1 
ATOM   7518  O  O   . GLU A 1 995  ? -47.565  18.761  1.210   1.00 173.35 ? 995  GLU A O   1 
ATOM   7519  C  CB  . GLU A 1 995  ? -50.635  18.006  2.449   1.00 180.49 ? 995  GLU A CB  1 
ATOM   7520  C  CG  . GLU A 1 995  ? -52.103  17.611  2.291   1.00 184.61 ? 995  GLU A CG  1 
ATOM   7521  C  CD  . GLU A 1 995  ? -52.379  16.187  2.742   1.00 188.44 ? 995  GLU A CD  1 
ATOM   7522  O  OE1 . GLU A 1 995  ? -51.527  15.621  3.469   1.00 189.87 ? 995  GLU A OE1 1 
ATOM   7523  O  OE2 . GLU A 1 995  ? -53.446  15.641  2.371   1.00 189.68 ? 995  GLU A OE2 1 
ATOM   7524  N  N   . GLY A 1 996  ? -49.271  20.223  1.010   1.00 175.84 ? 996  GLY A N   1 
ATOM   7525  C  CA  . GLY A 1 996  ? -48.417  21.396  0.997   1.00 178.19 ? 996  GLY A CA  1 
ATOM   7526  C  C   . GLY A 1 996  ? -47.338  21.348  -0.069  1.00 178.84 ? 996  GLY A C   1 
ATOM   7527  O  O   . GLY A 1 996  ? -46.545  20.406  -0.136  1.00 179.06 ? 996  GLY A O   1 
ATOM   7528  N  N   . ILE A 1 997  ? -47.303  22.384  -0.898  1.00 180.14 ? 997  ILE A N   1 
ATOM   7529  C  CA  . ILE A 1 997  ? -46.368  22.470  -2.016  1.00 179.67 ? 997  ILE A CA  1 
ATOM   7530  C  C   . ILE A 1 997  ? -44.904  22.248  -1.579  1.00 183.63 ? 997  ILE A C   1 
ATOM   7531  O  O   . ILE A 1 997  ? -44.524  22.572  -0.451  1.00 185.55 ? 997  ILE A O   1 
ATOM   7532  C  CB  . ILE A 1 997  ? -46.537  23.823  -2.715  1.00 175.21 ? 997  ILE A CB  1 
ATOM   7533  C  CG1 . ILE A 1 997  ? -45.746  24.899  -1.980  1.00 175.33 ? 997  ILE A CG1 1 
ATOM   7534  C  CG2 . ILE A 1 997  ? -48.010  24.209  -2.733  1.00 174.80 ? 997  ILE A CG2 1 
ATOM   7535  C  CD1 . ILE A 1 997  ? -46.206  26.298  -2.277  1.00 174.40 ? 997  ILE A CD1 1 
ATOM   7536  N  N   . ASN A 1 998  ? -44.092  21.697  -2.480  1.00 184.38 ? 998  ASN A N   1 
ATOM   7537  C  CA  . ASN A 1 998  ? -42.743  21.249  -2.137  1.00 185.94 ? 998  ASN A CA  1 
ATOM   7538  C  C   . ASN A 1 998  ? -41.800  21.239  -3.340  1.00 179.19 ? 998  ASN A C   1 
ATOM   7539  O  O   . ASN A 1 998  ? -42.230  20.926  -4.442  1.00 180.98 ? 998  ASN A O   1 
ATOM   7540  C  CB  . ASN A 1 998  ? -42.814  19.847  -1.522  1.00 193.93 ? 998  ASN A CB  1 
ATOM   7541  C  CG  . ASN A 1 998  ? -41.505  19.074  -1.653  1.00 200.23 ? 998  ASN A CG  1 
ATOM   7542  O  OD1 . ASN A 1 998  ? -40.430  19.590  -1.348  1.00 203.27 ? 998  ASN A OD1 1 
ATOM   7543  N  ND2 . ASN A 1 998  ? -41.597  17.821  -2.093  1.00 202.25 ? 998  ASN A ND2 1 
ATOM   7544  N  N   . ILE A 1 999  ? -40.524  21.582  -3.115  1.00 170.09 ? 999  ILE A N   1 
ATOM   7545  C  CA  . ILE A 1 999  ? -39.466  21.544  -4.147  1.00 160.07 ? 999  ILE A CA  1 
ATOM   7546  C  C   . ILE A 1 999  ? -39.092  20.104  -4.533  1.00 150.99 ? 999  ILE A C   1 
ATOM   7547  O  O   . ILE A 1 999  ? -39.279  19.161  -3.760  1.00 148.19 ? 999  ILE A O   1 
ATOM   7548  C  CB  . ILE A 1 999  ? -38.166  22.310  -3.719  1.00 271.68 ? 999  ILE A CB  1 
ATOM   7549  C  CG1 . ILE A 1 999  ? -38.495  23.624  -3.005  1.00 272.21 ? 999  ILE A CG1 1 
ATOM   7550  C  CG2 . ILE A 1 999  ? -37.248  22.565  -4.924  1.00 270.70 ? 999  ILE A CG2 1 
ATOM   7551  C  CD1 . ILE A 1 999  ? -39.085  24.682  -3.907  1.00 271.13 ? 999  ILE A CD1 1 
ATOM   7552  N  N   . LEU A 1 1000 ? -38.556  19.938  -5.733  1.00 144.37 ? 1000 LEU A N   1 
ATOM   7553  C  CA  . LEU A 1 1000 ? -38.397  18.602  -6.263  1.00 136.43 ? 1000 LEU A CA  1 
ATOM   7554  C  C   . LEU A 1 1000 ? -36.956  18.101  -6.239  1.00 134.17 ? 1000 LEU A C   1 
ATOM   7555  O  O   . LEU A 1 1000 ? -36.575  17.129  -6.901  1.00 134.00 ? 1000 LEU A O   1 
ATOM   7556  C  CB  . LEU A 1 1000 ? -39.047  18.511  -7.633  1.00 128.50 ? 1000 LEU A CB  1 
ATOM   7557  C  CG  . LEU A 1 1000 ? -40.524  18.155  -7.512  1.00 118.80 ? 1000 LEU A CG  1 
ATOM   7558  C  CD1 . LEU A 1 1000 ? -41.046  17.833  -8.877  1.00 115.73 ? 1000 LEU A CD1 1 
ATOM   7559  C  CD2 . LEU A 1 1000 ? -40.731  16.966  -6.554  1.00 116.62 ? 1000 LEU A CD2 1 
ATOM   7560  N  N   . THR A 1 1001 ? -36.146  18.746  -5.430  1.00 132.13 ? 1001 THR A N   1 
ATOM   7561  C  CA  . THR A 1 1001 ? -34.795  18.266  -5.297  1.00 131.77 ? 1001 THR A CA  1 
ATOM   7562  C  C   . THR A 1 1001 ? -34.305  18.457  -3.870  1.00 136.93 ? 1001 THR A C   1 
ATOM   7563  O  O   . THR A 1 1001 ? -35.087  18.743  -2.966  1.00 139.42 ? 1001 THR A O   1 
ATOM   7564  C  CB  . THR A 1 1001 ? -33.901  19.001  -6.277  1.00 124.15 ? 1001 THR A CB  1 
ATOM   7565  O  OG1 . THR A 1 1001 ? -34.720  19.554  -7.320  1.00 118.06 ? 1001 THR A OG1 1 
ATOM   7566  C  CG2 . THR A 1 1001 ? -32.872  18.037  -6.846  1.00 124.04 ? 1001 THR A CG2 1 
ATOM   7567  N  N   . HIS A 1 1002 ? -33.015  18.270  -3.652  1.00 138.89 ? 1002 HIS A N   1 
ATOM   7568  C  CA  . HIS A 1 1002 ? -32.464  18.678  -2.379  1.00 143.85 ? 1002 HIS A CA  1 
ATOM   7569  C  C   . HIS A 1 1002 ? -32.092  20.183  -2.406  1.00 118.93 ? 1002 HIS A C   1 
ATOM   7570  O  O   . HIS A 1 1002 ? -31.622  20.741  -1.417  1.00 121.03 ? 1002 HIS A O   1 
ATOM   7571  C  CB  . HIS A 1 1002 ? -31.292  17.765  -1.978  1.00 152.98 ? 1002 HIS A CB  1 
ATOM   7572  C  CG  . HIS A 1 1002 ? -31.683  16.326  -1.767  1.00 160.68 ? 1002 HIS A CG  1 
ATOM   7573  N  ND1 . HIS A 1 1002 ? -31.502  15.356  -2.729  1.00 163.04 ? 1002 HIS A ND1 1 
ATOM   7574  C  CD2 . HIS A 1 1002 ? -32.237  15.698  -0.701  1.00 164.57 ? 1002 HIS A CD2 1 
ATOM   7575  C  CE1 . HIS A 1 1002 ? -31.925  14.192  -2.266  1.00 164.58 ? 1002 HIS A CE1 1 
ATOM   7576  N  NE2 . HIS A 1 1002 ? -32.379  14.372  -1.040  1.00 165.40 ? 1002 HIS A NE2 1 
ATOM   7577  N  N   . LEU A 1 1003 ? -32.350  20.850  -3.527  1.00 113.29 ? 1003 LEU A N   1 
ATOM   7578  C  CA  . LEU A 1 1003 ? -31.878  22.221  -3.720  1.00 108.73 ? 1003 LEU A CA  1 
ATOM   7579  C  C   . LEU A 1 1003 ? -32.453  23.276  -2.768  1.00 111.39 ? 1003 LEU A C   1 
ATOM   7580  O  O   . LEU A 1 1003 ? -33.662  23.551  -2.775  1.00 114.24 ? 1003 LEU A O   1 
ATOM   7581  C  CB  . LEU A 1 1003 ? -32.042  22.656  -5.178  1.00 99.09  ? 1003 LEU A CB  1 
ATOM   7582  C  CG  . LEU A 1 1003 ? -31.117  21.891  -6.123  1.00 92.13  ? 1003 LEU A CG  1 
ATOM   7583  C  CD1 . LEU A 1 1003 ? -30.429  22.827  -7.121  1.00 87.39  ? 1003 LEU A CD1 1 
ATOM   7584  C  CD2 . LEU A 1 1003 ? -30.073  21.121  -5.314  1.00 92.06  ? 1003 LEU A CD2 1 
ATOM   7585  N  N   . PRO A 1 1004 ? -31.558  23.890  -1.974  1.00 110.84 ? 1004 PRO A N   1 
ATOM   7586  C  CA  . PRO A 1 1004 ? -31.632  24.905  -0.911  1.00 109.05 ? 1004 PRO A CA  1 
ATOM   7587  C  C   . PRO A 1 1004 ? -32.477  26.128  -1.245  1.00 106.70 ? 1004 PRO A C   1 
ATOM   7588  O  O   . PRO A 1 1004 ? -32.373  26.683  -2.334  1.00 105.37 ? 1004 PRO A O   1 
ATOM   7589  C  CB  . PRO A 1 1004 ? -30.178  25.348  -0.799  1.00 112.88 ? 1004 PRO A CB  1 
ATOM   7590  C  CG  . PRO A 1 1004 ? -29.532  24.856  -2.110  1.00 110.53 ? 1004 PRO A CG  1 
ATOM   7591  C  CD  . PRO A 1 1004 ? -30.159  23.551  -2.251  1.00 109.40 ? 1004 PRO A CD  1 
ATOM   7592  N  N   . LYS A 1 1005 ? -33.266  26.585  -0.288  1.00 105.49 ? 1005 LYS A N   1 
ATOM   7593  C  CA  . LYS A 1 1005 ? -34.347  27.522  -0.602  1.00 108.75 ? 1005 LYS A CA  1 
ATOM   7594  C  C   . LYS A 1 1005 ? -34.006  29.008  -0.813  1.00 108.60 ? 1005 LYS A C   1 
ATOM   7595  O  O   . LYS A 1 1005 ? -34.936  29.808  -0.968  1.00 105.64 ? 1005 LYS A O   1 
ATOM   7596  C  CB  . LYS A 1 1005 ? -35.491  27.420  0.434   1.00 115.06 ? 1005 LYS A CB  1 
ATOM   7597  C  CG  . LYS A 1 1005 ? -36.198  26.068  0.514   1.00 122.71 ? 1005 LYS A CG  1 
ATOM   7598  C  CD  . LYS A 1 1005 ? -37.367  25.952  -0.464  1.00 127.88 ? 1005 LYS A CD  1 
ATOM   7599  C  CE  . LYS A 1 1005 ? -38.557  26.827  -0.069  1.00 131.97 ? 1005 LYS A CE  1 
ATOM   7600  N  NZ  . LYS A 1 1005 ? -39.659  26.634  -1.061  1.00 132.13 ? 1005 LYS A NZ  1 
ATOM   7601  N  N   . GLY A 1 1006 ? -32.731  29.397  -0.839  1.00 111.97 ? 1006 GLY A N   1 
ATOM   7602  C  CA  . GLY A 1 1006 ? -32.395  30.825  -0.814  1.00 114.94 ? 1006 GLY A CA  1 
ATOM   7603  C  C   . GLY A 1 1006 ? -32.954  31.783  -1.878  1.00 109.85 ? 1006 GLY A C   1 
ATOM   7604  O  O   . GLY A 1 1006 ? -33.475  32.895  -1.620  1.00 107.38 ? 1006 GLY A O   1 
ATOM   7605  N  N   . SER A 1 1007 ? -32.817  31.336  -3.113  1.00 108.71 ? 1007 SER A N   1 
ATOM   7606  C  CA  . SER A 1 1007 ? -33.207  32.124  -4.268  1.00 105.07 ? 1007 SER A CA  1 
ATOM   7607  C  C   . SER A 1 1007 ? -34.691  32.401  -4.249  1.00 99.11  ? 1007 SER A C   1 
ATOM   7608  O  O   . SER A 1 1007 ? -35.462  31.720  -3.563  1.00 95.66  ? 1007 SER A O   1 
ATOM   7609  C  CB  . SER A 1 1007 ? -32.848  31.359  -5.555  1.00 106.20 ? 1007 SER A CB  1 
ATOM   7610  O  OG  . SER A 1 1007 ? -33.193  32.070  -6.725  1.00 106.72 ? 1007 SER A OG  1 
ATOM   7611  N  N   . ALA A 1 1008 ? -35.078  33.411  -5.019  1.00 99.69  ? 1008 ALA A N   1 
ATOM   7612  C  CA  . ALA A 1 1008 ? -36.469  33.604  -5.390  1.00 99.22  ? 1008 ALA A CA  1 
ATOM   7613  C  C   . ALA A 1 1008 ? -36.838  32.457  -6.303  1.00 96.40  ? 1008 ALA A C   1 
ATOM   7614  O  O   . ALA A 1 1008 ? -37.984  32.025  -6.369  1.00 96.38  ? 1008 ALA A O   1 
ATOM   7615  C  CB  . ALA A 1 1008 ? -36.650  34.912  -6.112  1.00 100.58 ? 1008 ALA A CB  1 
ATOM   7616  N  N   . GLU A 1 1009 ? -35.840  31.953  -7.007  1.00 94.22  ? 1009 GLU A N   1 
ATOM   7617  C  CA  . GLU A 1 1009 ? -36.068  30.869  -7.945  1.00 92.37  ? 1009 GLU A CA  1 
ATOM   7618  C  C   . GLU A 1 1009 ? -36.626  29.647  -7.217  1.00 90.42  ? 1009 GLU A C   1 
ATOM   7619  O  O   . GLU A 1 1009 ? -37.401  28.885  -7.789  1.00 90.30  ? 1009 GLU A O   1 
ATOM   7620  C  CB  . GLU A 1 1009 ? -34.776  30.524  -8.717  1.00 91.19  ? 1009 GLU A CB  1 
ATOM   7621  C  CG  . GLU A 1 1009 ? -34.963  29.770  -10.045 1.00 85.97  ? 1009 GLU A CG  1 
ATOM   7622  C  CD  . GLU A 1 1009 ? -33.734  28.947  -10.416 1.00 83.92  ? 1009 GLU A CD  1 
ATOM   7623  O  OE1 . GLU A 1 1009 ? -32.586  29.460  -10.352 1.00 83.35  ? 1009 GLU A OE1 1 
ATOM   7624  O  OE2 . GLU A 1 1009 ? -33.929  27.767  -10.752 1.00 83.24  ? 1009 GLU A OE2 1 
ATOM   7625  N  N   . ALA A 1 1010 ? -36.256  29.451  -5.962  1.00 88.57  ? 1010 ALA A N   1 
ATOM   7626  C  CA  . ALA A 1 1010 ? -36.707  28.241  -5.309  1.00 91.37  ? 1010 ALA A CA  1 
ATOM   7627  C  C   . ALA A 1 1010 ? -38.151  28.400  -4.835  1.00 88.69  ? 1010 ALA A C   1 
ATOM   7628  O  O   . ALA A 1 1010 ? -38.910  27.448  -4.613  1.00 84.65  ? 1010 ALA A O   1 
ATOM   7629  C  CB  . ALA A 1 1010 ? -35.773  27.898  -4.181  1.00 96.68  ? 1010 ALA A CB  1 
ATOM   7630  N  N   . GLU A 1 1011 ? -38.527  29.649  -4.692  1.00 91.70  ? 1011 GLU A N   1 
ATOM   7631  C  CA  . GLU A 1 1011 ? -39.853  29.940  -4.215  1.00 94.35  ? 1011 GLU A CA  1 
ATOM   7632  C  C   . GLU A 1 1011 ? -40.781  29.709  -5.384  1.00 92.65  ? 1011 GLU A C   1 
ATOM   7633  O  O   . GLU A 1 1011 ? -41.891  29.206  -5.197  1.00 93.24  ? 1011 GLU A O   1 
ATOM   7634  C  CB  . GLU A 1 1011 ? -39.950  31.385  -3.717  1.00 97.69  ? 1011 GLU A CB  1 
ATOM   7635  C  CG  . GLU A 1 1011 ? -40.488  31.455  -2.329  1.00 99.56  ? 1011 GLU A CG  1 
ATOM   7636  C  CD  . GLU A 1 1011 ? -39.923  30.353  -1.495  1.00 102.50 ? 1011 GLU A CD  1 
ATOM   7637  O  OE1 . GLU A 1 1011 ? -38.698  30.404  -1.222  1.00 104.64 ? 1011 GLU A OE1 1 
ATOM   7638  O  OE2 . GLU A 1 1011 ? -40.698  29.429  -1.148  1.00 103.09 ? 1011 GLU A OE2 1 
ATOM   7639  N  N   . LEU A 1 1012 ? -40.307  30.076  -6.580  1.00 88.57  ? 1012 LEU A N   1 
ATOM   7640  C  CA  . LEU A 1 1012 ? -41.059  29.926  -7.820  1.00 83.01  ? 1012 LEU A CA  1 
ATOM   7641  C  C   . LEU A 1 1012 ? -41.230  28.459  -8.183  1.00 85.63  ? 1012 LEU A C   1 
ATOM   7642  O  O   . LEU A 1 1012 ? -42.351  28.001  -8.430  1.00 86.91  ? 1012 LEU A O   1 
ATOM   7643  C  CB  . LEU A 1 1012 ? -40.380  30.691  -8.949  1.00 75.95  ? 1012 LEU A CB  1 
ATOM   7644  C  CG  . LEU A 1 1012 ? -40.981  32.082  -9.079  1.00 73.21  ? 1012 LEU A CG  1 
ATOM   7645  C  CD1 . LEU A 1 1012 ? -40.293  32.922  -10.129 1.00 71.59  ? 1012 LEU A CD1 1 
ATOM   7646  C  CD2 . LEU A 1 1012 ? -42.438  31.932  -9.408  1.00 72.05  ? 1012 LEU A CD2 1 
ATOM   7647  N  N   . MET A 1 1013 ? -40.121  27.723  -8.172  1.00 85.12  ? 1013 MET A N   1 
ATOM   7648  C  CA  . MET A 1 1013 ? -40.105  26.302  -8.514  1.00 85.07  ? 1013 MET A CA  1 
ATOM   7649  C  C   . MET A 1 1013 ? -41.031  25.438  -7.656  1.00 88.63  ? 1013 MET A C   1 
ATOM   7650  O  O   . MET A 1 1013 ? -41.182  24.250  -7.897  1.00 90.34  ? 1013 MET A O   1 
ATOM   7651  C  CB  . MET A 1 1013 ? -38.688  25.767  -8.388  1.00 84.44  ? 1013 MET A CB  1 
ATOM   7652  C  CG  . MET A 1 1013 ? -38.445  24.461  -9.111  1.00 84.54  ? 1013 MET A CG  1 
ATOM   7653  S  SD  . MET A 1 1013 ? -38.200  24.828  -10.846 1.00 104.54 ? 1013 MET A SD  1 
ATOM   7654  C  CE  . MET A 1 1013 ? -37.410  26.428  -10.679 1.00 83.28  ? 1013 MET A CE  1 
ATOM   7655  N  N   . SER A 1 1014 ? -41.625  26.039  -6.638  1.00 91.49  ? 1014 SER A N   1 
ATOM   7656  C  CA  . SER A 1 1014 ? -42.524  25.349  -5.719  1.00 91.67  ? 1014 SER A CA  1 
ATOM   7657  C  C   . SER A 1 1014 ? -43.921  25.263  -6.301  1.00 85.53  ? 1014 SER A C   1 
ATOM   7658  O  O   . SER A 1 1014 ? -44.613  24.254  -6.158  1.00 82.72  ? 1014 SER A O   1 
ATOM   7659  C  CB  . SER A 1 1014 ? -42.626  26.164  -4.433  1.00 98.81  ? 1014 SER A CB  1 
ATOM   7660  O  OG  . SER A 1 1014 ? -43.545  27.256  -4.581  1.00 101.48 ? 1014 SER A OG  1 
ATOM   7661  N  N   . VAL A 1 1015 ? -44.346  26.360  -6.913  1.00 82.65  ? 1015 VAL A N   1 
ATOM   7662  C  CA  . VAL A 1 1015 ? -45.624  26.400  -7.558  1.00 83.47  ? 1015 VAL A CA  1 
ATOM   7663  C  C   . VAL A 1 1015 ? -45.624  25.386  -8.724  1.00 83.82  ? 1015 VAL A C   1 
ATOM   7664  O  O   . VAL A 1 1015 ? -46.664  24.806  -9.038  1.00 86.99  ? 1015 VAL A O   1 
ATOM   7665  C  CB  . VAL A 1 1015 ? -45.956  27.849  -8.015  1.00 90.06  ? 1015 VAL A CB  1 
ATOM   7666  C  CG1 . VAL A 1 1015 ? -44.925  28.375  -8.981  1.00 88.99  ? 1015 VAL A CG1 1 
ATOM   7667  C  CG2 . VAL A 1 1015 ? -47.352  27.937  -8.627  1.00 90.65  ? 1015 VAL A CG2 1 
ATOM   7668  N  N   . VAL A 1 1016 ? -44.450  25.126  -9.312  1.00 77.44  ? 1016 VAL A N   1 
ATOM   7669  C  CA  . VAL A 1 1016 ? -44.331  24.363  -10.572 1.00 69.43  ? 1016 VAL A CA  1 
ATOM   7670  C  C   . VAL A 1 1016 ? -45.113  23.047  -10.662 1.00 63.78  ? 1016 VAL A C   1 
ATOM   7671  O  O   . VAL A 1 1016 ? -46.060  22.977  -11.440 1.00 59.99  ? 1016 VAL A O   1 
ATOM   7672  C  CB  . VAL A 1 1016 ? -42.856  24.151  -10.976 1.00 66.94  ? 1016 VAL A CB  1 
ATOM   7673  C  CG1 . VAL A 1 1016 ? -42.688  22.891  -11.800 1.00 65.69  ? 1016 VAL A CG1 1 
ATOM   7674  C  CG2 . VAL A 1 1016 ? -42.321  25.345  -11.719 1.00 66.73  ? 1016 VAL A CG2 1 
ATOM   7675  N  N   . PRO A 1 1017 ? -44.720  22.011  -9.887  1.00 66.36  ? 1017 PRO A N   1 
ATOM   7676  C  CA  . PRO A 1 1017 ? -45.331  20.678  -9.970  1.00 68.22  ? 1017 PRO A CA  1 
ATOM   7677  C  C   . PRO A 1 1017 ? -46.828  20.627  -9.696  1.00 70.36  ? 1017 PRO A C   1 
ATOM   7678  O  O   . PRO A 1 1017 ? -47.535  19.710  -10.109 1.00 69.03  ? 1017 PRO A O   1 
ATOM   7679  C  CB  . PRO A 1 1017 ? -44.564  19.878  -8.907  1.00 67.71  ? 1017 PRO A CB  1 
ATOM   7680  C  CG  . PRO A 1 1017 ? -43.259  20.493  -8.895  1.00 67.22  ? 1017 PRO A CG  1 
ATOM   7681  C  CD  . PRO A 1 1017 ? -43.550  21.972  -9.000  1.00 67.08  ? 1017 PRO A CD  1 
ATOM   7682  N  N   . VAL A 1 1018 ? -47.331  21.604  -8.979  1.00 75.51  ? 1018 VAL A N   1 
ATOM   7683  C  CA  . VAL A 1 1018 ? -48.773  21.687  -8.902  1.00 83.50  ? 1018 VAL A CA  1 
ATOM   7684  C  C   . VAL A 1 1018 ? -49.253  22.211  -10.258 1.00 85.82  ? 1018 VAL A C   1 
ATOM   7685  O  O   . VAL A 1 1018 ? -50.099  21.589  -10.906 1.00 85.70  ? 1018 VAL A O   1 
ATOM   7686  C  CB  . VAL A 1 1018 ? -49.264  22.574  -7.734  1.00 89.01  ? 1018 VAL A CB  1 
ATOM   7687  C  CG1 . VAL A 1 1018 ? -50.810  22.545  -7.618  1.00 91.79  ? 1018 VAL A CG1 1 
ATOM   7688  C  CG2 . VAL A 1 1018 ? -48.596  22.118  -6.431  1.00 91.09  ? 1018 VAL A CG2 1 
ATOM   7689  N  N   . PHE A 1 1019 ? -48.684  23.326  -10.715 1.00 86.75  ? 1019 PHE A N   1 
ATOM   7690  C  CA  . PHE A 1 1019 ? -49.167  23.926  -11.953 1.00 85.38  ? 1019 PHE A CA  1 
ATOM   7691  C  C   . PHE A 1 1019 ? -49.221  22.925  -13.081 1.00 81.45  ? 1019 PHE A C   1 
ATOM   7692  O  O   . PHE A 1 1019 ? -50.256  22.803  -13.738 1.00 81.80  ? 1019 PHE A O   1 
ATOM   7693  C  CB  . PHE A 1 1019 ? -48.310  25.078  -12.445 1.00 86.10  ? 1019 PHE A CB  1 
ATOM   7694  C  CG  . PHE A 1 1019 ? -48.587  25.419  -13.879 1.00 83.58  ? 1019 PHE A CG  1 
ATOM   7695  C  CD1 . PHE A 1 1019 ? -49.894  25.703  -14.283 1.00 81.95  ? 1019 PHE A CD1 1 
ATOM   7696  C  CD2 . PHE A 1 1019 ? -47.573  25.407  -14.824 1.00 81.17  ? 1019 PHE A CD2 1 
ATOM   7697  C  CE1 . PHE A 1 1019 ? -50.182  25.996  -15.588 1.00 80.54  ? 1019 PHE A CE1 1 
ATOM   7698  C  CE2 . PHE A 1 1019 ? -47.853  25.703  -16.136 1.00 80.01  ? 1019 PHE A CE2 1 
ATOM   7699  C  CZ  . PHE A 1 1019 ? -49.160  25.998  -16.521 1.00 80.42  ? 1019 PHE A CZ  1 
ATOM   7700  N  N   . TYR A 1 1020 ? -48.105  22.246  -13.339 1.00 76.06  ? 1020 TYR A N   1 
ATOM   7701  C  CA  . TYR A 1 1020 ? -48.117  21.239  -14.379 1.00 73.62  ? 1020 TYR A CA  1 
ATOM   7702  C  C   . TYR A 1 1020 ? -49.155  20.148  -14.107 1.00 72.05  ? 1020 TYR A C   1 
ATOM   7703  O  O   . TYR A 1 1020 ? -49.945  19.800  -15.003 1.00 72.36  ? 1020 TYR A O   1 
ATOM   7704  C  CB  . TYR A 1 1020 ? -46.713  20.705  -14.667 1.00 74.70  ? 1020 TYR A CB  1 
ATOM   7705  C  CG  . TYR A 1 1020 ? -45.896  21.755  -15.362 1.00 77.77  ? 1020 TYR A CG  1 
ATOM   7706  C  CD1 . TYR A 1 1020 ? -46.378  22.383  -16.495 1.00 80.11  ? 1020 TYR A CD1 1 
ATOM   7707  C  CD2 . TYR A 1 1020 ? -44.681  22.160  -14.860 1.00 80.86  ? 1020 TYR A CD2 1 
ATOM   7708  C  CE1 . TYR A 1 1020 ? -45.664  23.375  -17.124 1.00 82.98  ? 1020 TYR A CE1 1 
ATOM   7709  C  CE2 . TYR A 1 1020 ? -43.948  23.151  -15.473 1.00 83.29  ? 1020 TYR A CE2 1 
ATOM   7710  C  CZ  . TYR A 1 1020 ? -44.448  23.761  -16.604 1.00 85.58  ? 1020 TYR A CZ  1 
ATOM   7711  O  OH  . TYR A 1 1020 ? -43.724  24.757  -17.220 1.00 88.76  ? 1020 TYR A OH  1 
ATOM   7712  N  N   . VAL A 1 1021 ? -49.205  19.650  -12.874 1.00 70.25  ? 1021 VAL A N   1 
ATOM   7713  C  CA  . VAL A 1 1021 ? -50.235  18.669  -12.539 1.00 70.31  ? 1021 VAL A CA  1 
ATOM   7714  C  C   . VAL A 1 1021 ? -51.631  19.208  -12.805 1.00 69.53  ? 1021 VAL A C   1 
ATOM   7715  O  O   . VAL A 1 1021 ? -52.430  18.590  -13.473 1.00 68.35  ? 1021 VAL A O   1 
ATOM   7716  C  CB  . VAL A 1 1021 ? -50.093  18.097  -11.100 1.00 61.39  ? 1021 VAL A CB  1 
ATOM   7717  C  CG1 . VAL A 1 1021 ? -51.431  17.590  -10.583 1.00 60.71  ? 1021 VAL A CG1 1 
ATOM   7718  C  CG2 . VAL A 1 1021 ? -49.076  16.970  -11.093 1.00 61.61  ? 1021 VAL A CG2 1 
ATOM   7719  N  N   . PHE A 1 1022 ? -51.911  20.395  -12.324 1.00 73.08  ? 1022 PHE A N   1 
ATOM   7720  C  CA  . PHE A 1 1022 ? -53.232  20.945  -12.532 1.00 78.08  ? 1022 PHE A CA  1 
ATOM   7721  C  C   . PHE A 1 1022 ? -53.513  21.203  -13.998 1.00 80.04  ? 1022 PHE A C   1 
ATOM   7722  O  O   . PHE A 1 1022 ? -54.663  21.172  -14.436 1.00 82.43  ? 1022 PHE A O   1 
ATOM   7723  C  CB  . PHE A 1 1022 ? -53.426  22.228  -11.742 1.00 79.79  ? 1022 PHE A CB  1 
ATOM   7724  C  CG  . PHE A 1 1022 ? -54.838  22.698  -11.734 1.00 79.79  ? 1022 PHE A CG  1 
ATOM   7725  C  CD1 . PHE A 1 1022 ? -55.703  22.311  -10.725 1.00 80.33  ? 1022 PHE A CD1 1 
ATOM   7726  C  CD2 . PHE A 1 1022 ? -55.311  23.499  -12.754 1.00 79.54  ? 1022 PHE A CD2 1 
ATOM   7727  C  CE1 . PHE A 1 1022 ? -57.010  22.739  -10.724 1.00 82.13  ? 1022 PHE A CE1 1 
ATOM   7728  C  CE2 . PHE A 1 1022 ? -56.622  23.921  -12.760 1.00 81.64  ? 1022 PHE A CE2 1 
ATOM   7729  C  CZ  . PHE A 1 1022 ? -57.475  23.537  -11.744 1.00 82.74  ? 1022 PHE A CZ  1 
ATOM   7730  N  N   . HIS A 1 1023 ? -52.460  21.468  -14.758 1.00 79.94  ? 1023 HIS A N   1 
ATOM   7731  C  CA  . HIS A 1 1023 ? -52.604  21.717  -16.196 1.00 78.96  ? 1023 HIS A CA  1 
ATOM   7732  C  C   . HIS A 1 1023 ? -52.888  20.432  -16.965 1.00 75.29  ? 1023 HIS A C   1 
ATOM   7733  O  O   . HIS A 1 1023 ? -53.834  20.377  -17.769 1.00 76.37  ? 1023 HIS A O   1 
ATOM   7734  C  CB  . HIS A 1 1023 ? -51.349  22.366  -16.758 1.00 79.31  ? 1023 HIS A CB  1 
ATOM   7735  C  CG  . HIS A 1 1023 ? -51.441  22.668  -18.213 1.00 80.26  ? 1023 HIS A CG  1 
ATOM   7736  N  ND1 . HIS A 1 1023 ? -50.506  22.227  -19.126 1.00 81.28  ? 1023 HIS A ND1 1 
ATOM   7737  C  CD2 . HIS A 1 1023 ? -52.371  23.351  -18.917 1.00 80.98  ? 1023 HIS A CD2 1 
ATOM   7738  C  CE1 . HIS A 1 1023 ? -50.850  22.642  -20.331 1.00 82.44  ? 1023 HIS A CE1 1 
ATOM   7739  N  NE2 . HIS A 1 1023 ? -51.979  23.325  -20.230 1.00 82.89  ? 1023 HIS A NE2 1 
ATOM   7740  N  N   . TYR A 1 1024 ? -52.073  19.409  -16.723 1.00 70.38  ? 1024 TYR A N   1 
ATOM   7741  C  CA  . TYR A 1 1024 ? -52.392  18.100  -17.234 1.00 69.68  ? 1024 TYR A CA  1 
ATOM   7742  C  C   . TYR A 1 1024 ? -53.726  17.541  -16.723 1.00 71.73  ? 1024 TYR A C   1 
ATOM   7743  O  O   . TYR A 1 1024 ? -54.400  16.785  -17.402 1.00 71.70  ? 1024 TYR A O   1 
ATOM   7744  C  CB  . TYR A 1 1024 ? -51.278  17.145  -16.890 1.00 71.38  ? 1024 TYR A CB  1 
ATOM   7745  C  CG  . TYR A 1 1024 ? -51.706  15.704  -16.992 1.00 75.64  ? 1024 TYR A CG  1 
ATOM   7746  C  CD1 . TYR A 1 1024 ? -51.268  14.906  -18.037 1.00 79.07  ? 1024 TYR A CD1 1 
ATOM   7747  C  CD2 . TYR A 1 1024 ? -52.556  15.142  -16.047 1.00 78.29  ? 1024 TYR A CD2 1 
ATOM   7748  C  CE1 . TYR A 1 1024 ? -51.656  13.594  -18.143 1.00 82.61  ? 1024 TYR A CE1 1 
ATOM   7749  C  CE2 . TYR A 1 1024 ? -52.950  13.839  -16.135 1.00 81.82  ? 1024 TYR A CE2 1 
ATOM   7750  C  CZ  . TYR A 1 1024 ? -52.495  13.061  -17.184 1.00 86.24  ? 1024 TYR A CZ  1 
ATOM   7751  O  OH  . TYR A 1 1024 ? -52.883  11.738  -17.288 1.00 91.96  ? 1024 TYR A OH  1 
ATOM   7752  N  N   . LEU A 1 1025 ? -54.100  17.876  -15.503 1.00 75.27  ? 1025 LEU A N   1 
ATOM   7753  C  CA  . LEU A 1 1025 ? -55.318  17.298  -14.944 1.00 78.37  ? 1025 LEU A CA  1 
ATOM   7754  C  C   . LEU A 1 1025 ? -56.536  17.888  -15.593 1.00 78.76  ? 1025 LEU A C   1 
ATOM   7755  O  O   . LEU A 1 1025 ? -57.497  17.196  -15.867 1.00 77.68  ? 1025 LEU A O   1 
ATOM   7756  C  CB  . LEU A 1 1025 ? -55.415  17.552  -13.444 1.00 79.57  ? 1025 LEU A CB  1 
ATOM   7757  C  CG  . LEU A 1 1025 ? -54.936  16.458  -12.498 1.00 80.22  ? 1025 LEU A CG  1 
ATOM   7758  C  CD1 . LEU A 1 1025 ? -55.341  16.854  -11.096 1.00 81.25  ? 1025 LEU A CD1 1 
ATOM   7759  C  CD2 . LEU A 1 1025 ? -55.513  15.100  -12.853 1.00 80.63  ? 1025 LEU A CD2 1 
ATOM   7760  N  N   . GLU A 1 1026 ? -56.475  19.192  -15.812 1.00 82.18  ? 1026 GLU A N   1 
ATOM   7761  C  CA  . GLU A 1 1026 ? -57.610  19.966  -16.269 1.00 88.69  ? 1026 GLU A CA  1 
ATOM   7762  C  C   . GLU A 1 1026 ? -57.645  20.016  -17.783 1.00 92.34  ? 1026 GLU A C   1 
ATOM   7763  O  O   . GLU A 1 1026 ? -58.682  19.790  -18.421 1.00 96.46  ? 1026 GLU A O   1 
ATOM   7764  C  CB  . GLU A 1 1026 ? -57.505  21.390  -15.728 1.00 91.42  ? 1026 GLU A CB  1 
ATOM   7765  C  CG  . GLU A 1 1026 ? -58.470  22.372  -16.371 1.00 95.81  ? 1026 GLU A CG  1 
ATOM   7766  C  CD  . GLU A 1 1026 ? -59.867  22.290  -15.791 1.00 100.03 ? 1026 GLU A CD  1 
ATOM   7767  O  OE1 . GLU A 1 1026 ? -60.048  21.491  -14.841 1.00 101.10 ? 1026 GLU A OE1 1 
ATOM   7768  O  OE2 . GLU A 1 1026 ? -60.765  23.031  -16.283 1.00 101.08 ? 1026 GLU A OE2 1 
ATOM   7769  N  N   . THR A 1 1027 ? -56.509  20.325  -18.379 1.00 90.47  ? 1027 THR A N   1 
ATOM   7770  C  CA  . THR A 1 1027 ? -56.549  20.544  -19.799 1.00 89.96  ? 1027 THR A CA  1 
ATOM   7771  C  C   . THR A 1 1027 ? -56.600  19.269  -20.598 1.00 91.14  ? 1027 THR A C   1 
ATOM   7772  O  O   . THR A 1 1027 ? -56.692  19.308  -21.800 1.00 93.42  ? 1027 THR A O   1 
ATOM   7773  C  CB  . THR A 1 1027 ? -55.440  21.448  -20.256 1.00 87.49  ? 1027 THR A CB  1 
ATOM   7774  O  OG1 . THR A 1 1027 ? -55.958  22.781  -20.343 1.00 88.97  ? 1027 THR A OG1 1 
ATOM   7775  C  CG2 . THR A 1 1027 ? -54.975  21.035  -21.626 1.00 86.29  ? 1027 THR A CG2 1 
ATOM   7776  N  N   . GLY A 1 1028 ? -56.588  18.130  -19.933 1.00 92.24  ? 1028 GLY A N   1 
ATOM   7777  C  CA  . GLY A 1 1028 ? -56.787  16.884  -20.646 1.00 95.28  ? 1028 GLY A CA  1 
ATOM   7778  C  C   . GLY A 1 1028 ? -57.901  16.118  -19.967 1.00 98.25  ? 1028 GLY A C   1 
ATOM   7779  O  O   . GLY A 1 1028 ? -57.884  14.901  -19.915 1.00 97.06  ? 1028 GLY A O   1 
ATOM   7780  N  N   . ASN A 1 1029 ? -58.881  16.851  -19.452 1.00 104.73 ? 1029 ASN A N   1 
ATOM   7781  C  CA  . ASN A 1 1029 ? -59.746  16.320  -18.406 1.00 111.81 ? 1029 ASN A CA  1 
ATOM   7782  C  C   . ASN A 1 1029 ? -59.384  14.885  -18.010 1.00 109.73 ? 1029 ASN A C   1 
ATOM   7783  O  O   . ASN A 1 1029 ? -59.574  13.924  -18.755 1.00 108.03 ? 1029 ASN A O   1 
ATOM   7784  C  CB  . ASN A 1 1029 ? -61.236  16.511  -18.702 1.00 121.79 ? 1029 ASN A CB  1 
ATOM   7785  C  CG  . ASN A 1 1029 ? -61.826  15.373  -19.497 1.00 131.69 ? 1029 ASN A CG  1 
ATOM   7786  O  OD1 . ASN A 1 1029 ? -62.886  14.847  -19.144 1.00 136.68 ? 1029 ASN A OD1 1 
ATOM   7787  N  ND2 . ASN A 1 1029 ? -61.152  14.985  -20.584 1.00 133.34 ? 1029 ASN A ND2 1 
ATOM   7788  N  N   . HIS A 1 1030 ? -58.817  14.783  -16.817 1.00 111.07 ? 1030 HIS A N   1 
ATOM   7789  C  CA  . HIS A 1 1030 ? -58.410  13.518  -16.215 1.00 110.08 ? 1030 HIS A CA  1 
ATOM   7790  C  C   . HIS A 1 1030 ? -58.868  13.475  -14.744 1.00 108.86 ? 1030 HIS A C   1 
ATOM   7791  O  O   . HIS A 1 1030 ? -58.580  12.532  -14.001 1.00 107.67 ? 1030 HIS A O   1 
ATOM   7792  C  CB  . HIS A 1 1030 ? -56.891  13.325  -16.349 1.00 106.51 ? 1030 HIS A CB  1 
ATOM   7793  C  CG  . HIS A 1 1030 ? -56.444  13.097  -17.758 1.00 103.77 ? 1030 HIS A CG  1 
ATOM   7794  N  ND1 . HIS A 1 1030 ? -56.882  12.029  -18.513 1.00 103.05 ? 1030 HIS A ND1 1 
ATOM   7795  C  CD2 . HIS A 1 1030 ? -55.605  13.802  -18.552 1.00 101.93 ? 1030 HIS A CD2 1 
ATOM   7796  C  CE1 . HIS A 1 1030 ? -56.328  12.088  -19.709 1.00 101.81 ? 1030 HIS A CE1 1 
ATOM   7797  N  NE2 . HIS A 1 1030 ? -55.545  13.150  -19.757 1.00 100.65 ? 1030 HIS A NE2 1 
ATOM   7798  N  N   . TRP A 1 1031 ? -59.605  14.509  -14.349 1.00 107.07 ? 1031 TRP A N   1 
ATOM   7799  C  CA  . TRP A 1 1031 ? -60.122  14.633  -13.007 1.00 104.20 ? 1031 TRP A CA  1 
ATOM   7800  C  C   . TRP A 1 1031 ? -60.835  13.379  -12.545 1.00 105.90 ? 1031 TRP A C   1 
ATOM   7801  O  O   . TRP A 1 1031 ? -61.096  13.200  -11.356 1.00 109.75 ? 1031 TRP A O   1 
ATOM   7802  C  CB  . TRP A 1 1031 ? -61.086  15.793  -12.959 1.00 102.44 ? 1031 TRP A CB  1 
ATOM   7803  C  CG  . TRP A 1 1031 ? -60.434  17.099  -13.054 1.00 98.67  ? 1031 TRP A CG  1 
ATOM   7804  C  CD1 . TRP A 1 1031 ? -60.598  18.027  -14.031 1.00 98.36  ? 1031 TRP A CD1 1 
ATOM   7805  C  CD2 . TRP A 1 1031 ? -59.512  17.644  -12.129 1.00 97.49  ? 1031 TRP A CD2 1 
ATOM   7806  N  NE1 . TRP A 1 1031 ? -59.830  19.128  -13.768 1.00 97.49  ? 1031 TRP A NE1 1 
ATOM   7807  C  CE2 . TRP A 1 1031 ? -59.155  18.916  -12.599 1.00 97.91  ? 1031 TRP A CE2 1 
ATOM   7808  C  CE3 . TRP A 1 1031 ? -58.956  17.183  -10.942 1.00 98.10  ? 1031 TRP A CE3 1 
ATOM   7809  C  CZ2 . TRP A 1 1031 ? -58.260  19.724  -11.931 1.00 99.60  ? 1031 TRP A CZ2 1 
ATOM   7810  C  CZ3 . TRP A 1 1031 ? -58.075  17.987  -10.278 1.00 99.44  ? 1031 TRP A CZ3 1 
ATOM   7811  C  CH2 . TRP A 1 1031 ? -57.727  19.243  -10.773 1.00 100.09 ? 1031 TRP A CH2 1 
ATOM   7812  N  N   . ASN A 1 1032 ? -61.170  12.508  -13.477 1.00 104.86 ? 1032 ASN A N   1 
ATOM   7813  C  CA  . ASN A 1 1032 ? -61.840  11.284  -13.094 1.00 107.31 ? 1032 ASN A CA  1 
ATOM   7814  C  C   . ASN A 1 1032 ? -60.844  10.249  -12.607 1.00 104.76 ? 1032 ASN A C   1 
ATOM   7815  O  O   . ASN A 1 1032 ? -61.199  9.074   -12.456 1.00 104.99 ? 1032 ASN A O   1 
ATOM   7816  C  CB  . ASN A 1 1032 ? -62.558  10.711  -14.287 1.00 110.16 ? 1032 ASN A CB  1 
ATOM   7817  C  CG  . ASN A 1 1032 ? -61.607  10.381  -15.374 1.00 108.82 ? 1032 ASN A CG  1 
ATOM   7818  O  OD1 . ASN A 1 1032 ? -60.963  11.272  -15.937 1.00 105.96 ? 1032 ASN A OD1 1 
ATOM   7819  N  ND2 . ASN A 1 1032 ? -61.462  9.091   -15.658 1.00 110.04 ? 1032 ASN A ND2 1 
ATOM   7820  N  N   . ILE A 1 1033 ? -59.594  10.665  -12.397 1.00 101.37 ? 1033 ILE A N   1 
ATOM   7821  C  CA  . ILE A 1 1033 ? -58.615  9.753   -11.826 1.00 100.34 ? 1033 ILE A CA  1 
ATOM   7822  C  C   . ILE A 1 1033 ? -59.142  9.361   -10.483 1.00 103.50 ? 1033 ILE A C   1 
ATOM   7823  O  O   . ILE A 1 1033 ? -58.947  8.222   -10.042 1.00 104.65 ? 1033 ILE A O   1 
ATOM   7824  C  CB  . ILE A 1 1033 ? -57.280  10.397  -11.496 1.00 96.75  ? 1033 ILE A CB  1 
ATOM   7825  C  CG1 . ILE A 1 1033 ? -56.522  10.828  -12.737 1.00 94.91  ? 1033 ILE A CG1 1 
ATOM   7826  C  CG2 . ILE A 1 1033 ? -56.420  9.394   -10.760 1.00 96.73  ? 1033 ILE A CG2 1 
ATOM   7827  C  CD1 . ILE A 1 1033 ? -55.103  11.205  -12.411 1.00 93.69  ? 1033 ILE A CD1 1 
ATOM   7828  N  N   . PHE A 1 1034 ? -59.805  10.335  -9.847  1.00 105.41 ? 1034 PHE A N   1 
ATOM   7829  C  CA  . PHE A 1 1034 ? -60.099  10.306  -8.420  1.00 107.57 ? 1034 PHE A CA  1 
ATOM   7830  C  C   . PHE A 1 1034 ? -61.283  9.467   -8.068  1.00 115.98 ? 1034 PHE A C   1 
ATOM   7831  O  O   . PHE A 1 1034 ? -62.388  9.654   -8.588  1.00 117.25 ? 1034 PHE A O   1 
ATOM   7832  C  CB  . PHE A 1 1034 ? -60.290  11.711  -7.873  1.00 101.65 ? 1034 PHE A CB  1 
ATOM   7833  C  CG  . PHE A 1 1034 ? -59.113  12.593  -8.096  1.00 95.19  ? 1034 PHE A CG  1 
ATOM   7834  C  CD1 . PHE A 1 1034 ? -57.936  12.374  -7.427  1.00 92.68  ? 1034 PHE A CD1 1 
ATOM   7835  C  CD2 . PHE A 1 1034 ? -59.171  13.634  -8.993  1.00 92.00  ? 1034 PHE A CD2 1 
ATOM   7836  C  CE1 . PHE A 1 1034 ? -56.844  13.183  -7.660  1.00 89.49  ? 1034 PHE A CE1 1 
ATOM   7837  C  CE2 . PHE A 1 1034 ? -58.075  14.449  -9.212  1.00 87.91  ? 1034 PHE A CE2 1 
ATOM   7838  C  CZ  . PHE A 1 1034 ? -56.921  14.217  -8.557  1.00 86.80  ? 1034 PHE A CZ  1 
ATOM   7839  N  N   . HIS A 1 1035 ? -61.039  8.530   -7.173  1.00 124.09 ? 1035 HIS A N   1 
ATOM   7840  C  CA  . HIS A 1 1035 ? -62.099  7.685   -6.716  1.00 136.29 ? 1035 HIS A CA  1 
ATOM   7841  C  C   . HIS A 1 1035 ? -62.968  8.580   -5.876  1.00 140.98 ? 1035 HIS A C   1 
ATOM   7842  O  O   . HIS A 1 1035 ? -64.193  8.437   -5.868  1.00 144.93 ? 1035 HIS A O   1 
ATOM   7843  C  CB  . HIS A 1 1035 ? -61.499  6.534   -5.935  1.00 145.58 ? 1035 HIS A CB  1 
ATOM   7844  C  CG  . HIS A 1 1035 ? -60.391  5.856   -6.677  1.00 152.26 ? 1035 HIS A CG  1 
ATOM   7845  N  ND1 . HIS A 1 1035 ? -60.492  4.571   -7.165  1.00 156.32 ? 1035 HIS A ND1 1 
ATOM   7846  C  CD2 . HIS A 1 1035 ? -59.176  6.311   -7.067  1.00 153.19 ? 1035 HIS A CD2 1 
ATOM   7847  C  CE1 . HIS A 1 1035 ? -59.377  4.252   -7.801  1.00 156.17 ? 1035 HIS A CE1 1 
ATOM   7848  N  NE2 . HIS A 1 1035 ? -58.563  5.293   -7.758  1.00 154.61 ? 1035 HIS A NE2 1 
ATOM   7849  N  N   . SER A 1 1036 ? -62.315  9.542   -5.218  1.00 139.42 ? 1036 SER A N   1 
ATOM   7850  C  CA  . SER A 1 1036 ? -62.975  10.511  -4.336  1.00 140.26 ? 1036 SER A CA  1 
ATOM   7851  C  C   . SER A 1 1036 ? -63.788  11.558  -5.101  1.00 138.81 ? 1036 SER A C   1 
ATOM   7852  O  O   . SER A 1 1036 ? -64.104  11.390  -6.283  1.00 137.73 ? 1036 SER A O   1 
ATOM   7853  C  CB  . SER A 1 1036 ? -61.945  11.232  -3.464  1.00 140.70 ? 1036 SER A CB  1 
ATOM   7854  O  OG  . SER A 1 1036 ? -61.230  12.194  -4.223  1.00 139.57 ? 1036 SER A OG  1 
ATOM   7855  N  N   . ASP A 1 1037 ? -64.146  12.636  -4.415  1.00 137.18 ? 1037 ASP A N   1 
ATOM   7856  C  CA  . ASP A 1 1037 ? -64.822  13.724  -5.088  1.00 134.12 ? 1037 ASP A CA  1 
ATOM   7857  C  C   . ASP A 1 1037 ? -63.790  14.576  -5.776  1.00 124.21 ? 1037 ASP A C   1 
ATOM   7858  O  O   . ASP A 1 1037 ? -62.907  15.119  -5.131  1.00 122.99 ? 1037 ASP A O   1 
ATOM   7859  C  CB  . ASP A 1 1037 ? -65.615  14.572  -4.111  1.00 137.82 ? 1037 ASP A CB  1 
ATOM   7860  C  CG  . ASP A 1 1037 ? -66.273  15.756  -4.786  1.00 136.51 ? 1037 ASP A CG  1 
ATOM   7861  O  OD1 . ASP A 1 1037 ? -65.844  16.109  -5.916  1.00 131.34 ? 1037 ASP A OD1 1 
ATOM   7862  O  OD2 . ASP A 1 1037 ? -67.217  16.322  -4.178  1.00 138.99 ? 1037 ASP A OD2 1 
ATOM   7863  N  N   . PRO A 1 1038 ? -63.911  14.703  -7.096  1.00 118.59 ? 1038 PRO A N   1 
ATOM   7864  C  CA  . PRO A 1 1038 ? -62.928  15.361  -7.961  1.00 113.49 ? 1038 PRO A CA  1 
ATOM   7865  C  C   . PRO A 1 1038 ? -63.029  16.859  -7.869  1.00 111.34 ? 1038 PRO A C   1 
ATOM   7866  O  O   . PRO A 1 1038 ? -62.022  17.565  -7.965  1.00 110.07 ? 1038 PRO A O   1 
ATOM   7867  C  CB  . PRO A 1 1038 ? -63.346  14.929  -9.369  1.00 113.53 ? 1038 PRO A CB  1 
ATOM   7868  C  CG  . PRO A 1 1038 ? -64.299  13.786  -9.174  1.00 117.42 ? 1038 PRO A CG  1 
ATOM   7869  C  CD  . PRO A 1 1038 ? -64.983  14.075  -7.875  1.00 119.78 ? 1038 PRO A CD  1 
ATOM   7870  N  N   . LEU A 1 1039 ? -64.250  17.340  -7.679  1.00 111.56 ? 1039 LEU A N   1 
ATOM   7871  C  CA  . LEU A 1 1039 ? -64.508  18.776  -7.667  1.00 109.66 ? 1039 LEU A CA  1 
ATOM   7872  C  C   . LEU A 1 1039 ? -63.780  19.474  -6.520  1.00 105.31 ? 1039 LEU A C   1 
ATOM   7873  O  O   . LEU A 1 1039 ? -63.402  20.650  -6.626  1.00 102.26 ? 1039 LEU A O   1 
ATOM   7874  C  CB  . LEU A 1 1039 ? -66.009  19.030  -7.591  1.00 112.41 ? 1039 LEU A CB  1 
ATOM   7875  C  CG  . LEU A 1 1039 ? -66.441  20.440  -7.946  1.00 114.05 ? 1039 LEU A CG  1 
ATOM   7876  C  CD1 . LEU A 1 1039 ? -65.525  21.059  -9.012  1.00 110.94 ? 1039 LEU A CD1 1 
ATOM   7877  C  CD2 . LEU A 1 1039 ? -67.907  20.408  -8.391  1.00 117.17 ? 1039 LEU A CD2 1 
ATOM   7878  N  N   . ILE A 1 1040 ? -63.597  18.720  -5.434  1.00 104.52 ? 1040 ILE A N   1 
ATOM   7879  C  CA  . ILE A 1 1040 ? -62.971  19.204  -4.211  1.00 102.54 ? 1040 ILE A CA  1 
ATOM   7880  C  C   . ILE A 1 1040 ? -61.483  18.898  -4.190  1.00 102.09 ? 1040 ILE A C   1 
ATOM   7881  O  O   . ILE A 1 1040 ? -60.710  19.575  -3.513  1.00 101.82 ? 1040 ILE A O   1 
ATOM   7882  C  CB  . ILE A 1 1040 ? -63.635  18.579  -2.967  1.00 101.91 ? 1040 ILE A CB  1 
ATOM   7883  C  CG1 . ILE A 1 1040 ? -64.114  19.673  -1.987  1.00 104.96 ? 1040 ILE A CG1 1 
ATOM   7884  C  CG2 . ILE A 1 1040 ? -62.734  17.518  -2.336  1.00 98.46  ? 1040 ILE A CG2 1 
ATOM   7885  C  CD1 . ILE A 1 1040 ? -63.472  21.101  -2.154  1.00 123.02 ? 1040 ILE A CD1 1 
ATOM   7886  N  N   . GLU A 1 1041 ? -61.087  17.867  -4.929  1.00 103.40 ? 1041 GLU A N   1 
ATOM   7887  C  CA  . GLU A 1 1041 ? -59.680  17.582  -5.133  1.00 104.69 ? 1041 GLU A CA  1 
ATOM   7888  C  C   . GLU A 1 1041 ? -59.118  18.668  -6.007  1.00 104.53 ? 1041 GLU A C   1 
ATOM   7889  O  O   . GLU A 1 1041 ? -57.897  18.878  -6.039  1.00 100.94 ? 1041 GLU A O   1 
ATOM   7890  C  CB  . GLU A 1 1041 ? -59.488  16.272  -5.867  1.00 108.13 ? 1041 GLU A CB  1 
ATOM   7891  C  CG  . GLU A 1 1041 ? -58.188  15.636  -5.552  1.00 111.80 ? 1041 GLU A CG  1 
ATOM   7892  C  CD  . GLU A 1 1041 ? -58.299  14.896  -4.268  1.00 120.02 ? 1041 GLU A CD  1 
ATOM   7893  O  OE1 . GLU A 1 1041 ? -59.388  14.322  -4.035  1.00 122.88 ? 1041 GLU A OE1 1 
ATOM   7894  O  OE2 . GLU A 1 1041 ? -57.328  14.909  -3.484  1.00 123.89 ? 1041 GLU A OE2 1 
ATOM   7895  N  N   . LYS A 1 1042 ? -60.018  19.321  -6.747  1.00 107.45 ? 1042 LYS A N   1 
ATOM   7896  C  CA  . LYS A 1 1042 ? -59.653  20.422  -7.610  1.00 111.54 ? 1042 LYS A CA  1 
ATOM   7897  C  C   . LYS A 1 1042 ? -59.533  21.724  -6.835  1.00 116.92 ? 1042 LYS A C   1 
ATOM   7898  O  O   . LYS A 1 1042 ? -58.662  22.545  -7.137  1.00 117.36 ? 1042 LYS A O   1 
ATOM   7899  C  CB  . LYS A 1 1042 ? -60.654  20.599  -8.738  1.00 113.62 ? 1042 LYS A CB  1 
ATOM   7900  C  CG  . LYS A 1 1042 ? -60.443  21.926  -9.456  1.00 116.83 ? 1042 LYS A CG  1 
ATOM   7901  C  CD  . LYS A 1 1042 ? -61.567  22.300  -10.411 1.00 120.83 ? 1042 LYS A CD  1 
ATOM   7902  C  CE  . LYS A 1 1042 ? -61.253  21.969  -11.869 1.00 119.40 ? 1042 LYS A CE  1 
ATOM   7903  N  NZ  . LYS A 1 1042 ? -62.303  22.556  -12.768 1.00 120.70 ? 1042 LYS A NZ  1 
ATOM   7904  N  N   . GLN A 1 1043 ? -60.409  21.926  -5.849  1.00 121.61 ? 1043 GLN A N   1 
ATOM   7905  C  CA  . GLN A 1 1043 ? -60.297  23.094  -4.971  1.00 124.44 ? 1043 GLN A CA  1 
ATOM   7906  C  C   . GLN A 1 1043 ? -58.916  23.114  -4.368  1.00 118.43 ? 1043 GLN A C   1 
ATOM   7907  O  O   . GLN A 1 1043 ? -58.214  24.125  -4.410  1.00 117.69 ? 1043 GLN A O   1 
ATOM   7908  C  CB  . GLN A 1 1043 ? -61.343  23.080  -3.839  1.00 132.04 ? 1043 GLN A CB  1 
ATOM   7909  C  CG  . GLN A 1 1043 ? -62.643  23.752  -4.222  1.00 139.34 ? 1043 GLN A CG  1 
ATOM   7910  C  CD  . GLN A 1 1043 ? -62.475  24.572  -5.501  1.00 142.48 ? 1043 GLN A CD  1 
ATOM   7911  O  OE1 . GLN A 1 1043 ? -61.841  25.633  -5.488  1.00 142.47 ? 1043 GLN A OE1 1 
ATOM   7912  N  NE2 . GLN A 1 1043 ? -63.013  24.063  -6.622  1.00 143.33 ? 1043 GLN A NE2 1 
ATOM   7913  N  N   . LYS A 1 1044 ? -58.540  21.968  -3.811  1.00 115.58 ? 1044 LYS A N   1 
ATOM   7914  C  CA  . LYS A 1 1044 ? -57.263  21.805  -3.131  1.00 112.35 ? 1044 LYS A CA  1 
ATOM   7915  C  C   . LYS A 1 1044 ? -56.117  22.333  -3.995  1.00 109.60 ? 1044 LYS A C   1 
ATOM   7916  O  O   . LYS A 1 1044 ? -55.265  23.080  -3.522  1.00 109.93 ? 1044 LYS A O   1 
ATOM   7917  C  CB  . LYS A 1 1044 ? -57.019  20.323  -2.767  1.00 111.88 ? 1044 LYS A CB  1 
ATOM   7918  C  CG  . LYS A 1 1044 ? -57.698  19.825  -1.455  1.00 148.16 ? 1044 LYS A CG  1 
ATOM   7919  C  CD  . LYS A 1 1044 ? -57.693  18.266  -1.301  1.00 145.36 ? 1044 LYS A CD  1 
ATOM   7920  C  CE  . LYS A 1 1044 ? -56.334  17.687  -0.837  1.00 143.75 ? 1044 LYS A CE  1 
ATOM   7921  N  NZ  . LYS A 1 1044 ? -56.314  16.187  -0.727  1.00 142.79 ? 1044 LYS A NZ  1 
ATOM   7922  N  N   . LEU A 1 1045 ? -56.106  21.952  -5.269  1.00 106.63 ? 1045 LEU A N   1 
ATOM   7923  C  CA  . LEU A 1 1045 ? -54.986  22.282  -6.130  1.00 101.17 ? 1045 LEU A CA  1 
ATOM   7924  C  C   . LEU A 1 1045 ? -54.994  23.737  -6.528  1.00 100.03 ? 1045 LEU A C   1 
ATOM   7925  O  O   . LEU A 1 1045 ? -53.938  24.352  -6.640  1.00 98.37  ? 1045 LEU A O   1 
ATOM   7926  C  CB  . LEU A 1 1045 ? -54.939  21.370  -7.339  1.00 97.26  ? 1045 LEU A CB  1 
ATOM   7927  C  CG  . LEU A 1 1045 ? -54.772  19.924  -6.928  1.00 93.90  ? 1045 LEU A CG  1 
ATOM   7928  C  CD1 . LEU A 1 1045 ? -54.584  19.124  -8.176  1.00 93.84  ? 1045 LEU A CD1 1 
ATOM   7929  C  CD2 . LEU A 1 1045 ? -53.586  19.752  -5.993  1.00 90.45  ? 1045 LEU A CD2 1 
ATOM   7930  N  N   . LYS A 1 1046 ? -56.173  24.296  -6.751  1.00 101.46 ? 1046 LYS A N   1 
ATOM   7931  C  CA  . LYS A 1 1046 ? -56.225  25.723  -6.987  1.00 105.49 ? 1046 LYS A CA  1 
ATOM   7932  C  C   . LYS A 1 1046 ? -55.507  26.370  -5.812  1.00 109.32 ? 1046 LYS A C   1 
ATOM   7933  O  O   . LYS A 1 1046 ? -54.616  27.198  -5.992  1.00 110.34 ? 1046 LYS A O   1 
ATOM   7934  C  CB  . LYS A 1 1046 ? -57.660  26.234  -7.049  1.00 108.13 ? 1046 LYS A CB  1 
ATOM   7935  C  CG  . LYS A 1 1046 ? -58.505  25.723  -8.200  1.00 109.93 ? 1046 LYS A CG  1 
ATOM   7936  C  CD  . LYS A 1 1046 ? -59.669  26.690  -8.401  1.00 115.27 ? 1046 LYS A CD  1 
ATOM   7937  C  CE  . LYS A 1 1046 ? -60.875  26.058  -9.099  1.00 118.81 ? 1046 LYS A CE  1 
ATOM   7938  N  NZ  . LYS A 1 1046 ? -62.104  26.934  -8.998  1.00 121.80 ? 1046 LYS A NZ  1 
ATOM   7939  N  N   . LYS A 1 1047 ? -55.889  25.956  -4.606  1.00 111.13 ? 1047 LYS A N   1 
ATOM   7940  C  CA  . LYS A 1 1047 ? -55.307  26.478  -3.372  1.00 112.21 ? 1047 LYS A CA  1 
ATOM   7941  C  C   . LYS A 1 1047 ? -53.801  26.366  -3.380  1.00 104.46 ? 1047 LYS A C   1 
ATOM   7942  O  O   . LYS A 1 1047 ? -53.106  27.386  -3.418  1.00 101.99 ? 1047 LYS A O   1 
ATOM   7943  C  CB  . LYS A 1 1047 ? -55.862  25.723  -2.165  1.00 120.72 ? 1047 LYS A CB  1 
ATOM   7944  C  CG  . LYS A 1 1047 ? -55.439  26.257  -0.808  1.00 129.77 ? 1047 LYS A CG  1 
ATOM   7945  C  CD  . LYS A 1 1047 ? -56.437  25.771  0.243   1.00 139.67 ? 1047 LYS A CD  1 
ATOM   7946  C  CE  . LYS A 1 1047 ? -56.187  26.376  1.627   1.00 146.92 ? 1047 LYS A CE  1 
ATOM   7947  N  NZ  . LYS A 1 1047 ? -54.812  26.086  2.148   1.00 148.70 ? 1047 LYS A NZ  1 
ATOM   7948  N  N   . LYS A 1 1048 ? -53.316  25.118  -3.350  1.00 99.88  ? 1048 LYS A N   1 
ATOM   7949  C  CA  . LYS A 1 1048 ? -51.885  24.809  -3.327  1.00 93.40  ? 1048 LYS A CA  1 
ATOM   7950  C  C   . LYS A 1 1048 ? -51.198  25.714  -4.298  1.00 88.63  ? 1048 LYS A C   1 
ATOM   7951  O  O   . LYS A 1 1048 ? -50.109  26.209  -4.062  1.00 86.66  ? 1048 LYS A O   1 
ATOM   7952  C  CB  . LYS A 1 1048 ? -51.639  23.378  -3.765  1.00 90.07  ? 1048 LYS A CB  1 
ATOM   7953  C  CG  . LYS A 1 1048 ? -51.463  22.381  -2.667  1.00 89.92  ? 1048 LYS A CG  1 
ATOM   7954  C  CD  . LYS A 1 1048 ? -50.432  21.375  -3.113  1.00 89.72  ? 1048 LYS A CD  1 
ATOM   7955  C  CE  . LYS A 1 1048 ? -50.853  19.940  -2.853  1.00 90.28  ? 1048 LYS A CE  1 
ATOM   7956  N  NZ  . LYS A 1 1048 ? -49.687  19.034  -3.086  1.00 89.85  ? 1048 LYS A NZ  1 
ATOM   7957  N  N   . LEU A 1 1049 ? -51.884  25.934  -5.401  1.00 87.60  ? 1049 LEU A N   1 
ATOM   7958  C  CA  . LEU A 1 1049 ? -51.399  26.777  -6.461  1.00 86.12  ? 1049 LEU A CA  1 
ATOM   7959  C  C   . LEU A 1 1049 ? -51.355  28.245  -6.043  1.00 89.66  ? 1049 LEU A C   1 
ATOM   7960  O  O   . LEU A 1 1049 ? -50.454  28.974  -6.448  1.00 91.51  ? 1049 LEU A O   1 
ATOM   7961  C  CB  . LEU A 1 1049 ? -52.314  26.632  -7.661  1.00 81.10  ? 1049 LEU A CB  1 
ATOM   7962  C  CG  . LEU A 1 1049 ? -51.577  26.752  -8.967  1.00 75.62  ? 1049 LEU A CG  1 
ATOM   7963  C  CD1 . LEU A 1 1049 ? -50.807  25.468  -9.223  1.00 70.45  ? 1049 LEU A CD1 1 
ATOM   7964  C  CD2 . LEU A 1 1049 ? -52.632  27.002  -9.986  1.00 75.53  ? 1049 LEU A CD2 1 
ATOM   7965  N  N   . LYS A 1 1050 ? -52.328  28.693  -5.259  1.00 90.87  ? 1050 LYS A N   1 
ATOM   7966  C  CA  . LYS A 1 1050 ? -52.334  30.083  -4.858  1.00 92.62  ? 1050 LYS A CA  1 
ATOM   7967  C  C   . LYS A 1 1050 ? -51.376  30.307  -3.707  1.00 96.87  ? 1050 LYS A C   1 
ATOM   7968  O  O   . LYS A 1 1050 ? -50.536  31.202  -3.738  1.00 95.84  ? 1050 LYS A O   1 
ATOM   7969  C  CB  . LYS A 1 1050 ? -53.732  30.543  -4.470  1.00 92.55  ? 1050 LYS A CB  1 
ATOM   7970  C  CG  . LYS A 1 1050 ? -53.774  32.028  -4.311  1.00 92.02  ? 1050 LYS A CG  1 
ATOM   7971  C  CD  . LYS A 1 1050 ? -55.080  32.548  -3.810  1.00 93.51  ? 1050 LYS A CD  1 
ATOM   7972  C  CE  . LYS A 1 1050 ? -54.856  34.006  -3.465  1.00 96.49  ? 1050 LYS A CE  1 
ATOM   7973  N  NZ  . LYS A 1 1050 ? -55.940  34.930  -3.896  1.00 99.83  ? 1050 LYS A NZ  1 
ATOM   7974  N  N   . GLU A 1 1051 ? -51.489  29.506  -2.666  1.00 103.18 ? 1051 GLU A N   1 
ATOM   7975  C  CA  . GLU A 1 1051 ? -50.670  29.831  -1.527  1.00 111.73 ? 1051 GLU A CA  1 
ATOM   7976  C  C   . GLU A 1 1051 ? -49.243  29.849  -2.042  1.00 110.27 ? 1051 GLU A C   1 
ATOM   7977  O  O   . GLU A 1 1051 ? -48.466  30.727  -1.705  1.00 111.15 ? 1051 GLU A O   1 
ATOM   7978  C  CB  . GLU A 1 1051 ? -50.929  28.911  -0.315  1.00 121.58 ? 1051 GLU A CB  1 
ATOM   7979  C  CG  . GLU A 1 1051 ? -50.157  27.602  -0.249  1.00 129.49 ? 1051 GLU A CG  1 
ATOM   7980  C  CD  . GLU A 1 1051 ? -50.908  26.533  0.548   1.00 136.98 ? 1051 GLU A CD  1 
ATOM   7981  O  OE1 . GLU A 1 1051 ? -51.937  26.875  1.187   1.00 139.67 ? 1051 GLU A OE1 1 
ATOM   7982  O  OE2 . GLU A 1 1051 ? -50.474  25.355  0.515   1.00 139.46 ? 1051 GLU A OE2 1 
ATOM   7983  N  N   . GLY A 1 1052 ? -48.933  28.937  -2.946  1.00 108.38 ? 1052 GLY A N   1 
ATOM   7984  C  CA  . GLY A 1 1052 ? -47.594  28.862  -3.491  1.00 109.31 ? 1052 GLY A CA  1 
ATOM   7985  C  C   . GLY A 1 1052 ? -47.219  30.040  -4.364  1.00 107.86 ? 1052 GLY A C   1 
ATOM   7986  O  O   . GLY A 1 1052 ? -46.047  30.357  -4.532  1.00 108.36 ? 1052 GLY A O   1 
ATOM   7987  N  N   . MET A 1 1053 ? -48.220  30.692  -4.930  1.00 109.57 ? 1053 MET A N   1 
ATOM   7988  C  CA  . MET A 1 1053 ? -47.962  31.802  -5.831  1.00 110.30 ? 1053 MET A CA  1 
ATOM   7989  C  C   . MET A 1 1053 ? -47.518  33.015  -5.044  1.00 110.52 ? 1053 MET A C   1 
ATOM   7990  O  O   . MET A 1 1053 ? -46.599  33.717  -5.462  1.00 110.43 ? 1053 MET A O   1 
ATOM   7991  C  CB  . MET A 1 1053 ? -49.207  32.156  -6.663  1.00 113.99 ? 1053 MET A CB  1 
ATOM   7992  C  CG  . MET A 1 1053 ? -48.859  32.757  -8.010  1.00 113.85 ? 1053 MET A CG  1 
ATOM   7993  S  SD  . MET A 1 1053 ? -47.550  31.750  -8.759  1.00 222.22 ? 1053 MET A SD  1 
ATOM   7994  C  CE  . MET A 1 1053 ? -46.842  32.875  -9.953  1.00 51.12  ? 1053 MET A CE  1 
ATOM   7995  N  N   . LEU A 1 1054 ? -48.185  33.257  -3.914  1.00 110.29 ? 1054 LEU A N   1 
ATOM   7996  C  CA  . LEU A 1 1054 ? -47.859  34.377  -3.039  1.00 111.87 ? 1054 LEU A CA  1 
ATOM   7997  C  C   . LEU A 1 1054 ? -46.452  34.210  -2.469  1.00 109.06 ? 1054 LEU A C   1 
ATOM   7998  O  O   . LEU A 1 1054 ? -45.688  35.170  -2.363  1.00 108.44 ? 1054 LEU A O   1 
ATOM   7999  C  CB  . LEU A 1 1054 ? -48.888  34.481  -1.908  1.00 117.59 ? 1054 LEU A CB  1 
ATOM   8000  C  CG  . LEU A 1 1054 ? -50.378  34.628  -2.266  1.00 122.08 ? 1054 LEU A CG  1 
ATOM   8001  C  CD1 . LEU A 1 1054 ? -51.279  34.608  -1.012  1.00 124.56 ? 1054 LEU A CD1 1 
ATOM   8002  C  CD2 . LEU A 1 1054 ? -50.635  35.886  -3.104  1.00 124.14 ? 1054 LEU A CD2 1 
ATOM   8003  N  N   . SER A 1 1055 ? -46.127  32.971  -2.115  1.00 105.95 ? 1055 SER A N   1 
ATOM   8004  C  CA  . SER A 1 1055 ? -44.814  32.602  -1.614  1.00 104.52 ? 1055 SER A CA  1 
ATOM   8005  C  C   . SER A 1 1055 ? -43.741  33.477  -2.220  1.00 98.41  ? 1055 SER A C   1 
ATOM   8006  O  O   . SER A 1 1055 ? -42.798  33.851  -1.554  1.00 100.43 ? 1055 SER A O   1 
ATOM   8007  C  CB  . SER A 1 1055 ? -44.539  31.128  -1.950  1.00 109.34 ? 1055 SER A CB  1 
ATOM   8008  O  OG  . SER A 1 1055 ? -43.188  30.737  -1.765  1.00 112.24 ? 1055 SER A OG  1 
ATOM   8009  N  N   . ILE A 1 1056 ? -43.869  33.808  -3.488  1.00 93.36  ? 1056 ILE A N   1 
ATOM   8010  C  CA  . ILE A 1 1056 ? -42.782  34.525  -4.150  1.00 92.71  ? 1056 ILE A CA  1 
ATOM   8011  C  C   . ILE A 1 1056 ? -42.762  36.041  -3.841  1.00 91.32  ? 1056 ILE A C   1 
ATOM   8012  O  O   . ILE A 1 1056 ? -41.710  36.672  -3.781  1.00 91.11  ? 1056 ILE A O   1 
ATOM   8013  C  CB  . ILE A 1 1056 ? -42.629  34.088  -5.689  1.00 80.40  ? 1056 ILE A CB  1 
ATOM   8014  C  CG1 . ILE A 1 1056 ? -42.359  35.274  -6.654  1.00 76.87  ? 1056 ILE A CG1 1 
ATOM   8015  C  CG2 . ILE A 1 1056 ? -43.814  33.217  -6.119  1.00 77.42  ? 1056 ILE A CG2 1 
ATOM   8016  C  CD1 . ILE A 1 1056 ? -43.587  36.066  -7.061  1.00 76.04  ? 1056 ILE A CD1 1 
ATOM   8017  N  N   . MET A 1 1057 ? -43.927  36.593  -3.560  1.00 93.44  ? 1057 MET A N   1 
ATOM   8018  C  CA  . MET A 1 1057 ? -44.092  38.049  -3.439  1.00 100.43 ? 1057 MET A CA  1 
ATOM   8019  C  C   . MET A 1 1057 ? -42.972  38.854  -2.720  1.00 104.84 ? 1057 MET A C   1 
ATOM   8020  O  O   . MET A 1 1057 ? -42.707  40.023  -3.073  1.00 104.91 ? 1057 MET A O   1 
ATOM   8021  C  CB  . MET A 1 1057 ? -45.440  38.365  -2.769  1.00 107.00 ? 1057 MET A CB  1 
ATOM   8022  C  CG  . MET A 1 1057 ? -45.997  39.748  -3.121  1.00 110.67 ? 1057 MET A CG  1 
ATOM   8023  S  SD  . MET A 1 1057 ? -47.078  39.715  -4.554  1.00 143.19 ? 1057 MET A SD  1 
ATOM   8024  C  CE  . MET A 1 1057 ? -48.466  38.779  -3.906  1.00 173.66 ? 1057 MET A CE  1 
ATOM   8025  N  N   . SER A 1 1058 ? -42.361  38.245  -1.698  1.00 104.22 ? 1058 SER A N   1 
ATOM   8026  C  CA  . SER A 1 1058 ? -41.313  38.876  -0.904  1.00 102.26 ? 1058 SER A CA  1 
ATOM   8027  C  C   . SER A 1 1058 ? -40.180  39.330  -1.823  1.00 99.29  ? 1058 SER A C   1 
ATOM   8028  O  O   . SER A 1 1058 ? -39.513  40.352  -1.588  1.00 99.33  ? 1058 SER A O   1 
ATOM   8029  C  CB  . SER A 1 1058 ? -40.779  37.866  0.104   1.00 100.29 ? 1058 SER A CB  1 
ATOM   8030  O  OG  . SER A 1 1058 ? -41.732  36.851  0.357   1.00 98.14  ? 1058 SER A OG  1 
ATOM   8031  N  N   . TYR A 1 1059 ? -39.965  38.546  -2.870  1.00 96.34  ? 1059 TYR A N   1 
ATOM   8032  C  CA  . TYR A 1 1059 ? -38.955  38.854  -3.847  1.00 96.26  ? 1059 TYR A CA  1 
ATOM   8033  C  C   . TYR A 1 1059 ? -39.527  39.749  -4.953  1.00 101.94 ? 1059 TYR A C   1 
ATOM   8034  O  O   . TYR A 1 1059 ? -38.863  39.970  -5.967  1.00 104.00 ? 1059 TYR A O   1 
ATOM   8035  C  CB  . TYR A 1 1059 ? -38.361  37.565  -4.438  1.00 90.16  ? 1059 TYR A CB  1 
ATOM   8036  C  CG  . TYR A 1 1059 ? -37.896  36.550  -3.444  1.00 87.69  ? 1059 TYR A CG  1 
ATOM   8037  C  CD1 . TYR A 1 1059 ? -38.799  35.826  -2.684  1.00 89.05  ? 1059 TYR A CD1 1 
ATOM   8038  C  CD2 . TYR A 1 1059 ? -36.555  36.301  -3.277  1.00 90.04  ? 1059 TYR A CD2 1 
ATOM   8039  C  CE1 . TYR A 1 1059 ? -38.371  34.872  -1.748  1.00 92.98  ? 1059 TYR A CE1 1 
ATOM   8040  C  CE2 . TYR A 1 1059 ? -36.093  35.353  -2.345  1.00 95.08  ? 1059 TYR A CE2 1 
ATOM   8041  C  CZ  . TYR A 1 1059 ? -37.004  34.634  -1.575  1.00 96.28  ? 1059 TYR A CZ  1 
ATOM   8042  O  OH  . TYR A 1 1059 ? -36.536  33.697  -0.651  1.00 97.38  ? 1059 TYR A OH  1 
ATOM   8043  N  N   . ARG A 1 1060 ? -40.752  40.246  -4.791  1.00 105.28 ? 1060 ARG A N   1 
ATOM   8044  C  CA  . ARG A 1 1060 ? -41.243  41.243  -5.747  1.00 109.22 ? 1060 ARG A CA  1 
ATOM   8045  C  C   . ARG A 1 1060 ? -40.834  42.607  -5.285  1.00 112.67 ? 1060 ARG A C   1 
ATOM   8046  O  O   . ARG A 1 1060 ? -41.184  43.016  -4.190  1.00 113.70 ? 1060 ARG A O   1 
ATOM   8047  C  CB  . ARG A 1 1060 ? -42.765  41.220  -5.935  1.00 111.77 ? 1060 ARG A CB  1 
ATOM   8048  C  CG  . ARG A 1 1060 ? -43.238  41.896  -7.249  1.00 106.27 ? 1060 ARG A CG  1 
ATOM   8049  C  CD  . ARG A 1 1060 ? -44.762  41.977  -7.367  1.00 108.03 ? 1060 ARG A CD  1 
ATOM   8050  N  NE  . ARG A 1 1060 ? -45.277  43.297  -6.976  1.00 113.76 ? 1060 ARG A NE  1 
ATOM   8051  C  CZ  . ARG A 1 1060 ? -46.566  43.579  -6.768  1.00 117.00 ? 1060 ARG A CZ  1 
ATOM   8052  N  NH1 . ARG A 1 1060 ? -47.485  42.635  -6.912  1.00 119.28 ? 1060 ARG A NH1 1 
ATOM   8053  N  NH2 . ARG A 1 1060 ? -46.950  44.800  -6.419  1.00 117.03 ? 1060 ARG A NH2 1 
ATOM   8054  N  N   . ASN A 1 1061 ? -40.093  43.316  -6.119  1.00 116.04 ? 1061 ASN A N   1 
ATOM   8055  C  CA  . ASN A 1 1061 ? -39.663  44.649  -5.745  1.00 123.15 ? 1061 ASN A CA  1 
ATOM   8056  C  C   . ASN A 1 1061 ? -40.780  45.688  -5.899  1.00 126.28 ? 1061 ASN A C   1 
ATOM   8057  O  O   . ASN A 1 1061 ? -41.918  45.342  -6.200  1.00 125.20 ? 1061 ASN A O   1 
ATOM   8058  C  CB  . ASN A 1 1061 ? -38.367  45.046  -6.466  1.00 127.97 ? 1061 ASN A CB  1 
ATOM   8059  C  CG  . ASN A 1 1061 ? -37.118  44.802  -5.606  1.00 133.86 ? 1061 ASN A CG  1 
ATOM   8060  O  OD1 . ASN A 1 1061 ? -37.039  43.816  -4.869  1.00 134.75 ? 1061 ASN A OD1 1 
ATOM   8061  N  ND2 . ASN A 1 1061 ? -36.145  45.714  -5.688  1.00 137.64 ? 1061 ASN A ND2 1 
ATOM   8062  N  N   . ALA A 1 1062 ? -40.453  46.952  -5.658  1.00 129.59 ? 1062 ALA A N   1 
ATOM   8063  C  CA  . ALA A 1 1062 ? -41.439  48.023  -5.636  1.00 131.85 ? 1062 ALA A CA  1 
ATOM   8064  C  C   . ALA A 1 1062 ? -41.897  48.394  -7.040  1.00 131.18 ? 1062 ALA A C   1 
ATOM   8065  O  O   . ALA A 1 1062 ? -43.048  48.768  -7.259  1.00 132.80 ? 1062 ALA A O   1 
ATOM   8066  C  CB  . ALA A 1 1062 ? -40.856  49.237  -4.936  1.00 135.03 ? 1062 ALA A CB  1 
ATOM   8067  N  N   . ASP A 1 1063 ? -40.973  48.296  -7.987  1.00 128.37 ? 1063 ASP A N   1 
ATOM   8068  C  CA  . ASP A 1 1063 ? -41.215  48.687  -9.375  1.00 126.66 ? 1063 ASP A CA  1 
ATOM   8069  C  C   . ASP A 1 1063 ? -41.906  47.574  -10.160 1.00 120.33 ? 1063 ASP A C   1 
ATOM   8070  O  O   . ASP A 1 1063 ? -42.172  47.708  -11.348 1.00 118.71 ? 1063 ASP A O   1 
ATOM   8071  C  CB  . ASP A 1 1063 ? -39.887  49.046  -10.038 1.00 129.49 ? 1063 ASP A CB  1 
ATOM   8072  C  CG  . ASP A 1 1063 ? -38.802  48.032  -9.729  1.00 131.20 ? 1063 ASP A CG  1 
ATOM   8073  O  OD1 . ASP A 1 1063 ? -39.148  46.949  -9.204  1.00 130.64 ? 1063 ASP A OD1 1 
ATOM   8074  O  OD2 . ASP A 1 1063 ? -37.614  48.314  -10.006 1.00 133.48 ? 1063 ASP A OD2 1 
ATOM   8075  N  N   . TYR A 1 1064 ? -42.198  46.481  -9.470  1.00 117.32 ? 1064 TYR A N   1 
ATOM   8076  C  CA  . TYR A 1 1064 ? -42.826  45.320  -10.070 1.00 113.47 ? 1064 TYR A CA  1 
ATOM   8077  C  C   . TYR A 1 1064 ? -41.769  44.388  -10.617 1.00 113.17 ? 1064 TYR A C   1 
ATOM   8078  O  O   . TYR A 1 1064 ? -42.062  43.277  -11.056 1.00 115.70 ? 1064 TYR A O   1 
ATOM   8079  C  CB  . TYR A 1 1064 ? -43.885  45.724  -11.103 1.00 110.83 ? 1064 TYR A CB  1 
ATOM   8080  C  CG  . TYR A 1 1064 ? -45.088  46.238  -10.391 1.00 111.35 ? 1064 TYR A CG  1 
ATOM   8081  C  CD1 . TYR A 1 1064 ? -45.929  45.365  -9.723  1.00 110.26 ? 1064 TYR A CD1 1 
ATOM   8082  C  CD2 . TYR A 1 1064 ? -45.343  47.594  -10.297 1.00 113.30 ? 1064 TYR A CD2 1 
ATOM   8083  C  CE1 . TYR A 1 1064 ? -47.019  45.823  -9.011  1.00 112.65 ? 1064 TYR A CE1 1 
ATOM   8084  C  CE2 . TYR A 1 1064 ? -46.432  48.062  -9.582  1.00 115.91 ? 1064 TYR A CE2 1 
ATOM   8085  C  CZ  . TYR A 1 1064 ? -47.269  47.171  -8.937  1.00 114.76 ? 1064 TYR A CZ  1 
ATOM   8086  O  OH  . TYR A 1 1064 ? -48.359  47.622  -8.212  1.00 116.06 ? 1064 TYR A OH  1 
ATOM   8087  N  N   . SER A 1 1065 ? -40.521  44.824  -10.551 1.00 110.21 ? 1065 SER A N   1 
ATOM   8088  C  CA  . SER A 1 1065 ? -39.435  43.941  -10.919 1.00 106.71 ? 1065 SER A CA  1 
ATOM   8089  C  C   . SER A 1 1065 ? -39.173  42.957  -9.793  1.00 103.99 ? 1065 SER A C   1 
ATOM   8090  O  O   . SER A 1 1065 ? -38.965  43.353  -8.650  1.00 104.88 ? 1065 SER A O   1 
ATOM   8091  C  CB  . SER A 1 1065 ? -38.178  44.737  -11.222 1.00 108.50 ? 1065 SER A CB  1 
ATOM   8092  O  OG  . SER A 1 1065 ? -37.517  45.086  -10.032 1.00 111.26 ? 1065 SER A OG  1 
ATOM   8093  N  N   . TYR A 1 1066 ? -39.196  41.670  -10.106 1.00 101.08 ? 1066 TYR A N   1 
ATOM   8094  C  CA  . TYR A 1 1066 ? -38.803  40.670  -9.123  1.00 100.93 ? 1066 TYR A CA  1 
ATOM   8095  C  C   . TYR A 1 1066 ? -37.294  40.604  -9.029  1.00 102.32 ? 1066 TYR A C   1 
ATOM   8096  O  O   . TYR A 1 1066 ? -36.576  41.114  -9.897  1.00 103.89 ? 1066 TYR A O   1 
ATOM   8097  C  CB  . TYR A 1 1066 ? -39.378  39.303  -9.465  1.00 97.32  ? 1066 TYR A CB  1 
ATOM   8098  C  CG  . TYR A 1 1066 ? -40.859  39.368  -9.607  1.00 97.25  ? 1066 TYR A CG  1 
ATOM   8099  C  CD1 . TYR A 1 1066 ? -41.433  40.189  -10.569 1.00 97.75  ? 1066 TYR A CD1 1 
ATOM   8100  C  CD2 . TYR A 1 1066 ? -41.693  38.632  -8.771  1.00 97.51  ? 1066 TYR A CD2 1 
ATOM   8101  C  CE1 . TYR A 1 1066 ? -42.798  40.275  -10.711 1.00 100.33 ? 1066 TYR A CE1 1 
ATOM   8102  C  CE2 . TYR A 1 1066 ? -43.073  38.714  -8.899  1.00 99.73  ? 1066 TYR A CE2 1 
ATOM   8103  C  CZ  . TYR A 1 1066 ? -43.622  39.541  -9.872  1.00 101.88 ? 1066 TYR A CZ  1 
ATOM   8104  O  OH  . TYR A 1 1066 ? -44.996  39.641  -10.010 1.00 104.43 ? 1066 TYR A OH  1 
ATOM   8105  N  N   . SER A 1 1067 ? -36.806  39.967  -7.979  1.00 100.79 ? 1067 SER A N   1 
ATOM   8106  C  CA  . SER A 1 1067 ? -35.383  39.974  -7.753  1.00 101.50 ? 1067 SER A CA  1 
ATOM   8107  C  C   . SER A 1 1067 ? -34.894  38.689  -7.091  1.00 102.00 ? 1067 SER A C   1 
ATOM   8108  O  O   . SER A 1 1067 ? -35.492  38.194  -6.136  1.00 101.84 ? 1067 SER A O   1 
ATOM   8109  C  CB  . SER A 1 1067 ? -35.013  41.198  -6.933  1.00 102.75 ? 1067 SER A CB  1 
ATOM   8110  O  OG  . SER A 1 1067 ? -33.866  41.807  -7.479  1.00 103.87 ? 1067 SER A OG  1 
ATOM   8111  N  N   . VAL A 1 1068 ? -33.796  38.160  -7.615  1.00 102.70 ? 1068 VAL A N   1 
ATOM   8112  C  CA  . VAL A 1 1068 ? -33.301  36.844  -7.256  1.00 103.56 ? 1068 VAL A CA  1 
ATOM   8113  C  C   . VAL A 1 1068 ? -33.378  36.486  -5.767  1.00 108.57 ? 1068 VAL A C   1 
ATOM   8114  O  O   . VAL A 1 1068 ? -34.053  35.524  -5.428  1.00 109.09 ? 1068 VAL A O   1 
ATOM   8115  C  CB  . VAL A 1 1068 ? -31.886  36.736  -7.631  1.00 103.47 ? 1068 VAL A CB  1 
ATOM   8116  C  CG1 . VAL A 1 1068 ? -31.144  37.921  -6.990  1.00 107.85 ? 1068 VAL A CG1 1 
ATOM   8117  C  CG2 . VAL A 1 1068 ? -31.373  35.407  -7.139  1.00 101.97 ? 1068 VAL A CG2 1 
ATOM   8118  N  N   . TRP A 1 1069 ? -32.655  37.199  -4.887  1.00 112.45 ? 1069 TRP A N   1 
ATOM   8119  C  CA  . TRP A 1 1069 ? -32.897  37.075  -3.427  1.00 114.32 ? 1069 TRP A CA  1 
ATOM   8120  C  C   . TRP A 1 1069 ? -33.459  38.371  -2.811  1.00 116.23 ? 1069 TRP A C   1 
ATOM   8121  O  O   . TRP A 1 1069 ? -33.478  39.409  -3.481  1.00 116.29 ? 1069 TRP A O   1 
ATOM   8122  C  CB  . TRP A 1 1069 ? -31.672  36.623  -2.603  1.00 114.41 ? 1069 TRP A CB  1 
ATOM   8123  C  CG  . TRP A 1 1069 ? -30.711  35.679  -3.241  1.00 110.99 ? 1069 TRP A CG  1 
ATOM   8124  C  CD1 . TRP A 1 1069 ? -30.661  34.306  -3.115  1.00 108.83 ? 1069 TRP A CD1 1 
ATOM   8125  C  CD2 . TRP A 1 1069 ? -29.623  36.047  -4.058  1.00 107.66 ? 1069 TRP A CD2 1 
ATOM   8126  N  NE1 . TRP A 1 1069 ? -29.604  33.802  -3.838  1.00 107.26 ? 1069 TRP A NE1 1 
ATOM   8127  C  CE2 . TRP A 1 1069 ? -28.953  34.851  -4.430  1.00 108.15 ? 1069 TRP A CE2 1 
ATOM   8128  C  CE3 . TRP A 1 1069 ? -29.153  37.270  -4.531  1.00 105.97 ? 1069 TRP A CE3 1 
ATOM   8129  C  CZ2 . TRP A 1 1069 ? -27.851  34.850  -5.255  1.00 109.94 ? 1069 TRP A CZ2 1 
ATOM   8130  C  CZ3 . TRP A 1 1069 ? -28.058  37.272  -5.337  1.00 108.72 ? 1069 TRP A CZ3 1 
ATOM   8131  C  CH2 . TRP A 1 1069 ? -27.412  36.067  -5.699  1.00 111.16 ? 1069 TRP A CH2 1 
ATOM   8132  N  N   . LYS A 1 1070 ? -33.880  38.309  -1.537  1.00 116.44 ? 1070 LYS A N   1 
ATOM   8133  C  CA  . LYS A 1 1070 ? -34.582  39.432  -0.900  1.00 115.41 ? 1070 LYS A CA  1 
ATOM   8134  C  C   . LYS A 1 1070 ? -33.775  40.705  -0.772  1.00 118.20 ? 1070 LYS A C   1 
ATOM   8135  O  O   . LYS A 1 1070 ? -32.720  40.738  -0.138  1.00 119.59 ? 1070 LYS A O   1 
ATOM   8136  C  CB  . LYS A 1 1070 ? -35.190  39.046  0.447   1.00 113.08 ? 1070 LYS A CB  1 
ATOM   8137  C  CG  . LYS A 1 1070 ? -36.652  38.693  0.316   1.00 110.51 ? 1070 LYS A CG  1 
ATOM   8138  C  CD  . LYS A 1 1070 ? -37.487  39.133  1.501   1.00 111.84 ? 1070 LYS A CD  1 
ATOM   8139  C  CE  . LYS A 1 1070 ? -37.472  38.119  2.638   1.00 111.92 ? 1070 LYS A CE  1 
ATOM   8140  N  NZ  . LYS A 1 1070 ? -38.254  38.525  3.861   1.00 113.48 ? 1070 LYS A NZ  1 
ATOM   8141  N  N   . GLY A 1 1071 ? -34.296  41.757  -1.385  1.00 120.63 ? 1071 GLY A N   1 
ATOM   8142  C  CA  . GLY A 1 1071 ? -33.689  43.065  -1.279  1.00 125.90 ? 1071 GLY A CA  1 
ATOM   8143  C  C   . GLY A 1 1071 ? -32.519  43.184  -2.216  1.00 128.98 ? 1071 GLY A C   1 
ATOM   8144  O  O   . GLY A 1 1071 ? -31.816  44.194  -2.228  1.00 134.59 ? 1071 GLY A O   1 
ATOM   8145  N  N   . GLY A 1 1072 ? -32.320  42.135  -3.003  1.00 125.72 ? 1072 GLY A N   1 
ATOM   8146  C  CA  . GLY A 1 1072 ? -31.279  42.102  -4.016  1.00 126.62 ? 1072 GLY A CA  1 
ATOM   8147  C  C   . GLY A 1 1072 ? -31.669  42.852  -5.272  1.00 127.12 ? 1072 GLY A C   1 
ATOM   8148  O  O   . GLY A 1 1072 ? -32.818  42.807  -5.709  1.00 126.27 ? 1072 GLY A O   1 
ATOM   8149  N  N   . SER A 1 1073 ? -30.702  43.552  -5.850  1.00 128.70 ? 1073 SER A N   1 
ATOM   8150  C  CA  . SER A 1 1073 ? -30.973  44.398  -6.998  1.00 128.08 ? 1073 SER A CA  1 
ATOM   8151  C  C   . SER A 1 1073 ? -31.775  43.613  -8.014  1.00 122.93 ? 1073 SER A C   1 
ATOM   8152  O  O   . SER A 1 1073 ? -31.597  42.396  -8.147  1.00 120.17 ? 1073 SER A O   1 
ATOM   8153  C  CB  . SER A 1 1073 ? -29.660  44.899  -7.581  1.00 130.36 ? 1073 SER A CB  1 
ATOM   8154  O  OG  . SER A 1 1073 ? -28.595  44.080  -7.122  1.00 131.55 ? 1073 SER A OG  1 
ATOM   8155  N  N   . ALA A 1 1074 ? -32.680  44.307  -8.696  1.00 123.16 ? 1074 ALA A N   1 
ATOM   8156  C  CA  . ALA A 1 1074 ? -33.608  43.666  -9.618  1.00 119.47 ? 1074 ALA A CA  1 
ATOM   8157  C  C   . ALA A 1 1074 ? -32.801  42.836  -10.560 1.00 116.51 ? 1074 ALA A C   1 
ATOM   8158  O  O   . ALA A 1 1074 ? -31.773  43.301  -11.055 1.00 118.44 ? 1074 ALA A O   1 
ATOM   8159  C  CB  . ALA A 1 1074 ? -34.380  44.688  -10.391 1.00 121.61 ? 1074 ALA A CB  1 
ATOM   8160  N  N   . SER A 1 1075 ? -33.236  41.599  -10.783 1.00 110.72 ? 1075 SER A N   1 
ATOM   8161  C  CA  . SER A 1 1075 ? -32.598  40.775  -11.799 1.00 108.34 ? 1075 SER A CA  1 
ATOM   8162  C  C   . SER A 1 1075 ? -33.554  40.686  -12.947 1.00 106.73 ? 1075 SER A C   1 
ATOM   8163  O  O   . SER A 1 1075 ? -34.723  40.317  -12.774 1.00 103.91 ? 1075 SER A O   1 
ATOM   8164  C  CB  . SER A 1 1075 ? -32.289  39.366  -11.319 1.00 108.39 ? 1075 SER A CB  1 
ATOM   8165  O  OG  . SER A 1 1075 ? -33.111  38.453  -12.018 1.00 107.67 ? 1075 SER A OG  1 
ATOM   8166  N  N   . THR A 1 1076 ? -33.031  41.033  -14.116 1.00 106.59 ? 1076 THR A N   1 
ATOM   8167  C  CA  . THR A 1 1076 ? -33.765  41.014  -15.356 1.00 102.42 ? 1076 THR A CA  1 
ATOM   8168  C  C   . THR A 1 1076 ? -34.181  39.592  -15.583 1.00 99.46  ? 1076 THR A C   1 
ATOM   8169  O  O   . THR A 1 1076 ? -35.235  39.327  -16.120 1.00 98.87  ? 1076 THR A O   1 
ATOM   8170  C  CB  . THR A 1 1076 ? -32.844  41.401  -16.486 1.00 100.56 ? 1076 THR A CB  1 
ATOM   8171  O  OG1 . THR A 1 1076 ? -33.424  42.464  -17.236 1.00 102.25 ? 1076 THR A OG1 1 
ATOM   8172  C  CG2 . THR A 1 1076 ? -32.607  40.215  -17.387 1.00 97.53  ? 1076 THR A CG2 1 
ATOM   8173  N  N   . TRP A 1 1077 ? -33.330  38.680  -15.128 1.00 99.78  ? 1077 TRP A N   1 
ATOM   8174  C  CA  . TRP A 1 1077 ? -33.509  37.241  -15.325 1.00 98.22  ? 1077 TRP A CA  1 
ATOM   8175  C  C   . TRP A 1 1077 ? -34.727  36.697  -14.584 1.00 92.92  ? 1077 TRP A C   1 
ATOM   8176  O  O   . TRP A 1 1077 ? -35.650  36.128  -15.176 1.00 88.39  ? 1077 TRP A O   1 
ATOM   8177  C  CB  . TRP A 1 1077 ? -32.244  36.487  -14.872 1.00 100.95 ? 1077 TRP A CB  1 
ATOM   8178  C  CG  . TRP A 1 1077 ? -32.237  35.046  -15.228 1.00 103.78 ? 1077 TRP A CG  1 
ATOM   8179  C  CD1 . TRP A 1 1077 ? -32.027  34.519  -16.465 1.00 105.99 ? 1077 TRP A CD1 1 
ATOM   8180  C  CD2 . TRP A 1 1077 ? -32.438  33.934  -14.345 1.00 105.59 ? 1077 TRP A CD2 1 
ATOM   8181  N  NE1 . TRP A 1 1077 ? -32.088  33.152  -16.413 1.00 107.01 ? 1077 TRP A NE1 1 
ATOM   8182  C  CE2 . TRP A 1 1077 ? -32.337  32.765  -15.120 1.00 106.51 ? 1077 TRP A CE2 1 
ATOM   8183  C  CE3 . TRP A 1 1077 ? -32.698  33.812  -12.979 1.00 106.54 ? 1077 TRP A CE3 1 
ATOM   8184  C  CZ2 . TRP A 1 1077 ? -32.484  31.484  -14.570 1.00 105.12 ? 1077 TRP A CZ2 1 
ATOM   8185  C  CZ3 . TRP A 1 1077 ? -32.840  32.535  -12.436 1.00 106.66 ? 1077 TRP A CZ3 1 
ATOM   8186  C  CH2 . TRP A 1 1077 ? -32.733  31.394  -13.231 1.00 104.83 ? 1077 TRP A CH2 1 
ATOM   8187  N  N   . LEU A 1 1078 ? -34.718  36.884  -13.274 1.00 92.57  ? 1078 LEU A N   1 
ATOM   8188  C  CA  . LEU A 1 1078 ? -35.753  36.310  -12.447 1.00 90.23  ? 1078 LEU A CA  1 
ATOM   8189  C  C   . LEU A 1 1078 ? -37.085  36.983  -12.742 1.00 92.06  ? 1078 LEU A C   1 
ATOM   8190  O  O   . LEU A 1 1078 ? -38.133  36.342  -12.711 1.00 92.93  ? 1078 LEU A O   1 
ATOM   8191  C  CB  . LEU A 1 1078 ? -35.377  36.349  -10.969 1.00 86.55  ? 1078 LEU A CB  1 
ATOM   8192  C  CG  . LEU A 1 1078 ? -36.177  35.356  -10.133 1.00 80.52  ? 1078 LEU A CG  1 
ATOM   8193  C  CD1 . LEU A 1 1078 ? -35.311  34.460  -9.264  1.00 77.57  ? 1078 LEU A CD1 1 
ATOM   8194  C  CD2 . LEU A 1 1078 ? -37.183  36.131  -9.315  1.00 80.61  ? 1078 LEU A CD2 1 
ATOM   8195  N  N   . THR A 1 1079 ? -37.047  38.263  -13.081 1.00 92.81  ? 1079 THR A N   1 
ATOM   8196  C  CA  . THR A 1 1079 ? -38.270  38.931  -13.531 1.00 93.43  ? 1079 THR A CA  1 
ATOM   8197  C  C   . THR A 1 1079 ? -38.912  38.161  -14.707 1.00 91.21  ? 1079 THR A C   1 
ATOM   8198  O  O   . THR A 1 1079 ? -40.116  37.896  -14.725 1.00 91.78  ? 1079 THR A O   1 
ATOM   8199  C  CB  . THR A 1 1079 ? -38.011  40.424  -13.885 1.00 105.02 ? 1079 THR A CB  1 
ATOM   8200  O  OG1 . THR A 1 1079 ? -37.522  41.104  -12.718 1.00 106.52 ? 1079 THR A OG1 1 
ATOM   8201  C  CG2 . THR A 1 1079 ? -39.286  41.097  -14.383 1.00 103.93 ? 1079 THR A CG2 1 
ATOM   8202  N  N   . ALA A 1 1080 ? -38.096  37.772  -15.676 1.00 89.62  ? 1080 ALA A N   1 
ATOM   8203  C  CA  . ALA A 1 1080 ? -38.626  37.031  -16.798 1.00 85.73  ? 1080 ALA A CA  1 
ATOM   8204  C  C   . ALA A 1 1080 ? -39.248  35.768  -16.233 1.00 83.02  ? 1080 ALA A C   1 
ATOM   8205  O  O   . ALA A 1 1080 ? -40.460  35.558  -16.357 1.00 81.47  ? 1080 ALA A O   1 
ATOM   8206  C  CB  . ALA A 1 1080 ? -37.529  36.706  -17.798 1.00 85.88  ? 1080 ALA A CB  1 
ATOM   8207  N  N   . PHE A 1 1081 ? -38.410  34.967  -15.577 1.00 80.18  ? 1081 PHE A N   1 
ATOM   8208  C  CA  . PHE A 1 1081 ? -38.777  33.633  -15.117 1.00 77.44  ? 1081 PHE A CA  1 
ATOM   8209  C  C   . PHE A 1 1081 ? -40.001  33.690  -14.231 1.00 74.01  ? 1081 PHE A C   1 
ATOM   8210  O  O   . PHE A 1 1081 ? -40.793  32.754  -14.157 1.00 70.08  ? 1081 PHE A O   1 
ATOM   8211  C  CB  . PHE A 1 1081 ? -37.604  33.004  -14.366 1.00 80.22  ? 1081 PHE A CB  1 
ATOM   8212  C  CG  . PHE A 1 1081 ? -37.860  31.603  -13.891 1.00 82.55  ? 1081 PHE A CG  1 
ATOM   8213  C  CD1 . PHE A 1 1081 ? -37.669  30.525  -14.723 1.00 82.72  ? 1081 PHE A CD1 1 
ATOM   8214  C  CD2 . PHE A 1 1081 ? -38.285  31.363  -12.605 1.00 86.48  ? 1081 PHE A CD2 1 
ATOM   8215  C  CE1 . PHE A 1 1081 ? -37.912  29.233  -14.281 1.00 83.31  ? 1081 PHE A CE1 1 
ATOM   8216  C  CE2 . PHE A 1 1081 ? -38.525  30.078  -12.162 1.00 87.28  ? 1081 PHE A CE2 1 
ATOM   8217  C  CZ  . PHE A 1 1081 ? -38.339  29.014  -13.005 1.00 85.51  ? 1081 PHE A CZ  1 
ATOM   8218  N  N   . ALA A 1 1082 ? -40.158  34.809  -13.549 1.00 75.65  ? 1082 ALA A N   1 
ATOM   8219  C  CA  . ALA A 1 1082 ? -41.326  34.998  -12.709 1.00 76.85  ? 1082 ALA A CA  1 
ATOM   8220  C  C   . ALA A 1 1082 ? -42.542  35.182  -13.598 1.00 76.09  ? 1082 ALA A C   1 
ATOM   8221  O  O   . ALA A 1 1082 ? -43.504  34.430  -13.485 1.00 75.95  ? 1082 ALA A O   1 
ATOM   8222  C  CB  . ALA A 1 1082 ? -41.142  36.188  -11.827 1.00 79.54  ? 1082 ALA A CB  1 
ATOM   8223  N  N   . LEU A 1 1083 ? -42.483  36.165  -14.492 1.00 74.74  ? 1083 LEU A N   1 
ATOM   8224  C  CA  . LEU A 1 1083 ? -43.427  36.247  -15.591 1.00 72.24  ? 1083 LEU A CA  1 
ATOM   8225  C  C   . LEU A 1 1083 ? -43.751  34.899  -16.233 1.00 72.70  ? 1083 LEU A C   1 
ATOM   8226  O  O   . LEU A 1 1083 ? -44.910  34.488  -16.228 1.00 74.77  ? 1083 LEU A O   1 
ATOM   8227  C  CB  . LEU A 1 1083 ? -42.851  37.150  -16.636 1.00 69.03  ? 1083 LEU A CB  1 
ATOM   8228  C  CG  . LEU A 1 1083 ? -43.044  38.568  -16.150 1.00 67.76  ? 1083 LEU A CG  1 
ATOM   8229  C  CD1 . LEU A 1 1083 ? -42.107  39.456  -16.926 1.00 68.77  ? 1083 LEU A CD1 1 
ATOM   8230  C  CD2 . LEU A 1 1083 ? -44.510  39.009  -16.283 1.00 65.76  ? 1083 LEU A CD2 1 
ATOM   8231  N  N   . ARG A 1 1084 ? -42.750  34.228  -16.802 1.00 69.73  ? 1084 ARG A N   1 
ATOM   8232  C  CA  . ARG A 1 1084 ? -42.941  32.857  -17.299 1.00 70.86  ? 1084 ARG A CA  1 
ATOM   8233  C  C   . ARG A 1 1084 ? -43.831  31.997  -16.390 1.00 73.27  ? 1084 ARG A C   1 
ATOM   8234  O  O   . ARG A 1 1084 ? -44.825  31.444  -16.857 1.00 73.98  ? 1084 ARG A O   1 
ATOM   8235  C  CB  . ARG A 1 1084 ? -41.596  32.134  -17.532 1.00 72.20  ? 1084 ARG A CB  1 
ATOM   8236  C  CG  . ARG A 1 1084 ? -41.610  30.597  -17.280 1.00 68.46  ? 1084 ARG A CG  1 
ATOM   8237  C  CD  . ARG A 1 1084 ? -41.465  29.842  -18.545 1.00 69.78  ? 1084 ARG A CD  1 
ATOM   8238  N  NE  . ARG A 1 1084 ? -41.718  28.409  -18.448 1.00 74.30  ? 1084 ARG A NE  1 
ATOM   8239  C  CZ  . ARG A 1 1084 ? -40.795  27.485  -18.707 1.00 80.71  ? 1084 ARG A CZ  1 
ATOM   8240  N  NH1 . ARG A 1 1084 ? -39.559  27.873  -19.023 1.00 84.79  ? 1084 ARG A NH1 1 
ATOM   8241  N  NH2 . ARG A 1 1084 ? -41.084  26.180  -18.655 1.00 80.70  ? 1084 ARG A NH2 1 
ATOM   8242  N  N   . VAL A 1 1085 ? -43.490  31.870  -15.105 1.00 76.19  ? 1085 VAL A N   1 
ATOM   8243  C  CA  . VAL A 1 1085 ? -44.266  30.970  -14.234 1.00 79.12  ? 1085 VAL A CA  1 
ATOM   8244  C  C   . VAL A 1 1085 ? -45.627  31.548  -13.836 1.00 79.42  ? 1085 VAL A C   1 
ATOM   8245  O  O   . VAL A 1 1085 ? -46.566  30.823  -13.523 1.00 78.16  ? 1085 VAL A O   1 
ATOM   8246  C  CB  . VAL A 1 1085 ? -43.480  30.482  -12.978 1.00 69.33  ? 1085 VAL A CB  1 
ATOM   8247  C  CG1 . VAL A 1 1085 ? -44.330  29.465  -12.180 1.00 68.33  ? 1085 VAL A CG1 1 
ATOM   8248  C  CG2 . VAL A 1 1085 ? -42.115  29.883  -13.369 1.00 66.68  ? 1085 VAL A CG2 1 
ATOM   8249  N  N   . LEU A 1 1086 ? -45.711  32.869  -13.862 1.00 82.87  ? 1086 LEU A N   1 
ATOM   8250  C  CA  . LEU A 1 1086 ? -46.948  33.581  -13.576 1.00 87.71  ? 1086 LEU A CA  1 
ATOM   8251  C  C   . LEU A 1 1086 ? -47.903  33.409  -14.741 1.00 87.73  ? 1086 LEU A C   1 
ATOM   8252  O  O   . LEU A 1 1086 ? -49.091  33.111  -14.548 1.00 89.38  ? 1086 LEU A O   1 
ATOM   8253  C  CB  . LEU A 1 1086 ? -46.685  35.094  -13.377 1.00 91.76  ? 1086 LEU A CB  1 
ATOM   8254  C  CG  . LEU A 1 1086 ? -46.466  35.788  -12.008 1.00 99.41  ? 1086 LEU A CG  1 
ATOM   8255  C  CD1 . LEU A 1 1086 ? -47.732  35.806  -11.148 1.00 98.54  ? 1086 LEU A CD1 1 
ATOM   8256  C  CD2 . LEU A 1 1086 ? -45.290  35.200  -11.251 1.00 99.97  ? 1086 LEU A CD2 1 
ATOM   8257  N  N   . GLY A 1 1087 ? -47.377  33.623  -15.948 1.00 85.23  ? 1087 GLY A N   1 
ATOM   8258  C  CA  . GLY A 1 1087 ? -48.159  33.514  -17.163 1.00 83.42  ? 1087 GLY A CA  1 
ATOM   8259  C  C   . GLY A 1 1087 ? -48.757  32.133  -17.173 1.00 80.38  ? 1087 GLY A C   1 
ATOM   8260  O  O   . GLY A 1 1087 ? -49.977  31.964  -17.252 1.00 82.57  ? 1087 GLY A O   1 
ATOM   8261  N  N   . GLN A 1 1088 ? -47.885  31.144  -17.051 1.00 76.45  ? 1088 GLN A N   1 
ATOM   8262  C  CA  . GLN A 1 1088 ? -48.311  29.773  -16.896 1.00 77.63  ? 1088 GLN A CA  1 
ATOM   8263  C  C   . GLN A 1 1088 ? -49.497  29.563  -15.933 1.00 82.99  ? 1088 GLN A C   1 
ATOM   8264  O  O   . GLN A 1 1088 ? -50.502  28.953  -16.299 1.00 83.73  ? 1088 GLN A O   1 
ATOM   8265  C  CB  . GLN A 1 1088 ? -47.121  28.949  -16.454 1.00 76.13  ? 1088 GLN A CB  1 
ATOM   8266  C  CG  . GLN A 1 1088 ? -45.970  29.138  -17.387 1.00 77.39  ? 1088 GLN A CG  1 
ATOM   8267  C  CD  . GLN A 1 1088 ? -44.872  28.090  -17.233 1.00 77.79  ? 1088 GLN A CD  1 
ATOM   8268  O  OE1 . GLN A 1 1088 ? -43.676  28.414  -17.290 1.00 76.43  ? 1088 GLN A OE1 1 
ATOM   8269  N  NE2 . GLN A 1 1088 ? -45.268  26.829  -17.048 1.00 77.58  ? 1088 GLN A NE2 1 
ATOM   8270  N  N   . VAL A 1 1089 ? -49.388  30.065  -14.704 1.00 88.52  ? 1089 VAL A N   1 
ATOM   8271  C  CA  . VAL A 1 1089 ? -50.389  29.764  -13.668 1.00 89.70  ? 1089 VAL A CA  1 
ATOM   8272  C  C   . VAL A 1 1089 ? -51.628  30.661  -13.789 1.00 92.84  ? 1089 VAL A C   1 
ATOM   8273  O  O   . VAL A 1 1089 ? -52.657  30.427  -13.170 1.00 92.04  ? 1089 VAL A O   1 
ATOM   8274  C  CB  . VAL A 1 1089 ? -49.770  29.809  -12.245 1.00 82.29  ? 1089 VAL A CB  1 
ATOM   8275  C  CG1 . VAL A 1 1089 ? -50.662  29.107  -11.262 1.00 81.00  ? 1089 VAL A CG1 1 
ATOM   8276  C  CG2 . VAL A 1 1089 ? -48.412  29.112  -12.246 1.00 81.95  ? 1089 VAL A CG2 1 
ATOM   8277  N  N   . ASN A 1 1090 ? -51.536  31.673  -14.627 1.00 96.09  ? 1090 ASN A N   1 
ATOM   8278  C  CA  . ASN A 1 1090 ? -52.683  32.505  -14.878 1.00 101.86 ? 1090 ASN A CA  1 
ATOM   8279  C  C   . ASN A 1 1090 ? -53.833  31.758  -15.539 1.00 104.31 ? 1090 ASN A C   1 
ATOM   8280  O  O   . ASN A 1 1090 ? -54.989  32.131  -15.386 1.00 105.53 ? 1090 ASN A O   1 
ATOM   8281  C  CB  . ASN A 1 1090 ? -52.284  33.681  -15.739 1.00 104.47 ? 1090 ASN A CB  1 
ATOM   8282  C  CG  . ASN A 1 1090 ? -53.374  34.711  -15.820 1.00 108.09 ? 1090 ASN A CG  1 
ATOM   8283  O  OD1 . ASN A 1 1090 ? -54.548  34.434  -15.547 1.00 107.92 ? 1090 ASN A OD1 1 
ATOM   8284  N  ND2 . ASN A 1 1090 ? -52.997  35.918  -16.183 1.00 111.43 ? 1090 ASN A ND2 1 
ATOM   8285  N  N   . LYS A 1 1091 ? -53.517  30.721  -16.301 1.00 106.29 ? 1091 LYS A N   1 
ATOM   8286  C  CA  . LYS A 1 1091 ? -54.561  29.928  -16.933 1.00 109.02 ? 1091 LYS A CA  1 
ATOM   8287  C  C   . LYS A 1 1091 ? -55.572  29.582  -15.879 1.00 105.90 ? 1091 LYS A C   1 
ATOM   8288  O  O   . LYS A 1 1091 ? -56.756  29.775  -16.079 1.00 107.82 ? 1091 LYS A O   1 
ATOM   8289  C  CB  . LYS A 1 1091 ? -54.020  28.607  -17.482 1.00 116.28 ? 1091 LYS A CB  1 
ATOM   8290  C  CG  . LYS A 1 1091 ? -53.526  28.619  -18.917 1.00 123.44 ? 1091 LYS A CG  1 
ATOM   8291  C  CD  . LYS A 1 1091 ? -53.874  27.289  -19.576 1.00 129.11 ? 1091 LYS A CD  1 
ATOM   8292  C  CE  . LYS A 1 1091 ? -55.373  27.004  -19.406 1.00 135.21 ? 1091 LYS A CE  1 
ATOM   8293  N  NZ  . LYS A 1 1091 ? -55.996  26.273  -20.563 1.00 137.31 ? 1091 LYS A NZ  1 
ATOM   8294  N  N   . TYR A 1 1092 ? -55.091  29.065  -14.753 1.00 101.28 ? 1092 TYR A N   1 
ATOM   8295  C  CA  . TYR A 1 1092 ? -55.970  28.500  -13.742 1.00 100.95 ? 1092 TYR A CA  1 
ATOM   8296  C  C   . TYR A 1 1092 ? -56.154  29.347  -12.490 1.00 107.41 ? 1092 TYR A C   1 
ATOM   8297  O  O   . TYR A 1 1092 ? -57.086  29.123  -11.708 1.00 110.76 ? 1092 TYR A O   1 
ATOM   8298  C  CB  . TYR A 1 1092 ? -55.475  27.133  -13.354 1.00 95.85  ? 1092 TYR A CB  1 
ATOM   8299  C  CG  . TYR A 1 1092 ? -55.201  26.296  -14.541 1.00 93.31  ? 1092 TYR A CG  1 
ATOM   8300  C  CD1 . TYR A 1 1092 ? -56.197  26.019  -15.444 1.00 93.96  ? 1092 TYR A CD1 1 
ATOM   8301  C  CD2 . TYR A 1 1092 ? -53.940  25.782  -14.772 1.00 93.08  ? 1092 TYR A CD2 1 
ATOM   8302  C  CE1 . TYR A 1 1092 ? -55.950  25.238  -16.544 1.00 94.54  ? 1092 TYR A CE1 1 
ATOM   8303  C  CE2 . TYR A 1 1092 ? -53.677  25.001  -15.877 1.00 93.01  ? 1092 TYR A CE2 1 
ATOM   8304  C  CZ  . TYR A 1 1092 ? -54.689  24.729  -16.760 1.00 93.71  ? 1092 TYR A CZ  1 
ATOM   8305  O  OH  . TYR A 1 1092 ? -54.446  23.943  -17.863 1.00 93.05  ? 1092 TYR A OH  1 
ATOM   8306  N  N   . VAL A 1 1093 ? -55.268  30.313  -12.282 1.00 107.87 ? 1093 VAL A N   1 
ATOM   8307  C  CA  . VAL A 1 1093 ? -55.445  31.255  -11.181 1.00 108.15 ? 1093 VAL A CA  1 
ATOM   8308  C  C   . VAL A 1 1093 ? -55.114  32.680  -11.655 1.00 105.90 ? 1093 VAL A C   1 
ATOM   8309  O  O   . VAL A 1 1093 ? -53.940  33.011  -11.861 1.00 104.31 ? 1093 VAL A O   1 
ATOM   8310  C  CB  . VAL A 1 1093 ? -54.596  30.858  -9.967  1.00 108.59 ? 1093 VAL A CB  1 
ATOM   8311  C  CG1 . VAL A 1 1093 ? -54.819  31.848  -8.843  1.00 111.83 ? 1093 VAL A CG1 1 
ATOM   8312  C  CG2 . VAL A 1 1093 ? -54.919  29.425  -9.517  1.00 107.32 ? 1093 VAL A CG2 1 
ATOM   8313  N  N   . GLU A 1 1094 ? -56.152  33.504  -11.843 1.00 105.24 ? 1094 GLU A N   1 
ATOM   8314  C  CA  . GLU A 1 1094 ? -55.992  34.811  -12.485 1.00 104.60 ? 1094 GLU A CA  1 
ATOM   8315  C  C   . GLU A 1 1094 ? -54.954  35.577  -11.705 1.00 102.88 ? 1094 GLU A C   1 
ATOM   8316  O  O   . GLU A 1 1094 ? -55.007  35.586  -10.485 1.00 106.48 ? 1094 GLU A O   1 
ATOM   8317  C  CB  . GLU A 1 1094 ? -57.320  35.560  -12.488 1.00 109.53 ? 1094 GLU A CB  1 
ATOM   8318  C  CG  . GLU A 1 1094 ? -57.330  36.846  -13.303 1.00 115.05 ? 1094 GLU A CG  1 
ATOM   8319  C  CD  . GLU A 1 1094 ? -58.677  37.587  -13.229 1.00 122.53 ? 1094 GLU A CD  1 
ATOM   8320  O  OE1 . GLU A 1 1094 ? -59.577  37.127  -12.492 1.00 125.37 ? 1094 GLU A OE1 1 
ATOM   8321  O  OE2 . GLU A 1 1094 ? -58.838  38.633  -13.903 1.00 125.15 ? 1094 GLU A OE2 1 
ATOM   8322  N  N   . GLN A 1 1095 ? -53.968  36.170  -12.361 1.00 99.00  ? 1095 GLN A N   1 
ATOM   8323  C  CA  . GLN A 1 1095 ? -53.000  36.938  -11.591 1.00 99.82  ? 1095 GLN A CA  1 
ATOM   8324  C  C   . GLN A 1 1095 ? -53.290  38.383  -11.865 1.00 106.68 ? 1095 GLN A C   1 
ATOM   8325  O  O   . GLN A 1 1095 ? -53.944  38.681  -12.849 1.00 108.71 ? 1095 GLN A O   1 
ATOM   8326  C  CB  . GLN A 1 1095 ? -51.566  36.545  -11.910 1.00 97.05  ? 1095 GLN A CB  1 
ATOM   8327  C  CG  . GLN A 1 1095 ? -51.322  35.018  -11.781 1.00 100.38 ? 1095 GLN A CG  1 
ATOM   8328  C  CD  . GLN A 1 1095 ? -51.334  34.470  -10.323 1.00 129.56 ? 1095 GLN A CD  1 
ATOM   8329  O  OE1 . GLN A 1 1095 ? -50.446  34.768  -9.528  1.00 129.78 ? 1095 GLN A OE1 1 
ATOM   8330  N  NE2 . GLN A 1 1095 ? -52.319  33.631  -9.999  1.00 129.16 ? 1095 GLN A NE2 1 
ATOM   8331  N  N   . ASN A 1 1096 ? -52.867  39.267  -10.967 1.00 111.21 ? 1096 ASN A N   1 
ATOM   8332  C  CA  . ASN A 1 1096 ? -53.213  40.691  -11.014 1.00 117.08 ? 1096 ASN A CA  1 
ATOM   8333  C  C   . ASN A 1 1096 ? -52.758  41.317  -12.322 1.00 118.26 ? 1096 ASN A C   1 
ATOM   8334  O  O   . ASN A 1 1096 ? -51.580  41.266  -12.645 1.00 117.10 ? 1096 ASN A O   1 
ATOM   8335  C  CB  . ASN A 1 1096 ? -52.544  41.376  -9.813  1.00 121.74 ? 1096 ASN A CB  1 
ATOM   8336  C  CG  . ASN A 1 1096 ? -52.567  42.895  -9.889  1.00 128.01 ? 1096 ASN A CG  1 
ATOM   8337  O  OD1 . ASN A 1 1096 ? -53.132  43.573  -9.025  1.00 132.51 ? 1096 ASN A OD1 1 
ATOM   8338  N  ND2 . ASN A 1 1096 ? -51.918  43.435  -10.895 1.00 128.22 ? 1096 ASN A ND2 1 
ATOM   8339  N  N   . GLN A 1 1097 ? -53.657  41.908  -13.094 1.00 121.53 ? 1097 GLN A N   1 
ATOM   8340  C  CA  . GLN A 1 1097 ? -53.209  42.375  -14.401 1.00 123.64 ? 1097 GLN A CA  1 
ATOM   8341  C  C   . GLN A 1 1097 ? -52.164  43.478  -14.275 1.00 126.49 ? 1097 GLN A C   1 
ATOM   8342  O  O   . GLN A 1 1097 ? -51.019  43.314  -14.687 1.00 124.44 ? 1097 GLN A O   1 
ATOM   8343  C  CB  . GLN A 1 1097 ? -54.372  42.818  -15.279 1.00 123.52 ? 1097 GLN A CB  1 
ATOM   8344  C  CG  . GLN A 1 1097 ? -53.965  42.998  -16.732 1.00 122.05 ? 1097 GLN A CG  1 
ATOM   8345  C  CD  . GLN A 1 1097 ? -55.037  43.675  -17.577 1.00 124.34 ? 1097 GLN A CD  1 
ATOM   8346  O  OE1 . GLN A 1 1097 ? -56.159  43.936  -17.116 1.00 125.17 ? 1097 GLN A OE1 1 
ATOM   8347  N  NE2 . GLN A 1 1097 ? -54.693  43.964  -18.829 1.00 124.26 ? 1097 GLN A NE2 1 
ATOM   8348  N  N   . ASN A 1 1098 ? -52.573  44.592  -13.676 1.00 134.95 ? 1098 ASN A N   1 
ATOM   8349  C  CA  . ASN A 1 1098 ? -51.701  45.752  -13.437 1.00 138.46 ? 1098 ASN A CA  1 
ATOM   8350  C  C   . ASN A 1 1098 ? -50.254  45.419  -12.975 1.00 122.75 ? 1098 ASN A C   1 
ATOM   8351  O  O   . ASN A 1 1098 ? -49.287  45.959  -13.520 1.00 120.91 ? 1098 ASN A O   1 
ATOM   8352  C  CB  . ASN A 1 1098 ? -52.403  46.723  -12.467 1.00 143.96 ? 1098 ASN A CB  1 
ATOM   8353  C  CG  . ASN A 1 1098 ? -51.534  47.901  -12.080 1.00 149.22 ? 1098 ASN A CG  1 
ATOM   8354  O  OD1 . ASN A 1 1098 ? -51.042  47.977  -10.956 1.00 151.35 ? 1098 ASN A OD1 1 
ATOM   8355  N  ND2 . ASN A 1 1098 ? -51.336  48.824  -13.009 1.00 152.04 ? 1098 ASN A ND2 1 
ATOM   8356  N  N   . SER A 1 1099 ? -50.107  44.541  -11.981 1.00 121.63 ? 1099 SER A N   1 
ATOM   8357  C  CA  . SER A 1 1099 ? -48.795  44.011  -11.616 1.00 117.37 ? 1099 SER A CA  1 
ATOM   8358  C  C   . SER A 1 1099 ? -48.116  43.493  -12.872 1.00 112.44 ? 1099 SER A C   1 
ATOM   8359  O  O   . SER A 1 1099 ? -47.137  44.065  -13.328 1.00 113.93 ? 1099 SER A O   1 
ATOM   8360  C  CB  . SER A 1 1099 ? -48.910  42.884  -10.575 1.00 114.71 ? 1099 SER A CB  1 
ATOM   8361  O  OG  . SER A 1 1099 ? -47.741  42.070  -10.554 1.00 111.66 ? 1099 SER A OG  1 
ATOM   8362  N  N   . ILE A 1 1100 ? -48.672  42.434  -13.453 1.00 105.48 ? 1100 ILE A N   1 
ATOM   8363  C  CA  . ILE A 1 1100 ? -48.028  41.748  -14.569 1.00 98.75  ? 1100 ILE A CA  1 
ATOM   8364  C  C   . ILE A 1 1100 ? -47.660  42.703  -15.710 1.00 101.05 ? 1100 ILE A C   1 
ATOM   8365  O  O   . ILE A 1 1100 ? -46.680  42.471  -16.432 1.00 100.24 ? 1100 ILE A O   1 
ATOM   8366  C  CB  . ILE A 1 1100 ? -48.882  40.603  -15.127 1.00 90.24  ? 1100 ILE A CB  1 
ATOM   8367  C  CG1 . ILE A 1 1100 ? -48.834  39.400  -14.215 1.00 84.30  ? 1100 ILE A CG1 1 
ATOM   8368  C  CG2 . ILE A 1 1100 ? -48.330  40.161  -16.438 1.00 88.30  ? 1100 ILE A CG2 1 
ATOM   8369  C  CD1 . ILE A 1 1100 ? -47.554  38.668  -14.328 1.00 81.65  ? 1100 ILE A CD1 1 
ATOM   8370  N  N   . CYS A 1 1101 ? -48.447  43.765  -15.880 1.00 103.03 ? 1101 CYS A N   1 
ATOM   8371  C  CA  . CYS A 1 1101 ? -48.163  44.749  -16.919 1.00 104.15 ? 1101 CYS A CA  1 
ATOM   8372  C  C   . CYS A 1 1101 ? -46.820  45.400  -16.628 1.00 103.30 ? 1101 CYS A C   1 
ATOM   8373  O  O   . CYS A 1 1101 ? -45.892  45.322  -17.436 1.00 101.90 ? 1101 CYS A O   1 
ATOM   8374  C  CB  . CYS A 1 1101 ? -49.250  45.827  -16.979 1.00 107.21 ? 1101 CYS A CB  1 
ATOM   8375  S  SG  . CYS A 1 1101 ? -50.653  45.456  -18.061 1.00 132.59 ? 1101 CYS A SG  1 
ATOM   8376  N  N   . ASN A 1 1102 ? -46.725  46.023  -15.455 1.00 104.17 ? 1102 ASN A N   1 
ATOM   8377  C  CA  . ASN A 1 1102 ? -45.518  46.717  -15.015 1.00 103.84 ? 1102 ASN A CA  1 
ATOM   8378  C  C   . ASN A 1 1102 ? -44.308  45.819  -14.850 1.00 101.68 ? 1102 ASN A C   1 
ATOM   8379  O  O   . ASN A 1 1102 ? -43.184  46.251  -15.099 1.00 101.31 ? 1102 ASN A O   1 
ATOM   8380  C  CB  . ASN A 1 1102 ? -45.790  47.444  -13.708 1.00 104.59 ? 1102 ASN A CB  1 
ATOM   8381  C  CG  . ASN A 1 1102 ? -46.685  48.623  -13.900 1.00 106.12 ? 1102 ASN A CG  1 
ATOM   8382  O  OD1 . ASN A 1 1102 ? -46.636  49.275  -14.947 1.00 108.00 ? 1102 ASN A OD1 1 
ATOM   8383  N  ND2 . ASN A 1 1102 ? -47.516  48.914  -12.904 1.00 104.99 ? 1102 ASN A ND2 1 
ATOM   8384  N  N   . SER A 1 1103 ? -44.538  44.579  -14.418 1.00 101.11 ? 1103 SER A N   1 
ATOM   8385  C  CA  . SER A 1 1103 ? -43.459  43.594  -14.341 1.00 99.12  ? 1103 SER A CA  1 
ATOM   8386  C  C   . SER A 1 1103 ? -42.927  43.407  -15.753 1.00 99.53  ? 1103 SER A C   1 
ATOM   8387  O  O   . SER A 1 1103 ? -41.719  43.413  -15.950 1.00 98.64  ? 1103 SER A O   1 
ATOM   8388  C  CB  . SER A 1 1103 ? -43.926  42.243  -13.758 1.00 97.33  ? 1103 SER A CB  1 
ATOM   8389  O  OG  . SER A 1 1103 ? -44.528  42.353  -12.462 1.00 97.91  ? 1103 SER A OG  1 
ATOM   8390  N  N   . LEU A 1 1104 ? -43.844  43.264  -16.723 1.00 101.02 ? 1104 LEU A N   1 
ATOM   8391  C  CA  . LEU A 1 1104 ? -43.522  43.152  -18.158 1.00 101.31 ? 1104 LEU A CA  1 
ATOM   8392  C  C   . LEU A 1 1104 ? -42.885  44.430  -18.676 1.00 107.09 ? 1104 LEU A C   1 
ATOM   8393  O  O   . LEU A 1 1104 ? -41.794  44.398  -19.247 1.00 107.06 ? 1104 LEU A O   1 
ATOM   8394  C  CB  . LEU A 1 1104 ? -44.782  42.864  -18.986 1.00 98.47  ? 1104 LEU A CB  1 
ATOM   8395  C  CG  . LEU A 1 1104 ? -45.236  41.423  -19.232 1.00 94.88  ? 1104 LEU A CG  1 
ATOM   8396  C  CD1 . LEU A 1 1104 ? -46.575  41.393  -19.977 1.00 94.22  ? 1104 LEU A CD1 1 
ATOM   8397  C  CD2 . LEU A 1 1104 ? -44.175  40.671  -20.008 1.00 91.26  ? 1104 LEU A CD2 1 
ATOM   8398  N  N   . LEU A 1 1105 ? -43.589  45.546  -18.461 1.00 111.37 ? 1105 LEU A N   1 
ATOM   8399  C  CA  . LEU A 1 1105 ? -43.176  46.892  -18.884 1.00 114.88 ? 1105 LEU A CA  1 
ATOM   8400  C  C   . LEU A 1 1105 ? -41.845  47.314  -18.283 1.00 115.99 ? 1105 LEU A C   1 
ATOM   8401  O  O   . LEU A 1 1105 ? -41.290  48.346  -18.635 1.00 118.50 ? 1105 LEU A O   1 
ATOM   8402  C  CB  . LEU A 1 1105 ? -44.250  47.926  -18.516 1.00 116.69 ? 1105 LEU A CB  1 
ATOM   8403  C  CG  . LEU A 1 1105 ? -45.469  48.035  -19.437 1.00 118.21 ? 1105 LEU A CG  1 
ATOM   8404  C  CD1 . LEU A 1 1105 ? -46.758  48.308  -18.652 1.00 120.73 ? 1105 LEU A CD1 1 
ATOM   8405  C  CD2 . LEU A 1 1105 ? -45.254  49.073  -20.544 1.00 120.04 ? 1105 LEU A CD2 1 
ATOM   8406  N  N   . TRP A 1 1106 ? -41.340  46.515  -17.364 1.00 114.71 ? 1106 TRP A N   1 
ATOM   8407  C  CA  . TRP A 1 1106 ? -40.087  46.830  -16.728 1.00 116.18 ? 1106 TRP A CA  1 
ATOM   8408  C  C   . TRP A 1 1106 ? -38.950  46.341  -17.596 1.00 114.73 ? 1106 TRP A C   1 
ATOM   8409  O  O   . TRP A 1 1106 ? -38.010  47.077  -17.867 1.00 116.32 ? 1106 TRP A O   1 
ATOM   8410  C  CB  . TRP A 1 1106 ? -40.037  46.158  -15.361 1.00 116.24 ? 1106 TRP A CB  1 
ATOM   8411  C  CG  . TRP A 1 1106 ? -38.765  46.373  -14.621 1.00 115.65 ? 1106 TRP A CG  1 
ATOM   8412  C  CD1 . TRP A 1 1106 ? -38.447  47.433  -13.853 1.00 115.82 ? 1106 TRP A CD1 1 
ATOM   8413  C  CD2 . TRP A 1 1106 ? -37.650  45.487  -14.568 1.00 115.51 ? 1106 TRP A CD2 1 
ATOM   8414  N  NE1 . TRP A 1 1106 ? -37.202  47.275  -13.327 1.00 115.80 ? 1106 TRP A NE1 1 
ATOM   8415  C  CE2 . TRP A 1 1106 ? -36.687  46.086  -13.755 1.00 116.24 ? 1106 TRP A CE2 1 
ATOM   8416  C  CE3 . TRP A 1 1106 ? -37.375  44.240  -15.137 1.00 116.24 ? 1106 TRP A CE3 1 
ATOM   8417  C  CZ2 . TRP A 1 1106 ? -35.461  45.491  -13.489 1.00 118.78 ? 1106 TRP A CZ2 1 
ATOM   8418  C  CZ3 . TRP A 1 1106 ? -36.155  43.644  -14.873 1.00 116.77 ? 1106 TRP A CZ3 1 
ATOM   8419  C  CH2 . TRP A 1 1106 ? -35.210  44.272  -14.056 1.00 118.07 ? 1106 TRP A CH2 1 
ATOM   8420  N  N   . LEU A 1 1107 ? -39.034  45.086  -18.024 1.00 113.74 ? 1107 LEU A N   1 
ATOM   8421  C  CA  . LEU A 1 1107 ? -37.947  44.496  -18.786 1.00 113.98 ? 1107 LEU A CA  1 
ATOM   8422  C  C   . LEU A 1 1107 ? -37.772  45.303  -20.043 1.00 120.78 ? 1107 LEU A C   1 
ATOM   8423  O  O   . LEU A 1 1107 ? -36.672  45.761  -20.355 1.00 122.81 ? 1107 LEU A O   1 
ATOM   8424  C  CB  . LEU A 1 1107 ? -38.239  43.049  -19.180 1.00 107.79 ? 1107 LEU A CB  1 
ATOM   8425  C  CG  . LEU A 1 1107 ? -38.252  41.964  -18.121 1.00 102.91 ? 1107 LEU A CG  1 
ATOM   8426  C  CD1 . LEU A 1 1107 ? -39.674  41.688  -17.759 1.00 102.18 ? 1107 LEU A CD1 1 
ATOM   8427  C  CD2 . LEU A 1 1107 ? -37.614  40.714  -18.656 1.00 99.73  ? 1107 LEU A CD2 1 
ATOM   8428  N  N   . VAL A 1 1108 ? -38.884  45.480  -20.749 1.00 123.82 ? 1108 VAL A N   1 
ATOM   8429  C  CA  . VAL A 1 1108 ? -38.867  46.000  -22.103 1.00 125.97 ? 1108 VAL A CA  1 
ATOM   8430  C  C   . VAL A 1 1108 ? -38.525  47.481  -22.195 1.00 131.09 ? 1108 VAL A C   1 
ATOM   8431  O  O   . VAL A 1 1108 ? -37.865  47.885  -23.144 1.00 133.10 ? 1108 VAL A O   1 
ATOM   8432  C  CB  . VAL A 1 1108 ? -40.184  45.718  -22.824 1.00 124.88 ? 1108 VAL A CB  1 
ATOM   8433  C  CG1 . VAL A 1 1108 ? -41.351  45.956  -21.897 1.00 125.32 ? 1108 VAL A CG1 1 
ATOM   8434  C  CG2 . VAL A 1 1108 ? -40.295  46.589  -24.039 1.00 126.56 ? 1108 VAL A CG2 1 
ATOM   8435  N  N   . GLU A 1 1109 ? -38.949  48.293  -21.229 1.00 133.73 ? 1109 GLU A N   1 
ATOM   8436  C  CA  . GLU A 1 1109 ? -38.640  49.731  -21.282 1.00 138.37 ? 1109 GLU A CA  1 
ATOM   8437  C  C   . GLU A 1 1109 ? -37.225  50.094  -20.821 1.00 140.19 ? 1109 GLU A C   1 
ATOM   8438  O  O   . GLU A 1 1109 ? -36.690  51.120  -21.227 1.00 142.70 ? 1109 GLU A O   1 
ATOM   8439  C  CB  . GLU A 1 1109 ? -39.675  50.566  -20.516 1.00 140.28 ? 1109 GLU A CB  1 
ATOM   8440  C  CG  . GLU A 1 1109 ? -41.094  50.404  -21.029 1.00 139.89 ? 1109 GLU A CG  1 
ATOM   8441  C  CD  . GLU A 1 1109 ? -42.068  51.365  -20.381 1.00 140.86 ? 1109 GLU A CD  1 
ATOM   8442  O  OE1 . GLU A 1 1109 ? -43.159  50.926  -19.960 1.00 139.74 ? 1109 GLU A OE1 1 
ATOM   8443  O  OE2 . GLU A 1 1109 ? -41.738  52.561  -20.296 1.00 142.64 ? 1109 GLU A OE2 1 
ATOM   8444  N  N   . ASN A 1 1110 ? -36.625  49.261  -19.975 1.00 139.12 ? 1110 ASN A N   1 
ATOM   8445  C  CA  . ASN A 1 1110 ? -35.312  49.563  -19.418 1.00 139.76 ? 1110 ASN A CA  1 
ATOM   8446  C  C   . ASN A 1 1110 ? -34.198  48.624  -19.889 1.00 137.53 ? 1110 ASN A C   1 
ATOM   8447  O  O   . ASN A 1 1110 ? -33.030  49.010  -19.951 1.00 139.18 ? 1110 ASN A O   1 
ATOM   8448  C  CB  . ASN A 1 1110 ? -35.376  49.573  -17.886 1.00 140.90 ? 1110 ASN A CB  1 
ATOM   8449  C  CG  . ASN A 1 1110 ? -36.470  50.481  -17.347 1.00 143.30 ? 1110 ASN A CG  1 
ATOM   8450  O  OD1 . ASN A 1 1110 ? -37.503  50.010  -16.873 1.00 143.26 ? 1110 ASN A OD1 1 
ATOM   8451  N  ND2 . ASN A 1 1110 ? -36.248  51.786  -17.416 1.00 146.00 ? 1110 ASN A ND2 1 
ATOM   8452  N  N   . TYR A 1 1111 ? -34.559  47.402  -20.251 1.00 134.96 ? 1111 TYR A N   1 
ATOM   8453  C  CA  . TYR A 1 1111 ? -33.563  46.347  -20.389 1.00 133.66 ? 1111 TYR A CA  1 
ATOM   8454  C  C   . TYR A 1 1111 ? -33.546  45.615  -21.727 1.00 133.72 ? 1111 TYR A C   1 
ATOM   8455  O  O   . TYR A 1 1111 ? -33.285  44.414  -21.792 1.00 131.13 ? 1111 TYR A O   1 
ATOM   8456  C  CB  . TYR A 1 1111 ? -33.736  45.374  -19.240 1.00 131.41 ? 1111 TYR A CB  1 
ATOM   8457  C  CG  . TYR A 1 1111 ? -33.327  46.019  -17.946 1.00 132.70 ? 1111 TYR A CG  1 
ATOM   8458  C  CD1 . TYR A 1 1111 ? -32.050  45.834  -17.448 1.00 134.07 ? 1111 TYR A CD1 1 
ATOM   8459  C  CD2 . TYR A 1 1111 ? -34.195  46.843  -17.241 1.00 132.80 ? 1111 TYR A CD2 1 
ATOM   8460  C  CE1 . TYR A 1 1111 ? -31.639  46.432  -16.278 1.00 135.91 ? 1111 TYR A CE1 1 
ATOM   8461  C  CE2 . TYR A 1 1111 ? -33.798  47.447  -16.062 1.00 134.65 ? 1111 TYR A CE2 1 
ATOM   8462  C  CZ  . TYR A 1 1111 ? -32.508  47.234  -15.588 1.00 136.41 ? 1111 TYR A CZ  1 
ATOM   8463  O  OH  . TYR A 1 1111 ? -32.054  47.809  -14.423 1.00 138.61 ? 1111 TYR A OH  1 
ATOM   8464  N  N   . GLN A 1 1112 ? -33.810  46.362  -22.793 1.00 135.67 ? 1112 GLN A N   1 
ATOM   8465  C  CA  . GLN A 1 1112 ? -33.733  45.848  -24.152 1.00 136.06 ? 1112 GLN A CA  1 
ATOM   8466  C  C   . GLN A 1 1112 ? -32.868  46.804  -24.940 1.00 142.16 ? 1112 GLN A C   1 
ATOM   8467  O  O   . GLN A 1 1112 ? -33.232  47.959  -25.148 1.00 144.66 ? 1112 GLN A O   1 
ATOM   8468  C  CB  . GLN A 1 1112 ? -35.122  45.770  -24.787 1.00 132.62 ? 1112 GLN A CB  1 
ATOM   8469  C  CG  . GLN A 1 1112 ? -35.137  45.319  -26.253 1.00 129.01 ? 1112 GLN A CG  1 
ATOM   8470  C  CD  . GLN A 1 1112 ? -36.548  45.022  -26.756 1.00 125.94 ? 1112 GLN A CD  1 
ATOM   8471  O  OE1 . GLN A 1 1112 ? -37.476  45.800  -26.526 1.00 126.71 ? 1112 GLN A OE1 1 
ATOM   8472  N  NE2 . GLN A 1 1112 ? -36.713  43.893  -27.443 1.00 122.51 ? 1112 GLN A NE2 1 
ATOM   8473  N  N   . LEU A 1 1113 ? -31.713  46.313  -25.364 1.00 144.81 ? 1113 LEU A N   1 
ATOM   8474  C  CA  . LEU A 1 1113 ? -30.733  47.128  -26.056 1.00 148.60 ? 1113 LEU A CA  1 
ATOM   8475  C  C   . LEU A 1 1113 ? -31.244  47.578  -27.421 1.00 151.11 ? 1113 LEU A C   1 
ATOM   8476  O  O   . LEU A 1 1113 ? -32.226  47.037  -27.936 1.00 149.21 ? 1113 LEU A O   1 
ATOM   8477  C  CB  . LEU A 1 1113 ? -29.417  46.357  -26.188 1.00 146.41 ? 1113 LEU A CB  1 
ATOM   8478  C  CG  . LEU A 1 1113 ? -28.756  45.970  -24.863 1.00 143.59 ? 1113 LEU A CG  1 
ATOM   8479  C  CD1 . LEU A 1 1113 ? -28.046  44.637  -24.970 1.00 142.09 ? 1113 LEU A CD1 1 
ATOM   8480  C  CD2 . LEU A 1 1113 ? -27.799  47.053  -24.414 1.00 145.59 ? 1113 LEU A CD2 1 
ATOM   8481  N  N   . ASP A 1 1114 ? -30.571  48.578  -27.988 1.00 156.28 ? 1114 ASP A N   1 
ATOM   8482  C  CA  . ASP A 1 1114 ? -30.916  49.119  -29.297 1.00 159.65 ? 1114 ASP A CA  1 
ATOM   8483  C  C   . ASP A 1 1114 ? -30.599  48.143  -30.417 1.00 156.50 ? 1114 ASP A C   1 
ATOM   8484  O  O   . ASP A 1 1114 ? -30.252  48.543  -31.528 1.00 158.12 ? 1114 ASP A O   1 
ATOM   8485  C  CB  . ASP A 1 1114 ? -30.204  50.446  -29.542 1.00 166.80 ? 1114 ASP A CB  1 
ATOM   8486  C  CG  . ASP A 1 1114 ? -31.056  51.634  -29.165 1.00 172.92 ? 1114 ASP A CG  1 
ATOM   8487  O  OD1 . ASP A 1 1114 ? -32.294  51.562  -29.356 1.00 172.91 ? 1114 ASP A OD1 1 
ATOM   8488  O  OD2 . ASP A 1 1114 ? -30.486  52.640  -28.686 1.00 177.00 ? 1114 ASP A OD2 1 
ATOM   8489  N  N   . ASN A 1 1115 ? -30.715  46.859  -30.108 1.00 152.07 ? 1115 ASN A N   1 
ATOM   8490  C  CA  . ASN A 1 1115 ? -30.635  45.810  -31.109 1.00 147.74 ? 1115 ASN A CA  1 
ATOM   8491  C  C   . ASN A 1 1115 ? -31.769  44.833  -30.873 1.00 138.95 ? 1115 ASN A C   1 
ATOM   8492  O  O   . ASN A 1 1115 ? -32.025  43.950  -31.679 1.00 135.42 ? 1115 ASN A O   1 
ATOM   8493  C  CB  . ASN A 1 1115 ? -29.271  45.104  -31.076 1.00 150.14 ? 1115 ASN A CB  1 
ATOM   8494  C  CG  . ASN A 1 1115 ? -28.987  44.406  -29.747 1.00 149.92 ? 1115 ASN A CG  1 
ATOM   8495  O  OD1 . ASN A 1 1115 ? -27.922  43.807  -29.563 1.00 150.27 ? 1115 ASN A OD1 1 
ATOM   8496  N  ND2 . ASN A 1 1115 ? -29.934  44.479  -28.821 1.00 149.12 ? 1115 ASN A ND2 1 
ATOM   8497  N  N   . GLY A 1 1116 ? -32.460  45.018  -29.758 1.00 136.33 ? 1116 GLY A N   1 
ATOM   8498  C  CA  . GLY A 1 1116 ? -33.535  44.129  -29.385 1.00 130.76 ? 1116 GLY A CA  1 
ATOM   8499  C  C   . GLY A 1 1116 ? -33.162  43.066  -28.375 1.00 124.99 ? 1116 GLY A C   1 
ATOM   8500  O  O   . GLY A 1 1116 ? -34.037  42.375  -27.881 1.00 123.41 ? 1116 GLY A O   1 
ATOM   8501  N  N   . SER A 1 1117 ? -31.879  42.914  -28.070 1.00 120.49 ? 1117 SER A N   1 
ATOM   8502  C  CA  . SER A 1 1117 ? -31.470  41.948  -27.049 1.00 118.59 ? 1117 SER A CA  1 
ATOM   8503  C  C   . SER A 1 1117 ? -31.666  42.533  -25.649 1.00 120.34 ? 1117 SER A C   1 
ATOM   8504  O  O   . SER A 1 1117 ? -31.820  43.742  -25.508 1.00 123.58 ? 1117 SER A O   1 
ATOM   8505  C  CB  . SER A 1 1117 ? -30.019  41.485  -27.252 1.00 118.76 ? 1117 SER A CB  1 
ATOM   8506  O  OG  . SER A 1 1117 ? -29.068  42.475  -26.889 1.00 120.56 ? 1117 SER A OG  1 
ATOM   8507  N  N   . PHE A 1 1118 ? -31.671  41.689  -24.620 1.00 117.10 ? 1118 PHE A N   1 
ATOM   8508  C  CA  . PHE A 1 1118 ? -31.945  42.150  -23.263 1.00 115.49 ? 1118 PHE A CA  1 
ATOM   8509  C  C   . PHE A 1 1118 ? -30.709  42.152  -22.362 1.00 115.12 ? 1118 PHE A C   1 
ATOM   8510  O  O   . PHE A 1 1118 ? -29.976  41.185  -22.334 1.00 114.78 ? 1118 PHE A O   1 
ATOM   8511  C  CB  . PHE A 1 1118 ? -33.038  41.274  -22.665 1.00 113.85 ? 1118 PHE A CB  1 
ATOM   8512  C  CG  . PHE A 1 1118 ? -34.422  41.711  -23.034 1.00 114.40 ? 1118 PHE A CG  1 
ATOM   8513  C  CD1 . PHE A 1 1118 ? -34.757  41.950  -24.345 1.00 114.21 ? 1118 PHE A CD1 1 
ATOM   8514  C  CD2 . PHE A 1 1118 ? -35.390  41.896  -22.070 1.00 115.13 ? 1118 PHE A CD2 1 
ATOM   8515  C  CE1 . PHE A 1 1118 ? -36.035  42.364  -24.686 1.00 113.77 ? 1118 PHE A CE1 1 
ATOM   8516  C  CE2 . PHE A 1 1118 ? -36.673  42.304  -22.412 1.00 114.43 ? 1118 PHE A CE2 1 
ATOM   8517  C  CZ  . PHE A 1 1118 ? -36.990  42.538  -23.716 1.00 113.57 ? 1118 PHE A CZ  1 
ATOM   8518  N  N   . LYS A 1 1119 ? -30.462  43.235  -21.629 1.00 116.58 ? 1119 LYS A N   1 
ATOM   8519  C  CA  . LYS A 1 1119 ? -29.334  43.246  -20.685 1.00 117.13 ? 1119 LYS A CA  1 
ATOM   8520  C  C   . LYS A 1 1119 ? -29.775  42.751  -19.335 1.00 115.34 ? 1119 LYS A C   1 
ATOM   8521  O  O   . LYS A 1 1119 ? -30.886  43.031  -18.907 1.00 114.56 ? 1119 LYS A O   1 
ATOM   8522  C  CB  . LYS A 1 1119 ? -28.649  44.633  -20.550 1.00 128.80 ? 1119 LYS A CB  1 
ATOM   8523  C  CG  . LYS A 1 1119 ? -29.571  45.890  -20.503 1.00 137.70 ? 1119 LYS A CG  1 
ATOM   8524  C  CD  . LYS A 1 1119 ? -28.817  47.173  -19.995 1.00 168.56 ? 1119 LYS A CD  1 
ATOM   8525  C  CE  . LYS A 1 1119 ? -28.398  48.181  -21.092 1.00 169.32 ? 1119 LYS A CE  1 
ATOM   8526  N  NZ  . LYS A 1 1119 ? -29.362  49.305  -21.301 1.00 169.20 ? 1119 LYS A NZ  1 
ATOM   8527  N  N   . GLU A 1 1120 ? -28.921  41.999  -18.659 1.00 118.08 ? 1120 GLU A N   1 
ATOM   8528  C  CA  . GLU A 1 1120 ? -29.217  41.692  -17.268 1.00 120.26 ? 1120 GLU A CA  1 
ATOM   8529  C  C   . GLU A 1 1120 ? -28.724  42.865  -16.442 1.00 125.45 ? 1120 GLU A C   1 
ATOM   8530  O  O   . GLU A 1 1120 ? -27.716  43.486  -16.792 1.00 127.97 ? 1120 GLU A O   1 
ATOM   8531  C  CB  . GLU A 1 1120 ? -28.590  40.367  -16.817 1.00 120.45 ? 1120 GLU A CB  1 
ATOM   8532  C  CG  . GLU A 1 1120 ? -28.676  40.058  -15.296 1.00 121.90 ? 1120 GLU A CG  1 
ATOM   8533  C  CD  . GLU A 1 1120 ? -30.085  40.137  -14.678 1.00 119.69 ? 1120 GLU A CD  1 
ATOM   8534  O  OE1 . GLU A 1 1120 ? -30.731  39.085  -14.482 1.00 117.25 ? 1120 GLU A OE1 1 
ATOM   8535  O  OE2 . GLU A 1 1120 ? -30.533  41.252  -14.353 1.00 120.08 ? 1120 GLU A OE2 1 
ATOM   8536  N  N   . ASN A 1 1121 ? -29.462  43.181  -15.379 1.00 125.54 ? 1121 ASN A N   1 
ATOM   8537  C  CA  . ASN A 1 1121 ? -29.163  44.301  -14.488 1.00 128.49 ? 1121 ASN A CA  1 
ATOM   8538  C  C   . ASN A 1 1121 ? -28.147  43.956  -13.395 1.00 132.82 ? 1121 ASN A C   1 
ATOM   8539  O  O   . ASN A 1 1121 ? -27.009  44.417  -13.424 1.00 134.36 ? 1121 ASN A O   1 
ATOM   8540  C  CB  . ASN A 1 1121 ? -30.464  44.780  -13.843 1.00 125.84 ? 1121 ASN A CB  1 
ATOM   8541  C  CG  . ASN A 1 1121 ? -30.241  45.851  -12.806 1.00 124.19 ? 1121 ASN A CG  1 
ATOM   8542  O  OD1 . ASN A 1 1121 ? -29.723  46.920  -13.118 1.00 125.24 ? 1121 ASN A OD1 1 
ATOM   8543  N  ND2 . ASN A 1 1121 ? -30.648  45.577  -11.567 1.00 121.01 ? 1121 ASN A ND2 1 
ATOM   8544  N  N   . SER A 1 1122 ? -28.574  43.141  -12.435 1.00 133.87 ? 1122 SER A N   1 
ATOM   8545  C  CA  . SER A 1 1122 ? -27.734  42.741  -11.323 1.00 136.94 ? 1122 SER A CA  1 
ATOM   8546  C  C   . SER A 1 1122 ? -26.595  41.866  -11.794 1.00 140.33 ? 1122 SER A C   1 
ATOM   8547  O  O   . SER A 1 1122 ? -26.475  41.544  -12.975 1.00 141.08 ? 1122 SER A O   1 
ATOM   8548  C  CB  . SER A 1 1122 ? -28.544  41.949  -10.319 1.00 132.80 ? 1122 SER A CB  1 
ATOM   8549  O  OG  . SER A 1 1122 ? -28.587  40.600  -10.709 1.00 129.58 ? 1122 SER A OG  1 
ATOM   8550  N  N   . GLN A 1 1123 ? -25.761  41.457  -10.852 1.00 144.69 ? 1123 GLN A N   1 
ATOM   8551  C  CA  . GLN A 1 1123 ? -24.591  40.660  -11.186 1.00 147.80 ? 1123 GLN A CA  1 
ATOM   8552  C  C   . GLN A 1 1123 ? -24.909  39.167  -11.294 1.00 139.56 ? 1123 GLN A C   1 
ATOM   8553  O  O   . GLN A 1 1123 ? -24.055  38.383  -11.703 1.00 140.02 ? 1123 GLN A O   1 
ATOM   8554  C  CB  . GLN A 1 1123 ? -23.461  40.920  -10.176 1.00 159.01 ? 1123 GLN A CB  1 
ATOM   8555  C  CG  . GLN A 1 1123 ? -23.085  42.389  -10.065 1.00 169.78 ? 1123 GLN A CG  1 
ATOM   8556  C  CD  . GLN A 1 1123 ? -21.728  42.614  -9.423  1.00 180.80 ? 1123 GLN A CD  1 
ATOM   8557  O  OE1 . GLN A 1 1123 ? -20.723  42.029  -9.828  1.00 184.30 ? 1123 GLN A OE1 1 
ATOM   8558  N  NE2 . GLN A 1 1123 ? -21.690  43.492  -8.432  1.00 186.25 ? 1123 GLN A NE2 1 
ATOM   8559  N  N   . TYR A 1 1124 ? -26.136  38.778  -10.950 1.00 131.14 ? 1124 TYR A N   1 
ATOM   8560  C  CA  . TYR A 1 1124 ? -26.481  37.361  -10.868 1.00 122.15 ? 1124 TYR A CA  1 
ATOM   8561  C  C   . TYR A 1 1124 ? -26.077  36.618  -12.116 1.00 119.31 ? 1124 TYR A C   1 
ATOM   8562  O  O   . TYR A 1 1124 ? -26.603  36.879  -13.185 1.00 116.93 ? 1124 TYR A O   1 
ATOM   8563  C  CB  . TYR A 1 1124 ? -27.975  37.168  -10.660 1.00 115.22 ? 1124 TYR A CB  1 
ATOM   8564  C  CG  . TYR A 1 1124 ? -28.414  35.721  -10.480 1.00 108.60 ? 1124 TYR A CG  1 
ATOM   8565  C  CD1 . TYR A 1 1124 ? -28.345  35.089  -9.239  1.00 107.05 ? 1124 TYR A CD1 1 
ATOM   8566  C  CD2 . TYR A 1 1124 ? -28.912  34.992  -11.542 1.00 104.77 ? 1124 TYR A CD2 1 
ATOM   8567  C  CE1 . TYR A 1 1124 ? -28.760  33.754  -9.070  1.00 103.34 ? 1124 TYR A CE1 1 
ATOM   8568  C  CE2 . TYR A 1 1124 ? -29.330  33.662  -11.388 1.00 100.85 ? 1124 TYR A CE2 1 
ATOM   8569  C  CZ  . TYR A 1 1124 ? -29.256  33.049  -10.153 1.00 98.09  ? 1124 TYR A CZ  1 
ATOM   8570  O  OH  . TYR A 1 1124 ? -29.682  31.745  -10.014 1.00 91.69  ? 1124 TYR A OH  1 
ATOM   8571  N  N   . GLN A 1 1125 ? -25.130  35.698  -11.972 1.00 118.86 ? 1125 GLN A N   1 
ATOM   8572  C  CA  . GLN A 1 1125 ? -24.759  34.794  -13.044 1.00 117.07 ? 1125 GLN A CA  1 
ATOM   8573  C  C   . GLN A 1 1125 ? -25.606  33.567  -12.867 1.00 108.67 ? 1125 GLN A C   1 
ATOM   8574  O  O   . GLN A 1 1125 ? -25.457  32.872  -11.871 1.00 104.51 ? 1125 GLN A O   1 
ATOM   8575  C  CB  . GLN A 1 1125 ? -23.296  34.393  -12.909 1.00 126.78 ? 1125 GLN A CB  1 
ATOM   8576  C  CG  . GLN A 1 1125 ? -22.318  35.504  -13.220 1.00 136.22 ? 1125 GLN A CG  1 
ATOM   8577  C  CD  . GLN A 1 1125 ? -22.282  35.846  -14.703 1.00 142.33 ? 1125 GLN A CD  1 
ATOM   8578  O  OE1 . GLN A 1 1125 ? -23.332  35.923  -15.358 1.00 142.19 ? 1125 GLN A OE1 1 
ATOM   8579  N  NE2 . GLN A 1 1125 ? -21.068  36.044  -15.247 1.00 146.13 ? 1125 GLN A NE2 1 
ATOM   8580  N  N   . PRO A 1 1126 ? -26.500  33.290  -13.824 1.00 105.13 ? 1126 PRO A N   1 
ATOM   8581  C  CA  . PRO A 1 1126 ? -27.398  32.164  -13.615 1.00 103.94 ? 1126 PRO A CA  1 
ATOM   8582  C  C   . PRO A 1 1126 ? -26.722  30.914  -14.140 1.00 107.13 ? 1126 PRO A C   1 
ATOM   8583  O  O   . PRO A 1 1126 ? -26.653  29.918  -13.414 1.00 109.23 ? 1126 PRO A O   1 
ATOM   8584  C  CB  . PRO A 1 1126 ? -28.614  32.527  -14.469 1.00 99.93  ? 1126 PRO A CB  1 
ATOM   8585  C  CG  . PRO A 1 1126 ? -28.277  33.851  -15.141 1.00 101.52 ? 1126 PRO A CG  1 
ATOM   8586  C  CD  . PRO A 1 1126 ? -26.781  33.954  -15.102 1.00 104.82 ? 1126 PRO A CD  1 
ATOM   8587  N  N   . ILE A 1 1127 ? -26.243  30.965  -15.387 1.00 108.92 ? 1127 ILE A N   1 
ATOM   8588  C  CA  . ILE A 1 1127 ? -25.451  29.875  -15.979 1.00 110.49 ? 1127 ILE A CA  1 
ATOM   8589  C  C   . ILE A 1 1127 ? -24.025  30.322  -16.221 1.00 113.38 ? 1127 ILE A C   1 
ATOM   8590  O  O   . ILE A 1 1127 ? -23.733  31.518  -16.314 1.00 112.89 ? 1127 ILE A O   1 
ATOM   8591  C  CB  . ILE A 1 1127 ? -26.032  29.283  -17.331 1.00 114.43 ? 1127 ILE A CB  1 
ATOM   8592  C  CG1 . ILE A 1 1127 ? -26.903  30.297  -18.068 1.00 113.38 ? 1127 ILE A CG1 1 
ATOM   8593  C  CG2 . ILE A 1 1127 ? -26.852  28.033  -17.085 1.00 113.26 ? 1127 ILE A CG2 1 
ATOM   8594  C  CD1 . ILE A 1 1127 ? -26.268  31.673  -18.184 1.00 115.71 ? 1127 ILE A CD1 1 
ATOM   8595  N  N   . LYS A 1 1128 ? -23.142  29.337  -16.290 1.00 117.42 ? 1128 LYS A N   1 
ATOM   8596  C  CA  . LYS A 1 1128 ? -21.804  29.528  -16.802 1.00 121.78 ? 1128 LYS A CA  1 
ATOM   8597  C  C   . LYS A 1 1128 ? -21.841  28.915  -18.182 1.00 126.05 ? 1128 LYS A C   1 
ATOM   8598  O  O   . LYS A 1 1128 ? -22.103  27.720  -18.306 1.00 126.53 ? 1128 LYS A O   1 
ATOM   8599  C  CB  . LYS A 1 1128 ? -20.820  28.760  -15.925 1.00 121.84 ? 1128 LYS A CB  1 
ATOM   8600  C  CG  . LYS A 1 1128 ? -19.458  28.512  -16.545 1.00 123.04 ? 1128 LYS A CG  1 
ATOM   8601  C  CD  . LYS A 1 1128 ? -18.474  29.660  -16.335 1.00 123.88 ? 1128 LYS A CD  1 
ATOM   8602  C  CE  . LYS A 1 1128 ? -18.706  30.808  -17.309 1.00 122.49 ? 1128 LYS A CE  1 
ATOM   8603  N  NZ  . LYS A 1 1128 ? -17.472  31.629  -17.482 1.00 124.36 ? 1128 LYS A NZ  1 
ATOM   8604  N  N   . LEU A 1 1129 ? -21.626  29.714  -19.224 1.00 129.22 ? 1129 LEU A N   1 
ATOM   8605  C  CA  . LEU A 1 1129 ? -21.579  29.152  -20.579 1.00 132.85 ? 1129 LEU A CA  1 
ATOM   8606  C  C   . LEU A 1 1129 ? -20.119  28.914  -21.014 1.00 140.74 ? 1129 LEU A C   1 
ATOM   8607  O  O   . LEU A 1 1129 ? -19.198  29.463  -20.407 1.00 145.47 ? 1129 LEU A O   1 
ATOM   8608  C  CB  . LEU A 1 1129 ? -22.311  30.044  -21.595 1.00 128.57 ? 1129 LEU A CB  1 
ATOM   8609  C  CG  . LEU A 1 1129 ? -23.734  30.546  -21.330 1.00 124.05 ? 1129 LEU A CG  1 
ATOM   8610  C  CD1 . LEU A 1 1129 ? -24.270  31.283  -22.543 1.00 122.51 ? 1129 LEU A CD1 1 
ATOM   8611  C  CD2 . LEU A 1 1129 ? -24.693  29.433  -20.924 1.00 122.23 ? 1129 LEU A CD2 1 
ATOM   8612  N  N   . GLN A 1 1130 ? -19.893  28.099  -22.044 1.00 142.97 ? 1130 GLN A N   1 
ATOM   8613  C  CA  . GLN A 1 1130 ? -18.536  27.918  -22.546 1.00 145.32 ? 1130 GLN A CA  1 
ATOM   8614  C  C   . GLN A 1 1130 ? -18.228  29.038  -23.510 1.00 140.11 ? 1130 GLN A C   1 
ATOM   8615  O  O   . GLN A 1 1130 ? -19.133  29.671  -24.041 1.00 135.90 ? 1130 GLN A O   1 
ATOM   8616  C  CB  . GLN A 1 1130 ? -18.383  26.585  -23.262 1.00 151.99 ? 1130 GLN A CB  1 
ATOM   8617  C  CG  . GLN A 1 1130 ? -19.236  25.459  -22.712 1.00 155.73 ? 1130 GLN A CG  1 
ATOM   8618  C  CD  . GLN A 1 1130 ? -18.817  24.100  -23.268 1.00 160.25 ? 1130 GLN A CD  1 
ATOM   8619  O  OE1 . GLN A 1 1130 ? -17.634  23.870  -23.551 1.00 163.99 ? 1130 GLN A OE1 1 
ATOM   8620  N  NE2 . GLN A 1 1130 ? -19.787  23.197  -23.433 1.00 159.01 ? 1130 GLN A NE2 1 
ATOM   8621  N  N   . GLY A 1 1131 ? -16.950  29.288  -23.739 1.00 142.49 ? 1131 GLY A N   1 
ATOM   8622  C  CA  . GLY A 1 1131 ? -16.565  30.290  -24.708 1.00 144.29 ? 1131 GLY A CA  1 
ATOM   8623  C  C   . GLY A 1 1131 ? -15.368  31.125  -24.307 1.00 149.62 ? 1131 GLY A C   1 
ATOM   8624  O  O   . GLY A 1 1131 ? -14.831  30.991  -23.204 1.00 152.79 ? 1131 GLY A O   1 
ATOM   8625  N  N   . THR A 1 1132 ? -14.941  31.987  -25.222 1.00 148.27 ? 1132 THR A N   1 
ATOM   8626  C  CA  . THR A 1 1132 ? -13.864  32.923  -24.953 1.00 149.37 ? 1132 THR A CA  1 
ATOM   8627  C  C   . THR A 1 1132 ? -14.479  34.114  -24.262 1.00 146.57 ? 1132 THR A C   1 
ATOM   8628  O  O   . THR A 1 1132 ? -15.673  34.304  -24.332 1.00 142.54 ? 1132 THR A O   1 
ATOM   8629  C  CB  . THR A 1 1132 ? -13.232  33.395  -26.255 1.00 152.44 ? 1132 THR A CB  1 
ATOM   8630  O  OG1 . THR A 1 1132 ? -13.514  32.452  -27.306 1.00 151.87 ? 1132 THR A OG1 1 
ATOM   8631  C  CG2 . THR A 1 1132 ? -11.722  33.562  -26.075 1.00 157.02 ? 1132 THR A CG2 1 
ATOM   8632  N  N   . LEU A 1 1133 ? -13.691  34.938  -23.600 1.00 150.84 ? 1133 LEU A N   1 
ATOM   8633  C  CA  . LEU A 1 1133 ? -14.311  36.069  -22.925 1.00 153.08 ? 1133 LEU A CA  1 
ATOM   8634  C  C   . LEU A 1 1133 ? -15.303  36.835  -23.805 1.00 155.57 ? 1133 LEU A C   1 
ATOM   8635  O  O   . LEU A 1 1133 ? -16.323  37.300  -23.308 1.00 156.80 ? 1133 LEU A O   1 
ATOM   8636  C  CB  . LEU A 1 1133 ? -13.279  36.998  -22.290 1.00 154.40 ? 1133 LEU A CB  1 
ATOM   8637  C  CG  . LEU A 1 1133 ? -12.955  36.531  -20.871 1.00 152.55 ? 1133 LEU A CG  1 
ATOM   8638  C  CD1 . LEU A 1 1133 ? -12.038  35.313  -20.909 1.00 153.54 ? 1133 LEU A CD1 1 
ATOM   8639  C  CD2 . LEU A 1 1133 ? -12.344  37.648  -20.037 1.00 153.87 ? 1133 LEU A CD2 1 
ATOM   8640  N  N   . PRO A 1 1134 ? -15.010  36.958  -25.111 1.00 155.92 ? 1134 PRO A N   1 
ATOM   8641  C  CA  . PRO A 1 1134 ? -15.885  37.580  -26.117 1.00 155.71 ? 1134 PRO A CA  1 
ATOM   8642  C  C   . PRO A 1 1134 ? -17.067  36.702  -26.494 1.00 155.29 ? 1134 PRO A C   1 
ATOM   8643  O  O   . PRO A 1 1134 ? -18.218  37.135  -26.402 1.00 152.63 ? 1134 PRO A O   1 
ATOM   8644  C  CB  . PRO A 1 1134 ? -14.974  37.708  -27.341 1.00 156.86 ? 1134 PRO A CB  1 
ATOM   8645  C  CG  . PRO A 1 1134 ? -13.605  37.649  -26.804 1.00 160.07 ? 1134 PRO A CG  1 
ATOM   8646  C  CD  . PRO A 1 1134 ? -13.672  36.706  -25.657 1.00 159.08 ? 1134 PRO A CD  1 
ATOM   8647  N  N   . VAL A 1 1135 ? -16.766  35.486  -26.946 1.00 156.47 ? 1135 VAL A N   1 
ATOM   8648  C  CA  . VAL A 1 1135 ? -17.776  34.474  -27.234 1.00 152.36 ? 1135 VAL A CA  1 
ATOM   8649  C  C   . VAL A 1 1135 ? -18.830  34.459  -26.138 1.00 149.42 ? 1135 VAL A C   1 
ATOM   8650  O  O   . VAL A 1 1135 ? -19.992  34.756  -26.374 1.00 146.82 ? 1135 VAL A O   1 
ATOM   8651  C  CB  . VAL A 1 1135 ? -17.138  33.083  -27.280 1.00 152.34 ? 1135 VAL A CB  1 
ATOM   8652  C  CG1 . VAL A 1 1135 ? -18.161  32.029  -26.958 1.00 149.13 ? 1135 VAL A CG1 1 
ATOM   8653  C  CG2 . VAL A 1 1135 ? -16.489  32.822  -28.627 1.00 153.53 ? 1135 VAL A CG2 1 
ATOM   8654  N  N   . GLU A 1 1136 ? -18.400  34.124  -24.928 1.00 150.67 ? 1136 GLU A N   1 
ATOM   8655  C  CA  . GLU A 1 1136 ? -19.279  34.093  -23.768 1.00 147.92 ? 1136 GLU A CA  1 
ATOM   8656  C  C   . GLU A 1 1136 ? -20.280  35.236  -23.795 1.00 147.55 ? 1136 GLU A C   1 
ATOM   8657  O  O   . GLU A 1 1136 ? -21.475  35.008  -23.905 1.00 146.39 ? 1136 GLU A O   1 
ATOM   8658  C  CB  . GLU A 1 1136 ? -18.464  34.146  -22.471 1.00 147.52 ? 1136 GLU A CB  1 
ATOM   8659  C  CG  . GLU A 1 1136 ? -19.323  34.237  -21.238 1.00 145.48 ? 1136 GLU A CG  1 
ATOM   8660  C  CD  . GLU A 1 1136 ? -18.699  33.548  -20.059 1.00 145.72 ? 1136 GLU A CD  1 
ATOM   8661  O  OE1 . GLU A 1 1136 ? -17.457  33.439  -20.058 1.00 145.84 ? 1136 GLU A OE1 1 
ATOM   8662  O  OE2 . GLU A 1 1136 ? -19.454  33.121  -19.148 1.00 145.24 ? 1136 GLU A OE2 1 
ATOM   8663  N  N   . ALA A 1 1137 ? -19.793  36.467  -23.713 1.00 150.16 ? 1137 ALA A N   1 
ATOM   8664  C  CA  . ALA A 1 1137 ? -20.688  37.615  -23.682 1.00 150.28 ? 1137 ALA A CA  1 
ATOM   8665  C  C   . ALA A 1 1137 ? -21.684  37.552  -24.835 1.00 148.37 ? 1137 ALA A C   1 
ATOM   8666  O  O   . ALA A 1 1137 ? -22.867  37.858  -24.672 1.00 146.42 ? 1137 ALA A O   1 
ATOM   8667  C  CB  . ALA A 1 1137 ? -19.896  38.909  -23.720 1.00 153.56 ? 1137 ALA A CB  1 
ATOM   8668  N  N   . ARG A 1 1138 ? -21.205  37.152  -26.003 1.00 149.09 ? 1138 ARG A N   1 
ATOM   8669  C  CA  . ARG A 1 1138 ? -22.097  36.959  -27.126 1.00 147.60 ? 1138 ARG A CA  1 
ATOM   8670  C  C   . ARG A 1 1138 ? -23.140  35.936  -26.698 1.00 141.45 ? 1138 ARG A C   1 
ATOM   8671  O  O   . ARG A 1 1138 ? -24.307  36.271  -26.527 1.00 138.64 ? 1138 ARG A O   1 
ATOM   8672  C  CB  . ARG A 1 1138 ? -21.310  36.494  -28.359 1.00 153.79 ? 1138 ARG A CB  1 
ATOM   8673  C  CG  . ARG A 1 1138 ? -22.135  36.352  -29.624 1.00 156.28 ? 1138 ARG A CG  1 
ATOM   8674  C  CD  . ARG A 1 1138 ? -21.325  36.662  -30.878 1.00 161.71 ? 1138 ARG A CD  1 
ATOM   8675  N  NE  . ARG A 1 1138 ? -22.200  36.692  -32.048 1.00 164.79 ? 1138 ARG A NE  1 
ATOM   8676  C  CZ  . ARG A 1 1138 ? -21.855  37.154  -33.248 1.00 169.10 ? 1138 ARG A CZ  1 
ATOM   8677  N  NH1 . ARG A 1 1138 ? -20.634  37.641  -33.451 1.00 172.28 ? 1138 ARG A NH1 1 
ATOM   8678  N  NH2 . ARG A 1 1138 ? -22.735  37.132  -34.248 1.00 168.74 ? 1138 ARG A NH2 1 
ATOM   8679  N  N   . GLU A 1 1139 ? -22.691  34.701  -26.486 1.00 138.58 ? 1139 GLU A N   1 
ATOM   8680  C  CA  . GLU A 1 1139 ? -23.528  33.595  -26.026 1.00 132.18 ? 1139 GLU A CA  1 
ATOM   8681  C  C   . GLU A 1 1139 ? -24.457  34.015  -24.914 1.00 131.19 ? 1139 GLU A C   1 
ATOM   8682  O  O   . GLU A 1 1139 ? -25.672  33.875  -25.005 1.00 128.91 ? 1139 GLU A O   1 
ATOM   8683  C  CB  . GLU A 1 1139 ? -22.640  32.505  -25.442 1.00 130.32 ? 1139 GLU A CB  1 
ATOM   8684  C  CG  . GLU A 1 1139 ? -22.044  31.571  -26.435 1.00 128.00 ? 1139 GLU A CG  1 
ATOM   8685  C  CD  . GLU A 1 1139 ? -23.052  30.610  -26.967 1.00 124.95 ? 1139 GLU A CD  1 
ATOM   8686  O  OE1 . GLU A 1 1139 ? -22.927  29.405  -26.662 1.00 125.94 ? 1139 GLU A OE1 1 
ATOM   8687  O  OE2 . GLU A 1 1139 ? -23.970  31.063  -27.682 1.00 123.05 ? 1139 GLU A OE2 1 
ATOM   8688  N  N   . ASN A 1 1140 ? -23.849  34.497  -23.843 1.00 131.12 ? 1140 ASN A N   1 
ATOM   8689  C  CA  . ASN A 1 1140 ? -24.558  34.886  -22.654 1.00 130.28 ? 1140 ASN A CA  1 
ATOM   8690  C  C   . ASN A 1 1140 ? -25.733  35.758  -23.025 1.00 124.22 ? 1140 ASN A C   1 
ATOM   8691  O  O   . ASN A 1 1140 ? -26.842  35.565  -22.534 1.00 121.58 ? 1140 ASN A O   1 
ATOM   8692  C  CB  . ASN A 1 1140 ? -23.615  35.649  -21.748 1.00 138.25 ? 1140 ASN A CB  1 
ATOM   8693  C  CG  . ASN A 1 1140 ? -24.147  35.782  -20.354 1.00 144.39 ? 1140 ASN A CG  1 
ATOM   8694  O  OD1 . ASN A 1 1140 ? -23.587  36.510  -19.539 1.00 149.53 ? 1140 ASN A OD1 1 
ATOM   8695  N  ND2 . ASN A 1 1140 ? -25.240  35.079  -20.060 1.00 144.39 ? 1140 ASN A ND2 1 
ATOM   8696  N  N   . SER A 1 1141 ? -25.489  36.706  -23.921 1.00 122.15 ? 1141 SER A N   1 
ATOM   8697  C  CA  . SER A 1 1141 ? -26.541  37.602  -24.387 1.00 119.26 ? 1141 SER A CA  1 
ATOM   8698  C  C   . SER A 1 1141 ? -27.713  36.851  -25.027 1.00 112.53 ? 1141 SER A C   1 
ATOM   8699  O  O   . SER A 1 1141 ? -28.861  37.053  -24.636 1.00 109.78 ? 1141 SER A O   1 
ATOM   8700  C  CB  . SER A 1 1141 ? -25.984  38.646  -25.360 1.00 122.18 ? 1141 SER A CB  1 
ATOM   8701  O  OG  . SER A 1 1141 ? -26.974  39.616  -25.686 1.00 122.56 ? 1141 SER A OG  1 
ATOM   8702  N  N   . LEU A 1 1142 ? -27.423  35.996  -26.010 1.00 109.69 ? 1142 LEU A N   1 
ATOM   8703  C  CA  . LEU A 1 1142 ? -28.454  35.152  -26.605 1.00 103.33 ? 1142 LEU A CA  1 
ATOM   8704  C  C   . LEU A 1 1142 ? -29.218  34.595  -25.430 1.00 101.37 ? 1142 LEU A C   1 
ATOM   8705  O  O   . LEU A 1 1142 ? -30.416  34.862  -25.282 1.00 99.69  ? 1142 LEU A O   1 
ATOM   8706  C  CB  . LEU A 1 1142 ? -27.845  33.993  -27.412 1.00 99.75  ? 1142 LEU A CB  1 
ATOM   8707  C  CG  . LEU A 1 1142 ? -28.293  33.702  -28.857 1.00 94.07  ? 1142 LEU A CG  1 
ATOM   8708  C  CD1 . LEU A 1 1142 ? -27.287  32.802  -29.568 1.00 93.48  ? 1142 LEU A CD1 1 
ATOM   8709  C  CD2 . LEU A 1 1142 ? -29.697  33.131  -28.966 1.00 89.47  ? 1142 LEU A CD2 1 
ATOM   8710  N  N   . TYR A 1 1143 ? -28.500  33.866  -24.565 1.00 101.41 ? 1143 TYR A N   1 
ATOM   8711  C  CA  . TYR A 1 1143 ? -29.140  33.090  -23.490 1.00 98.58  ? 1143 TYR A CA  1 
ATOM   8712  C  C   . TYR A 1 1143 ? -30.151  33.905  -22.722 1.00 96.20  ? 1143 TYR A C   1 
ATOM   8713  O  O   . TYR A 1 1143 ? -31.261  33.429  -22.474 1.00 93.35  ? 1143 TYR A O   1 
ATOM   8714  C  CB  . TYR A 1 1143 ? -28.161  32.423  -22.505 1.00 97.87  ? 1143 TYR A CB  1 
ATOM   8715  C  CG  . TYR A 1 1143 ? -28.883  31.827  -21.302 1.00 96.10  ? 1143 TYR A CG  1 
ATOM   8716  C  CD1 . TYR A 1 1143 ? -29.337  30.517  -21.310 1.00 94.01  ? 1143 TYR A CD1 1 
ATOM   8717  C  CD2 . TYR A 1 1143 ? -29.139  32.596  -20.166 1.00 96.55  ? 1143 TYR A CD2 1 
ATOM   8718  C  CE1 . TYR A 1 1143 ? -30.010  29.986  -20.219 1.00 94.06  ? 1143 TYR A CE1 1 
ATOM   8719  C  CE2 . TYR A 1 1143 ? -29.808  32.066  -19.060 1.00 95.19  ? 1143 TYR A CE2 1 
ATOM   8720  C  CZ  . TYR A 1 1143 ? -30.237  30.763  -19.095 1.00 94.05  ? 1143 TYR A CZ  1 
ATOM   8721  O  OH  . TYR A 1 1143 ? -30.897  30.231  -18.009 1.00 93.01  ? 1143 TYR A OH  1 
ATOM   8722  N  N   . LEU A 1 1144 ? -29.780  35.126  -22.354 1.00 96.63  ? 1144 LEU A N   1 
ATOM   8723  C  CA  . LEU A 1 1144 ? -30.745  35.992  -21.703 1.00 97.23  ? 1144 LEU A CA  1 
ATOM   8724  C  C   . LEU A 1 1144 ? -31.911  36.335  -22.652 1.00 97.54  ? 1144 LEU A C   1 
ATOM   8725  O  O   . LEU A 1 1144 ? -33.078  36.010  -22.391 1.00 96.70  ? 1144 LEU A O   1 
ATOM   8726  C  CB  . LEU A 1 1144 ? -30.079  37.257  -21.170 1.00 96.90  ? 1144 LEU A CB  1 
ATOM   8727  C  CG  . LEU A 1 1144 ? -30.902  38.013  -20.128 1.00 94.26  ? 1144 LEU A CG  1 
ATOM   8728  C  CD1 . LEU A 1 1144 ? -30.733  37.336  -18.779 1.00 93.42  ? 1144 LEU A CD1 1 
ATOM   8729  C  CD2 . LEU A 1 1144 ? -30.484  39.475  -20.060 1.00 95.12  ? 1144 LEU A CD2 1 
ATOM   8730  N  N   . THR A 1 1145 ? -31.588  36.974  -23.767 1.00 98.20  ? 1145 THR A N   1 
ATOM   8731  C  CA  . THR A 1 1145 ? -32.619  37.410  -24.690 1.00 96.89  ? 1145 THR A CA  1 
ATOM   8732  C  C   . THR A 1 1145 ? -33.579  36.255  -25.037 1.00 95.37  ? 1145 THR A C   1 
ATOM   8733  O  O   . THR A 1 1145 ? -34.790  36.437  -24.997 1.00 94.61  ? 1145 THR A O   1 
ATOM   8734  C  CB  . THR A 1 1145 ? -32.013  38.109  -25.939 1.00 102.13 ? 1145 THR A CB  1 
ATOM   8735  O  OG1 . THR A 1 1145 ? -31.114  39.137  -25.508 1.00 102.59 ? 1145 THR A OG1 1 
ATOM   8736  C  CG2 . THR A 1 1145 ? -33.093  38.761  -26.755 1.00 102.68 ? 1145 THR A CG2 1 
ATOM   8737  N  N   . ALA A 1 1146 ? -33.068  35.063  -25.324 1.00 94.27  ? 1146 ALA A N   1 
ATOM   8738  C  CA  . ALA A 1 1146 ? -33.979  33.946  -25.568 1.00 96.87  ? 1146 ALA A CA  1 
ATOM   8739  C  C   . ALA A 1 1146 ? -34.920  33.710  -24.370 1.00 97.49  ? 1146 ALA A C   1 
ATOM   8740  O  O   . ALA A 1 1146 ? -36.153  33.669  -24.509 1.00 95.14  ? 1146 ALA A O   1 
ATOM   8741  C  CB  . ALA A 1 1146 ? -33.206  32.702  -25.904 1.00 97.30  ? 1146 ALA A CB  1 
ATOM   8742  N  N   . PHE A 1 1147 ? -34.302  33.568  -23.199 1.00 99.56  ? 1147 PHE A N   1 
ATOM   8743  C  CA  . PHE A 1 1147 ? -34.973  33.336  -21.912 1.00 98.23  ? 1147 PHE A CA  1 
ATOM   8744  C  C   . PHE A 1 1147 ? -36.030  34.388  -21.615 1.00 96.84  ? 1147 PHE A C   1 
ATOM   8745  O  O   . PHE A 1 1147 ? -37.201  34.078  -21.382 1.00 96.43  ? 1147 PHE A O   1 
ATOM   8746  C  CB  . PHE A 1 1147 ? -33.923  33.387  -20.780 1.00 98.63  ? 1147 PHE A CB  1 
ATOM   8747  C  CG  . PHE A 1 1147 ? -34.422  32.915  -19.422 1.00 96.66  ? 1147 PHE A CG  1 
ATOM   8748  C  CD1 . PHE A 1 1147 ? -33.678  32.007  -18.687 1.00 94.31  ? 1147 PHE A CD1 1 
ATOM   8749  C  CD2 . PHE A 1 1147 ? -35.610  33.377  -18.887 1.00 96.47  ? 1147 PHE A CD2 1 
ATOM   8750  C  CE1 . PHE A 1 1147 ? -34.113  31.567  -17.475 1.00 92.93  ? 1147 PHE A CE1 1 
ATOM   8751  C  CE2 . PHE A 1 1147 ? -36.036  32.928  -17.669 1.00 95.64  ? 1147 PHE A CE2 1 
ATOM   8752  C  CZ  . PHE A 1 1147 ? -35.280  32.030  -16.965 1.00 93.77  ? 1147 PHE A CZ  1 
ATOM   8753  N  N   . THR A 1 1148 ? -35.598  35.639  -21.579 1.00 97.99  ? 1148 THR A N   1 
ATOM   8754  C  CA  . THR A 1 1148 ? -36.530  36.725  -21.326 1.00 99.97  ? 1148 THR A CA  1 
ATOM   8755  C  C   . THR A 1 1148 ? -37.642  36.807  -22.431 1.00 92.95  ? 1148 THR A C   1 
ATOM   8756  O  O   . THR A 1 1148 ? -38.740  37.344  -22.200 1.00 92.35  ? 1148 THR A O   1 
ATOM   8757  C  CB  . THR A 1 1148 ? -35.780  38.078  -20.980 1.00 93.88  ? 1148 THR A CB  1 
ATOM   8758  O  OG1 . THR A 1 1148 ? -36.532  39.207  -21.441 1.00 96.12  ? 1148 THR A OG1 1 
ATOM   8759  C  CG2 . THR A 1 1148 ? -34.383  38.133  -21.578 1.00 92.63  ? 1148 THR A CG2 1 
ATOM   8760  N  N   . VAL A 1 1149 ? -37.397  36.237  -23.609 1.00 90.31  ? 1149 VAL A N   1 
ATOM   8761  C  CA  . VAL A 1 1149 ? -38.496  36.158  -24.557 1.00 89.21  ? 1149 VAL A CA  1 
ATOM   8762  C  C   . VAL A 1 1149 ? -39.537  35.170  -23.995 1.00 86.15  ? 1149 VAL A C   1 
ATOM   8763  O  O   . VAL A 1 1149 ? -40.655  35.560  -23.648 1.00 85.60  ? 1149 VAL A O   1 
ATOM   8764  C  CB  . VAL A 1 1149 ? -38.034  35.870  -26.020 1.00 72.89  ? 1149 VAL A CB  1 
ATOM   8765  C  CG1 . VAL A 1 1149 ? -39.139  35.174  -26.830 1.00 72.66  ? 1149 VAL A CG1 1 
ATOM   8766  C  CG2 . VAL A 1 1149 ? -37.600  37.175  -26.718 1.00 71.46  ? 1149 VAL A CG2 1 
ATOM   8767  N  N   . ILE A 1 1150 ? -39.134  33.913  -23.845 1.00 82.94  ? 1150 ILE A N   1 
ATOM   8768  C  CA  . ILE A 1 1150 ? -40.001  32.852  -23.328 1.00 77.71  ? 1150 ILE A CA  1 
ATOM   8769  C  C   . ILE A 1 1150 ? -40.860  33.335  -22.193 1.00 76.85  ? 1150 ILE A C   1 
ATOM   8770  O  O   . ILE A 1 1150 ? -41.981  32.887  -22.030 1.00 77.33  ? 1150 ILE A O   1 
ATOM   8771  C  CB  . ILE A 1 1150 ? -39.147  31.712  -22.795 1.00 73.61  ? 1150 ILE A CB  1 
ATOM   8772  C  CG1 . ILE A 1 1150 ? -37.821  31.712  -23.573 1.00 75.53  ? 1150 ILE A CG1 1 
ATOM   8773  C  CG2 . ILE A 1 1150 ? -39.928  30.391  -22.781 1.00 67.90  ? 1150 ILE A CG2 1 
ATOM   8774  C  CD1 . ILE A 1 1150 ? -37.122  30.424  -23.649 1.00 76.71  ? 1150 ILE A CD1 1 
ATOM   8775  N  N   . GLY A 1 1151 ? -40.312  34.240  -21.393 1.00 76.92  ? 1151 GLY A N   1 
ATOM   8776  C  CA  . GLY A 1 1151 ? -41.044  34.817  -20.284 1.00 78.60  ? 1151 GLY A CA  1 
ATOM   8777  C  C   . GLY A 1 1151 ? -42.145  35.746  -20.769 1.00 80.43  ? 1151 GLY A C   1 
ATOM   8778  O  O   . GLY A 1 1151 ? -43.326  35.519  -20.484 1.00 80.67  ? 1151 GLY A O   1 
ATOM   8779  N  N   . ILE A 1 1152 ? -41.760  36.789  -21.505 1.00 82.97  ? 1152 ILE A N   1 
ATOM   8780  C  CA  . ILE A 1 1152 ? -42.722  37.779  -21.979 1.00 85.72  ? 1152 ILE A CA  1 
ATOM   8781  C  C   . ILE A 1 1152 ? -43.731  37.069  -22.834 1.00 89.43  ? 1152 ILE A C   1 
ATOM   8782  O  O   . ILE A 1 1152 ? -44.935  37.279  -22.739 1.00 90.66  ? 1152 ILE A O   1 
ATOM   8783  C  CB  . ILE A 1 1152 ? -42.042  38.827  -22.843 1.00 82.81  ? 1152 ILE A CB  1 
ATOM   8784  C  CG1 . ILE A 1 1152 ? -40.892  39.452  -22.048 1.00 78.45  ? 1152 ILE A CG1 1 
ATOM   8785  C  CG2 . ILE A 1 1152 ? -43.104  39.828  -23.382 1.00 53.11  ? 1152 ILE A CG2 1 
ATOM   8786  C  CD1 . ILE A 1 1152 ? -39.817  40.128  -22.856 1.00 75.39  ? 1152 ILE A CD1 1 
ATOM   8787  N  N   . ARG A 1 1153 ? -43.190  36.219  -23.685 1.00 90.96  ? 1153 ARG A N   1 
ATOM   8788  C  CA  . ARG A 1 1153 ? -43.969  35.304  -24.465 1.00 92.61  ? 1153 ARG A CA  1 
ATOM   8789  C  C   . ARG A 1 1153 ? -44.923  34.528  -23.583 1.00 89.74  ? 1153 ARG A C   1 
ATOM   8790  O  O   . ARG A 1 1153 ? -46.105  34.474  -23.868 1.00 91.62  ? 1153 ARG A O   1 
ATOM   8791  C  CB  . ARG A 1 1153 ? -43.032  34.339  -25.186 1.00 97.69  ? 1153 ARG A CB  1 
ATOM   8792  C  CG  . ARG A 1 1153 ? -42.392  34.923  -26.440 1.00 104.24 ? 1153 ARG A CG  1 
ATOM   8793  C  CD  . ARG A 1 1153 ? -43.478  35.372  -27.427 1.00 108.99 ? 1153 ARG A CD  1 
ATOM   8794  N  NE  . ARG A 1 1153 ? -43.005  35.557  -28.799 1.00 110.51 ? 1153 ARG A NE  1 
ATOM   8795  C  CZ  . ARG A 1 1153 ? -43.677  36.248  -29.710 1.00 111.44 ? 1153 ARG A CZ  1 
ATOM   8796  N  NH1 . ARG A 1 1153 ? -44.830  36.824  -29.396 1.00 110.43 ? 1153 ARG A NH1 1 
ATOM   8797  N  NH2 . ARG A 1 1153 ? -43.193  36.376  -30.931 1.00 114.01 ? 1153 ARG A NH2 1 
ATOM   8798  N  N   . LYS A 1 1154 ? -44.417  33.932  -22.509 1.00 86.68  ? 1154 LYS A N   1 
ATOM   8799  C  CA  . LYS A 1 1154 ? -45.215  32.984  -21.729 1.00 86.02  ? 1154 LYS A CA  1 
ATOM   8800  C  C   . LYS A 1 1154 ? -46.427  33.648  -21.101 1.00 89.93  ? 1154 LYS A C   1 
ATOM   8801  O  O   . LYS A 1 1154 ? -47.480  33.019  -20.913 1.00 89.11  ? 1154 LYS A O   1 
ATOM   8802  C  CB  . LYS A 1 1154 ? -44.369  32.342  -20.631 1.00 83.85  ? 1154 LYS A CB  1 
ATOM   8803  C  CG  . LYS A 1 1154 ? -43.708  31.047  -21.020 1.00 82.02  ? 1154 LYS A CG  1 
ATOM   8804  C  CD  . LYS A 1 1154 ? -44.659  29.888  -20.886 1.00 82.28  ? 1154 LYS A CD  1 
ATOM   8805  C  CE  . LYS A 1 1154 ? -43.908  28.593  -21.088 1.00 82.29  ? 1154 LYS A CE  1 
ATOM   8806  N  NZ  . LYS A 1 1154 ? -44.466  27.515  -20.234 1.00 82.57  ? 1154 LYS A NZ  1 
ATOM   8807  N  N   . ALA A 1 1155 ? -46.254  34.928  -20.785 1.00 94.17  ? 1155 ALA A N   1 
ATOM   8808  C  CA  . ALA A 1 1155 ? -47.184  35.676  -19.956 1.00 98.15  ? 1155 ALA A CA  1 
ATOM   8809  C  C   . ALA A 1 1155 ? -47.864  36.787  -20.736 1.00 105.53 ? 1155 ALA A C   1 
ATOM   8810  O  O   . ALA A 1 1155 ? -48.794  37.406  -20.231 1.00 108.35 ? 1155 ALA A O   1 
ATOM   8811  C  CB  . ALA A 1 1155 ? -46.445  36.260  -18.772 1.00 95.73  ? 1155 ALA A CB  1 
ATOM   8812  N  N   . PHE A 1 1156 ? -47.396  37.041  -21.960 1.00 109.16 ? 1156 PHE A N   1 
ATOM   8813  C  CA  . PHE A 1 1156 ? -47.835  38.206  -22.742 1.00 113.42 ? 1156 PHE A CA  1 
ATOM   8814  C  C   . PHE A 1 1156 ? -49.343  38.342  -22.755 1.00 113.00 ? 1156 PHE A C   1 
ATOM   8815  O  O   . PHE A 1 1156 ? -49.887  39.448  -22.804 1.00 114.21 ? 1156 PHE A O   1 
ATOM   8816  C  CB  . PHE A 1 1156 ? -47.301  38.138  -24.187 1.00 115.35 ? 1156 PHE A CB  1 
ATOM   8817  C  CG  . PHE A 1 1156 ? -47.997  39.084  -25.157 1.00 118.01 ? 1156 PHE A CG  1 
ATOM   8818  C  CD1 . PHE A 1 1156 ? -47.565  40.393  -25.306 1.00 120.01 ? 1156 PHE A CD1 1 
ATOM   8819  C  CD2 . PHE A 1 1156 ? -49.068  38.651  -25.931 1.00 118.89 ? 1156 PHE A CD2 1 
ATOM   8820  C  CE1 . PHE A 1 1156 ? -48.194  41.252  -26.184 1.00 121.47 ? 1156 PHE A CE1 1 
ATOM   8821  C  CE2 . PHE A 1 1156 ? -49.697  39.502  -26.814 1.00 120.62 ? 1156 PHE A CE2 1 
ATOM   8822  C  CZ  . PHE A 1 1156 ? -49.257  40.805  -26.940 1.00 122.40 ? 1156 PHE A CZ  1 
ATOM   8823  N  N   . ASP A 1 1157 ? -50.017  37.206  -22.684 1.00 111.26 ? 1157 ASP A N   1 
ATOM   8824  C  CA  . ASP A 1 1157 ? -51.444  37.200  -22.925 1.00 113.14 ? 1157 ASP A CA  1 
ATOM   8825  C  C   . ASP A 1 1157 ? -52.335  37.958  -21.918 1.00 113.60 ? 1157 ASP A C   1 
ATOM   8826  O  O   . ASP A 1 1157 ? -53.491  38.223  -22.238 1.00 114.08 ? 1157 ASP A O   1 
ATOM   8827  C  CB  . ASP A 1 1157 ? -51.942  35.775  -23.159 1.00 116.23 ? 1157 ASP A CB  1 
ATOM   8828  C  CG  . ASP A 1 1157 ? -52.099  35.461  -24.642 1.00 122.37 ? 1157 ASP A CG  1 
ATOM   8829  O  OD1 . ASP A 1 1157 ? -52.163  36.440  -25.436 1.00 125.23 ? 1157 ASP A OD1 1 
ATOM   8830  O  OD2 . ASP A 1 1157 ? -52.168  34.256  -25.013 1.00 122.86 ? 1157 ASP A OD2 1 
ATOM   8831  N  N   . ILE A 1 1158 ? -51.830  38.310  -20.728 1.00 112.34 ? 1158 ILE A N   1 
ATOM   8832  C  CA  . ILE A 1 1158 ? -52.655  39.024  -19.748 1.00 108.51 ? 1158 ILE A CA  1 
ATOM   8833  C  C   . ILE A 1 1158 ? -52.426  40.482  -19.885 1.00 112.96 ? 1158 ILE A C   1 
ATOM   8834  O  O   . ILE A 1 1158 ? -53.025  41.286  -19.170 1.00 116.62 ? 1158 ILE A O   1 
ATOM   8835  C  CB  . ILE A 1 1158 ? -52.271  38.744  -18.331 1.00 101.00 ? 1158 ILE A CB  1 
ATOM   8836  C  CG1 . ILE A 1 1158 ? -51.340  37.528  -18.256 1.00 93.06  ? 1158 ILE A CG1 1 
ATOM   8837  C  CG2 . ILE A 1 1158 ? -53.547  38.675  -17.486 1.00 100.09 ? 1158 ILE A CG2 1 
ATOM   8838  C  CD1 . ILE A 1 1158 ? -50.445  37.529  -17.076 1.00 89.95  ? 1158 ILE A CD1 1 
ATOM   8839  N  N   . CYS A 1 1159 ? -51.508  40.820  -20.777 1.00 112.60 ? 1159 CYS A N   1 
ATOM   8840  C  CA  . CYS A 1 1159 ? -51.215  42.210  -21.024 1.00 115.53 ? 1159 CYS A CA  1 
ATOM   8841  C  C   . CYS A 1 1159 ? -50.774  42.457  -22.462 1.00 119.42 ? 1159 CYS A C   1 
ATOM   8842  O  O   . CYS A 1 1159 ? -49.832  43.229  -22.676 1.00 122.15 ? 1159 CYS A O   1 
ATOM   8843  C  CB  . CYS A 1 1159 ? -50.139  42.707  -20.046 1.00 111.84 ? 1159 CYS A CB  1 
ATOM   8844  S  SG  . CYS A 1 1159 ? -50.181  44.499  -19.762 1.00 174.89 ? 1159 CYS A SG  1 
ATOM   8845  N  N   . PRO A 1 1160 ? -51.438  41.815  -23.450 1.00 122.82 ? 1160 PRO A N   1 
ATOM   8846  C  CA  . PRO A 1 1160 ? -51.109  42.216  -24.818 1.00 121.56 ? 1160 PRO A CA  1 
ATOM   8847  C  C   . PRO A 1 1160 ? -51.124  43.726  -24.856 1.00 122.86 ? 1160 PRO A C   1 
ATOM   8848  O  O   . PRO A 1 1160 ? -52.125  44.346  -24.509 1.00 122.37 ? 1160 PRO A O   1 
ATOM   8849  C  CB  . PRO A 1 1160 ? -52.264  41.635  -25.640 1.00 125.07 ? 1160 PRO A CB  1 
ATOM   8850  C  CG  . PRO A 1 1160 ? -53.313  41.262  -24.623 1.00 126.05 ? 1160 PRO A CG  1 
ATOM   8851  C  CD  . PRO A 1 1160 ? -52.522  40.827  -23.446 1.00 123.55 ? 1160 PRO A CD  1 
ATOM   8852  N  N   . LEU A 1 1161 ? -50.001  44.311  -25.240 1.00 121.74 ? 1161 LEU A N   1 
ATOM   8853  C  CA  . LEU A 1 1161 ? -49.788  45.728  -25.034 1.00 123.76 ? 1161 LEU A CA  1 
ATOM   8854  C  C   . LEU A 1 1161 ? -48.985  46.189  -26.218 1.00 126.44 ? 1161 LEU A C   1 
ATOM   8855  O  O   . LEU A 1 1161 ? -47.874  45.701  -26.445 1.00 126.47 ? 1161 LEU A O   1 
ATOM   8856  C  CB  . LEU A 1 1161 ? -48.983  45.953  -23.754 1.00 119.52 ? 1161 LEU A CB  1 
ATOM   8857  C  CG  . LEU A 1 1161 ? -49.020  47.346  -23.138 1.00 117.70 ? 1161 LEU A CG  1 
ATOM   8858  C  CD1 . LEU A 1 1161 ? -49.771  48.353  -24.053 1.00 111.88 ? 1161 LEU A CD1 1 
ATOM   8859  C  CD2 . LEU A 1 1161 ? -49.648  47.259  -21.768 1.00 114.55 ? 1161 LEU A CD2 1 
ATOM   8860  N  N   . VAL A 1 1162 ? -49.542  47.121  -26.981 1.00 129.53 ? 1162 VAL A N   1 
ATOM   8861  C  CA  . VAL A 1 1162 ? -48.917  47.483  -28.238 1.00 132.16 ? 1162 VAL A CA  1 
ATOM   8862  C  C   . VAL A 1 1162 ? -47.439  47.563  -27.967 1.00 131.36 ? 1162 VAL A C   1 
ATOM   8863  O  O   . VAL A 1 1162 ? -46.633  46.897  -28.618 1.00 128.20 ? 1162 VAL A O   1 
ATOM   8864  C  CB  . VAL A 1 1162 ? -49.412  48.841  -28.773 1.00 139.07 ? 1162 VAL A CB  1 
ATOM   8865  C  CG1 . VAL A 1 1162 ? -50.362  48.648  -29.971 1.00 140.15 ? 1162 VAL A CG1 1 
ATOM   8866  C  CG2 . VAL A 1 1162 ? -50.038  49.678  -27.634 1.00 142.46 ? 1162 VAL A CG2 1 
ATOM   8867  N  N   . LYS A 1 1163 ? -47.100  48.339  -26.948 1.00 133.59 ? 1163 LYS A N   1 
ATOM   8868  C  CA  . LYS A 1 1163 ? -45.717  48.697  -26.724 1.00 134.74 ? 1163 LYS A CA  1 
ATOM   8869  C  C   . LYS A 1 1163 ? -44.833  47.480  -26.531 1.00 132.78 ? 1163 LYS A C   1 
ATOM   8870  O  O   . LYS A 1 1163 ? -43.654  47.497  -26.889 1.00 132.46 ? 1163 LYS A O   1 
ATOM   8871  C  CB  . LYS A 1 1163 ? -45.584  49.661  -25.549 1.00 135.27 ? 1163 LYS A CB  1 
ATOM   8872  C  CG  . LYS A 1 1163 ? -44.417  50.600  -25.725 1.00 135.35 ? 1163 LYS A CG  1 
ATOM   8873  C  CD  . LYS A 1 1163 ? -44.189  51.432  -24.502 1.00 135.73 ? 1163 LYS A CD  1 
ATOM   8874  C  CE  . LYS A 1 1163 ? -42.885  52.176  -24.619 1.00 136.28 ? 1163 LYS A CE  1 
ATOM   8875  N  NZ  . LYS A 1 1163 ? -42.309  52.390  -23.272 1.00 136.66 ? 1163 LYS A NZ  1 
ATOM   8876  N  N   . ILE A 1 1164 ? -45.392  46.419  -25.970 1.00 131.88 ? 1164 ILE A N   1 
ATOM   8877  C  CA  . ILE A 1 1164 ? -44.567  45.261  -25.681 1.00 132.17 ? 1164 ILE A CA  1 
ATOM   8878  C  C   . ILE A 1 1164 ? -44.653  44.195  -26.771 1.00 132.61 ? 1164 ILE A C   1 
ATOM   8879  O  O   . ILE A 1 1164 ? -43.954  43.182  -26.714 1.00 131.78 ? 1164 ILE A O   1 
ATOM   8880  C  CB  . ILE A 1 1164 ? -44.804  44.687  -24.245 1.00 107.74 ? 1164 ILE A CB  1 
ATOM   8881  C  CG1 . ILE A 1 1164 ? -45.526  43.345  -24.274 1.00 106.09 ? 1164 ILE A CG1 1 
ATOM   8882  C  CG2 . ILE A 1 1164 ? -45.528  45.691  -23.341 1.00 108.38 ? 1164 ILE A CG2 1 
ATOM   8883  C  CD1 . ILE A 1 1164 ? -45.776  42.830  -22.875 1.00 105.65 ? 1164 ILE A CD1 1 
ATOM   8884  N  N   . ASP A 1 1165 ? -45.497  44.434  -27.773 1.00 136.50 ? 1165 ASP A N   1 
ATOM   8885  C  CA  . ASP A 1 1165 ? -45.531  43.565  -28.958 1.00 136.95 ? 1165 ASP A CA  1 
ATOM   8886  C  C   . ASP A 1 1165 ? -44.362  43.915  -29.865 1.00 136.74 ? 1165 ASP A C   1 
ATOM   8887  O  O   . ASP A 1 1165 ? -43.604  43.047  -30.291 1.00 134.73 ? 1165 ASP A O   1 
ATOM   8888  C  CB  . ASP A 1 1165 ? -46.854  43.698  -29.722 1.00 139.94 ? 1165 ASP A CB  1 
ATOM   8889  C  CG  . ASP A 1 1165 ? -46.907  42.825  -30.969 1.00 139.81 ? 1165 ASP A CG  1 
ATOM   8890  O  OD1 . ASP A 1 1165 ? -46.600  41.606  -30.895 1.00 137.25 ? 1165 ASP A OD1 1 
ATOM   8891  O  OD2 . ASP A 1 1165 ? -47.277  43.378  -32.027 1.00 141.98 ? 1165 ASP A OD2 1 
ATOM   8892  N  N   . THR A 1 1166 ? -44.235  45.207  -30.145 1.00 137.69 ? 1166 THR A N   1 
ATOM   8893  C  CA  . THR A 1 1166 ? -43.028  45.767  -30.733 1.00 138.23 ? 1166 THR A CA  1 
ATOM   8894  C  C   . THR A 1 1166 ? -41.790  45.162  -30.093 1.00 136.05 ? 1166 THR A C   1 
ATOM   8895  O  O   . THR A 1 1166 ? -40.967  44.546  -30.774 1.00 136.19 ? 1166 THR A O   1 
ATOM   8896  C  CB  . THR A 1 1166 ? -42.948  47.273  -30.479 1.00 140.97 ? 1166 THR A CB  1 
ATOM   8897  O  OG1 . THR A 1 1166 ? -43.984  47.931  -31.214 1.00 143.51 ? 1166 THR A OG1 1 
ATOM   8898  C  CG2 . THR A 1 1166 ? -41.576  47.819  -30.892 1.00 141.50 ? 1166 THR A CG2 1 
ATOM   8899  N  N   . ALA A 1 1167 ? -41.653  45.352  -28.783 1.00 132.65 ? 1167 ALA A N   1 
ATOM   8900  C  CA  . ALA A 1 1167 ? -40.509  44.825  -28.053 1.00 128.09 ? 1167 ALA A CA  1 
ATOM   8901  C  C   . ALA A 1 1167 ? -40.322  43.339  -28.326 1.00 120.97 ? 1167 ALA A C   1 
ATOM   8902  O  O   . ALA A 1 1167 ? -39.206  42.896  -28.608 1.00 119.12 ? 1167 ALA A O   1 
ATOM   8903  C  CB  . ALA A 1 1167 ? -40.674  45.066  -26.582 1.00 128.00 ? 1167 ALA A CB  1 
ATOM   8904  N  N   . LEU A 1 1168 ? -41.411  42.575  -28.248 1.00 117.96 ? 1168 LEU A N   1 
ATOM   8905  C  CA  . LEU A 1 1168 ? -41.332  41.132  -28.443 1.00 114.67 ? 1168 LEU A CA  1 
ATOM   8906  C  C   . LEU A 1 1168 ? -40.691  40.797  -29.769 1.00 119.72 ? 1168 LEU A C   1 
ATOM   8907  O  O   . LEU A 1 1168 ? -39.945  39.828  -29.897 1.00 120.57 ? 1168 LEU A O   1 
ATOM   8908  C  CB  . LEU A 1 1168 ? -42.708  40.493  -28.357 1.00 109.14 ? 1168 LEU A CB  1 
ATOM   8909  C  CG  . LEU A 1 1168 ? -42.730  39.624  -27.108 1.00 106.30 ? 1168 LEU A CG  1 
ATOM   8910  C  CD1 . LEU A 1 1168 ? -43.994  38.784  -27.036 1.00 105.91 ? 1168 LEU A CD1 1 
ATOM   8911  C  CD2 . LEU A 1 1168 ? -41.472  38.758  -27.095 1.00 103.23 ? 1168 LEU A CD2 1 
ATOM   8912  N  N   . ILE A 1 1169 ? -40.999  41.623  -30.756 1.00 122.80 ? 1169 ILE A N   1 
ATOM   8913  C  CA  . ILE A 1 1169 ? -40.504  41.450  -32.107 1.00 120.46 ? 1169 ILE A CA  1 
ATOM   8914  C  C   . ILE A 1 1169 ? -39.045  41.853  -32.203 1.00 121.55 ? 1169 ILE A C   1 
ATOM   8915  O  O   . ILE A 1 1169 ? -38.209  41.032  -32.533 1.00 120.31 ? 1169 ILE A O   1 
ATOM   8916  C  CB  . ILE A 1 1169 ? -41.380  42.236  -33.084 1.00 119.92 ? 1169 ILE A CB  1 
ATOM   8917  C  CG1 . ILE A 1 1169 ? -42.511  41.329  -33.594 1.00 116.84 ? 1169 ILE A CG1 1 
ATOM   8918  C  CG2 . ILE A 1 1169 ? -40.543  42.800  -34.205 1.00 120.56 ? 1169 ILE A CG2 1 
ATOM   8919  C  CD1 . ILE A 1 1169 ? -43.831  42.025  -33.777 1.00 116.93 ? 1169 ILE A CD1 1 
ATOM   8920  N  N   . LYS A 1 1170 ? -38.744  43.108  -31.882 1.00 124.55 ? 1170 LYS A N   1 
ATOM   8921  C  CA  . LYS A 1 1170 ? -37.368  43.590  -31.846 1.00 128.13 ? 1170 LYS A CA  1 
ATOM   8922  C  C   . LYS A 1 1170 ? -36.501  42.553  -31.168 1.00 123.25 ? 1170 LYS A C   1 
ATOM   8923  O  O   . LYS A 1 1170 ? -35.343  42.356  -31.519 1.00 121.75 ? 1170 LYS A O   1 
ATOM   8924  C  CB  . LYS A 1 1170 ? -37.271  44.896  -31.055 1.00 135.91 ? 1170 LYS A CB  1 
ATOM   8925  C  CG  . LYS A 1 1170 ? -38.000  46.074  -31.672 1.00 144.65 ? 1170 LYS A CG  1 
ATOM   8926  C  CD  . LYS A 1 1170 ? -37.591  46.260  -33.122 1.00 152.39 ? 1170 LYS A CD  1 
ATOM   8927  C  CE  . LYS A 1 1170 ? -36.163  46.803  -33.257 1.00 158.40 ? 1170 LYS A CE  1 
ATOM   8928  N  NZ  . LYS A 1 1170 ? -35.722  46.923  -34.697 1.00 160.71 ? 1170 LYS A NZ  1 
ATOM   8929  N  N   . ALA A 1 1171 ? -37.081  41.899  -30.176 1.00 121.30 ? 1171 ALA A N   1 
ATOM   8930  C  CA  . ALA A 1 1171 ? -36.409  40.822  -29.485 1.00 121.59 ? 1171 ALA A CA  1 
ATOM   8931  C  C   . ALA A 1 1171 ? -36.310  39.605  -30.388 1.00 121.03 ? 1171 ALA A C   1 
ATOM   8932  O  O   . ALA A 1 1171 ? -35.216  39.162  -30.712 1.00 121.26 ? 1171 ALA A O   1 
ATOM   8933  C  CB  . ALA A 1 1171 ? -37.157  40.475  -28.232 1.00 122.00 ? 1171 ALA A CB  1 
ATOM   8934  N  N   . ASP A 1 1172 ? -37.462  39.066  -30.781 1.00 121.59 ? 1172 ASP A N   1 
ATOM   8935  C  CA  . ASP A 1 1172 ? -37.536  37.917  -31.680 1.00 121.35 ? 1172 ASP A CA  1 
ATOM   8936  C  C   . ASP A 1 1172 ? -36.582  38.085  -32.853 1.00 122.41 ? 1172 ASP A C   1 
ATOM   8937  O  O   . ASP A 1 1172 ? -35.959  37.122  -33.309 1.00 120.68 ? 1172 ASP A O   1 
ATOM   8938  C  CB  . ASP A 1 1172 ? -38.951  37.799  -32.232 1.00 123.15 ? 1172 ASP A CB  1 
ATOM   8939  C  CG  . ASP A 1 1172 ? -39.725  36.651  -31.631 1.00 124.38 ? 1172 ASP A CG  1 
ATOM   8940  O  OD1 . ASP A 1 1172 ? -39.216  35.979  -30.709 1.00 124.11 ? 1172 ASP A OD1 1 
ATOM   8941  O  OD2 . ASP A 1 1172 ? -40.854  36.414  -32.102 1.00 125.84 ? 1172 ASP A OD2 1 
ATOM   8942  N  N   . ASN A 1 1173 ? -36.501  39.323  -33.344 1.00 125.13 ? 1173 ASN A N   1 
ATOM   8943  C  CA  . ASN A 1 1173 ? -35.648  39.691  -34.470 1.00 127.87 ? 1173 ASN A CA  1 
ATOM   8944  C  C   . ASN A 1 1173 ? -34.198  39.341  -34.181 1.00 125.74 ? 1173 ASN A C   1 
ATOM   8945  O  O   . ASN A 1 1173 ? -33.604  38.519  -34.872 1.00 125.59 ? 1173 ASN A O   1 
ATOM   8946  C  CB  . ASN A 1 1173 ? -35.789  41.188  -34.803 1.00 134.94 ? 1173 ASN A CB  1 
ATOM   8947  C  CG  . ASN A 1 1173 ? -36.806  41.460  -35.926 1.00 141.41 ? 1173 ASN A CG  1 
ATOM   8948  O  OD1 . ASN A 1 1173 ? -36.644  42.403  -36.706 1.00 145.65 ? 1173 ASN A OD1 1 
ATOM   8949  N  ND2 . ASN A 1 1173 ? -37.850  40.635  -36.010 1.00 141.32 ? 1173 ASN A ND2 1 
ATOM   8950  N  N   . PHE A 1 1174 ? -33.639  39.944  -33.141 1.00 124.48 ? 1174 PHE A N   1 
ATOM   8951  C  CA  . PHE A 1 1174 ? -32.268  39.659  -32.740 1.00 123.39 ? 1174 PHE A CA  1 
ATOM   8952  C  C   . PHE A 1 1174 ? -31.950  38.175  -32.799 1.00 119.51 ? 1174 PHE A C   1 
ATOM   8953  O  O   . PHE A 1 1174 ? -30.927  37.775  -33.336 1.00 120.91 ? 1174 PHE A O   1 
ATOM   8954  C  CB  . PHE A 1 1174 ? -32.015  40.189  -31.331 1.00 123.13 ? 1174 PHE A CB  1 
ATOM   8955  C  CG  . PHE A 1 1174 ? -30.672  39.817  -30.764 1.00 121.60 ? 1174 PHE A CG  1 
ATOM   8956  C  CD1 . PHE A 1 1174 ? -29.552  40.570  -31.049 1.00 123.16 ? 1174 PHE A CD1 1 
ATOM   8957  C  CD2 . PHE A 1 1174 ? -30.539  38.726  -29.924 1.00 119.78 ? 1174 PHE A CD2 1 
ATOM   8958  C  CE1 . PHE A 1 1174 ? -28.319  40.231  -30.510 1.00 123.88 ? 1174 PHE A CE1 1 
ATOM   8959  C  CE2 . PHE A 1 1174 ? -29.312  38.388  -29.383 1.00 120.01 ? 1174 PHE A CE2 1 
ATOM   8960  C  CZ  . PHE A 1 1174 ? -28.203  39.139  -29.676 1.00 122.16 ? 1174 PHE A CZ  1 
ATOM   8961  N  N   . LEU A 1 1175 ? -32.841  37.358  -32.260 1.00 116.19 ? 1175 LEU A N   1 
ATOM   8962  C  CA  . LEU A 1 1175 ? -32.594  35.922  -32.177 1.00 114.54 ? 1175 LEU A CA  1 
ATOM   8963  C  C   . LEU A 1 1175 ? -32.486  35.254  -33.557 1.00 113.93 ? 1175 LEU A C   1 
ATOM   8964  O  O   . LEU A 1 1175 ? -31.538  34.523  -33.827 1.00 113.00 ? 1175 LEU A O   1 
ATOM   8965  C  CB  . LEU A 1 1175 ? -33.664  35.243  -31.310 1.00 113.69 ? 1175 LEU A CB  1 
ATOM   8966  C  CG  . LEU A 1 1175 ? -33.701  35.626  -29.825 1.00 113.41 ? 1175 LEU A CG  1 
ATOM   8967  C  CD1 . LEU A 1 1175 ? -34.883  34.949  -29.136 1.00 111.62 ? 1175 LEU A CD1 1 
ATOM   8968  C  CD2 . LEU A 1 1175 ? -32.380  35.281  -29.130 1.00 113.61 ? 1175 LEU A CD2 1 
ATOM   8969  N  N   . LEU A 1 1176 ? -33.457  35.507  -34.427 1.00 114.25 ? 1176 LEU A N   1 
ATOM   8970  C  CA  . LEU A 1 1176 ? -33.364  35.061  -35.805 1.00 114.80 ? 1176 LEU A CA  1 
ATOM   8971  C  C   . LEU A 1 1176 ? -32.042  35.508  -36.387 1.00 121.43 ? 1176 LEU A C   1 
ATOM   8972  O  O   . LEU A 1 1176 ? -31.280  34.719  -36.953 1.00 123.34 ? 1176 LEU A O   1 
ATOM   8973  C  CB  . LEU A 1 1176 ? -34.458  35.712  -36.619 1.00 110.64 ? 1176 LEU A CB  1 
ATOM   8974  C  CG  . LEU A 1 1176 ? -35.858  35.285  -36.277 1.00 105.74 ? 1176 LEU A CG  1 
ATOM   8975  C  CD1 . LEU A 1 1176 ? -36.778  35.936  -37.267 1.00 105.42 ? 1176 LEU A CD1 1 
ATOM   8976  C  CD2 . LEU A 1 1176 ? -35.947  33.781  -36.374 1.00 103.95 ? 1176 LEU A CD2 1 
ATOM   8977  N  N   . GLU A 1 1177 ? -31.795  36.805  -36.243 1.00 125.13 ? 1177 GLU A N   1 
ATOM   8978  C  CA  . GLU A 1 1177 ? -30.653  37.460  -36.850 1.00 129.78 ? 1177 GLU A CA  1 
ATOM   8979  C  C   . GLU A 1 1177 ? -29.339  37.109  -36.166 1.00 130.36 ? 1177 GLU A C   1 
ATOM   8980  O  O   . GLU A 1 1177 ? -28.287  37.450  -36.700 1.00 134.00 ? 1177 GLU A O   1 
ATOM   8981  C  CB  . GLU A 1 1177 ? -30.834  38.986  -36.838 1.00 135.74 ? 1177 GLU A CB  1 
ATOM   8982  C  CG  . GLU A 1 1177 ? -31.710  39.562  -37.957 1.00 141.21 ? 1177 GLU A CG  1 
ATOM   8983  C  CD  . GLU A 1 1177 ? -31.371  41.018  -38.254 1.00 148.36 ? 1177 GLU A CD  1 
ATOM   8984  O  OE1 . GLU A 1 1177 ? -31.253  41.384  -39.449 1.00 151.33 ? 1177 GLU A OE1 1 
ATOM   8985  O  OE2 . GLU A 1 1177 ? -31.201  41.795  -37.287 1.00 150.70 ? 1177 GLU A OE2 1 
ATOM   8986  N  N   . ASN A 1 1178 ? -29.383  36.426  -35.013 1.00 127.08 ? 1178 ASN A N   1 
ATOM   8987  C  CA  . ASN A 1 1178 ? -28.169  36.224  -34.190 1.00 124.90 ? 1178 ASN A CA  1 
ATOM   8988  C  C   . ASN A 1 1178 ? -27.882  34.857  -33.556 1.00 121.48 ? 1178 ASN A C   1 
ATOM   8989  O  O   . ASN A 1 1178 ? -26.929  34.718  -32.775 1.00 122.22 ? 1178 ASN A O   1 
ATOM   8990  C  CB  . ASN A 1 1178 ? -28.077  37.289  -33.104 1.00 123.71 ? 1178 ASN A CB  1 
ATOM   8991  C  CG  . ASN A 1 1178 ? -26.977  38.263  -33.359 1.00 123.92 ? 1178 ASN A CG  1 
ATOM   8992  O  OD1 . ASN A 1 1178 ? -25.804  37.888  -33.394 1.00 124.29 ? 1178 ASN A OD1 1 
ATOM   8993  N  ND2 . ASN A 1 1178 ? -27.337  39.527  -33.549 1.00 124.33 ? 1178 ASN A ND2 1 
ATOM   8994  N  N   . THR A 1 1179 ? -28.692  33.862  -33.888 1.00 117.45 ? 1179 THR A N   1 
ATOM   8995  C  CA  . THR A 1 1179 ? -28.470  32.503  -33.426 1.00 114.40 ? 1179 THR A CA  1 
ATOM   8996  C  C   . THR A 1 1179 ? -27.468  31.773  -34.312 1.00 112.69 ? 1179 THR A C   1 
ATOM   8997  O  O   . THR A 1 1179 ? -26.428  31.299  -33.849 1.00 111.41 ? 1179 THR A O   1 
ATOM   8998  C  CB  . THR A 1 1179 ? -29.808  31.703  -33.491 1.00 98.85  ? 1179 THR A CB  1 
ATOM   8999  O  OG1 . THR A 1 1179 ? -30.858  32.465  -32.882 1.00 99.34  ? 1179 THR A OG1 1 
ATOM   9000  C  CG2 . THR A 1 1179 ? -29.709  30.301  -32.836 1.00 89.90  ? 1179 THR A CG2 1 
ATOM   9001  N  N   . LEU A 1 1180 ? -27.772  31.754  -35.606 1.00 112.69 ? 1180 LEU A N   1 
ATOM   9002  C  CA  . LEU A 1 1180 ? -27.593  30.531  -36.385 1.00 113.08 ? 1180 LEU A CA  1 
ATOM   9003  C  C   . LEU A 1 1180 ? -26.229  29.943  -36.656 1.00 119.97 ? 1180 LEU A C   1 
ATOM   9004  O  O   . LEU A 1 1180 ? -26.130  28.706  -36.773 1.00 120.91 ? 1180 LEU A O   1 
ATOM   9005  C  CB  . LEU A 1 1180 ? -28.462  30.510  -37.633 1.00 108.92 ? 1180 LEU A CB  1 
ATOM   9006  C  CG  . LEU A 1 1180 ? -29.602  29.530  -37.303 1.00 103.18 ? 1180 LEU A CG  1 
ATOM   9007  C  CD1 . LEU A 1 1180 ? -30.554  29.332  -38.458 1.00 101.31 ? 1180 LEU A CD1 1 
ATOM   9008  C  CD2 . LEU A 1 1180 ? -29.024  28.206  -36.828 1.00 101.40 ? 1180 LEU A CD2 1 
ATOM   9009  N  N   . PRO A 1 1181 ? -25.186  30.798  -36.786 1.00 122.29 ? 1181 PRO A N   1 
ATOM   9010  C  CA  . PRO A 1 1181 ? -23.827  30.257  -36.643 1.00 122.43 ? 1181 PRO A CA  1 
ATOM   9011  C  C   . PRO A 1 1181 ? -23.753  29.832  -35.187 1.00 121.38 ? 1181 PRO A C   1 
ATOM   9012  O  O   . PRO A 1 1181 ? -23.191  30.543  -34.358 1.00 121.12 ? 1181 PRO A O   1 
ATOM   9013  C  CB  . PRO A 1 1181 ? -22.934  31.464  -36.905 1.00 122.09 ? 1181 PRO A CB  1 
ATOM   9014  C  CG  . PRO A 1 1181 ? -23.788  32.432  -37.643 1.00 121.82 ? 1181 PRO A CG  1 
ATOM   9015  C  CD  . PRO A 1 1181 ? -25.181  32.228  -37.140 1.00 121.16 ? 1181 PRO A CD  1 
ATOM   9016  N  N   . ALA A 1 1182 ? -24.378  28.691  -34.894 1.00 120.66 ? 1182 ALA A N   1 
ATOM   9017  C  CA  . ALA A 1 1182 ? -24.692  28.277  -33.537 1.00 117.92 ? 1182 ALA A CA  1 
ATOM   9018  C  C   . ALA A 1 1182 ? -23.418  28.013  -32.732 1.00 121.66 ? 1182 ALA A C   1 
ATOM   9019  O  O   . ALA A 1 1182 ? -22.509  27.311  -33.192 1.00 124.42 ? 1182 ALA A O   1 
ATOM   9020  C  CB  . ALA A 1 1182 ? -25.614  27.058  -33.556 1.00 112.46 ? 1182 ALA A CB  1 
ATOM   9021  N  N   . GLN A 1 1183 ? -23.362  28.596  -31.531 1.00 120.67 ? 1183 GLN A N   1 
ATOM   9022  C  CA  . GLN A 1 1183 ? -22.181  28.518  -30.670 1.00 119.00 ? 1183 GLN A CA  1 
ATOM   9023  C  C   . GLN A 1 1183 ? -22.257  27.397  -29.638 1.00 113.69 ? 1183 GLN A C   1 
ATOM   9024  O  O   . GLN A 1 1183 ? -21.262  26.729  -29.364 1.00 115.05 ? 1183 GLN A O   1 
ATOM   9025  C  CB  . GLN A 1 1183 ? -21.940  29.855  -29.988 1.00 121.91 ? 1183 GLN A CB  1 
ATOM   9026  C  CG  . GLN A 1 1183 ? -20.596  29.937  -29.342 1.00 126.96 ? 1183 GLN A CG  1 
ATOM   9027  C  CD  . GLN A 1 1183 ? -19.491  29.535  -30.291 1.00 130.92 ? 1183 GLN A CD  1 
ATOM   9028  O  OE1 . GLN A 1 1183 ? -19.731  29.348  -31.490 1.00 131.20 ? 1183 GLN A OE1 1 
ATOM   9029  N  NE2 . GLN A 1 1183 ? -18.265  29.402  -29.766 1.00 133.21 ? 1183 GLN A NE2 1 
ATOM   9030  N  N   . SER A 1 1184 ? -23.446  27.199  -29.074 1.00 108.30 ? 1184 SER A N   1 
ATOM   9031  C  CA  . SER A 1 1184 ? -23.739  25.976  -28.323 1.00 105.90 ? 1184 SER A CA  1 
ATOM   9032  C  C   . SER A 1 1184 ? -25.132  25.384  -28.557 1.00 102.51 ? 1184 SER A C   1 
ATOM   9033  O  O   . SER A 1 1184 ? -26.116  26.108  -28.661 1.00 100.66 ? 1184 SER A O   1 
ATOM   9034  C  CB  . SER A 1 1184 ? -23.611  26.209  -26.832 1.00 107.79 ? 1184 SER A CB  1 
ATOM   9035  O  OG  . SER A 1 1184 ? -24.587  25.421  -26.165 1.00 106.98 ? 1184 SER A OG  1 
ATOM   9036  N  N   . THR A 1 1185 ? -25.201  24.060  -28.589 1.00 100.08 ? 1185 THR A N   1 
ATOM   9037  C  CA  . THR A 1 1185 ? -26.459  23.345  -28.606 1.00 97.11  ? 1185 THR A CA  1 
ATOM   9038  C  C   . THR A 1 1185 ? -27.469  23.856  -27.572 1.00 95.77  ? 1185 THR A C   1 
ATOM   9039  O  O   . THR A 1 1185 ? -28.645  24.070  -27.888 1.00 92.15  ? 1185 THR A O   1 
ATOM   9040  C  CB  . THR A 1 1185 ? -26.207  21.891  -28.314 1.00 96.32  ? 1185 THR A CB  1 
ATOM   9041  O  OG1 . THR A 1 1185 ? -25.441  21.318  -29.389 1.00 96.42  ? 1185 THR A OG1 1 
ATOM   9042  C  CG2 . THR A 1 1185 ? -27.533  21.163  -28.143 1.00 94.12  ? 1185 THR A CG2 1 
ATOM   9043  N  N   . PHE A 1 1186 ? -27.001  24.039  -26.337 1.00 97.93  ? 1186 PHE A N   1 
ATOM   9044  C  CA  . PHE A 1 1186 ? -27.783  24.696  -25.290 1.00 96.64  ? 1186 PHE A CA  1 
ATOM   9045  C  C   . PHE A 1 1186 ? -28.307  26.067  -25.718 1.00 98.48  ? 1186 PHE A C   1 
ATOM   9046  O  O   . PHE A 1 1186 ? -29.512  26.310  -25.693 1.00 98.97  ? 1186 PHE A O   1 
ATOM   9047  C  CB  . PHE A 1 1186 ? -26.967  24.881  -24.009 1.00 94.15  ? 1186 PHE A CB  1 
ATOM   9048  C  CG  . PHE A 1 1186 ? -27.721  25.607  -22.931 1.00 91.29  ? 1186 PHE A CG  1 
ATOM   9049  C  CD1 . PHE A 1 1186 ? -28.457  24.910  -21.988 1.00 89.82  ? 1186 PHE A CD1 1 
ATOM   9050  C  CD2 . PHE A 1 1186 ? -27.732  26.987  -22.883 1.00 91.22  ? 1186 PHE A CD2 1 
ATOM   9051  C  CE1 . PHE A 1 1186 ? -29.180  25.567  -21.018 1.00 88.47  ? 1186 PHE A CE1 1 
ATOM   9052  C  CE2 . PHE A 1 1186 ? -28.447  27.650  -21.905 1.00 90.54  ? 1186 PHE A CE2 1 
ATOM   9053  C  CZ  . PHE A 1 1186 ? -29.177  26.936  -20.981 1.00 89.17  ? 1186 PHE A CZ  1 
ATOM   9054  N  N   . THR A 1 1187 ? -27.399  26.978  -26.072 1.00 99.94  ? 1187 THR A N   1 
ATOM   9055  C  CA  . THR A 1 1187 ? -27.794  28.291  -26.604 1.00 97.77  ? 1187 THR A CA  1 
ATOM   9056  C  C   . THR A 1 1187 ? -28.838  28.144  -27.707 1.00 95.54  ? 1187 THR A C   1 
ATOM   9057  O  O   . THR A 1 1187 ? -29.875  28.819  -27.693 1.00 94.37  ? 1187 THR A O   1 
ATOM   9058  C  CB  . THR A 1 1187 ? -26.599  29.049  -27.220 1.00 97.82  ? 1187 THR A CB  1 
ATOM   9059  O  OG1 . THR A 1 1187 ? -25.493  29.000  -26.318 1.00 97.90  ? 1187 THR A OG1 1 
ATOM   9060  C  CG2 . THR A 1 1187 ? -26.984  30.493  -27.482 1.00 97.83  ? 1187 THR A CG2 1 
ATOM   9061  N  N   . LEU A 1 1188 ? -28.547  27.249  -28.651 1.00 92.92  ? 1188 LEU A N   1 
ATOM   9062  C  CA  . LEU A 1 1188 ? -29.379  27.041  -29.823 1.00 91.71  ? 1188 LEU A CA  1 
ATOM   9063  C  C   . LEU A 1 1188 ? -30.759  26.703  -29.375 1.00 89.86  ? 1188 LEU A C   1 
ATOM   9064  O  O   . LEU A 1 1188 ? -31.723  27.386  -29.696 1.00 89.28  ? 1188 LEU A O   1 
ATOM   9065  C  CB  . LEU A 1 1188 ? -28.848  25.873  -30.638 1.00 91.90  ? 1188 LEU A CB  1 
ATOM   9066  C  CG  . LEU A 1 1188 ? -29.397  25.652  -32.040 1.00 87.58  ? 1188 LEU A CG  1 
ATOM   9067  C  CD1 . LEU A 1 1188 ? -28.988  26.771  -33.013 1.00 86.47  ? 1188 LEU A CD1 1 
ATOM   9068  C  CD2 . LEU A 1 1188 ? -28.875  24.325  -32.497 1.00 86.27  ? 1188 LEU A CD2 1 
ATOM   9069  N  N   . ALA A 1 1189 ? -30.832  25.626  -28.614 1.00 89.02  ? 1189 ALA A N   1 
ATOM   9070  C  CA  . ALA A 1 1189 ? -32.103  25.094  -28.123 1.00 90.74  ? 1189 ALA A CA  1 
ATOM   9071  C  C   . ALA A 1 1189 ? -33.068  26.122  -27.492 1.00 88.78  ? 1189 ALA A C   1 
ATOM   9072  O  O   . ALA A 1 1189 ? -34.268  26.100  -27.758 1.00 86.24  ? 1189 ALA A O   1 
ATOM   9073  C  CB  . ALA A 1 1189 ? -31.835  23.942  -27.140 1.00 91.00  ? 1189 ALA A CB  1 
ATOM   9074  N  N   . ILE A 1 1190 ? -32.557  27.005  -26.641 1.00 92.28  ? 1190 ILE A N   1 
ATOM   9075  C  CA  . ILE A 1 1190 ? -33.419  28.027  -26.065 1.00 93.32  ? 1190 ILE A CA  1 
ATOM   9076  C  C   . ILE A 1 1190 ? -33.824  28.947  -27.208 1.00 93.32  ? 1190 ILE A C   1 
ATOM   9077  O  O   . ILE A 1 1190 ? -35.012  29.097  -27.515 1.00 92.10  ? 1190 ILE A O   1 
ATOM   9078  C  CB  . ILE A 1 1190 ? -32.760  28.786  -24.892 1.00 92.73  ? 1190 ILE A CB  1 
ATOM   9079  C  CG1 . ILE A 1 1190 ? -32.505  27.829  -23.737 1.00 92.55  ? 1190 ILE A CG1 1 
ATOM   9080  C  CG2 . ILE A 1 1190 ? -33.673  29.900  -24.381 1.00 92.22  ? 1190 ILE A CG2 1 
ATOM   9081  C  CD1 . ILE A 1 1190 ? -32.297  28.527  -22.431 1.00 93.41  ? 1190 ILE A CD1 1 
ATOM   9082  N  N   . SER A 1 1191 ? -32.829  29.517  -27.874 1.00 95.24  ? 1191 SER A N   1 
ATOM   9083  C  CA  . SER A 1 1191 ? -33.112  30.301  -29.057 1.00 93.34  ? 1191 SER A CA  1 
ATOM   9084  C  C   . SER A 1 1191 ? -34.253  29.649  -29.832 1.00 90.95  ? 1191 SER A C   1 
ATOM   9085  O  O   . SER A 1 1191 ? -35.259  30.295  -30.124 1.00 89.03  ? 1191 SER A O   1 
ATOM   9086  C  CB  . SER A 1 1191 ? -31.874  30.424  -29.935 1.00 93.97  ? 1191 SER A CB  1 
ATOM   9087  O  OG  . SER A 1 1191 ? -31.931  31.653  -30.636 1.00 94.58  ? 1191 SER A OG  1 
ATOM   9088  N  N   . ALA A 1 1192 ? -34.106  28.360  -30.132 1.00 89.76  ? 1192 ALA A N   1 
ATOM   9089  C  CA  . ALA A 1 1192 ? -35.144  27.622  -30.838 1.00 87.51  ? 1192 ALA A CA  1 
ATOM   9090  C  C   . ALA A 1 1192 ? -36.472  27.682  -30.080 1.00 90.88  ? 1192 ALA A C   1 
ATOM   9091  O  O   . ALA A 1 1192 ? -37.433  28.283  -30.572 1.00 92.75  ? 1192 ALA A O   1 
ATOM   9092  C  CB  . ALA A 1 1192 ? -34.722  26.178  -31.085 1.00 84.43  ? 1192 ALA A CB  1 
ATOM   9093  N  N   . TYR A 1 1193 ? -36.532  27.085  -28.885 1.00 90.57  ? 1193 TYR A N   1 
ATOM   9094  C  CA  . TYR A 1 1193 ? -37.793  27.026  -28.139 1.00 89.56  ? 1193 TYR A CA  1 
ATOM   9095  C  C   . TYR A 1 1193 ? -38.438  28.416  -28.020 1.00 89.98  ? 1193 TYR A C   1 
ATOM   9096  O  O   . TYR A 1 1193 ? -39.657  28.528  -27.966 1.00 91.80  ? 1193 TYR A O   1 
ATOM   9097  C  CB  . TYR A 1 1193 ? -37.629  26.379  -26.743 1.00 89.23  ? 1193 TYR A CB  1 
ATOM   9098  C  CG  . TYR A 1 1193 ? -38.895  26.468  -25.916 1.00 88.24  ? 1193 TYR A CG  1 
ATOM   9099  C  CD1 . TYR A 1 1193 ? -39.995  25.698  -26.241 1.00 89.54  ? 1193 TYR A CD1 1 
ATOM   9100  C  CD2 . TYR A 1 1193 ? -39.014  27.356  -24.847 1.00 86.41  ? 1193 TYR A CD2 1 
ATOM   9101  C  CE1 . TYR A 1 1193 ? -41.190  25.785  -25.516 1.00 89.35  ? 1193 TYR A CE1 1 
ATOM   9102  C  CE2 . TYR A 1 1193 ? -40.211  27.457  -24.114 1.00 86.29  ? 1193 TYR A CE2 1 
ATOM   9103  C  CZ  . TYR A 1 1193 ? -41.300  26.659  -24.459 1.00 86.75  ? 1193 TYR A CZ  1 
ATOM   9104  O  OH  . TYR A 1 1193 ? -42.507  26.704  -23.780 1.00 84.13  ? 1193 TYR A OH  1 
ATOM   9105  N  N   . ALA A 1 1194 ? -37.631  29.471  -28.007 1.00 86.41  ? 1194 ALA A N   1 
ATOM   9106  C  CA  . ALA A 1 1194 ? -38.163  30.810  -27.784 1.00 85.48  ? 1194 ALA A CA  1 
ATOM   9107  C  C   . ALA A 1 1194 ? -38.910  31.364  -28.996 1.00 83.12  ? 1194 ALA A C   1 
ATOM   9108  O  O   . ALA A 1 1194 ? -39.894  32.117  -28.862 1.00 82.60  ? 1194 ALA A O   1 
ATOM   9109  C  CB  . ALA A 1 1194 ? -37.044  31.753  -27.362 1.00 87.10  ? 1194 ALA A CB  1 
ATOM   9110  N  N   . LEU A 1 1195 ? -38.416  31.008  -30.179 1.00 82.73  ? 1195 LEU A N   1 
ATOM   9111  C  CA  . LEU A 1 1195 ? -39.021  31.455  -31.426 1.00 81.60  ? 1195 LEU A CA  1 
ATOM   9112  C  C   . LEU A 1 1195 ? -40.243  30.602  -31.576 1.00 82.59  ? 1195 LEU A C   1 
ATOM   9113  O  O   . LEU A 1 1195 ? -41.343  31.107  -31.732 1.00 84.17  ? 1195 LEU A O   1 
ATOM   9114  C  CB  . LEU A 1 1195 ? -38.042  31.289  -32.596 1.00 79.11  ? 1195 LEU A CB  1 
ATOM   9115  C  CG  . LEU A 1 1195 ? -36.690  32.012  -32.348 1.00 81.18  ? 1195 LEU A CG  1 
ATOM   9116  C  CD1 . LEU A 1 1195 ? -35.538  31.452  -33.161 1.00 81.46  ? 1195 LEU A CD1 1 
ATOM   9117  C  CD2 . LEU A 1 1195 ? -36.790  33.527  -32.545 1.00 81.84  ? 1195 LEU A CD2 1 
ATOM   9118  N  N   . SER A 1 1196 ? -40.039  29.300  -31.444 1.00 83.12  ? 1196 SER A N   1 
ATOM   9119  C  CA  . SER A 1 1196 ? -41.121  28.333  -31.320 1.00 84.85  ? 1196 SER A CA  1 
ATOM   9120  C  C   . SER A 1 1196 ? -42.401  28.938  -30.725 1.00 88.28  ? 1196 SER A C   1 
ATOM   9121  O  O   . SER A 1 1196 ? -43.518  28.528  -31.032 1.00 85.97  ? 1196 SER A O   1 
ATOM   9122  C  CB  . SER A 1 1196 ? -40.629  27.158  -30.483 1.00 84.30  ? 1196 SER A CB  1 
ATOM   9123  O  OG  . SER A 1 1196 ? -41.693  26.449  -29.921 1.00 84.93  ? 1196 SER A OG  1 
ATOM   9124  N  N   . LEU A 1 1197 ? -42.234  29.926  -29.864 1.00 96.77  ? 1197 LEU A N   1 
ATOM   9125  C  CA  . LEU A 1 1197 ? -43.379  30.577  -29.227 1.00 106.20 ? 1197 LEU A CA  1 
ATOM   9126  C  C   . LEU A 1 1197 ? -43.715  31.921  -29.883 1.00 112.31 ? 1197 LEU A C   1 
ATOM   9127  O  O   . LEU A 1 1197 ? -43.881  32.937  -29.219 1.00 112.83 ? 1197 LEU A O   1 
ATOM   9128  C  CB  . LEU A 1 1197 ? -43.129  30.750  -27.718 1.00 109.34 ? 1197 LEU A CB  1 
ATOM   9129  C  CG  . LEU A 1 1197 ? -42.543  29.554  -26.948 1.00 111.97 ? 1197 LEU A CG  1 
ATOM   9130  C  CD1 . LEU A 1 1197 ? -42.343  29.929  -25.494 1.00 114.34 ? 1197 LEU A CD1 1 
ATOM   9131  C  CD2 . LEU A 1 1197 ? -43.405  28.296  -27.059 1.00 112.12 ? 1197 LEU A CD2 1 
ATOM   9132  N  N   . GLY A 1 1198 ? -43.809  31.925  -31.196 1.00 117.77 ? 1198 GLY A N   1 
ATOM   9133  C  CA  . GLY A 1 1198 ? -44.092  33.152  -31.906 1.00 123.97 ? 1198 GLY A CA  1 
ATOM   9134  C  C   . GLY A 1 1198 ? -44.566  32.809  -33.297 1.00 126.73 ? 1198 GLY A C   1 
ATOM   9135  O  O   . GLY A 1 1198 ? -45.580  32.118  -33.472 1.00 129.09 ? 1198 GLY A O   1 
ATOM   9136  N  N   . ASP A 1 1199 ? -43.828  33.293  -34.294 1.00 125.57 ? 1199 ASP A N   1 
ATOM   9137  C  CA  . ASP A 1 1199 ? -44.029  32.841  -35.667 1.00 121.99 ? 1199 ASP A CA  1 
ATOM   9138  C  C   . ASP A 1 1199 ? -43.124  31.664  -35.969 1.00 112.66 ? 1199 ASP A C   1 
ATOM   9139  O  O   . ASP A 1 1199 ? -41.906  31.830  -36.064 1.00 111.92 ? 1199 ASP A O   1 
ATOM   9140  C  CB  . ASP A 1 1199 ? -43.729  33.951  -36.659 1.00 127.75 ? 1199 ASP A CB  1 
ATOM   9141  C  CG  . ASP A 1 1199 ? -43.666  33.439  -38.070 1.00 132.74 ? 1199 ASP A CG  1 
ATOM   9142  O  OD1 . ASP A 1 1199 ? -44.224  32.343  -38.327 1.00 132.05 ? 1199 ASP A OD1 1 
ATOM   9143  O  OD2 . ASP A 1 1199 ? -43.052  34.129  -38.913 1.00 136.83 ? 1199 ASP A OD2 1 
ATOM   9144  N  N   . LYS A 1 1200 ? -43.708  30.483  -36.121 1.00 104.25 ? 1200 LYS A N   1 
ATOM   9145  C  CA  . LYS A 1 1200 ? -42.911  29.298  -36.337 1.00 99.29  ? 1200 LYS A CA  1 
ATOM   9146  C  C   . LYS A 1 1200 ? -42.917  28.956  -37.825 1.00 102.77 ? 1200 LYS A C   1 
ATOM   9147  O  O   . LYS A 1 1200 ? -42.974  27.784  -38.214 1.00 107.05 ? 1200 LYS A O   1 
ATOM   9148  C  CB  . LYS A 1 1200 ? -43.415  28.156  -35.463 1.00 94.59  ? 1200 LYS A CB  1 
ATOM   9149  C  CG  . LYS A 1 1200 ? -44.860  28.345  -35.072 1.00 96.72  ? 1200 LYS A CG  1 
ATOM   9150  C  CD  . LYS A 1 1200 ? -45.231  27.702  -33.738 1.00 99.94  ? 1200 LYS A CD  1 
ATOM   9151  C  CE  . LYS A 1 1200 ? -45.712  26.250  -33.884 1.00 101.89 ? 1200 LYS A CE  1 
ATOM   9152  N  NZ  . LYS A 1 1200 ? -46.703  25.875  -32.811 1.00 102.47 ? 1200 LYS A NZ  1 
ATOM   9153  N  N   . THR A 1 1201 ? -42.857  29.977  -38.678 1.00 100.42 ? 1201 THR A N   1 
ATOM   9154  C  CA  . THR A 1 1201 ? -42.676  29.722  -40.105 1.00 97.42  ? 1201 THR A CA  1 
ATOM   9155  C  C   . THR A 1 1201 ? -41.677  30.636  -40.763 1.00 99.21  ? 1201 THR A C   1 
ATOM   9156  O  O   . THR A 1 1201 ? -41.327  30.437  -41.922 1.00 99.50  ? 1201 THR A O   1 
ATOM   9157  C  CB  . THR A 1 1201 ? -43.947  29.860  -40.886 1.00 95.42  ? 1201 THR A CB  1 
ATOM   9158  O  OG1 . THR A 1 1201 ? -44.483  31.166  -40.662 1.00 95.16  ? 1201 THR A OG1 1 
ATOM   9159  C  CG2 . THR A 1 1201 ? -44.950  28.746  -40.522 1.00 93.05  ? 1201 THR A CG2 1 
ATOM   9160  N  N   . HIS A 1 1202 ? -41.215  31.648  -40.048 1.00 102.56 ? 1202 HIS A N   1 
ATOM   9161  C  CA  . HIS A 1 1202 ? -40.128  32.428  -40.595 1.00 106.68 ? 1202 HIS A CA  1 
ATOM   9162  C  C   . HIS A 1 1202 ? -39.121  31.408  -41.062 1.00 109.58 ? 1202 HIS A C   1 
ATOM   9163  O  O   . HIS A 1 1202 ? -38.779  30.477  -40.331 1.00 109.15 ? 1202 HIS A O   1 
ATOM   9164  C  CB  . HIS A 1 1202 ? -39.482  33.358  -39.586 1.00 105.81 ? 1202 HIS A CB  1 
ATOM   9165  C  CG  . HIS A 1 1202 ? -38.546  34.336  -40.214 1.00 108.55 ? 1202 HIS A CG  1 
ATOM   9166  N  ND1 . HIS A 1 1202 ? -38.639  35.694  -40.012 1.00 111.13 ? 1202 HIS A ND1 1 
ATOM   9167  C  CD2 . HIS A 1 1202 ? -37.510  34.155  -41.064 1.00 108.79 ? 1202 HIS A CD2 1 
ATOM   9168  C  CE1 . HIS A 1 1202 ? -37.689  36.312  -40.694 1.00 111.06 ? 1202 HIS A CE1 1 
ATOM   9169  N  NE2 . HIS A 1 1202 ? -36.992  35.399  -41.343 1.00 110.78 ? 1202 HIS A NE2 1 
ATOM   9170  N  N   . PRO A 1 1203 ? -38.667  31.569  -42.305 1.00 113.34 ? 1203 PRO A N   1 
ATOM   9171  C  CA  . PRO A 1 1203 ? -37.769  30.658  -43.016 1.00 113.42 ? 1203 PRO A CA  1 
ATOM   9172  C  C   . PRO A 1 1203 ? -36.569  30.414  -42.129 1.00 111.43 ? 1203 PRO A C   1 
ATOM   9173  O  O   . PRO A 1 1203 ? -36.173  29.271  -41.884 1.00 111.86 ? 1203 PRO A O   1 
ATOM   9174  C  CB  . PRO A 1 1203 ? -37.327  31.492  -44.213 1.00 116.91 ? 1203 PRO A CB  1 
ATOM   9175  C  CG  . PRO A 1 1203 ? -38.425  32.482  -44.411 1.00 117.01 ? 1203 PRO A CG  1 
ATOM   9176  C  CD  . PRO A 1 1203 ? -38.945  32.796  -43.067 1.00 114.72 ? 1203 PRO A CD  1 
ATOM   9177  N  N   . GLN A 1 1204 ? -36.019  31.526  -41.650 1.00 106.37 ? 1204 GLN A N   1 
ATOM   9178  C  CA  . GLN A 1 1204 ? -34.939  31.565  -40.687 1.00 101.36 ? 1204 GLN A CA  1 
ATOM   9179  C  C   . GLN A 1 1204 ? -35.168  30.671  -39.461 1.00 94.63  ? 1204 GLN A C   1 
ATOM   9180  O  O   . GLN A 1 1204 ? -34.330  29.842  -39.157 1.00 91.66  ? 1204 GLN A O   1 
ATOM   9181  C  CB  . GLN A 1 1204 ? -34.739  33.020  -40.291 1.00 101.62 ? 1204 GLN A CB  1 
ATOM   9182  C  CG  . GLN A 1 1204 ? -33.652  33.272  -39.321 1.00 100.20 ? 1204 GLN A CG  1 
ATOM   9183  C  CD  . GLN A 1 1204 ? -32.347  32.721  -39.778 1.00 98.24  ? 1204 GLN A CD  1 
ATOM   9184  O  OE1 . GLN A 1 1204 ? -32.216  32.196  -40.889 1.00 96.19  ? 1204 GLN A OE1 1 
ATOM   9185  N  NE2 . GLN A 1 1204 ? -31.357  32.823  -38.911 1.00 98.94  ? 1204 GLN A NE2 1 
ATOM   9186  N  N   . PHE A 1 1205 ? -36.294  30.829  -38.767 1.00 93.61  ? 1205 PHE A N   1 
ATOM   9187  C  CA  . PHE A 1 1205 ? -36.646  29.896  -37.687 1.00 91.68  ? 1205 PHE A CA  1 
ATOM   9188  C  C   . PHE A 1 1205 ? -36.445  28.457  -38.153 1.00 91.36  ? 1205 PHE A C   1 
ATOM   9189  O  O   . PHE A 1 1205 ? -35.735  27.696  -37.488 1.00 91.80  ? 1205 PHE A O   1 
ATOM   9190  C  CB  . PHE A 1 1205 ? -38.090  30.104  -37.162 1.00 80.78  ? 1205 PHE A CB  1 
ATOM   9191  C  CG  . PHE A 1 1205 ? -38.591  29.001  -36.211 1.00 76.95  ? 1205 PHE A CG  1 
ATOM   9192  C  CD1 . PHE A 1 1205 ? -38.024  28.805  -34.967 1.00 77.57  ? 1205 PHE A CD1 1 
ATOM   9193  C  CD2 . PHE A 1 1205 ? -39.661  28.201  -36.559 1.00 73.37  ? 1205 PHE A CD2 1 
ATOM   9194  C  CE1 . PHE A 1 1205 ? -38.506  27.809  -34.115 1.00 76.38  ? 1205 PHE A CE1 1 
ATOM   9195  C  CE2 . PHE A 1 1205 ? -40.142  27.204  -35.713 1.00 71.85  ? 1205 PHE A CE2 1 
ATOM   9196  C  CZ  . PHE A 1 1205 ? -39.565  27.004  -34.503 1.00 73.41  ? 1205 PHE A CZ  1 
ATOM   9197  N  N   . ARG A 1 1206 ? -37.045  28.091  -39.292 1.00 90.46  ? 1206 ARG A N   1 
ATOM   9198  C  CA  . ARG A 1 1206 ? -36.915  26.729  -39.824 1.00 91.16  ? 1206 ARG A CA  1 
ATOM   9199  C  C   . ARG A 1 1206 ? -35.432  26.333  -40.031 1.00 90.74  ? 1206 ARG A C   1 
ATOM   9200  O  O   . ARG A 1 1206 ? -35.061  25.144  -39.938 1.00 89.15  ? 1206 ARG A O   1 
ATOM   9201  C  CB  . ARG A 1 1206 ? -37.724  26.556  -41.115 1.00 95.05  ? 1206 ARG A CB  1 
ATOM   9202  C  CG  . ARG A 1 1206 ? -39.196  26.918  -40.994 1.00 99.84  ? 1206 ARG A CG  1 
ATOM   9203  C  CD  . ARG A 1 1206 ? -40.060  25.936  -41.790 1.00 106.18 ? 1206 ARG A CD  1 
ATOM   9204  N  NE  . ARG A 1 1206 ? -41.479  26.305  -41.951 1.00 111.43 ? 1206 ARG A NE  1 
ATOM   9205  C  CZ  . ARG A 1 1206 ? -41.947  27.139  -42.897 1.00 115.23 ? 1206 ARG A CZ  1 
ATOM   9206  N  NH1 . ARG A 1 1206 ? -41.112  27.755  -43.760 1.00 116.10 ? 1206 ARG A NH1 1 
ATOM   9207  N  NH2 . ARG A 1 1206 ? -43.259  27.385  -42.978 1.00 115.30 ? 1206 ARG A NH2 1 
ATOM   9208  N  N   . SER A 1 1207 ? -34.595  27.338  -40.300 1.00 89.15  ? 1207 SER A N   1 
ATOM   9209  C  CA  . SER A 1 1207 ? -33.155  27.141  -40.436 1.00 87.83  ? 1207 SER A CA  1 
ATOM   9210  C  C   . SER A 1 1207 ? -32.672  26.682  -39.081 1.00 85.42  ? 1207 SER A C   1 
ATOM   9211  O  O   . SER A 1 1207 ? -32.050  25.627  -38.959 1.00 86.53  ? 1207 SER A O   1 
ATOM   9212  C  CB  . SER A 1 1207 ? -32.452  28.461  -40.841 1.00 88.67  ? 1207 SER A CB  1 
ATOM   9213  O  OG  . SER A 1 1207 ? -31.115  28.290  -41.331 1.00 88.66  ? 1207 SER A OG  1 
ATOM   9214  N  N   . ILE A 1 1208 ? -32.999  27.476  -38.062 1.00 81.25  ? 1208 ILE A N   1 
ATOM   9215  C  CA  . ILE A 1 1208 ? -32.493  27.261  -36.713 1.00 74.40  ? 1208 ILE A CA  1 
ATOM   9216  C  C   . ILE A 1 1208 ? -32.921  25.886  -36.213 1.00 68.17  ? 1208 ILE A C   1 
ATOM   9217  O  O   . ILE A 1 1208 ? -32.112  25.120  -35.677 1.00 65.56  ? 1208 ILE A O   1 
ATOM   9218  C  CB  . ILE A 1 1208 ? -32.962  28.367  -35.741 1.00 72.13  ? 1208 ILE A CB  1 
ATOM   9219  C  CG1 . ILE A 1 1208 ? -33.304  29.654  -36.479 1.00 69.65  ? 1208 ILE A CG1 1 
ATOM   9220  C  CG2 . ILE A 1 1208 ? -31.881  28.663  -34.733 1.00 74.02  ? 1208 ILE A CG2 1 
ATOM   9221  C  CD1 . ILE A 1 1208 ? -32.944  30.897  -35.705 1.00 68.36  ? 1208 ILE A CD1 1 
ATOM   9222  N  N   . VAL A 1 1209 ? -34.194  25.573  -36.411 1.00 65.77  ? 1209 VAL A N   1 
ATOM   9223  C  CA  . VAL A 1 1209 ? -34.711  24.267  -36.044 1.00 69.10  ? 1209 VAL A CA  1 
ATOM   9224  C  C   . VAL A 1 1209 ? -33.993  23.190  -36.822 1.00 76.44  ? 1209 VAL A C   1 
ATOM   9225  O  O   . VAL A 1 1209 ? -33.850  22.060  -36.332 1.00 76.89  ? 1209 VAL A O   1 
ATOM   9226  C  CB  . VAL A 1 1209 ? -36.180  24.130  -36.380 1.00 68.36  ? 1209 VAL A CB  1 
ATOM   9227  C  CG1 . VAL A 1 1209 ? -36.686  22.773  -35.938 1.00 67.83  ? 1209 VAL A CG1 1 
ATOM   9228  C  CG2 . VAL A 1 1209 ? -36.977  25.249  -35.749 1.00 68.72  ? 1209 VAL A CG2 1 
ATOM   9229  N  N   . SER A 1 1210 ? -33.586  23.522  -38.053 1.00 81.56  ? 1210 SER A N   1 
ATOM   9230  C  CA  . SER A 1 1210 ? -32.702  22.643  -38.809 1.00 87.61  ? 1210 SER A CA  1 
ATOM   9231  C  C   . SER A 1 1210 ? -31.394  22.486  -38.029 1.00 92.10  ? 1210 SER A C   1 
ATOM   9232  O  O   . SER A 1 1210 ? -31.061  21.385  -37.555 1.00 93.86  ? 1210 SER A O   1 
ATOM   9233  C  CB  . SER A 1 1210 ? -32.396  23.205  -40.190 1.00 90.25  ? 1210 SER A CB  1 
ATOM   9234  O  OG  . SER A 1 1210 ? -31.170  22.656  -40.671 1.00 93.57  ? 1210 SER A OG  1 
ATOM   9235  N  N   . ALA A 1 1211 ? -30.669  23.593  -37.877 1.00 92.32  ? 1211 ALA A N   1 
ATOM   9236  C  CA  . ALA A 1 1211 ? -29.496  23.619  -37.028 1.00 92.89  ? 1211 ALA A CA  1 
ATOM   9237  C  C   . ALA A 1 1211 ? -29.664  22.656  -35.873 1.00 90.71  ? 1211 ALA A C   1 
ATOM   9238  O  O   . ALA A 1 1211 ? -28.993  21.631  -35.789 1.00 89.88  ? 1211 ALA A O   1 
ATOM   9239  C  CB  . ALA A 1 1211 ? -29.301  25.018  -36.502 1.00 93.25  ? 1211 ALA A CB  1 
ATOM   9240  N  N   . LEU A 1 1212 ? -30.599  22.998  -34.998 1.00 91.16  ? 1212 LEU A N   1 
ATOM   9241  C  CA  . LEU A 1 1212 ? -30.814  22.251  -33.767 1.00 91.49  ? 1212 LEU A CA  1 
ATOM   9242  C  C   . LEU A 1 1212 ? -30.994  20.780  -34.055 1.00 90.82  ? 1212 LEU A C   1 
ATOM   9243  O  O   . LEU A 1 1212 ? -30.377  19.918  -33.411 1.00 92.13  ? 1212 LEU A O   1 
ATOM   9244  C  CB  . LEU A 1 1212 ? -32.047  22.777  -33.011 1.00 88.55  ? 1212 LEU A CB  1 
ATOM   9245  C  CG  . LEU A 1 1212 ? -32.545  21.909  -31.851 1.00 86.14  ? 1212 LEU A CG  1 
ATOM   9246  C  CD1 . LEU A 1 1212 ? -31.420  21.564  -30.926 1.00 86.94  ? 1212 LEU A CD1 1 
ATOM   9247  C  CD2 . LEU A 1 1212 ? -33.602  22.635  -31.095 1.00 84.80  ? 1212 LEU A CD2 1 
ATOM   9248  N  N   . LYS A 1 1213 ? -31.841  20.505  -35.039 1.00 87.82  ? 1213 LYS A N   1 
ATOM   9249  C  CA  . LYS A 1 1213 ? -32.338  19.164  -35.232 1.00 85.39  ? 1213 LYS A CA  1 
ATOM   9250  C  C   . LYS A 1 1213 ? -31.218  18.322  -35.764 1.00 90.43  ? 1213 LYS A C   1 
ATOM   9251  O  O   . LYS A 1 1213 ? -31.223  17.096  -35.652 1.00 90.33  ? 1213 LYS A O   1 
ATOM   9252  C  CB  . LYS A 1 1213 ? -33.527  19.180  -36.166 1.00 78.51  ? 1213 LYS A CB  1 
ATOM   9253  C  CG  . LYS A 1 1213 ? -34.381  17.958  -36.026 1.00 77.04  ? 1213 LYS A CG  1 
ATOM   9254  C  CD  . LYS A 1 1213 ? -35.821  18.317  -36.289 1.00 77.23  ? 1213 LYS A CD  1 
ATOM   9255  C  CE  . LYS A 1 1213 ? -36.654  17.114  -36.663 1.00 78.04  ? 1213 LYS A CE  1 
ATOM   9256  N  NZ  . LYS A 1 1213 ? -38.053  17.432  -36.341 1.00 77.56  ? 1213 LYS A NZ  1 
ATOM   9257  N  N   . ARG A 1 1214 ? -30.243  19.014  -36.328 1.00 96.70  ? 1214 ARG A N   1 
ATOM   9258  C  CA  . ARG A 1 1214 ? -29.099  18.371  -36.904 1.00 107.13 ? 1214 ARG A CA  1 
ATOM   9259  C  C   . ARG A 1 1214 ? -28.168  18.047  -35.759 1.00 109.16 ? 1214 ARG A C   1 
ATOM   9260  O  O   . ARG A 1 1214 ? -27.397  17.101  -35.812 1.00 112.27 ? 1214 ARG A O   1 
ATOM   9261  C  CB  . ARG A 1 1214 ? -28.452  19.307  -37.930 1.00 118.28 ? 1214 ARG A CB  1 
ATOM   9262  C  CG  . ARG A 1 1214 ? -26.993  19.019  -38.264 1.00 131.71 ? 1214 ARG A CG  1 
ATOM   9263  C  CD  . ARG A 1 1214 ? -26.514  19.884  -39.430 1.00 141.80 ? 1214 ARG A CD  1 
ATOM   9264  N  NE  . ARG A 1 1214 ? -27.009  21.258  -39.323 1.00 147.40 ? 1214 ARG A NE  1 
ATOM   9265  C  CZ  . ARG A 1 1214 ? -27.075  22.116  -40.338 1.00 151.88 ? 1214 ARG A CZ  1 
ATOM   9266  N  NH1 . ARG A 1 1214 ? -26.679  21.742  -41.547 1.00 154.86 ? 1214 ARG A NH1 1 
ATOM   9267  N  NH2 . ARG A 1 1214 ? -27.542  23.345  -40.152 1.00 151.96 ? 1214 ARG A NH2 1 
ATOM   9268  N  N   . GLU A 1 1215 ? -28.259  18.816  -34.686 1.00 108.92 ? 1215 GLU A N   1 
ATOM   9269  C  CA  . GLU A 1 1215 ? -27.267  18.674  -33.620 1.00 107.73 ? 1215 GLU A CA  1 
ATOM   9270  C  C   . GLU A 1 1215 ? -27.425  17.420  -32.763 1.00 103.98 ? 1215 GLU A C   1 
ATOM   9271  O  O   . GLU A 1 1215 ? -26.444  16.951  -32.178 1.00 106.05 ? 1215 GLU A O   1 
ATOM   9272  C  CB  . GLU A 1 1215 ? -27.191  19.945  -32.774 1.00 106.31 ? 1215 GLU A CB  1 
ATOM   9273  C  CG  . GLU A 1 1215 ? -26.313  20.978  -33.438 1.00 107.86 ? 1215 GLU A CG  1 
ATOM   9274  C  CD  . GLU A 1 1215 ? -24.906  20.462  -33.588 1.00 111.91 ? 1215 GLU A CD  1 
ATOM   9275  O  OE1 . GLU A 1 1215 ? -24.526  19.580  -32.787 1.00 113.65 ? 1215 GLU A OE1 1 
ATOM   9276  O  OE2 . GLU A 1 1215 ? -24.188  20.927  -34.499 1.00 113.55 ? 1215 GLU A OE2 1 
ATOM   9277  N  N   . ALA A 1 1216 ? -28.645  16.871  -32.749 1.00 96.25  ? 1216 ALA A N   1 
ATOM   9278  C  CA  . ALA A 1 1216 ? -29.070  15.832  -31.808 1.00 91.15  ? 1216 ALA A CA  1 
ATOM   9279  C  C   . ALA A 1 1216 ? -28.331  14.496  -31.926 1.00 90.80  ? 1216 ALA A C   1 
ATOM   9280  O  O   . ALA A 1 1216 ? -27.534  14.304  -32.853 1.00 93.68  ? 1216 ALA A O   1 
ATOM   9281  C  CB  . ALA A 1 1216 ? -30.557  15.624  -31.925 1.00 87.47  ? 1216 ALA A CB  1 
ATOM   9282  N  N   . LEU A 1 1217 ? -28.608  13.585  -30.984 1.00 88.38  ? 1217 LEU A N   1 
ATOM   9283  C  CA  . LEU A 1 1217 ? -27.998  12.248  -30.962 1.00 87.56  ? 1217 LEU A CA  1 
ATOM   9284  C  C   . LEU A 1 1217 ? -29.013  11.148  -30.608 1.00 86.62  ? 1217 LEU A C   1 
ATOM   9285  O  O   . LEU A 1 1217 ? -30.105  11.407  -30.068 1.00 80.76  ? 1217 LEU A O   1 
ATOM   9286  C  CB  . LEU A 1 1217 ? -26.842  12.208  -29.976 1.00 87.31  ? 1217 LEU A CB  1 
ATOM   9287  C  CG  . LEU A 1 1217 ? -26.171  13.559  -29.746 1.00 86.53  ? 1217 LEU A CG  1 
ATOM   9288  C  CD1 . LEU A 1 1217 ? -26.090  13.856  -28.279 1.00 85.10  ? 1217 LEU A CD1 1 
ATOM   9289  C  CD2 . LEU A 1 1217 ? -24.783  13.685  -30.433 1.00 89.48  ? 1217 LEU A CD2 1 
ATOM   9290  N  N   . VAL A 1 1218 ? -28.638  9.904   -30.875 1.00 91.18  ? 1218 VAL A N   1 
ATOM   9291  C  CA  . VAL A 1 1218 ? -29.638  8.843   -30.866 1.00 93.11  ? 1218 VAL A CA  1 
ATOM   9292  C  C   . VAL A 1 1218 ? -29.047  7.576   -30.350 1.00 93.45  ? 1218 VAL A C   1 
ATOM   9293  O  O   . VAL A 1 1218 ? -27.874  7.295   -30.587 1.00 91.17  ? 1218 VAL A O   1 
ATOM   9294  C  CB  . VAL A 1 1218 ? -30.009  8.544   -32.273 1.00 98.44  ? 1218 VAL A CB  1 
ATOM   9295  C  CG1 . VAL A 1 1218 ? -31.304  9.241   -32.671 1.00 96.61  ? 1218 VAL A CG1 1 
ATOM   9296  C  CG2 . VAL A 1 1218 ? -28.853  9.016   -33.131 1.00 104.82 ? 1218 VAL A CG2 1 
ATOM   9297  N  N   . LYS A 1 1219 ? -29.857  6.809   -29.644 1.00 97.92  ? 1219 LYS A N   1 
ATOM   9298  C  CA  . LYS A 1 1219 ? -29.374  5.576   -29.082 1.00 110.32 ? 1219 LYS A CA  1 
ATOM   9299  C  C   . LYS A 1 1219 ? -30.119  4.438   -29.762 1.00 117.66 ? 1219 LYS A C   1 
ATOM   9300  O  O   . LYS A 1 1219 ? -31.356  4.436   -29.807 1.00 117.75 ? 1219 LYS A O   1 
ATOM   9301  C  CB  . LYS A 1 1219 ? -29.527  5.559   -27.544 1.00 114.19 ? 1219 LYS A CB  1 
ATOM   9302  C  CG  . LYS A 1 1219 ? -28.202  5.748   -26.698 1.00 178.22 ? 1219 LYS A CG  1 
ATOM   9303  C  CD  . LYS A 1 1219 ? -28.371  6.647   -25.416 1.00 163.94 ? 1219 LYS A CD  1 
ATOM   9304  C  CE  . LYS A 1 1219 ? -28.209  5.950   -24.033 1.00 148.13 ? 1219 LYS A CE  1 
ATOM   9305  N  NZ  . LYS A 1 1219 ? -28.578  6.878   -22.873 1.00 146.04 ? 1219 LYS A NZ  1 
ATOM   9306  N  N   . GLY A 1 1220 ? -29.339  3.494   -30.308 1.00 122.90 ? 1220 GLY A N   1 
ATOM   9307  C  CA  . GLY A 1 1220 ? -29.849  2.285   -30.944 1.00 124.38 ? 1220 GLY A CA  1 
ATOM   9308  C  C   . GLY A 1 1220 ? -30.412  2.524   -32.327 1.00 124.89 ? 1220 GLY A C   1 
ATOM   9309  O  O   . GLY A 1 1220 ? -30.886  3.623   -32.624 1.00 123.74 ? 1220 GLY A O   1 
ATOM   9310  N  N   . ASN A 1 1221 ? -30.355  1.512   -33.187 1.00 128.81 ? 1221 ASN A N   1 
ATOM   9311  C  CA  . ASN A 1 1221 ? -30.886  1.686   -34.540 1.00 128.49 ? 1221 ASN A CA  1 
ATOM   9312  C  C   . ASN A 1 1221 ? -32.138  0.883   -34.858 1.00 124.47 ? 1221 ASN A C   1 
ATOM   9313  O  O   . ASN A 1 1221 ? -32.107  -0.351  -34.844 1.00 126.21 ? 1221 ASN A O   1 
ATOM   9314  C  CB  . ASN A 1 1221 ? -29.846  1.386   -35.611 1.00 133.23 ? 1221 ASN A CB  1 
ATOM   9315  C  CG  . ASN A 1 1221 ? -30.415  1.548   -36.988 1.00 133.18 ? 1221 ASN A CG  1 
ATOM   9316  O  OD1 . ASN A 1 1221 ? -30.558  0.580   -37.733 1.00 134.06 ? 1221 ASN A OD1 1 
ATOM   9317  N  ND2 . ASN A 1 1221 ? -30.816  2.774   -37.313 1.00 131.42 ? 1221 ASN A ND2 1 
ATOM   9318  N  N   . PRO A 1 1222 ? -33.227  1.576   -35.212 1.00 117.73 ? 1222 PRO A N   1 
ATOM   9319  C  CA  . PRO A 1 1222 ? -33.327  3.020   -35.438 1.00 113.15 ? 1222 PRO A CA  1 
ATOM   9320  C  C   . PRO A 1 1222 ? -33.287  3.764   -34.110 1.00 111.84 ? 1222 PRO A C   1 
ATOM   9321  O  O   . PRO A 1 1222 ? -33.055  3.129   -33.086 1.00 114.49 ? 1222 PRO A O   1 
ATOM   9322  C  CB  . PRO A 1 1222 ? -34.718  3.172   -36.048 1.00 111.46 ? 1222 PRO A CB  1 
ATOM   9323  C  CG  . PRO A 1 1222 ? -35.291  1.788   -36.149 1.00 112.79 ? 1222 PRO A CG  1 
ATOM   9324  C  CD  . PRO A 1 1222 ? -34.545  0.933   -35.223 1.00 115.23 ? 1222 PRO A CD  1 
ATOM   9325  N  N   . PRO A 1 1223 ? -33.539  5.089   -34.110 1.00 105.44 ? 1223 PRO A N   1 
ATOM   9326  C  CA  . PRO A 1 1223 ? -33.675  5.783   -32.837 1.00 98.19  ? 1223 PRO A CA  1 
ATOM   9327  C  C   . PRO A 1 1223 ? -34.612  5.033   -31.947 1.00 92.31  ? 1223 PRO A C   1 
ATOM   9328  O  O   . PRO A 1 1223 ? -35.762  4.833   -32.349 1.00 88.39  ? 1223 PRO A O   1 
ATOM   9329  C  CB  . PRO A 1 1223 ? -34.385  7.086   -33.230 1.00 95.46  ? 1223 PRO A CB  1 
ATOM   9330  C  CG  . PRO A 1 1223 ? -33.888  7.379   -34.517 1.00 98.79  ? 1223 PRO A CG  1 
ATOM   9331  C  CD  . PRO A 1 1223 ? -33.764  6.024   -35.221 1.00 104.77 ? 1223 PRO A CD  1 
ATOM   9332  N  N   . ILE A 1 1224 ? -34.126  4.611   -30.781 1.00 91.30  ? 1224 ILE A N   1 
ATOM   9333  C  CA  . ILE A 1 1224 ? -35.015  4.336   -29.665 1.00 87.98  ? 1224 ILE A CA  1 
ATOM   9334  C  C   . ILE A 1 1224 ? -34.969  5.451   -28.627 1.00 86.51  ? 1224 ILE A C   1 
ATOM   9335  O  O   . ILE A 1 1224 ? -35.980  5.700   -27.938 1.00 85.40  ? 1224 ILE A O   1 
ATOM   9336  C  CB  . ILE A 1 1224 ? -34.762  2.998   -29.039 1.00 87.50  ? 1224 ILE A CB  1 
ATOM   9337  C  CG1 . ILE A 1 1224 ? -34.860  1.955   -30.156 1.00 91.53  ? 1224 ILE A CG1 1 
ATOM   9338  C  CG2 . ILE A 1 1224 ? -35.778  2.792   -27.924 1.00 83.33  ? 1224 ILE A CG2 1 
ATOM   9339  C  CD1 . ILE A 1 1224 ? -35.251  0.563   -29.726 1.00 94.82  ? 1224 ILE A CD1 1 
ATOM   9340  N  N   . TYR A 1 1225 ? -33.811  6.122   -28.559 1.00 84.85  ? 1225 TYR A N   1 
ATOM   9341  C  CA  . TYR A 1 1225 ? -33.597  7.286   -27.708 1.00 82.37  ? 1225 TYR A CA  1 
ATOM   9342  C  C   . TYR A 1 1225 ? -32.987  8.388   -28.517 1.00 80.30  ? 1225 TYR A C   1 
ATOM   9343  O  O   . TYR A 1 1225 ? -32.056  8.158   -29.271 1.00 81.41  ? 1225 TYR A O   1 
ATOM   9344  C  CB  . TYR A 1 1225 ? -32.586  6.994   -26.590 1.00 85.37  ? 1225 TYR A CB  1 
ATOM   9345  C  CG  . TYR A 1 1225 ? -32.993  5.916   -25.639 1.00 87.64  ? 1225 TYR A CG  1 
ATOM   9346  C  CD1 . TYR A 1 1225 ? -34.129  6.042   -24.860 1.00 87.72  ? 1225 TYR A CD1 1 
ATOM   9347  C  CD2 . TYR A 1 1225 ? -32.261  4.759   -25.532 1.00 90.83  ? 1225 TYR A CD2 1 
ATOM   9348  C  CE1 . TYR A 1 1225 ? -34.523  5.024   -23.995 1.00 89.36  ? 1225 TYR A CE1 1 
ATOM   9349  C  CE2 . TYR A 1 1225 ? -32.641  3.742   -24.675 1.00 92.74  ? 1225 TYR A CE2 1 
ATOM   9350  C  CZ  . TYR A 1 1225 ? -33.769  3.876   -23.910 1.00 91.14  ? 1225 TYR A CZ  1 
ATOM   9351  O  OH  . TYR A 1 1225 ? -34.126  2.855   -23.067 1.00 91.54  ? 1225 TYR A OH  1 
ATOM   9352  N  N   . ARG A 1 1226 ? -33.460  9.601   -28.297 1.00 79.84  ? 1226 ARG A N   1 
ATOM   9353  C  CA  . ARG A 1 1226 ? -32.787  10.778  -28.805 1.00 84.19  ? 1226 ARG A CA  1 
ATOM   9354  C  C   . ARG A 1 1226 ? -32.606  11.715  -27.621 1.00 85.14  ? 1226 ARG A C   1 
ATOM   9355  O  O   . ARG A 1 1226 ? -33.357  11.603  -26.652 1.00 84.72  ? 1226 ARG A O   1 
ATOM   9356  C  CB  . ARG A 1 1226 ? -33.674  11.458  -29.848 1.00 87.21  ? 1226 ARG A CB  1 
ATOM   9357  C  CG  . ARG A 1 1226 ? -33.108  12.771  -30.426 1.00 89.04  ? 1226 ARG A CG  1 
ATOM   9358  C  CD  . ARG A 1 1226 ? -34.051  13.428  -31.441 1.00 86.93  ? 1226 ARG A CD  1 
ATOM   9359  N  NE  . ARG A 1 1226 ? -34.882  12.439  -32.119 1.00 84.30  ? 1226 ARG A NE  1 
ATOM   9360  C  CZ  . ARG A 1 1226 ? -34.503  11.734  -33.176 1.00 79.23  ? 1226 ARG A CZ  1 
ATOM   9361  N  NH1 . ARG A 1 1226 ? -33.279  11.911  -33.710 1.00 76.65  ? 1226 ARG A NH1 1 
ATOM   9362  N  NH2 . ARG A 1 1226 ? -35.369  10.860  -33.682 1.00 76.59  ? 1226 ARG A NH2 1 
ATOM   9363  N  N   . PHE A 1 1227 ? -31.622  12.621  -27.701 1.00 84.76  ? 1227 PHE A N   1 
ATOM   9364  C  CA  . PHE A 1 1227 ? -31.432  13.730  -26.751 1.00 81.79  ? 1227 PHE A CA  1 
ATOM   9365  C  C   . PHE A 1 1227 ? -30.339  14.585  -27.326 1.00 81.03  ? 1227 PHE A C   1 
ATOM   9366  O  O   . PHE A 1 1227 ? -29.607  14.118  -28.212 1.00 81.88  ? 1227 PHE A O   1 
ATOM   9367  C  CB  . PHE A 1 1227 ? -30.914  13.217  -25.427 1.00 83.93  ? 1227 PHE A CB  1 
ATOM   9368  C  CG  . PHE A 1 1227 ? -29.774  12.250  -25.577 1.00 88.34  ? 1227 PHE A CG  1 
ATOM   9369  C  CD1 . PHE A 1 1227 ? -28.463  12.678  -25.534 1.00 89.25  ? 1227 PHE A CD1 1 
ATOM   9370  C  CD2 . PHE A 1 1227 ? -30.022  10.906  -25.803 1.00 88.92  ? 1227 PHE A CD2 1 
ATOM   9371  C  CE1 . PHE A 1 1227 ? -27.431  11.777  -25.692 1.00 89.57  ? 1227 PHE A CE1 1 
ATOM   9372  C  CE2 . PHE A 1 1227 ? -29.001  10.013  -25.949 1.00 88.59  ? 1227 PHE A CE2 1 
ATOM   9373  C  CZ  . PHE A 1 1227 ? -27.706  10.450  -25.894 1.00 89.59  ? 1227 PHE A CZ  1 
ATOM   9374  N  N   . TRP A 1 1228 ? -30.197  15.821  -26.838 1.00 81.08  ? 1228 TRP A N   1 
ATOM   9375  C  CA  . TRP A 1 1228 ? -29.005  16.627  -27.189 1.00 83.77  ? 1228 TRP A CA  1 
ATOM   9376  C  C   . TRP A 1 1228 ? -27.945  16.750  -26.048 1.00 103.23 ? 1228 TRP A C   1 
ATOM   9377  O  O   . TRP A 1 1228 ? -28.243  16.576  -24.871 1.00 102.16 ? 1228 TRP A O   1 
ATOM   9378  C  CB  . TRP A 1 1228 ? -29.368  18.008  -27.757 1.00 81.02  ? 1228 TRP A CB  1 
ATOM   9379  C  CG  . TRP A 1 1228 ? -30.323  18.013  -28.935 1.00 81.24  ? 1228 TRP A CG  1 
ATOM   9380  C  CD1 . TRP A 1 1228 ? -30.168  18.687  -30.122 1.00 82.24  ? 1228 TRP A CD1 1 
ATOM   9381  C  CD2 . TRP A 1 1228 ? -31.599  17.341  -29.027 1.00 80.07  ? 1228 TRP A CD2 1 
ATOM   9382  N  NE1 . TRP A 1 1228 ? -31.266  18.478  -30.939 1.00 80.59  ? 1228 TRP A NE1 1 
ATOM   9383  C  CE2 . TRP A 1 1228 ? -32.155  17.657  -30.291 1.00 79.60  ? 1228 TRP A CE2 1 
ATOM   9384  C  CE3 . TRP A 1 1228 ? -32.324  16.504  -28.169 1.00 77.77  ? 1228 TRP A CE3 1 
ATOM   9385  C  CZ2 . TRP A 1 1228 ? -33.393  17.155  -30.712 1.00 77.08  ? 1228 TRP A CZ2 1 
ATOM   9386  C  CZ3 . TRP A 1 1228 ? -33.550  16.010  -28.597 1.00 75.58  ? 1228 TRP A CZ3 1 
ATOM   9387  C  CH2 . TRP A 1 1228 ? -34.070  16.337  -29.851 1.00 74.96  ? 1228 TRP A CH2 1 
ATOM   9388  N  N   . LYS A 1 1229 ? -26.699  16.998  -26.423 1.00 104.90 ? 1229 LYS A N   1 
ATOM   9389  C  CA  . LYS A 1 1229 ? -25.628  17.154  -25.482 1.00 108.64 ? 1229 LYS A CA  1 
ATOM   9390  C  C   . LYS A 1 1229 ? -25.395  18.641  -25.472 1.00 116.48 ? 1229 LYS A C   1 
ATOM   9391  O  O   . LYS A 1 1229 ? -25.741  19.312  -26.426 1.00 116.70 ? 1229 LYS A O   1 
ATOM   9392  C  CB  . LYS A 1 1229 ? -24.412  16.470  -26.047 1.00 109.57 ? 1229 LYS A CB  1 
ATOM   9393  C  CG  . LYS A 1 1229 ? -23.651  15.584  -25.089 1.00 113.13 ? 1229 LYS A CG  1 
ATOM   9394  C  CD  . LYS A 1 1229 ? -22.572  14.704  -25.811 1.00 148.97 ? 1229 LYS A CD  1 
ATOM   9395  C  CE  . LYS A 1 1229 ? -21.202  15.393  -26.022 1.00 145.92 ? 1229 LYS A CE  1 
ATOM   9396  N  NZ  . LYS A 1 1229 ? -20.443  15.799  -24.782 1.00 142.27 ? 1229 LYS A NZ  1 
ATOM   9397  N  N   . ASP A 1 1230 ? -24.797  19.164  -24.408 1.00 128.46 ? 1230 ASP A N   1 
ATOM   9398  C  CA  . ASP A 1 1230 ? -24.650  20.618  -24.207 1.00 135.58 ? 1230 ASP A CA  1 
ATOM   9399  C  C   . ASP A 1 1230 ? -23.710  21.321  -25.196 1.00 143.36 ? 1230 ASP A C   1 
ATOM   9400  O  O   . ASP A 1 1230 ? -24.069  22.345  -25.780 1.00 141.24 ? 1230 ASP A O   1 
ATOM   9401  C  CB  . ASP A 1 1230 ? -24.184  20.915  -22.780 1.00 140.18 ? 1230 ASP A CB  1 
ATOM   9402  C  CG  . ASP A 1 1230 ? -23.768  22.355  -22.606 1.00 144.97 ? 1230 ASP A CG  1 
ATOM   9403  O  OD1 . ASP A 1 1230 ? -24.244  23.186  -23.405 1.00 145.51 ? 1230 ASP A OD1 1 
ATOM   9404  O  OD2 . ASP A 1 1230 ? -22.974  22.665  -21.686 1.00 147.48 ? 1230 ASP A OD2 1 
ATOM   9405  N  N   . ASN A 1 1231 ? -22.497  20.786  -25.328 1.00 151.85 ? 1231 ASN A N   1 
ATOM   9406  C  CA  . ASN A 1 1231 ? -21.549  21.152  -26.374 1.00 161.59 ? 1231 ASN A CA  1 
ATOM   9407  C  C   . ASN A 1 1231 ? -22.239  21.438  -27.699 1.00 166.81 ? 1231 ASN A C   1 
ATOM   9408  O  O   . ASN A 1 1231 ? -23.460  21.390  -27.794 1.00 164.66 ? 1231 ASN A O   1 
ATOM   9409  C  CB  . ASN A 1 1231 ? -20.614  19.971  -26.606 1.00 168.15 ? 1231 ASN A CB  1 
ATOM   9410  C  CG  . ASN A 1 1231 ? -21.226  18.908  -27.536 1.00 171.67 ? 1231 ASN A CG  1 
ATOM   9411  O  OD1 . ASN A 1 1231 ? -21.817  17.933  -27.079 1.00 172.92 ? 1231 ASN A OD1 1 
ATOM   9412  N  ND2 . ASN A 1 1231 ? -21.090  19.109  -28.843 1.00 173.24 ? 1231 ASN A ND2 1 
ATOM   9413  N  N   . LEU A 1 1232 ? -21.449  21.681  -28.740 1.00 173.58 ? 1232 LEU A N   1 
ATOM   9414  C  CA  . LEU A 1 1232 ? -21.981  21.855  -30.088 1.00 175.87 ? 1232 LEU A CA  1 
ATOM   9415  C  C   . LEU A 1 1232 ? -21.020  21.269  -31.107 1.00 186.07 ? 1232 LEU A C   1 
ATOM   9416  O  O   . LEU A 1 1232 ? -19.965  21.849  -31.339 1.00 192.07 ? 1232 LEU A O   1 
ATOM   9417  C  CB  . LEU A 1 1232 ? -22.144  23.337  -30.377 1.00 166.08 ? 1232 LEU A CB  1 
ATOM   9418  C  CG  . LEU A 1 1232 ? -22.258  23.714  -31.842 1.00 155.83 ? 1232 LEU A CG  1 
ATOM   9419  C  CD1 . LEU A 1 1232 ? -23.710  23.857  -32.186 1.00 150.13 ? 1232 LEU A CD1 1 
ATOM   9420  C  CD2 . LEU A 1 1232 ? -21.520  25.012  -32.048 1.00 153.59 ? 1232 LEU A CD2 1 
ATOM   9421  N  N   . GLN A 1 1233 ? -21.376  20.126  -31.701 1.00 191.74 ? 1233 GLN A N   1 
ATOM   9422  C  CA  . GLN A 1 1233 ? -20.544  19.428  -32.705 1.00 199.97 ? 1233 GLN A CA  1 
ATOM   9423  C  C   . GLN A 1 1233 ? -19.019  19.306  -32.412 1.00 214.44 ? 1233 GLN A C   1 
ATOM   9424  O  O   . GLN A 1 1233 ? -18.230  19.017  -33.318 1.00 213.99 ? 1233 GLN A O   1 
ATOM   9425  C  CB  . GLN A 1 1233 ? -20.794  20.009  -34.109 1.00 208.26 ? 1233 GLN A CB  1 
ATOM   9426  C  CG  . GLN A 1 1233 ? -20.513  21.505  -34.215 1.00 217.48 ? 1233 GLN A CG  1 
ATOM   9427  C  CD  . GLN A 1 1233 ? -20.773  22.097  -35.593 1.00 223.90 ? 1233 GLN A CD  1 
ATOM   9428  O  OE1 . GLN A 1 1233 ? -20.282  21.597  -36.605 1.00 228.03 ? 1233 GLN A OE1 1 
ATOM   9429  N  NE2 . GLN A 1 1233 ? -21.531  23.189  -35.629 1.00 223.93 ? 1233 GLN A NE2 1 
ATOM   9430  N  N   . HIS A 1 1234 ? -18.613  19.541  -31.161 1.00 217.19 ? 1234 HIS A N   1 
ATOM   9431  C  CA  . HIS A 1 1234 ? -17.219  19.375  -30.724 1.00 221.46 ? 1234 HIS A CA  1 
ATOM   9432  C  C   . HIS A 1 1234 ? -17.010  17.968  -30.225 1.00 226.68 ? 1234 HIS A C   1 
ATOM   9433  O  O   . HIS A 1 1234 ? -15.935  17.607  -29.752 1.00 228.60 ? 1234 HIS A O   1 
ATOM   9434  C  CB  . HIS A 1 1234 ? -16.870  20.370  -29.628 1.00 217.62 ? 1234 HIS A CB  1 
ATOM   9435  C  CG  . HIS A 1 1234 ? -17.003  21.790  -30.065 1.00 213.80 ? 1234 HIS A CG  1 
ATOM   9436  N  ND1 . HIS A 1 1234 ? -16.347  22.283  -31.170 1.00 214.64 ? 1234 HIS A ND1 1 
ATOM   9437  C  CD2 . HIS A 1 1234 ? -17.732  22.816  -29.569 1.00 210.88 ? 1234 HIS A CD2 1 
ATOM   9438  C  CE1 . HIS A 1 1234 ? -16.655  23.557  -31.331 1.00 212.90 ? 1234 HIS A CE1 1 
ATOM   9439  N  NE2 . HIS A 1 1234 ? -17.495  23.905  -30.373 1.00 210.67 ? 1234 HIS A NE2 1 
ATOM   9440  N  N   . LYS A 1 1235 ? -18.097  17.213  -30.281 1.00 231.40 ? 1235 LYS A N   1 
ATOM   9441  C  CA  . LYS A 1 1235 ? -18.080  15.763  -30.255 1.00 239.02 ? 1235 LYS A CA  1 
ATOM   9442  C  C   . LYS A 1 1235 ? -16.901  15.125  -29.532 1.00 251.64 ? 1235 LYS A C   1 
ATOM   9443  O  O   . LYS A 1 1235 ? -16.251  14.234  -30.079 1.00 255.45 ? 1235 LYS A O   1 
ATOM   9444  C  CB  . LYS A 1 1235 ? -18.147  15.240  -31.691 1.00 237.09 ? 1235 LYS A CB  1 
ATOM   9445  C  CG  . LYS A 1 1235 ? -19.324  15.782  -32.498 1.00 231.40 ? 1235 LYS A CG  1 
ATOM   9446  C  CD  . LYS A 1 1235 ? -20.626  15.106  -32.105 1.00 226.16 ? 1235 LYS A CD  1 
ATOM   9447  C  CE  . LYS A 1 1235 ? -21.781  15.609  -32.946 1.00 221.26 ? 1235 LYS A CE  1 
ATOM   9448  N  NZ  . LYS A 1 1235 ? -22.005  17.064  -32.758 1.00 218.32 ? 1235 LYS A NZ  1 
ATOM   9449  N  N   . ASP A 1 1236 ? -16.612  15.564  -28.313 1.00 259.30 ? 1236 ASP A N   1 
ATOM   9450  C  CA  . ASP A 1 1236 ? -15.689  14.791  -27.499 1.00 270.22 ? 1236 ASP A CA  1 
ATOM   9451  C  C   . ASP A 1 1236 ? -16.407  13.478  -27.205 1.00 274.69 ? 1236 ASP A C   1 
ATOM   9452  O  O   . ASP A 1 1236 ? -15.779  12.453  -26.938 1.00 276.69 ? 1236 ASP A O   1 
ATOM   9453  C  CB  . ASP A 1 1236 ? -15.306  15.525  -26.213 1.00 273.56 ? 1236 ASP A CB  1 
ATOM   9454  C  CG  . ASP A 1 1236 ? -14.054  14.948  -25.563 1.00 280.00 ? 1236 ASP A CG  1 
ATOM   9455  O  OD1 . ASP A 1 1236 ? -13.820  13.730  -25.701 1.00 282.44 ? 1236 ASP A OD1 1 
ATOM   9456  O  OD2 . ASP A 1 1236 ? -13.303  15.709  -24.916 1.00 282.65 ? 1236 ASP A OD2 1 
ATOM   9457  N  N   . SER A 1 1237 ? -17.736  13.533  -27.284 1.00 276.10 ? 1237 SER A N   1 
ATOM   9458  C  CA  . SER A 1 1237 ? -18.621  12.369  -27.163 1.00 277.96 ? 1237 SER A CA  1 
ATOM   9459  C  C   . SER A 1 1237 ? -18.641  11.727  -25.784 1.00 279.01 ? 1237 SER A C   1 
ATOM   9460  O  O   . SER A 1 1237 ? -19.192  10.638  -25.609 1.00 282.56 ? 1237 SER A O   1 
ATOM   9461  C  CB  . SER A 1 1237 ? -18.319  11.313  -28.227 1.00 279.69 ? 1237 SER A CB  1 
ATOM   9462  O  OG  . SER A 1 1237 ? -19.307  10.296  -28.202 1.00 277.74 ? 1237 SER A OG  1 
ATOM   9463  N  N   . SER A 1 1238 ? -18.033  12.394  -24.809 1.00 275.04 ? 1238 SER A N   1 
ATOM   9464  C  CA  . SER A 1 1238 ? -18.172  11.966  -23.426 1.00 270.11 ? 1238 SER A CA  1 
ATOM   9465  C  C   . SER A 1 1238 ? -19.600  12.253  -22.957 1.00 260.46 ? 1238 SER A C   1 
ATOM   9466  O  O   . SER A 1 1238 ? -19.882  13.306  -22.379 1.00 253.37 ? 1238 SER A O   1 
ATOM   9467  C  CB  . SER A 1 1238 ? -17.140  12.652  -22.519 1.00 278.84 ? 1238 SER A CB  1 
ATOM   9468  O  OG  . SER A 1 1238 ? -17.275  14.064  -22.545 1.00 281.82 ? 1238 SER A OG  1 
ATOM   9469  N  N   . VAL A 1 1239 ? -20.503  11.317  -23.237 1.00 244.15 ? 1239 VAL A N   1 
ATOM   9470  C  CA  . VAL A 1 1239 ? -21.845  11.337  -22.674 1.00 237.13 ? 1239 VAL A CA  1 
ATOM   9471  C  C   . VAL A 1 1239 ? -21.846  10.321  -21.545 1.00 234.00 ? 1239 VAL A C   1 
ATOM   9472  O  O   . VAL A 1 1239 ? -22.828  9.613   -21.342 1.00 231.39 ? 1239 VAL A O   1 
ATOM   9473  C  CB  . VAL A 1 1239 ? -22.906  10.954  -23.727 1.00 236.99 ? 1239 VAL A CB  1 
ATOM   9474  C  CG1 . VAL A 1 1239 ? -22.666  11.706  -25.004 1.00 238.60 ? 1239 VAL A CG1 1 
ATOM   9475  C  CG2 . VAL A 1 1239 ? -22.864  9.471   -24.019 1.00 241.39 ? 1239 VAL A CG2 1 
ATOM   9476  N  N   . PRO A 1 1240 ? -20.745  10.290  -20.773 1.00 237.50 ? 1240 PRO A N   1 
ATOM   9477  C  CA  . PRO A 1 1240 ? -20.240  9.134   -20.024 1.00 238.61 ? 1240 PRO A CA  1 
ATOM   9478  C  C   . PRO A 1 1240 ? -21.316  8.392   -19.254 1.00 231.24 ? 1240 PRO A C   1 
ATOM   9479  O  O   . PRO A 1 1240 ? -21.329  8.435   -18.024 1.00 234.41 ? 1240 PRO A O   1 
ATOM   9480  C  CB  . PRO A 1 1240 ? -19.238  9.766   -19.040 1.00 243.86 ? 1240 PRO A CB  1 
ATOM   9481  C  CG  . PRO A 1 1240 ? -19.716  11.169  -18.891 1.00 242.01 ? 1240 PRO A CG  1 
ATOM   9482  C  CD  . PRO A 1 1240 ? -20.126  11.532  -20.278 1.00 239.38 ? 1240 PRO A CD  1 
ATOM   9483  N  N   . ASN A 1 1241 ? -22.206  7.716   -19.967 1.00 219.67 ? 1241 ASN A N   1 
ATOM   9484  C  CA  . ASN A 1 1241 ? -23.256  6.952   -19.314 1.00 207.12 ? 1241 ASN A CA  1 
ATOM   9485  C  C   . ASN A 1 1241 ? -23.946  7.799   -18.246 1.00 185.12 ? 1241 ASN A C   1 
ATOM   9486  O  O   . ASN A 1 1241 ? -24.410  7.265   -17.238 1.00 180.72 ? 1241 ASN A O   1 
ATOM   9487  C  CB  . ASN A 1 1241 ? -22.680  5.688   -18.649 1.00 220.01 ? 1241 ASN A CB  1 
ATOM   9488  C  CG  . ASN A 1 1241 ? -22.080  4.690   -19.653 1.00 230.19 ? 1241 ASN A CG  1 
ATOM   9489  O  OD1 . ASN A 1 1241 ? -22.511  4.604   -20.808 1.00 231.28 ? 1241 ASN A OD1 1 
ATOM   9490  N  ND2 . ASN A 1 1241 ? -21.091  3.915   -19.196 1.00 235.62 ? 1241 ASN A ND2 1 
ATOM   9491  N  N   . THR A 1 1242 ? -23.997  9.115   -18.443 1.00 166.16 ? 1242 THR A N   1 
ATOM   9492  C  CA  . THR A 1 1242 ? -24.548  9.979   -17.407 1.00 147.23 ? 1242 THR A CA  1 
ATOM   9493  C  C   . THR A 1 1242 ? -25.169  11.271  -17.888 1.00 124.39 ? 1242 THR A C   1 
ATOM   9494  O  O   . THR A 1 1242 ? -24.563  12.042  -18.638 1.00 118.29 ? 1242 THR A O   1 
ATOM   9495  C  CB  . THR A 1 1242 ? -23.493  10.353  -16.392 1.00 152.77 ? 1242 THR A CB  1 
ATOM   9496  O  OG1 . THR A 1 1242 ? -22.361  10.894  -17.085 1.00 155.85 ? 1242 THR A OG1 1 
ATOM   9497  C  CG2 . THR A 1 1242 ? -23.081  9.134   -15.563 1.00 155.40 ? 1242 THR A CG2 1 
ATOM   9498  N  N   . GLY A 1 1243 ? -26.385  11.494  -17.404 1.00 109.86 ? 1243 GLY A N   1 
ATOM   9499  C  CA  . GLY A 1 1243 ? -27.146  12.685  -17.707 1.00 99.16  ? 1243 GLY A CA  1 
ATOM   9500  C  C   . GLY A 1 1243 ? -26.663  13.876  -16.910 1.00 91.78  ? 1243 GLY A C   1 
ATOM   9501  O  O   . GLY A 1 1243 ? -25.658  13.798  -16.224 1.00 94.09  ? 1243 GLY A O   1 
ATOM   9502  N  N   . THR A 1 1244 ? -27.389  14.978  -16.975 1.00 84.99  ? 1244 THR A N   1 
ATOM   9503  C  CA  . THR A 1 1244 ? -26.831  16.223  -16.534 1.00 83.89  ? 1244 THR A CA  1 
ATOM   9504  C  C   . THR A 1 1244 ? -27.863  17.301  -16.550 1.00 90.32  ? 1244 THR A C   1 
ATOM   9505  O  O   . THR A 1 1244 ? -28.626  17.413  -17.499 1.00 91.82  ? 1244 THR A O   1 
ATOM   9506  C  CB  . THR A 1 1244 ? -25.830  16.695  -17.530 1.00 80.52  ? 1244 THR A CB  1 
ATOM   9507  O  OG1 . THR A 1 1244 ? -24.529  16.234  -17.162 1.00 81.55  ? 1244 THR A OG1 1 
ATOM   9508  C  CG2 . THR A 1 1244 ? -25.846  18.208  -17.582 1.00 79.09  ? 1244 THR A CG2 1 
ATOM   9509  N  N   . ALA A 1 1245 ? -27.856  18.131  -15.516 1.00 96.43  ? 1245 ALA A N   1 
ATOM   9510  C  CA  . ALA A 1 1245 ? -28.749  19.289  -15.456 1.00 97.07  ? 1245 ALA A CA  1 
ATOM   9511  C  C   . ALA A 1 1245 ? -28.901  20.015  -16.796 1.00 97.48  ? 1245 ALA A C   1 
ATOM   9512  O  O   . ALA A 1 1245 ? -30.022  20.319  -17.199 1.00 94.18  ? 1245 ALA A O   1 
ATOM   9513  C  CB  . ALA A 1 1245 ? -28.256  20.265  -14.400 1.00 98.59  ? 1245 ALA A CB  1 
ATOM   9514  N  N   . ARG A 1 1246 ? -27.778  20.302  -17.465 1.00 101.30 ? 1246 ARG A N   1 
ATOM   9515  C  CA  . ARG A 1 1246 ? -27.799  21.022  -18.741 1.00 102.06 ? 1246 ARG A CA  1 
ATOM   9516  C  C   . ARG A 1 1246 ? -28.141  20.105  -19.915 1.00 98.98  ? 1246 ARG A C   1 
ATOM   9517  O  O   . ARG A 1 1246 ? -28.867  20.487  -20.841 1.00 97.16  ? 1246 ARG A O   1 
ATOM   9518  C  CB  . ARG A 1 1246 ? -26.493  21.774  -19.002 1.00 103.96 ? 1246 ARG A CB  1 
ATOM   9519  C  CG  . ARG A 1 1246 ? -26.690  22.902  -20.003 1.00 104.59 ? 1246 ARG A CG  1 
ATOM   9520  C  CD  . ARG A 1 1246 ? -25.449  23.690  -20.193 1.00 110.01 ? 1246 ARG A CD  1 
ATOM   9521  N  NE  . ARG A 1 1246 ? -25.013  24.266  -18.939 1.00 117.45 ? 1246 ARG A NE  1 
ATOM   9522  C  CZ  . ARG A 1 1246 ? -24.855  25.568  -18.731 1.00 123.95 ? 1246 ARG A CZ  1 
ATOM   9523  N  NH1 . ARG A 1 1246 ? -25.089  26.421  -19.716 1.00 125.27 ? 1246 ARG A NH1 1 
ATOM   9524  N  NH2 . ARG A 1 1246 ? -24.453  26.021  -17.540 1.00 126.89 ? 1246 ARG A NH2 1 
ATOM   9525  N  N   . MET A 1 1247 ? -27.627  18.892  -19.877 1.00 96.35  ? 1247 MET A N   1 
ATOM   9526  C  CA  . MET A 1 1247 ? -28.106  17.905  -20.811 1.00 93.18  ? 1247 MET A CA  1 
ATOM   9527  C  C   . MET A 1 1247 ? -29.636  17.872  -20.864 1.00 90.50  ? 1247 MET A C   1 
ATOM   9528  O  O   . MET A 1 1247 ? -30.258  18.236  -21.869 1.00 88.90  ? 1247 MET A O   1 
ATOM   9529  C  CB  . MET A 1 1247 ? -27.621  16.551  -20.391 1.00 91.76  ? 1247 MET A CB  1 
ATOM   9530  C  CG  . MET A 1 1247 ? -27.696  15.553  -21.484 1.00 90.95  ? 1247 MET A CG  1 
ATOM   9531  S  SD  . MET A 1 1247 ? -26.238  14.554  -21.258 1.00 107.75 ? 1247 MET A SD  1 
ATOM   9532  C  CE  . MET A 1 1247 ? -25.002  15.838  -20.966 1.00 87.82  ? 1247 MET A CE  1 
ATOM   9533  N  N   . VAL A 1 1248 ? -30.244  17.424  -19.770 1.00 91.26  ? 1248 VAL A N   1 
ATOM   9534  C  CA  . VAL A 1 1248 ? -31.710  17.384  -19.678 1.00 87.60  ? 1248 VAL A CA  1 
ATOM   9535  C  C   . VAL A 1 1248 ? -32.318  18.743  -19.988 1.00 82.42  ? 1248 VAL A C   1 
ATOM   9536  O  O   . VAL A 1 1248 ? -33.452  18.821  -20.450 1.00 78.88  ? 1248 VAL A O   1 
ATOM   9537  C  CB  . VAL A 1 1248 ? -32.253  16.878  -18.281 1.00 63.58  ? 1248 VAL A CB  1 
ATOM   9538  C  CG1 . VAL A 1 1248 ? -33.783  17.050  -18.194 1.00 58.49  ? 1248 VAL A CG1 1 
ATOM   9539  C  CG2 . VAL A 1 1248 ? -31.841  15.409  -18.011 1.00 65.32  ? 1248 VAL A CG2 1 
ATOM   9540  N  N   . GLU A 1 1249 ? -31.577  19.815  -19.739 1.00 80.71  ? 1249 GLU A N   1 
ATOM   9541  C  CA  . GLU A 1 1249 ? -32.137  21.108  -20.041 1.00 82.74  ? 1249 GLU A CA  1 
ATOM   9542  C  C   . GLU A 1 1249 ? -32.277  21.254  -21.533 1.00 84.02  ? 1249 GLU A C   1 
ATOM   9543  O  O   . GLU A 1 1249 ? -33.382  21.485  -22.033 1.00 84.25  ? 1249 GLU A O   1 
ATOM   9544  C  CB  . GLU A 1 1249 ? -31.294  22.246  -19.516 1.00 87.47  ? 1249 GLU A CB  1 
ATOM   9545  C  CG  . GLU A 1 1249 ? -31.783  23.574  -20.037 1.00 91.70  ? 1249 GLU A CG  1 
ATOM   9546  C  CD  . GLU A 1 1249 ? -31.947  24.564  -18.938 1.00 98.12  ? 1249 GLU A CD  1 
ATOM   9547  O  OE1 . GLU A 1 1249 ? -31.649  24.162  -17.797 1.00 103.18 ? 1249 GLU A OE1 1 
ATOM   9548  O  OE2 . GLU A 1 1249 ? -32.364  25.722  -19.190 1.00 98.15  ? 1249 GLU A OE2 1 
ATOM   9549  N  N   . THR A 1 1250 ? -31.162  21.117  -22.256 1.00 83.39  ? 1250 THR A N   1 
ATOM   9550  C  CA  . THR A 1 1250 ? -31.173  21.422  -23.693 1.00 79.80  ? 1250 THR A CA  1 
ATOM   9551  C  C   . THR A 1 1250 ? -32.173  20.517  -24.402 1.00 72.47  ? 1250 THR A C   1 
ATOM   9552  O  O   . THR A 1 1250 ? -33.027  20.991  -25.144 1.00 67.54  ? 1250 THR A O   1 
ATOM   9553  C  CB  . THR A 1 1250 ? -29.783  21.313  -24.353 1.00 84.58  ? 1250 THR A CB  1 
ATOM   9554  O  OG1 . THR A 1 1250 ? -29.425  19.938  -24.481 1.00 88.25  ? 1250 THR A OG1 1 
ATOM   9555  C  CG2 . THR A 1 1250 ? -28.721  22.010  -23.525 1.00 84.45  ? 1250 THR A CG2 1 
ATOM   9556  N  N   . THR A 1 1251 ? -32.088  19.217  -24.147 1.00 71.36  ? 1251 THR A N   1 
ATOM   9557  C  CA  . THR A 1 1251 ? -32.988  18.300  -24.807 1.00 71.62  ? 1251 THR A CA  1 
ATOM   9558  C  C   . THR A 1 1251 ? -34.452  18.656  -24.489 1.00 71.17  ? 1251 THR A C   1 
ATOM   9559  O  O   . THR A 1 1251 ? -35.323  18.516  -25.328 1.00 72.39  ? 1251 THR A O   1 
ATOM   9560  C  CB  . THR A 1 1251 ? -32.610  16.817  -24.546 1.00 72.56  ? 1251 THR A CB  1 
ATOM   9561  O  OG1 . THR A 1 1251 ? -33.349  16.299  -23.440 1.00 74.83  ? 1251 THR A OG1 1 
ATOM   9562  C  CG2 . THR A 1 1251 ? -31.144  16.699  -24.250 1.00 71.65  ? 1251 THR A CG2 1 
ATOM   9563  N  N   . ALA A 1 1252 ? -34.732  19.170  -23.307 1.00 69.74  ? 1252 ALA A N   1 
ATOM   9564  C  CA  . ALA A 1 1252 ? -36.076  19.654  -23.074 1.00 71.30  ? 1252 ALA A CA  1 
ATOM   9565  C  C   . ALA A 1 1252 ? -36.359  20.845  -24.006 1.00 72.25  ? 1252 ALA A C   1 
ATOM   9566  O  O   . ALA A 1 1252 ? -37.456  20.988  -24.532 1.00 70.16  ? 1252 ALA A O   1 
ATOM   9567  C  CB  . ALA A 1 1252 ? -36.280  20.016  -21.622 1.00 72.54  ? 1252 ALA A CB  1 
ATOM   9568  N  N   . TYR A 1 1253 ? -35.375  21.700  -24.236 1.00 75.69  ? 1253 TYR A N   1 
ATOM   9569  C  CA  . TYR A 1 1253 ? -35.599  22.800  -25.173 1.00 78.15  ? 1253 TYR A CA  1 
ATOM   9570  C  C   . TYR A 1 1253 ? -35.890  22.342  -26.591 1.00 78.12  ? 1253 TYR A C   1 
ATOM   9571  O  O   . TYR A 1 1253 ? -36.740  22.933  -27.251 1.00 80.15  ? 1253 TYR A O   1 
ATOM   9572  C  CB  . TYR A 1 1253 ? -34.422  23.756  -25.199 1.00 81.44  ? 1253 TYR A CB  1 
ATOM   9573  C  CG  . TYR A 1 1253 ? -34.485  24.669  -24.033 1.00 84.36  ? 1253 TYR A CG  1 
ATOM   9574  C  CD1 . TYR A 1 1253 ? -35.553  25.544  -23.878 1.00 84.09  ? 1253 TYR A CD1 1 
ATOM   9575  C  CD2 . TYR A 1 1253 ? -33.517  24.629  -23.053 1.00 85.53  ? 1253 TYR A CD2 1 
ATOM   9576  C  CE1 . TYR A 1 1253 ? -35.620  26.368  -22.802 1.00 83.44  ? 1253 TYR A CE1 1 
ATOM   9577  C  CE2 . TYR A 1 1253 ? -33.587  25.449  -21.971 1.00 85.50  ? 1253 TYR A CE2 1 
ATOM   9578  C  CZ  . TYR A 1 1253 ? -34.636  26.311  -21.850 1.00 84.68  ? 1253 TYR A CZ  1 
ATOM   9579  O  OH  . TYR A 1 1253 ? -34.691  27.106  -20.737 1.00 87.51  ? 1253 TYR A OH  1 
ATOM   9580  N  N   . ALA A 1 1254 ? -35.158  21.331  -27.071 1.00 73.96  ? 1254 ALA A N   1 
ATOM   9581  C  CA  . ALA A 1 1254 ? -35.478  20.672  -28.330 1.00 67.60  ? 1254 ALA A CA  1 
ATOM   9582  C  C   . ALA A 1 1254 ? -36.884  20.059  -28.247 1.00 65.78  ? 1254 ALA A C   1 
ATOM   9583  O  O   . ALA A 1 1254 ? -37.808  20.500  -28.945 1.00 62.77  ? 1254 ALA A O   1 
ATOM   9584  C  CB  . ALA A 1 1254 ? -34.429  19.628  -28.667 1.00 64.82  ? 1254 ALA A CB  1 
ATOM   9585  N  N   . LEU A 1 1255 ? -37.056  19.078  -27.367 1.00 68.32  ? 1255 LEU A N   1 
ATOM   9586  C  CA  . LEU A 1 1255 ? -38.376  18.473  -27.149 1.00 72.31  ? 1255 LEU A CA  1 
ATOM   9587  C  C   . LEU A 1 1255 ? -39.513  19.483  -27.061 1.00 70.52  ? 1255 LEU A C   1 
ATOM   9588  O  O   . LEU A 1 1255 ? -40.642  19.189  -27.449 1.00 67.15  ? 1255 LEU A O   1 
ATOM   9589  C  CB  . LEU A 1 1255 ? -38.418  17.624  -25.872 1.00 76.61  ? 1255 LEU A CB  1 
ATOM   9590  C  CG  . LEU A 1 1255 ? -39.845  17.187  -25.497 1.00 76.73  ? 1255 LEU A CG  1 
ATOM   9591  C  CD1 . LEU A 1 1255 ? -40.469  16.298  -26.598 1.00 76.38  ? 1255 LEU A CD1 1 
ATOM   9592  C  CD2 . LEU A 1 1255 ? -39.940  16.513  -24.114 1.00 76.02  ? 1255 LEU A CD2 1 
ATOM   9593  N  N   . LEU A 1 1256 ? -39.230  20.653  -26.504 1.00 73.36  ? 1256 LEU A N   1 
ATOM   9594  C  CA  . LEU A 1 1256 ? -40.287  21.634  -26.292 1.00 78.10  ? 1256 LEU A CA  1 
ATOM   9595  C  C   . LEU A 1 1256 ? -40.562  22.392  -27.577 1.00 81.21  ? 1256 LEU A C   1 
ATOM   9596  O  O   . LEU A 1 1256 ? -41.729  22.706  -27.864 1.00 82.50  ? 1256 LEU A O   1 
ATOM   9597  C  CB  . LEU A 1 1256 ? -39.966  22.595  -25.140 1.00 80.26  ? 1256 LEU A CB  1 
ATOM   9598  C  CG  . LEU A 1 1256 ? -40.423  22.293  -23.706 1.00 80.46  ? 1256 LEU A CG  1 
ATOM   9599  C  CD1 . LEU A 1 1256 ? -40.191  23.534  -22.905 1.00 83.17  ? 1256 LEU A CD1 1 
ATOM   9600  C  CD2 . LEU A 1 1256 ? -41.874  21.873  -23.561 1.00 76.70  ? 1256 LEU A CD2 1 
ATOM   9601  N  N   . THR A 1 1257 ? -39.489  22.682  -28.333 1.00 80.60  ? 1257 THR A N   1 
ATOM   9602  C  CA  . THR A 1 1257 ? -39.576  23.295  -29.667 1.00 77.98  ? 1257 THR A CA  1 
ATOM   9603  C  C   . THR A 1 1257 ? -40.400  22.362  -30.531 1.00 73.36  ? 1257 THR A C   1 
ATOM   9604  O  O   . THR A 1 1257 ? -41.529  22.699  -30.949 1.00 70.11  ? 1257 THR A O   1 
ATOM   9605  C  CB  . THR A 1 1257 ? -38.187  23.511  -30.324 1.00 67.38  ? 1257 THR A CB  1 
ATOM   9606  O  OG1 . THR A 1 1257 ? -37.355  24.253  -29.430 1.00 68.86  ? 1257 THR A OG1 1 
ATOM   9607  C  CG2 . THR A 1 1257 ? -38.324  24.322  -31.590 1.00 65.77  ? 1257 THR A CG2 1 
ATOM   9608  N  N   . SER A 1 1258 ? -39.853  21.169  -30.738 1.00 72.89  ? 1258 SER A N   1 
ATOM   9609  C  CA  . SER A 1 1258 ? -40.576  20.114  -31.428 1.00 76.17  ? 1258 SER A CA  1 
ATOM   9610  C  C   . SER A 1 1258 ? -42.040  19.935  -30.989 1.00 76.16  ? 1258 SER A C   1 
ATOM   9611  O  O   . SER A 1 1258 ? -42.937  19.985  -31.827 1.00 74.47  ? 1258 SER A O   1 
ATOM   9612  C  CB  . SER A 1 1258 ? -39.801  18.808  -31.331 1.00 77.33  ? 1258 SER A CB  1 
ATOM   9613  O  OG  . SER A 1 1258 ? -38.559  18.947  -31.983 1.00 78.63  ? 1258 SER A OG  1 
ATOM   9614  N  N   . LEU A 1 1259 ? -42.281  19.727  -29.696 1.00 77.39  ? 1259 LEU A N   1 
ATOM   9615  C  CA  . LEU A 1 1259 ? -43.651  19.543  -29.202 1.00 74.76  ? 1259 LEU A CA  1 
ATOM   9616  C  C   . LEU A 1 1259 ? -44.568  20.669  -29.683 1.00 74.68  ? 1259 LEU A C   1 
ATOM   9617  O  O   . LEU A 1 1259 ? -45.795  20.482  -29.861 1.00 73.67  ? 1259 LEU A O   1 
ATOM   9618  C  CB  . LEU A 1 1259 ? -43.695  19.377  -27.676 1.00 70.11  ? 1259 LEU A CB  1 
ATOM   9619  C  CG  . LEU A 1 1259 ? -43.595  17.904  -27.268 1.00 66.54  ? 1259 LEU A CG  1 
ATOM   9620  C  CD1 . LEU A 1 1259 ? -43.548  17.769  -25.783 1.00 67.70  ? 1259 LEU A CD1 1 
ATOM   9621  C  CD2 . LEU A 1 1259 ? -44.755  17.080  -27.833 1.00 63.64  ? 1259 LEU A CD2 1 
ATOM   9622  N  N   . ASN A 1 1260 ? -43.965  21.828  -29.925 1.00 75.15  ? 1260 ASN A N   1 
ATOM   9623  C  CA  . ASN A 1 1260 ? -44.710  22.946  -30.458 1.00 77.19  ? 1260 ASN A CA  1 
ATOM   9624  C  C   . ASN A 1 1260 ? -45.141  22.721  -31.907 1.00 80.36  ? 1260 ASN A C   1 
ATOM   9625  O  O   . ASN A 1 1260 ? -46.322  22.887  -32.254 1.00 83.45  ? 1260 ASN A O   1 
ATOM   9626  C  CB  . ASN A 1 1260 ? -43.927  24.242  -30.281 1.00 75.50  ? 1260 ASN A CB  1 
ATOM   9627  C  CG  . ASN A 1 1260 ? -44.507  25.104  -29.178 1.00 77.07  ? 1260 ASN A CG  1 
ATOM   9628  O  OD1 . ASN A 1 1260 ? -45.722  25.270  -29.088 1.00 79.06  ? 1260 ASN A OD1 1 
ATOM   9629  N  ND2 . ASN A 1 1260 ? -43.652  25.637  -28.325 1.00 76.39  ? 1260 ASN A ND2 1 
ATOM   9630  N  N   . LEU A 1 1261 ? -44.185  22.307  -32.732 1.00 77.32  ? 1261 LEU A N   1 
ATOM   9631  C  CA  . LEU A 1 1261 ? -44.421  22.038  -34.139 1.00 72.37  ? 1261 LEU A CA  1 
ATOM   9632  C  C   . LEU A 1 1261 ? -45.069  20.656  -34.362 1.00 71.77  ? 1261 LEU A C   1 
ATOM   9633  O  O   . LEU A 1 1261 ? -44.815  19.990  -35.360 1.00 70.93  ? 1261 LEU A O   1 
ATOM   9634  C  CB  . LEU A 1 1261 ? -43.096  22.161  -34.873 1.00 68.65  ? 1261 LEU A CB  1 
ATOM   9635  C  CG  . LEU A 1 1261 ? -42.215  23.367  -34.534 1.00 66.34  ? 1261 LEU A CG  1 
ATOM   9636  C  CD1 . LEU A 1 1261 ? -40.886  23.288  -35.317 1.00 67.53  ? 1261 LEU A CD1 1 
ATOM   9637  C  CD2 . LEU A 1 1261 ? -42.915  24.730  -34.738 1.00 62.51  ? 1261 LEU A CD2 1 
ATOM   9638  N  N   . LYS A 1 1262 ? -45.914  20.245  -33.418 1.00 72.41  ? 1262 LYS A N   1 
ATOM   9639  C  CA  . LYS A 1 1262 ? -46.537  18.917  -33.401 1.00 71.30  ? 1262 LYS A CA  1 
ATOM   9640  C  C   . LYS A 1 1262 ? -45.703  17.857  -34.104 1.00 67.88  ? 1262 LYS A C   1 
ATOM   9641  O  O   . LYS A 1 1262 ? -46.236  16.954  -34.721 1.00 66.95  ? 1262 LYS A O   1 
ATOM   9642  C  CB  . LYS A 1 1262 ? -47.957  19.000  -33.931 1.00 75.61  ? 1262 LYS A CB  1 
ATOM   9643  C  CG  . LYS A 1 1262 ? -48.562  20.356  -33.573 1.00 84.35  ? 1262 LYS A CG  1 
ATOM   9644  C  CD  . LYS A 1 1262 ? -49.984  20.283  -33.008 1.00 92.89  ? 1262 LYS A CD  1 
ATOM   9645  C  CE  . LYS A 1 1262 ? -50.164  21.315  -31.893 1.00 97.62  ? 1262 LYS A CE  1 
ATOM   9646  N  NZ  . LYS A 1 1262 ? -48.958  21.330  -30.965 1.00 99.18  ? 1262 LYS A NZ  1 
ATOM   9647  N  N   . ASP A 1 1263 ? -44.387  17.966  -33.938 1.00 65.66  ? 1263 ASP A N   1 
ATOM   9648  C  CA  . ASP A 1 1263 ? -43.395  17.127  -34.590 1.00 67.15  ? 1263 ASP A CA  1 
ATOM   9649  C  C   . ASP A 1 1263 ? -43.463  15.693  -34.136 1.00 64.73  ? 1263 ASP A C   1 
ATOM   9650  O  O   . ASP A 1 1263 ? -42.493  14.975  -34.219 1.00 69.24  ? 1263 ASP A O   1 
ATOM   9651  C  CB  . ASP A 1 1263 ? -42.006  17.671  -34.241 1.00 69.42  ? 1263 ASP A CB  1 
ATOM   9652  C  CG  . ASP A 1 1263 ? -40.974  17.519  -35.395 1.00 96.69  ? 1263 ASP A CG  1 
ATOM   9653  O  OD1 . ASP A 1 1263 ? -41.102  16.516  -36.173 1.00 95.97  ? 1263 ASP A OD1 1 
ATOM   9654  O  OD2 . ASP A 1 1263 ? -40.055  18.412  -35.492 1.00 94.88  ? 1263 ASP A OD2 1 
ATOM   9655  N  N   . ILE A 1 1264 ? -44.638  15.279  -33.710 1.00 62.13  ? 1264 ILE A N   1 
ATOM   9656  C  CA  . ILE A 1 1264 ? -44.891  14.027  -32.988 1.00 64.58  ? 1264 ILE A CA  1 
ATOM   9657  C  C   . ILE A 1 1264 ? -43.977  12.813  -33.049 1.00 68.12  ? 1264 ILE A C   1 
ATOM   9658  O  O   . ILE A 1 1264 ? -43.521  12.329  -32.020 1.00 69.40  ? 1264 ILE A O   1 
ATOM   9659  C  CB  . ILE A 1 1264 ? -46.272  13.579  -33.266 1.00 59.59  ? 1264 ILE A CB  1 
ATOM   9660  C  CG1 . ILE A 1 1264 ? -47.161  14.777  -32.940 1.00 57.74  ? 1264 ILE A CG1 1 
ATOM   9661  C  CG2 . ILE A 1 1264 ? -46.546  12.304  -32.478 1.00 43.25  ? 1264 ILE A CG2 1 
ATOM   9662  C  CD1 . ILE A 1 1264 ? -48.561  14.524  -33.029 1.00 56.65  ? 1264 ILE A CD1 1 
ATOM   9663  N  N   . ASN A 1 1265 ? -43.734  12.279  -34.227 1.00 71.82  ? 1265 ASN A N   1 
ATOM   9664  C  CA  . ASN A 1 1265 ? -42.841  11.127  -34.295 1.00 78.65  ? 1265 ASN A CA  1 
ATOM   9665  C  C   . ASN A 1 1265 ? -41.422  11.404  -33.803 1.00 79.68  ? 1265 ASN A C   1 
ATOM   9666  O  O   . ASN A 1 1265 ? -40.846  10.587  -33.085 1.00 81.24  ? 1265 ASN A O   1 
ATOM   9667  C  CB  . ASN A 1 1265 ? -42.829  10.489  -35.691 1.00 82.76  ? 1265 ASN A CB  1 
ATOM   9668  C  CG  . ASN A 1 1265 ? -43.870  9.391   -35.822 1.00 88.20  ? 1265 ASN A CG  1 
ATOM   9669  O  OD1 . ASN A 1 1265 ? -43.738  8.336   -35.214 1.00 91.96  ? 1265 ASN A OD1 1 
ATOM   9670  N  ND2 . ASN A 1 1265 ? -44.915  9.638   -36.605 1.00 88.26  ? 1265 ASN A ND2 1 
ATOM   9671  N  N   . TYR A 1 1266 ? -40.869  12.555  -34.196 1.00 79.79  ? 1266 TYR A N   1 
ATOM   9672  C  CA  . TYR A 1 1266 ? -39.477  12.922  -33.883 1.00 79.45  ? 1266 TYR A CA  1 
ATOM   9673  C  C   . TYR A 1 1266 ? -39.254  12.719  -32.425 1.00 82.47  ? 1266 TYR A C   1 
ATOM   9674  O  O   . TYR A 1 1266 ? -38.227  12.178  -32.005 1.00 86.78  ? 1266 TYR A O   1 
ATOM   9675  C  CB  . TYR A 1 1266 ? -39.232  14.414  -34.140 1.00 73.92  ? 1266 TYR A CB  1 
ATOM   9676  C  CG  . TYR A 1 1266 ? -37.785  14.822  -34.056 1.00 70.18  ? 1266 TYR A CG  1 
ATOM   9677  C  CD1 . TYR A 1 1266 ? -36.813  14.031  -34.621 1.00 70.63  ? 1266 TYR A CD1 1 
ATOM   9678  C  CD2 . TYR A 1 1266 ? -37.393  16.006  -33.432 1.00 67.84  ? 1266 TYR A CD2 1 
ATOM   9679  C  CE1 . TYR A 1 1266 ? -35.479  14.393  -34.573 1.00 73.36  ? 1266 TYR A CE1 1 
ATOM   9680  C  CE2 . TYR A 1 1266 ? -36.046  16.386  -33.373 1.00 68.49  ? 1266 TYR A CE2 1 
ATOM   9681  C  CZ  . TYR A 1 1266 ? -35.087  15.564  -33.956 1.00 71.64  ? 1266 TYR A CZ  1 
ATOM   9682  O  OH  . TYR A 1 1266 ? -33.728  15.855  -33.954 1.00 72.35  ? 1266 TYR A OH  1 
ATOM   9683  N  N   . VAL A 1 1267 ? -40.277  13.148  -31.687 1.00 77.90  ? 1267 VAL A N   1 
ATOM   9684  C  CA  . VAL A 1 1267 ? -40.222  13.470  -30.290 1.00 71.81  ? 1267 VAL A CA  1 
ATOM   9685  C  C   . VAL A 1 1267 ? -40.300  12.228  -29.445 1.00 72.34  ? 1267 VAL A C   1 
ATOM   9686  O  O   . VAL A 1 1267 ? -39.654  12.153  -28.432 1.00 72.05  ? 1267 VAL A O   1 
ATOM   9687  C  CB  . VAL A 1 1267 ? -41.335  14.463  -29.982 1.00 69.00  ? 1267 VAL A CB  1 
ATOM   9688  C  CG1 . VAL A 1 1267 ? -42.193  14.003  -28.830 1.00 68.42  ? 1267 VAL A CG1 1 
ATOM   9689  C  CG2 . VAL A 1 1267 ? -40.772  15.861  -29.767 1.00 66.94  ? 1267 VAL A CG2 1 
ATOM   9690  N  N   . ASN A 1 1268 ? -41.043  11.226  -29.879 1.00 75.89  ? 1268 ASN A N   1 
ATOM   9691  C  CA  . ASN A 1 1268 ? -41.135  9.994   -29.095 1.00 84.55  ? 1268 ASN A CA  1 
ATOM   9692  C  C   . ASN A 1 1268 ? -39.852  9.586   -28.356 1.00 87.02  ? 1268 ASN A C   1 
ATOM   9693  O  O   . ASN A 1 1268 ? -39.834  9.645   -27.138 1.00 91.42  ? 1268 ASN A O   1 
ATOM   9694  C  CB  . ASN A 1 1268 ? -41.684  8.832   -29.927 1.00 90.83  ? 1268 ASN A CB  1 
ATOM   9695  C  CG  . ASN A 1 1268 ? -43.091  9.094   -30.435 1.00 96.38  ? 1268 ASN A CG  1 
ATOM   9696  O  OD1 . ASN A 1 1268 ? -43.919  9.703   -29.744 1.00 97.51  ? 1268 ASN A OD1 1 
ATOM   9697  N  ND2 . ASN A 1 1268 ? -43.374  8.625   -31.645 1.00 98.42  ? 1268 ASN A ND2 1 
ATOM   9698  N  N   . PRO A 1 1269 ? -38.770  9.214   -29.078 1.00 87.94  ? 1269 PRO A N   1 
ATOM   9699  C  CA  . PRO A 1 1269 ? -37.526  8.718   -28.457 1.00 86.43  ? 1269 PRO A CA  1 
ATOM   9700  C  C   . PRO A 1 1269 ? -36.880  9.762   -27.553 1.00 82.30  ? 1269 PRO A C   1 
ATOM   9701  O  O   . PRO A 1 1269 ? -36.079  9.465   -26.659 1.00 80.69  ? 1269 PRO A O   1 
ATOM   9702  C  CB  . PRO A 1 1269 ? -36.585  8.482   -29.648 1.00 90.92  ? 1269 PRO A CB  1 
ATOM   9703  C  CG  . PRO A 1 1269 ? -37.384  8.729   -30.871 1.00 91.90  ? 1269 PRO A CG  1 
ATOM   9704  C  CD  . PRO A 1 1269 ? -38.551  9.572   -30.484 1.00 89.65  ? 1269 PRO A CD  1 
ATOM   9705  N  N   . VAL A 1 1270 ? -37.215  11.008  -27.827 1.00 76.20  ? 1270 VAL A N   1 
ATOM   9706  C  CA  . VAL A 1 1270 ? -36.896  12.060  -26.909 1.00 72.49  ? 1270 VAL A CA  1 
ATOM   9707  C  C   . VAL A 1 1270 ? -37.598  11.837  -25.573 1.00 68.14  ? 1270 VAL A C   1 
ATOM   9708  O  O   . VAL A 1 1270 ? -36.946  11.689  -24.556 1.00 70.06  ? 1270 VAL A O   1 
ATOM   9709  C  CB  . VAL A 1 1270 ? -37.257  13.389  -27.511 1.00 70.41  ? 1270 VAL A CB  1 
ATOM   9710  C  CG1 . VAL A 1 1270 ? -37.718  14.365  -26.439 1.00 67.33  ? 1270 VAL A CG1 1 
ATOM   9711  C  CG2 . VAL A 1 1270 ? -36.085  13.904  -28.328 1.00 71.91  ? 1270 VAL A CG2 1 
ATOM   9712  N  N   . ILE A 1 1271 ? -38.918  11.786  -25.537 1.00 63.65  ? 1271 ILE A N   1 
ATOM   9713  C  CA  . ILE A 1 1271 ? -39.519  11.526  -24.237 1.00 61.62  ? 1271 ILE A CA  1 
ATOM   9714  C  C   . ILE A 1 1271 ? -39.211  10.116  -23.727 1.00 61.57  ? 1271 ILE A C   1 
ATOM   9715  O  O   . ILE A 1 1271 ? -39.203  9.886   -22.550 1.00 63.79  ? 1271 ILE A O   1 
ATOM   9716  C  CB  . ILE A 1 1271 ? -41.047  11.936  -24.068 1.00 62.97  ? 1271 ILE A CB  1 
ATOM   9717  C  CG1 . ILE A 1 1271 ? -41.973  10.804  -24.460 1.00 62.59  ? 1271 ILE A CG1 1 
ATOM   9718  C  CG2 . ILE A 1 1271 ? -41.392  13.251  -24.753 1.00 62.74  ? 1271 ILE A CG2 1 
ATOM   9719  C  CD1 . ILE A 1 1271 ? -42.167  9.814   -23.347 1.00 63.56  ? 1271 ILE A CD1 1 
ATOM   9720  N  N   . LYS A 1 1272 ? -38.932  9.148   -24.569 1.00 63.37  ? 1272 LYS A N   1 
ATOM   9721  C  CA  . LYS A 1 1272 ? -38.561  7.857   -23.972 1.00 70.91  ? 1272 LYS A CA  1 
ATOM   9722  C  C   . LYS A 1 1272 ? -37.397  8.072   -23.000 1.00 74.90  ? 1272 LYS A C   1 
ATOM   9723  O  O   . LYS A 1 1272 ? -37.338  7.426   -21.954 1.00 77.53  ? 1272 LYS A O   1 
ATOM   9724  C  CB  . LYS A 1 1272 ? -38.222  6.779   -25.033 1.00 74.89  ? 1272 LYS A CB  1 
ATOM   9725  C  CG  . LYS A 1 1272 ? -37.518  5.507   -24.546 1.00 75.04  ? 1272 LYS A CG  1 
ATOM   9726  C  CD  . LYS A 1 1272 ? -38.453  4.362   -24.248 1.00 75.22  ? 1272 LYS A CD  1 
ATOM   9727  C  CE  . LYS A 1 1272 ? -37.629  3.083   -24.189 1.00 79.63  ? 1272 LYS A CE  1 
ATOM   9728  N  NZ  . LYS A 1 1272 ? -38.322  1.924   -23.529 1.00 82.30  ? 1272 LYS A NZ  1 
ATOM   9729  N  N   . TRP A 1 1273 ? -36.502  9.003   -23.350 1.00 73.30  ? 1273 TRP A N   1 
ATOM   9730  C  CA  . TRP A 1 1273 ? -35.263  9.281   -22.606 1.00 70.31  ? 1273 TRP A CA  1 
ATOM   9731  C  C   . TRP A 1 1273 ? -35.465  10.256  -21.442 1.00 65.73  ? 1273 TRP A C   1 
ATOM   9732  O  O   . TRP A 1 1273 ? -34.877  10.053  -20.401 1.00 68.01  ? 1273 TRP A O   1 
ATOM   9733  C  CB  . TRP A 1 1273 ? -34.163  9.719   -23.594 1.00 70.47  ? 1273 TRP A CB  1 
ATOM   9734  C  CG  . TRP A 1 1273 ? -32.874  10.293  -23.068 1.00 71.11  ? 1273 TRP A CG  1 
ATOM   9735  C  CD1 . TRP A 1 1273 ? -31.645  9.688   -23.050 1.00 74.51  ? 1273 TRP A CD1 1 
ATOM   9736  C  CD2 . TRP A 1 1273 ? -32.676  11.615  -22.569 1.00 70.39  ? 1273 TRP A CD2 1 
ATOM   9737  N  NE1 . TRP A 1 1273 ? -30.690  10.555  -22.539 1.00 74.63  ? 1273 TRP A NE1 1 
ATOM   9738  C  CE2 . TRP A 1 1273 ? -31.305  11.733  -22.235 1.00 71.85  ? 1273 TRP A CE2 1 
ATOM   9739  C  CE3 . TRP A 1 1273 ? -33.525  12.698  -22.350 1.00 70.17  ? 1273 TRP A CE3 1 
ATOM   9740  C  CZ2 . TRP A 1 1273 ? -30.784  12.892  -21.697 1.00 73.19  ? 1273 TRP A CZ2 1 
ATOM   9741  C  CZ3 . TRP A 1 1273 ? -32.993  13.845  -21.829 1.00 71.25  ? 1273 TRP A CZ3 1 
ATOM   9742  C  CH2 . TRP A 1 1273 ? -31.634  13.934  -21.501 1.00 72.58  ? 1273 TRP A CH2 1 
ATOM   9743  N  N   . LEU A 1 1274 ? -36.303  11.279  -21.575 1.00 61.28  ? 1274 LEU A N   1 
ATOM   9744  C  CA  . LEU A 1 1274 ? -36.744  11.979  -20.363 1.00 65.32  ? 1274 LEU A CA  1 
ATOM   9745  C  C   . LEU A 1 1274 ? -37.473  11.067  -19.334 1.00 70.55  ? 1274 LEU A C   1 
ATOM   9746  O  O   . LEU A 1 1274 ? -36.969  10.807  -18.272 1.00 73.04  ? 1274 LEU A O   1 
ATOM   9747  C  CB  . LEU A 1 1274 ? -37.537  13.246  -20.685 1.00 68.77  ? 1274 LEU A CB  1 
ATOM   9748  C  CG  . LEU A 1 1274 ? -36.662  14.389  -21.211 1.00 72.67  ? 1274 LEU A CG  1 
ATOM   9749  C  CD1 . LEU A 1 1274 ? -37.445  15.709  -21.358 1.00 72.70  ? 1274 LEU A CD1 1 
ATOM   9750  C  CD2 . LEU A 1 1274 ? -35.510  14.591  -20.275 1.00 74.17  ? 1274 LEU A CD2 1 
ATOM   9751  N  N   . SER A 1 1275 ? -38.639  10.548  -19.656 1.00 69.53  ? 1275 SER A N   1 
ATOM   9752  C  CA  . SER A 1 1275 ? -39.363  9.623   -18.770 1.00 74.61  ? 1275 SER A CA  1 
ATOM   9753  C  C   . SER A 1 1275 ? -38.565  8.401   -18.313 1.00 75.54  ? 1275 SER A C   1 
ATOM   9754  O  O   . SER A 1 1275 ? -39.151  7.356   -17.956 1.00 74.54  ? 1275 SER A O   1 
ATOM   9755  C  CB  . SER A 1 1275 ? -40.621  9.111   -19.473 1.00 82.71  ? 1275 SER A CB  1 
ATOM   9756  O  OG  . SER A 1 1275 ? -41.792  9.256   -18.699 1.00 87.53  ? 1275 SER A OG  1 
ATOM   9757  N  N   . GLU A 1 1276 ? -37.239  8.536   -18.332 1.00 79.87  ? 1276 GLU A N   1 
ATOM   9758  C  CA  . GLU A 1 1276 ? -36.299  7.481   -17.932 1.00 86.13  ? 1276 GLU A CA  1 
ATOM   9759  C  C   . GLU A 1 1276 ? -35.040  8.163   -17.496 1.00 87.04  ? 1276 GLU A C   1 
ATOM   9760  O  O   . GLU A 1 1276 ? -33.985  7.512   -17.416 1.00 90.10  ? 1276 GLU A O   1 
ATOM   9761  C  CB  . GLU A 1 1276 ? -35.869  6.608   -19.115 1.00 91.58  ? 1276 GLU A CB  1 
ATOM   9762  C  CG  . GLU A 1 1276 ? -36.820  5.474   -19.496 1.00 93.75  ? 1276 GLU A CG  1 
ATOM   9763  C  CD  . GLU A 1 1276 ? -36.118  4.371   -20.272 1.00 93.57  ? 1276 GLU A CD  1 
ATOM   9764  O  OE1 . GLU A 1 1276 ? -34.925  4.563   -20.621 1.00 92.77  ? 1276 GLU A OE1 1 
ATOM   9765  O  OE2 . GLU A 1 1276 ? -36.764  3.318   -20.505 1.00 93.97  ? 1276 GLU A OE2 1 
ATOM   9766  N  N   . GLU A 1 1277 ? -35.148  9.480   -17.298 1.00 84.62  ? 1277 GLU A N   1 
ATOM   9767  C  CA  . GLU A 1 1277 ? -34.045  10.338  -16.863 1.00 85.97  ? 1277 GLU A CA  1 
ATOM   9768  C  C   . GLU A 1 1277 ? -34.374  10.913  -15.502 1.00 85.05  ? 1277 GLU A C   1 
ATOM   9769  O  O   . GLU A 1 1277 ? -33.645  10.671  -14.522 1.00 85.40  ? 1277 GLU A O   1 
ATOM   9770  C  CB  . GLU A 1 1277 ? -33.803  11.469  -17.873 1.00 85.65  ? 1277 GLU A CB  1 
ATOM   9771  C  CG  . GLU A 1 1277 ? -32.403  12.087  -17.853 1.00 86.43  ? 1277 GLU A CG  1 
ATOM   9772  C  CD  . GLU A 1 1277 ? -31.328  11.053  -18.044 1.00 88.72  ? 1277 GLU A CD  1 
ATOM   9773  O  OE1 . GLU A 1 1277 ? -30.137  11.380  -17.886 1.00 90.97  ? 1277 GLU A OE1 1 
ATOM   9774  O  OE2 . GLU A 1 1277 ? -31.674  9.893   -18.318 1.00 89.32  ? 1277 GLU A OE2 1 
ATOM   9775  N  N   . GLN A 1 1278 ? -35.475  11.667  -15.478 1.00 85.35  ? 1278 GLN A N   1 
ATOM   9776  C  CA  . GLN A 1 1278 ? -36.098  12.164  -14.250 1.00 89.24  ? 1278 GLN A CA  1 
ATOM   9777  C  C   . GLN A 1 1278 ? -36.042  11.053  -13.188 1.00 93.60  ? 1278 GLN A C   1 
ATOM   9778  O  O   . GLN A 1 1278 ? -36.154  9.853   -13.510 1.00 93.93  ? 1278 GLN A O   1 
ATOM   9779  C  CB  . GLN A 1 1278 ? -37.550  12.681  -14.479 1.00 95.66  ? 1278 GLN A CB  1 
ATOM   9780  C  CG  . GLN A 1 1278 ? -37.758  13.689  -15.670 1.00 126.84 ? 1278 GLN A CG  1 
ATOM   9781  C  CD  . GLN A 1 1278 ? -36.833  14.953  -15.678 1.00 81.13  ? 1278 GLN A CD  1 
ATOM   9782  O  OE1 . GLN A 1 1278 ? -37.325  16.082  -15.800 1.00 79.11  ? 1278 GLN A OE1 1 
ATOM   9783  N  NE2 . GLN A 1 1278 ? -35.511  14.754  -15.566 1.00 80.93  ? 1278 GLN A NE2 1 
ATOM   9784  N  N   . ARG A 1 1279 ? -35.814  11.460  -11.935 1.00 93.50  ? 1279 ARG A N   1 
ATOM   9785  C  CA  . ARG A 1 1279 ? -35.502  10.523  -10.869 1.00 92.65  ? 1279 ARG A CA  1 
ATOM   9786  C  C   . ARG A 1 1279 ? -36.751  10.300  -10.109 1.00 87.16  ? 1279 ARG A C   1 
ATOM   9787  O  O   . ARG A 1 1279 ? -37.688  11.028  -10.326 1.00 85.19  ? 1279 ARG A O   1 
ATOM   9788  C  CB  . ARG A 1 1279 ? -34.438  11.117  -9.966  1.00 98.08  ? 1279 ARG A CB  1 
ATOM   9789  C  CG  . ARG A 1 1279 ? -33.177  11.442  -10.731 1.00 102.79 ? 1279 ARG A CG  1 
ATOM   9790  C  CD  . ARG A 1 1279 ? -31.905  10.795  -10.166 1.00 109.28 ? 1279 ARG A CD  1 
ATOM   9791  N  NE  . ARG A 1 1279 ? -31.901  10.715  -8.711  1.00 112.75 ? 1279 ARG A NE  1 
ATOM   9792  C  CZ  . ARG A 1 1279 ? -30.834  10.398  -8.003  1.00 116.33 ? 1279 ARG A CZ  1 
ATOM   9793  N  NH1 . ARG A 1 1279 ? -29.706  10.148  -8.635  1.00 116.56 ? 1279 ARG A NH1 1 
ATOM   9794  N  NH2 . ARG A 1 1279 ? -30.899  10.343  -6.681  1.00 118.58 ? 1279 ARG A NH2 1 
ATOM   9795  N  N   . TYR A 1 1280 ? -36.787  9.317   -9.218  1.00 87.45  ? 1280 TYR A N   1 
ATOM   9796  C  CA  . TYR A 1 1280 ? -37.976  9.118   -8.362  1.00 87.99  ? 1280 TYR A CA  1 
ATOM   9797  C  C   . TYR A 1 1280 ? -38.556  10.421  -7.735  1.00 68.73  ? 1280 TYR A C   1 
ATOM   9798  O  O   . TYR A 1 1280 ? -37.850  11.210  -7.126  1.00 67.40  ? 1280 TYR A O   1 
ATOM   9799  C  CB  . TYR A 1 1280 ? -37.638  8.098   -7.287  1.00 88.73  ? 1280 TYR A CB  1 
ATOM   9800  C  CG  . TYR A 1 1280 ? -38.562  8.090   -6.111  1.00 87.28  ? 1280 TYR A CG  1 
ATOM   9801  C  CD1 . TYR A 1 1280 ? -38.132  7.596   -4.891  1.00 92.66  ? 1280 TYR A CD1 1 
ATOM   9802  C  CD2 . TYR A 1 1280 ? -39.838  8.557   -6.204  1.00 83.02  ? 1280 TYR A CD2 1 
ATOM   9803  C  CE1 . TYR A 1 1280 ? -38.960  7.553   -3.781  1.00 93.68  ? 1280 TYR A CE1 1 
ATOM   9804  C  CE2 . TYR A 1 1280 ? -40.671  8.536   -5.099  1.00 86.51  ? 1280 TYR A CE2 1 
ATOM   9805  C  CZ  . TYR A 1 1280 ? -40.225  8.030   -3.884  1.00 91.44  ? 1280 TYR A CZ  1 
ATOM   9806  O  OH  . TYR A 1 1280 ? -41.031  7.996   -2.770  1.00 93.96  ? 1280 TYR A OH  1 
ATOM   9807  N  N   . GLY A 1 1281 ? -39.841  10.676  -7.902  1.00 68.55  ? 1281 GLY A N   1 
ATOM   9808  C  CA  . GLY A 1 1281 ? -40.350  11.943  -7.424  1.00 70.60  ? 1281 GLY A CA  1 
ATOM   9809  C  C   . GLY A 1 1281 ? -40.403  13.122  -8.381  1.00 75.85  ? 1281 GLY A C   1 
ATOM   9810  O  O   . GLY A 1 1281 ? -41.484  13.611  -8.610  1.00 78.80  ? 1281 GLY A O   1 
ATOM   9811  N  N   . GLY A 1 1282 ? -39.283  13.603  -8.922  1.00 77.78  ? 1282 GLY A N   1 
ATOM   9812  C  CA  . GLY A 1 1282 ? -39.320  14.686  -9.912  1.00 83.85  ? 1282 GLY A CA  1 
ATOM   9813  C  C   . GLY A 1 1282 ? -37.997  14.872  -10.643 1.00 97.62  ? 1282 GLY A C   1 
ATOM   9814  O  O   . GLY A 1 1282 ? -37.078  14.038  -10.512 1.00 98.21  ? 1282 GLY A O   1 
ATOM   9815  N  N   . GLY A 1 1283 ? -37.858  15.971  -11.382 1.00 109.38 ? 1283 GLY A N   1 
ATOM   9816  C  CA  . GLY A 1 1283 ? -36.765  16.114  -12.364 1.00 119.56 ? 1283 GLY A CA  1 
ATOM   9817  C  C   . GLY A 1 1283 ? -35.257  15.991  -12.107 1.00 121.72 ? 1283 GLY A C   1 
ATOM   9818  O  O   . GLY A 1 1283 ? -34.458  16.505  -12.882 1.00 118.66 ? 1283 GLY A O   1 
ATOM   9819  N  N   . PHE A 1 1284 ? -34.884  15.263  -11.063 1.00 131.89 ? 1284 PHE A N   1 
ATOM   9820  C  CA  . PHE A 1 1284 ? -33.538  15.296  -10.462 1.00 144.03 ? 1284 PHE A CA  1 
ATOM   9821  C  C   . PHE A 1 1284 ? -32.548  16.418  -10.789 1.00 135.32 ? 1284 PHE A C   1 
ATOM   9822  O  O   . PHE A 1 1284 ? -32.109  17.120  -9.877  1.00 138.78 ? 1284 PHE A O   1 
ATOM   9823  C  CB  . PHE A 1 1284 ? -32.801  13.974  -10.596 1.00 167.34 ? 1284 PHE A CB  1 
ATOM   9824  C  CG  . PHE A 1 1284 ? -31.703  13.768  -9.560  1.00 196.94 ? 1284 PHE A CG  1 
ATOM   9825  C  CD1 . PHE A 1 1284 ? -32.004  13.701  -8.200  1.00 211.62 ? 1284 PHE A CD1 1 
ATOM   9826  C  CD2 . PHE A 1 1284 ? -30.376  13.612  -9.952  1.00 212.06 ? 1284 PHE A CD2 1 
ATOM   9827  C  CE1 . PHE A 1 1284 ? -30.999  13.501  -7.256  1.00 226.87 ? 1284 PHE A CE1 1 
ATOM   9828  C  CE2 . PHE A 1 1284 ? -29.369  13.411  -9.010  1.00 225.52 ? 1284 PHE A CE2 1 
ATOM   9829  C  CZ  . PHE A 1 1284 ? -29.683  13.356  -7.664  1.00 235.43 ? 1284 PHE A CZ  1 
ATOM   9830  N  N   . TYR A 1 1285 ? -32.105  16.567  -12.028 1.00 122.04 ? 1285 TYR A N   1 
ATOM   9831  C  CA  . TYR A 1 1285 ? -31.000  17.495  -12.196 1.00 112.56 ? 1285 TYR A CA  1 
ATOM   9832  C  C   . TYR A 1 1285 ? -31.455  18.916  -11.916 1.00 107.61 ? 1285 TYR A C   1 
ATOM   9833  O  O   . TYR A 1 1285 ? -32.286  19.430  -12.650 1.00 110.32 ? 1285 TYR A O   1 
ATOM   9834  C  CB  . TYR A 1 1285 ? -30.363  17.353  -13.574 1.00 108.28 ? 1285 TYR A CB  1 
ATOM   9835  C  CG  . TYR A 1 1285 ? -29.956  15.927  -13.854 1.00 107.03 ? 1285 TYR A CG  1 
ATOM   9836  C  CD1 . TYR A 1 1285 ? -29.437  15.124  -12.850 1.00 107.48 ? 1285 TYR A CD1 1 
ATOM   9837  C  CD2 . TYR A 1 1285 ? -30.114  15.371  -15.111 1.00 105.22 ? 1285 TYR A CD2 1 
ATOM   9838  C  CE1 . TYR A 1 1285 ? -29.093  13.819  -13.089 1.00 107.07 ? 1285 TYR A CE1 1 
ATOM   9839  C  CE2 . TYR A 1 1285 ? -29.774  14.062  -15.360 1.00 103.99 ? 1285 TYR A CE2 1 
ATOM   9840  C  CZ  . TYR A 1 1285 ? -29.266  13.297  -14.345 1.00 105.46 ? 1285 TYR A CZ  1 
ATOM   9841  O  OH  . TYR A 1 1285 ? -28.917  12.004  -14.592 1.00 107.24 ? 1285 TYR A OH  1 
ATOM   9842  N  N   . SER A 1 1286 ? -30.956  19.539  -10.844 1.00 98.43  ? 1286 SER A N   1 
ATOM   9843  C  CA  . SER A 1 1286 ? -31.240  20.963  -10.602 1.00 91.77  ? 1286 SER A CA  1 
ATOM   9844  C  C   . SER A 1 1286 ? -32.686  21.434  -10.885 1.00 86.58  ? 1286 SER A C   1 
ATOM   9845  O  O   . SER A 1 1286 ? -33.647  20.675  -10.794 1.00 85.52  ? 1286 SER A O   1 
ATOM   9846  C  CB  . SER A 1 1286 ? -30.227  21.843  -11.345 1.00 91.38  ? 1286 SER A CB  1 
ATOM   9847  O  OG  . SER A 1 1286 ? -30.707  23.139  -11.626 1.00 89.13  ? 1286 SER A OG  1 
ATOM   9848  N  N   . THR A 1 1287 ? -32.838  22.707  -11.205 1.00 85.83  ? 1287 THR A N   1 
ATOM   9849  C  CA  . THR A 1 1287 ? -34.151  23.307  -11.278 1.00 88.92  ? 1287 THR A CA  1 
ATOM   9850  C  C   . THR A 1 1287 ? -34.573  23.529  -12.705 1.00 96.06  ? 1287 THR A C   1 
ATOM   9851  O  O   . THR A 1 1287 ? -35.569  22.965  -13.194 1.00 97.48  ? 1287 THR A O   1 
ATOM   9852  C  CB  . THR A 1 1287 ? -34.093  24.706  -10.706 1.00 85.94  ? 1287 THR A CB  1 
ATOM   9853  O  OG1 . THR A 1 1287 ? -32.825  25.281  -11.043 1.00 85.08  ? 1287 THR A OG1 1 
ATOM   9854  C  CG2 . THR A 1 1287 ? -34.248  24.665  -9.223  1.00 87.10  ? 1287 THR A CG2 1 
ATOM   9855  N  N   . GLN A 1 1288 ? -33.798  24.396  -13.350 1.00 99.18  ? 1288 GLN A N   1 
ATOM   9856  C  CA  . GLN A 1 1288 ? -34.155  24.981  -14.624 1.00 100.56 ? 1288 GLN A CA  1 
ATOM   9857  C  C   . GLN A 1 1288 ? -34.476  23.957  -15.688 1.00 103.01 ? 1288 GLN A C   1 
ATOM   9858  O  O   . GLN A 1 1288 ? -35.409  24.149  -16.455 1.00 105.77 ? 1288 GLN A O   1 
ATOM   9859  C  CB  . GLN A 1 1288 ? -33.053  25.907  -15.096 1.00 100.03 ? 1288 GLN A CB  1 
ATOM   9860  C  CG  . GLN A 1 1288 ? -33.093  27.213  -14.399 1.00 101.11 ? 1288 GLN A CG  1 
ATOM   9861  C  CD  . GLN A 1 1288 ? -34.214  28.077  -14.888 1.00 99.99  ? 1288 GLN A CD  1 
ATOM   9862  O  OE1 . GLN A 1 1288 ? -34.437  28.179  -16.099 1.00 101.44 ? 1288 GLN A OE1 1 
ATOM   9863  N  NE2 . GLN A 1 1288 ? -34.918  28.729  -13.959 1.00 97.69  ? 1288 GLN A NE2 1 
ATOM   9864  N  N   . ASP A 1 1289 ? -33.723  22.870  -15.759 1.00 102.54 ? 1289 ASP A N   1 
ATOM   9865  C  CA  . ASP A 1 1289 ? -34.138  21.819  -16.663 1.00 102.29 ? 1289 ASP A CA  1 
ATOM   9866  C  C   . ASP A 1 1289 ? -35.474  21.281  -16.149 1.00 100.94 ? 1289 ASP A C   1 
ATOM   9867  O  O   . ASP A 1 1289 ? -36.479  21.223  -16.880 1.00 103.50 ? 1289 ASP A O   1 
ATOM   9868  C  CB  . ASP A 1 1289 ? -33.142  20.694  -16.647 1.00 103.59 ? 1289 ASP A CB  1 
ATOM   9869  C  CG  . ASP A 1 1289 ? -32.884  20.233  -15.277 1.00 105.07 ? 1289 ASP A CG  1 
ATOM   9870  O  OD1 . ASP A 1 1289 ? -32.399  21.087  -14.510 1.00 104.84 ? 1289 ASP A OD1 1 
ATOM   9871  O  OD2 . ASP A 1 1289 ? -33.199  19.062  -14.965 1.00 106.90 ? 1289 ASP A OD2 1 
ATOM   9872  N  N   . THR A 1 1290 ? -35.496  20.900  -14.879 1.00 96.18  ? 1290 THR A N   1 
ATOM   9873  C  CA  . THR A 1 1290 ? -36.670  20.222  -14.359 1.00 88.81  ? 1290 THR A CA  1 
ATOM   9874  C  C   . THR A 1 1290 ? -38.007  20.914  -14.656 1.00 80.22  ? 1290 THR A C   1 
ATOM   9875  O  O   . THR A 1 1290 ? -39.032  20.251  -14.766 1.00 77.39  ? 1290 THR A O   1 
ATOM   9876  C  CB  . THR A 1 1290 ? -36.533  19.866  -12.864 1.00 89.19  ? 1290 THR A CB  1 
ATOM   9877  O  OG1 . THR A 1 1290 ? -35.406  18.984  -12.681 1.00 90.57  ? 1290 THR A OG1 1 
ATOM   9878  C  CG2 . THR A 1 1290 ? -37.823  19.155  -12.379 1.00 85.34  ? 1290 THR A CG2 1 
ATOM   9879  N  N   . ILE A 1 1291 ? -38.022  22.228  -14.806 1.00 76.26  ? 1291 ILE A N   1 
ATOM   9880  C  CA  . ILE A 1 1291 ? -39.300  22.839  -15.145 1.00 74.07  ? 1291 ILE A CA  1 
ATOM   9881  C  C   . ILE A 1 1291 ? -39.622  22.558  -16.592 1.00 72.21  ? 1291 ILE A C   1 
ATOM   9882  O  O   . ILE A 1 1291 ? -40.772  22.291  -16.928 1.00 73.78  ? 1291 ILE A O   1 
ATOM   9883  C  CB  . ILE A 1 1291 ? -39.361  24.376  -14.874 1.00 63.57  ? 1291 ILE A CB  1 
ATOM   9884  C  CG1 . ILE A 1 1291 ? -40.709  24.945  -15.318 1.00 58.42  ? 1291 ILE A CG1 1 
ATOM   9885  C  CG2 . ILE A 1 1291 ? -38.215  25.081  -15.550 1.00 63.97  ? 1291 ILE A CG2 1 
ATOM   9886  C  CD1 . ILE A 1 1291 ? -40.696  26.427  -15.422 1.00 55.57  ? 1291 ILE A CD1 1 
ATOM   9887  N  N   . ASN A 1 1292 ? -38.599  22.598  -17.437 1.00 67.76  ? 1292 ASN A N   1 
ATOM   9888  C  CA  . ASN A 1 1292 ? -38.794  22.422  -18.856 1.00 66.02  ? 1292 ASN A CA  1 
ATOM   9889  C  C   . ASN A 1 1292 ? -39.128  20.999  -19.153 1.00 67.39  ? 1292 ASN A C   1 
ATOM   9890  O  O   . ASN A 1 1292 ? -40.208  20.708  -19.660 1.00 70.03  ? 1292 ASN A O   1 
ATOM   9891  C  CB  . ASN A 1 1292 ? -37.569  22.892  -19.593 1.00 64.95  ? 1292 ASN A CB  1 
ATOM   9892  C  CG  . ASN A 1 1292 ? -37.423  24.382  -19.490 1.00 65.64  ? 1292 ASN A CG  1 
ATOM   9893  O  OD1 . ASN A 1 1292 ? -38.425  25.091  -19.534 1.00 65.39  ? 1292 ASN A OD1 1 
ATOM   9894  N  ND2 . ASN A 1 1292 ? -36.203  24.873  -19.320 1.00 65.51  ? 1292 ASN A ND2 1 
ATOM   9895  N  N   . ALA A 1 1293 ? -38.237  20.102  -18.772 1.00 66.61  ? 1293 ALA A N   1 
ATOM   9896  C  CA  . ALA A 1 1293 ? -38.526  18.680  -18.873 1.00 69.33  ? 1293 ALA A CA  1 
ATOM   9897  C  C   . ALA A 1 1293 ? -39.899  18.312  -18.308 1.00 71.34  ? 1293 ALA A C   1 
ATOM   9898  O  O   . ALA A 1 1293 ? -40.596  17.474  -18.857 1.00 71.28  ? 1293 ALA A O   1 
ATOM   9899  C  CB  . ALA A 1 1293 ? -37.450  17.869  -18.223 1.00 71.65  ? 1293 ALA A CB  1 
ATOM   9900  N  N   . ILE A 1 1294 ? -40.302  18.903  -17.194 1.00 75.02  ? 1294 ILE A N   1 
ATOM   9901  C  CA  . ILE A 1 1294 ? -41.649  18.595  -16.716 1.00 76.02  ? 1294 ILE A CA  1 
ATOM   9902  C  C   . ILE A 1 1294 ? -42.642  19.122  -17.735 1.00 76.97  ? 1294 ILE A C   1 
ATOM   9903  O  O   . ILE A 1 1294 ? -43.514  18.392  -18.173 1.00 78.84  ? 1294 ILE A O   1 
ATOM   9904  C  CB  . ILE A 1 1294 ? -41.994  19.198  -15.339 1.00 74.77  ? 1294 ILE A CB  1 
ATOM   9905  C  CG1 . ILE A 1 1294 ? -41.212  18.501  -14.231 1.00 73.32  ? 1294 ILE A CG1 1 
ATOM   9906  C  CG2 . ILE A 1 1294 ? -43.491  19.035  -15.078 1.00 73.86  ? 1294 ILE A CG2 1 
ATOM   9907  C  CD1 . ILE A 1 1294 ? -42.054  17.585  -13.417 1.00 71.62  ? 1294 ILE A CD1 1 
ATOM   9908  N  N   . GLU A 1 1295 ? -42.508  20.383  -18.124 1.00 76.13  ? 1295 GLU A N   1 
ATOM   9909  C  CA  . GLU A 1 1295 ? -43.468  20.938  -19.037 1.00 75.09  ? 1295 GLU A CA  1 
ATOM   9910  C  C   . GLU A 1 1295 ? -43.545  20.034  -20.230 1.00 69.62  ? 1295 GLU A C   1 
ATOM   9911  O  O   . GLU A 1 1295 ? -44.634  19.641  -20.642 1.00 68.87  ? 1295 GLU A O   1 
ATOM   9912  C  CB  . GLU A 1 1295 ? -43.078  22.315  -19.494 1.00 81.41  ? 1295 GLU A CB  1 
ATOM   9913  C  CG  . GLU A 1 1295 ? -44.205  22.908  -20.278 1.00 86.47  ? 1295 GLU A CG  1 
ATOM   9914  C  CD  . GLU A 1 1295 ? -43.936  24.315  -20.692 1.00 90.90  ? 1295 GLU A CD  1 
ATOM   9915  O  OE1 . GLU A 1 1295 ? -43.573  25.128  -19.806 1.00 89.71  ? 1295 GLU A OE1 1 
ATOM   9916  O  OE2 . GLU A 1 1295 ? -44.104  24.598  -21.908 1.00 94.17  ? 1295 GLU A OE2 1 
ATOM   9917  N  N   . GLY A 1 1296 ? -42.390  19.692  -20.779 1.00 65.45  ? 1296 GLY A N   1 
ATOM   9918  C  CA  . GLY A 1 1296 ? -42.346  18.729  -21.869 1.00 66.56  ? 1296 GLY A CA  1 
ATOM   9919  C  C   . GLY A 1 1296 ? -43.168  17.460  -21.620 1.00 65.61  ? 1296 GLY A C   1 
ATOM   9920  O  O   . GLY A 1 1296 ? -44.259  17.294  -22.139 1.00 65.47  ? 1296 GLY A O   1 
ATOM   9921  N  N   . LEU A 1 1297 ? -42.643  16.556  -20.815 1.00 64.77  ? 1297 LEU A N   1 
ATOM   9922  C  CA  . LEU A 1 1297 ? -43.429  15.454  -20.307 1.00 65.54  ? 1297 LEU A CA  1 
ATOM   9923  C  C   . LEU A 1 1297 ? -44.950  15.703  -20.146 1.00 69.95  ? 1297 LEU A C   1 
ATOM   9924  O  O   . LEU A 1 1297 ? -45.779  14.817  -20.418 1.00 69.50  ? 1297 LEU A O   1 
ATOM   9925  C  CB  . LEU A 1 1297 ? -42.836  15.007  -18.983 1.00 62.80  ? 1297 LEU A CB  1 
ATOM   9926  C  CG  . LEU A 1 1297 ? -41.978  13.837  -19.382 1.00 63.83  ? 1297 LEU A CG  1 
ATOM   9927  C  CD1 . LEU A 1 1297 ? -40.463  14.145  -19.432 1.00 63.02  ? 1297 LEU A CD1 1 
ATOM   9928  C  CD2 . LEU A 1 1297 ? -42.302  12.724  -18.434 1.00 65.74  ? 1297 LEU A CD2 1 
ATOM   9929  N  N   . THR A 1 1298 ? -45.350  16.880  -19.679 1.00 72.49  ? 1298 THR A N   1 
ATOM   9930  C  CA  . THR A 1 1298 ? -46.777  17.065  -19.463 1.00 73.34  ? 1298 THR A CA  1 
ATOM   9931  C  C   . THR A 1 1298 ? -47.360  17.263  -20.839 1.00 72.66  ? 1298 THR A C   1 
ATOM   9932  O  O   . THR A 1 1298 ? -48.161  16.444  -21.328 1.00 70.71  ? 1298 THR A O   1 
ATOM   9933  C  CB  . THR A 1 1298 ? -47.110  18.289  -18.588 1.00 70.74  ? 1298 THR A CB  1 
ATOM   9934  O  OG1 . THR A 1 1298 ? -46.094  18.482  -17.605 1.00 71.17  ? 1298 THR A OG1 1 
ATOM   9935  C  CG2 . THR A 1 1298 ? -48.443  18.089  -17.879 1.00 70.34  ? 1298 THR A CG2 1 
ATOM   9936  N  N   . GLU A 1 1299 ? -46.874  18.340  -21.457 1.00 75.45  ? 1299 GLU A N   1 
ATOM   9937  C  CA  . GLU A 1 1299 ? -47.405  18.906  -22.686 1.00 77.60  ? 1299 GLU A CA  1 
ATOM   9938  C  C   . GLU A 1 1299 ? -47.523  17.885  -23.827 1.00 77.47  ? 1299 GLU A C   1 
ATOM   9939  O  O   . GLU A 1 1299 ? -48.500  17.897  -24.598 1.00 80.89  ? 1299 GLU A O   1 
ATOM   9940  C  CB  . GLU A 1 1299 ? -46.560  20.110  -23.093 1.00 79.23  ? 1299 GLU A CB  1 
ATOM   9941  C  CG  . GLU A 1 1299 ? -47.343  21.146  -23.872 1.00 85.17  ? 1299 GLU A CG  1 
ATOM   9942  C  CD  . GLU A 1 1299 ? -48.240  22.029  -23.005 1.00 90.30  ? 1299 GLU A CD  1 
ATOM   9943  O  OE1 . GLU A 1 1299 ? -47.692  22.765  -22.157 1.00 93.02  ? 1299 GLU A OE1 1 
ATOM   9944  O  OE2 . GLU A 1 1299 ? -49.481  22.015  -23.201 1.00 91.02  ? 1299 GLU A OE2 1 
ATOM   9945  N  N   . TYR A 1 1300 ? -46.538  17.001  -23.917 1.00 72.47  ? 1300 TYR A N   1 
ATOM   9946  C  CA  . TYR A 1 1300 ? -46.614  15.830  -24.785 1.00 69.54  ? 1300 TYR A CA  1 
ATOM   9947  C  C   . TYR A 1 1300 ? -47.655  14.784  -24.388 1.00 66.08  ? 1300 TYR A C   1 
ATOM   9948  O  O   . TYR A 1 1300 ? -48.191  14.142  -25.251 1.00 61.06  ? 1300 TYR A O   1 
ATOM   9949  C  CB  . TYR A 1 1300 ? -45.237  15.161  -24.881 1.00 72.88  ? 1300 TYR A CB  1 
ATOM   9950  C  CG  . TYR A 1 1300 ? -45.240  13.740  -25.434 1.00 72.72  ? 1300 TYR A CG  1 
ATOM   9951  C  CD1 . TYR A 1 1300 ? -44.736  13.480  -26.695 1.00 74.06  ? 1300 TYR A CD1 1 
ATOM   9952  C  CD2 . TYR A 1 1300 ? -45.722  12.672  -24.691 1.00 70.86  ? 1300 TYR A CD2 1 
ATOM   9953  C  CE1 . TYR A 1 1300 ? -44.730  12.215  -27.209 1.00 74.68  ? 1300 TYR A CE1 1 
ATOM   9954  C  CE2 . TYR A 1 1300 ? -45.718  11.408  -25.189 1.00 71.93  ? 1300 TYR A CE2 1 
ATOM   9955  C  CZ  . TYR A 1 1300 ? -45.221  11.177  -26.452 1.00 75.37  ? 1300 TYR A CZ  1 
ATOM   9956  O  OH  . TYR A 1 1300 ? -45.220  9.896   -26.967 1.00 79.07  ? 1300 TYR A OH  1 
ATOM   9957  N  N   . SER A 1 1301 ? -47.907  14.563  -23.099 1.00 70.40  ? 1301 SER A N   1 
ATOM   9958  C  CA  . SER A 1 1301 ? -48.852  13.499  -22.716 1.00 73.98  ? 1301 SER A CA  1 
ATOM   9959  C  C   . SER A 1 1301 ? -50.227  14.043  -22.959 1.00 70.19  ? 1301 SER A C   1 
ATOM   9960  O  O   . SER A 1 1301 ? -51.219  13.318  -22.964 1.00 66.69  ? 1301 SER A O   1 
ATOM   9961  C  CB  . SER A 1 1301 ? -48.686  13.040  -21.260 1.00 79.63  ? 1301 SER A CB  1 
ATOM   9962  O  OG  . SER A 1 1301 ? -47.978  11.802  -21.188 1.00 82.70  ? 1301 SER A OG  1 
ATOM   9963  N  N   . LEU A 1 1302 ? -50.221  15.352  -23.164 1.00 70.67  ? 1302 LEU A N   1 
ATOM   9964  C  CA  . LEU A 1 1302 ? -51.352  16.134  -23.598 1.00 75.46  ? 1302 LEU A CA  1 
ATOM   9965  C  C   . LEU A 1 1302 ? -51.552  16.096  -25.096 1.00 78.17  ? 1302 LEU A C   1 
ATOM   9966  O  O   . LEU A 1 1302 ? -52.680  15.862  -25.555 1.00 84.55  ? 1302 LEU A O   1 
ATOM   9967  C  CB  . LEU A 1 1302 ? -51.104  17.575  -23.214 1.00 79.38  ? 1302 LEU A CB  1 
ATOM   9968  C  CG  . LEU A 1 1302 ? -51.522  17.785  -21.774 1.00 82.47  ? 1302 LEU A CG  1 
ATOM   9969  C  CD1 . LEU A 1 1302 ? -50.992  19.119  -21.258 1.00 82.09  ? 1302 LEU A CD1 1 
ATOM   9970  C  CD2 . LEU A 1 1302 ? -53.061  17.675  -21.743 1.00 84.20  ? 1302 LEU A CD2 1 
ATOM   9971  N  N   . LEU A 1 1303 ? -50.470  16.361  -25.845 1.00 72.14  ? 1303 LEU A N   1 
ATOM   9972  C  CA  . LEU A 1 1303 ? -50.443  16.288  -27.325 1.00 66.66  ? 1303 LEU A CA  1 
ATOM   9973  C  C   . LEU A 1 1303 ? -50.667  14.890  -27.936 1.00 61.56  ? 1303 LEU A C   1 
ATOM   9974  O  O   . LEU A 1 1303 ? -51.410  14.752  -28.877 1.00 61.15  ? 1303 LEU A O   1 
ATOM   9975  C  CB  . LEU A 1 1303 ? -49.159  16.946  -27.852 1.00 66.25  ? 1303 LEU A CB  1 
ATOM   9976  C  CG  . LEU A 1 1303 ? -48.479  16.808  -29.217 1.00 63.66  ? 1303 LEU A CG  1 
ATOM   9977  C  CD1 . LEU A 1 1303 ? -48.454  15.382  -29.645 1.00 60.79  ? 1303 LEU A CD1 1 
ATOM   9978  C  CD2 . LEU A 1 1303 ? -49.137  17.682  -30.263 1.00 65.87  ? 1303 LEU A CD2 1 
ATOM   9979  N  N   . VAL A 1 1304 ? -50.009  13.867  -27.413 1.00 60.59  ? 1304 VAL A N   1 
ATOM   9980  C  CA  . VAL A 1 1304 ? -50.269  12.468  -27.808 1.00 64.71  ? 1304 VAL A CA  1 
ATOM   9981  C  C   . VAL A 1 1304 ? -51.366  11.830  -26.941 1.00 65.20  ? 1304 VAL A C   1 
ATOM   9982  O  O   . VAL A 1 1304 ? -51.356  12.045  -25.735 1.00 69.28  ? 1304 VAL A O   1 
ATOM   9983  C  CB  . VAL A 1 1304 ? -49.020  11.594  -27.572 1.00 68.20  ? 1304 VAL A CB  1 
ATOM   9984  C  CG1 . VAL A 1 1304 ? -49.355  10.130  -27.757 1.00 71.83  ? 1304 VAL A CG1 1 
ATOM   9985  C  CG2 . VAL A 1 1304 ? -47.818  11.992  -28.447 1.00 66.48  ? 1304 VAL A CG2 1 
ATOM   9986  N  N   . LYS A 1 1305 ? -52.244  10.984  -27.475 1.00 93.56  ? 1305 LYS A N   1 
ATOM   9987  C  CA  . LYS A 1 1305 ? -53.254  10.406  -26.583 1.00 95.37  ? 1305 LYS A CA  1 
ATOM   9988  C  C   . LYS A 1 1305 ? -52.754  9.513   -25.434 1.00 98.23  ? 1305 LYS A C   1 
ATOM   9989  O  O   . LYS A 1 1305 ? -51.698  8.905   -25.543 1.00 99.09  ? 1305 LYS A O   1 
ATOM   9990  C  CB  . LYS A 1 1305 ? -54.295  9.660   -27.348 1.00 97.52  ? 1305 LYS A CB  1 
ATOM   9991  C  CG  . LYS A 1 1305 ? -55.604  9.727   -26.635 1.00 105.03 ? 1305 LYS A CG  1 
ATOM   9992  C  CD  . LYS A 1 1305 ? -56.784  10.009  -27.600 1.00 117.79 ? 1305 LYS A CD  1 
ATOM   9993  C  CE  . LYS A 1 1305 ? -56.958  11.494  -28.031 1.00 130.26 ? 1305 LYS A CE  1 
ATOM   9994  N  NZ  . LYS A 1 1305 ? -58.013  11.607  -29.093 1.00 130.72 ? 1305 LYS A NZ  1 
ATOM   9995  N  N   . GLN A 1 1306 ? -53.505  9.445   -24.323 1.00 100.95 ? 1306 GLN A N   1 
ATOM   9996  C  CA  . GLN A 1 1306 ? -53.118  8.584   -23.171 1.00 100.15 ? 1306 GLN A CA  1 
ATOM   9997  C  C   . GLN A 1 1306 ? -53.216  7.140   -23.621 1.00 101.46 ? 1306 GLN A C   1 
ATOM   9998  O  O   . GLN A 1 1306 ? -53.534  6.898   -24.783 1.00 103.90 ? 1306 GLN A O   1 
ATOM   9999  C  CB  . GLN A 1 1306 ? -53.969  8.838   -21.895 1.00 139.04 ? 1306 GLN A CB  1 
ATOM   10000 C  CG  . GLN A 1 1306 ? -53.176  9.532   -20.711 1.00 189.54 ? 1306 GLN A CG  1 
ATOM   10001 C  CD  . GLN A 1 1306 ? -53.893  9.530   -19.329 1.00 119.40 ? 1306 GLN A CD  1 
ATOM   10002 O  OE1 . GLN A 1 1306 ? -54.048  8.497   -18.674 1.00 118.72 ? 1306 GLN A OE1 1 
ATOM   10003 N  NE2 . GLN A 1 1306 ? -54.290  10.705  -18.886 1.00 120.58 ? 1306 GLN A NE2 1 
ATOM   10004 N  N   . LEU A 1 1307 ? -52.929  6.176   -22.753 1.00 97.70  ? 1307 LEU A N   1 
ATOM   10005 C  CA  . LEU A 1 1307 ? -53.204  4.787   -23.126 1.00 97.43  ? 1307 LEU A CA  1 
ATOM   10006 C  C   . LEU A 1 1307 ? -53.576  3.922   -21.940 1.00 96.06  ? 1307 LEU A C   1 
ATOM   10007 O  O   . LEU A 1 1307 ? -52.718  3.412   -21.205 1.00 95.46  ? 1307 LEU A O   1 
ATOM   10008 C  CB  . LEU A 1 1307 ? -52.042  4.112   -23.854 1.00 97.18  ? 1307 LEU A CB  1 
ATOM   10009 C  CG  . LEU A 1 1307 ? -51.115  4.738   -24.884 1.00 96.97  ? 1307 LEU A CG  1 
ATOM   10010 C  CD1 . LEU A 1 1307 ? -50.207  5.826   -24.254 1.00 100.09 ? 1307 LEU A CD1 1 
ATOM   10011 C  CD2 . LEU A 1 1307 ? -50.308  3.581   -25.471 1.00 96.40  ? 1307 LEU A CD2 1 
ATOM   10012 N  N   . ARG A 1 1308 ? -54.877  3.730   -21.806 1.00 95.29  ? 1308 ARG A N   1 
ATOM   10013 C  CA  . ARG A 1 1308 ? -55.470  2.878   -20.794 1.00 91.87  ? 1308 ARG A CA  1 
ATOM   10014 C  C   . ARG A 1 1308 ? -54.503  1.849   -20.241 1.00 86.61  ? 1308 ARG A C   1 
ATOM   10015 O  O   . ARG A 1 1308 ? -54.156  0.877   -20.913 1.00 83.32  ? 1308 ARG A O   1 
ATOM   10016 C  CB  . ARG A 1 1308 ? -56.708  2.212   -21.388 1.00 91.79  ? 1308 ARG A CB  1 
ATOM   10017 C  CG  . ARG A 1 1308 ? -57.061  0.889   -20.815 1.00 92.52  ? 1308 ARG A CG  1 
ATOM   10018 C  CD  . ARG A 1 1308 ? -58.555  0.660   -20.963 1.00 95.70  ? 1308 ARG A CD  1 
ATOM   10019 N  NE  . ARG A 1 1308 ? -59.028  -0.374  -20.061 1.00 98.32  ? 1308 ARG A NE  1 
ATOM   10020 C  CZ  . ARG A 1 1308 ? -58.503  -1.595  -20.018 1.00 100.72 ? 1308 ARG A CZ  1 
ATOM   10021 N  NH1 . ARG A 1 1308 ? -57.498  -1.941  -20.853 1.00 98.25  ? 1308 ARG A NH1 1 
ATOM   10022 N  NH2 . ARG A 1 1308 ? -58.976  -2.470  -19.135 1.00 103.67 ? 1308 ARG A NH2 1 
ATOM   10023 N  N   . LEU A 1 1309 ? -54.084  2.094   -18.999 1.00 86.73  ? 1309 LEU A N   1 
ATOM   10024 C  CA  . LEU A 1 1309 ? -53.168  1.218   -18.267 1.00 86.40  ? 1309 LEU A CA  1 
ATOM   10025 C  C   . LEU A 1 1309 ? -53.787  -0.108  -17.864 1.00 88.01  ? 1309 LEU A C   1 
ATOM   10026 O  O   . LEU A 1 1309 ? -54.905  -0.154  -17.316 1.00 87.45  ? 1309 LEU A O   1 
ATOM   10027 C  CB  . LEU A 1 1309 ? -52.681  1.904   -16.992 1.00 84.44  ? 1309 LEU A CB  1 
ATOM   10028 C  CG  . LEU A 1 1309 ? -51.594  2.957   -17.064 1.00 81.89  ? 1309 LEU A CG  1 
ATOM   10029 C  CD1 . LEU A 1 1309 ? -51.732  3.822   -15.881 1.00 82.85  ? 1309 LEU A CD1 1 
ATOM   10030 C  CD2 . LEU A 1 1309 ? -50.262  2.307   -17.040 1.00 78.10  ? 1309 LEU A CD2 1 
ATOM   10031 N  N   . SER A 1 1310 ? -53.043  -1.182  -18.097 1.00 81.48  ? 1310 SER A N   1 
ATOM   10032 C  CA  . SER A 1 1310 ? -53.480  -2.480  -17.617 1.00 83.77  ? 1310 SER A CA  1 
ATOM   10033 C  C   . SER A 1 1310 ? -52.399  -3.528  -17.706 1.00 87.28  ? 1310 SER A C   1 
ATOM   10034 O  O   . SER A 1 1310 ? -52.629  -4.634  -18.174 1.00 83.08  ? 1310 SER A O   1 
ATOM   10035 C  CB  . SER A 1 1310 ? -54.748  -2.955  -18.323 1.00 87.03  ? 1310 SER A CB  1 
ATOM   10036 O  OG  . SER A 1 1310 ? -54.876  -4.368  -18.243 1.00 88.97  ? 1310 SER A OG  1 
ATOM   10037 N  N   . MET A 1 1311 ? -51.215  -3.159  -17.245 1.00 89.14  ? 1311 MET A N   1 
ATOM   10038 C  CA  . MET A 1 1311 ? -50.211  -4.125  -16.847 1.00 91.59  ? 1311 MET A CA  1 
ATOM   10039 C  C   . MET A 1 1311 ? -50.569  -4.936  -15.610 1.00 96.45  ? 1311 MET A C   1 
ATOM   10040 O  O   . MET A 1 1311 ? -51.658  -4.815  -15.035 1.00 95.91  ? 1311 MET A O   1 
ATOM   10041 C  CB  . MET A 1 1311 ? -48.924  -3.417  -16.554 1.00 79.54  ? 1311 MET A CB  1 
ATOM   10042 C  CG  . MET A 1 1311 ? -48.159  -3.154  -17.769 1.00 78.29  ? 1311 MET A CG  1 
ATOM   10043 S  SD  . MET A 1 1311 ? -47.235  -1.650  -17.614 1.00 97.60  ? 1311 MET A SD  1 
ATOM   10044 C  CE  . MET A 1 1311 ? -48.432  -0.497  -18.257 1.00 101.13 ? 1311 MET A CE  1 
ATOM   10045 N  N   . ASP A 1 1312 ? -49.606  -5.752  -15.198 1.00 98.01  ? 1312 ASP A N   1 
ATOM   10046 C  CA  . ASP A 1 1312 ? -49.783  -6.739  -14.144 1.00 101.61 ? 1312 ASP A CA  1 
ATOM   10047 C  C   . ASP A 1 1312 ? -48.421  -6.956  -13.519 1.00 97.91  ? 1312 ASP A C   1 
ATOM   10048 O  O   . ASP A 1 1312 ? -47.861  -8.057  -13.527 1.00 97.46  ? 1312 ASP A O   1 
ATOM   10049 C  CB  . ASP A 1 1312 ? -50.280  -8.039  -14.736 1.00 107.18 ? 1312 ASP A CB  1 
ATOM   10050 C  CG  . ASP A 1 1312 ? -51.110  -8.813  -13.771 1.00 114.39 ? 1312 ASP A CG  1 
ATOM   10051 O  OD1 . ASP A 1 1312 ? -50.962  -8.583  -12.534 1.00 116.27 ? 1312 ASP A OD1 1 
ATOM   10052 O  OD2 . ASP A 1 1312 ? -51.911  -9.640  -14.268 1.00 117.67 ? 1312 ASP A OD2 1 
ATOM   10053 N  N   . ILE A 1 1313 ? -47.884  -5.863  -13.003 1.00 95.52  ? 1313 ILE A N   1 
ATOM   10054 C  CA  . ILE A 1 1313 ? -46.498  -5.797  -12.610 1.00 93.79  ? 1313 ILE A CA  1 
ATOM   10055 C  C   . ILE A 1 1313 ? -46.143  -6.782  -11.545 1.00 98.38  ? 1313 ILE A C   1 
ATOM   10056 O  O   . ILE A 1 1313 ? -46.989  -7.236  -10.779 1.00 105.35 ? 1313 ILE A O   1 
ATOM   10057 C  CB  . ILE A 1 1313 ? -46.190  -4.448  -12.089 1.00 89.04  ? 1313 ILE A CB  1 
ATOM   10058 C  CG1 . ILE A 1 1313 ? -47.031  -3.459  -12.864 1.00 89.15  ? 1313 ILE A CG1 1 
ATOM   10059 C  CG2 . ILE A 1 1313 ? -44.734  -4.168  -12.244 1.00 87.51  ? 1313 ILE A CG2 1 
ATOM   10060 C  CD1 . ILE A 1 1313 ? -46.215  -2.459  -13.573 1.00 89.75  ? 1313 ILE A CD1 1 
ATOM   10061 N  N   . ASP A 1 1314 ? -44.871  -7.114  -11.493 1.00 95.07  ? 1314 ASP A N   1 
ATOM   10062 C  CA  . ASP A 1 1314 ? -44.413  -8.005  -10.472 1.00 94.68  ? 1314 ASP A CA  1 
ATOM   10063 C  C   . ASP A 1 1314 ? -42.999  -7.680  -10.122 1.00 92.09  ? 1314 ASP A C   1 
ATOM   10064 O  O   . ASP A 1 1314 ? -42.088  -7.885  -10.921 1.00 91.92  ? 1314 ASP A O   1 
ATOM   10065 C  CB  . ASP A 1 1314 ? -44.469  -9.447  -10.916 1.00 96.32  ? 1314 ASP A CB  1 
ATOM   10066 C  CG  . ASP A 1 1314 ? -43.511  -10.312 -10.122 1.00 100.06 ? 1314 ASP A CG  1 
ATOM   10067 O  OD1 . ASP A 1 1314 ? -42.276  -10.277 -10.366 1.00 98.60  ? 1314 ASP A OD1 1 
ATOM   10068 O  OD2 . ASP A 1 1314 ? -43.994  -11.018 -9.219  1.00 104.99 ? 1314 ASP A OD2 1 
ATOM   10069 N  N   . VAL A 1 1315 ? -42.824  -7.177  -8.908  1.00 91.43  ? 1315 VAL A N   1 
ATOM   10070 C  CA  . VAL A 1 1315 ? -41.512  -6.862  -8.387  1.00 90.50  ? 1315 VAL A CA  1 
ATOM   10071 C  C   . VAL A 1 1315 ? -41.106  -8.083  -7.566  1.00 91.63  ? 1315 VAL A C   1 
ATOM   10072 O  O   . VAL A 1 1315 ? -41.949  -8.672  -6.902  1.00 93.83  ? 1315 VAL A O   1 
ATOM   10073 C  CB  . VAL A 1 1315 ? -41.561  -5.530  -7.634  1.00 90.41  ? 1315 VAL A CB  1 
ATOM   10074 C  CG1 . VAL A 1 1315 ? -42.637  -5.559  -6.565  1.00 82.74  ? 1315 VAL A CG1 1 
ATOM   10075 C  CG2 . VAL A 1 1315 ? -40.209  -5.160  -7.117  1.00 81.30  ? 1315 VAL A CG2 1 
ATOM   10076 N  N   . SER A 1 1316 ? -39.848  -8.509  -7.671  1.00 94.23  ? 1316 SER A N   1 
ATOM   10077 C  CA  . SER A 1 1316 ? -39.438  -9.812  -7.136  1.00 100.94 ? 1316 SER A CA  1 
ATOM   10078 C  C   . SER A 1 1316 ? -37.917  -9.985  -6.985  1.00 105.55 ? 1316 SER A C   1 
ATOM   10079 O  O   . SER A 1 1316 ? -37.147  -9.485  -7.801  1.00 105.86 ? 1316 SER A O   1 
ATOM   10080 C  CB  . SER A 1 1316 ? -39.992  -10.926 -8.022  1.00 101.68 ? 1316 SER A CB  1 
ATOM   10081 O  OG  . SER A 1 1316 ? -40.077  -12.126 -7.275  1.00 104.32 ? 1316 SER A OG  1 
ATOM   10082 N  N   . TYR A 1 1317 ? -37.478  -10.697 -5.952  1.00 109.39 ? 1317 TYR A N   1 
ATOM   10083 C  CA  . TYR A 1 1317 ? -36.048  -10.880 -5.747  1.00 113.60 ? 1317 TYR A CA  1 
ATOM   10084 C  C   . TYR A 1 1317 ? -35.549  -12.024 -6.589  1.00 114.94 ? 1317 TYR A C   1 
ATOM   10085 O  O   . TYR A 1 1317 ? -36.169  -13.083 -6.593  1.00 115.98 ? 1317 TYR A O   1 
ATOM   10086 C  CB  . TYR A 1 1317 ? -35.774  -11.192 -4.291  1.00 119.39 ? 1317 TYR A CB  1 
ATOM   10087 C  CG  . TYR A 1 1317 ? -36.084  -10.040 -3.402  1.00 124.19 ? 1317 TYR A CG  1 
ATOM   10088 C  CD1 . TYR A 1 1317 ? -37.316  -9.933  -2.781  1.00 127.55 ? 1317 TYR A CD1 1 
ATOM   10089 C  CD2 . TYR A 1 1317 ? -35.158  -9.031  -3.211  1.00 126.38 ? 1317 TYR A CD2 1 
ATOM   10090 C  CE1 . TYR A 1 1317 ? -37.611  -8.853  -1.971  1.00 130.31 ? 1317 TYR A CE1 1 
ATOM   10091 C  CE2 . TYR A 1 1317 ? -35.433  -7.948  -2.403  1.00 129.31 ? 1317 TYR A CE2 1 
ATOM   10092 C  CZ  . TYR A 1 1317 ? -36.661  -7.854  -1.779  1.00 131.71 ? 1317 TYR A CZ  1 
ATOM   10093 O  OH  . TYR A 1 1317 ? -36.921  -6.760  -0.956  1.00 133.35 ? 1317 TYR A OH  1 
ATOM   10094 N  N   . LYS A 1 1318 ? -34.427  -11.834 -7.280  1.00 114.68 ? 1318 LYS A N   1 
ATOM   10095 C  CA  . LYS A 1 1318 ? -33.871  -12.901 -8.110  1.00 116.82 ? 1318 LYS A CA  1 
ATOM   10096 C  C   . LYS A 1 1318 ? -33.757  -14.287 -7.449  1.00 122.80 ? 1318 LYS A C   1 
ATOM   10097 O  O   . LYS A 1 1318 ? -34.115  -15.282 -8.068  1.00 122.01 ? 1318 LYS A O   1 
ATOM   10098 C  CB  . LYS A 1 1318 ? -32.533  -12.498 -8.720  1.00 115.91 ? 1318 LYS A CB  1 
ATOM   10099 C  CG  . LYS A 1 1318 ? -31.700  -13.705 -9.140  1.00 119.15 ? 1318 LYS A CG  1 
ATOM   10100 C  CD  . LYS A 1 1318 ? -31.212  -13.627 -10.585 1.00 120.13 ? 1318 LYS A CD  1 
ATOM   10101 C  CE  . LYS A 1 1318 ? -30.099  -12.610 -10.755 1.00 120.80 ? 1318 LYS A CE  1 
ATOM   10102 N  NZ  . LYS A 1 1318 ? -29.609  -12.597 -12.163 1.00 120.99 ? 1318 LYS A NZ  1 
ATOM   10103 N  N   . HIS A 1 1319 ? -33.257  -14.362 -6.212  1.00 130.35 ? 1319 HIS A N   1 
ATOM   10104 C  CA  . HIS A 1 1319 ? -33.180  -15.646 -5.495  1.00 137.00 ? 1319 HIS A CA  1 
ATOM   10105 C  C   . HIS A 1 1319 ? -34.147  -15.789 -4.322  1.00 148.43 ? 1319 HIS A C   1 
ATOM   10106 O  O   . HIS A 1 1319 ? -34.706  -16.868 -4.107  1.00 149.57 ? 1319 HIS A O   1 
ATOM   10107 C  CB  . HIS A 1 1319 ? -31.763  -15.919 -5.031  1.00 132.66 ? 1319 HIS A CB  1 
ATOM   10108 C  CG  . HIS A 1 1319 ? -30.739  -15.591 -6.059  1.00 130.22 ? 1319 HIS A CG  1 
ATOM   10109 N  ND1 . HIS A 1 1319 ? -30.156  -14.348 -6.154  1.00 129.17 ? 1319 HIS A ND1 1 
ATOM   10110 C  CD2 . HIS A 1 1319 ? -30.210  -16.332 -7.058  1.00 131.23 ? 1319 HIS A CD2 1 
ATOM   10111 C  CE1 . HIS A 1 1319 ? -29.295  -14.339 -7.155  1.00 129.16 ? 1319 HIS A CE1 1 
ATOM   10112 N  NE2 . HIS A 1 1319 ? -29.311  -15.531 -7.723  1.00 130.66 ? 1319 HIS A NE2 1 
ATOM   10113 N  N   . LYS A 1 1320 ? -34.332  -14.712 -3.560  1.00 159.01 ? 1320 LYS A N   1 
ATOM   10114 C  CA  . LYS A 1 1320 ? -35.318  -14.705 -2.480  1.00 171.64 ? 1320 LYS A CA  1 
ATOM   10115 C  C   . LYS A 1 1320 ? -36.743  -14.830 -3.016  1.00 178.57 ? 1320 LYS A C   1 
ATOM   10116 O  O   . LYS A 1 1320 ? -37.038  -14.384 -4.127  1.00 179.44 ? 1320 LYS A O   1 
ATOM   10117 C  CB  . LYS A 1 1320 ? -35.213  -13.431 -1.645  1.00 175.44 ? 1320 LYS A CB  1 
ATOM   10118 C  CG  . LYS A 1 1320 ? -36.383  -13.242 -0.680  1.00 180.68 ? 1320 LYS A CG  1 
ATOM   10119 C  CD  . LYS A 1 1320 ? -36.450  -14.360 0.371   1.00 186.52 ? 1320 LYS A CD  1 
ATOM   10120 C  CE  . LYS A 1 1320 ? -37.631  -14.181 1.338   1.00 189.08 ? 1320 LYS A CE  1 
ATOM   10121 N  NZ  . LYS A 1 1320 ? -37.625  -15.169 2.469   1.00 191.45 ? 1320 LYS A NZ  1 
ATOM   10122 N  N   . GLY A 1 1321 ? -37.627  -15.424 -2.216  1.00 182.19 ? 1321 GLY A N   1 
ATOM   10123 C  CA  . GLY A 1 1321 ? -39.030  -15.533 -2.573  1.00 182.32 ? 1321 GLY A CA  1 
ATOM   10124 C  C   . GLY A 1 1321 ? -39.583  -14.250 -3.172  1.00 179.83 ? 1321 GLY A C   1 
ATOM   10125 O  O   . GLY A 1 1321 ? -38.996  -13.175 -3.039  1.00 181.83 ? 1321 GLY A O   1 
ATOM   10126 N  N   . ALA A 1 1322 ? -40.720  -14.362 -3.846  1.00 173.22 ? 1322 ALA A N   1 
ATOM   10127 C  CA  . ALA A 1 1322 ? -41.332  -13.209 -4.492  1.00 166.36 ? 1322 ALA A CA  1 
ATOM   10128 C  C   . ALA A 1 1322 ? -41.674  -12.121 -3.487  1.00 160.27 ? 1322 ALA A C   1 
ATOM   10129 O  O   . ALA A 1 1322 ? -42.244  -12.384 -2.431  1.00 157.52 ? 1322 ALA A O   1 
ATOM   10130 C  CB  . ALA A 1 1322 ? -42.586  -13.628 -5.263  1.00 163.60 ? 1322 ALA A CB  1 
ATOM   10131 N  N   . LEU A 1 1323 ? -41.312  -10.895 -3.814  1.00 160.02 ? 1323 LEU A N   1 
ATOM   10132 C  CA  . LEU A 1 1323 ? -41.880  -9.765  -3.125  1.00 154.63 ? 1323 LEU A CA  1 
ATOM   10133 C  C   . LEU A 1 1323 ? -43.163  -9.422  -3.886  1.00 158.86 ? 1323 LEU A C   1 
ATOM   10134 O  O   . LEU A 1 1323 ? -43.629  -10.220 -4.712  1.00 165.51 ? 1323 LEU A O   1 
ATOM   10135 C  CB  . LEU A 1 1323 ? -40.858  -8.642  -3.084  1.00 131.54 ? 1323 LEU A CB  1 
ATOM   10136 C  CG  . LEU A 1 1323 ? -41.209  -7.167  -2.996  1.00 113.54 ? 1323 LEU A CG  1 
ATOM   10137 C  CD1 . LEU A 1 1323 ? -42.257  -6.877  -1.952  1.00 104.61 ? 1323 LEU A CD1 1 
ATOM   10138 C  CD2 . LEU A 1 1323 ? -39.943  -6.390  -2.727  1.00 101.38 ? 1323 LEU A CD2 1 
ATOM   10139 N  N   . HIS A 1 1324 ? -43.746  -8.264  -3.604  1.00 155.04 ? 1324 HIS A N   1 
ATOM   10140 C  CA  . HIS A 1 1324 ? -45.071  -7.916  -4.121  1.00 153.58 ? 1324 HIS A CA  1 
ATOM   10141 C  C   . HIS A 1 1324 ? -45.214  -7.842  -5.657  1.00 150.25 ? 1324 HIS A C   1 
ATOM   10142 O  O   . HIS A 1 1324 ? -44.235  -7.738  -6.388  1.00 147.80 ? 1324 HIS A O   1 
ATOM   10143 C  CB  . HIS A 1 1324 ? -45.576  -6.627  -3.454  1.00 155.07 ? 1324 HIS A CB  1 
ATOM   10144 C  CG  . HIS A 1 1324 ? -45.019  -5.369  -4.049  1.00 160.31 ? 1324 HIS A CG  1 
ATOM   10145 N  ND1 . HIS A 1 1324 ? -45.611  -4.724  -5.116  1.00 162.22 ? 1324 HIS A ND1 1 
ATOM   10146 C  CD2 . HIS A 1 1324 ? -43.940  -4.623  -3.713  1.00 162.57 ? 1324 HIS A CD2 1 
ATOM   10147 C  CE1 . HIS A 1 1324 ? -44.917  -3.642  -5.417  1.00 163.08 ? 1324 HIS A CE1 1 
ATOM   10148 N  NE2 . HIS A 1 1324 ? -43.896  -3.558  -4.582  1.00 163.72 ? 1324 HIS A NE2 1 
ATOM   10149 N  N   . ASN A 1 1325 ? -46.460  -7.887  -6.121  1.00 152.98 ? 1325 ASN A N   1 
ATOM   10150 C  CA  . ASN A 1 1325 ? -46.783  -7.900  -7.542  1.00 154.73 ? 1325 ASN A CA  1 
ATOM   10151 C  C   . ASN A 1 1325 ? -48.242  -7.574  -7.755  1.00 149.88 ? 1325 ASN A C   1 
ATOM   10152 O  O   . ASN A 1 1325 ? -49.118  -8.318  -7.323  1.00 149.55 ? 1325 ASN A O   1 
ATOM   10153 C  CB  . ASN A 1 1325 ? -46.476  -9.270  -8.161  1.00 162.35 ? 1325 ASN A CB  1 
ATOM   10154 C  CG  . ASN A 1 1325 ? -47.092  -10.429 -7.385  1.00 167.84 ? 1325 ASN A CG  1 
ATOM   10155 O  OD1 . ASN A 1 1325 ? -46.483  -10.967 -6.449  1.00 168.95 ? 1325 ASN A OD1 1 
ATOM   10156 N  ND2 . ASN A 1 1325 ? -48.294  -10.840 -7.794  1.00 169.50 ? 1325 ASN A ND2 1 
ATOM   10157 N  N   . TYR A 1 1326 ? -48.510  -6.486  -8.457  1.00 146.67 ? 1326 TYR A N   1 
ATOM   10158 C  CA  . TYR A 1 1326 ? -49.866  -5.964  -8.466  1.00 147.75 ? 1326 TYR A CA  1 
ATOM   10159 C  C   . TYR A 1 1326 ? -50.439  -5.553  -9.805  1.00 137.56 ? 1326 TYR A C   1 
ATOM   10160 O  O   . TYR A 1 1326 ? -49.787  -4.888  -10.596 1.00 135.57 ? 1326 TYR A O   1 
ATOM   10161 C  CB  . TYR A 1 1326 ? -49.931  -4.748  -7.570  1.00 156.30 ? 1326 TYR A CB  1 
ATOM   10162 C  CG  . TYR A 1 1326 ? -48.916  -3.720  -7.947  1.00 162.90 ? 1326 TYR A CG  1 
ATOM   10163 C  CD1 . TYR A 1 1326 ? -49.298  -2.497  -8.486  1.00 165.78 ? 1326 TYR A CD1 1 
ATOM   10164 C  CD2 . TYR A 1 1326 ? -47.566  -3.977  -7.768  1.00 166.43 ? 1326 TYR A CD2 1 
ATOM   10165 C  CE1 . TYR A 1 1326 ? -48.355  -1.551  -8.823  1.00 167.43 ? 1326 TYR A CE1 1 
ATOM   10166 C  CE2 . TYR A 1 1326 ? -46.620  -3.048  -8.096  1.00 168.17 ? 1326 TYR A CE2 1 
ATOM   10167 C  CZ  . TYR A 1 1326 ? -47.012  -1.835  -8.624  1.00 168.78 ? 1326 TYR A CZ  1 
ATOM   10168 O  OH  . TYR A 1 1326 ? -46.045  -0.910  -8.945  1.00 168.71 ? 1326 TYR A OH  1 
ATOM   10169 N  N   . LYS A 1 1327 ? -51.699  -5.911  -10.010 1.00 131.53 ? 1327 LYS A N   1 
ATOM   10170 C  CA  . LYS A 1 1327 ? -52.453  -5.457  -11.156 1.00 124.02 ? 1327 LYS A CA  1 
ATOM   10171 C  C   . LYS A 1 1327 ? -52.581  -3.919  -11.180 1.00 114.28 ? 1327 LYS A C   1 
ATOM   10172 O  O   . LYS A 1 1327 ? -53.285  -3.329  -10.363 1.00 113.54 ? 1327 LYS A O   1 
ATOM   10173 C  CB  . LYS A 1 1327 ? -53.827  -6.149  -11.191 1.00 128.35 ? 1327 LYS A CB  1 
ATOM   10174 C  CG  . LYS A 1 1327 ? -54.558  -5.948  -12.516 1.00 132.38 ? 1327 LYS A CG  1 
ATOM   10175 C  CD  . LYS A 1 1327 ? -55.336  -7.181  -13.017 1.00 136.33 ? 1327 LYS A CD  1 
ATOM   10176 C  CE  . LYS A 1 1327 ? -55.644  -7.093  -14.552 1.00 134.06 ? 1327 LYS A CE  1 
ATOM   10177 N  NZ  . LYS A 1 1327 ? -54.441  -7.226  -15.470 1.00 130.54 ? 1327 LYS A NZ  1 
ATOM   10178 N  N   . MET A 1 1328 ? -51.880  -3.290  -12.129 1.00 106.24 ? 1328 MET A N   1 
ATOM   10179 C  CA  . MET A 1 1328 ? -51.963  -1.849  -12.411 1.00 96.35  ? 1328 MET A CA  1 
ATOM   10180 C  C   . MET A 1 1328 ? -53.109  -1.539  -13.354 1.00 97.36  ? 1328 MET A C   1 
ATOM   10181 O  O   . MET A 1 1328 ? -53.407  -2.331  -14.242 1.00 96.99  ? 1328 MET A O   1 
ATOM   10182 C  CB  . MET A 1 1328 ? -50.674  -1.377  -13.050 1.00 87.09  ? 1328 MET A CB  1 
ATOM   10183 C  CG  . MET A 1 1328 ? -50.713  0.019   -13.570 1.00 82.51  ? 1328 MET A CG  1 
ATOM   10184 S  SD  . MET A 1 1328 ? -49.016  0.635   -13.586 1.00 79.26  ? 1328 MET A SD  1 
ATOM   10185 C  CE  . MET A 1 1328 ? -49.019  1.510   -12.019 1.00 129.77 ? 1328 MET A CE  1 
ATOM   10186 N  N   . THR A 1 1329 ? -53.740  -0.382  -13.171 1.00 99.16  ? 1329 THR A N   1 
ATOM   10187 C  CA  . THR A 1 1329 ? -54.976  -0.025  -13.886 1.00 99.53  ? 1329 THR A CA  1 
ATOM   10188 C  C   . THR A 1 1329 ? -55.223  1.468   -13.801 1.00 98.21  ? 1329 THR A C   1 
ATOM   10189 O  O   . THR A 1 1329 ? -54.538  2.161   -13.079 1.00 98.24  ? 1329 THR A O   1 
ATOM   10190 C  CB  . THR A 1 1329 ? -56.193  -0.719  -13.280 1.00 102.05 ? 1329 THR A CB  1 
ATOM   10191 O  OG1 . THR A 1 1329 ? -56.163  -0.607  -11.841 1.00 102.29 ? 1329 THR A OG1 1 
ATOM   10192 C  CG2 . THR A 1 1329 ? -56.189  -2.181  -13.686 1.00 103.68 ? 1329 THR A CG2 1 
ATOM   10193 N  N   . ASP A 1 1330 ? -56.178  2.011   -14.523 1.00 98.27  ? 1330 ASP A N   1 
ATOM   10194 C  CA  . ASP A 1 1330 ? -56.325  3.444   -14.347 1.00 100.97 ? 1330 ASP A CA  1 
ATOM   10195 C  C   . ASP A 1 1330 ? -56.922  3.757   -12.964 1.00 104.14 ? 1330 ASP A C   1 
ATOM   10196 O  O   . ASP A 1 1330 ? -57.062  4.914   -12.583 1.00 106.49 ? 1330 ASP A O   1 
ATOM   10197 C  CB  . ASP A 1 1330 ? -57.126  4.099   -15.482 1.00 102.99 ? 1330 ASP A CB  1 
ATOM   10198 C  CG  . ASP A 1 1330 ? -56.734  3.588   -16.851 1.00 102.60 ? 1330 ASP A CG  1 
ATOM   10199 O  OD1 . ASP A 1 1330 ? -55.573  3.792   -17.306 1.00 98.06  ? 1330 ASP A OD1 1 
ATOM   10200 O  OD2 . ASP A 1 1330 ? -57.642  2.996   -17.468 1.00 105.86 ? 1330 ASP A OD2 1 
ATOM   10201 N  N   . LYS A 1 1331 ? -57.276  2.728   -12.210 1.00 104.98 ? 1331 LYS A N   1 
ATOM   10202 C  CA  . LYS A 1 1331 ? -57.829  2.945   -10.884 1.00 106.80 ? 1331 LYS A CA  1 
ATOM   10203 C  C   . LYS A 1 1331 ? -56.744  3.464   -9.944  1.00 106.19 ? 1331 LYS A C   1 
ATOM   10204 O  O   . LYS A 1 1331 ? -56.744  4.637   -9.557  1.00 106.24 ? 1331 LYS A O   1 
ATOM   10205 C  CB  . LYS A 1 1331 ? -58.429  1.642   -10.385 1.00 107.96 ? 1331 LYS A CB  1 
ATOM   10206 C  CG  . LYS A 1 1331 ? -59.444  1.108   -11.365 1.00 106.82 ? 1331 LYS A CG  1 
ATOM   10207 C  CD  . LYS A 1 1331 ? -60.406  2.220   -11.708 1.00 107.04 ? 1331 LYS A CD  1 
ATOM   10208 C  CE  . LYS A 1 1331 ? -61.650  1.681   -12.374 1.00 109.76 ? 1331 LYS A CE  1 
ATOM   10209 N  NZ  . LYS A 1 1331 ? -62.882  2.274   -11.800 1.00 111.72 ? 1331 LYS A NZ  1 
ATOM   10210 N  N   . ASN A 1 1332 ? -55.821  2.574   -9.593  1.00 106.23 ? 1332 ASN A N   1 
ATOM   10211 C  CA  . ASN A 1 1332 ? -54.550  2.949   -8.989  1.00 108.17 ? 1332 ASN A CA  1 
ATOM   10212 C  C   . ASN A 1 1332 ? -53.428  2.874   -10.003 1.00 109.47 ? 1332 ASN A C   1 
ATOM   10213 O  O   . ASN A 1 1332 ? -53.226  1.829   -10.618 1.00 110.44 ? 1332 ASN A O   1 
ATOM   10214 C  CB  . ASN A 1 1332 ? -54.170  1.925   -7.936  1.00 111.04 ? 1332 ASN A CB  1 
ATOM   10215 C  CG  . ASN A 1 1332 ? -53.441  0.712   -8.543  1.00 111.46 ? 1332 ASN A CG  1 
ATOM   10216 O  OD1 . ASN A 1 1332 ? -54.023  -0.027  -9.355  1.00 109.84 ? 1332 ASN A OD1 1 
ATOM   10217 N  ND2 . ASN A 1 1332 ? -52.162  0.520   -8.168  1.00 110.50 ? 1332 ASN A ND2 1 
ATOM   10218 N  N   . PHE A 1 1333 ? -52.652  3.930   -10.175 1.00 109.09 ? 1333 PHE A N   1 
ATOM   10219 C  CA  . PHE A 1 1333 ? -51.380  3.723   -10.864 1.00 105.27 ? 1333 PHE A CA  1 
ATOM   10220 C  C   . PHE A 1 1333 ? -50.310  4.356   -10.028 1.00 110.34 ? 1333 PHE A C   1 
ATOM   10221 O  O   . PHE A 1 1333 ? -49.166  3.910   -10.048 1.00 111.74 ? 1333 PHE A O   1 
ATOM   10222 C  CB  . PHE A 1 1333 ? -51.342  4.199   -12.332 1.00 96.09  ? 1333 PHE A CB  1 
ATOM   10223 C  CG  . PHE A 1 1333 ? -52.038  5.520   -12.597 1.00 89.25  ? 1333 PHE A CG  1 
ATOM   10224 C  CD1 . PHE A 1 1333 ? -51.313  6.664   -12.825 1.00 85.22  ? 1333 PHE A CD1 1 
ATOM   10225 C  CD2 . PHE A 1 1333 ? -53.418  5.610   -12.671 1.00 89.82  ? 1333 PHE A CD2 1 
ATOM   10226 C  CE1 . PHE A 1 1333 ? -51.961  7.875   -13.087 1.00 86.16  ? 1333 PHE A CE1 1 
ATOM   10227 C  CE2 . PHE A 1 1333 ? -54.046  6.822   -12.929 1.00 83.66  ? 1333 PHE A CE2 1 
ATOM   10228 C  CZ  . PHE A 1 1333 ? -53.322  7.942   -13.134 1.00 82.93  ? 1333 PHE A CZ  1 
ATOM   10229 N  N   . LEU A 1 1334 ? -50.704  5.366   -9.252  1.00 109.09 ? 1334 LEU A N   1 
ATOM   10230 C  CA  . LEU A 1 1334 ? -49.754  6.072   -8.412  1.00 103.99 ? 1334 LEU A CA  1 
ATOM   10231 C  C   . LEU A 1 1334 ? -49.668  5.386   -7.066  1.00 110.77 ? 1334 LEU A C   1 
ATOM   10232 O  O   . LEU A 1 1334 ? -49.701  6.028   -6.021  1.00 112.61 ? 1334 LEU A O   1 
ATOM   10233 C  CB  . LEU A 1 1334 ? -50.085  7.553   -8.231  1.00 94.68  ? 1334 LEU A CB  1 
ATOM   10234 C  CG  . LEU A 1 1334 ? -51.098  8.327   -9.070  1.00 88.54  ? 1334 LEU A CG  1 
ATOM   10235 C  CD1 . LEU A 1 1334 ? -50.471  8.987   -10.264 1.00 84.36  ? 1334 LEU A CD1 1 
ATOM   10236 C  CD2 . LEU A 1 1334 ? -52.313  7.465   -9.437  1.00 87.51  ? 1334 LEU A CD2 1 
ATOM   10237 N  N   . GLY A 1 1335 ? -49.551  4.067   -7.117  1.00 115.06 ? 1335 GLY A N   1 
ATOM   10238 C  CA  . GLY A 1 1335 ? -49.236  3.262   -5.948  1.00 122.09 ? 1335 GLY A CA  1 
ATOM   10239 C  C   . GLY A 1 1335 ? -48.100  3.678   -5.010  1.00 126.60 ? 1335 GLY A C   1 
ATOM   10240 O  O   . GLY A 1 1335 ? -47.409  4.685   -5.189  1.00 126.90 ? 1335 GLY A O   1 
ATOM   10241 N  N   . ARG A 1 1336 ? -47.940  2.868   -3.976  1.00 132.70 ? 1336 ARG A N   1 
ATOM   10242 C  CA  . ARG A 1 1336 ? -46.974  3.089   -2.924  1.00 139.57 ? 1336 ARG A CA  1 
ATOM   10243 C  C   . ARG A 1 1336 ? -45.584  2.918   -3.507  1.00 131.11 ? 1336 ARG A C   1 
ATOM   10244 O  O   . ARG A 1 1336 ? -45.440  2.206   -4.514  1.00 130.48 ? 1336 ARG A O   1 
ATOM   10245 C  CB  . ARG A 1 1336 ? -47.197  1.980   -1.916  1.00 154.21 ? 1336 ARG A CB  1 
ATOM   10246 C  CG  . ARG A 1 1336 ? -47.579  0.680   -2.631  1.00 165.73 ? 1336 ARG A CG  1 
ATOM   10247 C  CD  . ARG A 1 1336 ? -47.193  -0.555  -1.843  1.00 176.54 ? 1336 ARG A CD  1 
ATOM   10248 N  NE  . ARG A 1 1336 ? -47.357  -1.769  -2.639  1.00 184.72 ? 1336 ARG A NE  1 
ATOM   10249 C  CZ  . ARG A 1 1336 ? -47.479  -2.984  -2.113  1.00 191.66 ? 1336 ARG A CZ  1 
ATOM   10250 N  NH1 . ARG A 1 1336 ? -47.461  -3.135  -0.791  1.00 194.86 ? 1336 ARG A NH1 1 
ATOM   10251 N  NH2 . ARG A 1 1336 ? -47.629  -4.043  -2.901  1.00 193.23 ? 1336 ARG A NH2 1 
ATOM   10252 N  N   . PRO A 1 1337 ? -44.566  3.591   -2.921  1.00 123.34 ? 1337 PRO A N   1 
ATOM   10253 C  CA  . PRO A 1 1337 ? -43.188  3.152   -3.183  1.00 115.12 ? 1337 PRO A CA  1 
ATOM   10254 C  C   . PRO A 1 1337 ? -42.936  1.923   -2.373  1.00 111.82 ? 1337 PRO A C   1 
ATOM   10255 O  O   . PRO A 1 1337 ? -43.880  1.435   -1.763  1.00 110.50 ? 1337 PRO A O   1 
ATOM   10256 C  CB  . PRO A 1 1337 ? -42.332  4.312   -2.697  1.00 116.37 ? 1337 PRO A CB  1 
ATOM   10257 C  CG  . PRO A 1 1337 ? -43.234  5.488   -2.810  1.00 119.98 ? 1337 PRO A CG  1 
ATOM   10258 C  CD  . PRO A 1 1337 ? -44.607  4.974   -2.425  1.00 122.44 ? 1337 PRO A CD  1 
ATOM   10259 N  N   . VAL A 1 1338 ? -41.712  1.417   -2.385  1.00 111.52 ? 1338 VAL A N   1 
ATOM   10260 C  CA  . VAL A 1 1338 ? -41.389  0.157   -1.703  1.00 116.73 ? 1338 VAL A CA  1 
ATOM   10261 C  C   . VAL A 1 1338 ? -39.891  0.085   -1.487  1.00 122.85 ? 1338 VAL A C   1 
ATOM   10262 O  O   . VAL A 1 1338 ? -39.127  0.139   -2.454  1.00 123.97 ? 1338 VAL A O   1 
ATOM   10263 C  CB  . VAL A 1 1338 ? -41.857  -1.103  -2.508  1.00 156.64 ? 1338 VAL A CB  1 
ATOM   10264 C  CG1 . VAL A 1 1338 ? -40.789  -2.199  -2.537  1.00 156.01 ? 1338 VAL A CG1 1 
ATOM   10265 C  CG2 . VAL A 1 1338 ? -43.157  -1.654  -1.946  1.00 157.98 ? 1338 VAL A CG2 1 
ATOM   10266 N  N   . GLU A 1 1339 ? -39.460  -0.017  -0.232  1.00 126.73 ? 1339 GLU A N   1 
ATOM   10267 C  CA  . GLU A 1 1339 ? -38.034  -0.126  0.027   1.00 131.39 ? 1339 GLU A CA  1 
ATOM   10268 C  C   . GLU A 1 1339 ? -37.654  -1.559  -0.121  1.00 130.21 ? 1339 GLU A C   1 
ATOM   10269 O  O   . GLU A 1 1339 ? -38.246  -2.437  0.498   1.00 129.13 ? 1339 GLU A O   1 
ATOM   10270 C  CB  . GLU A 1 1339 ? -37.662  0.397   1.402   1.00 138.60 ? 1339 GLU A CB  1 
ATOM   10271 C  CG  . GLU A 1 1339 ? -37.256  1.856   1.352   1.00 144.23 ? 1339 GLU A CG  1 
ATOM   10272 C  CD  . GLU A 1 1339 ? -37.284  2.519   2.708   1.00 149.99 ? 1339 GLU A CD  1 
ATOM   10273 O  OE1 . GLU A 1 1339 ? -36.472  2.097   3.572   1.00 152.24 ? 1339 GLU A OE1 1 
ATOM   10274 O  OE2 . GLU A 1 1339 ? -38.110  3.458   2.893   1.00 151.19 ? 1339 GLU A OE2 1 
ATOM   10275 N  N   . VAL A 1 1340 ? -36.693  -1.797  -0.993  1.00 132.05 ? 1340 VAL A N   1 
ATOM   10276 C  CA  . VAL A 1 1340 ? -36.323  -3.149  -1.307  1.00 134.84 ? 1340 VAL A CA  1 
ATOM   10277 C  C   . VAL A 1 1340 ? -35.394  -3.541  -0.210  1.00 137.64 ? 1340 VAL A C   1 
ATOM   10278 O  O   . VAL A 1 1340 ? -34.308  -2.976  -0.095  1.00 140.09 ? 1340 VAL A O   1 
ATOM   10279 C  CB  . VAL A 1 1340 ? -35.596  -3.232  -2.646  1.00 135.92 ? 1340 VAL A CB  1 
ATOM   10280 C  CG1 . VAL A 1 1340 ? -34.897  -4.571  -2.774  1.00 137.35 ? 1340 VAL A CG1 1 
ATOM   10281 C  CG2 . VAL A 1 1340 ? -36.575  -3.026  -3.791  1.00 134.93 ? 1340 VAL A CG2 1 
ATOM   10282 N  N   . LEU A 1 1341 ? -35.823  -4.478  0.627   1.00 138.48 ? 1341 LEU A N   1 
ATOM   10283 C  CA  . LEU A 1 1341 ? -35.034  -4.793  1.809   1.00 140.69 ? 1341 LEU A CA  1 
ATOM   10284 C  C   . LEU A 1 1341 ? -33.889  -5.733  1.454   1.00 145.19 ? 1341 LEU A C   1 
ATOM   10285 O  O   . LEU A 1 1341 ? -32.702  -5.401  1.589   1.00 145.11 ? 1341 LEU A O   1 
ATOM   10286 C  CB  . LEU A 1 1341 ? -35.898  -5.399  2.940   1.00 140.57 ? 1341 LEU A CB  1 
ATOM   10287 C  CG  . LEU A 1 1341 ? -36.449  -4.608  4.158   1.00 159.27 ? 1341 LEU A CG  1 
ATOM   10288 C  CD1 . LEU A 1 1341 ? -35.483  -3.525  4.685   1.00 158.69 ? 1341 LEU A CD1 1 
ATOM   10289 C  CD2 . LEU A 1 1341 ? -37.864  -4.030  3.922   1.00 158.50 ? 1341 LEU A CD2 1 
ATOM   10290 N  N   . LEU A 1 1342 ? -34.250  -6.905  0.970   1.00 146.73 ? 1342 LEU A N   1 
ATOM   10291 C  CA  . LEU A 1 1342 ? -33.317  -8.004  1.019   1.00 147.93 ? 1342 LEU A CA  1 
ATOM   10292 C  C   . LEU A 1 1342 ? -32.074  -7.798  0.152   1.00 146.19 ? 1342 LEU A C   1 
ATOM   10293 O  O   . LEU A 1 1342 ? -32.011  -6.902  -0.692  1.00 143.97 ? 1342 LEU A O   1 
ATOM   10294 C  CB  . LEU A 1 1342 ? -34.056  -9.319  0.766   1.00 146.66 ? 1342 LEU A CB  1 
ATOM   10295 C  CG  . LEU A 1 1342 ? -35.509  -9.208  1.283   1.00 143.15 ? 1342 LEU A CG  1 
ATOM   10296 C  CD1 . LEU A 1 1342 ? -36.319  -10.484 1.097   1.00 143.04 ? 1342 LEU A CD1 1 
ATOM   10297 C  CD2 . LEU A 1 1342 ? -35.592  -8.758  2.739   1.00 143.28 ? 1342 LEU A CD2 1 
ATOM   10298 N  N   . ASN A 1 1343 ? -31.062  -8.605  0.436   1.00 149.63 ? 1343 ASN A N   1 
ATOM   10299 C  CA  . ASN A 1 1343 ? -29.793  -8.572  -0.283  1.00 154.25 ? 1343 ASN A CA  1 
ATOM   10300 C  C   . ASN A 1 1343 ? -29.809  -9.514  -1.494  1.00 153.15 ? 1343 ASN A C   1 
ATOM   10301 O  O   . ASN A 1 1343 ? -29.275  -10.627 -1.447  1.00 153.29 ? 1343 ASN A O   1 
ATOM   10302 C  CB  . ASN A 1 1343 ? -28.621  -8.912  0.659   1.00 162.73 ? 1343 ASN A CB  1 
ATOM   10303 C  CG  . ASN A 1 1343 ? -28.306  -7.776  1.657   1.00 171.53 ? 1343 ASN A CG  1 
ATOM   10304 O  OD1 . ASN A 1 1343 ? -27.145  -7.392  1.834   1.00 174.94 ? 1343 ASN A OD1 1 
ATOM   10305 N  ND2 . ASN A 1 1343 ? -29.346  -7.222  2.287   1.00 173.99 ? 1343 ASN A ND2 1 
ATOM   10306 N  N   . ASP A 1 1344 ? -30.420  -9.052  -2.582  1.00 151.83 ? 1344 ASP A N   1 
ATOM   10307 C  CA  . ASP A 1 1344 ? -30.642  -9.881  -3.764  1.00 147.86 ? 1344 ASP A CA  1 
ATOM   10308 C  C   . ASP A 1 1344 ? -30.813  -8.967  -4.970  1.00 146.06 ? 1344 ASP A C   1 
ATOM   10309 O  O   . ASP A 1 1344 ? -31.102  -7.784  -4.831  1.00 146.95 ? 1344 ASP A O   1 
ATOM   10310 C  CB  . ASP A 1 1344 ? -31.906  -10.726 -3.577  1.00 142.71 ? 1344 ASP A CB  1 
ATOM   10311 C  CG  . ASP A 1 1344 ? -31.812  -12.076 -4.245  1.00 135.82 ? 1344 ASP A CG  1 
ATOM   10312 O  OD1 . ASP A 1 1344 ? -30.939  -12.242 -5.116  1.00 133.91 ? 1344 ASP A OD1 1 
ATOM   10313 O  OD2 . ASP A 1 1344 ? -32.609  -12.971 -3.899  1.00 132.60 ? 1344 ASP A OD2 1 
ATOM   10314 N  N   . ASP A 1 1345 ? -30.619  -9.503  -6.161  1.00 142.36 ? 1345 ASP A N   1 
ATOM   10315 C  CA  . ASP A 1 1345 ? -30.917  -8.727  -7.344  1.00 139.26 ? 1345 ASP A CA  1 
ATOM   10316 C  C   . ASP A 1 1345 ? -32.461  -8.606  -7.447  1.00 109.37 ? 1345 ASP A C   1 
ATOM   10317 O  O   . ASP A 1 1345 ? -33.184  -9.594  -7.269  1.00 110.42 ? 1345 ASP A O   1 
ATOM   10318 C  CB  . ASP A 1 1345 ? -30.294  -9.383  -8.595  1.00 139.59 ? 1345 ASP A CB  1 
ATOM   10319 C  CG  . ASP A 1 1345 ? -28.842  -9.878  -8.373  1.00 144.43 ? 1345 ASP A CG  1 
ATOM   10320 O  OD1 . ASP A 1 1345 ? -28.085  -9.969  -9.370  1.00 145.62 ? 1345 ASP A OD1 1 
ATOM   10321 O  OD2 . ASP A 1 1345 ? -28.456  -10.201 -7.224  1.00 146.32 ? 1345 ASP A OD2 1 
ATOM   10322 N  N   . LEU A 1 1346 ? -32.970  -7.401  -7.708  1.00 106.78 ? 1346 LEU A N   1 
ATOM   10323 C  CA  . LEU A 1 1346 ? -34.412  -7.187  -7.890  1.00 103.62 ? 1346 LEU A CA  1 
ATOM   10324 C  C   . LEU A 1 1346 ? -34.871  -7.359  -9.347  1.00 105.05 ? 1346 LEU A C   1 
ATOM   10325 O  O   . LEU A 1 1346 ? -34.051  -7.222  -10.260 1.00 108.00 ? 1346 LEU A O   1 
ATOM   10326 C  CB  . LEU A 1 1346 ? -34.776  -5.790  -7.452  1.00 98.02  ? 1346 LEU A CB  1 
ATOM   10327 C  CG  . LEU A 1 1346 ? -36.279  -5.665  -7.366  1.00 95.65  ? 1346 LEU A CG  1 
ATOM   10328 C  CD1 . LEU A 1 1346 ? -36.783  -6.685  -6.381  1.00 96.27  ? 1346 LEU A CD1 1 
ATOM   10329 C  CD2 . LEU A 1 1346 ? -36.649  -4.269  -6.944  1.00 95.16  ? 1346 LEU A CD2 1 
ATOM   10330 N  N   . ILE A 1 1347 ? -36.166  -7.647  -9.569  1.00 101.47 ? 1347 ILE A N   1 
ATOM   10331 C  CA  . ILE A 1 1347 ? -36.738  -7.729  -10.933 1.00 94.47  ? 1347 ILE A CA  1 
ATOM   10332 C  C   . ILE A 1 1347 ? -38.203  -7.327  -11.127 1.00 88.18  ? 1347 ILE A C   1 
ATOM   10333 O  O   . ILE A 1 1347 ? -39.094  -8.163  -10.953 1.00 87.70  ? 1347 ILE A O   1 
ATOM   10334 C  CB  . ILE A 1 1347 ? -36.720  -9.138  -11.531 1.00 94.37  ? 1347 ILE A CB  1 
ATOM   10335 C  CG1 . ILE A 1 1347 ? -35.617  -10.009 -10.966 1.00 96.04  ? 1347 ILE A CG1 1 
ATOM   10336 C  CG2 . ILE A 1 1347 ? -36.606  -9.040  -13.042 1.00 93.45  ? 1347 ILE A CG2 1 
ATOM   10337 C  CD1 . ILE A 1 1347 ? -35.641  -11.404 -11.590 1.00 98.96  ? 1347 ILE A CD1 1 
ATOM   10338 N  N   . VAL A 1 1348 ? -38.436  -6.084  -11.550 1.00 84.48  ? 1348 VAL A N   1 
ATOM   10339 C  CA  . VAL A 1 1348 ? -39.736  -5.632  -12.070 1.00 83.80  ? 1348 VAL A CA  1 
ATOM   10340 C  C   . VAL A 1 1348 ? -40.063  -6.390  -13.383 1.00 93.66  ? 1348 VAL A C   1 
ATOM   10341 O  O   . VAL A 1 1348 ? -39.148  -6.632  -14.161 1.00 96.15  ? 1348 VAL A O   1 
ATOM   10342 C  CB  . VAL A 1 1348 ? -39.654  -4.104  -12.337 1.00 78.05  ? 1348 VAL A CB  1 
ATOM   10343 C  CG1 . VAL A 1 1348 ? -41.027  -3.486  -12.556 1.00 78.94  ? 1348 VAL A CG1 1 
ATOM   10344 C  CG2 . VAL A 1 1348 ? -38.970  -3.434  -11.191 1.00 77.56  ? 1348 VAL A CG2 1 
ATOM   10345 N  N   . SER A 1 1349 ? -41.320  -6.767  -13.651 1.00 91.66  ? 1349 SER A N   1 
ATOM   10346 C  CA  . SER A 1 1349 ? -41.595  -7.627  -14.819 1.00 92.43  ? 1349 SER A CA  1 
ATOM   10347 C  C   . SER A 1 1349 ? -43.059  -7.883  -15.219 1.00 97.09  ? 1349 SER A C   1 
ATOM   10348 O  O   . SER A 1 1349 ? -43.550  -9.028  -15.187 1.00 97.00  ? 1349 SER A O   1 
ATOM   10349 C  CB  . SER A 1 1349 ? -40.888  -8.971  -14.682 1.00 90.53  ? 1349 SER A CB  1 
ATOM   10350 O  OG  . SER A 1 1349 ? -41.120  -9.541  -13.419 1.00 90.63  ? 1349 SER A OG  1 
ATOM   10351 N  N   . THR A 1 1350 ? -43.725  -6.809  -15.637 1.00 99.26  ? 1350 THR A N   1 
ATOM   10352 C  CA  . THR A 1 1350 ? -45.085  -6.854  -16.198 1.00 101.12 ? 1350 THR A CA  1 
ATOM   10353 C  C   . THR A 1 1350 ? -45.412  -7.976  -17.199 1.00 99.58  ? 1350 THR A C   1 
ATOM   10354 O  O   . THR A 1 1350 ? -44.596  -8.339  -18.060 1.00 97.24  ? 1350 THR A O   1 
ATOM   10355 C  CB  . THR A 1 1350 ? -45.442  -5.529  -16.923 1.00 110.45 ? 1350 THR A CB  1 
ATOM   10356 O  OG1 . THR A 1 1350 ? -46.853  -5.483  -17.152 1.00 113.40 ? 1350 THR A OG1 1 
ATOM   10357 C  CG2 . THR A 1 1350 ? -44.758  -5.443  -18.282 1.00 108.71 ? 1350 THR A CG2 1 
ATOM   10358 N  N   . GLY A 1 1351 ? -46.653  -8.459  -17.105 1.00 99.25  ? 1351 GLY A N   1 
ATOM   10359 C  CA  . GLY A 1 1351 ? -47.190  -9.459  -18.010 1.00 98.12  ? 1351 GLY A CA  1 
ATOM   10360 C  C   . GLY A 1 1351 ? -47.334  -8.921  -19.405 1.00 94.26  ? 1351 GLY A C   1 
ATOM   10361 O  O   . GLY A 1 1351 ? -46.599  -8.023  -19.790 1.00 92.04  ? 1351 GLY A O   1 
ATOM   10362 N  N   . PHE A 1 1352 ? -48.260  -9.471  -20.179 1.00 95.50  ? 1352 PHE A N   1 
ATOM   10363 C  CA  . PHE A 1 1352 ? -48.548  -8.852  -21.465 1.00 93.43  ? 1352 PHE A CA  1 
ATOM   10364 C  C   . PHE A 1 1352 ? -49.195  -7.470  -21.220 1.00 92.05  ? 1352 PHE A C   1 
ATOM   10365 O  O   . PHE A 1 1352 ? -48.477  -6.508  -20.983 1.00 92.61  ? 1352 PHE A O   1 
ATOM   10366 C  CB  . PHE A 1 1352 ? -49.334  -9.760  -22.442 1.00 92.05  ? 1352 PHE A CB  1 
ATOM   10367 C  CG  . PHE A 1 1352 ? -49.767  -9.042  -23.688 1.00 89.36  ? 1352 PHE A CG  1 
ATOM   10368 C  CD1 . PHE A 1 1352 ? -48.887  -8.213  -24.361 1.00 86.33  ? 1352 PHE A CD1 1 
ATOM   10369 C  CD2 . PHE A 1 1352 ? -51.051  -9.162  -24.165 1.00 89.73  ? 1352 PHE A CD2 1 
ATOM   10370 C  CE1 . PHE A 1 1352 ? -49.274  -7.517  -25.475 1.00 83.62  ? 1352 PHE A CE1 1 
ATOM   10371 C  CE2 . PHE A 1 1352 ? -51.445  -8.468  -25.289 1.00 87.12  ? 1352 PHE A CE2 1 
ATOM   10372 C  CZ  . PHE A 1 1352 ? -50.554  -7.643  -25.938 1.00 84.66  ? 1352 PHE A CZ  1 
ATOM   10373 N  N   . GLY A 1 1353 ? -50.520  -7.357  -21.250 1.00 91.64  ? 1353 GLY A N   1 
ATOM   10374 C  CA  . GLY A 1 1353 ? -51.173  -6.094  -20.917 1.00 91.05  ? 1353 GLY A CA  1 
ATOM   10375 C  C   . GLY A 1 1353 ? -50.941  -4.886  -21.826 1.00 90.50  ? 1353 GLY A C   1 
ATOM   10376 O  O   . GLY A 1 1353 ? -50.718  -5.046  -23.014 1.00 89.12  ? 1353 GLY A O   1 
ATOM   10377 N  N   . SER A 1 1354 ? -50.988  -3.679  -21.254 1.00 89.68  ? 1354 SER A N   1 
ATOM   10378 C  CA  . SER A 1 1354 ? -51.098  -2.437  -22.016 1.00 88.06  ? 1354 SER A CA  1 
ATOM   10379 C  C   . SER A 1 1354 ? -50.912  -1.176  -21.179 1.00 85.45  ? 1354 SER A C   1 
ATOM   10380 O  O   . SER A 1 1354 ? -51.227  -1.158  -19.988 1.00 85.69  ? 1354 SER A O   1 
ATOM   10381 C  CB  . SER A 1 1354 ? -52.493  -2.357  -22.624 1.00 90.86  ? 1354 SER A CB  1 
ATOM   10382 O  OG  . SER A 1 1354 ? -53.378  -1.599  -21.793 1.00 91.42  ? 1354 SER A OG  1 
ATOM   10383 N  N   . GLY A 1 1355 ? -50.459  -0.105  -21.829 1.00 82.74  ? 1355 GLY A N   1 
ATOM   10384 C  CA  . GLY A 1 1355 ? -50.209  1.162   -21.154 1.00 81.76  ? 1355 GLY A CA  1 
ATOM   10385 C  C   . GLY A 1 1355 ? -48.721  1.443   -20.965 1.00 82.43  ? 1355 GLY A C   1 
ATOM   10386 O  O   . GLY A 1 1355 ? -47.872  0.798   -21.587 1.00 85.02  ? 1355 GLY A O   1 
ATOM   10387 N  N   . LEU A 1 1356 ? -48.391  2.388   -20.094 1.00 83.09  ? 1356 LEU A N   1 
ATOM   10388 C  CA  . LEU A 1 1356 ? -46.997  2.729   -19.867 1.00 84.25  ? 1356 LEU A CA  1 
ATOM   10389 C  C   . LEU A 1 1356 ? -46.684  2.992   -18.391 1.00 92.62  ? 1356 LEU A C   1 
ATOM   10390 O  O   . LEU A 1 1356 ? -47.124  3.991   -17.817 1.00 97.49  ? 1356 LEU A O   1 
ATOM   10391 C  CB  . LEU A 1 1356 ? -46.674  3.967   -20.673 1.00 82.22  ? 1356 LEU A CB  1 
ATOM   10392 C  CG  . LEU A 1 1356 ? -46.075  3.713   -22.036 1.00 78.10  ? 1356 LEU A CG  1 
ATOM   10393 C  CD1 . LEU A 1 1356 ? -46.228  4.922   -22.914 1.00 75.15  ? 1356 LEU A CD1 1 
ATOM   10394 C  CD2 . LEU A 1 1356 ? -44.650  3.432   -21.768 1.00 76.50  ? 1356 LEU A CD2 1 
ATOM   10395 N  N   . ALA A 1 1357 ? -45.926  2.101   -17.765 1.00 88.76  ? 1357 ALA A N   1 
ATOM   10396 C  CA  . ALA A 1 1357 ? -45.597  2.285   -16.349 1.00 82.73  ? 1357 ALA A CA  1 
ATOM   10397 C  C   . ALA A 1 1357 ? -44.110  2.609   -16.133 1.00 79.25  ? 1357 ALA A C   1 
ATOM   10398 O  O   . ALA A 1 1357 ? -43.251  1.859   -16.581 1.00 77.10  ? 1357 ALA A O   1 
ATOM   10399 C  CB  . ALA A 1 1357 ? -46.015  1.063   -15.541 1.00 79.91  ? 1357 ALA A CB  1 
ATOM   10400 N  N   . THR A 1 1358 ? -43.815  3.725   -15.465 1.00 75.62  ? 1358 THR A N   1 
ATOM   10401 C  CA  . THR A 1 1358 ? -42.441  4.094   -15.181 1.00 74.29  ? 1358 THR A CA  1 
ATOM   10402 C  C   . THR A 1 1358 ? -41.878  3.485   -13.887 1.00 76.40  ? 1358 THR A C   1 
ATOM   10403 O  O   . THR A 1 1358 ? -42.253  3.889   -12.779 1.00 76.57  ? 1358 THR A O   1 
ATOM   10404 C  CB  . THR A 1 1358 ? -42.208  5.649   -15.188 1.00 94.52  ? 1358 THR A CB  1 
ATOM   10405 O  OG1 . THR A 1 1358 ? -43.204  6.350   -14.416 1.00 94.70  ? 1358 THR A OG1 1 
ATOM   10406 C  CG2 . THR A 1 1358 ? -42.172  6.177   -16.610 1.00 93.18  ? 1358 THR A CG2 1 
ATOM   10407 N  N   . VAL A 1 1359 ? -40.961  2.533   -14.041 1.00 74.59  ? 1359 VAL A N   1 
ATOM   10408 C  CA  . VAL A 1 1359 ? -40.114  2.083   -12.944 1.00 79.53  ? 1359 VAL A CA  1 
ATOM   10409 C  C   . VAL A 1 1359 ? -38.886  3.001   -12.699 1.00 84.74  ? 1359 VAL A C   1 
ATOM   10410 O  O   . VAL A 1 1359 ? -38.016  3.121   -13.564 1.00 82.44  ? 1359 VAL A O   1 
ATOM   10411 C  CB  . VAL A 1 1359 ? -39.563  0.671   -13.227 1.00 75.07  ? 1359 VAL A CB  1 
ATOM   10412 C  CG1 . VAL A 1 1359 ? -38.688  0.221   -12.069 1.00 75.70  ? 1359 VAL A CG1 1 
ATOM   10413 C  CG2 . VAL A 1 1359 ? -40.669  -0.318  -13.465 1.00 75.41  ? 1359 VAL A CG2 1 
ATOM   10414 N  N   . HIS A 1 1360 ? -38.824  3.657   -11.538 1.00 84.67  ? 1360 HIS A N   1 
ATOM   10415 C  CA  . HIS A 1 1360 ? -37.559  4.213   -11.032 1.00 87.79  ? 1360 HIS A CA  1 
ATOM   10416 C  C   . HIS A 1 1360 ? -37.145  3.519   -9.761  1.00 89.08  ? 1360 HIS A C   1 
ATOM   10417 O  O   . HIS A 1 1360 ? -37.990  3.074   -8.987  1.00 92.23  ? 1360 HIS A O   1 
ATOM   10418 C  CB  . HIS A 1 1360 ? -37.655  5.680   -10.687 1.00 91.52  ? 1360 HIS A CB  1 
ATOM   10419 C  CG  . HIS A 1 1360 ? -37.884  6.552   -11.863 1.00 91.97  ? 1360 HIS A CG  1 
ATOM   10420 N  ND1 . HIS A 1 1360 ? -39.098  6.604   -12.513 1.00 90.98  ? 1360 HIS A ND1 1 
ATOM   10421 C  CD2 . HIS A 1 1360 ? -37.067  7.425   -12.495 1.00 92.00  ? 1360 HIS A CD2 1 
ATOM   10422 C  CE1 . HIS A 1 1360 ? -39.017  7.468   -13.506 1.00 91.05  ? 1360 HIS A CE1 1 
ATOM   10423 N  NE2 . HIS A 1 1360 ? -37.796  7.977   -13.520 1.00 92.10  ? 1360 HIS A NE2 1 
ATOM   10424 N  N   . VAL A 1 1361 ? -35.844  3.492   -9.506  1.00 85.49  ? 1361 VAL A N   1 
ATOM   10425 C  CA  . VAL A 1 1361 ? -35.332  2.767   -8.357  1.00 86.50  ? 1361 VAL A CA  1 
ATOM   10426 C  C   . VAL A 1 1361 ? -34.109  3.457   -7.801  1.00 88.36  ? 1361 VAL A C   1 
ATOM   10427 O  O   . VAL A 1 1361 ? -32.975  3.214   -8.217  1.00 88.22  ? 1361 VAL A O   1 
ATOM   10428 C  CB  . VAL A 1 1361 ? -35.051  1.303   -8.721  1.00 84.14  ? 1361 VAL A CB  1 
ATOM   10429 C  CG1 . VAL A 1 1361 ? -33.696  0.892   -8.286  1.00 78.26  ? 1361 VAL A CG1 1 
ATOM   10430 C  CG2 . VAL A 1 1361 ? -36.094  0.404   -8.115  1.00 78.09  ? 1361 VAL A CG2 1 
ATOM   10431 N  N   . THR A 1 1362 ? -34.376  4.344   -6.848  1.00 90.38  ? 1362 THR A N   1 
ATOM   10432 C  CA  . THR A 1 1362 ? -33.396  5.319   -6.413  1.00 90.31  ? 1362 THR A CA  1 
ATOM   10433 C  C   . THR A 1 1362 ? -32.671  4.833   -5.166  1.00 88.37  ? 1362 THR A C   1 
ATOM   10434 O  O   . THR A 1 1362 ? -33.259  4.700   -4.108  1.00 85.94  ? 1362 THR A O   1 
ATOM   10435 C  CB  . THR A 1 1362 ? -34.060  6.702   -6.290  1.00 92.80  ? 1362 THR A CB  1 
ATOM   10436 O  OG1 . THR A 1 1362 ? -33.067  7.707   -6.062  1.00 94.70  ? 1362 THR A OG1 1 
ATOM   10437 C  CG2 . THR A 1 1362 ? -35.097  6.694   -5.205  1.00 93.83  ? 1362 THR A CG2 1 
ATOM   10438 N  N   . THR A 1 1363 ? -31.392  4.510   -5.355  1.00 90.64  ? 1363 THR A N   1 
ATOM   10439 C  CA  . THR A 1 1363 ? -30.596  3.719   -4.400  1.00 97.45  ? 1363 THR A CA  1 
ATOM   10440 C  C   . THR A 1 1363 ? -29.520  4.522   -3.643  1.00 104.84 ? 1363 THR A C   1 
ATOM   10441 O  O   . THR A 1 1363 ? -28.552  5.010   -4.238  1.00 106.17 ? 1363 THR A O   1 
ATOM   10442 C  CB  . THR A 1 1363 ? -29.907  2.462   -5.064  1.00 154.31 ? 1363 THR A CB  1 
ATOM   10443 O  OG1 . THR A 1 1363 ? -28.490  2.645   -5.130  1.00 154.29 ? 1363 THR A OG1 1 
ATOM   10444 C  CG2 . THR A 1 1363 ? -30.437  2.190   -6.453  1.00 153.18 ? 1363 THR A CG2 1 
ATOM   10445 N  N   . VAL A 1 1364 ? -29.694  4.625   -2.324  1.00 107.49 ? 1364 VAL A N   1 
ATOM   10446 C  CA  . VAL A 1 1364 ? -28.831  5.411   -1.451  1.00 106.72 ? 1364 VAL A CA  1 
ATOM   10447 C  C   . VAL A 1 1364 ? -27.762  4.590   -0.771  1.00 110.81 ? 1364 VAL A C   1 
ATOM   10448 O  O   . VAL A 1 1364 ? -28.002  3.476   -0.299  1.00 112.84 ? 1364 VAL A O   1 
ATOM   10449 C  CB  . VAL A 1 1364 ? -29.638  6.000   -0.342  1.00 103.78 ? 1364 VAL A CB  1 
ATOM   10450 C  CG1 . VAL A 1 1364 ? -28.748  6.253   0.865   1.00 106.33 ? 1364 VAL A CG1 1 
ATOM   10451 C  CG2 . VAL A 1 1364 ? -30.303  7.244   -0.836  1.00 102.04 ? 1364 VAL A CG2 1 
ATOM   10452 N  N   . VAL A 1 1365 ? -26.571  5.141   -0.685  1.00 111.88 ? 1365 VAL A N   1 
ATOM   10453 C  CA  . VAL A 1 1365 ? -25.548  4.402   -0.004  1.00 114.36 ? 1365 VAL A CA  1 
ATOM   10454 C  C   . VAL A 1 1365 ? -24.575  5.391   0.637   1.00 122.70 ? 1365 VAL A C   1 
ATOM   10455 O  O   . VAL A 1 1365 ? -24.498  6.543   0.208   1.00 125.65 ? 1365 VAL A O   1 
ATOM   10456 C  CB  . VAL A 1 1365 ? -24.899  3.398   -0.970  1.00 108.58 ? 1365 VAL A CB  1 
ATOM   10457 C  CG1 . VAL A 1 1365 ? -23.720  4.023   -1.744  1.00 107.54 ? 1365 VAL A CG1 1 
ATOM   10458 C  CG2 . VAL A 1 1365 ? -24.510  2.145   -0.217  1.00 108.03 ? 1365 VAL A CG2 1 
ATOM   10459 N  N   . HIS A 1 1366 ? -23.893  4.977   1.708   1.00 125.55 ? 1366 HIS A N   1 
ATOM   10460 C  CA  . HIS A 1 1366 ? -22.889  5.828   2.347   1.00 126.43 ? 1366 HIS A CA  1 
ATOM   10461 C  C   . HIS A 1 1366 ? -21.523  5.302   2.027   1.00 123.31 ? 1366 HIS A C   1 
ATOM   10462 O  O   . HIS A 1 1366 ? -21.247  4.121   2.247   1.00 123.13 ? 1366 HIS A O   1 
ATOM   10463 C  CB  . HIS A 1 1366 ? -23.039  5.812   3.858   1.00 130.20 ? 1366 HIS A CB  1 
ATOM   10464 C  CG  . HIS A 1 1366 ? -24.351  6.324   4.340   1.00 132.18 ? 1366 HIS A CG  1 
ATOM   10465 N  ND1 . HIS A 1 1366 ? -25.544  5.974   3.752   1.00 131.93 ? 1366 HIS A ND1 1 
ATOM   10466 C  CD2 . HIS A 1 1366 ? -24.662  7.146   5.368   1.00 135.18 ? 1366 HIS A CD2 1 
ATOM   10467 C  CE1 . HIS A 1 1366 ? -26.536  6.569   4.388   1.00 133.23 ? 1366 HIS A CE1 1 
ATOM   10468 N  NE2 . HIS A 1 1366 ? -26.028  7.284   5.377   1.00 135.30 ? 1366 HIS A NE2 1 
ATOM   10469 N  N   . LYS A 1 1367 ? -20.662  6.163   1.506   1.00 123.47 ? 1367 LYS A N   1 
ATOM   10470 C  CA  . LYS A 1 1367 ? -19.279  5.744   1.315   1.00 126.70 ? 1367 LYS A CA  1 
ATOM   10471 C  C   . LYS A 1 1367 ? -18.310  6.429   2.273   1.00 127.46 ? 1367 LYS A C   1 
ATOM   10472 O  O   . LYS A 1 1367 ? -18.666  7.407   2.929   1.00 128.46 ? 1367 LYS A O   1 
ATOM   10473 C  CB  . LYS A 1 1367 ? -18.826  5.877   -0.144  1.00 129.96 ? 1367 LYS A CB  1 
ATOM   10474 C  CG  . LYS A 1 1367 ? -19.246  7.126   -0.882  1.00 131.81 ? 1367 LYS A CG  1 
ATOM   10475 C  CD  . LYS A 1 1367 ? -18.989  6.931   -2.369  1.00 132.29 ? 1367 LYS A CD  1 
ATOM   10476 C  CE  . LYS A 1 1367 ? -19.607  5.619   -2.846  1.00 131.42 ? 1367 LYS A CE  1 
ATOM   10477 N  NZ  . LYS A 1 1367 ? -18.888  5.093   -4.026  1.00 131.33 ? 1367 LYS A NZ  1 
ATOM   10478 N  N   . THR A 1 1368 ? -17.094  5.903   2.372   1.00 123.70 ? 1368 THR A N   1 
ATOM   10479 C  CA  . THR A 1 1368 ? -16.126  6.471   3.291   1.00 121.44 ? 1368 THR A CA  1 
ATOM   10480 C  C   . THR A 1 1368 ? -15.220  7.499   2.630   1.00 121.54 ? 1368 THR A C   1 
ATOM   10481 O  O   . THR A 1 1368 ? -14.382  8.102   3.301   1.00 123.79 ? 1368 THR A O   1 
ATOM   10482 C  CB  . THR A 1 1368 ? -15.262  5.380   3.930   1.00 123.23 ? 1368 THR A CB  1 
ATOM   10483 O  OG1 . THR A 1 1368 ? -14.205  5.017   3.035   1.00 125.30 ? 1368 THR A OG1 1 
ATOM   10484 C  CG2 . THR A 1 1368 ? -16.097  4.159   4.236   1.00 121.45 ? 1368 THR A CG2 1 
ATOM   10485 N  N   . SER A 1 1369 ? -15.397  7.721   1.329   1.00 119.93 ? 1369 SER A N   1 
ATOM   10486 C  CA  . SER A 1 1369 ? -14.415  8.497   0.567   1.00 121.21 ? 1369 SER A CA  1 
ATOM   10487 C  C   . SER A 1 1369 ? -14.908  9.243   -0.657  1.00 121.22 ? 1369 SER A C   1 
ATOM   10488 O  O   . SER A 1 1369 ? -15.897  8.890   -1.289  1.00 117.42 ? 1369 SER A O   1 
ATOM   10489 C  CB  . SER A 1 1369 ? -13.266  7.596   0.128   1.00 124.38 ? 1369 SER A CB  1 
ATOM   10490 O  OG  . SER A 1 1369 ? -12.774  6.853   1.226   1.00 127.34 ? 1369 SER A OG  1 
ATOM   10491 N  N   . THR A 1 1370 ? -14.165  10.276  -0.999  1.00 126.29 ? 1370 THR A N   1 
ATOM   10492 C  CA  . THR A 1 1370 ? -14.455  11.035  -2.182  1.00 130.83 ? 1370 THR A CA  1 
ATOM   10493 C  C   . THR A 1 1370 ? -13.349  10.801  -3.189  1.00 142.77 ? 1370 THR A C   1 
ATOM   10494 O  O   . THR A 1 1370 ? -13.539  11.015  -4.375  1.00 144.42 ? 1370 THR A O   1 
ATOM   10495 C  CB  . THR A 1 1370 ? -14.584  12.527  -1.847  1.00 125.50 ? 1370 THR A CB  1 
ATOM   10496 O  OG1 . THR A 1 1370 ? -15.803  12.728  -1.139  1.00 120.43 ? 1370 THR A OG1 1 
ATOM   10497 C  CG2 . THR A 1 1370 ? -14.611  13.380  -3.106  1.00 124.78 ? 1370 THR A CG2 1 
ATOM   10498 N  N   . SER A 1 1371 ? -12.202  10.328  -2.719  1.00 151.92 ? 1371 SER A N   1 
ATOM   10499 C  CA  . SER A 1 1371 ? -11.032  10.191  -3.583  1.00 162.36 ? 1371 SER A CA  1 
ATOM   10500 C  C   . SER A 1 1371 ? -11.414  9.884   -5.032  1.00 167.22 ? 1371 SER A C   1 
ATOM   10501 O  O   . SER A 1 1371 ? -10.880  10.480  -5.971  1.00 170.07 ? 1371 SER A O   1 
ATOM   10502 C  CB  . SER A 1 1371 ? -10.098  9.104   -3.045  1.00 167.75 ? 1371 SER A CB  1 
ATOM   10503 O  OG  . SER A 1 1371 ? -10.662  7.809   -3.180  1.00 169.41 ? 1371 SER A OG  1 
ATOM   10504 N  N   . GLU A 1 1372 ? -12.345  8.949   -5.195  1.00 169.28 ? 1372 GLU A N   1 
ATOM   10505 C  CA  . GLU A 1 1372 ? -12.875  8.573   -6.501  1.00 172.00 ? 1372 GLU A CA  1 
ATOM   10506 C  C   . GLU A 1 1372 ? -13.394  9.781   -7.292  1.00 162.10 ? 1372 GLU A C   1 
ATOM   10507 O  O   . GLU A 1 1372 ? -12.806  10.160  -8.301  1.00 162.86 ? 1372 GLU A O   1 
ATOM   10508 C  CB  . GLU A 1 1372 ? -13.999  7.535   -6.329  1.00 182.39 ? 1372 GLU A CB  1 
ATOM   10509 C  CG  . GLU A 1 1372 ? -14.981  7.868   -5.187  1.00 191.06 ? 1372 GLU A CG  1 
ATOM   10510 C  CD  . GLU A 1 1372 ? -16.297  7.086   -5.229  1.00 197.61 ? 1372 GLU A CD  1 
ATOM   10511 O  OE1 . GLU A 1 1372 ? -16.362  6.029   -5.900  1.00 201.65 ? 1372 GLU A OE1 1 
ATOM   10512 O  OE2 . GLU A 1 1372 ? -17.265  7.537   -4.573  1.00 197.70 ? 1372 GLU A OE2 1 
ATOM   10513 N  N   . GLU A 1 1373 ? -14.476  10.386  -6.799  1.00 151.29 ? 1373 GLU A N   1 
ATOM   10514 C  CA  . GLU A 1 1373 ? -15.262  11.422  -7.495  1.00 140.85 ? 1373 GLU A CA  1 
ATOM   10515 C  C   . GLU A 1 1373 ? -14.488  12.517  -8.243  1.00 136.98 ? 1373 GLU A C   1 
ATOM   10516 O  O   . GLU A 1 1373 ? -13.276  12.667  -8.089  1.00 138.49 ? 1373 GLU A O   1 
ATOM   10517 C  CB  . GLU A 1 1373 ? -16.247  12.078  -6.511  1.00 132.99 ? 1373 GLU A CB  1 
ATOM   10518 C  CG  . GLU A 1 1373 ? -17.110  11.078  -5.747  1.00 126.29 ? 1373 GLU A CG  1 
ATOM   10519 C  CD  . GLU A 1 1373 ? -17.944  11.714  -4.654  1.00 118.55 ? 1373 GLU A CD  1 
ATOM   10520 O  OE1 . GLU A 1 1373 ? -17.737  12.924  -4.371  1.00 115.35 ? 1373 GLU A OE1 1 
ATOM   10521 O  OE2 . GLU A 1 1373 ? -18.803  10.987  -4.089  1.00 114.63 ? 1373 GLU A OE2 1 
ATOM   10522 N  N   . VAL A 1 1374 ? -15.214  13.286  -9.047  1.00 131.44 ? 1374 VAL A N   1 
ATOM   10523 C  CA  . VAL A 1 1374 ? -14.624  14.338  -9.858  1.00 127.76 ? 1374 VAL A CA  1 
ATOM   10524 C  C   . VAL A 1 1374 ? -14.756  15.721  -9.253  1.00 125.92 ? 1374 VAL A C   1 
ATOM   10525 O  O   . VAL A 1 1374 ? -15.864  16.260  -9.132  1.00 125.34 ? 1374 VAL A O   1 
ATOM   10526 C  CB  . VAL A 1 1374 ? -15.324  14.437  -11.181 1.00 125.02 ? 1374 VAL A CB  1 
ATOM   10527 C  CG1 . VAL A 1 1374 ? -14.435  15.169  -12.152 1.00 126.23 ? 1374 VAL A CG1 1 
ATOM   10528 C  CG2 . VAL A 1 1374 ? -15.708  13.054  -11.680 1.00 124.03 ? 1374 VAL A CG2 1 
ATOM   10529 N  N   . CYS A 1 1375 ? -13.627  16.323  -8.907  1.00 127.25 ? 1375 CYS A N   1 
ATOM   10530 C  CA  . CYS A 1 1375 ? -13.672  17.647  -8.274  1.00 124.03 ? 1375 CYS A CA  1 
ATOM   10531 C  C   . CYS A 1 1375 ? -13.647  18.853  -9.237  1.00 124.54 ? 1375 CYS A C   1 
ATOM   10532 O  O   . CYS A 1 1375 ? -12.671  19.097  -9.951  1.00 124.47 ? 1375 CYS A O   1 
ATOM   10533 C  CB  . CYS A 1 1375 ? -12.639  17.781  -7.132  1.00 123.13 ? 1375 CYS A CB  1 
ATOM   10534 S  SG  . CYS A 1 1375 ? -13.345  17.474  -5.477  1.00 201.00 ? 1375 CYS A SG  1 
ATOM   10535 N  N   . SER A 1 1376 ? -14.746  19.598  -9.220  1.00 123.66 ? 1376 SER A N   1 
ATOM   10536 C  CA  . SER A 1 1376 ? -14.940  20.733  -10.095 1.00 124.65 ? 1376 SER A CA  1 
ATOM   10537 C  C   . SER A 1 1376 ? -14.602  22.051  -9.372  1.00 128.16 ? 1376 SER A C   1 
ATOM   10538 O  O   . SER A 1 1376 ? -14.606  23.128  -9.974  1.00 129.70 ? 1376 SER A O   1 
ATOM   10539 C  CB  . SER A 1 1376 ? -16.380  20.691  -10.587 1.00 121.08 ? 1376 SER A CB  1 
ATOM   10540 O  OG  . SER A 1 1376 ? -16.903  19.382  -10.393 1.00 118.25 ? 1376 SER A OG  1 
ATOM   10541 N  N   . PHE A 1 1377 ? -14.287  21.933  -8.079  1.00 127.46 ? 1377 PHE A N   1 
ATOM   10542 C  CA  . PHE A 1 1377 ? -13.929  23.047  -7.191  1.00 124.93 ? 1377 PHE A CA  1 
ATOM   10543 C  C   . PHE A 1 1377 ? -12.720  22.727  -6.301  1.00 129.09 ? 1377 PHE A C   1 
ATOM   10544 O  O   . PHE A 1 1377 ? -12.651  21.644  -5.700  1.00 129.79 ? 1377 PHE A O   1 
ATOM   10545 C  CB  . PHE A 1 1377 ? -15.090  23.335  -6.262  1.00 120.60 ? 1377 PHE A CB  1 
ATOM   10546 C  CG  . PHE A 1 1377 ? -16.126  24.182  -6.863  1.00 120.04 ? 1377 PHE A CG  1 
ATOM   10547 C  CD1 . PHE A 1 1377 ? -15.898  25.519  -7.066  1.00 120.57 ? 1377 PHE A CD1 1 
ATOM   10548 C  CD2 . PHE A 1 1377 ? -17.331  23.649  -7.234  1.00 120.41 ? 1377 PHE A CD2 1 
ATOM   10549 C  CE1 . PHE A 1 1377 ? -16.857  26.313  -7.620  1.00 119.50 ? 1377 PHE A CE1 1 
ATOM   10550 C  CE2 . PHE A 1 1377 ? -18.291  24.445  -7.797  1.00 119.45 ? 1377 PHE A CE2 1 
ATOM   10551 C  CZ  . PHE A 1 1377 ? -18.046  25.778  -7.988  1.00 119.09 ? 1377 PHE A CZ  1 
ATOM   10552 N  N   . TYR A 1 1378 ? -11.777  23.665  -6.196  1.00 129.95 ? 1378 TYR A N   1 
ATOM   10553 C  CA  . TYR A 1 1378 ? -10.620  23.469  -5.323  1.00 128.51 ? 1378 TYR A CA  1 
ATOM   10554 C  C   . TYR A 1 1378 ? -11.031  23.888  -3.920  1.00 125.68 ? 1378 TYR A C   1 
ATOM   10555 O  O   . TYR A 1 1378 ? -11.514  24.999  -3.717  1.00 122.06 ? 1378 TYR A O   1 
ATOM   10556 C  CB  . TYR A 1 1378 ? -9.397   24.279  -5.799  1.00 128.60 ? 1378 TYR A CB  1 
ATOM   10557 C  CG  . TYR A 1 1378 ? -8.664   23.762  -7.043  1.00 127.18 ? 1378 TYR A CG  1 
ATOM   10558 C  CD1 . TYR A 1 1378 ? -8.156   22.477  -7.096  1.00 126.52 ? 1378 TYR A CD1 1 
ATOM   10559 C  CD2 . TYR A 1 1378 ? -8.451   24.587  -8.146  1.00 126.74 ? 1378 TYR A CD2 1 
ATOM   10560 C  CE1 . TYR A 1 1378 ? -7.480   22.011  -8.219  1.00 127.96 ? 1378 TYR A CE1 1 
ATOM   10561 C  CE2 . TYR A 1 1378 ? -7.777   24.132  -9.277  1.00 127.86 ? 1378 TYR A CE2 1 
ATOM   10562 C  CZ  . TYR A 1 1378 ? -7.292   22.841  -9.309  1.00 128.26 ? 1378 TYR A CZ  1 
ATOM   10563 O  OH  . TYR A 1 1378 ? -6.623   22.379  -10.427 1.00 128.84 ? 1378 TYR A OH  1 
ATOM   10564 N  N   . LEU A 1 1379 ? -10.857  23.002  -2.952  1.00 127.77 ? 1379 LEU A N   1 
ATOM   10565 C  CA  . LEU A 1 1379 ? -11.288  23.335  -1.605  1.00 131.91 ? 1379 LEU A CA  1 
ATOM   10566 C  C   . LEU A 1 1379 ? -10.197  23.256  -0.539  1.00 140.83 ? 1379 LEU A C   1 
ATOM   10567 O  O   . LEU A 1 1379 ? -9.163   22.584  -0.695  1.00 145.26 ? 1379 LEU A O   1 
ATOM   10568 C  CB  . LEU A 1 1379 ? -12.447  22.448  -1.192  1.00 128.21 ? 1379 LEU A CB  1 
ATOM   10569 C  CG  . LEU A 1 1379 ? -13.641  22.639  -2.096  1.00 125.27 ? 1379 LEU A CG  1 
ATOM   10570 C  CD1 . LEU A 1 1379 ? -14.782  21.712  -1.684  1.00 122.58 ? 1379 LEU A CD1 1 
ATOM   10571 C  CD2 . LEU A 1 1379 ? -14.015  24.088  -2.006  1.00 124.58 ? 1379 LEU A CD2 1 
ATOM   10572 N  N   . LYS A 1 1380 ? -10.451  23.969  0.550   1.00 142.47 ? 1380 LYS A N   1 
ATOM   10573 C  CA  . LYS A 1 1380 ? -9.648   23.862  1.744   1.00 144.66 ? 1380 LYS A CA  1 
ATOM   10574 C  C   . LYS A 1 1380 ? -10.572  24.257  2.885   1.00 141.38 ? 1380 LYS A C   1 
ATOM   10575 O  O   . LYS A 1 1380 ? -11.512  25.038  2.703   1.00 139.27 ? 1380 LYS A O   1 
ATOM   10576 C  CB  . LYS A 1 1380 ? -8.335   24.685  1.669   1.00 131.87 ? 1380 LYS A CB  1 
ATOM   10577 C  CG  . LYS A 1 1380 ? -8.415   26.147  1.136   1.00 138.09 ? 1380 LYS A CG  1 
ATOM   10578 C  CD  . LYS A 1 1380 ? -7.000   26.830  1.008   1.00 138.91 ? 1380 LYS A CD  1 
ATOM   10579 C  CE  . LYS A 1 1380 ? -7.053   28.382  0.874   1.00 121.18 ? 1380 LYS A CE  1 
ATOM   10580 N  NZ  . LYS A 1 1380 ? -5.774   29.120  1.150   1.00 123.13 ? 1380 LYS A NZ  1 
ATOM   10581 N  N   . ILE A 1 1381 ? -10.338  23.650  4.039   1.00 142.15 ? 1381 ILE A N   1 
ATOM   10582 C  CA  . ILE A 1 1381 ? -11.119  23.917  5.235   1.00 137.82 ? 1381 ILE A CA  1 
ATOM   10583 C  C   . ILE A 1 1381 ? -10.312  23.468  6.451   1.00 145.50 ? 1381 ILE A C   1 
ATOM   10584 O  O   . ILE A 1 1381 ? -9.511   22.527  6.360   1.00 151.06 ? 1381 ILE A O   1 
ATOM   10585 C  CB  . ILE A 1 1381 ? -12.442  23.149  5.218   1.00 126.82 ? 1381 ILE A CB  1 
ATOM   10586 C  CG1 . ILE A 1 1381 ? -13.479  23.920  5.998   1.00 123.37 ? 1381 ILE A CG1 1 
ATOM   10587 C  CG2 . ILE A 1 1381 ? -12.298  21.758  5.835   1.00 123.80 ? 1381 ILE A CG2 1 
ATOM   10588 C  CD1 . ILE A 1 1381 ? -14.519  23.038  6.537   1.00 121.18 ? 1381 ILE A CD1 1 
ATOM   10589 N  N   . ASP A 1 1382 ? -10.502  24.150  7.578   1.00 145.90 ? 1382 ASP A N   1 
ATOM   10590 C  CA  . ASP A 1 1382 ? -9.969   23.679  8.857   1.00 148.70 ? 1382 ASP A CA  1 
ATOM   10591 C  C   . ASP A 1 1382 ? -10.500  24.499  10.026  1.00 148.37 ? 1382 ASP A C   1 
ATOM   10592 O  O   . ASP A 1 1382 ? -11.166  25.512  9.829   1.00 145.35 ? 1382 ASP A O   1 
ATOM   10593 C  CB  . ASP A 1 1382 ? -8.430   23.627  8.865   1.00 155.38 ? 1382 ASP A CB  1 
ATOM   10594 C  CG  . ASP A 1 1382 ? -7.787   24.875  8.275   1.00 159.60 ? 1382 ASP A CG  1 
ATOM   10595 O  OD1 . ASP A 1 1382 ? -7.977   25.120  7.063   1.00 159.62 ? 1382 ASP A OD1 1 
ATOM   10596 O  OD2 . ASP A 1 1382 ? -7.067   25.594  9.013   1.00 162.88 ? 1382 ASP A OD2 1 
ATOM   10597 N  N   . THR A 1 1383 ? -10.226  24.035  11.241  1.00 151.80 ? 1383 THR A N   1 
ATOM   10598 C  CA  . THR A 1 1383 ? -10.624  24.752  12.450  1.00 152.41 ? 1383 THR A CA  1 
ATOM   10599 C  C   . THR A 1 1383 ? -9.482   25.551  13.103  1.00 154.85 ? 1383 THR A C   1 
ATOM   10600 O  O   . THR A 1 1383 ? -8.488   24.993  13.585  1.00 155.30 ? 1383 THR A O   1 
ATOM   10601 C  CB  . THR A 1 1383 ? -11.311  23.818  13.483  1.00 151.26 ? 1383 THR A CB  1 
ATOM   10602 O  OG1 . THR A 1 1383 ? -10.860  22.472  13.301  1.00 152.92 ? 1383 THR A OG1 1 
ATOM   10603 C  CG2 . THR A 1 1383 ? -12.813  23.844  13.309  1.00 147.19 ? 1383 THR A CG2 1 
ATOM   10604 N  N   . GLN A 1 1384 ? -9.652   26.868  13.102  1.00 156.07 ? 1384 GLN A N   1 
ATOM   10605 C  CA  . GLN A 1 1384 ? -8.729   27.780  13.751  1.00 162.29 ? 1384 GLN A CA  1 
ATOM   10606 C  C   . GLN A 1 1384 ? -9.128   28.017  15.198  1.00 164.54 ? 1384 GLN A C   1 
ATOM   10607 O  O   . GLN A 1 1384 ? -10.282  27.809  15.574  1.00 162.01 ? 1384 GLN A O   1 
ATOM   10608 C  CB  . GLN A 1 1384 ? -8.726   29.118  13.024  1.00 164.80 ? 1384 GLN A CB  1 
ATOM   10609 C  CG  . GLN A 1 1384 ? -8.347   29.017  11.568  1.00 168.57 ? 1384 GLN A CG  1 
ATOM   10610 C  CD  . GLN A 1 1384 ? -8.148   30.376  10.927  1.00 172.18 ? 1384 GLN A CD  1 
ATOM   10611 O  OE1 . GLN A 1 1384 ? -8.898   31.315  11.191  1.00 172.29 ? 1384 GLN A OE1 1 
ATOM   10612 N  NE2 . GLN A 1 1384 ? -7.133   30.486  10.074  1.00 174.86 ? 1384 GLN A NE2 1 
ATOM   10613 N  N   . ASP A 1 1385 ? -8.173   28.468  16.008  1.00 169.12 ? 1385 ASP A N   1 
ATOM   10614 C  CA  . ASP A 1 1385 ? -8.456   28.804  17.400  1.00 171.09 ? 1385 ASP A CA  1 
ATOM   10615 C  C   . ASP A 1 1385 ? -8.601   30.321  17.626  1.00 171.60 ? 1385 ASP A C   1 
ATOM   10616 O  O   . ASP A 1 1385 ? -9.386   30.764  18.475  1.00 170.54 ? 1385 ASP A O   1 
ATOM   10617 C  CB  . ASP A 1 1385 ? -7.412   28.178  18.332  1.00 173.92 ? 1385 ASP A CB  1 
ATOM   10618 C  CG  . ASP A 1 1385 ? -7.554   26.664  18.439  1.00 173.63 ? 1385 ASP A CG  1 
ATOM   10619 O  OD1 . ASP A 1 1385 ? -8.582   26.197  18.970  1.00 172.33 ? 1385 ASP A OD1 1 
ATOM   10620 O  OD2 . ASP A 1 1385 ? -6.637   25.940  18.001  1.00 175.08 ? 1385 ASP A OD2 1 
ATOM   10621 N  N   . ILE A 1 1386 ? -7.863   31.108  16.845  1.00 173.39 ? 1386 ILE A N   1 
ATOM   10622 C  CA  . ILE A 1 1386 ? -7.876   32.571  16.968  1.00 173.22 ? 1386 ILE A CA  1 
ATOM   10623 C  C   . ILE A 1 1386 ? -9.276   33.169  16.744  1.00 168.04 ? 1386 ILE A C   1 
ATOM   10624 O  O   . ILE A 1 1386 ? -10.168  33.068  17.590  1.00 164.60 ? 1386 ILE A O   1 
ATOM   10625 C  CB  . ILE A 1 1386 ? -6.867   33.235  15.974  1.00 237.97 ? 1386 ILE A CB  1 
ATOM   10626 C  CG1 . ILE A 1 1386 ? -5.657   32.326  15.719  1.00 240.10 ? 1386 ILE A CG1 1 
ATOM   10627 C  CG2 . ILE A 1 1386 ? -6.414   34.602  16.484  1.00 239.74 ? 1386 ILE A CG2 1 
ATOM   10628 C  CD1 . ILE A 1 1386 ? -4.660   32.893  14.719  1.00 241.83 ? 1386 ILE A CD1 1 
ATOM   10629 N  N   . TYR A 1 1399 ? -12.001  31.066  20.690  1.00 217.50 ? 1399 TYR A N   1 
ATOM   10630 C  CA  . TYR A 1 1399 ? -12.357  29.746  21.195  1.00 217.44 ? 1399 TYR A CA  1 
ATOM   10631 C  C   . TYR A 1 1399 ? -12.051  28.735  20.092  1.00 203.70 ? 1399 TYR A C   1 
ATOM   10632 O  O   . TYR A 1 1399 ? -11.078  27.989  20.184  1.00 204.62 ? 1399 TYR A O   1 
ATOM   10633 C  CB  . TYR A 1 1399 ? -13.836  29.728  21.618  1.00 229.30 ? 1399 TYR A CB  1 
ATOM   10634 C  CG  . TYR A 1 1399 ? -14.400  28.410  22.158  1.00 241.73 ? 1399 TYR A CG  1 
ATOM   10635 C  CD1 . TYR A 1 1399 ? -13.725  27.669  23.132  1.00 248.91 ? 1399 TYR A CD1 1 
ATOM   10636 C  CD2 . TYR A 1 1399 ? -15.642  27.932  21.717  1.00 244.05 ? 1399 TYR A CD2 1 
ATOM   10637 C  CE1 . TYR A 1 1399 ? -14.262  26.470  23.627  1.00 251.58 ? 1399 TYR A CE1 1 
ATOM   10638 C  CE2 . TYR A 1 1399 ? -16.184  26.741  22.206  1.00 246.45 ? 1399 TYR A CE2 1 
ATOM   10639 C  CZ  . TYR A 1 1399 ? -15.492  26.017  23.158  1.00 249.97 ? 1399 TYR A CZ  1 
ATOM   10640 O  OH  . TYR A 1 1399 ? -16.032  24.842  23.638  1.00 250.16 ? 1399 TYR A OH  1 
ATOM   10641 N  N   . LYS A 1 1400 ? -12.871  28.732  19.044  1.00 187.46 ? 1400 LYS A N   1 
ATOM   10642 C  CA  . LYS A 1 1400 ? -12.599  27.975  17.823  1.00 172.04 ? 1400 LYS A CA  1 
ATOM   10643 C  C   . LYS A 1 1400 ? -13.498  28.481  16.688  1.00 156.64 ? 1400 LYS A C   1 
ATOM   10644 O  O   . LYS A 1 1400 ? -14.609  28.963  16.924  1.00 153.26 ? 1400 LYS A O   1 
ATOM   10645 C  CB  . LYS A 1 1400 ? -12.713  26.453  18.034  1.00 168.54 ? 1400 LYS A CB  1 
ATOM   10646 C  CG  . LYS A 1 1400 ? -13.762  26.000  19.060  1.00 165.34 ? 1400 LYS A CG  1 
ATOM   10647 C  CD  . LYS A 1 1400 ? -14.100  24.497  18.955  1.00 163.04 ? 1400 LYS A CD  1 
ATOM   10648 C  CE  . LYS A 1 1400 ? -12.992  23.579  19.495  1.00 164.60 ? 1400 LYS A CE  1 
ATOM   10649 N  NZ  . LYS A 1 1400 ? -13.405  22.136  19.528  1.00 162.95 ? 1400 LYS A NZ  1 
ATOM   10650 N  N   . ARG A 1 1401 ? -13.004  28.379  15.457  1.00 147.37 ? 1401 ARG A N   1 
ATOM   10651 C  CA  . ARG A 1 1401 ? -13.693  28.937  14.282  1.00 135.19 ? 1401 ARG A CA  1 
ATOM   10652 C  C   . ARG A 1 1401 ? -13.349  28.215  12.956  1.00 133.96 ? 1401 ARG A C   1 
ATOM   10653 O  O   . ARG A 1 1401 ? -12.198  27.791  12.754  1.00 136.74 ? 1401 ARG A O   1 
ATOM   10654 C  CB  . ARG A 1 1401 ? -13.330  30.409  14.156  1.00 126.27 ? 1401 ARG A CB  1 
ATOM   10655 C  CG  . ARG A 1 1401 ? -13.287  30.904  12.739  1.00 118.30 ? 1401 ARG A CG  1 
ATOM   10656 C  CD  . ARG A 1 1401 ? -12.010  31.659  12.461  1.00 116.43 ? 1401 ARG A CD  1 
ATOM   10657 N  NE  . ARG A 1 1401 ? -12.308  33.021  12.031  1.00 113.70 ? 1401 ARG A NE  1 
ATOM   10658 C  CZ  . ARG A 1 1401 ? -11.492  33.796  11.322  1.00 113.27 ? 1401 ARG A CZ  1 
ATOM   10659 N  NH1 . ARG A 1 1401 ? -10.309  33.352  10.928  1.00 114.56 ? 1401 ARG A NH1 1 
ATOM   10660 N  NH2 . ARG A 1 1401 ? -11.876  35.020  10.995  1.00 112.27 ? 1401 ARG A NH2 1 
ATOM   10661 N  N   . ILE A 1 1402 ? -14.332  28.091  12.057  1.00 129.47 ? 1402 ILE A N   1 
ATOM   10662 C  CA  . ILE A 1 1402 ? -14.110  27.425  10.768  1.00 125.23 ? 1402 ILE A CA  1 
ATOM   10663 C  C   . ILE A 1 1402 ? -13.772  28.347  9.607   1.00 126.15 ? 1402 ILE A C   1 
ATOM   10664 O  O   . ILE A 1 1402 ? -14.432  29.357  9.391   1.00 124.33 ? 1402 ILE A O   1 
ATOM   10665 C  CB  . ILE A 1 1402 ? -15.327  26.652  10.318  1.00 118.87 ? 1402 ILE A CB  1 
ATOM   10666 C  CG1 . ILE A 1 1402 ? -15.695  25.603  11.351  1.00 116.86 ? 1402 ILE A CG1 1 
ATOM   10667 C  CG2 . ILE A 1 1402 ? -15.034  26.012  8.996   1.00 117.80 ? 1402 ILE A CG2 1 
ATOM   10668 C  CD1 . ILE A 1 1402 ? -16.866  24.776  10.947  1.00 114.09 ? 1402 ILE A CD1 1 
ATOM   10669 N  N   . VAL A 1 1403 ? -12.768  27.967  8.832   1.00 129.73 ? 1403 VAL A N   1 
ATOM   10670 C  CA  . VAL A 1 1403 ? -12.369  28.759  7.682   1.00 133.77 ? 1403 VAL A CA  1 
ATOM   10671 C  C   . VAL A 1 1403 ? -12.396  27.898  6.420   1.00 137.92 ? 1403 VAL A C   1 
ATOM   10672 O  O   . VAL A 1 1403 ? -11.423  27.199  6.091   1.00 140.74 ? 1403 VAL A O   1 
ATOM   10673 C  CB  . VAL A 1 1403 ? -10.967  29.377  7.871   1.00 136.44 ? 1403 VAL A CB  1 
ATOM   10674 C  CG1 . VAL A 1 1403 ? -10.443  29.931  6.557   1.00 137.46 ? 1403 VAL A CG1 1 
ATOM   10675 C  CG2 . VAL A 1 1403 ? -10.999  30.467  8.923   1.00 137.28 ? 1403 VAL A CG2 1 
ATOM   10676 N  N   . ALA A 1 1404 ? -13.536  27.950  5.731   1.00 136.75 ? 1404 ALA A N   1 
ATOM   10677 C  CA  . ALA A 1 1404 ? -13.746  27.209  4.492   1.00 135.88 ? 1404 ALA A CA  1 
ATOM   10678 C  C   . ALA A 1 1404 ? -13.513  28.095  3.274   1.00 136.35 ? 1404 ALA A C   1 
ATOM   10679 O  O   . ALA A 1 1404 ? -13.939  29.256  3.241   1.00 133.28 ? 1404 ALA A O   1 
ATOM   10680 C  CB  . ALA A 1 1404 ? -15.144  26.616  4.455   1.00 131.18 ? 1404 ALA A CB  1 
ATOM   10681 N  N   . CYS A 1 1405 ? -12.834  27.530  2.278   1.00 139.89 ? 1405 CYS A N   1 
ATOM   10682 C  CA  . CYS A 1 1405 ? -12.537  28.236  1.043   1.00 141.55 ? 1405 CYS A CA  1 
ATOM   10683 C  C   . CYS A 1 1405 ? -12.841  27.364  -0.149  1.00 140.35 ? 1405 CYS A C   1 
ATOM   10684 O  O   . CYS A 1 1405 ? -13.078  26.154  -0.016  1.00 142.10 ? 1405 CYS A O   1 
ATOM   10685 C  CB  . CYS A 1 1405 ? -11.068  28.621  0.980   1.00 144.50 ? 1405 CYS A CB  1 
ATOM   10686 S  SG  . CYS A 1 1405 ? -10.373  28.993  2.556   1.00 163.61 ? 1405 CYS A SG  1 
ATOM   10687 N  N   . ALA A 1 1406 ? -12.806  27.994  -1.320  1.00 138.57 ? 1406 ALA A N   1 
ATOM   10688 C  CA  . ALA A 1 1406 ? -13.013  27.304  -2.588  1.00 135.43 ? 1406 ALA A CA  1 
ATOM   10689 C  C   . ALA A 1 1406 ? -12.461  28.130  -3.754  1.00 138.79 ? 1406 ALA A C   1 
ATOM   10690 O  O   . ALA A 1 1406 ? -12.345  29.356  -3.663  1.00 137.48 ? 1406 ALA A O   1 
ATOM   10691 C  CB  . ALA A 1 1406 ? -14.503  27.029  -2.806  1.00 130.00 ? 1406 ALA A CB  1 
ATOM   10692 N  N   . SER A 1 1407 ? -12.112  27.454  -4.843  1.00 141.36 ? 1407 SER A N   1 
ATOM   10693 C  CA  . SER A 1 1407 ? -11.899  28.127  -6.110  1.00 142.82 ? 1407 SER A CA  1 
ATOM   10694 C  C   . SER A 1 1407 ? -12.538  27.281  -7.181  1.00 143.14 ? 1407 SER A C   1 
ATOM   10695 O  O   . SER A 1 1407 ? -12.614  26.057  -7.052  1.00 144.62 ? 1407 SER A O   1 
ATOM   10696 C  CB  . SER A 1 1407 ? -10.426  28.287  -6.417  1.00 144.05 ? 1407 SER A CB  1 
ATOM   10697 O  OG  . SER A 1 1407 ? -10.270  28.623  -7.781  1.00 143.19 ? 1407 SER A OG  1 
ATOM   10698 N  N   . TYR A 1 1408 ? -13.023  27.930  -8.231  1.00 140.68 ? 1408 TYR A N   1 
ATOM   10699 C  CA  . TYR A 1 1408 ? -13.687  27.200  -9.297  1.00 138.34 ? 1408 TYR A CA  1 
ATOM   10700 C  C   . TYR A 1 1408 ? -12.667  26.721  -10.313 1.00 138.94 ? 1408 TYR A C   1 
ATOM   10701 O  O   . TYR A 1 1408 ? -11.885  27.522  -10.825 1.00 141.82 ? 1408 TYR A O   1 
ATOM   10702 C  CB  . TYR A 1 1408 ? -14.749  28.058  -9.978  1.00 138.06 ? 1408 TYR A CB  1 
ATOM   10703 C  CG  . TYR A 1 1408 ? -15.392  27.345  -11.125 1.00 140.26 ? 1408 TYR A CG  1 
ATOM   10704 C  CD1 . TYR A 1 1408 ? -15.661  25.990  -11.038 1.00 141.54 ? 1408 TYR A CD1 1 
ATOM   10705 C  CD2 . TYR A 1 1408 ? -15.725  28.016  -12.291 1.00 142.10 ? 1408 TYR A CD2 1 
ATOM   10706 C  CE1 . TYR A 1 1408 ? -16.232  25.316  -12.073 1.00 143.39 ? 1408 TYR A CE1 1 
ATOM   10707 C  CE2 . TYR A 1 1408 ? -16.306  27.352  -13.338 1.00 144.06 ? 1408 TYR A CE2 1 
ATOM   10708 C  CZ  . TYR A 1 1408 ? -16.557  25.992  -13.226 1.00 145.27 ? 1408 TYR A CZ  1 
ATOM   10709 O  OH  . TYR A 1 1408 ? -17.135  25.292  -14.268 1.00 146.63 ? 1408 TYR A OH  1 
ATOM   10710 N  N   . LYS A 1 1409 ? -12.663  25.415  -10.588 1.00 137.28 ? 1409 LYS A N   1 
ATOM   10711 C  CA  . LYS A 1 1409 ? -11.791  24.842  -11.619 1.00 137.42 ? 1409 LYS A CA  1 
ATOM   10712 C  C   . LYS A 1 1409 ? -12.498  24.953  -12.976 1.00 141.02 ? 1409 LYS A C   1 
ATOM   10713 O  O   . LYS A 1 1409 ? -13.470  24.237  -13.219 1.00 140.00 ? 1409 LYS A O   1 
ATOM   10714 C  CB  . LYS A 1 1409 ? -11.493  23.360  -11.330 1.00 133.06 ? 1409 LYS A CB  1 
ATOM   10715 C  CG  . LYS A 1 1409 ? -10.957  23.026  -9.949  1.00 128.44 ? 1409 LYS A CG  1 
ATOM   10716 C  CD  . LYS A 1 1409 ? -10.862  21.510  -9.717  1.00 125.44 ? 1409 LYS A CD  1 
ATOM   10717 C  CE  . LYS A 1 1409 ? -9.598   20.914  -10.323 1.00 127.79 ? 1409 LYS A CE  1 
ATOM   10718 N  NZ  . LYS A 1 1409 ? -9.394   19.458  -10.037 1.00 128.28 ? 1409 LYS A NZ  1 
ATOM   10719 N  N   . PRO A 1 1410 ? -12.040  25.855  -13.862 1.00 144.72 ? 1410 PRO A N   1 
ATOM   10720 C  CA  . PRO A 1 1410 ? -12.766  25.953  -15.130 1.00 148.12 ? 1410 PRO A CA  1 
ATOM   10721 C  C   . PRO A 1 1410 ? -12.610  24.714  -16.000 1.00 156.67 ? 1410 PRO A C   1 
ATOM   10722 O  O   . PRO A 1 1410 ? -11.534  24.120  -16.078 1.00 157.74 ? 1410 PRO A O   1 
ATOM   10723 C  CB  . PRO A 1 1410 ? -12.142  27.184  -15.794 1.00 146.48 ? 1410 PRO A CB  1 
ATOM   10724 C  CG  . PRO A 1 1410 ? -11.712  28.003  -14.658 1.00 145.61 ? 1410 PRO A CG  1 
ATOM   10725 C  CD  . PRO A 1 1410 ? -11.136  26.998  -13.687 1.00 146.61 ? 1410 PRO A CD  1 
ATOM   10726 N  N   . SER A 1 1411 ? -13.715  24.316  -16.616 1.00 164.80 ? 1411 SER A N   1 
ATOM   10727 C  CA  . SER A 1 1411 ? -13.720  23.212  -17.548 1.00 177.31 ? 1411 SER A CA  1 
ATOM   10728 C  C   . SER A 1 1411 ? -13.121  23.742  -18.828 1.00 191.18 ? 1411 SER A C   1 
ATOM   10729 O  O   . SER A 1 1411 ? -13.186  24.941  -19.092 1.00 191.71 ? 1411 SER A O   1 
ATOM   10730 C  CB  . SER A 1 1411 ? -15.150  22.734  -17.795 1.00 176.05 ? 1411 SER A CB  1 
ATOM   10731 O  OG  . SER A 1 1411 ? -15.892  22.655  -16.584 1.00 174.89 ? 1411 SER A OG  1 
ATOM   10732 N  N   . ARG A 1 1412 ? -12.528  22.855  -19.616 1.00 204.55 ? 1412 ARG A N   1 
ATOM   10733 C  CA  . ARG A 1 1412 ? -11.930  23.247  -20.880 1.00 218.63 ? 1412 ARG A CA  1 
ATOM   10734 C  C   . ARG A 1 1412 ? -12.923  24.095  -21.663 1.00 216.87 ? 1412 ARG A C   1 
ATOM   10735 O  O   . ARG A 1 1412 ? -14.133  23.892  -21.556 1.00 216.27 ? 1412 ARG A O   1 
ATOM   10736 C  CB  . ARG A 1 1412 ? -11.554  22.006  -21.689 1.00 232.35 ? 1412 ARG A CB  1 
ATOM   10737 C  CG  . ARG A 1 1412 ? -12.750  21.130  -22.041 1.00 242.31 ? 1412 ARG A CG  1 
ATOM   10738 C  CD  . ARG A 1 1412 ? -12.436  20.150  -23.166 1.00 253.94 ? 1412 ARG A CD  1 
ATOM   10739 N  NE  . ARG A 1 1412 ? -13.653  19.738  -23.861 1.00 260.20 ? 1412 ARG A NE  1 
ATOM   10740 C  CZ  . ARG A 1 1412 ? -13.679  18.905  -24.894 1.00 266.81 ? 1412 ARG A CZ  1 
ATOM   10741 N  NH1 . ARG A 1 1412 ? -12.548  18.386  -25.356 1.00 271.09 ? 1412 ARG A NH1 1 
ATOM   10742 N  NH2 . ARG A 1 1412 ? -14.838  18.593  -25.463 1.00 267.28 ? 1412 ARG A NH2 1 
ATOM   10743 N  N   . GLU A 1 1413 ? -12.407  25.038  -22.447 1.00 215.85 ? 1413 GLU A N   1 
ATOM   10744 C  CA  . GLU A 1 1413 ? -13.245  25.926  -23.249 1.00 212.23 ? 1413 GLU A CA  1 
ATOM   10745 C  C   . GLU A 1 1413 ? -13.836  27.053  -22.407 1.00 196.47 ? 1413 GLU A C   1 
ATOM   10746 O  O   . GLU A 1 1413 ? -14.362  28.025  -22.946 1.00 193.83 ? 1413 GLU A O   1 
ATOM   10747 C  CB  . GLU A 1 1413 ? -14.390  25.151  -23.916 1.00 221.48 ? 1413 GLU A CB  1 
ATOM   10748 C  CG  . GLU A 1 1413 ? -13.961  23.919  -24.700 1.00 232.11 ? 1413 GLU A CG  1 
ATOM   10749 C  CD  . GLU A 1 1413 ? -13.471  24.250  -26.096 1.00 240.68 ? 1413 GLU A CD  1 
ATOM   10750 O  OE1 . GLU A 1 1413 ? -14.035  25.172  -26.720 1.00 242.88 ? 1413 GLU A OE1 1 
ATOM   10751 O  OE2 . GLU A 1 1413 ? -12.529  23.582  -26.574 1.00 244.56 ? 1413 GLU A OE2 1 
ATOM   10752 N  N   . GLU A 1 1414 ? -13.754  26.921  -21.086 1.00 183.21 ? 1414 GLU A N   1 
ATOM   10753 C  CA  . GLU A 1 1414 ? -14.430  27.858  -20.196 1.00 166.92 ? 1414 GLU A CA  1 
ATOM   10754 C  C   . GLU A 1 1414 ? -13.680  29.145  -19.908 1.00 161.01 ? 1414 GLU A C   1 
ATOM   10755 O  O   . GLU A 1 1414 ? -12.463  29.192  -19.912 1.00 162.00 ? 1414 GLU A O   1 
ATOM   10756 C  CB  . GLU A 1 1414 ? -14.816  27.185  -18.884 1.00 157.63 ? 1414 GLU A CB  1 
ATOM   10757 C  CG  . GLU A 1 1414 ? -16.297  26.919  -18.750 1.00 147.51 ? 1414 GLU A CG  1 
ATOM   10758 C  CD  . GLU A 1 1414 ? -16.604  25.980  -17.605 1.00 140.79 ? 1414 GLU A CD  1 
ATOM   10759 O  OE1 . GLU A 1 1414 ? -15.684  25.652  -16.836 1.00 139.44 ? 1414 GLU A OE1 1 
ATOM   10760 O  OE2 . GLU A 1 1414 ? -17.765  25.555  -17.477 1.00 137.71 ? 1414 GLU A OE2 1 
ATOM   10761 N  N   . SER A 1 1415 ? -14.450  30.185  -19.634 1.00 155.04 ? 1415 SER A N   1 
ATOM   10762 C  CA  . SER A 1 1415 ? -13.934  31.504  -19.299 1.00 153.25 ? 1415 SER A CA  1 
ATOM   10763 C  C   . SER A 1 1415 ? -13.307  31.590  -17.898 1.00 153.15 ? 1415 SER A C   1 
ATOM   10764 O  O   . SER A 1 1415 ? -13.714  30.900  -16.968 1.00 153.31 ? 1415 SER A O   1 
ATOM   10765 C  CB  . SER A 1 1415 ? -15.073  32.512  -19.438 1.00 150.08 ? 1415 SER A CB  1 
ATOM   10766 O  OG  . SER A 1 1415 ? -14.906  33.613  -18.583 1.00 149.21 ? 1415 SER A OG  1 
ATOM   10767 N  N   . SER A 1 1416 ? -12.323  32.464  -17.746 1.00 154.16 ? 1416 SER A N   1 
ATOM   10768 C  CA  . SER A 1 1416 ? -11.602  32.607  -16.477 1.00 155.54 ? 1416 SER A CA  1 
ATOM   10769 C  C   . SER A 1 1416 ? -12.346  33.364  -15.370 1.00 153.79 ? 1416 SER A C   1 
ATOM   10770 O  O   . SER A 1 1416 ? -11.773  33.633  -14.312 1.00 153.20 ? 1416 SER A O   1 
ATOM   10771 C  CB  . SER A 1 1416 ? -10.249  33.285  -16.718 1.00 158.74 ? 1416 SER A CB  1 
ATOM   10772 O  OG  . SER A 1 1416 ? -10.396  34.475  -17.476 1.00 159.32 ? 1416 SER A OG  1 
ATOM   10773 N  N   . SER A 1 1417 ? -13.607  33.710  -15.618 1.00 153.47 ? 1417 SER A N   1 
ATOM   10774 C  CA  . SER A 1 1417 ? -14.353  34.602  -14.725 1.00 151.97 ? 1417 SER A CA  1 
ATOM   10775 C  C   . SER A 1 1417 ? -14.739  33.927  -13.417 1.00 148.88 ? 1417 SER A C   1 
ATOM   10776 O  O   . SER A 1 1417 ? -14.915  34.581  -12.383 1.00 152.74 ? 1417 SER A O   1 
ATOM   10777 C  CB  . SER A 1 1417 ? -15.612  35.123  -15.419 1.00 151.40 ? 1417 SER A CB  1 
ATOM   10778 O  OG  . SER A 1 1417 ? -16.417  34.050  -15.873 1.00 150.27 ? 1417 SER A OG  1 
ATOM   10779 N  N   . GLY A 1 1418 ? -14.875  32.608  -13.473 1.00 140.54 ? 1418 GLY A N   1 
ATOM   10780 C  CA  . GLY A 1 1418 ? -15.331  31.849  -12.325 1.00 133.20 ? 1418 GLY A CA  1 
ATOM   10781 C  C   . GLY A 1 1418 ? -16.787  31.436  -12.415 1.00 129.05 ? 1418 GLY A C   1 
ATOM   10782 O  O   . GLY A 1 1418 ? -17.484  31.760  -13.371 1.00 125.91 ? 1418 GLY A O   1 
ATOM   10783 N  N   . SER A 1 1419 ? -17.255  30.739  -11.392 1.00 127.22 ? 1419 SER A N   1 
ATOM   10784 C  CA  . SER A 1 1419 ? -18.515  30.037  -11.479 1.00 123.06 ? 1419 SER A CA  1 
ATOM   10785 C  C   . SER A 1 1419 ? -19.780  30.861  -11.652 1.00 115.52 ? 1419 SER A C   1 
ATOM   10786 O  O   . SER A 1 1419 ? -19.764  32.093  -11.662 1.00 115.55 ? 1419 SER A O   1 
ATOM   10787 C  CB  . SER A 1 1419 ? -18.694  29.125  -10.287 1.00 122.60 ? 1419 SER A CB  1 
ATOM   10788 O  OG  . SER A 1 1419 ? -19.908  28.430  -10.443 1.00 120.18 ? 1419 SER A OG  1 
ATOM   10789 N  N   . SER A 1 1420 ? -20.871  30.122  -11.835 1.00 109.14 ? 1420 SER A N   1 
ATOM   10790 C  CA  . SER A 1 1420 ? -22.228  30.651  -11.869 1.00 104.23 ? 1420 SER A CA  1 
ATOM   10791 C  C   . SER A 1 1420 ? -22.781  30.617  -10.466 1.00 104.26 ? 1420 SER A C   1 
ATOM   10792 O  O   . SER A 1 1420 ? -22.126  30.138  -9.549  1.00 107.38 ? 1420 SER A O   1 
ATOM   10793 C  CB  . SER A 1 1420 ? -23.144  29.765  -12.712 1.00 99.99  ? 1420 SER A CB  1 
ATOM   10794 O  OG  . SER A 1 1420 ? -23.876  28.863  -11.879 1.00 96.54  ? 1420 SER A OG  1 
ATOM   10795 N  N   . HIS A 1 1421 ? -24.006  31.089  -10.302 1.00 101.06 ? 1421 HIS A N   1 
ATOM   10796 C  CA  . HIS A 1 1421 ? -24.622  31.047  -8.995  1.00 97.65  ? 1421 HIS A CA  1 
ATOM   10797 C  C   . HIS A 1 1421 ? -24.382  29.677  -8.384  1.00 91.97  ? 1421 HIS A C   1 
ATOM   10798 O  O   . HIS A 1 1421 ? -24.757  28.655  -8.966  1.00 88.05  ? 1421 HIS A O   1 
ATOM   10799 C  CB  . HIS A 1 1421 ? -26.107  31.430  -9.118  1.00 99.91  ? 1421 HIS A CB  1 
ATOM   10800 C  CG  . HIS A 1 1421 ? -26.994  30.830  -8.077  1.00 99.05  ? 1421 HIS A CG  1 
ATOM   10801 N  ND1 . HIS A 1 1421 ? -28.336  30.609  -8.293  1.00 97.64  ? 1421 HIS A ND1 1 
ATOM   10802 C  CD2 . HIS A 1 1421 ? -26.736  30.391  -6.825  1.00 98.85  ? 1421 HIS A CD2 1 
ATOM   10803 C  CE1 . HIS A 1 1421 ? -28.866  30.060  -7.218  1.00 97.75  ? 1421 HIS A CE1 1 
ATOM   10804 N  NE2 . HIS A 1 1421 ? -27.915  29.918  -6.313  1.00 98.20  ? 1421 HIS A NE2 1 
ATOM   10805 N  N   . ALA A 1 1422 ? -23.717  29.676  -7.228  1.00 90.73  ? 1422 ALA A N   1 
ATOM   10806 C  CA  . ALA A 1 1422 ? -23.317  28.428  -6.574  1.00 94.35  ? 1422 ALA A CA  1 
ATOM   10807 C  C   . ALA A 1 1422 ? -23.480  28.460  -5.068  1.00 97.15  ? 1422 ALA A C   1 
ATOM   10808 O  O   . ALA A 1 1422 ? -23.621  29.528  -4.471  1.00 95.73  ? 1422 ALA A O   1 
ATOM   10809 C  CB  . ALA A 1 1422 ? -21.905  28.081  -6.903  1.00 94.13  ? 1422 ALA A CB  1 
ATOM   10810 N  N   . VAL A 1 1423 ? -23.456  27.274  -4.463  1.00 100.27 ? 1423 VAL A N   1 
ATOM   10811 C  CA  . VAL A 1 1423 ? -23.615  27.157  -3.026  1.00 102.60 ? 1423 VAL A CA  1 
ATOM   10812 C  C   . VAL A 1 1423 ? -22.471  26.352  -2.456  1.00 105.38 ? 1423 VAL A C   1 
ATOM   10813 O  O   . VAL A 1 1423 ? -21.924  25.497  -3.161  1.00 108.65 ? 1423 VAL A O   1 
ATOM   10814 C  CB  . VAL A 1 1423 ? -24.931  26.478  -2.620  1.00 83.45  ? 1423 VAL A CB  1 
ATOM   10815 C  CG1 . VAL A 1 1423 ? -25.964  26.649  -3.684  1.00 83.28  ? 1423 VAL A CG1 1 
ATOM   10816 C  CG2 . VAL A 1 1423 ? -24.719  25.033  -2.282  1.00 83.63  ? 1423 VAL A CG2 1 
ATOM   10817 N  N   . MET A 1 1424 ? -22.069  26.713  -1.221  1.00 105.38 ? 1424 MET A N   1 
ATOM   10818 C  CA  . MET A 1 1424 ? -21.180  25.933  -0.340  1.00 101.39 ? 1424 MET A CA  1 
ATOM   10819 C  C   . MET A 1 1424 ? -22.032  25.378  0.806   1.00 102.39 ? 1424 MET A C   1 
ATOM   10820 O  O   . MET A 1 1424 ? -22.943  26.055  1.304   1.00 102.83 ? 1424 MET A O   1 
ATOM   10821 C  CB  . MET A 1 1424 ? -20.061  26.809  0.207   1.00 94.82  ? 1424 MET A CB  1 
ATOM   10822 C  CG  . MET A 1 1424 ? -19.781  27.982  -0.691  1.00 93.35  ? 1424 MET A CG  1 
ATOM   10823 S  SD  . MET A 1 1424 ? -18.433  29.063  -0.172  1.00 99.94  ? 1424 MET A SD  1 
ATOM   10824 C  CE  . MET A 1 1424 ? -17.205  27.900  0.388   1.00 94.46  ? 1424 MET A CE  1 
ATOM   10825 N  N   . ASP A 1 1425 ? -21.749  24.148  1.218   1.00 105.13 ? 1425 ASP A N   1 
ATOM   10826 C  CA  . ASP A 1 1425 ? -22.617  23.451  2.154   1.00 106.40 ? 1425 ASP A CA  1 
ATOM   10827 C  C   . ASP A 1 1425 ? -21.734  22.734  3.165   1.00 110.52 ? 1425 ASP A C   1 
ATOM   10828 O  O   . ASP A 1 1425 ? -21.156  21.678  2.857   1.00 112.84 ? 1425 ASP A O   1 
ATOM   10829 C  CB  . ASP A 1 1425 ? -23.486  22.458  1.378   1.00 107.53 ? 1425 ASP A CB  1 
ATOM   10830 C  CG  . ASP A 1 1425 ? -24.261  21.498  2.272   1.00 110.41 ? 1425 ASP A CG  1 
ATOM   10831 O  OD1 . ASP A 1 1425 ? -25.271  20.927  1.796   1.00 110.15 ? 1425 ASP A OD1 1 
ATOM   10832 O  OD2 . ASP A 1 1425 ? -23.865  21.288  3.432   1.00 112.71 ? 1425 ASP A OD2 1 
ATOM   10833 N  N   . ILE A 1 1426 ? -21.633  23.323  4.363   1.00 108.56 ? 1426 ILE A N   1 
ATOM   10834 C  CA  . ILE A 1 1426 ? -20.897  22.737  5.470   1.00 105.41 ? 1426 ILE A CA  1 
ATOM   10835 C  C   . ILE A 1 1426 ? -21.780  22.004  6.470   1.00 102.40 ? 1426 ILE A C   1 
ATOM   10836 O  O   . ILE A 1 1426 ? -22.610  22.605  7.142   1.00 99.56  ? 1426 ILE A O   1 
ATOM   10837 C  CB  . ILE A 1 1426 ? -20.157  23.792  6.221   1.00 105.11 ? 1426 ILE A CB  1 
ATOM   10838 C  CG1 . ILE A 1 1426 ? -19.597  24.797  5.235   1.00 103.86 ? 1426 ILE A CG1 1 
ATOM   10839 C  CG2 . ILE A 1 1426 ? -19.071  23.140  7.067   1.00 107.25 ? 1426 ILE A CG2 1 
ATOM   10840 C  CD1 . ILE A 1 1426 ? -18.360  25.455  5.725   1.00 106.04 ? 1426 ILE A CD1 1 
ATOM   10841 N  N   . SER A 1 1427 ? -21.594  20.692  6.527   1.00 103.11 ? 1427 SER A N   1 
ATOM   10842 C  CA  . SER A 1 1427 ? -22.146  19.829  7.558   1.00 101.31 ? 1427 SER A CA  1 
ATOM   10843 C  C   . SER A 1 1427 ? -21.388  20.207  8.836   1.00 101.40 ? 1427 SER A C   1 
ATOM   10844 O  O   . SER A 1 1427 ? -20.154  20.364  8.806   1.00 102.87 ? 1427 SER A O   1 
ATOM   10845 C  CB  . SER A 1 1427 ? -21.926  18.351  7.126   1.00 92.77  ? 1427 SER A CB  1 
ATOM   10846 O  OG  . SER A 1 1427 ? -22.095  17.361  8.141   1.00 92.64  ? 1427 SER A OG  1 
ATOM   10847 N  N   . LEU A 1 1428 ? -22.114  20.413  9.936   1.00 97.99  ? 1428 LEU A N   1 
ATOM   10848 C  CA  . LEU A 1 1428 ? -21.464  20.652  11.227  1.00 98.24  ? 1428 LEU A CA  1 
ATOM   10849 C  C   . LEU A 1 1428 ? -21.366  19.337  11.957  1.00 99.44  ? 1428 LEU A C   1 
ATOM   10850 O  O   . LEU A 1 1428 ? -22.301  18.522  11.863  1.00 97.54  ? 1428 LEU A O   1 
ATOM   10851 C  CB  . LEU A 1 1428 ? -22.235  21.662  12.072  1.00 93.59  ? 1428 LEU A CB  1 
ATOM   10852 C  CG  . LEU A 1 1428 ? -22.320  22.994  11.327  1.00 91.36  ? 1428 LEU A CG  1 
ATOM   10853 C  CD1 . LEU A 1 1428 ? -23.248  23.959  12.030  1.00 89.91  ? 1428 LEU A CD1 1 
ATOM   10854 C  CD2 . LEU A 1 1428 ? -20.930  23.589  11.133  1.00 90.03  ? 1428 LEU A CD2 1 
ATOM   10855 N  N   . PRO A 1 1429 ? -20.216  19.104  12.643  1.00 100.41 ? 1429 PRO A N   1 
ATOM   10856 C  CA  . PRO A 1 1429 ? -19.974  17.896  13.446  1.00 99.72  ? 1429 PRO A CA  1 
ATOM   10857 C  C   . PRO A 1 1429 ? -20.940  17.821  14.600  1.00 98.74  ? 1429 PRO A C   1 
ATOM   10858 O  O   . PRO A 1 1429 ? -21.474  18.847  15.025  1.00 96.17  ? 1429 PRO A O   1 
ATOM   10859 C  CB  . PRO A 1 1429 ? -18.542  18.069  13.935  1.00 100.36 ? 1429 PRO A CB  1 
ATOM   10860 C  CG  . PRO A 1 1429 ? -17.923  18.900  12.902  1.00 101.24 ? 1429 PRO A CG  1 
ATOM   10861 C  CD  . PRO A 1 1429 ? -18.975  19.868  12.450  1.00 99.61  ? 1429 PRO A CD  1 
ATOM   10862 N  N   . THR A 1 1430 ? -21.183  16.609  15.071  1.00 100.39 ? 1430 THR A N   1 
ATOM   10863 C  CA  . THR A 1 1430 ? -22.316  16.362  15.938  1.00 100.65 ? 1430 THR A CA  1 
ATOM   10864 C  C   . THR A 1 1430 ? -22.202  17.246  17.183  1.00 105.04 ? 1430 THR A C   1 
ATOM   10865 O  O   . THR A 1 1430 ? -21.200  17.195  17.916  1.00 109.22 ? 1430 THR A O   1 
ATOM   10866 C  CB  . THR A 1 1430 ? -22.433  14.857  16.260  1.00 99.14  ? 1430 THR A CB  1 
ATOM   10867 O  OG1 . THR A 1 1430 ? -21.846  14.101  15.194  1.00 99.23  ? 1430 THR A OG1 1 
ATOM   10868 C  CG2 . THR A 1 1430 ? -23.878  14.430  16.404  1.00 95.77  ? 1430 THR A CG2 1 
ATOM   10869 N  N   . GLY A 1 1431 ? -23.221  18.089  17.375  1.00 104.53 ? 1431 GLY A N   1 
ATOM   10870 C  CA  . GLY A 1 1431 ? -23.243  19.082  18.442  1.00 105.19 ? 1431 GLY A CA  1 
ATOM   10871 C  C   . GLY A 1 1431 ? -22.127  20.126  18.413  1.00 108.17 ? 1431 GLY A C   1 
ATOM   10872 O  O   . GLY A 1 1431 ? -21.195  20.045  19.192  1.00 105.31 ? 1431 GLY A O   1 
ATOM   10873 N  N   . ILE A 1 1432 ? -22.237  21.107  17.519  1.00 111.40 ? 1432 ILE A N   1 
ATOM   10874 C  CA  . ILE A 1 1432 ? -21.228  22.138  17.329  1.00 115.85 ? 1432 ILE A CA  1 
ATOM   10875 C  C   . ILE A 1 1432 ? -21.869  23.320  16.625  1.00 115.98 ? 1432 ILE A C   1 
ATOM   10876 O  O   . ILE A 1 1432 ? -21.488  23.638  15.514  1.00 119.18 ? 1432 ILE A O   1 
ATOM   10877 C  CB  . ILE A 1 1432 ? -20.107  21.656  16.365  1.00 99.92  ? 1432 ILE A CB  1 
ATOM   10878 C  CG1 . ILE A 1 1432 ? -19.597  20.250  16.746  1.00 105.41 ? 1432 ILE A CG1 1 
ATOM   10879 C  CG2 . ILE A 1 1432 ? -18.990  22.695  16.260  1.00 98.27  ? 1432 ILE A CG2 1 
ATOM   10880 C  CD1 . ILE A 1 1432 ? -18.528  20.189  17.851  1.00 110.74 ? 1432 ILE A CD1 1 
ATOM   10881 N  N   . SER A 1 1433 ? -22.850  23.962  17.252  1.00 114.50 ? 1433 SER A N   1 
ATOM   10882 C  CA  . SER A 1 1433 ? -23.589  25.101  16.655  1.00 112.61 ? 1433 SER A CA  1 
ATOM   10883 C  C   . SER A 1 1433 ? -22.713  26.138  15.937  1.00 112.51 ? 1433 SER A C   1 
ATOM   10884 O  O   . SER A 1 1433 ? -21.620  26.460  16.399  1.00 113.23 ? 1433 SER A O   1 
ATOM   10885 C  CB  . SER A 1 1433 ? -24.389  25.853  17.740  1.00 114.22 ? 1433 SER A CB  1 
ATOM   10886 O  OG  . SER A 1 1433 ? -25.110  24.979  18.604  1.00 114.92 ? 1433 SER A OG  1 
ATOM   10887 N  N   . ALA A 1 1434 ? -23.186  26.685  14.824  1.00 111.89 ? 1434 ALA A N   1 
ATOM   10888 C  CA  . ALA A 1 1434 ? -22.401  27.709  14.147  1.00 115.73 ? 1434 ALA A CA  1 
ATOM   10889 C  C   . ALA A 1 1434 ? -22.807  29.065  14.640  1.00 116.46 ? 1434 ALA A C   1 
ATOM   10890 O  O   . ALA A 1 1434 ? -23.807  29.185  15.336  1.00 116.93 ? 1434 ALA A O   1 
ATOM   10891 C  CB  . ALA A 1 1434 ? -22.585  27.626  12.663  1.00 117.30 ? 1434 ALA A CB  1 
ATOM   10892 N  N   . ASN A 1 1435 ? -22.042  30.089  14.273  1.00 117.08 ? 1435 ASN A N   1 
ATOM   10893 C  CA  . ASN A 1 1435 ? -22.265  31.438  14.814  1.00 118.03 ? 1435 ASN A CA  1 
ATOM   10894 C  C   . ASN A 1 1435 ? -23.219  32.325  14.009  1.00 115.15 ? 1435 ASN A C   1 
ATOM   10895 O  O   . ASN A 1 1435 ? -22.789  33.232  13.298  1.00 114.26 ? 1435 ASN A O   1 
ATOM   10896 C  CB  . ASN A 1 1435 ? -20.930  32.164  15.032  1.00 120.45 ? 1435 ASN A CB  1 
ATOM   10897 C  CG  . ASN A 1 1435 ? -21.095  33.450  15.803  1.00 122.11 ? 1435 ASN A CG  1 
ATOM   10898 O  OD1 . ASN A 1 1435 ? -22.210  33.890  16.049  1.00 120.85 ? 1435 ASN A OD1 1 
ATOM   10899 N  ND2 . ASN A 1 1435 ? -19.984  34.058  16.195  1.00 125.68 ? 1435 ASN A ND2 1 
ATOM   10900 N  N   . GLU A 1 1436 ? -24.514  32.085  14.159  1.00 116.19 ? 1436 GLU A N   1 
ATOM   10901 C  CA  . GLU A 1 1436 ? -25.503  32.769  13.350  1.00 117.07 ? 1436 GLU A CA  1 
ATOM   10902 C  C   . GLU A 1 1436 ? -25.074  34.192  13.016  1.00 116.73 ? 1436 GLU A C   1 
ATOM   10903 O  O   . GLU A 1 1436 ? -25.158  34.625  11.883  1.00 116.88 ? 1436 GLU A O   1 
ATOM   10904 C  CB  . GLU A 1 1436 ? -26.849  32.776  14.068  1.00 119.84 ? 1436 GLU A CB  1 
ATOM   10905 C  CG  . GLU A 1 1436 ? -28.018  33.260  13.210  1.00 122.02 ? 1436 GLU A CG  1 
ATOM   10906 C  CD  . GLU A 1 1436 ? -28.932  32.122  12.723  1.00 123.16 ? 1436 GLU A CD  1 
ATOM   10907 O  OE1 . GLU A 1 1436 ? -28.507  30.936  12.789  1.00 125.15 ? 1436 GLU A OE1 1 
ATOM   10908 O  OE2 . GLU A 1 1436 ? -30.077  32.423  12.285  1.00 120.69 ? 1436 GLU A OE2 1 
ATOM   10909 N  N   . GLU A 1 1437 ? -24.586  34.915  14.011  1.00 118.70 ? 1437 GLU A N   1 
ATOM   10910 C  CA  . GLU A 1 1437 ? -24.281  36.341  13.848  1.00 117.37 ? 1437 GLU A CA  1 
ATOM   10911 C  C   . GLU A 1 1437 ? -23.117  36.523  12.894  1.00 120.24 ? 1437 GLU A C   1 
ATOM   10912 O  O   . GLU A 1 1437 ? -23.141  37.418  12.058  1.00 120.35 ? 1437 GLU A O   1 
ATOM   10913 C  CB  . GLU A 1 1437 ? -23.975  37.029  15.199  1.00 120.46 ? 1437 GLU A CB  1 
ATOM   10914 C  CG  . GLU A 1 1437 ? -24.556  36.303  16.447  1.00 165.05 ? 1437 GLU A CG  1 
ATOM   10915 C  CD  . GLU A 1 1437 ? -26.088  36.359  16.554  1.00 159.19 ? 1437 GLU A CD  1 
ATOM   10916 O  OE1 . GLU A 1 1437 ? -26.637  37.447  16.257  1.00 157.30 ? 1437 GLU A OE1 1 
ATOM   10917 O  OE2 . GLU A 1 1437 ? -26.726  35.332  16.944  1.00 155.14 ? 1437 GLU A OE2 1 
ATOM   10918 N  N   . ASP A 1 1438 ? -22.104  35.672  13.011  1.00 121.14 ? 1438 ASP A N   1 
ATOM   10919 C  CA  . ASP A 1 1438 ? -20.947  35.759  12.131  1.00 122.91 ? 1438 ASP A CA  1 
ATOM   10920 C  C   . ASP A 1 1438 ? -21.377  35.732  10.671  1.00 119.96 ? 1438 ASP A C   1 
ATOM   10921 O  O   . ASP A 1 1438 ? -20.858  36.496  9.858   1.00 120.56 ? 1438 ASP A O   1 
ATOM   10922 C  CB  . ASP A 1 1438 ? -19.984  34.597  12.392  1.00 125.92 ? 1438 ASP A CB  1 
ATOM   10923 C  CG  . ASP A 1 1438 ? -19.106  34.822  13.605  1.00 128.13 ? 1438 ASP A CG  1 
ATOM   10924 O  OD1 . ASP A 1 1438 ? -19.041  35.975  14.068  1.00 128.72 ? 1438 ASP A OD1 1 
ATOM   10925 O  OD2 . ASP A 1 1438 ? -18.479  33.849  14.090  1.00 128.81 ? 1438 ASP A OD2 1 
ATOM   10926 N  N   . LEU A 1 1439 ? -22.319  34.836  10.362  1.00 114.04 ? 1439 LEU A N   1 
ATOM   10927 C  CA  . LEU A 1 1439 ? -22.798  34.583  9.004   1.00 108.52 ? 1439 LEU A CA  1 
ATOM   10928 C  C   . LEU A 1 1439 ? -23.672  35.723  8.508   1.00 106.05 ? 1439 LEU A C   1 
ATOM   10929 O  O   . LEU A 1 1439 ? -23.520  36.190  7.383   1.00 105.84 ? 1439 LEU A O   1 
ATOM   10930 C  CB  . LEU A 1 1439 ? -23.577  33.267  8.953   1.00 103.78 ? 1439 LEU A CB  1 
ATOM   10931 C  CG  . LEU A 1 1439 ? -22.826  31.999  9.355   1.00 102.33 ? 1439 LEU A CG  1 
ATOM   10932 C  CD1 . LEU A 1 1439 ? -23.780  30.841  9.548   1.00 100.89 ? 1439 LEU A CD1 1 
ATOM   10933 C  CD2 . LEU A 1 1439 ? -21.803  31.652  8.310   1.00 102.30 ? 1439 LEU A CD2 1 
ATOM   10934 N  N   . LYS A 1 1440 ? -24.589  36.162  9.364   1.00 105.85 ? 1440 LYS A N   1 
ATOM   10935 C  CA  . LYS A 1 1440 ? -25.380  37.356  9.111   1.00 107.37 ? 1440 LYS A CA  1 
ATOM   10936 C  C   . LYS A 1 1440 ? -24.422  38.435  8.666   1.00 106.29 ? 1440 LYS A C   1 
ATOM   10937 O  O   . LYS A 1 1440 ? -24.739  39.247  7.806   1.00 104.50 ? 1440 LYS A O   1 
ATOM   10938 C  CB  . LYS A 1 1440 ? -26.073  37.838  10.391  1.00 112.61 ? 1440 LYS A CB  1 
ATOM   10939 C  CG  . LYS A 1 1440 ? -27.273  37.029  10.894  1.00 117.76 ? 1440 LYS A CG  1 
ATOM   10940 C  CD  . LYS A 1 1440 ? -28.584  37.425  10.194  1.00 122.37 ? 1440 LYS A CD  1 
ATOM   10941 C  CE  . LYS A 1 1440 ? -29.765  37.673  11.164  1.00 128.31 ? 1440 LYS A CE  1 
ATOM   10942 N  NZ  . LYS A 1 1440 ? -29.921  36.719  12.311  1.00 130.18 ? 1440 LYS A NZ  1 
ATOM   10943 N  N   . ALA A 1 1441 ? -23.242  38.435  9.277   1.00 109.96 ? 1441 ALA A N   1 
ATOM   10944 C  CA  . ALA A 1 1441 ? -22.222  39.445  9.031   1.00 113.24 ? 1441 ALA A CA  1 
ATOM   10945 C  C   . ALA A 1 1441 ? -21.795  39.434  7.587   1.00 117.73 ? 1441 ALA A C   1 
ATOM   10946 O  O   . ALA A 1 1441 ? -21.492  40.479  7.014   1.00 119.72 ? 1441 ALA A O   1 
ATOM   10947 C  CB  . ALA A 1 1441 ? -21.012  39.190  9.912   1.00 114.77 ? 1441 ALA A CB  1 
ATOM   10948 N  N   . LEU A 1 1442 ? -21.759  38.242  7.005   1.00 118.71 ? 1442 LEU A N   1 
ATOM   10949 C  CA  . LEU A 1 1442 ? -21.206  38.075  5.680   1.00 120.20 ? 1442 LEU A CA  1 
ATOM   10950 C  C   . LEU A 1 1442 ? -22.151  38.509  4.586   1.00 126.21 ? 1442 LEU A C   1 
ATOM   10951 O  O   . LEU A 1 1442 ? -21.735  39.194  3.659   1.00 130.51 ? 1442 LEU A O   1 
ATOM   10952 C  CB  . LEU A 1 1442 ? -20.792  36.639  5.485   1.00 116.48 ? 1442 LEU A CB  1 
ATOM   10953 C  CG  . LEU A 1 1442 ? -19.469  36.552  6.213   1.00 116.82 ? 1442 LEU A CG  1 
ATOM   10954 C  CD1 . LEU A 1 1442 ? -19.154  35.123  6.564   1.00 116.81 ? 1442 LEU A CD1 1 
ATOM   10955 C  CD2 . LEU A 1 1442 ? -18.391  37.179  5.347   1.00 118.37 ? 1442 LEU A CD2 1 
ATOM   10956 N  N   . VAL A 1 1443 ? -23.422  38.134  4.701   1.00 125.30 ? 1443 VAL A N   1 
ATOM   10957 C  CA  . VAL A 1 1443 ? -24.403  38.412  3.650   1.00 127.02 ? 1443 VAL A CA  1 
ATOM   10958 C  C   . VAL A 1 1443 ? -25.094  39.776  3.767   1.00 127.30 ? 1443 VAL A C   1 
ATOM   10959 O  O   . VAL A 1 1443 ? -25.630  40.290  2.793   1.00 127.40 ? 1443 VAL A O   1 
ATOM   10960 C  CB  . VAL A 1 1443 ? -25.495  37.322  3.613   1.00 126.27 ? 1443 VAL A CB  1 
ATOM   10961 C  CG1 . VAL A 1 1443 ? -25.063  36.118  4.423   1.00 127.69 ? 1443 VAL A CG1 1 
ATOM   10962 C  CG2 . VAL A 1 1443 ? -26.808  37.857  4.154   1.00 125.87 ? 1443 VAL A CG2 1 
ATOM   10963 N  N   . GLU A 1 1444 ? -25.072  40.362  4.956   1.00 130.83 ? 1444 GLU A N   1 
ATOM   10964 C  CA  . GLU A 1 1444 ? -26.000  41.428  5.288   1.00 133.49 ? 1444 GLU A CA  1 
ATOM   10965 C  C   . GLU A 1 1444 ? -25.464  42.806  4.985   1.00 131.68 ? 1444 GLU A C   1 
ATOM   10966 O  O   . GLU A 1 1444 ? -26.076  43.805  5.352   1.00 129.38 ? 1444 GLU A O   1 
ATOM   10967 C  CB  . GLU A 1 1444 ? -26.357  41.323  6.763   1.00 141.45 ? 1444 GLU A CB  1 
ATOM   10968 C  CG  . GLU A 1 1444 ? -27.529  42.159  7.215   1.00 148.04 ? 1444 GLU A CG  1 
ATOM   10969 C  CD  . GLU A 1 1444 ? -28.186  41.573  8.460   1.00 152.66 ? 1444 GLU A CD  1 
ATOM   10970 O  OE1 . GLU A 1 1444 ? -28.468  40.347  8.455   1.00 153.02 ? 1444 GLU A OE1 1 
ATOM   10971 O  OE2 . GLU A 1 1444 ? -28.419  42.332  9.437   1.00 154.92 ? 1444 GLU A OE2 1 
ATOM   10972 N  N   . GLY A 1 1445 ? -24.326  42.868  4.308   1.00 134.41 ? 1445 GLY A N   1 
ATOM   10973 C  CA  . GLY A 1 1445 ? -23.671  44.144  4.105   1.00 138.19 ? 1445 GLY A CA  1 
ATOM   10974 C  C   . GLY A 1 1445 ? -23.300  44.448  2.671   1.00 140.31 ? 1445 GLY A C   1 
ATOM   10975 O  O   . GLY A 1 1445 ? -23.086  43.544  1.877   1.00 140.90 ? 1445 GLY A O   1 
ATOM   10976 N  N   . VAL A 1 1446 ? -23.228  45.733  2.338   1.00 140.76 ? 1446 VAL A N   1 
ATOM   10977 C  CA  . VAL A 1 1446 ? -22.830  46.157  0.998   1.00 141.14 ? 1446 VAL A CA  1 
ATOM   10978 C  C   . VAL A 1 1446 ? -21.544  45.472  0.568   1.00 140.77 ? 1446 VAL A C   1 
ATOM   10979 O  O   . VAL A 1 1446 ? -21.279  45.304  -0.616  1.00 139.99 ? 1446 VAL A O   1 
ATOM   10980 C  CB  . VAL A 1 1446 ? -22.587  47.675  0.929   1.00 143.95 ? 1446 VAL A CB  1 
ATOM   10981 C  CG1 . VAL A 1 1446 ? -22.353  48.104  -0.518  1.00 144.99 ? 1446 VAL A CG1 1 
ATOM   10982 C  CG2 . VAL A 1 1446 ? -23.744  48.437  1.549   1.00 142.62 ? 1446 VAL A CG2 1 
ATOM   10983 N  N   . ASP A 1 1447 ? -20.731  45.102  1.544   1.00 141.51 ? 1447 ASP A N   1 
ATOM   10984 C  CA  . ASP A 1 1447 ? -19.529  44.348  1.266   1.00 144.12 ? 1447 ASP A CA  1 
ATOM   10985 C  C   . ASP A 1 1447 ? -19.882  42.873  1.137   1.00 141.60 ? 1447 ASP A C   1 
ATOM   10986 O  O   . ASP A 1 1447 ? -19.013  42.006  1.216   1.00 142.25 ? 1447 ASP A O   1 
ATOM   10987 C  CB  . ASP A 1 1447 ? -18.475  44.570  2.361   1.00 148.68 ? 1447 ASP A CB  1 
ATOM   10988 C  CG  . ASP A 1 1447 ? -18.992  44.252  3.764   1.00 150.57 ? 1447 ASP A CG  1 
ATOM   10989 O  OD1 . ASP A 1 1447 ? -20.232  44.163  3.943   1.00 148.54 ? 1447 ASP A OD1 1 
ATOM   10990 O  OD2 . ASP A 1 1447 ? -18.148  44.100  4.686   1.00 153.17 ? 1447 ASP A OD2 1 
ATOM   10991 N  N   . GLN A 1 1448 ? -21.161  42.589  0.922   1.00 138.41 ? 1448 GLN A N   1 
ATOM   10992 C  CA  . GLN A 1 1448 ? -21.625  41.215  1.017   1.00 136.01 ? 1448 GLN A CA  1 
ATOM   10993 C  C   . GLN A 1 1448 ? -20.713  40.281  0.269   1.00 135.40 ? 1448 GLN A C   1 
ATOM   10994 O  O   . GLN A 1 1448 ? -20.477  40.450  -0.916  1.00 136.39 ? 1448 GLN A O   1 
ATOM   10995 C  CB  . GLN A 1 1448 ? -23.073  41.048  0.558   1.00 134.60 ? 1448 GLN A CB  1 
ATOM   10996 C  CG  . GLN A 1 1448 ? -23.360  41.333  -0.889  1.00 135.78 ? 1448 GLN A CG  1 
ATOM   10997 C  CD  . GLN A 1 1448 ? -24.777  40.921  -1.274  1.00 135.78 ? 1448 GLN A CD  1 
ATOM   10998 O  OE1 . GLN A 1 1448 ? -25.225  39.816  -0.949  1.00 134.99 ? 1448 GLN A OE1 1 
ATOM   10999 N  NE2 . GLN A 1 1448 ? -25.491  41.811  -1.965  1.00 135.84 ? 1448 GLN A NE2 1 
ATOM   11000 N  N   . LEU A 1 1449 ? -20.177  39.315  1.002   1.00 135.60 ? 1449 LEU A N   1 
ATOM   11001 C  CA  . LEU A 1 1449 ? -19.348  38.258  0.446   1.00 137.43 ? 1449 LEU A CA  1 
ATOM   11002 C  C   . LEU A 1 1449 ? -20.260  37.143  -0.044  1.00 131.73 ? 1449 LEU A C   1 
ATOM   11003 O  O   . LEU A 1 1449 ? -20.086  36.613  -1.142  1.00 130.24 ? 1449 LEU A O   1 
ATOM   11004 C  CB  . LEU A 1 1449 ? -18.377  37.750  1.515   1.00 144.09 ? 1449 LEU A CB  1 
ATOM   11005 C  CG  . LEU A 1 1449 ? -17.517  36.515  1.253   1.00 149.88 ? 1449 LEU A CG  1 
ATOM   11006 C  CD1 . LEU A 1 1449 ? -16.853  36.604  -0.122  1.00 152.18 ? 1449 LEU A CD1 1 
ATOM   11007 C  CD2 . LEU A 1 1449 ? -16.491  36.331  2.385   1.00 153.07 ? 1449 LEU A CD2 1 
ATOM   11008 N  N   . PHE A 1 1450 ? -21.234  36.791  0.786   1.00 127.24 ? 1450 PHE A N   1 
ATOM   11009 C  CA  . PHE A 1 1450 ? -22.268  35.860  0.382   1.00 123.51 ? 1450 PHE A CA  1 
ATOM   11010 C  C   . PHE A 1 1450 ? -23.577  36.610  0.219   1.00 122.22 ? 1450 PHE A C   1 
ATOM   11011 O  O   . PHE A 1 1450 ? -23.659  37.801  0.526   1.00 122.73 ? 1450 PHE A O   1 
ATOM   11012 C  CB  . PHE A 1 1450 ? -22.380  34.724  1.384   1.00 121.54 ? 1450 PHE A CB  1 
ATOM   11013 C  CG  . PHE A 1 1450 ? -21.100  33.996  1.572   1.00 121.98 ? 1450 PHE A CG  1 
ATOM   11014 C  CD1 . PHE A 1 1450 ? -20.088  34.537  2.348   1.00 124.68 ? 1450 PHE A CD1 1 
ATOM   11015 C  CD2 . PHE A 1 1450 ? -20.874  32.798  0.946   1.00 121.27 ? 1450 PHE A CD2 1 
ATOM   11016 C  CE1 . PHE A 1 1450 ? -18.871  33.871  2.521   1.00 125.19 ? 1450 PHE A CE1 1 
ATOM   11017 C  CE2 . PHE A 1 1450 ? -19.667  32.137  1.111   1.00 122.73 ? 1450 PHE A CE2 1 
ATOM   11018 C  CZ  . PHE A 1 1450 ? -18.668  32.676  1.901   1.00 124.44 ? 1450 PHE A CZ  1 
ATOM   11019 N  N   . THR A 1 1451 ? -24.595  35.923  -0.282  1.00 118.43 ? 1451 THR A N   1 
ATOM   11020 C  CA  . THR A 1 1451 ? -25.849  36.576  -0.580  1.00 113.98 ? 1451 THR A CA  1 
ATOM   11021 C  C   . THR A 1 1451 ? -26.896  35.831  0.190   1.00 112.03 ? 1451 THR A C   1 
ATOM   11022 O  O   . THR A 1 1451 ? -28.048  36.267  0.276   1.00 110.67 ? 1451 THR A O   1 
ATOM   11023 C  CB  . THR A 1 1451 ? -26.199  36.487  -2.080  1.00 110.92 ? 1451 THR A CB  1 
ATOM   11024 O  OG1 . THR A 1 1451 ? -26.931  35.278  -2.335  1.00 108.98 ? 1451 THR A OG1 1 
ATOM   11025 C  CG2 . THR A 1 1451 ? -24.936  36.527  -2.948  1.00 112.01 ? 1451 THR A CG2 1 
ATOM   11026 N  N   . ASP A 1 1452 ? -26.503  34.698  0.758   1.00 112.00 ? 1452 ASP A N   1 
ATOM   11027 C  CA  . ASP A 1 1452 ? -27.487  33.923  1.477   1.00 111.08 ? 1452 ASP A CA  1 
ATOM   11028 C  C   . ASP A 1 1452 ? -26.987  32.738  2.294   1.00 113.29 ? 1452 ASP A C   1 
ATOM   11029 O  O   . ASP A 1 1452 ? -26.534  31.727  1.751   1.00 113.39 ? 1452 ASP A O   1 
ATOM   11030 C  CB  . ASP A 1 1452 ? -28.573  33.453  0.528   1.00 105.68 ? 1452 ASP A CB  1 
ATOM   11031 C  CG  . ASP A 1 1452 ? -29.849  33.226  1.234   1.00 99.77  ? 1452 ASP A CG  1 
ATOM   11032 O  OD1 . ASP A 1 1452 ? -30.213  32.052  1.439   1.00 99.60  ? 1452 ASP A OD1 1 
ATOM   11033 O  OD2 . ASP A 1 1452 ? -30.457  34.231  1.626   1.00 95.75  ? 1452 ASP A OD2 1 
ATOM   11034 N  N   . TYR A 1 1453 ? -27.126  32.881  3.611   1.00 114.96 ? 1453 TYR A N   1 
ATOM   11035 C  CA  . TYR A 1 1453 ? -26.821  31.832  4.576   1.00 115.31 ? 1453 TYR A CA  1 
ATOM   11036 C  C   . TYR A 1 1453 ? -28.098  31.195  5.132   1.00 113.36 ? 1453 TYR A C   1 
ATOM   11037 O  O   . TYR A 1 1453 ? -29.185  31.764  5.039   1.00 112.84 ? 1453 TYR A O   1 
ATOM   11038 C  CB  . TYR A 1 1453 ? -25.970  32.400  5.727   1.00 116.25 ? 1453 TYR A CB  1 
ATOM   11039 C  CG  . TYR A 1 1453 ? -26.787  32.884  6.885   1.00 116.17 ? 1453 TYR A CG  1 
ATOM   11040 C  CD1 . TYR A 1 1453 ? -27.510  34.046  6.785   1.00 118.22 ? 1453 TYR A CD1 1 
ATOM   11041 C  CD2 . TYR A 1 1453 ? -26.866  32.162  8.061   1.00 117.12 ? 1453 TYR A CD2 1 
ATOM   11042 C  CE1 . TYR A 1 1453 ? -28.295  34.497  7.829   1.00 119.04 ? 1453 TYR A CE1 1 
ATOM   11043 C  CE2 . TYR A 1 1453 ? -27.647  32.601  9.115   1.00 118.22 ? 1453 TYR A CE2 1 
ATOM   11044 C  CZ  . TYR A 1 1453 ? -28.365  33.781  8.996   1.00 117.55 ? 1453 TYR A CZ  1 
ATOM   11045 O  OH  . TYR A 1 1453 ? -29.159  34.262  10.023  1.00 114.01 ? 1453 TYR A OH  1 
ATOM   11046 N  N   . GLN A 1 1454 ? -27.954  30.009  5.707   1.00 113.92 ? 1454 GLN A N   1 
ATOM   11047 C  CA  . GLN A 1 1454 ? -29.045  29.359  6.416   1.00 112.22 ? 1454 GLN A CA  1 
ATOM   11048 C  C   . GLN A 1 1454 ? -28.550  28.097  7.124   1.00 112.74 ? 1454 GLN A C   1 
ATOM   11049 O  O   . GLN A 1 1454 ? -27.782  27.328  6.551   1.00 112.59 ? 1454 GLN A O   1 
ATOM   11050 C  CB  . GLN A 1 1454 ? -30.154  29.003  5.443   1.00 112.13 ? 1454 GLN A CB  1 
ATOM   11051 C  CG  . GLN A 1 1454 ? -29.683  28.286  4.207   1.00 113.82 ? 1454 GLN A CG  1 
ATOM   11052 C  CD  . GLN A 1 1454 ? -30.842  27.667  3.447   1.00 114.94 ? 1454 GLN A CD  1 
ATOM   11053 O  OE1 . GLN A 1 1454 ? -31.770  27.113  4.050   1.00 114.39 ? 1454 GLN A OE1 1 
ATOM   11054 N  NE2 . GLN A 1 1454 ? -30.802  27.761  2.116   1.00 116.06 ? 1454 GLN A NE2 1 
ATOM   11055 N  N   . ILE A 1 1455 ? -28.952  27.901  8.381   1.00 111.12 ? 1455 ILE A N   1 
ATOM   11056 C  CA  . ILE A 1 1455 ? -28.626  26.655  9.077   1.00 110.44 ? 1455 ILE A CA  1 
ATOM   11057 C  C   . ILE A 1 1455 ? -29.829  25.742  9.126   1.00 108.28 ? 1455 ILE A C   1 
ATOM   11058 O  O   . ILE A 1 1455 ? -30.650  25.839  10.040  1.00 106.85 ? 1455 ILE A O   1 
ATOM   11059 C  CB  . ILE A 1 1455 ? -28.126  26.845  10.540  1.00 118.45 ? 1455 ILE A CB  1 
ATOM   11060 C  CG1 . ILE A 1 1455 ? -26.735  27.489  10.586  1.00 120.00 ? 1455 ILE A CG1 1 
ATOM   11061 C  CG2 . ILE A 1 1455 ? -28.052  25.490  11.248  1.00 118.56 ? 1455 ILE A CG2 1 
ATOM   11062 C  CD1 . ILE A 1 1455 ? -26.756  28.996  10.562  1.00 119.96 ? 1455 ILE A CD1 1 
ATOM   11063 N  N   . LYS A 1 1456 ? -29.931  24.865  8.132   1.00 109.20 ? 1456 LYS A N   1 
ATOM   11064 C  CA  . LYS A 1 1456 ? -30.913  23.795  8.152   1.00 108.27 ? 1456 LYS A CA  1 
ATOM   11065 C  C   . LYS A 1 1456 ? -30.270  22.470  8.527   1.00 104.69 ? 1456 LYS A C   1 
ATOM   11066 O  O   . LYS A 1 1456 ? -29.149  22.157  8.123   1.00 103.48 ? 1456 LYS A O   1 
ATOM   11067 C  CB  . LYS A 1 1456 ? -31.634  23.667  6.814   1.00 111.98 ? 1456 LYS A CB  1 
ATOM   11068 C  CG  . LYS A 1 1456 ? -32.764  22.658  6.865   1.00 117.19 ? 1456 LYS A CG  1 
ATOM   11069 C  CD  . LYS A 1 1456 ? -33.529  22.554  5.544   1.00 121.26 ? 1456 LYS A CD  1 
ATOM   11070 C  CE  . LYS A 1 1456 ? -35.018  22.198  5.756   1.00 122.66 ? 1456 LYS A CE  1 
ATOM   11071 N  NZ  . LYS A 1 1456 ? -35.821  23.331  6.372   1.00 122.57 ? 1456 LYS A NZ  1 
ATOM   11072 N  N   . ASP A 1 1457 ? -30.990  21.714  9.337   1.00 103.81 ? 1457 ASP A N   1 
ATOM   11073 C  CA  . ASP A 1 1457 ? -30.610  20.352  9.668   1.00 105.17 ? 1457 ASP A CA  1 
ATOM   11074 C  C   . ASP A 1 1457 ? -29.111  20.082  9.783   1.00 103.43 ? 1457 ASP A C   1 
ATOM   11075 O  O   . ASP A 1 1457 ? -28.602  19.132  9.207   1.00 103.35 ? 1457 ASP A O   1 
ATOM   11076 C  CB  . ASP A 1 1457 ? -31.292  19.368  8.719   1.00 108.39 ? 1457 ASP A CB  1 
ATOM   11077 C  CG  . ASP A 1 1457 ? -32.785  19.327  8.938   1.00 111.62 ? 1457 ASP A CG  1 
ATOM   11078 O  OD1 . ASP A 1 1457 ? -33.206  19.741  10.043  1.00 114.13 ? 1457 ASP A OD1 1 
ATOM   11079 O  OD2 . ASP A 1 1457 ? -33.538  18.914  8.024   1.00 111.82 ? 1457 ASP A OD2 1 
ATOM   11080 N  N   . GLY A 1 1458 ? -28.414  20.897  10.561  1.00 101.58 ? 1458 GLY A N   1 
ATOM   11081 C  CA  . GLY A 1 1458 ? -27.046  20.580  10.902  1.00 99.47  ? 1458 GLY A CA  1 
ATOM   11082 C  C   . GLY A 1 1458 ? -26.095  20.964  9.799   1.00 97.91  ? 1458 GLY A C   1 
ATOM   11083 O  O   . GLY A 1 1458 ? -24.973  20.444  9.742   1.00 98.50  ? 1458 GLY A O   1 
ATOM   11084 N  N   . HIS A 1 1459 ? -26.538  21.881  8.937   1.00 95.29  ? 1459 HIS A N   1 
ATOM   11085 C  CA  . HIS A 1 1459 ? -25.746  22.310  7.789   1.00 95.77  ? 1459 HIS A CA  1 
ATOM   11086 C  C   . HIS A 1 1459 ? -25.790  23.822  7.666   1.00 93.02  ? 1459 HIS A C   1 
ATOM   11087 O  O   . HIS A 1 1459 ? -26.863  24.393  7.616   1.00 90.40  ? 1459 HIS A O   1 
ATOM   11088 C  CB  . HIS A 1 1459 ? -26.294  21.697  6.485   1.00 97.20  ? 1459 HIS A CB  1 
ATOM   11089 C  CG  . HIS A 1 1459 ? -26.210  20.195  6.415   1.00 101.83 ? 1459 HIS A CG  1 
ATOM   11090 N  ND1 . HIS A 1 1459 ? -25.112  19.526  5.916   1.00 105.19 ? 1459 HIS A ND1 1 
ATOM   11091 C  CD2 . HIS A 1 1459 ? -27.102  19.233  6.754   1.00 102.60 ? 1459 HIS A CD2 1 
ATOM   11092 C  CE1 . HIS A 1 1459 ? -25.325  18.222  5.966   1.00 105.17 ? 1459 HIS A CE1 1 
ATOM   11093 N  NE2 . HIS A 1 1459 ? -26.526  18.018  6.472   1.00 103.56 ? 1459 HIS A NE2 1 
ATOM   11094 N  N   . VAL A 1 1460 ? -24.637  24.478  7.630   1.00 94.99  ? 1460 VAL A N   1 
ATOM   11095 C  CA  . VAL A 1 1460 ? -24.597  25.878  7.218   1.00 97.05  ? 1460 VAL A CA  1 
ATOM   11096 C  C   . VAL A 1 1460 ? -24.564  25.888  5.698   1.00 101.36 ? 1460 VAL A C   1 
ATOM   11097 O  O   . VAL A 1 1460 ? -23.838  25.093  5.084   1.00 104.40 ? 1460 VAL A O   1 
ATOM   11098 C  CB  . VAL A 1 1460 ? -23.348  26.599  7.747   1.00 98.80  ? 1460 VAL A CB  1 
ATOM   11099 C  CG1 . VAL A 1 1460 ? -23.101  27.890  6.983   1.00 99.15  ? 1460 VAL A CG1 1 
ATOM   11100 C  CG2 . VAL A 1 1460 ? -23.505  26.878  9.226   1.00 99.36  ? 1460 VAL A CG2 1 
ATOM   11101 N  N   . ILE A 1 1461 ? -25.342  26.775  5.083   1.00 100.06 ? 1461 ILE A N   1 
ATOM   11102 C  CA  . ILE A 1 1461 ? -25.564  26.700  3.631   1.00 98.51  ? 1461 ILE A CA  1 
ATOM   11103 C  C   . ILE A 1 1461 ? -25.538  28.062  2.957   1.00 98.87  ? 1461 ILE A C   1 
ATOM   11104 O  O   . ILE A 1 1461 ? -26.512  28.836  2.994   1.00 97.33  ? 1461 ILE A O   1 
ATOM   11105 C  CB  . ILE A 1 1461 ? -26.892  25.991  3.298   1.00 92.67  ? 1461 ILE A CB  1 
ATOM   11106 C  CG1 . ILE A 1 1461 ? -26.655  24.493  3.195   1.00 92.37  ? 1461 ILE A CG1 1 
ATOM   11107 C  CG2 . ILE A 1 1461 ? -27.496  26.532  2.025   1.00 89.42  ? 1461 ILE A CG2 1 
ATOM   11108 C  CD1 . ILE A 1 1461 ? -27.928  23.684  3.394   1.00 91.50  ? 1461 ILE A CD1 1 
ATOM   11109 N  N   . LEU A 1 1462 ? -24.410  28.334  2.322   1.00 100.66 ? 1462 LEU A N   1 
ATOM   11110 C  CA  . LEU A 1 1462 ? -24.171  29.628  1.720   1.00 102.20 ? 1462 LEU A CA  1 
ATOM   11111 C  C   . LEU A 1 1462 ? -24.405  29.609  0.213   1.00 104.98 ? 1462 LEU A C   1 
ATOM   11112 O  O   . LEU A 1 1462 ? -24.254  28.573  -0.420  1.00 105.75 ? 1462 LEU A O   1 
ATOM   11113 C  CB  . LEU A 1 1462 ? -22.758  30.088  2.061   1.00 101.10 ? 1462 LEU A CB  1 
ATOM   11114 C  CG  . LEU A 1 1462 ? -22.572  30.311  3.561   1.00 86.92  ? 1462 LEU A CG  1 
ATOM   11115 C  CD1 . LEU A 1 1462 ? -21.188  30.806  3.874   1.00 89.03  ? 1462 LEU A CD1 1 
ATOM   11116 C  CD2 . LEU A 1 1462 ? -23.570  31.312  3.969   1.00 85.86  ? 1462 LEU A CD2 1 
ATOM   11117 N  N   . GLN A 1 1463 ? -24.770  30.760  -0.347  1.00 104.69 ? 1463 GLN A N   1 
ATOM   11118 C  CA  . GLN A 1 1463 ? -25.090  30.882  -1.760  1.00 102.41 ? 1463 GLN A CA  1 
ATOM   11119 C  C   . GLN A 1 1463 ? -24.574  32.228  -2.271  1.00 100.26 ? 1463 GLN A C   1 
ATOM   11120 O  O   . GLN A 1 1463 ? -24.874  33.263  -1.680  1.00 97.81  ? 1463 GLN A O   1 
ATOM   11121 C  CB  . GLN A 1 1463 ? -26.609  30.854  -1.952  1.00 102.67 ? 1463 GLN A CB  1 
ATOM   11122 C  CG  . GLN A 1 1463 ? -27.320  29.492  -2.074  1.00 103.81 ? 1463 GLN A CG  1 
ATOM   11123 C  CD  . GLN A 1 1463 ? -28.797  29.670  -2.496  1.00 105.61 ? 1463 GLN A CD  1 
ATOM   11124 O  OE1 . GLN A 1 1463 ? -29.583  28.725  -2.524  1.00 105.64 ? 1463 GLN A OE1 1 
ATOM   11125 N  NE2 . GLN A 1 1463 ? -29.164  30.902  -2.830  1.00 107.09 ? 1463 GLN A NE2 1 
ATOM   11126 N  N   . LEU A 1 1464 ? -23.813  32.216  -3.367  1.00 101.03 ? 1464 LEU A N   1 
ATOM   11127 C  CA  . LEU A 1 1464 ? -23.390  33.442  -4.058  1.00 101.50 ? 1464 LEU A CA  1 
ATOM   11128 C  C   . LEU A 1 1464 ? -23.399  33.242  -5.569  1.00 103.63 ? 1464 LEU A C   1 
ATOM   11129 O  O   . LEU A 1 1464 ? -23.515  32.117  -6.062  1.00 101.11 ? 1464 LEU A O   1 
ATOM   11130 C  CB  . LEU A 1 1464 ? -21.994  33.911  -3.618  1.00 103.16 ? 1464 LEU A CB  1 
ATOM   11131 C  CG  . LEU A 1 1464 ? -20.934  33.020  -2.920  1.00 101.18 ? 1464 LEU A CG  1 
ATOM   11132 C  CD1 . LEU A 1 1464 ? -21.071  31.497  -3.092  1.00 99.53  ? 1464 LEU A CD1 1 
ATOM   11133 C  CD2 . LEU A 1 1464 ? -19.546  33.473  -3.336  1.00 103.51 ? 1464 LEU A CD2 1 
ATOM   11134 N  N   . ASN A 1 1465 ? -23.269  34.342  -6.302  1.00 108.27 ? 1465 ASN A N   1 
ATOM   11135 C  CA  . ASN A 1 1465 ? -23.322  34.309  -7.775  1.00 112.17 ? 1465 ASN A CA  1 
ATOM   11136 C  C   . ASN A 1 1465 ? -22.107  33.701  -8.504  1.00 114.80 ? 1465 ASN A C   1 
ATOM   11137 O  O   . ASN A 1 1465 ? -22.187  33.427  -9.695  1.00 114.09 ? 1465 ASN A O   1 
ATOM   11138 C  CB  . ASN A 1 1465 ? -23.586  35.715  -8.361  1.00 113.96 ? 1465 ASN A CB  1 
ATOM   11139 C  CG  . ASN A 1 1465 ? -24.513  36.554  -7.504  1.00 113.10 ? 1465 ASN A CG  1 
ATOM   11140 O  OD1 . ASN A 1 1465 ? -25.627  36.887  -7.928  1.00 109.89 ? 1465 ASN A OD1 1 
ATOM   11141 N  ND2 . ASN A 1 1465 ? -24.055  36.910  -6.291  1.00 113.62 ? 1465 ASN A ND2 1 
ATOM   11142 N  N   . SER A 1 1466 ? -20.991  33.524  -7.798  1.00 118.29 ? 1466 SER A N   1 
ATOM   11143 C  CA  . SER A 1 1466 ? -19.746  33.054  -8.405  1.00 122.68 ? 1466 SER A CA  1 
ATOM   11144 C  C   . SER A 1 1466 ? -18.726  32.585  -7.376  1.00 122.56 ? 1466 SER A C   1 
ATOM   11145 O  O   . SER A 1 1466 ? -18.783  32.971  -6.211  1.00 120.29 ? 1466 SER A O   1 
ATOM   11146 C  CB  . SER A 1 1466 ? -19.113  34.165  -9.235  1.00 126.46 ? 1466 SER A CB  1 
ATOM   11147 O  OG  . SER A 1 1466 ? -17.796  33.800  -9.618  1.00 130.48 ? 1466 SER A OG  1 
ATOM   11148 N  N   . ILE A 1 1467 ? -17.773  31.773  -7.819  1.00 125.15 ? 1467 ILE A N   1 
ATOM   11149 C  CA  . ILE A 1 1467 ? -16.675  31.378  -6.951  1.00 128.72 ? 1467 ILE A CA  1 
ATOM   11150 C  C   . ILE A 1 1467 ? -15.321  31.572  -7.634  1.00 133.96 ? 1467 ILE A C   1 
ATOM   11151 O  O   . ILE A 1 1467 ? -14.551  30.628  -7.778  1.00 138.15 ? 1467 ILE A O   1 
ATOM   11152 C  CB  . ILE A 1 1467 ? -16.813  29.940  -6.475  1.00 124.31 ? 1467 ILE A CB  1 
ATOM   11153 C  CG1 . ILE A 1 1467 ? -18.162  29.714  -5.807  1.00 117.60 ? 1467 ILE A CG1 1 
ATOM   11154 C  CG2 . ILE A 1 1467 ? -15.710  29.592  -5.490  1.00 127.38 ? 1467 ILE A CG2 1 
ATOM   11155 C  CD1 . ILE A 1 1467 ? -18.243  28.376  -5.133  1.00 115.05 ? 1467 ILE A CD1 1 
ATOM   11156 N  N   . PRO A 1 1468 ? -15.013  32.825  -8.015  1.00 136.44 ? 1468 PRO A N   1 
ATOM   11157 C  CA  . PRO A 1 1468 ? -13.867  33.223  -8.837  1.00 137.41 ? 1468 PRO A CA  1 
ATOM   11158 C  C   . PRO A 1 1468 ? -12.773  32.167  -8.897  1.00 140.31 ? 1468 PRO A C   1 
ATOM   11159 O  O   . PRO A 1 1468 ? -12.492  31.513  -7.893  1.00 137.96 ? 1468 PRO A O   1 
ATOM   11160 C  CB  . PRO A 1 1468 ? -13.336  34.459  -8.092  1.00 137.41 ? 1468 PRO A CB  1 
ATOM   11161 C  CG  . PRO A 1 1468 ? -14.570  35.102  -7.540  1.00 134.97 ? 1468 PRO A CG  1 
ATOM   11162 C  CD  . PRO A 1 1468 ? -15.624  34.005  -7.376  1.00 134.19 ? 1468 PRO A CD  1 
ATOM   11163 N  N   . SER A 1 1469 ? -12.166  31.994  -10.066 1.00 143.44 ? 1469 SER A N   1 
ATOM   11164 C  CA  . SER A 1 1469 ? -11.036  31.093  -10.185 1.00 147.44 ? 1469 SER A CA  1 
ATOM   11165 C  C   . SER A 1 1469 ? -9.748   31.844  -9.942  1.00 151.28 ? 1469 SER A C   1 
ATOM   11166 O  O   . SER A 1 1469 ? -8.717   31.242  -9.652  1.00 155.56 ? 1469 SER A O   1 
ATOM   11167 C  CB  . SER A 1 1469 ? -11.014  30.453  -11.555 1.00 147.85 ? 1469 SER A CB  1 
ATOM   11168 O  OG  . SER A 1 1469 ? -12.208  29.735  -11.749 1.00 146.06 ? 1469 SER A OG  1 
ATOM   11169 N  N   . SER A 1 1470 ? -9.817   33.165  -10.058 1.00 149.19 ? 1470 SER A N   1 
ATOM   11170 C  CA  . SER A 1 1470 ? -8.658   34.019  -9.831  1.00 150.80 ? 1470 SER A CA  1 
ATOM   11171 C  C   . SER A 1 1470 ? -7.907   33.561  -8.601  1.00 149.37 ? 1470 SER A C   1 
ATOM   11172 O  O   . SER A 1 1470 ? -6.686   33.445  -8.598  1.00 152.64 ? 1470 SER A O   1 
ATOM   11173 C  CB  . SER A 1 1470 ? -9.101   35.470  -9.646  1.00 151.62 ? 1470 SER A CB  1 
ATOM   11174 O  OG  . SER A 1 1470 ? -10.072  35.579  -8.619  1.00 151.43 ? 1470 SER A OG  1 
ATOM   11175 N  N   . ASP A 1 1471 ? -8.662   33.295  -7.551  1.00 147.11 ? 1471 ASP A N   1 
ATOM   11176 C  CA  . ASP A 1 1471 ? -8.097   32.859  -6.290  1.00 147.42 ? 1471 ASP A CA  1 
ATOM   11177 C  C   . ASP A 1 1471 ? -9.188   32.135  -5.518  1.00 138.70 ? 1471 ASP A C   1 
ATOM   11178 O  O   . ASP A 1 1471 ? -10.140  31.628  -6.108  1.00 134.43 ? 1471 ASP A O   1 
ATOM   11179 C  CB  . ASP A 1 1471 ? -7.537   34.049  -5.497  1.00 154.70 ? 1471 ASP A CB  1 
ATOM   11180 C  CG  . ASP A 1 1471 ? -8.527   35.214  -5.394  1.00 158.28 ? 1471 ASP A CG  1 
ATOM   11181 O  OD1 . ASP A 1 1471 ? -8.067   36.376  -5.315  1.00 161.70 ? 1471 ASP A OD1 1 
ATOM   11182 O  OD2 . ASP A 1 1471 ? -9.762   34.978  -5.383  1.00 156.46 ? 1471 ASP A OD2 1 
ATOM   11183 N  N   . PHE A 1 1472 ? -9.042   32.075  -4.204  1.00 134.13 ? 1472 PHE A N   1 
ATOM   11184 C  CA  . PHE A 1 1472 ? -10.029  31.412  -3.385  1.00 126.87 ? 1472 PHE A CA  1 
ATOM   11185 C  C   . PHE A 1 1472 ? -11.070  32.350  -2.879  1.00 123.15 ? 1472 PHE A C   1 
ATOM   11186 O  O   . PHE A 1 1472 ? -10.911  33.572  -2.910  1.00 122.65 ? 1472 PHE A O   1 
ATOM   11187 C  CB  . PHE A 1 1472 ? -9.378   30.742  -2.204  1.00 127.15 ? 1472 PHE A CB  1 
ATOM   11188 C  CG  . PHE A 1 1472 ? -8.877   29.405  -2.515  1.00 127.89 ? 1472 PHE A CG  1 
ATOM   11189 C  CD1 . PHE A 1 1472 ? -7.870   29.240  -3.435  1.00 131.63 ? 1472 PHE A CD1 1 
ATOM   11190 C  CD2 . PHE A 1 1472 ? -9.426   28.302  -1.923  1.00 127.03 ? 1472 PHE A CD2 1 
ATOM   11191 C  CE1 . PHE A 1 1472 ? -7.398   27.986  -3.745  1.00 133.54 ? 1472 PHE A CE1 1 
ATOM   11192 C  CE2 . PHE A 1 1472 ? -8.964   27.047  -2.221  1.00 128.85 ? 1472 PHE A CE2 1 
ATOM   11193 C  CZ  . PHE A 1 1472 ? -7.945   26.886  -3.132  1.00 132.13 ? 1472 PHE A CZ  1 
ATOM   11194 N  N   . LEU A 1 1473 ? -12.140  31.754  -2.385  1.00 119.82 ? 1473 LEU A N   1 
ATOM   11195 C  CA  . LEU A 1 1473 ? -13.190  32.517  -1.762  1.00 118.82 ? 1473 LEU A CA  1 
ATOM   11196 C  C   . LEU A 1 1473 ? -13.485  31.842  -0.436  1.00 120.88 ? 1473 LEU A C   1 
ATOM   11197 O  O   . LEU A 1 1473 ? -13.755  30.634  -0.402  1.00 120.22 ? 1473 LEU A O   1 
ATOM   11198 C  CB  . LEU A 1 1473 ? -14.414  32.550  -2.654  1.00 113.28 ? 1473 LEU A CB  1 
ATOM   11199 C  CG  . LEU A 1 1473 ? -15.556  33.345  -2.056  1.00 111.56 ? 1473 LEU A CG  1 
ATOM   11200 C  CD1 . LEU A 1 1473 ? -16.127  34.311  -3.079  1.00 111.27 ? 1473 LEU A CD1 1 
ATOM   11201 C  CD2 . LEU A 1 1473 ? -16.630  32.418  -1.469  1.00 109.71 ? 1473 LEU A CD2 1 
ATOM   11202 N  N   . CYS A 1 1474 ? -13.424  32.626  0.649   1.00 122.09 ? 1474 CYS A N   1 
ATOM   11203 C  CA  . CYS A 1 1474 ? -13.458  32.066  1.995   1.00 119.76 ? 1474 CYS A CA  1 
ATOM   11204 C  C   . CYS A 1 1474 ? -14.568  32.596  2.855   1.00 119.70 ? 1474 CYS A C   1 
ATOM   11205 O  O   . CYS A 1 1474 ? -14.744  33.804  2.972   1.00 121.25 ? 1474 CYS A O   1 
ATOM   11206 C  CB  . CYS A 1 1474 ? -12.119  32.270  2.677   1.00 119.16 ? 1474 CYS A CB  1 
ATOM   11207 S  SG  . CYS A 1 1474 ? -11.058  30.882  2.288   1.00 131.86 ? 1474 CYS A SG  1 
ATOM   11208 N  N   . VAL A 1 1475 ? -15.351  31.679  3.414   1.00 120.08 ? 1475 VAL A N   1 
ATOM   11209 C  CA  . VAL A 1 1475 ? -16.265  32.011  4.494   1.00 120.87 ? 1475 VAL A CA  1 
ATOM   11210 C  C   . VAL A 1 1475 ? -15.500  31.660  5.752   1.00 125.42 ? 1475 VAL A C   1 
ATOM   11211 O  O   . VAL A 1 1475 ? -14.696  30.716  5.749   1.00 126.62 ? 1475 VAL A O   1 
ATOM   11212 C  CB  . VAL A 1 1475 ? -17.553  31.153  4.483   1.00 116.09 ? 1475 VAL A CB  1 
ATOM   11213 C  CG1 . VAL A 1 1475 ? -17.211  29.706  4.294   1.00 116.62 ? 1475 VAL A CG1 1 
ATOM   11214 C  CG2 . VAL A 1 1475 ? -18.305  31.305  5.783   1.00 114.09 ? 1475 VAL A CG2 1 
ATOM   11215 N  N   . ARG A 1 1476 ? -15.717  32.435  6.814   1.00 126.33 ? 1476 ARG A N   1 
ATOM   11216 C  CA  . ARG A 1 1476 ? -15.274  32.039  8.142   1.00 125.60 ? 1476 ARG A CA  1 
ATOM   11217 C  C   . ARG A 1 1476 ? -16.394  32.316  9.154   1.00 119.69 ? 1476 ARG A C   1 
ATOM   11218 O  O   . ARG A 1 1476 ? -17.217  33.211  8.958   1.00 115.85 ? 1476 ARG A O   1 
ATOM   11219 C  CB  . ARG A 1 1476 ? -13.937  32.688  8.519   1.00 131.00 ? 1476 ARG A CB  1 
ATOM   11220 C  CG  . ARG A 1 1476 ? -13.770  34.120  8.072   1.00 136.40 ? 1476 ARG A CG  1 
ATOM   11221 C  CD  . ARG A 1 1476 ? -12.946  34.277  6.791   1.00 143.61 ? 1476 ARG A CD  1 
ATOM   11222 N  NE  . ARG A 1 1476 ? -13.509  35.355  5.973   1.00 149.05 ? 1476 ARG A NE  1 
ATOM   11223 C  CZ  . ARG A 1 1476 ? -12.959  35.866  4.868   1.00 154.73 ? 1476 ARG A CZ  1 
ATOM   11224 N  NH1 . ARG A 1 1476 ? -11.778  35.424  4.407   1.00 157.87 ? 1476 ARG A NH1 1 
ATOM   11225 N  NH2 . ARG A 1 1476 ? -13.604  36.839  4.222   1.00 154.40 ? 1476 ARG A NH2 1 
ATOM   11226 N  N   . PHE A 1 1477 ? -16.453  31.494  10.198  1.00 118.53 ? 1477 PHE A N   1 
ATOM   11227 C  CA  . PHE A 1 1477 ? -17.489  31.600  11.226  1.00 115.95 ? 1477 PHE A CA  1 
ATOM   11228 C  C   . PHE A 1 1477 ? -17.176  30.710  12.439  1.00 117.03 ? 1477 PHE A C   1 
ATOM   11229 O  O   . PHE A 1 1477 ? -16.499  29.679  12.319  1.00 118.57 ? 1477 PHE A O   1 
ATOM   11230 C  CB  . PHE A 1 1477 ? -18.862  31.270  10.651  1.00 111.61 ? 1477 PHE A CB  1 
ATOM   11231 C  CG  . PHE A 1 1477 ? -19.043  29.821  10.312  1.00 111.63 ? 1477 PHE A CG  1 
ATOM   11232 C  CD1 . PHE A 1 1477 ? -19.661  28.954  11.200  1.00 111.09 ? 1477 PHE A CD1 1 
ATOM   11233 C  CD2 . PHE A 1 1477 ? -18.606  29.326  9.105   1.00 112.05 ? 1477 PHE A CD2 1 
ATOM   11234 C  CE1 . PHE A 1 1477 ? -19.827  27.623  10.886  1.00 110.90 ? 1477 PHE A CE1 1 
ATOM   11235 C  CE2 . PHE A 1 1477 ? -18.774  28.003  8.793   1.00 112.49 ? 1477 PHE A CE2 1 
ATOM   11236 C  CZ  . PHE A 1 1477 ? -19.383  27.149  9.685   1.00 111.45 ? 1477 PHE A CZ  1 
ATOM   11237 N  N   . ARG A 1 1478 ? -17.663  31.118  13.606  1.00 114.75 ? 1478 ARG A N   1 
ATOM   11238 C  CA  . ARG A 1 1478 ? -17.265  30.466  14.832  1.00 115.05 ? 1478 ARG A CA  1 
ATOM   11239 C  C   . ARG A 1 1478 ? -18.308  29.461  15.291  1.00 113.56 ? 1478 ARG A C   1 
ATOM   11240 O  O   . ARG A 1 1478 ? -19.474  29.564  14.927  1.00 107.08 ? 1478 ARG A O   1 
ATOM   11241 C  CB  . ARG A 1 1478 ? -17.014  31.516  15.890  1.00 116.03 ? 1478 ARG A CB  1 
ATOM   11242 C  CG  . ARG A 1 1478 ? -16.286  32.720  15.368  1.00 117.96 ? 1478 ARG A CG  1 
ATOM   11243 C  CD  . ARG A 1 1478 ? -16.045  33.684  16.501  1.00 121.99 ? 1478 ARG A CD  1 
ATOM   11244 N  NE  . ARG A 1 1478 ? -17.126  34.643  16.670  1.00 120.85 ? 1478 ARG A NE  1 
ATOM   11245 C  CZ  . ARG A 1 1478 ? -16.999  35.933  16.405  1.00 122.13 ? 1478 ARG A CZ  1 
ATOM   11246 N  NH1 . ARG A 1 1478 ? -15.839  36.404  15.966  1.00 126.08 ? 1478 ARG A NH1 1 
ATOM   11247 N  NH2 . ARG A 1 1478 ? -18.026  36.742  16.581  1.00 120.05 ? 1478 ARG A NH2 1 
ATOM   11248 N  N   . ILE A 1 1479 ? -17.878  28.503  16.111  1.00 121.00 ? 1479 ILE A N   1 
ATOM   11249 C  CA  . ILE A 1 1479 ? -18.718  27.370  16.503  1.00 126.17 ? 1479 ILE A CA  1 
ATOM   11250 C  C   . ILE A 1 1479 ? -18.601  27.000  17.985  1.00 132.10 ? 1479 ILE A C   1 
ATOM   11251 O  O   . ILE A 1 1479 ? -17.490  26.883  18.512  1.00 135.67 ? 1479 ILE A O   1 
ATOM   11252 C  CB  . ILE A 1 1479 ? -18.335  26.127  15.682  1.00 127.47 ? 1479 ILE A CB  1 
ATOM   11253 C  CG1 . ILE A 1 1479 ? -16.873  25.751  15.928  1.00 130.65 ? 1479 ILE A CG1 1 
ATOM   11254 C  CG2 . ILE A 1 1479 ? -18.530  26.393  14.208  1.00 128.33 ? 1479 ILE A CG2 1 
ATOM   11255 C  CD1 . ILE A 1 1479 ? -16.297  24.821  14.890  1.00 130.32 ? 1479 ILE A CD1 1 
ATOM   11256 N  N   . PHE A 1 1480 ? -19.737  26.809  18.661  1.00 134.64 ? 1480 PHE A N   1 
ATOM   11257 C  CA  . PHE A 1 1480 ? -19.712  26.468  20.094  1.00 144.29 ? 1480 PHE A CA  1 
ATOM   11258 C  C   . PHE A 1 1480 ? -20.184  25.064  20.452  1.00 138.16 ? 1480 PHE A C   1 
ATOM   11259 O  O   . PHE A 1 1480 ? -21.324  24.712  20.224  1.00 135.91 ? 1480 PHE A O   1 
ATOM   11260 C  CB  . PHE A 1 1480 ? -20.420  27.516  20.978  1.00 162.67 ? 1480 PHE A CB  1 
ATOM   11261 C  CG  . PHE A 1 1480 ? -21.390  28.431  20.234  1.00 170.33 ? 1480 PHE A CG  1 
ATOM   11262 C  CD1 . PHE A 1 1480 ? -22.487  27.910  19.541  1.00 168.96 ? 1480 PHE A CD1 1 
ATOM   11263 C  CD2 . PHE A 1 1480 ? -21.228  29.834  20.283  1.00 173.52 ? 1480 PHE A CD2 1 
ATOM   11264 C  CE1 . PHE A 1 1480 ? -23.387  28.763  18.881  1.00 166.51 ? 1480 PHE A CE1 1 
ATOM   11265 C  CE2 . PHE A 1 1480 ? -22.120  30.697  19.629  1.00 170.47 ? 1480 PHE A CE2 1 
ATOM   11266 C  CZ  . PHE A 1 1480 ? -23.201  30.158  18.923  1.00 167.35 ? 1480 PHE A CZ  1 
ATOM   11267 N  N   . GLU A 1 1481 ? -19.291  24.288  21.057  1.00 139.14 ? 1481 GLU A N   1 
ATOM   11268 C  CA  . GLU A 1 1481 ? -19.577  22.908  21.441  1.00 137.31 ? 1481 GLU A CA  1 
ATOM   11269 C  C   . GLU A 1 1481 ? -20.876  22.799  22.244  1.00 135.28 ? 1481 GLU A C   1 
ATOM   11270 O  O   . GLU A 1 1481 ? -20.860  22.730  23.468  1.00 137.11 ? 1481 GLU A O   1 
ATOM   11271 C  CB  . GLU A 1 1481 ? -18.395  22.302  22.236  1.00 139.62 ? 1481 GLU A CB  1 
ATOM   11272 C  CG  . GLU A 1 1481 ? -17.110  22.021  21.415  1.00 173.68 ? 1481 GLU A CG  1 
ATOM   11273 C  CD  . GLU A 1 1481 ? -16.042  21.229  22.180  1.00 174.98 ? 1481 GLU A CD  1 
ATOM   11274 O  OE1 . GLU A 1 1481 ? -16.302  20.807  23.332  1.00 174.90 ? 1481 GLU A OE1 1 
ATOM   11275 O  OE2 . GLU A 1 1481 ? -14.936  21.029  21.621  1.00 175.94 ? 1481 GLU A OE2 1 
ATOM   11276 N  N   . LEU A 1 1482 ? -22.003  22.753  21.552  1.00 131.78 ? 1482 LEU A N   1 
ATOM   11277 C  CA  . LEU A 1 1482 ? -23.288  22.733  22.236  1.00 128.44 ? 1482 LEU A CA  1 
ATOM   11278 C  C   . LEU A 1 1482 ? -23.356  21.657  23.318  1.00 125.73 ? 1482 LEU A C   1 
ATOM   11279 O  O   . LEU A 1 1482 ? -23.900  21.889  24.394  1.00 125.53 ? 1482 LEU A O   1 
ATOM   11280 C  CB  . LEU A 1 1482 ? -24.437  22.575  21.241  1.00 127.53 ? 1482 LEU A CB  1 
ATOM   11281 C  CG  . LEU A 1 1482 ? -25.815  22.354  21.865  1.00 128.06 ? 1482 LEU A CG  1 
ATOM   11282 C  CD1 . LEU A 1 1482 ? -26.890  23.126  21.099  1.00 125.98 ? 1482 LEU A CD1 1 
ATOM   11283 C  CD2 . LEU A 1 1482 ? -26.144  20.852  21.947  1.00 128.32 ? 1482 LEU A CD2 1 
ATOM   11284 N  N   . PHE A 1 1483 ? -22.783  20.482  23.029  1.00 122.48 ? 1483 PHE A N   1 
ATOM   11285 C  CA  . PHE A 1 1483 ? -22.667  19.447  24.042  1.00 121.88 ? 1483 PHE A CA  1 
ATOM   11286 C  C   . PHE A 1 1483 ? -21.451  18.585  23.789  1.00 126.34 ? 1483 PHE A C   1 
ATOM   11287 O  O   . PHE A 1 1483 ? -20.787  18.707  22.756  1.00 127.53 ? 1483 PHE A O   1 
ATOM   11288 C  CB  . PHE A 1 1483 ? -23.941  18.623  24.188  1.00 116.35 ? 1483 PHE A CB  1 
ATOM   11289 C  CG  . PHE A 1 1483 ? -24.489  18.038  22.946  1.00 111.81 ? 1483 PHE A CG  1 
ATOM   11290 C  CD1 . PHE A 1 1483 ? -23.671  17.791  21.854  1.00 111.05 ? 1483 PHE A CD1 1 
ATOM   11291 C  CD2 . PHE A 1 1483 ? -25.828  17.697  22.854  1.00 108.96 ? 1483 PHE A CD2 1 
ATOM   11292 C  CE1 . PHE A 1 1483 ? -24.179  17.235  20.689  1.00 106.57 ? 1483 PHE A CE1 1 
ATOM   11293 C  CE2 . PHE A 1 1483 ? -26.327  17.138  21.705  1.00 105.58 ? 1483 PHE A CE2 1 
ATOM   11294 C  CZ  . PHE A 1 1483 ? -25.499  16.910  20.616  1.00 104.37 ? 1483 PHE A CZ  1 
ATOM   11295 N  N   . GLU A 1 1484 ? -21.167  17.709  24.718  1.00 131.85 ? 1484 GLU A N   1 
ATOM   11296 C  CA  . GLU A 1 1484 ? -19.987  16.869  24.635  1.00 137.78 ? 1484 GLU A CA  1 
ATOM   11297 C  C   . GLU A 1 1484 ? -20.160  15.602  23.825  1.00 136.67 ? 1484 GLU A C   1 
ATOM   11298 O  O   . GLU A 1 1484 ? -20.849  14.663  24.212  1.00 136.76 ? 1484 GLU A O   1 
ATOM   11299 C  CB  . GLU A 1 1484 ? -19.527  16.506  26.047  1.00 146.46 ? 1484 GLU A CB  1 
ATOM   11300 C  CG  . GLU A 1 1484 ? -19.525  17.682  27.034  1.00 154.27 ? 1484 GLU A CG  1 
ATOM   11301 C  CD  . GLU A 1 1484 ? -20.903  18.105  27.476  1.00 157.80 ? 1484 GLU A CD  1 
ATOM   11302 O  OE1 . GLU A 1 1484 ? -21.887  17.488  27.004  1.00 157.70 ? 1484 GLU A OE1 1 
ATOM   11303 O  OE2 . GLU A 1 1484 ? -20.998  19.055  28.291  1.00 159.47 ? 1484 GLU A OE2 1 
ATOM   11304 N  N   . VAL A 1 1485 ? -19.523  15.618  22.659  1.00 135.87 ? 1485 VAL A N   1 
ATOM   11305 C  CA  . VAL A 1 1485 ? -19.549  14.451  21.803  1.00 131.72 ? 1485 VAL A CA  1 
ATOM   11306 C  C   . VAL A 1 1485 ? -18.294  13.629  22.025  1.00 131.31 ? 1485 VAL A C   1 
ATOM   11307 O  O   . VAL A 1 1485 ? -17.231  14.233  22.260  1.00 131.19 ? 1485 VAL A O   1 
ATOM   11308 C  CB  . VAL A 1 1485 ? -19.726  14.816  20.316  1.00 149.00 ? 1485 VAL A CB  1 
ATOM   11309 C  CG1 . VAL A 1 1485 ? -21.037  15.542  20.086  1.00 145.99 ? 1485 VAL A CG1 1 
ATOM   11310 C  CG2 . VAL A 1 1485 ? -18.546  15.660  19.835  1.00 151.24 ? 1485 VAL A CG2 1 
ATOM   11311 N  N   . GLY A 1 1486 ? -18.281  12.303  22.003  1.00 126.93 ? 1486 GLY A N   1 
ATOM   11312 C  CA  . GLY A 1 1486 ? -17.012  11.641  22.394  1.00 127.89 ? 1486 GLY A CA  1 
ATOM   11313 C  C   . GLY A 1 1486 ? -16.483  10.529  21.473  1.00 126.71 ? 1486 GLY A C   1 
ATOM   11314 O  O   . GLY A 1 1486 ? -16.768  9.351   21.670  1.00 129.17 ? 1486 GLY A O   1 
ATOM   11315 N  N   . PHE A 1 1487 ? -15.708  10.943  20.478  1.00 125.42 ? 1487 PHE A N   1 
ATOM   11316 C  CA  . PHE A 1 1487 ? -15.083  10.274  19.311  1.00 126.54 ? 1487 PHE A CA  1 
ATOM   11317 C  C   . PHE A 1 1487 ? -16.096  10.592  18.254  1.00 120.99 ? 1487 PHE A C   1 
ATOM   11318 O  O   . PHE A 1 1487 ? -16.983  9.809   17.910  1.00 118.50 ? 1487 PHE A O   1 
ATOM   11319 C  CB  . PHE A 1 1487 ? -14.861  8.738   19.186  1.00 131.99 ? 1487 PHE A CB  1 
ATOM   11320 C  CG  . PHE A 1 1487 ? -15.033  7.793   20.321  1.00 135.61 ? 1487 PHE A CG  1 
ATOM   11321 C  CD1 . PHE A 1 1487 ? -13.977  6.982   20.764  1.00 139.27 ? 1487 PHE A CD1 1 
ATOM   11322 C  CD2 . PHE A 1 1487 ? -16.254  7.703   20.971  1.00 134.63 ? 1487 PHE A CD2 1 
ATOM   11323 C  CE1 . PHE A 1 1487 ? -14.160  6.126   21.827  1.00 140.52 ? 1487 PHE A CE1 1 
ATOM   11324 C  CE2 . PHE A 1 1487 ? -16.441  6.824   22.035  1.00 135.91 ? 1487 PHE A CE2 1 
ATOM   11325 C  CZ  . PHE A 1 1487 ? -15.376  6.047   22.463  1.00 138.69 ? 1487 PHE A CZ  1 
ATOM   11326 N  N   . LEU A 1 1488 ? -15.903  11.792  17.750  1.00 119.14 ? 1488 LEU A N   1 
ATOM   11327 C  CA  . LEU A 1 1488 ? -16.757  12.253  16.730  1.00 115.73 ? 1488 LEU A CA  1 
ATOM   11328 C  C   . LEU A 1 1488 ? -16.204  11.976  15.342  1.00 117.03 ? 1488 LEU A C   1 
ATOM   11329 O  O   . LEU A 1 1488 ? -15.012  12.123  15.093  1.00 119.80 ? 1488 LEU A O   1 
ATOM   11330 C  CB  . LEU A 1 1488 ? -17.103  13.761  16.955  1.00 113.62 ? 1488 LEU A CB  1 
ATOM   11331 C  CG  . LEU A 1 1488 ? -16.179  14.894  16.444  1.00 114.01 ? 1488 LEU A CG  1 
ATOM   11332 C  CD1 . LEU A 1 1488 ? -15.410  14.450  15.215  1.00 114.60 ? 1488 LEU A CD1 1 
ATOM   11333 C  CD2 . LEU A 1 1488 ? -16.999  16.135  16.128  1.00 112.32 ? 1488 LEU A CD2 1 
ATOM   11334 N  N   . SER A 1 1489 ? -17.109  11.552  14.455  1.00 112.81 ? 1489 SER A N   1 
ATOM   11335 C  CA  . SER A 1 1489 ? -16.776  11.365  13.045  1.00 109.58 ? 1489 SER A CA  1 
ATOM   11336 C  C   . SER A 1 1489 ? -17.060  12.690  12.327  1.00 105.89 ? 1489 SER A C   1 
ATOM   11337 O  O   . SER A 1 1489 ? -17.860  13.501  12.822  1.00 105.24 ? 1489 SER A O   1 
ATOM   11338 C  CB  . SER A 1 1489 ? -17.577  10.212  12.437  1.00 104.23 ? 1489 SER A CB  1 
ATOM   11339 O  OG  . SER A 1 1489 ? -18.632  10.732  11.648  1.00 100.75 ? 1489 SER A OG  1 
ATOM   11340 N  N   . PRO A 1 1490 ? -16.379  12.924  11.186  1.00 105.34 ? 1490 PRO A N   1 
ATOM   11341 C  CA  . PRO A 1 1490 ? -16.375  14.202  10.481  1.00 102.22 ? 1490 PRO A CA  1 
ATOM   11342 C  C   . PRO A 1 1490 ? -17.613  14.369  9.687   1.00 101.95 ? 1490 PRO A C   1 
ATOM   11343 O  O   . PRO A 1 1490 ? -18.220  13.419  9.180   1.00 98.75  ? 1490 PRO A O   1 
ATOM   11344 C  CB  . PRO A 1 1490 ? -15.225  14.073  9.485   1.00 103.31 ? 1490 PRO A CB  1 
ATOM   11345 C  CG  . PRO A 1 1490 ? -14.540  12.831  9.825   1.00 106.44 ? 1490 PRO A CG  1 
ATOM   11346 C  CD  . PRO A 1 1490 ? -15.559  11.946  10.473  1.00 105.46 ? 1490 PRO A CD  1 
ATOM   11347 N  N   . ALA A 1 1491 ? -17.987  15.628  9.600   1.00 105.08 ? 1491 ALA A N   1 
ATOM   11348 C  CA  . ALA A 1 1491 ? -18.993  16.045  8.674   1.00 104.01 ? 1491 ALA A CA  1 
ATOM   11349 C  C   . ALA A 1 1491 ? -18.219  16.400  7.415   1.00 108.25 ? 1491 ALA A C   1 
ATOM   11350 O  O   . ALA A 1 1491 ? -17.035  16.035  7.265   1.00 108.01 ? 1491 ALA A O   1 
ATOM   11351 C  CB  . ALA A 1 1491 ? -19.726  17.246  9.213   1.00 100.59 ? 1491 ALA A CB  1 
ATOM   11352 N  N   . THR A 1 1492 ? -18.891  17.138  6.535   1.00 109.61 ? 1492 THR A N   1 
ATOM   11353 C  CA  . THR A 1 1492 ? -18.453  17.294  5.165   1.00 109.25 ? 1492 THR A CA  1 
ATOM   11354 C  C   . THR A 1 1492 ? -18.660  18.697  4.649   1.00 111.62 ? 1492 THR A C   1 
ATOM   11355 O  O   . THR A 1 1492 ? -19.618  19.381  5.003   1.00 110.76 ? 1492 THR A O   1 
ATOM   11356 C  CB  . THR A 1 1492 ? -19.237  16.376  4.283   1.00 103.77 ? 1492 THR A CB  1 
ATOM   11357 O  OG1 . THR A 1 1492 ? -20.500  16.137  4.902   1.00 90.26  ? 1492 THR A OG1 1 
ATOM   11358 C  CG2 . THR A 1 1492 ? -18.544  15.088  4.202   1.00 93.49  ? 1492 THR A CG2 1 
ATOM   11359 N  N   . PHE A 1 1493 ? -17.732  19.114  3.803   1.00 110.91 ? 1493 PHE A N   1 
ATOM   11360 C  CA  . PHE A 1 1493 ? -17.772  20.431  3.207   1.00 108.15 ? 1493 PHE A CA  1 
ATOM   11361 C  C   . PHE A 1 1493 ? -17.871  20.263  1.730   1.00 111.51 ? 1493 PHE A C   1 
ATOM   11362 O  O   . PHE A 1 1493 ? -16.854  20.025  1.058   1.00 113.43 ? 1493 PHE A O   1 
ATOM   11363 C  CB  . PHE A 1 1493 ? -16.500  21.189  3.488   1.00 103.52 ? 1493 PHE A CB  1 
ATOM   11364 C  CG  . PHE A 1 1493 ? -16.368  22.434  2.690   1.00 98.19  ? 1493 PHE A CG  1 
ATOM   11365 C  CD1 . PHE A 1 1493 ? -17.487  23.161  2.364   1.00 93.77  ? 1493 PHE A CD1 1 
ATOM   11366 C  CD2 . PHE A 1 1493 ? -15.120  22.893  2.295   1.00 99.04  ? 1493 PHE A CD2 1 
ATOM   11367 C  CE1 . PHE A 1 1493 ? -17.375  24.304  1.638   1.00 93.93  ? 1493 PHE A CE1 1 
ATOM   11368 C  CE2 . PHE A 1 1493 ? -14.991  24.045  1.578   1.00 97.99  ? 1493 PHE A CE2 1 
ATOM   11369 C  CZ  . PHE A 1 1493 ? -16.125  24.756  1.245   1.00 96.03  ? 1493 PHE A CZ  1 
ATOM   11370 N  N   . THR A 1 1494 ? -19.095  20.401  1.236   1.00 111.97 ? 1494 THR A N   1 
ATOM   11371 C  CA  . THR A 1 1494 ? -19.386  20.232  -0.173  1.00 111.21 ? 1494 THR A CA  1 
ATOM   11372 C  C   . THR A 1 1494 ? -19.763  21.590  -0.844  1.00 100.05 ? 1494 THR A C   1 
ATOM   11373 O  O   . THR A 1 1494 ? -20.359  22.469  -0.206  1.00 89.39  ? 1494 THR A O   1 
ATOM   11374 C  CB  . THR A 1 1494 ? -20.433  19.113  -0.317  1.00 107.58 ? 1494 THR A CB  1 
ATOM   11375 O  OG1 . THR A 1 1494 ? -21.192  19.292  -1.515  1.00 106.48 ? 1494 THR A OG1 1 
ATOM   11376 C  CG2 . THR A 1 1494 ? -21.352  19.076  0.926   1.00 104.38 ? 1494 THR A CG2 1 
ATOM   11377 N  N   . VAL A 1 1495 ? -19.341  21.778  -2.098  1.00 100.60 ? 1495 VAL A N   1 
ATOM   11378 C  CA  . VAL A 1 1495 ? -19.687  22.977  -2.872  1.00 106.08 ? 1495 VAL A CA  1 
ATOM   11379 C  C   . VAL A 1 1495 ? -19.832  22.662  -4.364  1.00 109.48 ? 1495 VAL A C   1 
ATOM   11380 O  O   . VAL A 1 1495 ? -18.863  22.284  -5.037  1.00 115.33 ? 1495 VAL A O   1 
ATOM   11381 C  CB  . VAL A 1 1495 ? -18.689  24.148  -2.683  1.00 92.10  ? 1495 VAL A CB  1 
ATOM   11382 C  CG1 . VAL A 1 1495 ? -17.326  23.624  -2.450  1.00 103.37 ? 1495 VAL A CG1 1 
ATOM   11383 C  CG2 . VAL A 1 1495 ? -18.693  25.055  -3.903  1.00 92.28  ? 1495 VAL A CG2 1 
ATOM   11384 N  N   . TYR A 1 1496 ? -21.070  22.820  -4.846  1.00 110.51 ? 1496 TYR A N   1 
ATOM   11385 C  CA  . TYR A 1 1496 ? -21.483  22.599  -6.232  1.00 109.21 ? 1496 TYR A CA  1 
ATOM   11386 C  C   . TYR A 1 1496 ? -22.130  23.890  -6.786  1.00 108.76 ? 1496 TYR A C   1 
ATOM   11387 O  O   . TYR A 1 1496 ? -22.408  24.843  -6.040  1.00 106.65 ? 1496 TYR A O   1 
ATOM   11388 C  CB  . TYR A 1 1496 ? -22.497  21.444  -6.304  1.00 106.63 ? 1496 TYR A CB  1 
ATOM   11389 C  CG  . TYR A 1 1496 ? -23.679  21.619  -5.347  1.00 106.27 ? 1496 TYR A CG  1 
ATOM   11390 C  CD1 . TYR A 1 1496 ? -24.031  22.885  -4.905  1.00 104.34 ? 1496 TYR A CD1 1 
ATOM   11391 C  CD2 . TYR A 1 1496 ? -24.456  20.527  -4.903  1.00 105.70 ? 1496 TYR A CD2 1 
ATOM   11392 C  CE1 . TYR A 1 1496 ? -25.072  23.077  -4.060  1.00 101.71 ? 1496 TYR A CE1 1 
ATOM   11393 C  CE2 . TYR A 1 1496 ? -25.532  20.721  -4.037  1.00 103.57 ? 1496 TYR A CE2 1 
ATOM   11394 C  CZ  . TYR A 1 1496 ? -25.814  22.020  -3.617  1.00 101.94 ? 1496 TYR A CZ  1 
ATOM   11395 O  OH  . TYR A 1 1496 ? -26.822  22.339  -2.742  1.00 100.22 ? 1496 TYR A OH  1 
ATOM   11396 N  N   . GLU A 1 1497 ? -22.366  23.905  -8.096  1.00 109.14 ? 1497 GLU A N   1 
ATOM   11397 C  CA  . GLU A 1 1497 ? -23.038  25.003  -8.799  1.00 106.87 ? 1497 GLU A CA  1 
ATOM   11398 C  C   . GLU A 1 1497 ? -24.552  24.780  -8.854  1.00 104.26 ? 1497 GLU A C   1 
ATOM   11399 O  O   . GLU A 1 1497 ? -25.017  23.709  -9.252  1.00 101.56 ? 1497 GLU A O   1 
ATOM   11400 C  CB  . GLU A 1 1497 ? -22.478  25.071  -10.217 1.00 106.27 ? 1497 GLU A CB  1 
ATOM   11401 C  CG  . GLU A 1 1497 ? -22.548  26.412  -10.901 1.00 104.90 ? 1497 GLU A CG  1 
ATOM   11402 C  CD  . GLU A 1 1497 ? -21.546  26.494  -12.035 1.00 104.94 ? 1497 GLU A CD  1 
ATOM   11403 O  OE1 . GLU A 1 1497 ? -20.736  25.564  -12.167 1.00 102.78 ? 1497 GLU A OE1 1 
ATOM   11404 O  OE2 . GLU A 1 1497 ? -21.559  27.475  -12.797 1.00 106.79 ? 1497 GLU A OE2 1 
ATOM   11405 N  N   . TYR A 1 1498 ? -25.324  25.796  -8.487  1.00 105.79 ? 1498 TYR A N   1 
ATOM   11406 C  CA  . TYR A 1 1498 ? -26.762  25.602  -8.304  1.00 106.24 ? 1498 TYR A CA  1 
ATOM   11407 C  C   . TYR A 1 1498 ? -27.416  24.941  -9.513  1.00 104.96 ? 1498 TYR A C   1 
ATOM   11408 O  O   . TYR A 1 1498 ? -28.059  23.892  -9.388  1.00 102.81 ? 1498 TYR A O   1 
ATOM   11409 C  CB  . TYR A 1 1498 ? -27.493  26.913  -7.952  1.00 106.68 ? 1498 TYR A CB  1 
ATOM   11410 C  CG  . TYR A 1 1498 ? -28.874  26.678  -7.343  1.00 107.75 ? 1498 TYR A CG  1 
ATOM   11411 C  CD1 . TYR A 1 1498 ? -29.020  25.882  -6.222  1.00 109.89 ? 1498 TYR A CD1 1 
ATOM   11412 C  CD2 . TYR A 1 1498 ? -30.021  27.243  -7.885  1.00 107.71 ? 1498 TYR A CD2 1 
ATOM   11413 C  CE1 . TYR A 1 1498 ? -30.251  25.651  -5.657  1.00 109.83 ? 1498 TYR A CE1 1 
ATOM   11414 C  CE2 . TYR A 1 1498 ? -31.258  27.013  -7.324  1.00 108.06 ? 1498 TYR A CE2 1 
ATOM   11415 C  CZ  . TYR A 1 1498 ? -31.364  26.209  -6.208  1.00 109.47 ? 1498 TYR A CZ  1 
ATOM   11416 O  OH  . TYR A 1 1498 ? -32.580  25.958  -5.613  1.00 110.68 ? 1498 TYR A OH  1 
ATOM   11417 N  N   . HIS A 1 1499 ? -27.233  25.555  -10.678 1.00 104.51 ? 1499 HIS A N   1 
ATOM   11418 C  CA  . HIS A 1 1499 ? -27.882  25.085  -11.887 1.00 102.42 ? 1499 HIS A CA  1 
ATOM   11419 C  C   . HIS A 1 1499 ? -27.183  23.898  -12.553 1.00 106.91 ? 1499 HIS A C   1 
ATOM   11420 O  O   . HIS A 1 1499 ? -27.761  23.247  -13.439 1.00 109.45 ? 1499 HIS A O   1 
ATOM   11421 C  CB  . HIS A 1 1499 ? -28.034  26.227  -12.863 1.00 97.21  ? 1499 HIS A CB  1 
ATOM   11422 C  CG  . HIS A 1 1499 ? -29.013  27.234  -12.415 1.00 92.28  ? 1499 HIS A CG  1 
ATOM   11423 N  ND1 . HIS A 1 1499 ? -28.809  28.583  -12.570 1.00 92.69  ? 1499 HIS A ND1 1 
ATOM   11424 C  CD2 . HIS A 1 1499 ? -30.198  27.095  -11.784 1.00 91.31  ? 1499 HIS A CD2 1 
ATOM   11425 C  CE1 . HIS A 1 1499 ? -29.843  29.238  -12.069 1.00 92.80  ? 1499 HIS A CE1 1 
ATOM   11426 N  NE2 . HIS A 1 1499 ? -30.697  28.358  -11.580 1.00 91.63  ? 1499 HIS A NE2 1 
ATOM   11427 N  N   . ARG A 1 1500 ? -25.946  23.620  -12.149 1.00 107.11 ? 1500 ARG A N   1 
ATOM   11428 C  CA  . ARG A 1 1500 ? -25.306  22.399  -12.589 1.00 106.38 ? 1500 ARG A CA  1 
ATOM   11429 C  C   . ARG A 1 1500 ? -24.534  21.736  -11.451 1.00 105.16 ? 1500 ARG A C   1 
ATOM   11430 O  O   . ARG A 1 1500 ? -23.311  21.817  -11.373 1.00 108.30 ? 1500 ARG A O   1 
ATOM   11431 C  CB  . ARG A 1 1500 ? -24.438  22.620  -13.837 1.00 109.56 ? 1500 ARG A CB  1 
ATOM   11432 C  CG  . ARG A 1 1500 ? -24.057  24.051  -14.136 1.00 111.58 ? 1500 ARG A CG  1 
ATOM   11433 C  CD  . ARG A 1 1500 ? -22.539  24.158  -14.291 1.00 116.18 ? 1500 ARG A CD  1 
ATOM   11434 N  NE  . ARG A 1 1500 ? -22.078  24.309  -15.664 1.00 118.51 ? 1500 ARG A NE  1 
ATOM   11435 C  CZ  . ARG A 1 1500 ? -20.798  24.283  -16.018 1.00 121.03 ? 1500 ARG A CZ  1 
ATOM   11436 N  NH1 . ARG A 1 1500 ? -19.856  24.089  -15.100 1.00 121.13 ? 1500 ARG A NH1 1 
ATOM   11437 N  NH2 . ARG A 1 1500 ? -20.459  24.431  -17.295 1.00 123.23 ? 1500 ARG A NH2 1 
ATOM   11438 N  N   . PRO A 1 1501 ? -25.270  21.053  -10.577 1.00 99.35  ? 1501 PRO A N   1 
ATOM   11439 C  CA  . PRO A 1 1501 ? -24.886  20.159  -9.484  1.00 100.26 ? 1501 PRO A CA  1 
ATOM   11440 C  C   . PRO A 1 1501 ? -23.913  19.090  -9.922  1.00 104.75 ? 1501 PRO A C   1 
ATOM   11441 O  O   . PRO A 1 1501 ? -23.554  18.238  -9.120  1.00 104.55 ? 1501 PRO A O   1 
ATOM   11442 C  CB  . PRO A 1 1501 ? -26.189  19.442  -9.157  1.00 98.16  ? 1501 PRO A CB  1 
ATOM   11443 C  CG  . PRO A 1 1501 ? -27.255  20.318  -9.641  1.00 97.05  ? 1501 PRO A CG  1 
ATOM   11444 C  CD  . PRO A 1 1501 ? -26.724  21.161  -10.726 1.00 97.18  ? 1501 PRO A CD  1 
ATOM   11445 N  N   . ASP A 1 1502 ? -23.553  19.083  -11.201 1.00 111.11 ? 1502 ASP A N   1 
ATOM   11446 C  CA  . ASP A 1 1502 ? -22.697  18.037  -11.749 1.00 116.10 ? 1502 ASP A CA  1 
ATOM   11447 C  C   . ASP A 1 1502 ? -21.309  18.425  -11.288 1.00 122.07 ? 1502 ASP A C   1 
ATOM   11448 O  O   . ASP A 1 1502 ? -20.342  17.715  -11.532 1.00 125.34 ? 1502 ASP A O   1 
ATOM   11449 C  CB  . ASP A 1 1502 ? -22.789  17.951  -13.294 1.00 116.62 ? 1502 ASP A CB  1 
ATOM   11450 C  CG  . ASP A 1 1502 ? -24.075  18.609  -13.868 1.00 112.81 ? 1502 ASP A CG  1 
ATOM   11451 O  OD1 . ASP A 1 1502 ? -25.231  18.320  -13.398 1.00 108.38 ? 1502 ASP A OD1 1 
ATOM   11452 O  OD2 . ASP A 1 1502 ? -23.905  19.419  -14.823 1.00 113.52 ? 1502 ASP A OD2 1 
ATOM   11453 N  N   . LYS A 1 1503 ? -21.230  19.561  -10.599 1.00 124.92 ? 1503 LYS A N   1 
ATOM   11454 C  CA  . LYS A 1 1503 ? -19.958  20.120  -10.145 1.00 131.67 ? 1503 LYS A CA  1 
ATOM   11455 C  C   . LYS A 1 1503 ? -19.635  19.969  -8.607  1.00 117.95 ? 1503 LYS A C   1 
ATOM   11456 O  O   . LYS A 1 1503 ? -19.010  20.835  -7.985  1.00 114.35 ? 1503 LYS A O   1 
ATOM   11457 C  CB  . LYS A 1 1503 ? -19.885  21.565  -10.626 1.00 135.45 ? 1503 LYS A CB  1 
ATOM   11458 C  CG  . LYS A 1 1503 ? -19.344  21.736  -12.062 1.00 139.60 ? 1503 LYS A CG  1 
ATOM   11459 C  CD  . LYS A 1 1503 ? -19.945  20.808  -13.092 1.00 141.76 ? 1503 LYS A CD  1 
ATOM   11460 C  CE  . LYS A 1 1503 ? -18.967  20.633  -14.273 1.00 147.27 ? 1503 LYS A CE  1 
ATOM   11461 N  NZ  . LYS A 1 1503 ? -19.240  19.434  -15.163 1.00 150.06 ? 1503 LYS A NZ  1 
ATOM   11462 N  N   . GLN A 1 1504 ? -20.033  18.828  -8.031  1.00 118.82 ? 1504 GLN A N   1 
ATOM   11463 C  CA  . GLN A 1 1504 ? -19.943  18.539  -6.591  1.00 111.04 ? 1504 GLN A CA  1 
ATOM   11464 C  C   . GLN A 1 1504 ? -18.584  18.074  -6.203  1.00 113.53 ? 1504 GLN A C   1 
ATOM   11465 O  O   . GLN A 1 1504 ? -18.292  16.882  -6.238  1.00 94.67  ? 1504 GLN A O   1 
ATOM   11466 C  CB  . GLN A 1 1504 ? -20.998  17.488  -6.134  1.00 109.13 ? 1504 GLN A CB  1 
ATOM   11467 C  CG  . GLN A 1 1504 ? -22.311  18.121  -5.478  1.00 150.61 ? 1504 GLN A CG  1 
ATOM   11468 C  CD  . GLN A 1 1504 ? -23.589  17.208  -5.443  1.00 127.58 ? 1504 GLN A CD  1 
ATOM   11469 O  OE1 . GLN A 1 1504 ? -24.720  17.661  -5.090  1.00 120.78 ? 1504 GLN A OE1 1 
ATOM   11470 N  NE2 . GLN A 1 1504 ? -23.402  15.931  -5.805  1.00 130.46 ? 1504 GLN A NE2 1 
ATOM   11471 N  N   . CYS A 1 1505 ? -17.759  19.046  -5.834  1.00 108.54 ? 1505 CYS A N   1 
ATOM   11472 C  CA  . CYS A 1 1505 ? -16.580  18.763  -5.009  1.00 111.61 ? 1505 CYS A CA  1 
ATOM   11473 C  C   . CYS A 1 1505 ? -16.952  18.600  -3.526  1.00 111.40 ? 1505 CYS A C   1 
ATOM   11474 O  O   . CYS A 1 1505 ? -17.590  19.462  -2.920  1.00 105.38 ? 1505 CYS A O   1 
ATOM   11475 C  CB  . CYS A 1 1505 ? -15.464  19.809  -5.159  1.00 113.32 ? 1505 CYS A CB  1 
ATOM   11476 S  SG  . CYS A 1 1505 ? -13.866  19.177  -4.517  1.00 167.38 ? 1505 CYS A SG  1 
ATOM   11477 N  N   . THR A 1 1506 ? -16.535  17.485  -2.952  1.00 112.59 ? 1506 THR A N   1 
ATOM   11478 C  CA  . THR A 1 1506 ? -16.963  17.146  -1.631  1.00 114.11 ? 1506 THR A CA  1 
ATOM   11479 C  C   . THR A 1 1506 ? -15.729  16.752  -0.904  1.00 117.21 ? 1506 THR A C   1 
ATOM   11480 O  O   . THR A 1 1506 ? -14.807  16.193  -1.503  1.00 118.48 ? 1506 THR A O   1 
ATOM   11481 C  CB  . THR A 1 1506 ? -17.905  15.960  -1.657  1.00 117.37 ? 1506 THR A CB  1 
ATOM   11482 O  OG1 . THR A 1 1506 ? -18.953  16.208  -2.601  1.00 120.07 ? 1506 THR A OG1 1 
ATOM   11483 C  CG2 . THR A 1 1506 ? -18.511  15.751  -0.293  1.00 115.39 ? 1506 THR A CG2 1 
ATOM   11484 N  N   . MET A 1 1507 ? -15.721  17.067  0.394   1.00 118.26 ? 1507 MET A N   1 
ATOM   11485 C  CA  . MET A 1 1507 ? -14.568  16.848  1.288   1.00 116.82 ? 1507 MET A CA  1 
ATOM   11486 C  C   . MET A 1 1507 ? -14.970  16.601  2.751   1.00 112.51 ? 1507 MET A C   1 
ATOM   11487 O  O   . MET A 1 1507 ? -15.767  17.353  3.323   1.00 106.98 ? 1507 MET A O   1 
ATOM   11488 C  CB  . MET A 1 1507 ? -13.653  18.060  1.249   1.00 116.31 ? 1507 MET A CB  1 
ATOM   11489 C  CG  . MET A 1 1507 ? -12.270  17.822  1.782   1.00 118.12 ? 1507 MET A CG  1 
ATOM   11490 S  SD  . MET A 1 1507 ? -11.638  19.477  2.006   1.00 108.14 ? 1507 MET A SD  1 
ATOM   11491 C  CE  . MET A 1 1507 ? -13.034  20.379  1.314   1.00 101.74 ? 1507 MET A CE  1 
ATOM   11492 N  N   . PHE A 1 1508 ? -14.427  15.540  3.342   1.00 113.59 ? 1508 PHE A N   1 
ATOM   11493 C  CA  . PHE A 1 1508 ? -14.571  15.327  4.766   1.00 115.88 ? 1508 PHE A CA  1 
ATOM   11494 C  C   . PHE A 1 1508 ? -13.595  16.268  5.469   1.00 126.63 ? 1508 PHE A C   1 
ATOM   11495 O  O   . PHE A 1 1508 ? -12.515  16.543  4.931   1.00 133.84 ? 1508 PHE A O   1 
ATOM   11496 C  CB  . PHE A 1 1508 ? -14.133  13.923  5.115   1.00 111.52 ? 1508 PHE A CB  1 
ATOM   11497 C  CG  . PHE A 1 1508 ? -15.146  12.879  4.870   1.00 103.03 ? 1508 PHE A CG  1 
ATOM   11498 C  CD1 . PHE A 1 1508 ? -16.363  12.926  5.496   1.00 101.47 ? 1508 PHE A CD1 1 
ATOM   11499 C  CD2 . PHE A 1 1508 ? -14.852  11.805  4.069   1.00 101.81 ? 1508 PHE A CD2 1 
ATOM   11500 C  CE1 . PHE A 1 1508 ? -17.307  11.929  5.284   1.00 100.25 ? 1508 PHE A CE1 1 
ATOM   11501 C  CE2 . PHE A 1 1508 ? -15.774  10.809  3.855   1.00 101.20 ? 1508 PHE A CE2 1 
ATOM   11502 C  CZ  . PHE A 1 1508 ? -17.012  10.870  4.460   1.00 99.99  ? 1508 PHE A CZ  1 
ATOM   11503 N  N   . TYR A 1 1509 ? -13.947  16.745  6.666   1.00 126.48 ? 1509 TYR A N   1 
ATOM   11504 C  CA  . TYR A 1 1509 ? -13.007  17.487  7.535   1.00 125.27 ? 1509 TYR A CA  1 
ATOM   11505 C  C   . TYR A 1 1509 ? -13.489  17.242  8.946   1.00 127.90 ? 1509 TYR A C   1 
ATOM   11506 O  O   . TYR A 1 1509 ? -14.607  16.740  9.158   1.00 128.04 ? 1509 TYR A O   1 
ATOM   11507 C  CB  . TYR A 1 1509 ? -13.023  18.998  7.288   1.00 117.42 ? 1509 TYR A CB  1 
ATOM   11508 C  CG  . TYR A 1 1509 ? -14.260  19.631  7.862   1.00 110.85 ? 1509 TYR A CG  1 
ATOM   11509 C  CD1 . TYR A 1 1509 ? -14.209  20.816  8.533   1.00 109.17 ? 1509 TYR A CD1 1 
ATOM   11510 C  CD2 . TYR A 1 1509 ? -15.493  18.998  7.752   1.00 109.66 ? 1509 TYR A CD2 1 
ATOM   11511 C  CE1 . TYR A 1 1509 ? -15.360  21.386  9.064   1.00 107.79 ? 1509 TYR A CE1 1 
ATOM   11512 C  CE2 . TYR A 1 1509 ? -16.648  19.542  8.275   1.00 107.73 ? 1509 TYR A CE2 1 
ATOM   11513 C  CZ  . TYR A 1 1509 ? -16.580  20.741  8.929   1.00 107.11 ? 1509 TYR A CZ  1 
ATOM   11514 O  OH  . TYR A 1 1509 ? -17.743  21.278  9.438   1.00 104.81 ? 1509 TYR A OH  1 
ATOM   11515 N  N   . SER A 1 1510 ? -12.666  17.602  9.919   1.00 129.13 ? 1510 SER A N   1 
ATOM   11516 C  CA  . SER A 1 1510 ? -13.099  17.431  11.285  1.00 127.75 ? 1510 SER A CA  1 
ATOM   11517 C  C   . SER A 1 1510 ? -12.894  18.709  12.037  1.00 130.12 ? 1510 SER A C   1 
ATOM   11518 O  O   . SER A 1 1510 ? -12.115  19.570  11.640  1.00 129.98 ? 1510 SER A O   1 
ATOM   11519 C  CB  . SER A 1 1510 ? -12.379  16.282  11.985  1.00 128.87 ? 1510 SER A CB  1 
ATOM   11520 O  OG  . SER A 1 1510 ? -13.116  15.888  13.137  1.00 126.60 ? 1510 SER A OG  1 
ATOM   11521 N  N   . THR A 1 1511 ? -13.613  18.826  13.135  1.00 130.66 ? 1511 THR A N   1 
ATOM   11522 C  CA  . THR A 1 1511 ? -13.668  20.059  13.858  1.00 131.61 ? 1511 THR A CA  1 
ATOM   11523 C  C   . THR A 1 1511 ? -12.780  19.963  15.067  1.00 142.31 ? 1511 THR A C   1 
ATOM   11524 O  O   . THR A 1 1511 ? -12.912  20.754  15.989  1.00 143.95 ? 1511 THR A O   1 
ATOM   11525 C  CB  . THR A 1 1511 ? -15.078  20.294  14.316  1.00 124.03 ? 1511 THR A CB  1 
ATOM   11526 O  OG1 . THR A 1 1511 ? -15.270  21.685  14.540  1.00 123.05 ? 1511 THR A OG1 1 
ATOM   11527 C  CG2 . THR A 1 1511 ? -15.364  19.508  15.588  1.00 122.20 ? 1511 THR A CG2 1 
ATOM   11528 N  N   . SER A 1 1512 ? -11.883  18.982  15.075  1.00 151.55 ? 1512 SER A N   1 
ATOM   11529 C  CA  . SER A 1 1512 ? -10.962  18.805  16.196  1.00 162.69 ? 1512 SER A CA  1 
ATOM   11530 C  C   . SER A 1 1512 ? -9.778   17.910  15.860  1.00 175.15 ? 1512 SER A C   1 
ATOM   11531 O  O   . SER A 1 1512 ? -9.875   17.001  15.037  1.00 175.68 ? 1512 SER A O   1 
ATOM   11532 C  CB  . SER A 1 1512 ? -11.689  18.244  17.414  1.00 161.01 ? 1512 SER A CB  1 
ATOM   11533 O  OG  . SER A 1 1512 ? -12.020  16.888  17.218  1.00 160.72 ? 1512 SER A OG  1 
ATOM   11534 N  N   . ASN A 1 1513 ? -8.658   18.173  16.520  1.00 188.25 ? 1513 ASN A N   1 
ATOM   11535 C  CA  . ASN A 1 1513 ? -7.427   17.440  16.269  1.00 201.23 ? 1513 ASN A CA  1 
ATOM   11536 C  C   . ASN A 1 1513 ? -7.216   16.258  17.222  1.00 208.84 ? 1513 ASN A C   1 
ATOM   11537 O  O   . ASN A 1 1513 ? -6.224   15.538  17.099  1.00 213.27 ? 1513 ASN A O   1 
ATOM   11538 C  CB  . ASN A 1 1513 ? -6.224   18.387  16.359  1.00 206.98 ? 1513 ASN A CB  1 
ATOM   11539 C  CG  . ASN A 1 1513 ? -6.574   19.818  15.998  1.00 208.37 ? 1513 ASN A CG  1 
ATOM   11540 O  OD1 . ASN A 1 1513 ? -7.203   20.082  14.973  1.00 206.82 ? 1513 ASN A OD1 1 
ATOM   11541 N  ND2 . ASN A 1 1513 ? -6.162   20.754  16.844  1.00 210.78 ? 1513 ASN A ND2 1 
ATOM   11542 N  N   . ILE A 1 1514 ? -8.144   16.063  18.162  1.00 210.63 ? 1514 ILE A N   1 
ATOM   11543 C  CA  . ILE A 1 1514 ? -7.957   15.112  19.271  1.00 213.57 ? 1514 ILE A CA  1 
ATOM   11544 C  C   . ILE A 1 1514 ? -7.633   13.677  18.847  1.00 214.90 ? 1514 ILE A C   1 
ATOM   11545 O  O   . ILE A 1 1514 ? -8.431   13.002  18.181  1.00 213.15 ? 1514 ILE A O   1 
ATOM   11546 C  CB  . ILE A 1 1514 ? -9.165   15.097  20.251  1.00 225.03 ? 1514 ILE A CB  1 
ATOM   11547 C  CG1 . ILE A 1 1514 ? -9.656   16.526  20.527  1.00 222.60 ? 1514 ILE A CG1 1 
ATOM   11548 C  CG2 . ILE A 1 1514 ? -8.795   14.348  21.538  1.00 227.50 ? 1514 ILE A CG2 1 
ATOM   11549 C  CD1 . ILE A 1 1514 ? -10.964  16.603  21.290  1.00 219.42 ? 1514 ILE A CD1 1 
ATOM   11550 N  N   . LYS A 1 1515 ? -6.424   13.259  19.221  1.00 241.46 ? 1515 LYS A N   1 
ATOM   11551 C  CA  . LYS A 1 1515 ? -5.948   11.894  19.061  1.00 241.64 ? 1515 LYS A CA  1 
ATOM   11552 C  C   . LYS A 1 1515 ? -6.232   11.143  20.360  1.00 245.24 ? 1515 LYS A C   1 
ATOM   11553 O  O   . LYS A 1 1515 ? -6.907   11.672  21.248  1.00 248.16 ? 1515 LYS A O   1 
ATOM   11554 C  CB  . LYS A 1 1515 ? -4.437   11.871  18.769  1.00 238.87 ? 1515 LYS A CB  1 
ATOM   11555 C  CG  . LYS A 1 1515 ? -3.960   12.879  17.721  1.00 233.58 ? 1515 LYS A CG  1 
ATOM   11556 C  CD  . LYS A 1 1515 ? -2.435   12.993  17.690  1.00 231.57 ? 1515 LYS A CD  1 
ATOM   11557 C  CE  . LYS A 1 1515 ? -1.977   14.117  16.763  1.00 227.55 ? 1515 LYS A CE  1 
ATOM   11558 N  NZ  . LYS A 1 1515 ? -0.498   14.304  16.773  1.00 226.96 ? 1515 LYS A NZ  1 
ATOM   11559 N  N   . ILE A 1 1516 ? -5.694   9.924   20.439  1.00 244.46 ? 1516 ILE A N   1 
ATOM   11560 C  CA  . ILE A 1 1516 ? -5.813   8.954   21.546  1.00 245.16 ? 1516 ILE A CA  1 
ATOM   11561 C  C   . ILE A 1 1516 ? -6.321   7.625   20.979  1.00 245.50 ? 1516 ILE A C   1 
ATOM   11562 O  O   . ILE A 1 1516 ? -7.259   7.596   20.182  1.00 243.55 ? 1516 ILE A O   1 
ATOM   11563 C  CB  . ILE A 1 1516 ? -6.653   9.419   22.789  1.00 269.26 ? 1516 ILE A CB  1 
ATOM   11564 C  CG1 . ILE A 1 1516 ? -8.104   9.764   22.422  1.00 267.96 ? 1516 ILE A CG1 1 
ATOM   11565 C  CG2 . ILE A 1 1516 ? -5.949   10.554  23.540  1.00 269.30 ? 1516 ILE A CG2 1 
ATOM   11566 C  CD1 . ILE A 1 1516 ? -9.013   8.563   22.263  1.00 268.91 ? 1516 ILE A CD1 1 
ATOM   11567 N  N   . GLN A 1 1517 ? -5.688   6.529   21.381  1.00 248.32 ? 1517 GLN A N   1 
ATOM   11568 C  CA  . GLN A 1 1517 ? -5.913   5.239   20.733  1.00 249.91 ? 1517 GLN A CA  1 
ATOM   11569 C  C   . GLN A 1 1517 ? -6.899   4.312   21.461  1.00 253.60 ? 1517 GLN A C   1 
ATOM   11570 O  O   . GLN A 1 1517 ? -7.264   4.550   22.617  1.00 255.39 ? 1517 GLN A O   1 
ATOM   11571 C  CB  . GLN A 1 1517 ? -4.573   4.506   20.536  1.00 249.42 ? 1517 GLN A CB  1 
ATOM   11572 C  CG  . GLN A 1 1517 ? -3.563   5.189   19.605  1.00 244.83 ? 1517 GLN A CG  1 
ATOM   11573 C  CD  . GLN A 1 1517 ? -2.178   4.542   19.663  1.00 243.03 ? 1517 GLN A CD  1 
ATOM   11574 O  OE1 . GLN A 1 1517 ? -1.710   4.145   20.732  1.00 243.69 ? 1517 GLN A OE1 1 
ATOM   11575 N  NE2 . GLN A 1 1517 ? -1.518   4.443   18.513  1.00 240.63 ? 1517 GLN A NE2 1 
ATOM   11576 N  N   . LYS A 1 1518 ? -7.328   3.271   20.741  1.00 254.58 ? 1518 LYS A N   1 
ATOM   11577 C  CA  . LYS A 1 1518 ? -7.996   2.078   21.283  1.00 257.67 ? 1518 LYS A CA  1 
ATOM   11578 C  C   . LYS A 1 1518 ? -7.805   0.943   20.257  1.00 260.39 ? 1518 LYS A C   1 
ATOM   11579 O  O   . LYS A 1 1518 ? -6.750   0.852   19.637  1.00 259.16 ? 1518 LYS A O   1 
ATOM   11580 C  CB  . LYS A 1 1518 ? -9.486   2.317   21.581  1.00 256.53 ? 1518 LYS A CB  1 
ATOM   11581 C  CG  . LYS A 1 1518 ? -9.844   3.719   22.078  1.00 254.78 ? 1518 LYS A CG  1 
ATOM   11582 C  CD  . LYS A 1 1518 ? -10.706  3.685   23.333  1.00 256.32 ? 1518 LYS A CD  1 
ATOM   11583 C  CE  . LYS A 1 1518 ? -11.413  2.350   23.502  1.00 258.01 ? 1518 LYS A CE  1 
ATOM   11584 N  NZ  . LYS A 1 1518 ? -10.624  1.378   24.320  1.00 260.01 ? 1518 LYS A NZ  1 
ATOM   11585 N  N   . VAL A 1 1519 ? -8.805   0.085   20.070  1.00 265.02 ? 1519 VAL A N   1 
ATOM   11586 C  CA  . VAL A 1 1519 ? -8.733   -0.954  19.032  1.00 268.88 ? 1519 VAL A CA  1 
ATOM   11587 C  C   . VAL A 1 1519 ? -10.131  -1.189  18.420  1.00 271.28 ? 1519 VAL A C   1 
ATOM   11588 O  O   . VAL A 1 1519 ? -10.396  -0.794  17.281  1.00 268.55 ? 1519 VAL A O   1 
ATOM   11589 C  CB  . VAL A 1 1519 ? -8.039   -2.278  19.560  1.00 171.55 ? 1519 VAL A CB  1 
ATOM   11590 C  CG1 . VAL A 1 1519 ? -8.513   -3.518  18.811  1.00 171.90 ? 1519 VAL A CG1 1 
ATOM   11591 C  CG2 . VAL A 1 1519 ? -6.504   -2.179  19.493  1.00 170.51 ? 1519 VAL A CG2 1 
ATOM   11592 N  N   . CYS A 1 1520 ? -11.020  -1.806  19.195  1.00 277.01 ? 1520 CYS A N   1 
ATOM   11593 C  CA  . CYS A 1 1520 ? -12.442  -1.956  18.848  1.00 280.43 ? 1520 CYS A CA  1 
ATOM   11594 C  C   . CYS A 1 1520 ? -12.807  -2.738  17.589  1.00 283.38 ? 1520 CYS A C   1 
ATOM   11595 O  O   . CYS A 1 1520 ? -12.513  -2.317  16.471  1.00 281.07 ? 1520 CYS A O   1 
ATOM   11596 C  CB  . CYS A 1 1520 ? -13.153  -0.604  18.850  1.00 278.85 ? 1520 CYS A CB  1 
ATOM   11597 S  SG  . CYS A 1 1520 ? -13.704  -0.122  20.497  1.00 347.32 ? 1520 CYS A SG  1 
ATOM   11598 N  N   . GLU A 1 1521 ? -13.489  -3.863  17.803  1.00 289.18 ? 1521 GLU A N   1 
ATOM   11599 C  CA  . GLU A 1 1521 ? -13.942  -4.750  16.730  1.00 292.09 ? 1521 GLU A CA  1 
ATOM   11600 C  C   . GLU A 1 1521 ? -15.336  -4.377  16.210  1.00 290.33 ? 1521 GLU A C   1 
ATOM   11601 O  O   . GLU A 1 1521 ? -15.615  -3.204  15.956  1.00 288.85 ? 1521 GLU A O   1 
ATOM   11602 C  CB  . GLU A 1 1521 ? -13.897  -6.218  17.188  1.00 297.50 ? 1521 GLU A CB  1 
ATOM   11603 C  CG  . GLU A 1 1521 ? -14.797  -6.560  18.378  1.00 301.65 ? 1521 GLU A CG  1 
ATOM   11604 C  CD  . GLU A 1 1521 ? -16.023  -7.370  17.981  1.00 303.01 ? 1521 GLU A CD  1 
ATOM   11605 O  OE1 . GLU A 1 1521 ? -15.876  -8.326  17.191  1.00 303.63 ? 1521 GLU A OE1 1 
ATOM   11606 O  OE2 . GLU A 1 1521 ? -17.132  -7.060  18.464  1.00 303.30 ? 1521 GLU A OE2 1 
ATOM   11607 N  N   . GLY A 1 1522 ? -16.198  -5.380  16.045  1.00 289.45 ? 1522 GLY A N   1 
ATOM   11608 C  CA  . GLY A 1 1522 ? -17.551  -5.184  15.549  1.00 285.58 ? 1522 GLY A CA  1 
ATOM   11609 C  C   . GLY A 1 1522 ? -18.468  -4.374  16.451  1.00 282.29 ? 1522 GLY A C   1 
ATOM   11610 O  O   . GLY A 1 1522 ? -19.688  -4.548  16.412  1.00 283.46 ? 1522 GLY A O   1 
ATOM   11611 N  N   . ALA A 1 1523 ? -17.868  -3.496  17.257  1.00 277.23 ? 1523 ALA A N   1 
ATOM   11612 C  CA  . ALA A 1 1523 ? -18.573  -2.569  18.152  1.00 271.62 ? 1523 ALA A CA  1 
ATOM   11613 C  C   . ALA A 1 1523 ? -18.675  -3.028  19.615  1.00 267.55 ? 1523 ALA A C   1 
ATOM   11614 O  O   . ALA A 1 1523 ? -18.790  -2.198  20.514  1.00 267.57 ? 1523 ALA A O   1 
ATOM   11615 C  CB  . ALA A 1 1523 ? -19.957  -2.187  17.595  1.00 271.14 ? 1523 ALA A CB  1 
ATOM   11616 N  N   . ALA A 1 1524 ? -18.623  -4.337  19.855  1.00 262.49 ? 1524 ALA A N   1 
ATOM   11617 C  CA  . ALA A 1 1524 ? -18.702  -4.864  21.218  1.00 257.51 ? 1524 ALA A CA  1 
ATOM   11618 C  C   . ALA A 1 1524 ? -17.549  -4.342  22.066  1.00 249.39 ? 1524 ALA A C   1 
ATOM   11619 O  O   . ALA A 1 1524 ? -17.414  -4.688  23.238  1.00 252.52 ? 1524 ALA A O   1 
ATOM   11620 C  CB  . ALA A 1 1524 ? -18.710  -6.385  21.205  1.00 259.89 ? 1524 ALA A CB  1 
ATOM   11621 N  N   . CYS A 1 1525 ? -16.719  -3.509  21.451  1.00 237.75 ? 1525 CYS A N   1 
ATOM   11622 C  CA  . CYS A 1 1525 ? -15.577  -2.900  22.116  1.00 229.27 ? 1525 CYS A CA  1 
ATOM   11623 C  C   . CYS A 1 1525 ? -15.934  -1.603  22.879  1.00 222.48 ? 1525 CYS A C   1 
ATOM   11624 O  O   . CYS A 1 1525 ? -15.706  -1.524  24.092  1.00 222.83 ? 1525 CYS A O   1 
ATOM   11625 C  CB  . CYS A 1 1525 ? -14.469  -2.655  21.092  1.00 226.18 ? 1525 CYS A CB  1 
ATOM   11626 S  SG  . CYS A 1 1525 ? -13.069  -1.669  21.666  1.00 282.43 ? 1525 CYS A SG  1 
ATOM   11627 N  N   . LYS A 1 1526 ? -16.496  -0.607  22.177  1.00 214.30 ? 1526 LYS A N   1 
ATOM   11628 C  CA  . LYS A 1 1526 ? -16.889  0.682   22.783  1.00 205.61 ? 1526 LYS A CA  1 
ATOM   11629 C  C   . LYS A 1 1526 ? -18.104  0.566   23.706  1.00 203.17 ? 1526 LYS A C   1 
ATOM   11630 O  O   . LYS A 1 1526 ? -18.894  1.498   23.812  1.00 199.97 ? 1526 LYS A O   1 
ATOM   11631 C  CB  . LYS A 1 1526 ? -17.179  1.741   21.708  1.00 198.79 ? 1526 LYS A CB  1 
ATOM   11632 C  CG  . LYS A 1 1526 ? -15.971  2.232   20.927  1.00 193.78 ? 1526 LYS A CG  1 
ATOM   11633 C  CD  . LYS A 1 1526 ? -16.408  2.990   19.679  1.00 189.06 ? 1526 LYS A CD  1 
ATOM   11634 C  CE  . LYS A 1 1526 ? -15.449  2.742   18.515  1.00 185.99 ? 1526 LYS A CE  1 
ATOM   11635 N  NZ  . LYS A 1 1526 ? -15.230  1.277   18.258  1.00 185.67 ? 1526 LYS A NZ  1 
ATOM   11636 N  N   . CYS A 1 1527 ? -18.252  -0.580  24.362  1.00 205.40 ? 1527 CYS A N   1 
ATOM   11637 C  CA  . CYS A 1 1527 ? -19.375  -0.821  25.262  1.00 207.44 ? 1527 CYS A CA  1 
ATOM   11638 C  C   . CYS A 1 1527 ? -18.906  -1.587  26.481  1.00 211.80 ? 1527 CYS A C   1 
ATOM   11639 O  O   . CYS A 1 1527 ? -19.438  -1.413  27.576  1.00 213.78 ? 1527 CYS A O   1 
ATOM   11640 C  CB  . CYS A 1 1527 ? -20.484  -1.610  24.568  1.00 206.59 ? 1527 CYS A CB  1 
ATOM   11641 S  SG  . CYS A 1 1527 ? -22.102  -1.418  25.352  1.00 232.15 ? 1527 CYS A SG  1 
ATOM   11642 N  N   . VAL A 1 1528 ? -17.909  -2.443  26.291  1.00 214.67 ? 1528 VAL A N   1 
ATOM   11643 C  CA  . VAL A 1 1528 ? -17.268  -3.091  27.427  1.00 221.07 ? 1528 VAL A CA  1 
ATOM   11644 C  C   . VAL A 1 1528 ? -16.660  -1.973  28.273  1.00 225.31 ? 1528 VAL A C   1 
ATOM   11645 O  O   . VAL A 1 1528 ? -16.324  -2.154  29.447  1.00 228.10 ? 1528 VAL A O   1 
ATOM   11646 C  CB  . VAL A 1 1528 ? -16.207  -4.135  26.988  1.00 227.21 ? 1528 VAL A CB  1 
ATOM   11647 C  CG1 . VAL A 1 1528 ? -15.495  -4.736  28.197  1.00 229.62 ? 1528 VAL A CG1 1 
ATOM   11648 C  CG2 . VAL A 1 1528 ? -16.860  -5.239  26.156  1.00 227.23 ? 1528 VAL A CG2 1 
ATOM   11649 N  N   . GLU A 1 1529 ? -16.532  -0.808  27.648  1.00 226.51 ? 1529 GLU A N   1 
ATOM   11650 C  CA  . GLU A 1 1529 ? -16.186  0.419   28.344  1.00 230.16 ? 1529 GLU A CA  1 
ATOM   11651 C  C   . GLU A 1 1529 ? -17.419  1.317   28.425  1.00 228.26 ? 1529 GLU A C   1 
ATOM   11652 O  O   . GLU A 1 1529 ? -17.623  2.186   27.571  1.00 226.28 ? 1529 GLU A O   1 
ATOM   11653 C  CB  . GLU A 1 1529 ? -15.057  1.135   27.607  1.00 232.98 ? 1529 GLU A CB  1 
ATOM   11654 C  CG  . GLU A 1 1529 ? -15.263  1.206   26.106  1.00 234.38 ? 1529 GLU A CG  1 
ATOM   11655 C  CD  . GLU A 1 1529 ? -14.238  2.083   25.422  1.00 234.85 ? 1529 GLU A CD  1 
ATOM   11656 O  OE1 . GLU A 1 1529 ? -13.450  2.736   26.139  1.00 235.98 ? 1529 GLU A OE1 1 
ATOM   11657 O  OE2 . GLU A 1 1529 ? -14.222  2.119   24.170  1.00 233.78 ? 1529 GLU A OE2 1 
ATOM   11658 N  N   . ALA A 1 1530 ? -18.224  1.112   29.466  1.00 228.15 ? 1530 ALA A N   1 
ATOM   11659 C  CA  . ALA A 1 1530 ? -19.531  1.768   29.607  1.00 225.78 ? 1530 ALA A CA  1 
ATOM   11660 C  C   . ALA A 1 1530 ? -19.582  3.254   29.210  1.00 220.98 ? 1530 ALA A C   1 
ATOM   11661 O  O   . ALA A 1 1530 ? -20.466  3.692   28.469  1.00 216.20 ? 1530 ALA A O   1 
ATOM   11662 C  CB  . ALA A 1 1530 ? -20.053  1.585   31.044  1.00 227.85 ? 1530 ALA A CB  1 
ATOM   11663 N  N   . ASP A 1 1531 ? -18.616  4.015   29.697  1.00 220.97 ? 1531 ASP A N   1 
ATOM   11664 C  CA  . ASP A 1 1531 ? -18.709  5.455   29.701  1.00 218.96 ? 1531 ASP A CA  1 
ATOM   11665 C  C   . ASP A 1 1531 ? -17.601  5.870   30.641  1.00 225.89 ? 1531 ASP A C   1 
ATOM   11666 O  O   . ASP A 1 1531 ? -17.159  7.014   30.637  1.00 224.30 ? 1531 ASP A O   1 
ATOM   11667 C  CB  . ASP A 1 1531 ? -20.080  5.858   30.260  1.00 213.62 ? 1531 ASP A CB  1 
ATOM   11668 C  CG  . ASP A 1 1531 ? -20.176  7.338   30.623  1.00 206.40 ? 1531 ASP A CG  1 
ATOM   11669 O  OD1 . ASP A 1 1531 ? -19.220  8.097   30.370  1.00 203.33 ? 1531 ASP A OD1 1 
ATOM   11670 O  OD2 . ASP A 1 1531 ? -21.226  7.748   31.168  1.00 203.88 ? 1531 ASP A OD2 1 
ATOM   11671 N  N   . CYS A 1 1532 ? -17.137  4.897   31.424  1.00 235.23 ? 1532 CYS A N   1 
ATOM   11672 C  CA  . CYS A 1 1532 ? -16.197  5.116   32.527  1.00 245.21 ? 1532 CYS A CA  1 
ATOM   11673 C  C   . CYS A 1 1532 ? -15.157  6.216   32.293  1.00 254.27 ? 1532 CYS A C   1 
ATOM   11674 O  O   . CYS A 1 1532 ? -14.868  6.588   31.159  1.00 250.85 ? 1532 CYS A O   1 
ATOM   11675 C  CB  . CYS A 1 1532 ? -15.517  3.801   32.924  1.00 246.25 ? 1532 CYS A CB  1 
ATOM   11676 S  SG  . CYS A 1 1532 ? -14.575  3.003   31.611  1.00 205.88 ? 1532 CYS A SG  1 
ATOM   11677 N  N   . GLY A 1 1533 ? -14.590  6.713   33.389  1.00 225.30 ? 1533 GLY A N   1 
ATOM   11678 C  CA  . GLY A 1 1533 ? -13.851  7.966   33.395  1.00 236.72 ? 1533 GLY A CA  1 
ATOM   11679 C  C   . GLY A 1 1533 ? -12.460  8.050   32.788  1.00 245.89 ? 1533 GLY A C   1 
ATOM   11680 O  O   . GLY A 1 1533 ? -11.955  7.095   32.200  1.00 247.30 ? 1533 GLY A O   1 
ATOM   11681 N  N   . GLN A 1 1534 ? -11.837  9.215   32.967  1.00 253.48 ? 1534 GLN A N   1 
ATOM   11682 C  CA  . GLN A 1 1534 ? -10.546  9.542   32.362  1.00 260.57 ? 1534 GLN A CA  1 
ATOM   11683 C  C   . GLN A 1 1534 ? -9.583   10.191  33.364  1.00 255.21 ? 1534 GLN A C   1 
ATOM   11684 O  O   . GLN A 1 1534 ? -9.954   11.123  34.073  1.00 255.62 ? 1534 GLN A O   1 
ATOM   11685 C  CB  . GLN A 1 1534 ? -10.757  10.504  31.187  1.00 273.55 ? 1534 GLN A CB  1 
ATOM   11686 C  CG  . GLN A 1 1534 ? -10.961  11.979  31.588  1.00 285.38 ? 1534 GLN A CG  1 
ATOM   11687 C  CD  . GLN A 1 1534 ? -12.367  12.292  32.086  1.00 294.94 ? 1534 GLN A CD  1 
ATOM   11688 O  OE1 . GLN A 1 1534 ? -13.062  11.430  32.625  1.00 298.15 ? 1534 GLN A OE1 1 
ATOM   11689 N  NE2 . GLN A 1 1534 ? -12.789  13.541  31.906  1.00 298.28 ? 1534 GLN A NE2 1 
ATOM   11690 N  N   . MET A 1 1535 ? -8.348   9.699   33.420  1.00 248.07 ? 1535 MET A N   1 
ATOM   11691 C  CA  . MET A 1 1535 ? -7.313   10.340  34.224  1.00 239.24 ? 1535 MET A CA  1 
ATOM   11692 C  C   . MET A 1 1535 ? -6.356   11.131  33.338  1.00 229.29 ? 1535 MET A C   1 
ATOM   11693 O  O   . MET A 1 1535 ? -5.509   10.553  32.658  1.00 228.55 ? 1535 MET A O   1 
ATOM   11694 C  CB  . MET A 1 1535 ? -6.529   9.321   35.068  1.00 238.82 ? 1535 MET A CB  1 
ATOM   11695 C  CG  . MET A 1 1535 ? -6.301   7.983   34.386  1.00 238.20 ? 1535 MET A CG  1 
ATOM   11696 S  SD  . MET A 1 1535 ? -4.556   7.522   34.259  1.00 236.54 ? 1535 MET A SD  1 
ATOM   11697 C  CE  . MET A 1 1535 ? -4.663   5.977   33.353  1.00 134.00 ? 1535 MET A CE  1 
ATOM   11698 N  N   . GLN A 1 1536 ? -6.491   12.452  33.343  1.00 220.51 ? 1536 GLN A N   1 
ATOM   11699 C  CA  . GLN A 1 1536 ? -5.663   13.287  32.483  1.00 212.25 ? 1536 GLN A CA  1 
ATOM   11700 C  C   . GLN A 1 1536 ? -4.198   12.856  32.593  1.00 209.65 ? 1536 GLN A C   1 
ATOM   11701 O  O   . GLN A 1 1536 ? -3.792   12.293  33.607  1.00 210.24 ? 1536 GLN A O   1 
ATOM   11702 C  CB  . GLN A 1 1536 ? -5.852   14.770  32.824  1.00 207.20 ? 1536 GLN A CB  1 
ATOM   11703 C  CG  . GLN A 1 1536 ? -7.161   15.363  32.310  1.00 203.60 ? 1536 GLN A CG  1 
ATOM   11704 C  CD  . GLN A 1 1536 ? -7.123   15.709  30.816  1.00 200.50 ? 1536 GLN A CD  1 
ATOM   11705 O  OE1 . GLN A 1 1536 ? -6.319   16.533  30.371  1.00 198.71 ? 1536 GLN A OE1 1 
ATOM   11706 N  NE2 . GLN A 1 1536 ? -8.024   15.102  30.046  1.00 199.80 ? 1536 GLN A NE2 1 
ATOM   11707 N  N   . GLU A 1 1537 ? -3.420   13.092  31.539  1.00 206.92 ? 1537 GLU A N   1 
ATOM   11708 C  CA  . GLU A 1 1537 ? -2.009   12.692  31.503  1.00 204.17 ? 1537 GLU A CA  1 
ATOM   11709 C  C   . GLU A 1 1537 ? -1.183   13.382  32.584  1.00 205.35 ? 1537 GLU A C   1 
ATOM   11710 O  O   . GLU A 1 1537 ? -1.464   14.528  32.924  1.00 204.20 ? 1537 GLU A O   1 
ATOM   11711 C  CB  . GLU A 1 1537 ? -1.411   13.032  30.139  1.00 199.88 ? 1537 GLU A CB  1 
ATOM   11712 C  CG  . GLU A 1 1537 ? -1.846   12.118  29.029  1.00 195.64 ? 1537 GLU A CG  1 
ATOM   11713 C  CD  . GLU A 1 1537 ? -1.103   10.814  29.062  1.00 192.22 ? 1537 GLU A CD  1 
ATOM   11714 O  OE1 . GLU A 1 1537 ? -0.611   10.428  30.147  1.00 190.50 ? 1537 GLU A OE1 1 
ATOM   11715 O  OE2 . GLU A 1 1537 ? -1.003   10.182  27.993  1.00 191.73 ? 1537 GLU A OE2 1 
ATOM   11716 N  N   . GLU A 1 1538 ? -0.161   12.698  33.106  1.00 207.75 ? 1538 GLU A N   1 
ATOM   11717 C  CA  . GLU A 1 1538 ? 0.749    13.309  34.086  1.00 210.24 ? 1538 GLU A CA  1 
ATOM   11718 C  C   . GLU A 1 1538 ? 1.414    14.524  33.451  1.00 216.74 ? 1538 GLU A C   1 
ATOM   11719 O  O   . GLU A 1 1538 ? 1.486    14.596  32.225  1.00 218.31 ? 1538 GLU A O   1 
ATOM   11720 C  CB  . GLU A 1 1538 ? 1.808    12.310  34.575  1.00 204.62 ? 1538 GLU A CB  1 
ATOM   11721 C  CG  . GLU A 1 1538 ? 3.022    12.951  35.271  1.00 198.51 ? 1538 GLU A CG  1 
ATOM   11722 C  CD  . GLU A 1 1538 ? 2.980    12.880  36.794  1.00 193.45 ? 1538 GLU A CD  1 
ATOM   11723 O  OE1 . GLU A 1 1538 ? 1.954    12.459  37.370  1.00 191.63 ? 1538 GLU A OE1 1 
ATOM   11724 O  OE2 . GLU A 1 1538 ? 3.997    13.240  37.417  1.00 191.49 ? 1538 GLU A OE2 1 
ATOM   11725 N  N   . LEU A 1 1539 ? 1.890    15.461  34.284  1.00 221.07 ? 1539 LEU A N   1 
ATOM   11726 C  CA  . LEU A 1 1539 ? 2.425    16.759  33.839  1.00 225.51 ? 1539 LEU A CA  1 
ATOM   11727 C  C   . LEU A 1 1539 ? 1.361    17.552  33.074  1.00 229.64 ? 1539 LEU A C   1 
ATOM   11728 O  O   . LEU A 1 1539 ? 0.259    17.050  32.851  1.00 229.17 ? 1539 LEU A O   1 
ATOM   11729 C  CB  . LEU A 1 1539 ? 3.711    16.582  33.007  1.00 227.75 ? 1539 LEU A CB  1 
ATOM   11730 C  CG  . LEU A 1 1539 ? 3.773    15.611  31.811  1.00 231.68 ? 1539 LEU A CG  1 
ATOM   11731 C  CD1 . LEU A 1 1539 ? 3.281    16.257  30.510  1.00 233.51 ? 1539 LEU A CD1 1 
ATOM   11732 C  CD2 . LEU A 1 1539 ? 5.167    15.027  31.625  1.00 232.06 ? 1539 LEU A CD2 1 
ATOM   11733 N  N   . ASP A 1 1540 ? 1.665    18.784  32.672  1.00 234.05 ? 1540 ASP A N   1 
ATOM   11734 C  CA  . ASP A 1 1540 ? 0.738    19.502  31.787  1.00 237.78 ? 1540 ASP A CA  1 
ATOM   11735 C  C   . ASP A 1 1540 ? 1.301    20.716  31.056  1.00 245.53 ? 1540 ASP A C   1 
ATOM   11736 O  O   . ASP A 1 1540 ? 2.147    21.447  31.580  1.00 245.77 ? 1540 ASP A O   1 
ATOM   11737 C  CB  . ASP A 1 1540 ? -0.552   19.887  32.510  1.00 231.86 ? 1540 ASP A CB  1 
ATOM   11738 C  CG  . ASP A 1 1540 ? -1.769   19.158  31.965  1.00 224.12 ? 1540 ASP A CG  1 
ATOM   11739 O  OD1 . ASP A 1 1540 ? -1.608   18.190  31.184  1.00 219.41 ? 1540 ASP A OD1 1 
ATOM   11740 O  OD2 . ASP A 1 1540 ? -2.893   19.568  32.320  1.00 222.96 ? 1540 ASP A OD2 1 
ATOM   11741 N  N   . LEU A 1 1541 ? 0.794    20.916  29.839  1.00 252.96 ? 1541 LEU A N   1 
ATOM   11742 C  CA  . LEU A 1 1541 ? 1.229    21.990  28.945  1.00 260.73 ? 1541 LEU A CA  1 
ATOM   11743 C  C   . LEU A 1 1541 ? 0.534    23.324  29.233  1.00 271.89 ? 1541 LEU A C   1 
ATOM   11744 O  O   . LEU A 1 1541 ? -0.617   23.346  29.666  1.00 274.22 ? 1541 LEU A O   1 
ATOM   11745 C  CB  . LEU A 1 1541 ? 1.023    21.579  27.475  1.00 258.92 ? 1541 LEU A CB  1 
ATOM   11746 C  CG  . LEU A 1 1541 ? -0.277   20.882  27.050  1.00 259.47 ? 1541 LEU A CG  1 
ATOM   11747 C  CD1 . LEU A 1 1541 ? -1.403   21.875  26.802  1.00 260.00 ? 1541 LEU A CD1 1 
ATOM   11748 C  CD2 . LEU A 1 1541 ? -0.032   20.050  25.804  1.00 259.40 ? 1541 LEU A CD2 1 
ATOM   11749 N  N   . THR A 1 1542 ? 1.237    24.430  28.988  1.00 280.42 ? 1542 THR A N   1 
ATOM   11750 C  CA  . THR A 1 1542 ? 0.679    25.774  29.180  1.00 289.01 ? 1542 THR A CA  1 
ATOM   11751 C  C   . THR A 1 1542 ? -0.521   26.051  28.248  1.00 294.81 ? 1542 THR A C   1 
ATOM   11752 O  O   . THR A 1 1542 ? -0.730   25.326  27.271  1.00 296.30 ? 1542 THR A O   1 
ATOM   11753 C  CB  . THR A 1 1542 ? 1.770    26.867  29.049  1.00 290.52 ? 1542 THR A CB  1 
ATOM   11754 O  OG1 . THR A 1 1542 ? 2.564    26.619  27.882  1.00 290.29 ? 1542 THR A OG1 1 
ATOM   11755 C  CG2 . THR A 1 1542 ? 2.679    26.860  30.277  1.00 291.38 ? 1542 THR A CG2 1 
ATOM   11756 N  N   . ILE A 1 1543 ? -1.289   27.101  28.553  1.00 297.69 ? 1543 ILE A N   1 
ATOM   11757 C  CA  . ILE A 1 1543 ? -2.637   27.328  27.997  1.00 299.26 ? 1543 ILE A CA  1 
ATOM   11758 C  C   . ILE A 1 1543 ? -3.659   26.516  28.803  1.00 300.17 ? 1543 ILE A C   1 
ATOM   11759 O  O   . ILE A 1 1543 ? -4.192   25.517  28.313  1.00 300.52 ? 1543 ILE A O   1 
ATOM   11760 C  CB  . ILE A 1 1543 ? -2.762   26.967  26.473  1.00 254.34 ? 1543 ILE A CB  1 
ATOM   11761 C  CG1 . ILE A 1 1543 ? -1.798   27.794  25.617  1.00 252.84 ? 1543 ILE A CG1 1 
ATOM   11762 C  CG2 . ILE A 1 1543 ? -4.193   27.171  25.973  1.00 254.93 ? 1543 ILE A CG2 1 
ATOM   11763 C  CD1 . ILE A 1 1543 ? -1.853   27.453  24.138  1.00 251.68 ? 1543 ILE A CD1 1 
ATOM   11764 N  N   . SER A 1 1544 ? -3.935   26.946  30.036  1.00 299.58 ? 1544 SER A N   1 
ATOM   11765 C  CA  . SER A 1 1544 ? -4.788   26.156  30.930  1.00 298.80 ? 1544 SER A CA  1 
ATOM   11766 C  C   . SER A 1 1544 ? -5.492   26.922  32.053  1.00 297.18 ? 1544 SER A C   1 
ATOM   11767 O  O   . SER A 1 1544 ? -6.471   26.428  32.601  1.00 297.00 ? 1544 SER A O   1 
ATOM   11768 C  CB  . SER A 1 1544 ? -4.001   25.002  31.557  1.00 299.18 ? 1544 SER A CB  1 
ATOM   11769 O  OG  . SER A 1 1544 ? -3.654   25.300  32.899  1.00 299.40 ? 1544 SER A OG  1 
ATOM   11770 N  N   . ALA A 1 1545 ? -5.007   28.100  32.427  1.00 295.00 ? 1545 ALA A N   1 
ATOM   11771 C  CA  . ALA A 1 1545 ? -5.696   28.851  33.474  1.00 292.25 ? 1545 ALA A CA  1 
ATOM   11772 C  C   . ALA A 1 1545 ? -7.151   29.104  33.062  1.00 286.34 ? 1545 ALA A C   1 
ATOM   11773 O  O   . ALA A 1 1545 ? -8.013   29.317  33.919  1.00 289.35 ? 1545 ALA A O   1 
ATOM   11774 C  CB  . ALA A 1 1545 ? -4.976   30.153  33.782  1.00 293.58 ? 1545 ALA A CB  1 
ATOM   11775 N  N   . GLU A 1 1546 ? -7.403   29.062  31.747  1.00 276.96 ? 1546 GLU A N   1 
ATOM   11776 C  CA  . GLU A 1 1546 ? -8.752   29.178  31.165  1.00 269.45 ? 1546 GLU A CA  1 
ATOM   11777 C  C   . GLU A 1 1546 ? -9.530   27.845  31.122  1.00 265.49 ? 1546 GLU A C   1 
ATOM   11778 O  O   . GLU A 1 1546 ? -10.744  27.830  31.328  1.00 265.16 ? 1546 GLU A O   1 
ATOM   11779 C  CB  . GLU A 1 1546 ? -8.720   29.840  29.760  1.00 302.98 ? 1546 GLU A CB  1 
ATOM   11780 C  CG  . GLU A 1 1546 ? -8.107   28.991  28.619  1.00 300.19 ? 1546 GLU A CG  1 
ATOM   11781 C  CD  . GLU A 1 1546 ? -8.370   29.546  27.206  1.00 295.94 ? 1546 GLU A CD  1 
ATOM   11782 O  OE1 . GLU A 1 1546 ? -9.331   30.321  27.018  1.00 294.54 ? 1546 GLU A OE1 1 
ATOM   11783 O  OE2 . GLU A 1 1546 ? -7.615   29.190  26.272  1.00 293.94 ? 1546 GLU A OE2 1 
ATOM   11784 N  N   . THR A 1 1547 ? -8.832   26.740  30.854  1.00 260.87 ? 1547 THR A N   1 
ATOM   11785 C  CA  . THR A 1 1547 ? -9.447   25.406  30.796  1.00 255.91 ? 1547 THR A CA  1 
ATOM   11786 C  C   . THR A 1 1547 ? -9.781   24.845  32.182  1.00 252.82 ? 1547 THR A C   1 
ATOM   11787 O  O   . THR A 1 1547 ? -10.735  24.078  32.339  1.00 244.54 ? 1547 THR A O   1 
ATOM   11788 C  CB  . THR A 1 1547 ? -8.520   24.390  30.090  1.00 253.60 ? 1547 THR A CB  1 
ATOM   11789 O  OG1 . THR A 1 1547 ? -8.105   24.903  28.818  1.00 252.14 ? 1547 THR A OG1 1 
ATOM   11790 C  CG2 . THR A 1 1547 ? -9.231   23.057  29.897  1.00 253.48 ? 1547 THR A CG2 1 
ATOM   11791 N  N   . ARG A 1 1548 ? -8.973   25.237  33.170  1.00 258.03 ? 1548 ARG A N   1 
ATOM   11792 C  CA  . ARG A 1 1548 ? -9.055   24.753  34.560  1.00 259.03 ? 1548 ARG A CA  1 
ATOM   11793 C  C   . ARG A 1 1548 ? -10.260  25.338  35.315  1.00 254.43 ? 1548 ARG A C   1 
ATOM   11794 O  O   . ARG A 1 1548 ? -11.058  24.601  35.906  1.00 254.42 ? 1548 ARG A O   1 
ATOM   11795 C  CB  . ARG A 1 1548 ? -7.738   25.042  35.327  1.00 214.57 ? 1548 ARG A CB  1 
ATOM   11796 C  CG  . ARG A 1 1548 ? -6.479   24.238  34.874  1.00 156.50 ? 1548 ARG A CG  1 
ATOM   11797 C  CD  . ARG A 1 1548 ? -6.386   22.893  35.572  1.00 148.09 ? 1548 ARG A CD  1 
ATOM   11798 N  NE  . ARG A 1 1548 ? -7.714   22.314  35.727  1.00 149.43 ? 1548 ARG A NE  1 
ATOM   11799 C  CZ  . ARG A 1 1548 ? -8.021   21.356  36.582  1.00 152.33 ? 1548 ARG A CZ  1 
ATOM   11800 N  NH1 . ARG A 1 1548 ? -7.087   20.871  37.364  1.00 155.89 ? 1548 ARG A NH1 1 
ATOM   11801 N  NH2 . ARG A 1 1548 ? -9.258   20.896  36.659  1.00 150.71 ? 1548 ARG A NH2 1 
ATOM   11802 N  N   . LYS A 1 1549 ? -10.389  26.661  35.296  1.00 250.61 ? 1549 LYS A N   1 
ATOM   11803 C  CA  . LYS A 1 1549 ? -11.586  27.302  35.821  1.00 250.12 ? 1549 LYS A CA  1 
ATOM   11804 C  C   . LYS A 1 1549 ? -12.851  26.684  35.186  1.00 256.83 ? 1549 LYS A C   1 
ATOM   11805 O  O   . LYS A 1 1549 ? -13.612  26.005  35.872  1.00 258.09 ? 1549 LYS A O   1 
ATOM   11806 C  CB  . LYS A 1 1549 ? -11.531  28.818  35.585  1.00 245.86 ? 1549 LYS A CB  1 
ATOM   11807 C  CG  . LYS A 1 1549 ? -12.530  29.622  36.414  1.00 245.19 ? 1549 LYS A CG  1 
ATOM   11808 C  CD  . LYS A 1 1549 ? -12.979  30.898  35.707  1.00 244.36 ? 1549 LYS A CD  1 
ATOM   11809 C  CE  . LYS A 1 1549 ? -11.949  32.009  35.813  1.00 243.46 ? 1549 LYS A CE  1 
ATOM   11810 N  NZ  . LYS A 1 1549 ? -12.522  33.320  35.399  1.00 242.32 ? 1549 LYS A NZ  1 
ATOM   11811 N  N   . GLN A 1 1550 ? -13.044  26.890  33.878  1.00 263.42 ? 1550 GLN A N   1 
ATOM   11812 C  CA  . GLN A 1 1550 ? -14.253  26.453  33.151  1.00 270.39 ? 1550 GLN A CA  1 
ATOM   11813 C  C   . GLN A 1 1550 ? -14.729  25.035  33.472  1.00 277.89 ? 1550 GLN A C   1 
ATOM   11814 O  O   . GLN A 1 1550 ? -15.929  24.762  33.458  1.00 278.36 ? 1550 GLN A O   1 
ATOM   11815 C  CB  . GLN A 1 1550 ? -14.053  26.561  31.633  1.00 270.19 ? 1550 GLN A CB  1 
ATOM   11816 C  CG  . GLN A 1 1550 ? -13.591  27.915  31.137  1.00 270.00 ? 1550 GLN A CG  1 
ATOM   11817 C  CD  . GLN A 1 1550 ? -14.728  28.820  30.748  1.00 270.12 ? 1550 GLN A CD  1 
ATOM   11818 O  OE1 . GLN A 1 1550 ? -15.671  28.400  30.080  1.00 270.14 ? 1550 GLN A OE1 1 
ATOM   11819 N  NE2 . GLN A 1 1550 ? -14.639  30.080  31.150  1.00 270.26 ? 1550 GLN A NE2 1 
ATOM   11820 N  N   . THR A 1 1551 ? -13.795  24.126  33.729  1.00 284.62 ? 1551 THR A N   1 
ATOM   11821 C  CA  . THR A 1 1551 ? -14.158  22.747  34.033  1.00 290.92 ? 1551 THR A CA  1 
ATOM   11822 C  C   . THR A 1 1551 ? -14.850  22.670  35.384  1.00 295.28 ? 1551 THR A C   1 
ATOM   11823 O  O   . THR A 1 1551 ? -15.222  21.590  35.837  1.00 296.19 ? 1551 THR A O   1 
ATOM   11824 C  CB  . THR A 1 1551 ? -12.931  21.830  34.056  1.00 292.37 ? 1551 THR A CB  1 
ATOM   11825 O  OG1 . THR A 1 1551 ? -11.925  22.417  34.887  1.00 293.27 ? 1551 THR A OG1 1 
ATOM   11826 C  CG2 . THR A 1 1551 ? -12.378  21.623  32.651  1.00 291.73 ? 1551 THR A CG2 1 
ATOM   11827 N  N   . ALA A 1 1552 ? -15.010  23.822  36.025  1.00 298.49 ? 1552 ALA A N   1 
ATOM   11828 C  CA  . ALA A 1 1552 ? -15.644  23.889  37.338  1.00 301.70 ? 1552 ALA A CA  1 
ATOM   11829 C  C   . ALA A 1 1552 ? -17.158  24.123  37.275  1.00 301.44 ? 1552 ALA A C   1 
ATOM   11830 O  O   . ALA A 1 1552 ? -17.923  23.180  37.136  1.00 305.22 ? 1552 ALA A O   1 
ATOM   11831 C  CB  . ALA A 1 1552 ? -14.971  24.945  38.200  1.00 303.39 ? 1552 ALA A CB  1 
ATOM   11832 N  N   . CYS A 1 1553 ? -17.587  25.380  37.356  1.00 295.08 ? 1553 CYS A N   1 
ATOM   11833 C  CA  . CYS A 1 1553 ? -19.011  25.694  37.514  1.00 287.30 ? 1553 CYS A CA  1 
ATOM   11834 C  C   . CYS A 1 1553 ? -19.943  25.244  36.371  1.00 280.38 ? 1553 CYS A C   1 
ATOM   11835 O  O   . CYS A 1 1553 ? -21.162  25.367  36.501  1.00 282.48 ? 1553 CYS A O   1 
ATOM   11836 C  CB  . CYS A 1 1553 ? -19.216  27.205  37.631  1.00 291.55 ? 1553 CYS A CB  1 
ATOM   11837 S  SG  . CYS A 1 1553 ? -17.681  28.182  37.550  1.00 414.93 ? 1553 CYS A SG  1 
ATOM   11838 N  N   . LYS A 1 1554 ? -19.386  24.742  35.264  1.00 269.14 ? 1554 LYS A N   1 
ATOM   11839 C  CA  . LYS A 1 1554 ? -20.200  24.180  34.178  1.00 255.21 ? 1554 LYS A CA  1 
ATOM   11840 C  C   . LYS A 1 1554 ? -21.271  23.309  34.816  1.00 242.46 ? 1554 LYS A C   1 
ATOM   11841 O  O   . LYS A 1 1554 ? -20.976  22.219  35.293  1.00 242.84 ? 1554 LYS A O   1 
ATOM   11842 C  CB  . LYS A 1 1554 ? -19.342  23.341  33.217  1.00 253.25 ? 1554 LYS A CB  1 
ATOM   11843 C  CG  . LYS A 1 1554 ? -20.127  22.577  32.137  1.00 250.85 ? 1554 LYS A CG  1 
ATOM   11844 C  CD  . LYS A 1 1554 ? -20.395  23.438  30.899  1.00 248.63 ? 1554 LYS A CD  1 
ATOM   11845 C  CE  . LYS A 1 1554 ? -21.150  22.685  29.796  1.00 247.12 ? 1554 LYS A CE  1 
ATOM   11846 N  NZ  . LYS A 1 1554 ? -22.637  22.742  29.939  1.00 246.57 ? 1554 LYS A NZ  1 
ATOM   11847 N  N   . PRO A 1 1555 ? -22.521  23.796  34.817  1.00 228.70 ? 1555 PRO A N   1 
ATOM   11848 C  CA  . PRO A 1 1555 ? -23.657  23.331  35.632  1.00 219.16 ? 1555 PRO A CA  1 
ATOM   11849 C  C   . PRO A 1 1555 ? -23.815  21.816  35.813  1.00 208.12 ? 1555 PRO A C   1 
ATOM   11850 O  O   . PRO A 1 1555 ? -24.394  21.399  36.822  1.00 208.03 ? 1555 PRO A O   1 
ATOM   11851 C  CB  . PRO A 1 1555 ? -24.860  23.920  34.907  1.00 219.94 ? 1555 PRO A CB  1 
ATOM   11852 C  CG  . PRO A 1 1555 ? -24.339  25.179  34.304  1.00 221.47 ? 1555 PRO A CG  1 
ATOM   11853 C  CD  . PRO A 1 1555 ? -22.900  24.917  33.938  1.00 224.26 ? 1555 PRO A CD  1 
ATOM   11854 N  N   . GLU A 1 1556 ? -23.326  21.019  34.864  1.00 197.87 ? 1556 GLU A N   1 
ATOM   11855 C  CA  . GLU A 1 1556 ? -23.254  19.571  35.054  1.00 189.17 ? 1556 GLU A CA  1 
ATOM   11856 C  C   . GLU A 1 1556 ? -22.243  19.196  36.153  1.00 184.07 ? 1556 GLU A C   1 
ATOM   11857 O  O   . GLU A 1 1556 ? -22.022  18.009  36.421  1.00 184.95 ? 1556 GLU A O   1 
ATOM   11858 C  CB  . GLU A 1 1556 ? -22.937  18.828  33.738  1.00 186.27 ? 1556 GLU A CB  1 
ATOM   11859 C  CG  . GLU A 1 1556 ? -22.091  19.581  32.708  1.00 183.60 ? 1556 GLU A CG  1 
ATOM   11860 C  CD  . GLU A 1 1556 ? -22.911  20.056  31.529  1.00 181.64 ? 1556 GLU A CD  1 
ATOM   11861 O  OE1 . GLU A 1 1556 ? -22.402  20.022  30.388  1.00 180.65 ? 1556 GLU A OE1 1 
ATOM   11862 O  OE2 . GLU A 1 1556 ? -24.075  20.450  31.743  1.00 181.56 ? 1556 GLU A OE2 1 
ATOM   11863 N  N   . ILE A 1 1557 ? -21.634  20.214  36.773  1.00 177.67 ? 1557 ILE A N   1 
ATOM   11864 C  CA  . ILE A 1 1557 ? -20.652  20.043  37.860  1.00 170.49 ? 1557 ILE A CA  1 
ATOM   11865 C  C   . ILE A 1 1557 ? -21.236  20.386  39.237  1.00 166.42 ? 1557 ILE A C   1 
ATOM   11866 O  O   . ILE A 1 1557 ? -21.135  21.518  39.734  1.00 165.27 ? 1557 ILE A O   1 
ATOM   11867 C  CB  . ILE A 1 1557 ? -19.375  20.872  37.615  1.00 166.72 ? 1557 ILE A CB  1 
ATOM   11868 C  CG1 . ILE A 1 1557 ? -18.469  20.204  36.556  1.00 165.53 ? 1557 ILE A CG1 1 
ATOM   11869 C  CG2 . ILE A 1 1557 ? -18.650  21.138  38.925  1.00 165.29 ? 1557 ILE A CG2 1 
ATOM   11870 C  CD1 . ILE A 1 1557 ? -18.080  18.749  36.820  1.00 165.00 ? 1557 ILE A CD1 1 
ATOM   11871 N  N   . ALA A 1 1558 ? -21.846  19.370  39.838  1.00 163.26 ? 1558 ALA A N   1 
ATOM   11872 C  CA  . ALA A 1 1558 ? -22.597  19.510  41.072  1.00 159.88 ? 1558 ALA A CA  1 
ATOM   11873 C  C   . ALA A 1 1558 ? -21.629  19.473  42.213  1.00 158.11 ? 1558 ALA A C   1 
ATOM   11874 O  O   . ALA A 1 1558 ? -22.000  19.199  43.351  1.00 158.73 ? 1558 ALA A O   1 
ATOM   11875 C  CB  . ALA A 1 1558 ? -23.605  18.387  41.208  1.00 158.89 ? 1558 ALA A CB  1 
ATOM   11876 N  N   . TYR A 1 1559 ? -20.371  19.720  41.886  1.00 157.03 ? 1559 TYR A N   1 
ATOM   11877 C  CA  . TYR A 1 1559 ? -19.338  19.820  42.897  1.00 158.31 ? 1559 TYR A CA  1 
ATOM   11878 C  C   . TYR A 1 1559 ? -17.956  19.940  42.279  1.00 157.50 ? 1559 TYR A C   1 
ATOM   11879 O  O   . TYR A 1 1559 ? -17.748  19.664  41.117  1.00 154.68 ? 1559 TYR A O   1 
ATOM   11880 C  CB  . TYR A 1 1559 ? -19.412  18.647  43.897  1.00 160.26 ? 1559 TYR A CB  1 
ATOM   11881 C  CG  . TYR A 1 1559 ? -19.056  17.272  43.347  1.00 161.80 ? 1559 TYR A CG  1 
ATOM   11882 C  CD1 . TYR A 1 1559 ? -19.922  16.190  43.489  1.00 162.36 ? 1559 TYR A CD1 1 
ATOM   11883 C  CD2 . TYR A 1 1559 ? -17.836  17.047  42.715  1.00 161.97 ? 1559 TYR A CD2 1 
ATOM   11884 C  CE1 . TYR A 1 1559 ? -19.575  14.921  43.002  1.00 161.89 ? 1559 TYR A CE1 1 
ATOM   11885 C  CE2 . TYR A 1 1559 ? -17.493  15.791  42.220  1.00 161.02 ? 1559 TYR A CE2 1 
ATOM   11886 C  CZ  . TYR A 1 1559 ? -18.362  14.742  42.362  1.00 160.48 ? 1559 TYR A CZ  1 
ATOM   11887 O  OH  . TYR A 1 1559 ? -17.991  13.526  41.858  1.00 159.16 ? 1559 TYR A OH  1 
ATOM   11888 N  N   . ALA A 1 1560 ? -17.007  20.378  43.069  1.00 161.62 ? 1560 ALA A N   1 
ATOM   11889 C  CA  . ALA A 1 1560 ? -15.644  20.338  42.636  1.00 166.38 ? 1560 ALA A CA  1 
ATOM   11890 C  C   . ALA A 1 1560 ? -14.842  20.385  43.931  1.00 174.53 ? 1560 ALA A C   1 
ATOM   11891 O  O   . ALA A 1 1560 ? -14.816  21.399  44.645  1.00 177.58 ? 1560 ALA A O   1 
ATOM   11892 C  CB  . ALA A 1 1560 ? -15.343  21.503  41.721  1.00 164.09 ? 1560 ALA A CB  1 
ATOM   11893 N  N   . TYR A 1 1561 ? -14.225  19.255  44.261  1.00 177.17 ? 1561 TYR A N   1 
ATOM   11894 C  CA  . TYR A 1 1561 ? -13.562  19.137  45.546  1.00 178.72 ? 1561 TYR A CA  1 
ATOM   11895 C  C   . TYR A 1 1561 ? -12.375  18.148  45.642  1.00 174.71 ? 1561 TYR A C   1 
ATOM   11896 O  O   . TYR A 1 1561 ? -12.494  16.953  45.359  1.00 173.02 ? 1561 TYR A O   1 
ATOM   11897 C  CB  . TYR A 1 1561 ? -14.606  18.962  46.663  1.00 185.79 ? 1561 TYR A CB  1 
ATOM   11898 C  CG  . TYR A 1 1561 ? -15.490  17.725  46.632  1.00 192.82 ? 1561 TYR A CG  1 
ATOM   11899 C  CD1 . TYR A 1 1561 ? -16.847  17.824  46.923  1.00 196.23 ? 1561 TYR A CD1 1 
ATOM   11900 C  CD2 . TYR A 1 1561 ? -14.968  16.461  46.370  1.00 195.94 ? 1561 TYR A CD2 1 
ATOM   11901 C  CE1 . TYR A 1 1561 ? -17.658  16.709  46.940  1.00 198.95 ? 1561 TYR A CE1 1 
ATOM   11902 C  CE2 . TYR A 1 1561 ? -15.776  15.337  46.378  1.00 198.40 ? 1561 TYR A CE2 1 
ATOM   11903 C  CZ  . TYR A 1 1561 ? -17.120  15.467  46.665  1.00 199.78 ? 1561 TYR A CZ  1 
ATOM   11904 O  OH  . TYR A 1 1561 ? -17.936  14.355  46.674  1.00 200.66 ? 1561 TYR A OH  1 
ATOM   11905 N  N   . LYS A 1 1562 ? -11.233  18.703  46.048  1.00 173.09 ? 1562 LYS A N   1 
ATOM   11906 C  CA  . LYS A 1 1562 ? -9.960   18.009  46.145  1.00 172.81 ? 1562 LYS A CA  1 
ATOM   11907 C  C   . LYS A 1 1562 ? -9.954   17.064  47.330  1.00 182.93 ? 1562 LYS A C   1 
ATOM   11908 O  O   . LYS A 1 1562 ? -10.426  17.405  48.419  1.00 191.09 ? 1562 LYS A O   1 
ATOM   11909 C  CB  . LYS A 1 1562 ? -8.826   19.029  46.264  1.00 165.72 ? 1562 LYS A CB  1 
ATOM   11910 C  CG  . LYS A 1 1562 ? -7.483   18.567  45.750  1.00 158.49 ? 1562 LYS A CG  1 
ATOM   11911 C  CD  . LYS A 1 1562 ? -6.643   18.011  46.872  1.00 153.76 ? 1562 LYS A CD  1 
ATOM   11912 C  CE  . LYS A 1 1562 ? -6.005   19.105  47.692  1.00 148.88 ? 1562 LYS A CE  1 
ATOM   11913 N  NZ  . LYS A 1 1562 ? -4.906   19.754  46.939  1.00 144.99 ? 1562 LYS A NZ  1 
ATOM   11914 N  N   . VAL A 1 1563 ? -9.404   15.875  47.089  1.00 182.35 ? 1563 VAL A N   1 
ATOM   11915 C  CA  . VAL A 1 1563 ? -9.442   14.751  48.023  1.00 186.01 ? 1563 VAL A CA  1 
ATOM   11916 C  C   . VAL A 1 1563 ? -8.302   13.791  47.721  1.00 186.24 ? 1563 VAL A C   1 
ATOM   11917 O  O   . VAL A 1 1563 ? -7.583   13.955  46.733  1.00 180.48 ? 1563 VAL A O   1 
ATOM   11918 C  CB  . VAL A 1 1563 ? -10.721  13.915  47.842  1.00 192.44 ? 1563 VAL A CB  1 
ATOM   11919 C  CG1 . VAL A 1 1563 ? -11.943  14.811  47.734  1.00 196.32 ? 1563 VAL A CG1 1 
ATOM   11920 C  CG2 . VAL A 1 1563 ? -10.612  13.011  46.605  1.00 193.58 ? 1563 VAL A CG2 1 
ATOM   11921 N  N   . SER A 1 1564 ? -8.175   12.762  48.552  1.00 193.44 ? 1564 SER A N   1 
ATOM   11922 C  CA  . SER A 1 1564 ? -7.151   11.746  48.382  1.00 197.78 ? 1564 SER A CA  1 
ATOM   11923 C  C   . SER A 1 1564 ? -7.711   10.395  48.757  1.00 202.60 ? 1564 SER A C   1 
ATOM   11924 O  O   . SER A 1 1564 ? -8.498   10.282  49.691  1.00 204.08 ? 1564 SER A O   1 
ATOM   11925 C  CB  . SER A 1 1564 ? -5.958   12.044  49.272  1.00 195.59 ? 1564 SER A CB  1 
ATOM   11926 O  OG  . SER A 1 1564 ? -5.093   10.932  49.320  1.00 192.51 ? 1564 SER A OG  1 
ATOM   11927 N  N   . ILE A 1 1565 ? -7.295   9.370   48.024  1.00 206.34 ? 1565 ILE A N   1 
ATOM   11928 C  CA  . ILE A 1 1565 ? -7.771   8.009   48.257  1.00 213.69 ? 1565 ILE A CA  1 
ATOM   11929 C  C   . ILE A 1 1565 ? -7.204   7.426   49.551  1.00 222.25 ? 1565 ILE A C   1 
ATOM   11930 O  O   . ILE A 1 1565 ? -5.997   7.207   49.658  1.00 220.78 ? 1565 ILE A O   1 
ATOM   11931 C  CB  . ILE A 1 1565 ? -7.405   7.073   47.080  1.00 213.51 ? 1565 ILE A CB  1 
ATOM   11932 C  CG1 . ILE A 1 1565 ? -7.976   7.611   45.768  1.00 214.61 ? 1565 ILE A CG1 1 
ATOM   11933 C  CG2 . ILE A 1 1565 ? -7.911   5.657   47.330  1.00 214.35 ? 1565 ILE A CG2 1 
ATOM   11934 C  CD1 . ILE A 1 1565 ? -7.169   8.732   45.151  1.00 214.87 ? 1565 ILE A CD1 1 
ATOM   11935 N  N   . THR A 1 1566 ? -8.076   7.177   50.528  1.00 232.21 ? 1566 THR A N   1 
ATOM   11936 C  CA  . THR A 1 1566 ? -7.672   6.497   51.756  1.00 240.45 ? 1566 THR A CA  1 
ATOM   11937 C  C   . THR A 1 1566 ? -8.002   5.008   51.737  1.00 251.02 ? 1566 THR A C   1 
ATOM   11938 O  O   . THR A 1 1566 ? -7.510   4.257   52.576  1.00 253.34 ? 1566 THR A O   1 
ATOM   11939 C  CB  . THR A 1 1566 ? -8.288   7.134   53.014  1.00 237.51 ? 1566 THR A CB  1 
ATOM   11940 O  OG1 . THR A 1 1566 ? -9.715   7.029   52.962  1.00 236.22 ? 1566 THR A OG1 1 
ATOM   11941 C  CG2 . THR A 1 1566 ? -7.881   8.585   53.112  1.00 235.95 ? 1566 THR A CG2 1 
ATOM   11942 N  N   . SER A 1 1567 ? -8.819   4.573   50.780  1.00 258.13 ? 1567 SER A N   1 
ATOM   11943 C  CA  . SER A 1 1567 ? -9.180   3.157   50.702  1.00 264.73 ? 1567 SER A CA  1 
ATOM   11944 C  C   . SER A 1 1567 ? -9.503   2.648   49.298  1.00 270.79 ? 1567 SER A C   1 
ATOM   11945 O  O   . SER A 1 1567 ? -10.614  2.822   48.801  1.00 272.62 ? 1567 SER A O   1 
ATOM   11946 C  CB  . SER A 1 1567 ? -10.355  2.847   51.634  1.00 265.97 ? 1567 SER A CB  1 
ATOM   11947 O  OG  . SER A 1 1567 ? -10.746  1.489   51.515  1.00 266.00 ? 1567 SER A OG  1 
ATOM   11948 N  N   . ILE A 1 1568 ? -8.528   1.999   48.674  1.00 275.18 ? 1568 ILE A N   1 
ATOM   11949 C  CA  . ILE A 1 1568 ? -8.782   1.221   47.469  1.00 279.54 ? 1568 ILE A CA  1 
ATOM   11950 C  C   . ILE A 1 1568 ? -8.171   -0.163  47.678  1.00 280.89 ? 1568 ILE A C   1 
ATOM   11951 O  O   . ILE A 1 1568 ? -7.035   -0.433  47.279  1.00 280.46 ? 1568 ILE A O   1 
ATOM   11952 C  CB  . ILE A 1 1568 ? -8.236   1.901   46.189  1.00 281.20 ? 1568 ILE A CB  1 
ATOM   11953 C  CG1 . ILE A 1 1568 ? -8.493   1.012   44.971  1.00 281.66 ? 1568 ILE A CG1 1 
ATOM   11954 C  CG2 . ILE A 1 1568 ? -6.754   2.233   46.328  1.00 281.23 ? 1568 ILE A CG2 1 
ATOM   11955 C  CD1 . ILE A 1 1568 ? -9.904   0.457   44.913  1.00 282.72 ? 1568 ILE A CD1 1 
ATOM   11956 N  N   . THR A 1 1569 ? -8.949   -1.031  48.321  1.00 281.51 ? 1569 THR A N   1 
ATOM   11957 C  CA  . THR A 1 1569 ? -8.456   -2.313  48.818  1.00 279.91 ? 1569 THR A CA  1 
ATOM   11958 C  C   . THR A 1 1569 ? -7.598   -3.065  47.797  1.00 278.15 ? 1569 THR A C   1 
ATOM   11959 O  O   . THR A 1 1569 ? -8.112   -3.628  46.829  1.00 278.09 ? 1569 THR A O   1 
ATOM   11960 C  CB  . THR A 1 1569 ? -9.618   -3.201  49.320  1.00 279.22 ? 1569 THR A CB  1 
ATOM   11961 O  OG1 . THR A 1 1569 ? -10.788  -2.955  48.528  1.00 278.77 ? 1569 THR A OG1 1 
ATOM   11962 C  CG2 . THR A 1 1569 ? -9.937   -2.885  50.776  1.00 279.80 ? 1569 THR A CG2 1 
ATOM   11963 N  N   . VAL A 1 1570 ? -6.286   -3.064  48.033  1.00 276.50 ? 1570 VAL A N   1 
ATOM   11964 C  CA  . VAL A 1 1570 ? -5.326   -3.709  47.139  1.00 274.41 ? 1570 VAL A CA  1 
ATOM   11965 C  C   . VAL A 1 1570 ? -5.771   -5.121  46.789  1.00 274.14 ? 1570 VAL A C   1 
ATOM   11966 O  O   . VAL A 1 1570 ? -5.738   -5.522  45.624  1.00 273.31 ? 1570 VAL A O   1 
ATOM   11967 C  CB  . VAL A 1 1570 ? -3.917   -3.780  47.770  1.00 273.00 ? 1570 VAL A CB  1 
ATOM   11968 C  CG1 . VAL A 1 1570 ? -2.931   -4.420  46.800  1.00 271.23 ? 1570 VAL A CG1 1 
ATOM   11969 C  CG2 . VAL A 1 1570 ? -3.444   -2.394  48.186  1.00 273.24 ? 1570 VAL A CG2 1 
ATOM   11970 N  N   . GLU A 1 1571 ? -6.192   -5.865  47.807  1.00 274.99 ? 1571 GLU A N   1 
ATOM   11971 C  CA  . GLU A 1 1571 ? -6.673   -7.228  47.624  1.00 275.12 ? 1571 GLU A CA  1 
ATOM   11972 C  C   . GLU A 1 1571 ? -7.621   -7.322  46.424  1.00 277.60 ? 1571 GLU A C   1 
ATOM   11973 O  O   . GLU A 1 1571 ? -8.451   -6.437  46.207  1.00 277.74 ? 1571 GLU A O   1 
ATOM   11974 C  CB  . GLU A 1 1571 ? -7.377   -7.726  48.895  1.00 274.06 ? 1571 GLU A CB  1 
ATOM   11975 C  CG  . GLU A 1 1571 ? -6.502   -7.768  50.149  1.00 272.52 ? 1571 GLU A CG  1 
ATOM   11976 C  CD  . GLU A 1 1571 ? -6.470   -6.446  50.897  1.00 272.36 ? 1571 GLU A CD  1 
ATOM   11977 O  OE1 . GLU A 1 1571 ? -7.046   -5.460  50.397  1.00 272.33 ? 1571 GLU A OE1 1 
ATOM   11978 O  OE2 . GLU A 1 1571 ? -5.871   -6.391  51.991  1.00 272.65 ? 1571 GLU A OE2 1 
ATOM   11979 N  N   . ASN A 1 1572 ? -7.481   -8.390  45.642  1.00 280.05 ? 1572 ASN A N   1 
ATOM   11980 C  CA  . ASN A 1 1572 ? -8.351   -8.632  44.491  1.00 283.48 ? 1572 ASN A CA  1 
ATOM   11981 C  C   . ASN A 1 1572 ? -9.761   -9.047  44.923  1.00 287.64 ? 1572 ASN A C   1 
ATOM   11982 O  O   . ASN A 1 1572 ? -9.950   -9.571  46.018  1.00 287.47 ? 1572 ASN A O   1 
ATOM   11983 C  CB  . ASN A 1 1572 ? -7.743   -9.698  43.569  1.00 282.66 ? 1572 ASN A CB  1 
ATOM   11984 C  CG  . ASN A 1 1572 ? -6.393   -9.282  42.992  1.00 281.92 ? 1572 ASN A CG  1 
ATOM   11985 O  OD1 . ASN A 1 1572 ? -6.114   -8.095  42.819  1.00 281.96 ? 1572 ASN A OD1 1 
ATOM   11986 N  ND2 . ASN A 1 1572 ? -5.552   -10.267 42.685  1.00 281.05 ? 1572 ASN A ND2 1 
ATOM   11987 N  N   . VAL A 1 1573 ? -10.744  -8.810  44.056  1.00 291.79 ? 1573 VAL A N   1 
ATOM   11988 C  CA  . VAL A 1 1573 ? -12.149  -9.112  44.349  1.00 295.85 ? 1573 VAL A CA  1 
ATOM   11989 C  C   . VAL A 1 1573 ? -12.797  -8.117  45.328  1.00 300.51 ? 1573 VAL A C   1 
ATOM   11990 O  O   . VAL A 1 1573 ? -14.024  -8.019  45.395  1.00 303.32 ? 1573 VAL A O   1 
ATOM   11991 C  CB  . VAL A 1 1573 ? -12.342  -10.567 44.846  1.00 294.91 ? 1573 VAL A CB  1 
ATOM   11992 C  CG1 . VAL A 1 1573 ? -13.812  -10.859 45.099  1.00 295.32 ? 1573 VAL A CG1 1 
ATOM   11993 C  CG2 . VAL A 1 1573 ? -11.775  -11.550 43.837  1.00 293.43 ? 1573 VAL A CG2 1 
ATOM   11994 N  N   . PHE A 1 1574 ? -11.975  -7.375  46.071  1.00 301.78 ? 1574 PHE A N   1 
ATOM   11995 C  CA  . PHE A 1 1574 ? -12.469  -6.345  46.995  1.00 304.30 ? 1574 PHE A CA  1 
ATOM   11996 C  C   . PHE A 1 1574 ? -13.157  -5.191  46.244  1.00 300.33 ? 1574 PHE A C   1 
ATOM   11997 O  O   . PHE A 1 1574 ? -12.835  -4.909  45.088  1.00 299.58 ? 1574 PHE A O   1 
ATOM   11998 C  CB  . PHE A 1 1574 ? -11.331  -5.812  47.886  1.00 310.86 ? 1574 PHE A CB  1 
ATOM   11999 C  CG  . PHE A 1 1574 ? -11.046  -6.661  49.113  1.00 318.46 ? 1574 PHE A CG  1 
ATOM   12000 C  CD1 . PHE A 1 1574 ? -10.996  -8.046  49.030  1.00 321.55 ? 1574 PHE A CD1 1 
ATOM   12001 C  CD2 . PHE A 1 1574 ? -10.800  -6.065  50.344  1.00 322.14 ? 1574 PHE A CD2 1 
ATOM   12002 C  CE1 . PHE A 1 1574 ? -10.726  -8.822  50.155  1.00 323.82 ? 1574 PHE A CE1 1 
ATOM   12003 C  CE2 . PHE A 1 1574 ? -10.527  -6.834  51.468  1.00 324.60 ? 1574 PHE A CE2 1 
ATOM   12004 C  CZ  . PHE A 1 1574 ? -10.490  -8.215  51.372  1.00 324.95 ? 1574 PHE A CZ  1 
ATOM   12005 N  N   . VAL A 1 1575 ? -14.105  -4.528  46.899  1.00 296.59 ? 1575 VAL A N   1 
ATOM   12006 C  CA  . VAL A 1 1575 ? -14.897  -3.500  46.225  1.00 290.80 ? 1575 VAL A CA  1 
ATOM   12007 C  C   . VAL A 1 1575 ? -14.308  -2.073  46.270  1.00 283.04 ? 1575 VAL A C   1 
ATOM   12008 O  O   . VAL A 1 1575 ? -13.145  -1.875  46.639  1.00 281.75 ? 1575 VAL A O   1 
ATOM   12009 C  CB  . VAL A 1 1575 ? -16.391  -3.541  46.645  1.00 283.32 ? 1575 VAL A CB  1 
ATOM   12010 C  CG1 . VAL A 1 1575 ? -17.099  -4.707  45.954  1.00 282.79 ? 1575 VAL A CG1 1 
ATOM   12011 C  CG2 . VAL A 1 1575 ? -16.528  -3.640  48.156  1.00 284.08 ? 1575 VAL A CG2 1 
ATOM   12012 N  N   . LYS A 1 1576 ? -15.146  -1.097  45.917  1.00 275.42 ? 1576 LYS A N   1 
ATOM   12013 C  CA  . LYS A 1 1576 ? -14.721  0.187   45.330  1.00 265.88 ? 1576 LYS A CA  1 
ATOM   12014 C  C   . LYS A 1 1576 ? -13.968  1.213   46.197  1.00 259.94 ? 1576 LYS A C   1 
ATOM   12015 O  O   . LYS A 1 1576 ? -13.653  0.954   47.359  1.00 260.49 ? 1576 LYS A O   1 
ATOM   12016 C  CB  . LYS A 1 1576 ? -15.912  0.850   44.622  1.00 262.93 ? 1576 LYS A CB  1 
ATOM   12017 C  CG  . LYS A 1 1576 ? -16.320  0.155   43.321  1.00 259.94 ? 1576 LYS A CG  1 
ATOM   12018 C  CD  . LYS A 1 1576 ? -16.754  -1.288  43.560  1.00 258.26 ? 1576 LYS A CD  1 
ATOM   12019 C  CE  . LYS A 1 1576 ? -16.980  -2.053  42.266  1.00 255.85 ? 1576 LYS A CE  1 
ATOM   12020 N  NZ  . LYS A 1 1576 ? -15.709  -2.310  41.544  1.00 253.80 ? 1576 LYS A NZ  1 
ATOM   12021 N  N   . TYR A 1 1577 ? -13.678  2.371   45.591  1.00 253.47 ? 1577 TYR A N   1 
ATOM   12022 C  CA  . TYR A 1 1577 ? -12.862  3.430   46.203  1.00 247.98 ? 1577 TYR A CA  1 
ATOM   12023 C  C   . TYR A 1 1577 ? -13.541  4.149   47.360  1.00 247.67 ? 1577 TYR A C   1 
ATOM   12024 O  O   . TYR A 1 1577 ? -14.738  4.014   47.580  1.00 247.52 ? 1577 TYR A O   1 
ATOM   12025 C  CB  . TYR A 1 1577 ? -12.473  4.505   45.178  1.00 243.55 ? 1577 TYR A CB  1 
ATOM   12026 C  CG  . TYR A 1 1577 ? -11.822  4.006   43.917  1.00 239.98 ? 1577 TYR A CG  1 
ATOM   12027 C  CD1 . TYR A 1 1577 ? -12.491  4.061   42.706  1.00 238.92 ? 1577 TYR A CD1 1 
ATOM   12028 C  CD2 . TYR A 1 1577 ? -10.536  3.498   43.928  1.00 238.42 ? 1577 TYR A CD2 1 
ATOM   12029 C  CE1 . TYR A 1 1577 ? -11.903  3.614   41.542  1.00 237.42 ? 1577 TYR A CE1 1 
ATOM   12030 C  CE2 . TYR A 1 1577 ? -9.941   3.042   42.767  1.00 236.83 ? 1577 TYR A CE2 1 
ATOM   12031 C  CZ  . TYR A 1 1577 ? -10.628  3.107   41.577  1.00 235.88 ? 1577 TYR A CZ  1 
ATOM   12032 O  OH  . TYR A 1 1577 ? -10.044  2.664   40.415  1.00 233.65 ? 1577 TYR A OH  1 
ATOM   12033 N  N   . LYS A 1 1578 ? -12.749  4.925   48.089  1.00 247.07 ? 1578 LYS A N   1 
ATOM   12034 C  CA  . LYS A 1 1578 ? -13.232  5.806   49.138  1.00 246.88 ? 1578 LYS A CA  1 
ATOM   12035 C  C   . LYS A 1 1578 ? -12.067  6.730   49.402  1.00 247.74 ? 1578 LYS A C   1 
ATOM   12036 O  O   . LYS A 1 1578 ? -10.927  6.284   49.448  1.00 247.43 ? 1578 LYS A O   1 
ATOM   12037 C  CB  . LYS A 1 1578 ? -13.580  5.039   50.417  1.00 245.70 ? 1578 LYS A CB  1 
ATOM   12038 C  CG  . LYS A 1 1578 ? -13.850  3.558   50.229  1.00 243.80 ? 1578 LYS A CG  1 
ATOM   12039 C  CD  . LYS A 1 1578 ? -14.997  3.068   51.095  1.00 243.63 ? 1578 LYS A CD  1 
ATOM   12040 C  CE  . LYS A 1 1578 ? -14.670  3.150   52.578  1.00 244.37 ? 1578 LYS A CE  1 
ATOM   12041 N  NZ  . LYS A 1 1578 ? -15.744  2.544   53.418  1.00 245.45 ? 1578 LYS A NZ  1 
ATOM   12042 N  N   . ALA A 1 1579 ? -12.335  8.015   49.576  1.00 249.10 ? 1579 ALA A N   1 
ATOM   12043 C  CA  . ALA A 1 1579 ? -11.249  8.973   49.710  1.00 249.19 ? 1579 ALA A CA  1 
ATOM   12044 C  C   . ALA A 1 1579 ? -11.550  10.026  50.772  1.00 248.56 ? 1579 ALA A C   1 
ATOM   12045 O  O   . ALA A 1 1579 ? -12.713  10.352  51.015  1.00 253.32 ? 1579 ALA A O   1 
ATOM   12046 C  CB  . ALA A 1 1579 ? -10.971  9.628   48.365  1.00 249.50 ? 1579 ALA A CB  1 
ATOM   12047 N  N   . THR A 1 1580 ? -10.499  10.538  51.414  1.00 242.83 ? 1580 THR A N   1 
ATOM   12048 C  CA  . THR A 1 1580 ? -10.628  11.616  52.402  1.00 240.11 ? 1580 THR A CA  1 
ATOM   12049 C  C   . THR A 1 1580 ? -10.535  13.003  51.755  1.00 239.15 ? 1580 THR A C   1 
ATOM   12050 O  O   . THR A 1 1580 ? -9.591   13.305  51.025  1.00 237.30 ? 1580 THR A O   1 
ATOM   12051 C  CB  . THR A 1 1580 ? -9.577   11.502  53.537  1.00 275.88 ? 1580 THR A CB  1 
ATOM   12052 O  OG1 . THR A 1 1580 ? -9.757   10.265  54.237  1.00 276.65 ? 1580 THR A OG1 1 
ATOM   12053 C  CG2 . THR A 1 1580 ? -9.720   12.656  54.525  1.00 276.30 ? 1580 THR A CG2 1 
ATOM   12054 N  N   . LEU A 1 1581 ? -11.523  13.842  52.036  1.00 239.23 ? 1581 LEU A N   1 
ATOM   12055 C  CA  . LEU A 1 1581 ? -11.621  15.155  51.424  1.00 237.75 ? 1581 LEU A CA  1 
ATOM   12056 C  C   . LEU A 1 1581 ? -10.684  16.125  52.139  1.00 242.27 ? 1581 LEU A C   1 
ATOM   12057 O  O   . LEU A 1 1581 ? -10.538  16.055  53.356  1.00 244.94 ? 1581 LEU A O   1 
ATOM   12058 C  CB  . LEU A 1 1581 ? -13.067  15.630  51.511  1.00 231.35 ? 1581 LEU A CB  1 
ATOM   12059 C  CG  . LEU A 1 1581 ? -13.669  16.262  50.261  1.00 222.10 ? 1581 LEU A CG  1 
ATOM   12060 C  CD1 . LEU A 1 1581 ? -15.193  16.115  50.262  1.00 218.94 ? 1581 LEU A CD1 1 
ATOM   12061 C  CD2 . LEU A 1 1581 ? -13.232  17.715  50.138  1.00 218.70 ? 1581 LEU A CD2 1 
ATOM   12062 N  N   . LEU A 1 1582 ? -10.046  17.023  51.389  1.00 242.91 ? 1582 LEU A N   1 
ATOM   12063 C  CA  . LEU A 1 1582 ? -9.046   17.934  51.971  1.00 244.29 ? 1582 LEU A CA  1 
ATOM   12064 C  C   . LEU A 1 1582 ? -9.439   19.417  52.053  1.00 246.75 ? 1582 LEU A C   1 
ATOM   12065 O  O   . LEU A 1 1582 ? -8.973   20.142  52.940  1.00 245.41 ? 1582 LEU A O   1 
ATOM   12066 C  CB  . LEU A 1 1582 ? -7.730   17.831  51.203  1.00 242.81 ? 1582 LEU A CB  1 
ATOM   12067 C  CG  . LEU A 1 1582 ? -6.854   16.609  51.423  1.00 242.32 ? 1582 LEU A CG  1 
ATOM   12068 C  CD1 . LEU A 1 1582 ? -7.577   15.359  51.002  1.00 241.76 ? 1582 LEU A CD1 1 
ATOM   12069 C  CD2 . LEU A 1 1582 ? -5.609   16.796  50.609  1.00 241.68 ? 1582 LEU A CD2 1 
ATOM   12070 N  N   . ASP A 1 1583 ? -10.266  19.854  51.105  1.00 249.85 ? 1583 ASP A N   1 
ATOM   12071 C  CA  . ASP A 1 1583 ? -10.671  21.250  50.964  1.00 252.40 ? 1583 ASP A CA  1 
ATOM   12072 C  C   . ASP A 1 1583 ? -11.791  21.283  49.871  1.00 199.09 ? 1583 ASP A C   1 
ATOM   12073 O  O   . ASP A 1 1583 ? -11.596  20.718  48.797  1.00 193.39 ? 1583 ASP A O   1 
ATOM   12074 C  CB  . ASP A 1 1583 ? -9.435   22.133  50.601  1.00 260.00 ? 1583 ASP A CB  1 
ATOM   12075 C  CG  . ASP A 1 1583 ? -8.405   22.298  51.775  1.00 232.82 ? 1583 ASP A CG  1 
ATOM   12076 O  OD1 . ASP A 1 1583 ? -8.815   22.595  52.913  1.00 235.67 ? 1583 ASP A OD1 1 
ATOM   12077 O  OD2 . ASP A 1 1583 ? -7.176   22.158  51.559  1.00 229.39 ? 1583 ASP A OD2 1 
ATOM   12078 N  N   . ILE A 1 1584 ? -12.963  21.881  50.162  1.00 205.24 ? 1584 ILE A N   1 
ATOM   12079 C  CA  . ILE A 1 1584 ? -14.101  21.977  49.204  1.00 207.76 ? 1584 ILE A CA  1 
ATOM   12080 C  C   . ILE A 1 1584 ? -14.198  23.307  48.462  1.00 206.33 ? 1584 ILE A C   1 
ATOM   12081 O  O   . ILE A 1 1584 ? -14.345  24.371  49.063  1.00 208.20 ? 1584 ILE A O   1 
ATOM   12082 C  CB  . ILE A 1 1584 ? -15.497  21.803  49.861  1.00 154.06 ? 1584 ILE A CB  1 
ATOM   12083 C  CG1 . ILE A 1 1584 ? -15.652  20.452  50.545  1.00 160.71 ? 1584 ILE A CG1 1 
ATOM   12084 C  CG2 . ILE A 1 1584 ? -16.596  21.980  48.819  1.00 148.19 ? 1584 ILE A CG2 1 
ATOM   12085 C  CD1 . ILE A 1 1584 ? -17.053  20.222  51.054  1.00 164.71 ? 1584 ILE A CD1 1 
ATOM   12086 N  N   . TYR A 1 1585 ? -14.171  23.243  47.145  1.00 205.24 ? 1585 TYR A N   1 
ATOM   12087 C  CA  . TYR A 1 1585 ? -14.275  24.453  46.365  1.00 208.16 ? 1585 TYR A CA  1 
ATOM   12088 C  C   . TYR A 1 1585 ? -15.727  24.726  45.978  1.00 214.59 ? 1585 TYR A C   1 
ATOM   12089 O  O   . TYR A 1 1585 ? -16.205  25.854  46.085  1.00 216.88 ? 1585 TYR A O   1 
ATOM   12090 C  CB  . TYR A 1 1585 ? -13.405  24.333  45.130  1.00 208.29 ? 1585 TYR A CB  1 
ATOM   12091 C  CG  . TYR A 1 1585 ? -11.964  23.982  45.420  1.00 212.32 ? 1585 TYR A CG  1 
ATOM   12092 C  CD1 . TYR A 1 1585 ? -11.221  24.703  46.358  1.00 215.06 ? 1585 TYR A CD1 1 
ATOM   12093 C  CD2 . TYR A 1 1585 ? -11.333  22.945  44.728  1.00 213.07 ? 1585 TYR A CD2 1 
ATOM   12094 C  CE1 . TYR A 1 1585 ? -9.889   24.390  46.605  1.00 215.94 ? 1585 TYR A CE1 1 
ATOM   12095 C  CE2 . TYR A 1 1585 ? -10.009  22.624  44.964  1.00 214.05 ? 1585 TYR A CE2 1 
ATOM   12096 C  CZ  . TYR A 1 1585 ? -9.289   23.345  45.902  1.00 215.11 ? 1585 TYR A CZ  1 
ATOM   12097 O  OH  . TYR A 1 1585 ? -7.970   23.006  46.115  1.00 214.42 ? 1585 TYR A OH  1 
ATOM   12098 N  N   . LYS A 1 1586 ? -16.422  23.684  45.527  1.00 219.71 ? 1586 LYS A N   1 
ATOM   12099 C  CA  . LYS A 1 1586 ? -17.852  23.754  45.233  1.00 224.66 ? 1586 LYS A CA  1 
ATOM   12100 C  C   . LYS A 1 1586 ? -18.543  22.676  46.072  1.00 229.65 ? 1586 LYS A C   1 
ATOM   12101 O  O   . LYS A 1 1586 ? -18.276  21.485  45.903  1.00 230.19 ? 1586 LYS A O   1 
ATOM   12102 C  CB  . LYS A 1 1586 ? -18.121  23.519  43.734  1.00 224.75 ? 1586 LYS A CB  1 
ATOM   12103 C  CG  . LYS A 1 1586 ? -18.091  24.779  42.829  1.00 232.59 ? 1586 LYS A CG  1 
ATOM   12104 C  CD  . LYS A 1 1586 ? -18.294  24.473  41.306  1.00 145.46 ? 1586 LYS A CD  1 
ATOM   12105 C  CE  . LYS A 1 1586 ? -19.767  24.523  40.837  1.00 143.68 ? 1586 LYS A CE  1 
ATOM   12106 N  NZ  . LYS A 1 1586 ? -20.294  25.905  40.673  1.00 141.47 ? 1586 LYS A NZ  1 
ATOM   12107 N  N   . THR A 1 1587 ? -19.415  23.085  46.991  1.00 234.39 ? 1587 THR A N   1 
ATOM   12108 C  CA  . THR A 1 1587 ? -20.017  22.129  47.923  1.00 239.70 ? 1587 THR A CA  1 
ATOM   12109 C  C   . THR A 1 1587 ? -20.980  21.193  47.208  1.00 244.62 ? 1587 THR A C   1 
ATOM   12110 O  O   . THR A 1 1587 ? -22.003  21.627  46.669  1.00 244.69 ? 1587 THR A O   1 
ATOM   12111 C  CB  . THR A 1 1587 ? -20.746  22.817  49.113  1.00 276.75 ? 1587 THR A CB  1 
ATOM   12112 O  OG1 . THR A 1 1587 ? -19.830  23.655  49.830  1.00 277.50 ? 1587 THR A OG1 1 
ATOM   12113 C  CG2 . THR A 1 1587 ? -21.307  21.774  50.074  1.00 276.88 ? 1587 THR A CG2 1 
ATOM   12114 N  N   . GLY A 1 1588 ? -20.643  19.908  47.202  1.00 249.31 ? 1588 GLY A N   1 
ATOM   12115 C  CA  . GLY A 1 1588 ? -21.523  18.914  46.625  1.00 254.12 ? 1588 GLY A CA  1 
ATOM   12116 C  C   . GLY A 1 1588 ? -22.896  19.042  47.251  1.00 259.57 ? 1588 GLY A C   1 
ATOM   12117 O  O   . GLY A 1 1588 ? -23.003  19.345  48.436  1.00 259.65 ? 1588 GLY A O   1 
ATOM   12118 N  N   . GLU A 1 1589 ? -23.943  18.832  46.458  1.00 264.34 ? 1589 GLU A N   1 
ATOM   12119 C  CA  . GLU A 1 1589 ? -25.315  18.853  46.961  1.00 269.47 ? 1589 GLU A CA  1 
ATOM   12120 C  C   . GLU A 1 1589 ? -25.624  17.608  47.805  1.00 277.22 ? 1589 GLU A C   1 
ATOM   12121 O  O   . GLU A 1 1589 ? -26.719  17.050  47.720  1.00 275.98 ? 1589 GLU A O   1 
ATOM   12122 C  CB  . GLU A 1 1589 ? -26.311  18.937  45.802  1.00 266.58 ? 1589 GLU A CB  1 
ATOM   12123 C  CG  . GLU A 1 1589 ? -25.988  19.968  44.726  1.00 263.84 ? 1589 GLU A CG  1 
ATOM   12124 C  CD  . GLU A 1 1589 ? -26.730  19.691  43.406  1.00 261.68 ? 1589 GLU A CD  1 
ATOM   12125 O  OE1 . GLU A 1 1589 ? -26.314  18.783  42.658  1.00 261.11 ? 1589 GLU A OE1 1 
ATOM   12126 O  OE2 . GLU A 1 1589 ? -27.725  20.383  43.103  1.00 260.50 ? 1589 GLU A OE2 1 
ATOM   12127 N  N   . ALA A 1 1590 ? -24.663  17.178  48.621  1.00 286.54 ? 1590 ALA A N   1 
ATOM   12128 C  CA  . ALA A 1 1590 ? -24.816  15.955  49.412  1.00 296.14 ? 1590 ALA A CA  1 
ATOM   12129 C  C   . ALA A 1 1590 ? -24.215  16.054  50.821  1.00 306.22 ? 1590 ALA A C   1 
ATOM   12130 O  O   . ALA A 1 1590 ? -23.489  16.998  51.138  1.00 305.95 ? 1590 ALA A O   1 
ATOM   12131 C  CB  . ALA A 1 1590 ? -24.222  14.768  48.662  1.00 295.82 ? 1590 ALA A CB  1 
ATOM   12132 N  N   . VAL A 1 1591 ? -24.520  15.061  51.655  1.00 316.53 ? 1591 VAL A N   1 
ATOM   12133 C  CA  . VAL A 1 1591 ? -24.129  15.066  53.066  1.00 326.94 ? 1591 VAL A CA  1 
ATOM   12134 C  C   . VAL A 1 1591 ? -22.667  14.695  53.331  1.00 335.73 ? 1591 VAL A C   1 
ATOM   12135 O  O   . VAL A 1 1591 ? -22.198  13.627  52.928  1.00 335.65 ? 1591 VAL A O   1 
ATOM   12136 C  CB  . VAL A 1 1591 ? -25.037  14.144  53.905  1.00 328.06 ? 1591 VAL A CB  1 
ATOM   12137 C  CG1 . VAL A 1 1591 ? -24.437  13.914  55.286  1.00 329.08 ? 1591 VAL A CG1 1 
ATOM   12138 C  CG2 . VAL A 1 1591 ? -26.433  14.734  54.012  1.00 328.21 ? 1591 VAL A CG2 1 
ATOM   12139 N  N   . ALA A 1 1592 ? -21.982  15.598  54.032  1.00 344.24 ? 1592 ALA A N   1 
ATOM   12140 C  CA  . ALA A 1 1592 ? -20.576  15.484  54.422  1.00 351.73 ? 1592 ALA A CA  1 
ATOM   12141 C  C   . ALA A 1 1592 ? -19.985  16.887  54.347  1.00 356.62 ? 1592 ALA A C   1 
ATOM   12142 O  O   . ALA A 1 1592 ? -20.423  17.694  53.526  1.00 356.30 ? 1592 ALA A O   1 
ATOM   12143 C  CB  . ALA A 1 1592 ? -19.815  14.536  53.510  1.00 352.44 ? 1592 ALA A CB  1 
ATOM   12144 N  N   . GLU A 1 1593 ? -19.002  17.190  55.190  1.00 361.25 ? 1593 GLU A N   1 
ATOM   12145 C  CA  . GLU A 1 1593 ? -18.375  18.513  55.152  1.00 364.21 ? 1593 GLU A CA  1 
ATOM   12146 C  C   . GLU A 1 1593 ? -16.861  18.458  55.369  1.00 356.43 ? 1593 GLU A C   1 
ATOM   12147 O  O   . GLU A 1 1593 ? -16.336  17.490  55.923  1.00 356.36 ? 1593 GLU A O   1 
ATOM   12148 C  CB  . GLU A 1 1593 ? -19.050  19.482  56.135  1.00 374.37 ? 1593 GLU A CB  1 
ATOM   12149 C  CG  . GLU A 1 1593 ? -18.877  20.963  55.779  1.00 380.74 ? 1593 GLU A CG  1 
ATOM   12150 C  CD  . GLU A 1 1593 ? -19.216  21.277  54.325  1.00 383.84 ? 1593 GLU A CD  1 
ATOM   12151 O  OE1 . GLU A 1 1593 ? -20.122  20.629  53.758  1.00 384.61 ? 1593 GLU A OE1 1 
ATOM   12152 O  OE2 . GLU A 1 1593 ? -18.573  22.179  53.747  1.00 384.86 ? 1593 GLU A OE2 1 
ATOM   12153 N  N   . LYS A 1 1594 ? -16.176  19.513  54.932  1.00 347.79 ? 1594 LYS A N   1 
ATOM   12154 C  CA  . LYS A 1 1594 ? -14.720  19.505  54.770  1.00 338.50 ? 1594 LYS A CA  1 
ATOM   12155 C  C   . LYS A 1 1594 ? -13.937  18.809  55.887  1.00 328.38 ? 1594 LYS A C   1 
ATOM   12156 O  O   . LYS A 1 1594 ? -13.842  19.318  57.001  1.00 329.95 ? 1594 LYS A O   1 
ATOM   12157 C  CB  . LYS A 1 1594 ? -14.180  20.923  54.500  1.00 339.72 ? 1594 LYS A CB  1 
ATOM   12158 C  CG  . LYS A 1 1594 ? -14.761  22.045  55.364  1.00 341.63 ? 1594 LYS A CG  1 
ATOM   12159 C  CD  . LYS A 1 1594 ? -14.643  23.389  54.643  1.00 341.87 ? 1594 LYS A CD  1 
ATOM   12160 C  CE  . LYS A 1 1594 ? -14.690  24.565  55.601  1.00 343.41 ? 1594 LYS A CE  1 
ATOM   12161 N  NZ  . LYS A 1 1594 ? -13.413  24.704  56.349  1.00 344.31 ? 1594 LYS A NZ  1 
ATOM   12162 N  N   . ASP A 1 1595 ? -13.392  17.640  55.547  1.00 316.11 ? 1595 ASP A N   1 
ATOM   12163 C  CA  . ASP A 1 1595 ? -12.562  16.794  56.415  1.00 305.09 ? 1595 ASP A CA  1 
ATOM   12164 C  C   . ASP A 1 1595 ? -13.038  15.345  56.335  1.00 298.30 ? 1595 ASP A C   1 
ATOM   12165 O  O   . ASP A 1 1595 ? -12.249  14.410  56.482  1.00 297.85 ? 1595 ASP A O   1 
ATOM   12166 C  CB  . ASP A 1 1595 ? -12.536  17.272  57.873  1.00 301.96 ? 1595 ASP A CB  1 
ATOM   12167 C  CG  . ASP A 1 1595 ? -11.370  18.211  58.167  1.00 298.44 ? 1595 ASP A CG  1 
ATOM   12168 O  OD1 . ASP A 1 1595 ? -10.519  18.408  57.277  1.00 296.64 ? 1595 ASP A OD1 1 
ATOM   12169 O  OD2 . ASP A 1 1595 ? -11.303  18.750  59.293  1.00 297.98 ? 1595 ASP A OD2 1 
ATOM   12170 N  N   . SER A 1 1596 ? -14.333  15.172  56.087  1.00 292.51 ? 1596 SER A N   1 
ATOM   12171 C  CA  . SER A 1 1596 ? -14.948  13.848  56.050  1.00 287.14 ? 1596 SER A CA  1 
ATOM   12172 C  C   . SER A 1 1596 ? -14.490  13.026  54.851  1.00 281.85 ? 1596 SER A C   1 
ATOM   12173 O  O   . SER A 1 1596 ? -13.995  13.571  53.863  1.00 281.82 ? 1596 SER A O   1 
ATOM   12174 C  CB  . SER A 1 1596 ? -16.476  13.962  56.035  1.00 286.41 ? 1596 SER A CB  1 
ATOM   12175 O  OG  . SER A 1 1596 ? -16.967  14.198  54.727  1.00 284.85 ? 1596 SER A OG  1 
ATOM   12176 N  N   . GLU A 1 1597 ? -14.650  11.710  54.955  1.00 276.63 ? 1597 GLU A N   1 
ATOM   12177 C  CA  . GLU A 1 1597 ? -14.414  10.810  53.831  1.00 269.74 ? 1597 GLU A CA  1 
ATOM   12178 C  C   . GLU A 1 1597 ? -15.688  10.675  53.015  1.00 256.24 ? 1597 GLU A C   1 
ATOM   12179 O  O   . GLU A 1 1597 ? -16.797  10.700  53.551  1.00 257.31 ? 1597 GLU A O   1 
ATOM   12180 C  CB  . GLU A 1 1597 ? -13.954  9.425   54.313  1.00 276.19 ? 1597 GLU A CB  1 
ATOM   12181 C  CG  . GLU A 1 1597 ? -13.932  8.347   53.221  1.00 279.46 ? 1597 GLU A CG  1 
ATOM   12182 C  CD  . GLU A 1 1597 ? -13.741  6.938   53.771  1.00 281.20 ? 1597 GLU A CD  1 
ATOM   12183 O  OE1 . GLU A 1 1597 ? -12.704  6.680   54.417  1.00 281.33 ? 1597 GLU A OE1 1 
ATOM   12184 O  OE2 . GLU A 1 1597 ? -14.624  6.084   53.543  1.00 281.78 ? 1597 GLU A OE2 1 
ATOM   12185 N  N   . ILE A 1 1598 ? -15.526  10.536  51.712  1.00 243.33 ? 1598 ILE A N   1 
ATOM   12186 C  CA  . ILE A 1 1598 ? -16.659  10.278  50.856  1.00 236.55 ? 1598 ILE A CA  1 
ATOM   12187 C  C   . ILE A 1 1598 ? -16.175  9.331   49.772  1.00 229.90 ? 1598 ILE A C   1 
ATOM   12188 O  O   . ILE A 1 1598 ? -15.180  9.588   49.100  1.00 228.10 ? 1598 ILE A O   1 
ATOM   12189 C  CB  . ILE A 1 1598 ? -17.275  11.590  50.311  1.00 238.04 ? 1598 ILE A CB  1 
ATOM   12190 C  CG1 . ILE A 1 1598 ? -18.520  11.297  49.467  1.00 229.57 ? 1598 ILE A CG1 1 
ATOM   12191 C  CG2 . ILE A 1 1598 ? -16.231  12.430  49.572  1.00 247.11 ? 1598 ILE A CG2 1 
ATOM   12192 C  CD1 . ILE A 1 1598 ? -19.694  10.778  50.271  1.00 224.33 ? 1598 ILE A CD1 1 
ATOM   12193 N  N   . THR A 1 1599 ? -16.871  8.208   49.656  1.00 228.69 ? 1599 THR A N   1 
ATOM   12194 C  CA  . THR A 1 1599 ? -16.461  7.084   48.821  1.00 230.39 ? 1599 THR A CA  1 
ATOM   12195 C  C   . THR A 1 1599 ? -16.561  7.428   47.331  1.00 231.09 ? 1599 THR A C   1 
ATOM   12196 O  O   . THR A 1 1599 ? -16.938  8.545   46.990  1.00 232.44 ? 1599 THR A O   1 
ATOM   12197 C  CB  . THR A 1 1599 ? -17.326  5.858   49.183  1.00 233.21 ? 1599 THR A CB  1 
ATOM   12198 O  OG1 . THR A 1 1599 ? -16.883  5.324   50.435  1.00 235.03 ? 1599 THR A OG1 1 
ATOM   12199 C  CG2 . THR A 1 1599 ? -17.245  4.782   48.139  1.00 234.38 ? 1599 THR A CG2 1 
ATOM   12200 N  N   . PHE A 1 1600 ? -16.189  6.496   46.452  1.00 230.60 ? 1600 PHE A N   1 
ATOM   12201 C  CA  . PHE A 1 1600 ? -16.447  6.628   45.007  1.00 229.79 ? 1600 PHE A CA  1 
ATOM   12202 C  C   . PHE A 1 1600 ? -16.655  5.247   44.341  1.00 230.94 ? 1600 PHE A C   1 
ATOM   12203 O  O   . PHE A 1 1600 ? -15.775  4.388   44.409  1.00 230.51 ? 1600 PHE A O   1 
ATOM   12204 C  CB  . PHE A 1 1600 ? -15.320  7.407   44.299  1.00 225.89 ? 1600 PHE A CB  1 
ATOM   12205 C  CG  . PHE A 1 1600 ? -15.343  8.913   44.537  1.00 221.48 ? 1600 PHE A CG  1 
ATOM   12206 C  CD1 . PHE A 1 1600 ? -16.442  9.682   44.175  1.00 218.88 ? 1600 PHE A CD1 1 
ATOM   12207 C  CD2 . PHE A 1 1600 ? -14.241  9.557   45.089  1.00 219.43 ? 1600 PHE A CD2 1 
ATOM   12208 C  CE1 . PHE A 1 1600 ? -16.446  11.048  44.384  1.00 217.55 ? 1600 PHE A CE1 1 
ATOM   12209 C  CE2 . PHE A 1 1600 ? -14.243  10.924  45.296  1.00 217.91 ? 1600 PHE A CE2 1 
ATOM   12210 C  CZ  . PHE A 1 1600 ? -15.345  11.668  44.944  1.00 217.40 ? 1600 PHE A CZ  1 
ATOM   12211 N  N   . ILE A 1 1601 ? -17.812  5.049   43.697  1.00 232.54 ? 1601 ILE A N   1 
ATOM   12212 C  CA  . ILE A 1 1601 ? -18.231  3.729   43.183  1.00 233.99 ? 1601 ILE A CA  1 
ATOM   12213 C  C   . ILE A 1 1601 ? -18.111  3.509   41.658  1.00 234.96 ? 1601 ILE A C   1 
ATOM   12214 O  O   . ILE A 1 1601 ? -18.368  4.414   40.868  1.00 234.04 ? 1601 ILE A O   1 
ATOM   12215 C  CB  . ILE A 1 1601 ? -19.686  3.368   43.640  1.00 212.48 ? 1601 ILE A CB  1 
ATOM   12216 C  CG1 . ILE A 1 1601 ? -20.698  4.413   43.163  1.00 212.33 ? 1601 ILE A CG1 1 
ATOM   12217 C  CG2 . ILE A 1 1601 ? -19.770  3.241   45.147  1.00 213.02 ? 1601 ILE A CG2 1 
ATOM   12218 C  CD1 . ILE A 1 1601 ? -22.049  4.313   43.854  1.00 212.51 ? 1601 ILE A CD1 1 
ATOM   12219 N  N   . LYS A 1 1602 ? -17.711  2.295   41.269  1.00 237.68 ? 1602 LYS A N   1 
ATOM   12220 C  CA  . LYS A 1 1602 ? -17.714  1.831   39.870  1.00 240.37 ? 1602 LYS A CA  1 
ATOM   12221 C  C   . LYS A 1 1602 ? -17.300  0.359   39.765  1.00 248.02 ? 1602 LYS A C   1 
ATOM   12222 O  O   . LYS A 1 1602 ? -16.386  -0.088  40.455  1.00 247.76 ? 1602 LYS A O   1 
ATOM   12223 C  CB  . LYS A 1 1602 ? -16.859  2.703   38.926  1.00 234.96 ? 1602 LYS A CB  1 
ATOM   12224 C  CG  . LYS A 1 1602 ? -15.663  3.427   39.540  1.00 230.14 ? 1602 LYS A CG  1 
ATOM   12225 C  CD  . LYS A 1 1602 ? -14.871  2.557   40.489  1.00 225.80 ? 1602 LYS A CD  1 
ATOM   12226 C  CE  . LYS A 1 1602 ? -14.078  1.497   39.777  1.00 221.43 ? 1602 LYS A CE  1 
ATOM   12227 N  NZ  . LYS A 1 1602 ? -13.600  0.508   40.779  1.00 219.52 ? 1602 LYS A NZ  1 
ATOM   12228 N  N   . LYS A 1 1603 ? -17.974  -0.377  38.883  1.00 255.74 ? 1603 LYS A N   1 
ATOM   12229 C  CA  . LYS A 1 1603 ? -17.765  -1.819  38.717  1.00 262.68 ? 1603 LYS A CA  1 
ATOM   12230 C  C   . LYS A 1 1603 ? -17.384  -2.098  37.259  1.00 272.20 ? 1603 LYS A C   1 
ATOM   12231 O  O   . LYS A 1 1603 ? -17.286  -1.167  36.456  1.00 272.69 ? 1603 LYS A O   1 
ATOM   12232 C  CB  . LYS A 1 1603 ? -19.046  -2.580  39.118  1.00 259.47 ? 1603 LYS A CB  1 
ATOM   12233 C  CG  . LYS A 1 1603 ? -19.210  -4.002  38.564  1.00 254.83 ? 1603 LYS A CG  1 
ATOM   12234 C  CD  . LYS A 1 1603 ? -19.054  -5.068  39.627  1.00 250.72 ? 1603 LYS A CD  1 
ATOM   12235 C  CE  . LYS A 1 1603 ? -19.547  -6.400  39.108  1.00 247.14 ? 1603 LYS A CE  1 
ATOM   12236 N  NZ  . LYS A 1 1603 ? -19.731  -7.366  40.209  1.00 245.92 ? 1603 LYS A NZ  1 
ATOM   12237 N  N   . VAL A 1 1604 ? -17.141  -3.365  36.928  1.00 280.73 ? 1604 VAL A N   1 
ATOM   12238 C  CA  . VAL A 1 1604 ? -16.887  -3.770  35.545  1.00 288.54 ? 1604 VAL A CA  1 
ATOM   12239 C  C   . VAL A 1 1604 ? -15.517  -3.304  35.047  1.00 295.85 ? 1604 VAL A C   1 
ATOM   12240 O  O   . VAL A 1 1604 ? -14.884  -2.440  35.659  1.00 296.09 ? 1604 VAL A O   1 
ATOM   12241 C  CB  . VAL A 1 1604 ? -18.011  -3.268  34.594  1.00 294.59 ? 1604 VAL A CB  1 
ATOM   12242 C  CG1 . VAL A 1 1604 ? -17.731  -3.664  33.149  1.00 293.80 ? 1604 VAL A CG1 1 
ATOM   12243 C  CG2 . VAL A 1 1604 ? -19.365  -3.803  35.042  1.00 295.36 ? 1604 VAL A CG2 1 
ATOM   12244 N  N   . THR A 1 1605 ? -15.062  -3.898  33.945  1.00 302.48 ? 1605 THR A N   1 
ATOM   12245 C  CA  . THR A 1 1605 ? -13.784  -3.542  33.340  1.00 308.39 ? 1605 THR A CA  1 
ATOM   12246 C  C   . THR A 1 1605 ? -13.774  -2.087  32.894  1.00 314.14 ? 1605 THR A C   1 
ATOM   12247 O  O   . THR A 1 1605 ? -14.626  -1.658  32.115  1.00 314.67 ? 1605 THR A O   1 
ATOM   12248 C  CB  . THR A 1 1605 ? -13.450  -4.432  32.115  1.00 314.04 ? 1605 THR A CB  1 
ATOM   12249 O  OG1 . THR A 1 1605 ? -14.411  -4.207  31.076  1.00 314.32 ? 1605 THR A OG1 1 
ATOM   12250 C  CG2 . THR A 1 1605 ? -13.445  -5.907  32.494  1.00 313.66 ? 1605 THR A CG2 1 
ATOM   12251 N  N   . CYS A 1 1606 ? -12.801  -1.331  33.390  1.00 318.10 ? 1606 CYS A N   1 
ATOM   12252 C  CA  . CYS A 1 1606 ? -12.590  0.030   32.923  1.00 320.53 ? 1606 CYS A CA  1 
ATOM   12253 C  C   . CYS A 1 1606 ? -11.103  0.311   32.777  1.00 318.68 ? 1606 CYS A C   1 
ATOM   12254 O  O   . CYS A 1 1606 ? -10.457  0.818   33.696  1.00 321.25 ? 1606 CYS A O   1 
ATOM   12255 C  CB  . CYS A 1 1606 ? -13.222  1.042   33.865  1.00 323.03 ? 1606 CYS A CB  1 
ATOM   12256 S  SG  . CYS A 1 1606 ? -13.259  2.675   33.138  1.00 262.71 ? 1606 CYS A SG  1 
ATOM   12257 N  N   . THR A 1 1607 ? -10.580  -0.018  31.600  1.00 313.90 ? 1607 THR A N   1 
ATOM   12258 C  CA  . THR A 1 1607 ? -9.149   0.026   31.324  1.00 309.92 ? 1607 THR A CA  1 
ATOM   12259 C  C   . THR A 1 1607 ? -8.682   1.438   30.979  1.00 308.27 ? 1607 THR A C   1 
ATOM   12260 O  O   . THR A 1 1607 ? -7.841   1.614   30.098  1.00 309.00 ? 1607 THR A O   1 
ATOM   12261 C  CB  . THR A 1 1607 ? -8.779   -0.917  30.141  1.00 336.23 ? 1607 THR A CB  1 
ATOM   12262 O  OG1 . THR A 1 1607 ? -9.649   -2.057  30.127  1.00 336.61 ? 1607 THR A OG1 1 
ATOM   12263 C  CG2 . THR A 1 1607 ? -7.333   -1.385  30.246  1.00 335.13 ? 1607 THR A CG2 1 
ATOM   12264 N  N   . ASN A 1 1608 ? -9.213   2.443   31.671  1.00 305.27 ? 1608 ASN A N   1 
ATOM   12265 C  CA  . ASN A 1 1608 ? -8.969   3.821   31.256  1.00 301.11 ? 1608 ASN A CA  1 
ATOM   12266 C  C   . ASN A 1 1608 ? -8.819   4.854   32.382  1.00 295.23 ? 1608 ASN A C   1 
ATOM   12267 O  O   . ASN A 1 1608 ? -9.152   6.023   32.196  1.00 295.38 ? 1608 ASN A O   1 
ATOM   12268 C  CB  . ASN A 1 1608 ? -10.057  4.267   30.270  1.00 302.53 ? 1608 ASN A CB  1 
ATOM   12269 C  CG  . ASN A 1 1608 ? -10.152  3.362   29.044  1.00 302.12 ? 1608 ASN A CG  1 
ATOM   12270 O  OD1 . ASN A 1 1608 ? -11.183  2.733   28.800  1.00 302.38 ? 1608 ASN A OD1 1 
ATOM   12271 N  ND2 . ASN A 1 1608 ? -9.074   3.295   28.271  1.00 301.25 ? 1608 ASN A ND2 1 
ATOM   12272 N  N   . ALA A 1 1609 ? -8.318   4.422   33.537  1.00 288.64 ? 1609 ALA A N   1 
ATOM   12273 C  CA  . ALA A 1 1609 ? -8.012   5.332   34.641  1.00 282.13 ? 1609 ALA A CA  1 
ATOM   12274 C  C   . ALA A 1 1609 ? -7.754   4.573   35.931  1.00 276.46 ? 1609 ALA A C   1 
ATOM   12275 O  O   . ALA A 1 1609 ? -8.605   3.810   36.386  1.00 277.27 ? 1609 ALA A O   1 
ATOM   12276 C  CB  . ALA A 1 1609 ? -9.134   6.331   34.847  1.00 282.20 ? 1609 ALA A CB  1 
ATOM   12277 N  N   . GLU A 1 1610 ? -6.589   4.794   36.531  1.00 270.37 ? 1610 GLU A N   1 
ATOM   12278 C  CA  . GLU A 1 1610 ? -6.262   4.127   37.788  1.00 265.38 ? 1610 GLU A CA  1 
ATOM   12279 C  C   . GLU A 1 1610 ? -5.716   5.092   38.820  1.00 260.45 ? 1610 GLU A C   1 
ATOM   12280 O  O   . GLU A 1 1610 ? -4.588   5.569   38.709  1.00 259.41 ? 1610 GLU A O   1 
ATOM   12281 C  CB  . GLU A 1 1610 ? -5.270   2.976   37.576  1.00 265.02 ? 1610 GLU A CB  1 
ATOM   12282 C  CG  . GLU A 1 1610 ? -5.916   1.648   37.202  1.00 265.69 ? 1610 GLU A CG  1 
ATOM   12283 C  CD  . GLU A 1 1610 ? -7.187   1.364   37.989  1.00 267.60 ? 1610 GLU A CD  1 
ATOM   12284 O  OE1 . GLU A 1 1610 ? -7.292   1.806   39.156  1.00 268.72 ? 1610 GLU A OE1 1 
ATOM   12285 O  OE2 . GLU A 1 1610 ? -8.085   0.696   37.434  1.00 268.00 ? 1610 GLU A OE2 1 
ATOM   12286 N  N   . LEU A 1 1611 ? -6.523   5.374   39.832  1.00 257.35 ? 1611 LEU A N   1 
ATOM   12287 C  CA  . LEU A 1 1611 ? -6.080   6.250   40.897  1.00 254.86 ? 1611 LEU A CA  1 
ATOM   12288 C  C   . LEU A 1 1611 ? -5.064   5.518   41.772  1.00 252.66 ? 1611 LEU A C   1 
ATOM   12289 O  O   . LEU A 1 1611 ? -5.288   4.373   42.172  1.00 252.85 ? 1611 LEU A O   1 
ATOM   12290 C  CB  . LEU A 1 1611 ? -7.274   6.787   41.704  1.00 254.80 ? 1611 LEU A CB  1 
ATOM   12291 C  CG  . LEU A 1 1611 ? -8.338   5.825   42.239  1.00 254.14 ? 1611 LEU A CG  1 
ATOM   12292 C  CD1 . LEU A 1 1611 ? -7.862   5.189   43.533  1.00 254.04 ? 1611 LEU A CD1 1 
ATOM   12293 C  CD2 . LEU A 1 1611 ? -9.667   6.544   42.456  1.00 254.28 ? 1611 LEU A CD2 1 
ATOM   12294 N  N   . VAL A 1 1612 ? -3.933   6.175   42.026  1.00 250.09 ? 1612 VAL A N   1 
ATOM   12295 C  CA  . VAL A 1 1612 ? -2.895   5.641   42.905  1.00 247.40 ? 1612 VAL A CA  1 
ATOM   12296 C  C   . VAL A 1 1612 ? -3.214   5.939   44.371  1.00 246.74 ? 1612 VAL A C   1 
ATOM   12297 O  O   . VAL A 1 1612 ? -3.311   7.103   44.767  1.00 248.21 ? 1612 VAL A O   1 
ATOM   12298 C  CB  . VAL A 1 1612 ? -1.514   6.245   42.575  1.00 245.80 ? 1612 VAL A CB  1 
ATOM   12299 C  CG1 . VAL A 1 1612 ? -0.416   5.539   43.365  1.00 245.35 ? 1612 VAL A CG1 1 
ATOM   12300 C  CG2 . VAL A 1 1612 ? -1.239   6.180   41.083  1.00 244.60 ? 1612 VAL A CG2 1 
ATOM   12301 N  N   . LYS A 1 1613 ? -3.372   4.891   45.175  1.00 243.66 ? 1613 LYS A N   1 
ATOM   12302 C  CA  . LYS A 1 1613 ? -3.662   5.056   46.598  1.00 240.93 ? 1613 LYS A CA  1 
ATOM   12303 C  C   . LYS A 1 1613 ? -2.595   5.918   47.271  1.00 236.65 ? 1613 LYS A C   1 
ATOM   12304 O  O   . LYS A 1 1613 ? -1.408   5.800   46.965  1.00 235.29 ? 1613 LYS A O   1 
ATOM   12305 C  CB  . LYS A 1 1613 ? -3.774   3.687   47.281  1.00 241.47 ? 1613 LYS A CB  1 
ATOM   12306 C  CG  . LYS A 1 1613 ? -3.674   3.719   48.800  1.00 242.84 ? 1613 LYS A CG  1 
ATOM   12307 C  CD  . LYS A 1 1613 ? -4.757   4.573   49.428  1.00 244.46 ? 1613 LYS A CD  1 
ATOM   12308 C  CE  . LYS A 1 1613 ? -4.418   4.904   50.875  1.00 245.78 ? 1613 LYS A CE  1 
ATOM   12309 N  NZ  . LYS A 1 1613 ? -4.483   3.710   51.760  1.00 246.02 ? 1613 LYS A NZ  1 
ATOM   12310 N  N   . GLY A 1 1614 ? -3.026   6.791   48.177  1.00 233.32 ? 1614 GLY A N   1 
ATOM   12311 C  CA  . GLY A 1 1614 ? -2.109   7.645   48.908  1.00 229.11 ? 1614 GLY A CA  1 
ATOM   12312 C  C   . GLY A 1 1614 ? -1.771   8.928   48.182  1.00 223.70 ? 1614 GLY A C   1 
ATOM   12313 O  O   . GLY A 1 1614 ? -1.023   9.768   48.682  1.00 223.90 ? 1614 GLY A O   1 
ATOM   12314 N  N   . ARG A 1 1615 ? -2.313   9.074   46.983  1.00 218.92 ? 1615 ARG A N   1 
ATOM   12315 C  CA  . ARG A 1 1615 ? -2.202   10.325  46.256  1.00 215.61 ? 1615 ARG A CA  1 
ATOM   12316 C  C   . ARG A 1 1615 ? -3.532   11.096  46.291  1.00 212.87 ? 1615 ARG A C   1 
ATOM   12317 O  O   . ARG A 1 1615 ? -4.611   10.503  46.407  1.00 211.56 ? 1615 ARG A O   1 
ATOM   12318 C  CB  . ARG A 1 1615 ? -1.778   10.069  44.813  1.00 216.29 ? 1615 ARG A CB  1 
ATOM   12319 C  CG  . ARG A 1 1615 ? -0.356   9.554   44.603  1.00 217.70 ? 1615 ARG A CG  1 
ATOM   12320 C  CD  . ARG A 1 1615 ? -0.272   9.078   43.160  1.00 219.85 ? 1615 ARG A CD  1 
ATOM   12321 N  NE  . ARG A 1 1615 ? 1.070    9.023   42.598  1.00 221.02 ? 1615 ARG A NE  1 
ATOM   12322 C  CZ  . ARG A 1 1615 ? 1.310    8.949   41.291  1.00 221.16 ? 1615 ARG A CZ  1 
ATOM   12323 N  NH1 . ARG A 1 1615 ? 0.299    8.933   40.427  1.00 220.85 ? 1615 ARG A NH1 1 
ATOM   12324 N  NH2 . ARG A 1 1615 ? 2.556    8.898   40.843  1.00 220.81 ? 1615 ARG A NH2 1 
ATOM   12325 N  N   . GLN A 1 1616 ? -3.432   12.421  46.183  1.00 211.76 ? 1616 GLN A N   1 
ATOM   12326 C  CA  . GLN A 1 1616 ? -4.574   13.337  46.259  1.00 210.61 ? 1616 GLN A CA  1 
ATOM   12327 C  C   . GLN A 1 1616 ? -5.068   13.796  44.899  1.00 213.40 ? 1616 GLN A C   1 
ATOM   12328 O  O   . GLN A 1 1616 ? -4.556   14.765  44.342  1.00 213.09 ? 1616 GLN A O   1 
ATOM   12329 C  CB  . GLN A 1 1616 ? -4.196   14.588  47.048  1.00 206.12 ? 1616 GLN A CB  1 
ATOM   12330 C  CG  . GLN A 1 1616 ? -3.732   14.326  48.465  1.00 201.77 ? 1616 GLN A CG  1 
ATOM   12331 C  CD  . GLN A 1 1616 ? -3.207   15.573  49.145  1.00 197.20 ? 1616 GLN A CD  1 
ATOM   12332 O  OE1 . GLN A 1 1616 ? -3.431   16.700  48.684  1.00 195.31 ? 1616 GLN A OE1 1 
ATOM   12333 N  NE2 . GLN A 1 1616 ? -2.512   15.379  50.258  1.00 195.54 ? 1616 GLN A NE2 1 
ATOM   12334 N  N   . TYR A 1 1617 ? -6.085   13.115  44.387  1.00 217.28 ? 1617 TYR A N   1 
ATOM   12335 C  CA  . TYR A 1 1617 ? -6.683   13.466  43.104  1.00 220.17 ? 1617 TYR A CA  1 
ATOM   12336 C  C   . TYR A 1 1617 ? -7.787   14.511  43.293  1.00 212.91 ? 1617 TYR A C   1 
ATOM   12337 O  O   . TYR A 1 1617 ? -8.600   14.412  44.216  1.00 210.94 ? 1617 TYR A O   1 
ATOM   12338 C  CB  . TYR A 1 1617 ? -7.215   12.206  42.378  1.00 230.66 ? 1617 TYR A CB  1 
ATOM   12339 C  CG  . TYR A 1 1617 ? -6.132   11.215  41.942  1.00 239.65 ? 1617 TYR A CG  1 
ATOM   12340 C  CD1 . TYR A 1 1617 ? -5.580   10.310  42.844  1.00 243.66 ? 1617 TYR A CD1 1 
ATOM   12341 C  CD2 . TYR A 1 1617 ? -5.668   11.187  40.629  1.00 242.88 ? 1617 TYR A CD2 1 
ATOM   12342 C  CE1 . TYR A 1 1617 ? -4.595   9.413   42.455  1.00 245.58 ? 1617 TYR A CE1 1 
ATOM   12343 C  CE2 . TYR A 1 1617 ? -4.680   10.291  40.232  1.00 244.67 ? 1617 TYR A CE2 1 
ATOM   12344 C  CZ  . TYR A 1 1617 ? -4.148   9.407   41.150  1.00 245.65 ? 1617 TYR A CZ  1 
ATOM   12345 O  OH  . TYR A 1 1617 ? -3.167   8.514   40.769  1.00 245.08 ? 1617 TYR A OH  1 
ATOM   12346 N  N   . LEU A 1 1618 ? -7.789   15.524  42.430  1.00 207.95 ? 1618 LEU A N   1 
ATOM   12347 C  CA  . LEU A 1 1618 ? -8.877   16.492  42.406  1.00 202.74 ? 1618 LEU A CA  1 
ATOM   12348 C  C   . LEU A 1 1618 ? -9.982   15.949  41.522  1.00 199.33 ? 1618 LEU A C   1 
ATOM   12349 O  O   . LEU A 1 1618 ? -9.723   15.304  40.509  1.00 197.97 ? 1618 LEU A O   1 
ATOM   12350 C  CB  . LEU A 1 1618 ? -8.417   17.880  41.952  1.00 197.77 ? 1618 LEU A CB  1 
ATOM   12351 C  CG  . LEU A 1 1618 ? -8.039   18.147  40.506  1.00 190.93 ? 1618 LEU A CG  1 
ATOM   12352 C  CD1 . LEU A 1 1618 ? -9.282   18.173  39.666  1.00 189.56 ? 1618 LEU A CD1 1 
ATOM   12353 C  CD2 . LEU A 1 1618 ? -7.349   19.481  40.447  1.00 188.30 ? 1618 LEU A CD2 1 
ATOM   12354 N  N   . ILE A 1 1619 ? -11.214  16.225  41.920  1.00 196.86 ? 1619 ILE A N   1 
ATOM   12355 C  CA  . ILE A 1 1619 ? -12.360  15.489  41.434  1.00 194.09 ? 1619 ILE A CA  1 
ATOM   12356 C  C   . ILE A 1 1619 ? -13.448  16.479  41.067  1.00 191.74 ? 1619 ILE A C   1 
ATOM   12357 O  O   . ILE A 1 1619 ? -13.597  17.496  41.734  1.00 192.13 ? 1619 ILE A O   1 
ATOM   12358 C  CB  . ILE A 1 1619 ? -12.879  14.502  42.522  1.00 202.37 ? 1619 ILE A CB  1 
ATOM   12359 C  CG1 . ILE A 1 1619 ? -12.171  13.126  42.433  1.00 184.64 ? 1619 ILE A CG1 1 
ATOM   12360 C  CG2 . ILE A 1 1619 ? -14.396  14.344  42.421  1.00 202.60 ? 1619 ILE A CG2 1 
ATOM   12361 C  CD1 . ILE A 1 1619 ? -10.953  12.932  43.348  1.00 183.18 ? 1619 ILE A CD1 1 
ATOM   12362 N  N   . MET A 1 1620 ? -14.196  16.187  40.001  1.00 190.51 ? 1620 MET A N   1 
ATOM   12363 C  CA  . MET A 1 1620 ? -15.230  17.104  39.504  1.00 190.33 ? 1620 MET A CA  1 
ATOM   12364 C  C   . MET A 1 1620 ? -16.323  16.390  38.706  1.00 189.14 ? 1620 MET A C   1 
ATOM   12365 O  O   . MET A 1 1620 ? -16.045  15.804  37.678  1.00 184.89 ? 1620 MET A O   1 
ATOM   12366 C  CB  . MET A 1 1620 ? -14.604  18.243  38.666  1.00 190.46 ? 1620 MET A CB  1 
ATOM   12367 C  CG  . MET A 1 1620 ? -14.020  19.397  39.507  1.00 190.83 ? 1620 MET A CG  1 
ATOM   12368 S  SD  . MET A 1 1620 ? -13.380  20.795  38.559  1.00 222.51 ? 1620 MET A SD  1 
ATOM   12369 C  CE  . MET A 1 1620 ? -12.037  20.018  37.659  1.00 250.71 ? 1620 MET A CE  1 
ATOM   12370 N  N   . GLY A 1 1621 ? -17.563  16.461  39.190  1.00 192.95 ? 1621 GLY A N   1 
ATOM   12371 C  CA  . GLY A 1 1621 ? -18.711  15.903  38.497  1.00 194.49 ? 1621 GLY A CA  1 
ATOM   12372 C  C   . GLY A 1 1621 ? -20.038  16.193  39.183  1.00 193.89 ? 1621 GLY A C   1 
ATOM   12373 O  O   . GLY A 1 1621 ? -20.095  16.992  40.111  1.00 191.87 ? 1621 GLY A O   1 
ATOM   12374 N  N   . LYS A 1 1622 ? -21.109  15.551  38.723  1.00 196.92 ? 1622 LYS A N   1 
ATOM   12375 C  CA  . LYS A 1 1622 ? -22.430  15.717  39.337  1.00 202.16 ? 1622 LYS A CA  1 
ATOM   12376 C  C   . LYS A 1 1622 ? -22.442  15.276  40.794  1.00 213.25 ? 1622 LYS A C   1 
ATOM   12377 O  O   . LYS A 1 1622 ? -21.404  14.954  41.348  1.00 213.19 ? 1622 LYS A O   1 
ATOM   12378 C  CB  . LYS A 1 1622 ? -23.513  14.965  38.557  1.00 197.63 ? 1622 LYS A CB  1 
ATOM   12379 C  CG  . LYS A 1 1622 ? -22.994  13.907  37.602  1.00 193.37 ? 1622 LYS A CG  1 
ATOM   12380 C  CD  . LYS A 1 1622 ? -22.603  14.556  36.303  1.00 189.46 ? 1622 LYS A CD  1 
ATOM   12381 C  CE  . LYS A 1 1622 ? -21.529  13.773  35.616  1.00 187.05 ? 1622 LYS A CE  1 
ATOM   12382 N  NZ  . LYS A 1 1622 ? -20.672  14.678  34.808  1.00 185.65 ? 1622 LYS A NZ  1 
ATOM   12383 N  N   . GLU A 1 1623 ? -23.615  15.266  41.418  1.00 224.91 ? 1623 GLU A N   1 
ATOM   12384 C  CA  . GLU A 1 1623 ? -23.688  14.925  42.833  1.00 236.99 ? 1623 GLU A CA  1 
ATOM   12385 C  C   . GLU A 1 1623 ? -23.652  13.419  43.042  1.00 248.83 ? 1623 GLU A C   1 
ATOM   12386 O  O   . GLU A 1 1623 ? -23.405  12.658  42.111  1.00 247.85 ? 1623 GLU A O   1 
ATOM   12387 C  CB  . GLU A 1 1623 ? -24.924  15.547  43.503  1.00 236.97 ? 1623 GLU A CB  1 
ATOM   12388 C  CG  . GLU A 1 1623 ? -26.156  14.643  43.582  1.00 236.78 ? 1623 GLU A CG  1 
ATOM   12389 C  CD  . GLU A 1 1623 ? -27.168  15.097  44.642  1.00 236.92 ? 1623 GLU A CD  1 
ATOM   12390 O  OE1 . GLU A 1 1623 ? -27.253  16.312  44.911  1.00 236.73 ? 1623 GLU A OE1 1 
ATOM   12391 O  OE2 . GLU A 1 1623 ? -27.888  14.241  45.205  1.00 237.14 ? 1623 GLU A OE2 1 
ATOM   12392 N  N   . ALA A 1 1624 ? -23.880  13.005  44.282  1.00 262.28 ? 1624 ALA A N   1 
ATOM   12393 C  CA  . ALA A 1 1624 ? -23.959  11.596  44.641  1.00 275.38 ? 1624 ALA A CA  1 
ATOM   12394 C  C   . ALA A 1 1624 ? -25.408  11.090  44.601  1.00 286.66 ? 1624 ALA A C   1 
ATOM   12395 O  O   . ALA A 1 1624 ? -26.338  11.834  44.912  1.00 287.18 ? 1624 ALA A O   1 
ATOM   12396 C  CB  . ALA A 1 1624 ? -23.365  11.394  46.016  1.00 277.43 ? 1624 ALA A CB  1 
ATOM   12397 N  N   . LEU A 1 1625 ? -25.595  9.825   44.231  1.00 296.76 ? 1625 LEU A N   1 
ATOM   12398 C  CA  . LEU A 1 1625 ? -26.939  9.263   44.063  1.00 305.93 ? 1625 LEU A CA  1 
ATOM   12399 C  C   . LEU A 1 1625 ? -27.580  8.797   45.372  1.00 309.17 ? 1625 LEU A C   1 
ATOM   12400 O  O   . LEU A 1 1625 ? -27.055  7.922   46.056  1.00 310.23 ? 1625 LEU A O   1 
ATOM   12401 C  CB  . LEU A 1 1625 ? -26.930  8.124   43.029  1.00 310.73 ? 1625 LEU A CB  1 
ATOM   12402 C  CG  . LEU A 1 1625 ? -26.123  6.838   43.259  1.00 314.03 ? 1625 LEU A CG  1 
ATOM   12403 C  CD1 . LEU A 1 1625 ? -26.921  5.814   44.056  1.00 315.63 ? 1625 LEU A CD1 1 
ATOM   12404 C  CD2 . LEU A 1 1625 ? -25.697  6.240   41.925  1.00 314.12 ? 1625 LEU A CD2 1 
ATOM   12405 N  N   . GLN A 1 1626 ? -28.723  9.381   45.714  1.00 310.12 ? 1626 GLN A N   1 
ATOM   12406 C  CA  . GLN A 1 1626 ? -29.425  8.984   46.929  1.00 310.67 ? 1626 GLN A CA  1 
ATOM   12407 C  C   . GLN A 1 1626 ? -30.342  7.787   46.714  1.00 305.36 ? 1626 GLN A C   1 
ATOM   12408 O  O   . GLN A 1 1626 ? -31.316  7.861   45.963  1.00 305.15 ? 1626 GLN A O   1 
ATOM   12409 C  CB  . GLN A 1 1626 ? -30.250  10.141  47.502  1.00 315.36 ? 1626 GLN A CB  1 
ATOM   12410 C  CG  . GLN A 1 1626 ? -29.461  11.231  48.194  1.00 318.73 ? 1626 GLN A CG  1 
ATOM   12411 C  CD  . GLN A 1 1626 ? -30.361  12.248  48.875  1.00 320.80 ? 1626 GLN A CD  1 
ATOM   12412 O  OE1 . GLN A 1 1626 ? -31.422  11.903  49.398  1.00 321.60 ? 1626 GLN A OE1 1 
ATOM   12413 N  NE2 . GLN A 1 1626 ? -29.939  13.508  48.873  1.00 321.14 ? 1626 GLN A NE2 1 
ATOM   12414 N  N   . ILE A 1 1627 ? -30.012  6.678   47.367  1.00 299.96 ? 1627 ILE A N   1 
ATOM   12415 C  CA  . ILE A 1 1627 ? -30.996  5.645   47.636  1.00 294.49 ? 1627 ILE A CA  1 
ATOM   12416 C  C   . ILE A 1 1627 ? -31.577  5.998   49.008  1.00 289.68 ? 1627 ILE A C   1 
ATOM   12417 O  O   . ILE A 1 1627 ? -31.165  5.433   50.020  1.00 289.58 ? 1627 ILE A O   1 
ATOM   12418 C  CB  . ILE A 1 1627 ? -30.374  4.220   47.631  1.00 287.96 ? 1627 ILE A CB  1 
ATOM   12419 C  CG1 . ILE A 1 1627 ? -28.985  4.219   48.272  1.00 287.76 ? 1627 ILE A CG1 1 
ATOM   12420 C  CG2 . ILE A 1 1627 ? -30.264  3.687   46.210  1.00 287.41 ? 1627 ILE A CG2 1 
ATOM   12421 C  CD1 . ILE A 1 1627 ? -27.865  4.547   47.309  1.00 286.87 ? 1627 ILE A CD1 1 
ATOM   12422 N  N   . LYS A 1 1628 ? -32.528  6.938   49.031  1.00 284.45 ? 1628 LYS A N   1 
ATOM   12423 C  CA  . LYS A 1 1628 ? -32.977  7.589   50.274  1.00 279.99 ? 1628 LYS A CA  1 
ATOM   12424 C  C   . LYS A 1 1628 ? -33.038  6.685   51.507  1.00 287.37 ? 1628 LYS A C   1 
ATOM   12425 O  O   . LYS A 1 1628 ? -32.351  6.949   52.498  1.00 288.53 ? 1628 LYS A O   1 
ATOM   12426 C  CB  . LYS A 1 1628 ? -34.325  8.303   50.092  1.00 268.14 ? 1628 LYS A CB  1 
ATOM   12427 C  CG  . LYS A 1 1628 ? -34.812  9.007   51.362  1.00 258.25 ? 1628 LYS A CG  1 
ATOM   12428 C  CD  . LYS A 1 1628 ? -36.135  9.731   51.163  1.00 249.41 ? 1628 LYS A CD  1 
ATOM   12429 C  CE  . LYS A 1 1628 ? -37.295  8.760   51.105  1.00 243.25 ? 1628 LYS A CE  1 
ATOM   12430 N  NZ  . LYS A 1 1628 ? -37.451  8.052   52.397  1.00 240.94 ? 1628 LYS A NZ  1 
ATOM   12431 N  N   . TYR A 1 1629 ? -33.849  5.627   51.454  1.00 293.36 ? 1629 TYR A N   1 
ATOM   12432 C  CA  . TYR A 1 1629 ? -34.015  4.758   52.622  1.00 300.00 ? 1629 TYR A CA  1 
ATOM   12433 C  C   . TYR A 1 1629 ? -34.797  3.456   52.372  1.00 308.33 ? 1629 TYR A C   1 
ATOM   12434 O  O   . TYR A 1 1629 ? -35.924  3.473   51.873  1.00 308.84 ? 1629 TYR A O   1 
ATOM   12435 C  CB  . TYR A 1 1629 ? -34.695  5.543   53.748  1.00 298.48 ? 1629 TYR A CB  1 
ATOM   12436 C  CG  . TYR A 1 1629 ? -33.972  5.520   55.078  1.00 297.57 ? 1629 TYR A CG  1 
ATOM   12437 C  CD1 . TYR A 1 1629 ? -32.825  6.276   55.276  1.00 296.55 ? 1629 TYR A CD1 1 
ATOM   12438 C  CD2 . TYR A 1 1629 ? -34.454  4.771   56.142  1.00 297.78 ? 1629 TYR A CD2 1 
ATOM   12439 C  CE1 . TYR A 1 1629 ? -32.172  6.275   56.486  1.00 296.78 ? 1629 TYR A CE1 1 
ATOM   12440 C  CE2 . TYR A 1 1629 ? -33.806  4.764   57.357  1.00 298.04 ? 1629 TYR A CE2 1 
ATOM   12441 C  CZ  . TYR A 1 1629 ? -32.667  5.519   57.523  1.00 297.54 ? 1629 TYR A CZ  1 
ATOM   12442 O  OH  . TYR A 1 1629 ? -32.016  5.516   58.731  1.00 298.20 ? 1629 TYR A OH  1 
ATOM   12443 N  N   . ASN A 1 1630 ? -34.169  2.335   52.720  1.00 315.96 ? 1630 ASN A N   1 
ATOM   12444 C  CA  . ASN A 1 1630 ? -34.860  1.071   52.981  1.00 322.71 ? 1630 ASN A CA  1 
ATOM   12445 C  C   . ASN A 1 1630 ? -34.129  0.343   54.117  1.00 323.55 ? 1630 ASN A C   1 
ATOM   12446 O  O   . ASN A 1 1630 ? -33.764  -0.831  54.013  1.00 323.08 ? 1630 ASN A O   1 
ATOM   12447 C  CB  . ASN A 1 1630 ? -35.064  0.207   51.719  1.00 327.28 ? 1630 ASN A CB  1 
ATOM   12448 C  CG  . ASN A 1 1630 ? -33.793  0.007   50.915  1.00 330.72 ? 1630 ASN A CG  1 
ATOM   12449 O  OD1 . ASN A 1 1630 ? -32.711  -0.177  51.469  1.00 332.38 ? 1630 ASN A OD1 1 
ATOM   12450 N  ND2 . ASN A 1 1630 ? -33.928  0.018   49.591  1.00 331.03 ? 1630 ASN A ND2 1 
ATOM   12451 N  N   . PHE A 1 1631 ? -33.937  1.101   55.199  1.00 323.54 ? 1631 PHE A N   1 
ATOM   12452 C  CA  . PHE A 1 1631 ? -33.178  0.726   56.399  1.00 321.86 ? 1631 PHE A CA  1 
ATOM   12453 C  C   . PHE A 1 1631 ? -31.760  1.321   56.466  1.00 320.34 ? 1631 PHE A C   1 
ATOM   12454 O  O   . PHE A 1 1631 ? -30.813  0.657   56.892  1.00 322.07 ? 1631 PHE A O   1 
ATOM   12455 C  CB  . PHE A 1 1631 ? -33.204  -0.782  56.688  1.00 319.58 ? 1631 PHE A CB  1 
ATOM   12456 C  CG  . PHE A 1 1631 ? -34.387  -1.212  57.517  1.00 317.27 ? 1631 PHE A CG  1 
ATOM   12457 C  CD1 . PHE A 1 1631 ? -34.831  -0.428  58.569  1.00 316.70 ? 1631 PHE A CD1 1 
ATOM   12458 C  CD2 . PHE A 1 1631 ? -35.048  -2.398  57.252  1.00 315.98 ? 1631 PHE A CD2 1 
ATOM   12459 C  CE1 . PHE A 1 1631 ? -35.915  -0.813  59.335  1.00 316.59 ? 1631 PHE A CE1 1 
ATOM   12460 C  CE2 . PHE A 1 1631 ? -36.134  -2.789  58.018  1.00 315.85 ? 1631 PHE A CE2 1 
ATOM   12461 C  CZ  . PHE A 1 1631 ? -36.566  -1.995  59.060  1.00 316.30 ? 1631 PHE A CZ  1 
ATOM   12462 N  N   . SER A 1 1632 ? -31.643  2.572   56.017  1.00 316.16 ? 1632 SER A N   1 
ATOM   12463 C  CA  . SER A 1 1632 ? -30.540  3.470   56.388  1.00 312.24 ? 1632 SER A CA  1 
ATOM   12464 C  C   . SER A 1 1632 ? -29.237  3.432   55.569  1.00 307.34 ? 1632 SER A C   1 
ATOM   12465 O  O   . SER A 1 1632 ? -28.421  2.526   55.746  1.00 308.86 ? 1632 SER A O   1 
ATOM   12466 C  CB  . SER A 1 1632 ? -30.209  3.290   57.874  1.00 313.57 ? 1632 SER A CB  1 
ATOM   12467 O  OG  . SER A 1 1632 ? -31.388  3.101   58.639  1.00 314.40 ? 1632 SER A OG  1 
ATOM   12468 N  N   . PHE A 1 1633 ? -29.051  4.431   54.697  1.00 300.35 ? 1633 PHE A N   1 
ATOM   12469 C  CA  . PHE A 1 1633 ? -27.726  4.770   54.128  1.00 293.77 ? 1633 PHE A CA  1 
ATOM   12470 C  C   . PHE A 1 1633 ? -27.635  5.904   53.074  1.00 311.97 ? 1633 PHE A C   1 
ATOM   12471 O  O   . PHE A 1 1633 ? -28.446  6.835   53.068  1.00 311.86 ? 1633 PHE A O   1 
ATOM   12472 C  CB  . PHE A 1 1633 ? -26.905  3.535   53.708  1.00 288.46 ? 1633 PHE A CB  1 
ATOM   12473 C  CG  . PHE A 1 1633 ? -25.713  3.267   54.604  1.00 285.67 ? 1633 PHE A CG  1 
ATOM   12474 C  CD1 . PHE A 1 1633 ? -24.697  4.202   54.719  1.00 284.46 ? 1633 PHE A CD1 1 
ATOM   12475 C  CD2 . PHE A 1 1633 ? -25.609  2.088   55.324  1.00 285.50 ? 1633 PHE A CD2 1 
ATOM   12476 C  CE1 . PHE A 1 1633 ? -23.609  3.971   55.534  1.00 285.05 ? 1633 PHE A CE1 1 
ATOM   12477 C  CE2 . PHE A 1 1633 ? -24.519  1.853   56.141  1.00 286.03 ? 1633 PHE A CE2 1 
ATOM   12478 C  CZ  . PHE A 1 1633 ? -23.520  2.794   56.244  1.00 285.98 ? 1633 PHE A CZ  1 
ATOM   12479 N  N   . ARG A 1 1634 ? -26.638  5.792   52.191  1.00 311.26 ? 1634 ARG A N   1 
ATOM   12480 C  CA  . ARG A 1 1634 ? -25.974  6.958   51.585  1.00 310.85 ? 1634 ARG A CA  1 
ATOM   12481 C  C   . ARG A 1 1634 ? -26.235  7.392   50.130  1.00 309.06 ? 1634 ARG A C   1 
ATOM   12482 O  O   . ARG A 1 1634 ? -27.378  7.499   49.680  1.00 308.16 ? 1634 ARG A O   1 
ATOM   12483 C  CB  . ARG A 1 1634 ? -24.458  6.838   51.782  1.00 311.96 ? 1634 ARG A CB  1 
ATOM   12484 C  CG  . ARG A 1 1634 ? -24.016  6.902   53.229  1.00 314.04 ? 1634 ARG A CG  1 
ATOM   12485 C  CD  . ARG A 1 1634 ? -24.457  8.200   53.874  1.00 316.05 ? 1634 ARG A CD  1 
ATOM   12486 N  NE  . ARG A 1 1634 ? -24.263  8.178   55.318  1.00 318.85 ? 1634 ARG A NE  1 
ATOM   12487 C  CZ  . ARG A 1 1634 ? -24.516  9.207   56.118  1.00 321.61 ? 1634 ARG A CZ  1 
ATOM   12488 N  NH1 . ARG A 1 1634 ? -24.970  10.347  55.615  1.00 321.92 ? 1634 ARG A NH1 1 
ATOM   12489 N  NH2 . ARG A 1 1634 ? -24.313  9.096   57.421  1.00 323.65 ? 1634 ARG A NH2 1 
ATOM   12490 N  N   . TYR A 1 1635 ? -25.131  7.630   49.415  1.00 308.65 ? 1635 TYR A N   1 
ATOM   12491 C  CA  . TYR A 1 1635 ? -25.081  8.575   48.299  1.00 308.29 ? 1635 TYR A CA  1 
ATOM   12492 C  C   . TYR A 1 1635 ? -24.200  8.178   47.107  1.00 306.87 ? 1635 TYR A C   1 
ATOM   12493 O  O   . TYR A 1 1635 ? -24.678  7.833   46.028  1.00 306.31 ? 1635 TYR A O   1 
ATOM   12494 C  CB  . TYR A 1 1635 ? -24.465  9.883   48.815  1.00 309.38 ? 1635 TYR A CB  1 
ATOM   12495 C  CG  . TYR A 1 1635 ? -25.407  10.905  49.406  1.00 310.62 ? 1635 TYR A CG  1 
ATOM   12496 C  CD1 . TYR A 1 1635 ? -25.647  10.951  50.771  1.00 311.93 ? 1635 TYR A CD1 1 
ATOM   12497 C  CD2 . TYR A 1 1635 ? -26.015  11.857  48.601  1.00 310.52 ? 1635 TYR A CD2 1 
ATOM   12498 C  CE1 . TYR A 1 1635 ? -26.492  11.900  51.313  1.00 312.71 ? 1635 TYR A CE1 1 
ATOM   12499 C  CE2 . TYR A 1 1635 ? -26.859  12.810  49.132  1.00 311.16 ? 1635 TYR A CE2 1 
ATOM   12500 C  CZ  . TYR A 1 1635 ? -27.096  12.827  50.487  1.00 312.20 ? 1635 TYR A CZ  1 
ATOM   12501 O  OH  . TYR A 1 1635 ? -27.940  13.779  51.012  1.00 312.47 ? 1635 TYR A OH  1 
ATOM   12502 N  N   . ILE A 1 1636 ? -22.897  8.210   47.361  1.00 306.09 ? 1636 ILE A N   1 
ATOM   12503 C  CA  . ILE A 1 1636 ? -21.870  8.641   46.400  1.00 304.98 ? 1636 ILE A CA  1 
ATOM   12504 C  C   . ILE A 1 1636 ? -21.975  8.445   44.875  1.00 305.18 ? 1636 ILE A C   1 
ATOM   12505 O  O   . ILE A 1 1636 ? -22.957  7.941   44.334  1.00 304.64 ? 1636 ILE A O   1 
ATOM   12506 C  CB  . ILE A 1 1636 ? -20.463  8.252   46.868  1.00 303.74 ? 1636 ILE A CB  1 
ATOM   12507 C  CG1 . ILE A 1 1636 ? -19.451  9.305   46.398  1.00 302.30 ? 1636 ILE A CG1 1 
ATOM   12508 C  CG2 . ILE A 1 1636 ? -20.124  6.847   46.388  1.00 303.29 ? 1636 ILE A CG2 1 
ATOM   12509 C  CD1 . ILE A 1 1636 ? -19.966  10.735  46.450  1.00 301.83 ? 1636 ILE A CD1 1 
ATOM   12510 N  N   . TYR A 1 1637 ? -20.884  8.842   44.226  1.00 306.02 ? 1637 TYR A N   1 
ATOM   12511 C  CA  . TYR A 1 1637 ? -20.852  9.360   42.870  1.00 306.56 ? 1637 TYR A CA  1 
ATOM   12512 C  C   . TYR A 1 1637 ? -20.531  8.342   41.777  1.00 305.68 ? 1637 TYR A C   1 
ATOM   12513 O  O   . TYR A 1 1637 ? -19.980  7.281   42.055  1.00 307.62 ? 1637 TYR A O   1 
ATOM   12514 C  CB  . TYR A 1 1637 ? -19.820  10.490  42.839  1.00 307.03 ? 1637 TYR A CB  1 
ATOM   12515 C  CG  . TYR A 1 1637 ? -19.798  11.277  41.559  1.00 306.51 ? 1637 TYR A CG  1 
ATOM   12516 C  CD1 . TYR A 1 1637 ? -18.794  11.087  40.621  1.00 305.79 ? 1637 TYR A CD1 1 
ATOM   12517 C  CD2 . TYR A 1 1637 ? -20.782  12.209  41.285  1.00 306.11 ? 1637 TYR A CD2 1 
ATOM   12518 C  CE1 . TYR A 1 1637 ? -18.771  11.809  39.445  1.00 304.78 ? 1637 TYR A CE1 1 
ATOM   12519 C  CE2 . TYR A 1 1637 ? -20.772  12.922  40.110  1.00 305.17 ? 1637 TYR A CE2 1 
ATOM   12520 C  CZ  . TYR A 1 1637 ? -19.765  12.726  39.198  1.00 304.48 ? 1637 TYR A CZ  1 
ATOM   12521 O  OH  . TYR A 1 1637 ? -19.760  13.445  38.028  1.00 303.65 ? 1637 TYR A OH  1 
ATOM   12522 N  N   . PRO A 1 1638 ? -20.903  8.669   40.527  1.00 301.17 ? 1638 PRO A N   1 
ATOM   12523 C  CA  . PRO A 1 1638 ? -20.603  7.943   39.283  1.00 294.44 ? 1638 PRO A CA  1 
ATOM   12524 C  C   . PRO A 1 1638 ? -19.123  7.862   38.846  1.00 284.85 ? 1638 PRO A C   1 
ATOM   12525 O  O   . PRO A 1 1638 ? -18.600  6.749   38.763  1.00 288.46 ? 1638 PRO A O   1 
ATOM   12526 C  CB  . PRO A 1 1638 ? -21.429  8.709   38.227  1.00 297.90 ? 1638 PRO A CB  1 
ATOM   12527 C  CG  . PRO A 1 1638 ? -21.838  9.988   38.902  1.00 301.30 ? 1638 PRO A CG  1 
ATOM   12528 C  CD  . PRO A 1 1638 ? -22.038  9.580   40.318  1.00 302.22 ? 1638 PRO A CD  1 
ATOM   12529 N  N   . LEU A 1 1639 ? -18.480  8.995   38.555  1.00 274.43 ? 1639 LEU A N   1 
ATOM   12530 C  CA  . LEU A 1 1639 ? -17.116  9.006   38.004  1.00 263.01 ? 1639 LEU A CA  1 
ATOM   12531 C  C   . LEU A 1 1639 ? -17.123  8.805   36.476  1.00 258.77 ? 1639 LEU A C   1 
ATOM   12532 O  O   . LEU A 1 1639 ? -16.530  7.850   35.965  1.00 260.26 ? 1639 LEU A O   1 
ATOM   12533 C  CB  . LEU A 1 1639 ? -16.241  7.949   38.695  1.00 251.61 ? 1639 LEU A CB  1 
ATOM   12534 C  CG  . LEU A 1 1639 ? -14.721  8.025   38.577  1.00 238.22 ? 1639 LEU A CG  1 
ATOM   12535 C  CD1 . LEU A 1 1639 ? -14.236  9.387   38.995  1.00 233.72 ? 1639 LEU A CD1 1 
ATOM   12536 C  CD2 . LEU A 1 1639 ? -14.099  6.953   39.439  1.00 233.85 ? 1639 LEU A CD2 1 
ATOM   12537 N  N   . ASP A 1 1640 ? -17.793  9.719   35.764  1.00 250.91 ? 1640 ASP A N   1 
ATOM   12538 C  CA  . ASP A 1 1640 ? -18.075  9.596   34.321  1.00 242.00 ? 1640 ASP A CA  1 
ATOM   12539 C  C   . ASP A 1 1640 ? -17.037  10.207  33.366  1.00 229.48 ? 1640 ASP A C   1 
ATOM   12540 O  O   . ASP A 1 1640 ? -15.849  10.287  33.683  1.00 228.60 ? 1640 ASP A O   1 
ATOM   12541 C  CB  . ASP A 1 1640 ? -19.456  10.184  33.992  1.00 246.68 ? 1640 ASP A CB  1 
ATOM   12542 C  CG  . ASP A 1 1640 ? -19.482  11.702  34.080  1.00 251.75 ? 1640 ASP A CG  1 
ATOM   12543 O  OD1 . ASP A 1 1640 ? -19.073  12.243  35.128  1.00 253.56 ? 1640 ASP A OD1 1 
ATOM   12544 O  OD2 . ASP A 1 1640 ? -19.914  12.356  33.103  1.00 253.53 ? 1640 ASP A OD2 1 
ATOM   12545 N  N   . SER A 1 1641 ? -17.515  10.634  32.193  1.00 218.25 ? 1641 SER A N   1 
ATOM   12546 C  CA  . SER A 1 1641 ? -16.656  11.122  31.104  1.00 207.72 ? 1641 SER A CA  1 
ATOM   12547 C  C   . SER A 1 1641 ? -16.376  12.641  31.032  1.00 197.63 ? 1641 SER A C   1 
ATOM   12548 O  O   . SER A 1 1641 ? -15.492  13.065  30.276  1.00 196.53 ? 1641 SER A O   1 
ATOM   12549 C  CB  . SER A 1 1641 ? -17.159  10.614  29.747  1.00 206.74 ? 1641 SER A CB  1 
ATOM   12550 O  OG  . SER A 1 1641 ? -16.736  9.283   29.519  1.00 205.88 ? 1641 SER A OG  1 
ATOM   12551 N  N   . LEU A 1 1642 ? -17.132  13.461  31.764  1.00 186.55 ? 1642 LEU A N   1 
ATOM   12552 C  CA  . LEU A 1 1642 ? -16.698  14.842  32.000  1.00 175.27 ? 1642 LEU A CA  1 
ATOM   12553 C  C   . LEU A 1 1642 ? -16.349  15.126  33.473  1.00 185.24 ? 1642 LEU A C   1 
ATOM   12554 O  O   . LEU A 1 1642 ? -16.410  16.284  33.884  1.00 194.92 ? 1642 LEU A O   1 
ATOM   12555 C  CB  . LEU A 1 1642 ? -17.658  15.897  31.407  1.00 151.76 ? 1642 LEU A CB  1 
ATOM   12556 C  CG  . LEU A 1 1642 ? -17.053  16.802  30.321  1.00 136.62 ? 1642 LEU A CG  1 
ATOM   12557 C  CD1 . LEU A 1 1642 ? -16.268  17.882  30.949  1.00 133.51 ? 1642 LEU A CD1 1 
ATOM   12558 C  CD2 . LEU A 1 1642 ? -16.155  16.047  29.391  1.00 133.25 ? 1642 LEU A CD2 1 
ATOM   12559 N  N   . THR A 1 1643 ? -15.997  14.090  34.261  1.00 184.63 ? 1643 THR A N   1 
ATOM   12560 C  CA  . THR A 1 1643 ? -15.327  14.312  35.563  1.00 183.60 ? 1643 THR A CA  1 
ATOM   12561 C  C   . THR A 1 1643 ? -13.871  14.537  35.268  1.00 184.12 ? 1643 THR A C   1 
ATOM   12562 O  O   . THR A 1 1643 ? -13.294  13.847  34.436  1.00 181.65 ? 1643 THR A O   1 
ATOM   12563 C  CB  . THR A 1 1643 ? -15.400  13.137  36.602  1.00 137.78 ? 1643 THR A CB  1 
ATOM   12564 O  OG1 . THR A 1 1643 ? -16.742  12.927  37.045  1.00 138.61 ? 1643 THR A OG1 1 
ATOM   12565 C  CG2 . THR A 1 1643 ? -14.584  13.486  37.835  1.00 135.73 ? 1643 THR A CG2 1 
ATOM   12566 N  N   . TRP A 1 1644 ? -13.269  15.502  35.941  1.00 192.73 ? 1644 TRP A N   1 
ATOM   12567 C  CA  . TRP A 1 1644 ? -11.916  15.864  35.587  1.00 204.75 ? 1644 TRP A CA  1 
ATOM   12568 C  C   . TRP A 1 1644 ? -10.857  15.230  36.475  1.00 223.31 ? 1644 TRP A C   1 
ATOM   12569 O  O   . TRP A 1 1644 ? -9.808   15.831  36.680  1.00 223.25 ? 1644 TRP A O   1 
ATOM   12570 C  CB  . TRP A 1 1644 ? -11.762  17.380  35.566  1.00 201.48 ? 1644 TRP A CB  1 
ATOM   12571 C  CG  . TRP A 1 1644 ? -10.532  17.839  34.865  1.00 200.23 ? 1644 TRP A CG  1 
ATOM   12572 C  CD1 . TRP A 1 1644 ? -9.481   18.485  35.423  1.00 199.46 ? 1644 TRP A CD1 1 
ATOM   12573 C  CD2 . TRP A 1 1644 ? -10.214  17.680  33.468  1.00 201.03 ? 1644 TRP A CD2 1 
ATOM   12574 N  NE1 . TRP A 1 1644 ? -8.528   18.747  34.471  1.00 199.78 ? 1644 TRP A NE1 1 
ATOM   12575 C  CE2 . TRP A 1 1644 ? -8.952   18.262  33.261  1.00 200.19 ? 1644 TRP A CE2 1 
ATOM   12576 C  CE3 . TRP A 1 1644 ? -10.876  17.100  32.376  1.00 202.26 ? 1644 TRP A CE3 1 
ATOM   12577 C  CZ2 . TRP A 1 1644 ? -8.332   18.292  32.005  1.00 199.83 ? 1644 TRP A CZ2 1 
ATOM   12578 C  CZ3 . TRP A 1 1644 ? -10.256  17.124  31.125  1.00 201.41 ? 1644 TRP A CZ3 1 
ATOM   12579 C  CH2 . TRP A 1 1644 ? -9.001   17.724  30.954  1.00 200.24 ? 1644 TRP A CH2 1 
ATOM   12580 N  N   . ILE A 1 1645 ? -11.114  14.022  36.986  1.00 242.63 ? 1645 ILE A N   1 
ATOM   12581 C  CA  . ILE A 1 1645 ? -10.144  13.358  37.867  1.00 260.86 ? 1645 ILE A CA  1 
ATOM   12582 C  C   . ILE A 1 1645 ? -8.740   13.630  37.341  1.00 277.50 ? 1645 ILE A C   1 
ATOM   12583 O  O   . ILE A 1 1645 ? -8.431   13.374  36.175  1.00 278.54 ? 1645 ILE A O   1 
ATOM   12584 C  CB  . ILE A 1 1645 ? -10.391  11.816  38.060  1.00 136.55 ? 1645 ILE A CB  1 
ATOM   12585 C  CG1 . ILE A 1 1645 ? -10.040  11.017  36.809  1.00 135.43 ? 1645 ILE A CG1 1 
ATOM   12586 C  CG2 . ILE A 1 1645 ? -11.820  11.510  38.485  1.00 137.69 ? 1645 ILE A CG2 1 
ATOM   12587 C  CD1 . ILE A 1 1645 ? -8.796   10.199  36.963  1.00 135.40 ? 1645 ILE A CD1 1 
ATOM   12588 N  N   . GLU A 1 1646 ? -7.901   14.184  38.206  1.00 292.16 ? 1646 GLU A N   1 
ATOM   12589 C  CA  . GLU A 1 1646 ? -6.616   14.702  37.772  1.00 304.49 ? 1646 GLU A CA  1 
ATOM   12590 C  C   . GLU A 1 1646 ? -5.646   14.818  38.937  1.00 302.81 ? 1646 GLU A C   1 
ATOM   12591 O  O   . GLU A 1 1646 ? -5.949   15.440  39.952  1.00 303.24 ? 1646 GLU A O   1 
ATOM   12592 C  CB  . GLU A 1 1646 ? -6.805   16.069  37.118  1.00 317.79 ? 1646 GLU A CB  1 
ATOM   12593 C  CG  . GLU A 1 1646 ? -5.563   16.619  36.456  1.00 327.34 ? 1646 GLU A CG  1 
ATOM   12594 C  CD  . GLU A 1 1646 ? -5.686   18.094  36.155  1.00 334.34 ? 1646 GLU A CD  1 
ATOM   12595 O  OE1 . GLU A 1 1646 ? -6.126   18.838  37.051  1.00 337.17 ? 1646 GLU A OE1 1 
ATOM   12596 O  OE2 . GLU A 1 1646 ? -5.345   18.510  35.029  1.00 336.06 ? 1646 GLU A OE2 1 
ATOM   12597 N  N   . TYR A 1 1647 ? -4.475   14.213  38.766  1.00 300.90 ? 1647 TYR A N   1 
ATOM   12598 C  CA  . TYR A 1 1647 ? -3.426   14.166  39.781  1.00 301.43 ? 1647 TYR A CA  1 
ATOM   12599 C  C   . TYR A 1 1647 ? -3.108   15.573  40.309  1.00 304.23 ? 1647 TYR A C   1 
ATOM   12600 O  O   . TYR A 1 1647 ? -2.979   16.518  39.522  1.00 297.21 ? 1647 TYR A O   1 
ATOM   12601 C  CB  . TYR A 1 1647 ? -2.184   13.488  39.165  1.00 300.12 ? 1647 TYR A CB  1 
ATOM   12602 C  CG  . TYR A 1 1647 ? -1.096   13.015  40.118  1.00 301.56 ? 1647 TYR A CG  1 
ATOM   12603 C  CD1 . TYR A 1 1647 ? -1.388   12.628  41.416  1.00 303.68 ? 1647 TYR A CD1 1 
ATOM   12604 C  CD2 . TYR A 1 1647 ? 0.228    12.917  39.691  1.00 301.83 ? 1647 TYR A CD2 1 
ATOM   12605 C  CE1 . TYR A 1 1647 ? -0.388   12.192  42.275  1.00 304.99 ? 1647 TYR A CE1 1 
ATOM   12606 C  CE2 . TYR A 1 1647 ? 1.231    12.478  40.541  1.00 302.97 ? 1647 TYR A CE2 1 
ATOM   12607 C  CZ  . TYR A 1 1647 ? 0.918    12.116  41.833  1.00 304.39 ? 1647 TYR A CZ  1 
ATOM   12608 O  OH  . TYR A 1 1647 ? 1.907    11.679  42.688  1.00 304.25 ? 1647 TYR A OH  1 
ATOM   12609 N  N   . TRP A 1 1648 ? -3.040   15.705  41.641  1.00 313.35 ? 1648 TRP A N   1 
ATOM   12610 C  CA  . TRP A 1 1648 ? -2.558   16.919  42.325  1.00 313.74 ? 1648 TRP A CA  1 
ATOM   12611 C  C   . TRP A 1 1648 ? -1.132   16.642  42.796  1.00 304.65 ? 1648 TRP A C   1 
ATOM   12612 O  O   . TRP A 1 1648 ? -0.906   16.390  43.978  1.00 303.03 ? 1648 TRP A O   1 
ATOM   12613 C  CB  . TRP A 1 1648 ? -3.466   17.302  43.525  1.00 244.40 ? 1648 TRP A CB  1 
ATOM   12614 C  CG  . TRP A 1 1648 ? -3.311   18.743  44.105  1.00 209.22 ? 1648 TRP A CG  1 
ATOM   12615 C  CD1 . TRP A 1 1648 ? -2.287   19.208  44.882  1.00 208.28 ? 1648 TRP A CD1 1 
ATOM   12616 C  CD2 . TRP A 1 1648 ? -4.234   19.848  43.971  1.00 211.48 ? 1648 TRP A CD2 1 
ATOM   12617 N  NE1 . TRP A 1 1648 ? -2.502   20.521  45.219  1.00 209.26 ? 1648 TRP A NE1 1 
ATOM   12618 C  CE2 . TRP A 1 1648 ? -3.687   20.937  44.671  1.00 211.78 ? 1648 TRP A CE2 1 
ATOM   12619 C  CE3 . TRP A 1 1648 ? -5.459   20.022  43.315  1.00 214.04 ? 1648 TRP A CE3 1 
ATOM   12620 C  CZ2 . TRP A 1 1648 ? -4.321   22.178  44.736  1.00 214.83 ? 1648 TRP A CZ2 1 
ATOM   12621 C  CZ3 . TRP A 1 1648 ? -6.086   21.260  43.382  1.00 215.31 ? 1648 TRP A CZ3 1 
ATOM   12622 C  CH2 . TRP A 1 1648 ? -5.517   22.317  44.087  1.00 215.62 ? 1648 TRP A CH2 1 
ATOM   12623 N  N   . PRO A 1 1649 ? -0.165   16.679  41.862  1.00 294.85 ? 1649 PRO A N   1 
ATOM   12624 C  CA  . PRO A 1 1649 ? 1.220    16.372  42.210  1.00 289.54 ? 1649 PRO A CA  1 
ATOM   12625 C  C   . PRO A 1 1649 ? 1.725    17.407  43.186  1.00 289.19 ? 1649 PRO A C   1 
ATOM   12626 O  O   . PRO A 1 1649 ? 2.448    18.313  42.789  1.00 284.76 ? 1649 PRO A O   1 
ATOM   12627 C  CB  . PRO A 1 1649 ? 1.971    16.520  40.877  1.00 285.95 ? 1649 PRO A CB  1 
ATOM   12628 C  CG  . PRO A 1 1649 ? 0.920    16.554  39.819  1.00 286.17 ? 1649 PRO A CG  1 
ATOM   12629 C  CD  . PRO A 1 1649 ? -0.283   17.149  40.474  1.00 290.12 ? 1649 PRO A CD  1 
ATOM   12630 N  N   . ARG A 1 1650 ? 1.327    17.285  44.445  1.00 294.02 ? 1650 ARG A N   1 
ATOM   12631 C  CA  . ARG A 1 1650 ? 1.903    18.091  45.508  1.00 296.96 ? 1650 ARG A CA  1 
ATOM   12632 C  C   . ARG A 1 1650 ? 3.362    17.675  45.678  1.00 306.67 ? 1650 ARG A C   1 
ATOM   12633 O  O   . ARG A 1 1650 ? 3.945    17.853  46.744  1.00 309.48 ? 1650 ARG A O   1 
ATOM   12634 C  CB  . ARG A 1 1650 ? 1.131    17.885  46.816  1.00 287.46 ? 1650 ARG A CB  1 
ATOM   12635 C  CG  . ARG A 1 1650 ? 0.008    18.895  47.087  1.00 275.99 ? 1650 ARG A CG  1 
ATOM   12636 C  CD  . ARG A 1 1650 ? 0.300    19.764  48.316  1.00 265.11 ? 1650 ARG A CD  1 
ATOM   12637 N  NE  . ARG A 1 1650 ? 0.281    18.986  49.556  1.00 256.34 ? 1650 ARG A NE  1 
ATOM   12638 C  CZ  . ARG A 1 1650 ? 0.615    19.460  50.752  1.00 249.57 ? 1650 ARG A CZ  1 
ATOM   12639 N  NH1 . ARG A 1 1650 ? 0.999    20.717  50.881  1.00 247.15 ? 1650 ARG A NH1 1 
ATOM   12640 N  NH2 . ARG A 1 1650 ? 0.568    18.672  51.818  1.00 247.59 ? 1650 ARG A NH2 1 
ATOM   12641 N  N   . ASP A 1 1651 ? 3.941    17.111  44.618  1.00 312.93 ? 1651 ASP A N   1 
ATOM   12642 C  CA  . ASP A 1 1651 ? 5.313    16.596  44.636  1.00 319.62 ? 1651 ASP A CA  1 
ATOM   12643 C  C   . ASP A 1 1651 ? 6.350    17.673  45.011  1.00 325.47 ? 1651 ASP A C   1 
ATOM   12644 O  O   . ASP A 1 1651 ? 7.416    17.354  45.547  1.00 325.39 ? 1651 ASP A O   1 
ATOM   12645 C  CB  . ASP A 1 1651 ? 5.664    15.946  43.289  1.00 321.40 ? 1651 ASP A CB  1 
ATOM   12646 C  CG  . ASP A 1 1651 ? 5.157    14.507  43.171  1.00 325.64 ? 1651 ASP A CG  1 
ATOM   12647 O  OD1 . ASP A 1 1651 ? 5.162    13.780  44.187  1.00 327.80 ? 1651 ASP A OD1 1 
ATOM   12648 O  OD2 . ASP A 1 1651 ? 4.772    14.091  42.057  1.00 326.81 ? 1651 ASP A OD2 1 
ATOM   12649 N  N   . THR A 1 1652 ? 6.030    18.936  44.721  1.00 331.27 ? 1652 THR A N   1 
ATOM   12650 C  CA  . THR A 1 1652 ? 6.852    20.100  45.095  1.00 335.56 ? 1652 THR A CA  1 
ATOM   12651 C  C   . THR A 1 1652 ? 8.350    19.939  44.841  1.00 338.40 ? 1652 THR A C   1 
ATOM   12652 O  O   . THR A 1 1652 ? 9.155    20.756  45.293  1.00 339.01 ? 1652 THR A O   1 
ATOM   12653 C  CB  . THR A 1 1652 ? 6.621    20.509  46.561  1.00 336.32 ? 1652 THR A CB  1 
ATOM   12654 O  OG1 . THR A 1 1652 ? 7.241    19.558  47.433  1.00 336.31 ? 1652 THR A OG1 1 
ATOM   12655 C  CG2 . THR A 1 1652 ? 5.136    20.579  46.865  1.00 337.07 ? 1652 THR A CG2 1 
ATOM   12656 N  N   . THR A 1 1653 ? 8.690    18.883  44.107  1.00 340.25 ? 1653 THR A N   1 
ATOM   12657 C  CA  . THR A 1 1653 ? 10.060   18.496  43.786  1.00 341.82 ? 1653 THR A CA  1 
ATOM   12658 C  C   . THR A 1 1653 ? 10.079   16.959  43.664  1.00 344.60 ? 1653 THR A C   1 
ATOM   12659 O  O   . THR A 1 1653 ? 10.152   16.233  44.656  1.00 345.59 ? 1653 THR A O   1 
ATOM   12660 C  CB  . THR A 1 1653 ? 11.101   19.070  44.806  1.00 274.54 ? 1653 THR A CB  1 
ATOM   12661 O  OG1 . THR A 1 1653 ? 12.339   19.354  44.143  1.00 273.75 ? 1653 THR A OG1 1 
ATOM   12662 C  CG2 . THR A 1 1653 ? 11.334   18.140  45.992  1.00 274.31 ? 1653 THR A CG2 1 
ATOM   12663 N  N   . CYS A 1 1654 ? 9.964    16.478  42.428  1.00 346.71 ? 1654 CYS A N   1 
ATOM   12664 C  CA  . CYS A 1 1654 ? 9.851    15.052  42.124  1.00 348.62 ? 1654 CYS A CA  1 
ATOM   12665 C  C   . CYS A 1 1654 ? 10.080   14.917  40.637  1.00 347.23 ? 1654 CYS A C   1 
ATOM   12666 O  O   . CYS A 1 1654 ? 9.496    15.675  39.871  1.00 348.19 ? 1654 CYS A O   1 
ATOM   12667 C  CB  . CYS A 1 1654 ? 8.434    14.555  42.403  1.00 351.45 ? 1654 CYS A CB  1 
ATOM   12668 S  SG  . CYS A 1 1654 ? 7.291    14.786  40.988  1.00 364.33 ? 1654 CYS A SG  1 
ATOM   12669 N  N   . SER A 1 1655 ? 10.910   13.968  40.214  1.00 344.86 ? 1655 SER A N   1 
ATOM   12670 C  CA  . SER A 1 1655 ? 11.170   13.788  38.786  1.00 342.81 ? 1655 SER A CA  1 
ATOM   12671 C  C   . SER A 1 1655 ? 11.038   15.125  38.033  1.00 339.56 ? 1655 SER A C   1 
ATOM   12672 O  O   . SER A 1 1655 ? 10.556   15.168  36.899  1.00 340.38 ? 1655 SER A O   1 
ATOM   12673 C  CB  . SER A 1 1655 ? 10.227   12.732  38.193  1.00 344.92 ? 1655 SER A CB  1 
ATOM   12674 O  OG  . SER A 1 1655 ? 8.868    13.137  38.277  1.00 347.16 ? 1655 SER A OG  1 
ATOM   12675 N  N   . SER A 1 1656 ? 11.466   16.204  38.696  1.00 334.51 ? 1656 SER A N   1 
ATOM   12676 C  CA  . SER A 1 1656 ? 11.276   17.600  38.258  1.00 328.49 ? 1656 SER A CA  1 
ATOM   12677 C  C   . SER A 1 1656 ? 9.885    17.941  37.700  1.00 322.49 ? 1656 SER A C   1 
ATOM   12678 O  O   . SER A 1 1656 ? 9.701    18.008  36.486  1.00 320.99 ? 1656 SER A O   1 
ATOM   12679 C  CB  . SER A 1 1656 ? 12.368   18.032  37.272  1.00 327.45 ? 1656 SER A CB  1 
ATOM   12680 O  OG  . SER A 1 1656 ? 12.422   19.445  37.165  1.00 327.36 ? 1656 SER A OG  1 
ATOM   12681 N  N   . CYS A 1 1657 ? 8.922    18.166  38.595  1.00 317.92 ? 1657 CYS A N   1 
ATOM   12682 C  CA  . CYS A 1 1657 ? 7.578    18.607  38.214  1.00 312.66 ? 1657 CYS A CA  1 
ATOM   12683 C  C   . CYS A 1 1657 ? 7.539    20.136  38.254  1.00 307.00 ? 1657 CYS A C   1 
ATOM   12684 O  O   . CYS A 1 1657 ? 8.487    20.756  38.730  1.00 306.08 ? 1657 CYS A O   1 
ATOM   12685 C  CB  . CYS A 1 1657 ? 6.511    18.040  39.169  1.00 313.80 ? 1657 CYS A CB  1 
ATOM   12686 S  SG  . CYS A 1 1657 ? 6.715    16.305  39.743  1.00 362.36 ? 1657 CYS A SG  1 
ATOM   12687 N  N   . GLN A 1 1658 ? 6.459    20.732  37.743  1.00 302.79 ? 1658 GLN A N   1 
ATOM   12688 C  CA  . GLN A 1 1658 ? 6.181    22.173  37.892  1.00 299.17 ? 1658 GLN A CA  1 
ATOM   12689 C  C   . GLN A 1 1658 ? 5.356    22.745  36.739  1.00 296.96 ? 1658 GLN A C   1 
ATOM   12690 O  O   . GLN A 1 1658 ? 5.015    22.032  35.801  1.00 297.67 ? 1658 GLN A O   1 
ATOM   12691 C  CB  . GLN A 1 1658 ? 7.459    22.994  38.064  1.00 297.11 ? 1658 GLN A CB  1 
ATOM   12692 C  CG  . GLN A 1 1658 ? 7.262    24.279  38.860  1.00 296.60 ? 1658 GLN A CG  1 
ATOM   12693 C  CD  . GLN A 1 1658 ? 6.561    24.046  40.188  1.00 296.61 ? 1658 GLN A CD  1 
ATOM   12694 O  OE1 . GLN A 1 1658 ? 5.344    23.873  40.239  1.00 296.88 ? 1658 GLN A OE1 1 
ATOM   12695 N  NE2 . GLN A 1 1658 ? 7.329    24.051  41.272  1.00 296.42 ? 1658 GLN A NE2 1 
ATOM   12696 N  N   . ALA A 1 1659 ? 5.037    24.033  36.811  1.00 294.11 ? 1659 ALA A N   1 
ATOM   12697 C  CA  . ALA A 1 1659 ? 4.214    24.668  35.788  1.00 291.46 ? 1659 ALA A CA  1 
ATOM   12698 C  C   . ALA A 1 1659 ? 2.830    24.019  35.698  1.00 291.01 ? 1659 ALA A C   1 
ATOM   12699 O  O   . ALA A 1 1659 ? 1.953    24.518  34.992  1.00 291.26 ? 1659 ALA A O   1 
ATOM   12700 C  CB  . ALA A 1 1659 ? 4.912    24.640  34.435  1.00 289.57 ? 1659 ALA A CB  1 
ATOM   12701 N  N   . PHE A 1 1660 ? 2.650    22.896  36.393  1.00 289.56 ? 1660 PHE A N   1 
ATOM   12702 C  CA  . PHE A 1 1660 ? 1.329    22.288  36.560  1.00 287.41 ? 1660 PHE A CA  1 
ATOM   12703 C  C   . PHE A 1 1660 ? 0.832    22.516  37.979  1.00 278.15 ? 1660 PHE A C   1 
ATOM   12704 O  O   . PHE A 1 1660 ? -0.369   22.501  38.235  1.00 277.80 ? 1660 PHE A O   1 
ATOM   12705 C  CB  . PHE A 1 1660 ? 1.341    20.788  36.245  1.00 293.50 ? 1660 PHE A CB  1 
ATOM   12706 C  CG  . PHE A 1 1660 ? 0.015    20.105  36.484  1.00 298.43 ? 1660 PHE A CG  1 
ATOM   12707 C  CD1 . PHE A 1 1660 ? -1.098   20.440  35.731  1.00 300.44 ? 1660 PHE A CD1 1 
ATOM   12708 C  CD2 . PHE A 1 1660 ? -0.117   19.128  37.456  1.00 299.69 ? 1660 PHE A CD2 1 
ATOM   12709 C  CE1 . PHE A 1 1660 ? -2.316   19.817  35.945  1.00 301.38 ? 1660 PHE A CE1 1 
ATOM   12710 C  CE2 . PHE A 1 1660 ? -1.334   18.501  37.672  1.00 300.64 ? 1660 PHE A CE2 1 
ATOM   12711 C  CZ  . PHE A 1 1660 ? -2.432   18.846  36.918  1.00 301.33 ? 1660 PHE A CZ  1 
ATOM   12712 N  N   . LEU A 1 1661 ? 1.766    22.717  38.902  1.00 269.41 ? 1661 LEU A N   1 
ATOM   12713 C  CA  . LEU A 1 1661 ? 1.413    23.070  40.270  1.00 263.47 ? 1661 LEU A CA  1 
ATOM   12714 C  C   . LEU A 1 1661 ? 1.118    24.560  40.412  1.00 271.05 ? 1661 LEU A C   1 
ATOM   12715 O  O   . LEU A 1 1661 ? 0.303    24.964  41.242  1.00 271.35 ? 1661 LEU A O   1 
ATOM   12716 C  CB  . LEU A 1 1661 ? 2.522    22.661  41.226  1.00 250.80 ? 1661 LEU A CB  1 
ATOM   12717 C  CG  . LEU A 1 1661 ? 2.350    21.248  41.750  1.00 241.51 ? 1661 LEU A CG  1 
ATOM   12718 C  CD1 . LEU A 1 1661 ? 3.690    20.728  42.186  1.00 238.08 ? 1661 LEU A CD1 1 
ATOM   12719 C  CD2 . LEU A 1 1661 ? 1.342    21.236  42.888  1.00 239.89 ? 1661 LEU A CD2 1 
ATOM   12720 N  N   . ALA A 1 1662 ? 1.784    25.373  39.597  1.00 278.77 ? 1662 ALA A N   1 
ATOM   12721 C  CA  . ALA A 1 1662 ? 1.581    26.815  39.627  1.00 286.99 ? 1662 ALA A CA  1 
ATOM   12722 C  C   . ALA A 1 1662 ? 0.122    27.147  39.357  1.00 294.05 ? 1662 ALA A C   1 
ATOM   12723 O  O   . ALA A 1 1662 ? -0.392   28.159  39.826  1.00 295.69 ? 1662 ALA A O   1 
ATOM   12724 C  CB  . ALA A 1 1662 ? 2.483    27.494  38.610  1.00 286.97 ? 1662 ALA A CB  1 
ATOM   12725 N  N   . ASN A 1 1663 ? -0.537   26.273  38.601  1.00 299.09 ? 1663 ASN A N   1 
ATOM   12726 C  CA  . ASN A 1 1663 ? -1.919   26.478  38.175  1.00 307.03 ? 1663 ASN A CA  1 
ATOM   12727 C  C   . ASN A 1 1663 ? -2.961   25.837  39.087  1.00 310.85 ? 1663 ASN A C   1 
ATOM   12728 O  O   . ASN A 1 1663 ? -4.051   26.372  39.261  1.00 318.38 ? 1663 ASN A O   1 
ATOM   12729 C  CB  . ASN A 1 1663 ? -2.114   25.973  36.745  1.00 318.54 ? 1663 ASN A CB  1 
ATOM   12730 C  CG  . ASN A 1 1663 ? -1.177   26.639  35.763  1.00 331.45 ? 1663 ASN A CG  1 
ATOM   12731 O  OD1 . ASN A 1 1663 ? -0.805   27.801  35.933  1.00 336.45 ? 1663 ASN A OD1 1 
ATOM   12732 N  ND2 . ASN A 1 1663 ? -0.789   25.907  34.727  1.00 335.14 ? 1663 ASN A ND2 1 
ATOM   12733 N  N   . LEU A 1 1664 ? -2.638   24.677  39.644  1.00 290.21 ? 1664 LEU A N   1 
ATOM   12734 C  CA  . LEU A 1 1664 ? -3.539   24.019  40.579  1.00 280.85 ? 1664 LEU A CA  1 
ATOM   12735 C  C   . LEU A 1 1664 ? -3.461   24.665  41.937  1.00 276.39 ? 1664 LEU A C   1 
ATOM   12736 O  O   . LEU A 1 1664 ? -4.353   24.513  42.768  1.00 276.75 ? 1664 LEU A O   1 
ATOM   12737 C  CB  . LEU A 1 1664 ? -3.213   22.543  40.697  1.00 277.81 ? 1664 LEU A CB  1 
ATOM   12738 C  CG  . LEU A 1 1664 ? -4.176   21.742  39.843  1.00 273.29 ? 1664 LEU A CG  1 
ATOM   12739 C  CD1 . LEU A 1 1664 ? -4.004   20.269  40.119  1.00 271.47 ? 1664 LEU A CD1 1 
ATOM   12740 C  CD2 . LEU A 1 1664 ? -5.584   22.202  40.159  1.00 272.41 ? 1664 LEU A CD2 1 
ATOM   12741 N  N   . ASP A 1 1665 ? -2.365   25.370  42.167  1.00 270.51 ? 1665 ASP A N   1 
ATOM   12742 C  CA  . ASP A 1 1665 ? -2.260   26.208  43.336  1.00 266.14 ? 1665 ASP A CA  1 
ATOM   12743 C  C   . ASP A 1 1665 ? -2.935   27.522  42.981  1.00 271.49 ? 1665 ASP A C   1 
ATOM   12744 O  O   . ASP A 1 1665 ? -3.437   28.221  43.856  1.00 279.82 ? 1665 ASP A O   1 
ATOM   12745 C  CB  . ASP A 1 1665 ? -0.797   26.415  43.717  1.00 256.89 ? 1665 ASP A CB  1 
ATOM   12746 C  CG  . ASP A 1 1665 ? -0.590   26.467  45.216  1.00 250.13 ? 1665 ASP A CG  1 
ATOM   12747 O  OD1 . ASP A 1 1665 ? 0.254    25.712  45.738  1.00 247.66 ? 1665 ASP A OD1 1 
ATOM   12748 O  OD2 . ASP A 1 1665 ? -1.284   27.256  45.876  1.00 248.39 ? 1665 ASP A OD2 1 
ATOM   12749 N  N   . GLU A 1 1666 ? -2.957   27.838  41.684  1.00 269.95 ? 1666 GLU A N   1 
ATOM   12750 C  CA  . GLU A 1 1666 ? -3.647   29.023  41.156  1.00 276.66 ? 1666 GLU A CA  1 
ATOM   12751 C  C   . GLU A 1 1666 ? -5.163   28.838  41.132  1.00 278.23 ? 1666 GLU A C   1 
ATOM   12752 O  O   . GLU A 1 1666 ? -5.898   29.446  41.907  1.00 283.53 ? 1666 GLU A O   1 
ATOM   12753 C  CB  . GLU A 1 1666 ? -3.157   29.338  39.739  1.00 288.62 ? 1666 GLU A CB  1 
ATOM   12754 C  CG  . GLU A 1 1666 ? -3.938   30.438  39.019  1.00 303.34 ? 1666 GLU A CG  1 
ATOM   12755 C  CD  . GLU A 1 1666 ? -3.831   31.781  39.717  1.00 319.40 ? 1666 GLU A CD  1 
ATOM   12756 O  OE1 . GLU A 1 1666 ? -3.482   32.781  39.052  1.00 324.86 ? 1666 GLU A OE1 1 
ATOM   12757 O  OE2 . GLU A 1 1666 ? -4.090   31.841  40.937  1.00 326.43 ? 1666 GLU A OE2 1 
ATOM   12758 N  N   . PHE A 1 1667 ? -5.617   28.008  40.207  1.00 267.25 ? 1667 PHE A N   1 
ATOM   12759 C  CA  . PHE A 1 1667 ? -6.962   27.485  40.226  1.00 251.09 ? 1667 PHE A CA  1 
ATOM   12760 C  C   . PHE A 1 1667 ? -7.497   27.469  41.663  1.00 250.15 ? 1667 PHE A C   1 
ATOM   12761 O  O   . PHE A 1 1667 ? -8.566   28.004  41.946  1.00 252.37 ? 1667 PHE A O   1 
ATOM   12762 C  CB  . PHE A 1 1667 ? -6.902   26.075  39.637  1.00 227.27 ? 1667 PHE A CB  1 
ATOM   12763 C  CG  . PHE A 1 1667 ? -8.191   25.331  39.682  1.00 198.21 ? 1667 PHE A CG  1 
ATOM   12764 C  CD1 . PHE A 1 1667 ? -8.996   25.265  38.585  1.00 183.46 ? 1667 PHE A CD1 1 
ATOM   12765 C  CD2 . PHE A 1 1667 ? -8.581   24.663  40.817  1.00 184.51 ? 1667 PHE A CD2 1 
ATOM   12766 C  CE1 . PHE A 1 1667 ? -10.173  24.569  38.636  1.00 175.87 ? 1667 PHE A CE1 1 
ATOM   12767 C  CE2 . PHE A 1 1667 ? -9.757   23.966  40.869  1.00 175.75 ? 1667 PHE A CE2 1 
ATOM   12768 C  CZ  . PHE A 1 1667 ? -10.548  23.921  39.786  1.00 173.15 ? 1667 PHE A CZ  1 
ATOM   12769 N  N   . ALA A 1 1668 ? -6.713   26.899  42.575  1.00 245.79 ? 1668 ALA A N   1 
ATOM   12770 C  CA  . ALA A 1 1668 ? -7.140   26.645  43.956  1.00 243.77 ? 1668 ALA A CA  1 
ATOM   12771 C  C   . ALA A 1 1668 ? -7.693   27.858  44.709  1.00 253.86 ? 1668 ALA A C   1 
ATOM   12772 O  O   . ALA A 1 1668 ? -8.878   27.907  45.034  1.00 253.62 ? 1668 ALA A O   1 
ATOM   12773 C  CB  . ALA A 1 1668 ? -6.001   26.005  44.749  1.00 236.25 ? 1668 ALA A CB  1 
ATOM   12774 N  N   . GLU A 1 1669 ? -6.831   28.824  45.004  1.00 265.90 ? 1669 GLU A N   1 
ATOM   12775 C  CA  . GLU A 1 1669 ? -7.259   30.022  45.712  1.00 277.75 ? 1669 GLU A CA  1 
ATOM   12776 C  C   . GLU A 1 1669 ? -8.075   30.926  44.798  1.00 286.33 ? 1669 GLU A C   1 
ATOM   12777 O  O   . GLU A 1 1669 ? -8.347   32.073  45.146  1.00 287.97 ? 1669 GLU A O   1 
ATOM   12778 C  CB  . GLU A 1 1669 ? -6.054   30.786  46.256  1.00 278.88 ? 1669 GLU A CB  1 
ATOM   12779 C  CG  . GLU A 1 1669 ? -6.354   31.576  47.511  1.00 279.97 ? 1669 GLU A CG  1 
ATOM   12780 C  CD  . GLU A 1 1669 ? -6.539   30.676  48.716  1.00 280.78 ? 1669 GLU A CD  1 
ATOM   12781 O  OE1 . GLU A 1 1669 ? -6.453   29.447  48.551  1.00 280.57 ? 1669 GLU A OE1 1 
ATOM   12782 O  OE2 . GLU A 1 1669 ? -6.763   31.188  49.830  1.00 281.63 ? 1669 GLU A OE2 1 
ATOM   12783 N  N   . ASP A 1 1670 ? -8.445   30.399  43.629  1.00 292.08 ? 1670 ASP A N   1 
ATOM   12784 C  CA  . ASP A 1 1670 ? -9.226   31.128  42.619  1.00 297.00 ? 1670 ASP A CA  1 
ATOM   12785 C  C   . ASP A 1 1670 ? -10.704  30.727  42.578  1.00 296.23 ? 1670 ASP A C   1 
ATOM   12786 O  O   . ASP A 1 1670 ? -11.560  31.519  42.185  1.00 296.28 ? 1670 ASP A O   1 
ATOM   12787 C  CB  . ASP A 1 1670 ? -8.608   30.936  41.222  1.00 302.22 ? 1670 ASP A CB  1 
ATOM   12788 C  CG  . ASP A 1 1670 ? -9.462   31.543  40.097  1.00 307.15 ? 1670 ASP A CG  1 
ATOM   12789 O  OD1 . ASP A 1 1670 ? -8.905   32.287  39.264  1.00 308.25 ? 1670 ASP A OD1 1 
ATOM   12790 O  OD2 . ASP A 1 1670 ? -10.681  31.276  40.027  1.00 309.13 ? 1670 ASP A OD2 1 
ATOM   12791 N  N   . ILE A 1 1671 ? -11.000  29.494  42.969  1.00 294.39 ? 1671 ILE A N   1 
ATOM   12792 C  CA  . ILE A 1 1671 ? -12.353  28.960  42.830  1.00 291.32 ? 1671 ILE A CA  1 
ATOM   12793 C  C   . ILE A 1 1671 ? -13.392  29.605  43.745  1.00 291.73 ? 1671 ILE A C   1 
ATOM   12794 O  O   . ILE A 1 1671 ? -14.324  30.260  43.275  1.00 290.30 ? 1671 ILE A O   1 
ATOM   12795 C  CB  . ILE A 1 1671 ? -12.378  27.458  43.099  1.00 288.42 ? 1671 ILE A CB  1 
ATOM   12796 C  CG1 . ILE A 1 1671 ? -13.824  26.978  43.191  1.00 286.62 ? 1671 ILE A CG1 1 
ATOM   12797 C  CG2 . ILE A 1 1671 ? -11.625  27.143  44.379  1.00 288.30 ? 1671 ILE A CG2 1 
ATOM   12798 C  CD1 . ILE A 1 1671 ? -14.628  27.272  41.956  1.00 284.78 ? 1671 ILE A CD1 1 
ATOM   12799 N  N   . PHE A 1 1672 ? -13.227  29.392  45.050  1.00 293.55 ? 1672 PHE A N   1 
ATOM   12800 C  CA  . PHE A 1 1672 ? -14.171  29.860  46.063  1.00 293.91 ? 1672 PHE A CA  1 
ATOM   12801 C  C   . PHE A 1 1672 ? -14.556  31.320  45.843  1.00 295.54 ? 1672 PHE A C   1 
ATOM   12802 O  O   . PHE A 1 1672 ? -15.732  31.692  45.932  1.00 298.53 ? 1672 PHE A O   1 
ATOM   12803 C  CB  . PHE A 1 1672 ? -13.586  29.667  47.477  1.00 291.08 ? 1672 PHE A CB  1 
ATOM   12804 C  CG  . PHE A 1 1672 ? -12.328  30.467  47.741  1.00 286.52 ? 1672 PHE A CG  1 
ATOM   12805 C  CD1 . PHE A 1 1672 ? -12.399  31.736  48.294  1.00 284.52 ? 1672 PHE A CD1 1 
ATOM   12806 C  CD2 . PHE A 1 1672 ? -11.079  29.944  47.445  1.00 284.11 ? 1672 PHE A CD2 1 
ATOM   12807 C  CE1 . PHE A 1 1672 ? -11.253  32.467  48.533  1.00 282.79 ? 1672 PHE A CE1 1 
ATOM   12808 C  CE2 . PHE A 1 1672 ? -9.930   30.674  47.685  1.00 282.24 ? 1672 PHE A CE2 1 
ATOM   12809 C  CZ  . PHE A 1 1672 ? -10.017  31.934  48.227  1.00 281.86 ? 1672 PHE A CZ  1 
ATOM   12810 N  N   . LEU A 1 1673 ? -13.553  32.138  45.541  1.00 292.97 ? 1673 LEU A N   1 
ATOM   12811 C  CA  . LEU A 1 1673 ? -13.748  33.572  45.391  1.00 289.97 ? 1673 LEU A CA  1 
ATOM   12812 C  C   . LEU A 1 1673 ? -14.552  33.946  44.138  1.00 279.86 ? 1673 LEU A C   1 
ATOM   12813 O  O   . LEU A 1 1673 ? -15.591  34.605  44.237  1.00 280.03 ? 1673 LEU A O   1 
ATOM   12814 C  CB  . LEU A 1 1673 ? -12.404  34.316  45.484  1.00 296.95 ? 1673 LEU A CB  1 
ATOM   12815 C  CG  . LEU A 1 1673 ? -11.085  33.811  44.884  1.00 303.70 ? 1673 LEU A CG  1 
ATOM   12816 C  CD1 . LEU A 1 1673 ? -10.983  34.106  43.402  1.00 304.88 ? 1673 LEU A CD1 1 
ATOM   12817 C  CD2 . LEU A 1 1673 ? -9.906   34.446  45.614  1.00 306.82 ? 1673 LEU A CD2 1 
ATOM   12818 N  N   . ASN A 1 1674 ? -14.094  33.517  42.966  1.00 268.75 ? 1674 ASN A N   1 
ATOM   12819 C  CA  . ASN A 1 1674 ? -14.849  33.777  41.745  1.00 256.12 ? 1674 ASN A CA  1 
ATOM   12820 C  C   . ASN A 1 1674 ? -16.193  33.062  41.738  1.00 242.78 ? 1674 ASN A C   1 
ATOM   12821 O  O   . ASN A 1 1674 ? -17.007  33.269  40.840  1.00 240.56 ? 1674 ASN A O   1 
ATOM   12822 C  CB  . ASN A 1 1674 ? -14.026  33.456  40.492  1.00 255.82 ? 1674 ASN A CB  1 
ATOM   12823 C  CG  . ASN A 1 1674 ? -13.432  34.702  39.843  1.00 254.05 ? 1674 ASN A CG  1 
ATOM   12824 O  OD1 . ASN A 1 1674 ? -14.078  35.749  39.772  1.00 253.00 ? 1674 ASN A OD1 1 
ATOM   12825 N  ND2 . ASN A 1 1674 ? -12.203  34.586  39.354  1.00 253.25 ? 1674 ASN A ND2 1 
ATOM   12826 N  N   . GLY A 1 1675 ? -16.423  32.231  42.749  1.00 231.54 ? 1675 GLY A N   1 
ATOM   12827 C  CA  . GLY A 1 1675 ? -17.682  31.529  42.882  1.00 219.87 ? 1675 GLY A CA  1 
ATOM   12828 C  C   . GLY A 1 1675 ? -18.178  31.116  41.517  1.00 207.72 ? 1675 GLY A C   1 
ATOM   12829 O  O   . GLY A 1 1675 ? -17.388  30.832  40.626  1.00 205.81 ? 1675 GLY A O   1 
ATOM   12830 N  N   . CYS A 1 1676 ? -19.490  31.100  41.339  1.00 199.62 ? 1676 CYS A N   1 
ATOM   12831 C  CA  . CYS A 1 1676 ? -20.065  30.741  40.053  1.00 192.67 ? 1676 CYS A CA  1 
ATOM   12832 C  C   . CYS A 1 1676 ? -21.574  30.884  40.098  1.00 187.22 ? 1676 CYS A C   1 
ATOM   12833 O  O   . CYS A 1 1676 ? -22.153  31.691  39.373  1.00 184.82 ? 1676 CYS A O   1 
ATOM   12834 C  CB  . CYS A 1 1676 ? -19.640  29.328  39.652  1.00 192.97 ? 1676 CYS A CB  1 
ATOM   12835 S  SG  . CYS A 1 1676 ? -17.854  29.136  39.352  1.00 276.68 ? 1676 CYS A SG  1 
ATOM   12836 O  OXT . CYS A 1 1676 ? -22.234  30.193  40.874  1.00 185.58 ? 1676 CYS A OXT 1 
ATOM   12837 N  N   . LEU B 2 40   ? -111.944 40.973  30.890  1.00 210.10 ? 40   LEU X N   1 
ATOM   12838 C  CA  . LEU B 2 40   ? -111.666 40.479  32.235  1.00 211.06 ? 40   LEU X CA  1 
ATOM   12839 C  C   . LEU B 2 40   ? -111.049 41.566  33.121  1.00 211.12 ? 40   LEU X C   1 
ATOM   12840 O  O   . LEU B 2 40   ? -111.273 41.594  34.333  1.00 212.93 ? 40   LEU X O   1 
ATOM   12841 C  CB  . LEU B 2 40   ? -110.792 39.226  32.169  1.00 208.42 ? 40   LEU X CB  1 
ATOM   12842 C  CG  . LEU B 2 40   ? -111.473 38.044  31.463  1.00 206.83 ? 40   LEU X CG  1 
ATOM   12843 C  CD1 . LEU B 2 40   ? -110.553 36.838  31.396  1.00 207.16 ? 40   LEU X CD1 1 
ATOM   12844 C  CD2 . LEU B 2 40   ? -112.796 37.677  32.141  1.00 206.35 ? 40   LEU X CD2 1 
ATOM   12845 N  N   . HIS B 2 41   ? -110.254 42.435  32.496  1.00 213.18 ? 41   HIS X N   1 
ATOM   12846 C  CA  . HIS B 2 41   ? -109.900 43.772  33.018  1.00 213.33 ? 41   HIS X CA  1 
ATOM   12847 C  C   . HIS B 2 41   ? -109.213 43.864  34.411  1.00 237.22 ? 41   HIS X C   1 
ATOM   12848 O  O   . HIS B 2 41   ? -109.716 43.339  35.407  1.00 237.71 ? 41   HIS X O   1 
ATOM   12849 C  CB  . HIS B 2 41   ? -111.133 44.707  32.943  1.00 235.30 ? 41   HIS X CB  1 
ATOM   12850 C  CG  . HIS B 2 41   ? -111.992 44.506  31.721  1.00 237.15 ? 41   HIS X CG  1 
ATOM   12851 N  ND1 . HIS B 2 41   ? -112.964 43.525  31.640  1.00 238.46 ? 41   HIS X ND1 1 
ATOM   12852 C  CD2 . HIS B 2 41   ? -112.047 45.175  30.542  1.00 236.15 ? 41   HIS X CD2 1 
ATOM   12853 C  CE1 . HIS B 2 41   ? -113.561 43.588  30.465  1.00 237.64 ? 41   HIS X CE1 1 
ATOM   12854 N  NE2 . HIS B 2 41   ? -113.023 44.582  29.777  1.00 236.38 ? 41   HIS X NE2 1 
ATOM   12855 N  N   . ASP B 2 42   ? -108.068 44.551  34.452  1.00 236.21 ? 42   ASP X N   1 
ATOM   12856 C  CA  . ASP B 2 42   ? -107.311 44.842  35.683  1.00 235.21 ? 42   ASP X CA  1 
ATOM   12857 C  C   . ASP B 2 42   ? -105.873 45.214  35.300  1.00 230.84 ? 42   ASP X C   1 
ATOM   12858 O  O   . ASP B 2 42   ? -105.405 44.818  34.237  1.00 232.42 ? 42   ASP X O   1 
ATOM   12859 C  CB  . ASP B 2 42   ? -107.304 43.647  36.645  1.00 239.29 ? 42   ASP X CB  1 
ATOM   12860 C  CG  . ASP B 2 42   ? -106.866 44.027  38.060  1.00 240.33 ? 42   ASP X CG  1 
ATOM   12861 O  OD1 . ASP B 2 42   ? -105.810 44.680  38.226  1.00 239.50 ? 42   ASP X OD1 1 
ATOM   12862 O  OD2 . ASP B 2 42   ? -107.580 43.659  39.016  1.00 241.18 ? 42   ASP X OD2 1 
ATOM   12863 N  N   . ILE B 2 43   ? -105.172 45.971  36.144  1.00 223.85 ? 43   ILE X N   1 
ATOM   12864 C  CA  . ILE B 2 43   ? -103.787 46.337  35.833  1.00 219.21 ? 43   ILE X CA  1 
ATOM   12865 C  C   . ILE B 2 43   ? -102.745 45.365  36.400  1.00 218.28 ? 43   ILE X C   1 
ATOM   12866 O  O   . ILE B 2 43   ? -101.743 45.071  35.744  1.00 216.76 ? 43   ILE X O   1 
ATOM   12867 C  CB  . ILE B 2 43   ? -103.442 47.790  36.243  1.00 216.79 ? 43   ILE X CB  1 
ATOM   12868 C  CG1 . ILE B 2 43   ? -102.082 48.184  35.648  1.00 212.91 ? 43   ILE X CG1 1 
ATOM   12869 C  CG2 . ILE B 2 43   ? -103.477 47.953  37.763  1.00 219.22 ? 43   ILE X CG2 1 
ATOM   12870 C  CD1 . ILE B 2 43   ? -101.674 49.614  35.887  1.00 209.27 ? 43   ILE X CD1 1 
ATOM   12871 N  N   . ARG B 2 44   ? -102.983 44.866  37.610  1.00 219.82 ? 44   ARG X N   1 
ATOM   12872 C  CA  . ARG B 2 44   ? -102.054 43.929  38.239  1.00 222.74 ? 44   ARG X CA  1 
ATOM   12873 C  C   . ARG B 2 44   ? -101.854 42.664  37.397  1.00 229.33 ? 44   ARG X C   1 
ATOM   12874 O  O   . ARG B 2 44   ? -100.720 42.233  37.175  1.00 231.38 ? 44   ARG X O   1 
ATOM   12875 C  CB  . ARG B 2 44   ? -102.502 43.586  39.669  1.00 219.03 ? 44   ARG X CB  1 
ATOM   12876 C  CG  . ARG B 2 44   ? -101.721 44.329  40.747  1.00 214.26 ? 44   ARG X CG  1 
ATOM   12877 C  CD  . ARG B 2 44   ? -102.570 44.649  41.971  1.00 210.46 ? 44   ARG X CD  1 
ATOM   12878 N  NE  . ARG B 2 44   ? -103.735 45.473  41.637  1.00 206.25 ? 44   ARG X NE  1 
ATOM   12879 C  CZ  . ARG B 2 44   ? -104.342 46.311  42.480  1.00 202.52 ? 44   ARG X CZ  1 
ATOM   12880 N  NH1 . ARG B 2 44   ? -103.897 46.464  43.722  1.00 201.23 ? 44   ARG X NH1 1 
ATOM   12881 N  NH2 . ARG B 2 44   ? -105.398 47.006  42.076  1.00 200.55 ? 44   ARG X NH2 1 
ATOM   12882 N  N   . ASP B 2 45   ? -102.958 42.095  36.914  1.00 234.00 ? 45   ASP X N   1 
ATOM   12883 C  CA  . ASP B 2 45   ? -102.943 40.841  36.148  1.00 238.57 ? 45   ASP X CA  1 
ATOM   12884 C  C   . ASP B 2 45   ? -102.246 40.957  34.791  1.00 239.79 ? 45   ASP X C   1 
ATOM   12885 O  O   . ASP B 2 45   ? -101.436 40.104  34.423  1.00 240.45 ? 45   ASP X O   1 
ATOM   12886 C  CB  . ASP B 2 45   ? -104.372 40.328  35.926  1.00 241.10 ? 45   ASP X CB  1 
ATOM   12887 C  CG  . ASP B 2 45   ? -105.071 39.950  37.217  1.00 244.01 ? 45   ASP X CG  1 
ATOM   12888 O  OD1 . ASP B 2 45   ? -104.392 39.854  38.264  1.00 245.35 ? 45   ASP X OD1 1 
ATOM   12889 O  OD2 . ASP B 2 45   ? -106.303 39.747  37.177  1.00 244.81 ? 45   ASP X OD2 1 
ATOM   12890 N  N   . LEU B 2 46   ? -102.576 42.006  34.045  1.00 239.90 ? 46   LEU X N   1 
ATOM   12891 C  CA  . LEU B 2 46   ? -102.036 42.190  32.702  1.00 240.93 ? 46   LEU X CA  1 
ATOM   12892 C  C   . LEU B 2 46   ? -100.506 42.316  32.709  1.00 241.12 ? 46   LEU X C   1 
ATOM   12893 O  O   . LEU B 2 46   ? -99.861  42.212  31.661  1.00 241.08 ? 46   LEU X O   1 
ATOM   12894 C  CB  . LEU B 2 46   ? -102.677 43.405  32.020  1.00 240.65 ? 46   LEU X CB  1 
ATOM   12895 C  CG  . LEU B 2 46   ? -104.201 43.578  32.080  1.00 240.90 ? 46   LEU X CG  1 
ATOM   12896 C  CD1 . LEU B 2 46   ? -104.659 44.674  31.119  1.00 239.54 ? 46   LEU X CD1 1 
ATOM   12897 C  CD2 . LEU B 2 46   ? -104.953 42.278  31.809  1.00 242.97 ? 46   LEU X CD2 1 
ATOM   12898 N  N   . HIS B 2 47   ? -99.940  42.543  33.893  1.00 240.63 ? 47   HIS X N   1 
ATOM   12899 C  CA  . HIS B 2 47   ? -98.487  42.613  34.075  1.00 239.54 ? 47   HIS X CA  1 
ATOM   12900 C  C   . HIS B 2 47   ? -97.887  41.241  34.392  1.00 239.76 ? 47   HIS X C   1 
ATOM   12901 O  O   . HIS B 2 47   ? -96.667  41.062  34.355  1.00 239.81 ? 47   HIS X O   1 
ATOM   12902 C  CB  . HIS B 2 47   ? -98.136  43.588  35.201  1.00 238.23 ? 47   HIS X CB  1 
ATOM   12903 C  CG  . HIS B 2 47   ? -96.688  43.962  35.246  1.00 237.37 ? 47   HIS X CG  1 
ATOM   12904 N  ND1 . HIS B 2 47   ? -96.260  45.253  35.463  1.00 235.54 ? 47   HIS X ND1 1 
ATOM   12905 C  CD2 . HIS B 2 47   ? -95.569  43.218  35.086  1.00 237.61 ? 47   HIS X CD2 1 
ATOM   12906 C  CE1 . HIS B 2 47   ? -94.940  45.288  35.444  1.00 235.29 ? 47   HIS X CE1 1 
ATOM   12907 N  NE2 . HIS B 2 47   ? -94.497  44.065  35.215  1.00 236.75 ? 47   HIS X NE2 1 
ATOM   12908 N  N   . ARG B 2 48   ? -98.750  40.282  34.718  1.00 239.07 ? 48   ARG X N   1 
ATOM   12909 C  CA  . ARG B 2 48   ? -98.313  38.937  35.092  1.00 238.93 ? 48   ARG X CA  1 
ATOM   12910 C  C   . ARG B 2 48   ? -98.464  37.919  33.958  1.00 235.53 ? 48   ARG X C   1 
ATOM   12911 O  O   . ARG B 2 48   ? -97.671  36.981  33.838  1.00 237.15 ? 48   ARG X O   1 
ATOM   12912 C  CB  . ARG B 2 48   ? -99.078  38.458  36.328  1.00 241.49 ? 48   ARG X CB  1 
ATOM   12913 C  CG  . ARG B 2 48   ? -99.014  39.419  37.508  1.00 242.40 ? 48   ARG X CG  1 
ATOM   12914 C  CD  . ARG B 2 48   ? -99.856  38.913  38.666  1.00 244.98 ? 48   ARG X CD  1 
ATOM   12915 N  NE  . ARG B 2 48   ? -101.174 38.468  38.221  1.00 246.48 ? 48   ARG X NE  1 
ATOM   12916 C  CZ  . ARG B 2 48   ? -102.043 37.824  38.991  1.00 248.40 ? 48   ARG X CZ  1 
ATOM   12917 N  NH1 . ARG B 2 48   ? -103.218 37.455  38.501  1.00 249.01 ? 48   ARG X NH1 1 
ATOM   12918 N  NH2 . ARG B 2 48   ? -101.735 37.546  40.250  1.00 249.47 ? 48   ARG X NH2 1 
ATOM   12919 N  N   . TYR B 2 49   ? -99.488  38.102  33.134  1.00 230.33 ? 49   TYR X N   1 
ATOM   12920 C  CA  . TYR B 2 49   ? -99.753  37.179  32.039  1.00 226.48 ? 49   TYR X CA  1 
ATOM   12921 C  C   . TYR B 2 49   ? -98.814  37.405  30.851  1.00 220.55 ? 49   TYR X C   1 
ATOM   12922 O  O   . TYR B 2 49   ? -98.381  36.452  30.205  1.00 221.42 ? 49   TYR X O   1 
ATOM   12923 C  CB  . TYR B 2 49   ? -101.212 37.296  31.585  1.00 226.73 ? 49   TYR X CB  1 
ATOM   12924 C  CG  . TYR B 2 49   ? -102.254 36.873  32.613  1.00 227.69 ? 49   TYR X CG  1 
ATOM   12925 C  CD1 . TYR B 2 49   ? -102.880 35.629  32.531  1.00 229.85 ? 49   TYR X CD1 1 
ATOM   12926 C  CD2 . TYR B 2 49   ? -102.628 37.725  33.649  1.00 226.41 ? 49   TYR X CD2 1 
ATOM   12927 C  CE1 . TYR B 2 49   ? -103.840 35.243  33.457  1.00 230.66 ? 49   TYR X CE1 1 
ATOM   12928 C  CE2 . TYR B 2 49   ? -103.585 37.346  34.580  1.00 227.38 ? 49   TYR X CE2 1 
ATOM   12929 C  CZ  . TYR B 2 49   ? -104.186 36.105  34.478  1.00 229.72 ? 49   TYR X CZ  1 
ATOM   12930 O  OH  . TYR B 2 49   ? -105.134 35.725  35.400  1.00 231.01 ? 49   TYR X OH  1 
ATOM   12931 N  N   . TYR B 2 50   ? -98.509  38.669  30.565  1.00 214.76 ? 50   TYR X N   1 
ATOM   12932 C  CA  . TYR B 2 50   ? -97.688  39.020  29.407  1.00 210.35 ? 50   TYR X CA  1 
ATOM   12933 C  C   . TYR B 2 50   ? -96.188  39.028  29.687  1.00 206.69 ? 50   TYR X C   1 
ATOM   12934 O  O   . TYR B 2 50   ? -95.380  39.239  28.784  1.00 204.46 ? 50   TYR X O   1 
ATOM   12935 C  CB  . TYR B 2 50   ? -98.134  40.357  28.807  1.00 210.07 ? 50   TYR X CB  1 
ATOM   12936 C  CG  . TYR B 2 50   ? -99.286  40.208  27.837  1.00 212.16 ? 50   TYR X CG  1 
ATOM   12937 C  CD1 . TYR B 2 50   ? -99.347  39.119  26.971  1.00 214.28 ? 50   TYR X CD1 1 
ATOM   12938 C  CD2 . TYR B 2 50   ? -100.303 41.152  27.771  1.00 211.84 ? 50   TYR X CD2 1 
ATOM   12939 C  CE1 . TYR B 2 50   ? -100.389 38.966  26.077  1.00 215.10 ? 50   TYR X CE1 1 
ATOM   12940 C  CE2 . TYR B 2 50   ? -101.354 41.006  26.872  1.00 212.93 ? 50   TYR X CE2 1 
ATOM   12941 C  CZ  . TYR B 2 50   ? -101.389 39.908  26.030  1.00 214.71 ? 50   TYR X CZ  1 
ATOM   12942 O  OH  . TYR B 2 50   ? -102.421 39.746  25.134  1.00 215.94 ? 50   TYR X OH  1 
ATOM   12943 N  N   . SER B 2 51   ? -95.825  38.806  30.945  1.00 206.06 ? 51   SER X N   1 
ATOM   12944 C  CA  . SER B 2 51   ? -94.422  38.703  31.339  1.00 205.05 ? 51   SER X CA  1 
ATOM   12945 C  C   . SER B 2 51   ? -93.987  37.238  31.355  1.00 207.67 ? 51   SER X C   1 
ATOM   12946 O  O   . SER B 2 51   ? -92.816  36.909  31.572  1.00 208.87 ? 51   SER X O   1 
ATOM   12947 C  CB  . SER B 2 51   ? -94.200  39.357  32.710  1.00 203.13 ? 51   SER X CB  1 
ATOM   12948 O  OG  . SER B 2 51   ? -95.230  39.024  33.624  1.00 202.56 ? 51   SER X OG  1 
ATOM   12949 N  N   . SER B 2 52   ? -94.960  36.372  31.101  1.00 207.95 ? 52   SER X N   1 
ATOM   12950 C  CA  . SER B 2 52   ? -94.804  34.930  31.220  1.00 210.19 ? 52   SER X CA  1 
ATOM   12951 C  C   . SER B 2 52   ? -93.780  34.320  30.264  1.00 211.13 ? 52   SER X C   1 
ATOM   12952 O  O   . SER B 2 52   ? -93.219  35.004  29.402  1.00 207.22 ? 52   SER X O   1 
ATOM   12953 C  CB  . SER B 2 52   ? -96.165  34.266  30.998  1.00 212.61 ? 52   SER X CB  1 
ATOM   12954 O  OG  . SER B 2 52   ? -96.763  34.720  29.789  1.00 212.79 ? 52   SER X OG  1 
ATOM   12955 N  N   . GLU B 2 53   ? -93.547  33.020  30.434  1.00 215.80 ? 53   GLU X N   1 
ATOM   12956 C  CA  . GLU B 2 53   ? -92.694  32.260  29.531  1.00 219.91 ? 53   GLU X CA  1 
ATOM   12957 C  C   . GLU B 2 53   ? -93.460  31.745  28.318  1.00 228.03 ? 53   GLU X C   1 
ATOM   12958 O  O   . GLU B 2 53   ? -94.270  30.826  28.421  1.00 229.57 ? 53   GLU X O   1 
ATOM   12959 C  CB  . GLU B 2 53   ? -92.014  31.099  30.262  1.00 214.68 ? 53   GLU X CB  1 
ATOM   12960 C  CG  . GLU B 2 53   ? -90.781  31.514  31.050  1.00 208.31 ? 53   GLU X CG  1 
ATOM   12961 C  CD  . GLU B 2 53   ? -89.703  32.142  30.173  1.00 202.16 ? 53   GLU X CD  1 
ATOM   12962 O  OE1 . GLU B 2 53   ? -89.011  31.393  29.449  1.00 200.30 ? 53   GLU X OE1 1 
ATOM   12963 O  OE2 . GLU B 2 53   ? -89.539  33.384  30.219  1.00 199.10 ? 53   GLU X OE2 1 
ATOM   12964 N  N   . SER B 2 54   ? -93.187  32.355  27.169  1.00 235.69 ? 54   SER X N   1 
ATOM   12965 C  CA  . SER B 2 54   ? -93.745  31.926  25.893  1.00 245.71 ? 54   SER X CA  1 
ATOM   12966 C  C   . SER B 2 54   ? -93.033  30.687  25.344  1.00 258.03 ? 54   SER X C   1 
ATOM   12967 O  O   . SER B 2 54   ? -91.901  30.387  25.721  1.00 258.32 ? 54   SER X O   1 
ATOM   12968 C  CB  . SER B 2 54   ? -93.653  33.065  24.877  1.00 243.80 ? 54   SER X CB  1 
ATOM   12969 O  OG  . SER B 2 54   ? -93.763  32.573  23.554  1.00 244.93 ? 54   SER X OG  1 
ATOM   12970 N  N   . PHE B 2 55   ? -93.702  29.979  24.441  1.00 271.01 ? 55   PHE X N   1 
ATOM   12971 C  CA  . PHE B 2 55   ? -93.135  28.796  23.805  1.00 282.89 ? 55   PHE X CA  1 
ATOM   12972 C  C   . PHE B 2 55   ? -93.769  28.639  22.431  1.00 289.71 ? 55   PHE X C   1 
ATOM   12973 O  O   . PHE B 2 55   ? -94.830  29.202  22.164  1.00 290.00 ? 55   PHE X O   1 
ATOM   12974 C  CB  . PHE B 2 55   ? -93.393  27.550  24.661  1.00 287.58 ? 55   PHE X CB  1 
ATOM   12975 C  CG  . PHE B 2 55   ? -92.655  26.317  24.199  1.00 290.83 ? 55   PHE X CG  1 
ATOM   12976 C  CD1 . PHE B 2 55   ? -91.318  26.131  24.516  1.00 291.41 ? 55   PHE X CD1 1 
ATOM   12977 C  CD2 . PHE B 2 55   ? -93.306  25.333  23.465  1.00 292.14 ? 55   PHE X CD2 1 
ATOM   12978 C  CE1 . PHE B 2 55   ? -90.641  24.995  24.099  1.00 292.86 ? 55   PHE X CE1 1 
ATOM   12979 C  CE2 . PHE B 2 55   ? -92.638  24.194  23.044  1.00 293.45 ? 55   PHE X CE2 1 
ATOM   12980 C  CZ  . PHE B 2 55   ? -91.304  24.025  23.361  1.00 293.72 ? 55   PHE X CZ  1 
ATOM   12981 N  N   . GLU B 2 56   ? -93.114  27.878  21.561  1.00 295.40 ? 56   GLU X N   1 
ATOM   12982 C  CA  . GLU B 2 56   ? -93.609  27.653  20.207  1.00 300.30 ? 56   GLU X CA  1 
ATOM   12983 C  C   . GLU B 2 56   ? -93.260  26.236  19.754  1.00 298.88 ? 56   GLU X C   1 
ATOM   12984 O  O   . GLU B 2 56   ? -92.208  25.707  20.111  1.00 299.65 ? 56   GLU X O   1 
ATOM   12985 C  CB  . GLU B 2 56   ? -93.018  28.692  19.247  1.00 306.69 ? 56   GLU X CB  1 
ATOM   12986 C  CG  . GLU B 2 56   ? -93.617  28.677  17.847  1.00 313.01 ? 56   GLU X CG  1 
ATOM   12987 C  CD  . GLU B 2 56   ? -92.996  27.623  16.952  1.00 318.71 ? 56   GLU X CD  1 
ATOM   12988 O  OE1 . GLU B 2 56   ? -91.817  27.271  17.173  1.00 320.00 ? 56   GLU X OE1 1 
ATOM   12989 O  OE2 . GLU B 2 56   ? -93.687  27.152  16.025  1.00 321.34 ? 56   GLU X OE2 1 
ATOM   12990 N  N   . TYR B 2 57   ? -94.137  25.621  18.968  1.00 295.22 ? 57   TYR X N   1 
ATOM   12991 C  CA  . TYR B 2 57   ? -93.937  24.231  18.577  1.00 291.83 ? 57   TYR X CA  1 
ATOM   12992 C  C   . TYR B 2 57   ? -94.341  23.977  17.121  1.00 287.59 ? 57   TYR X C   1 
ATOM   12993 O  O   . TYR B 2 57   ? -95.052  24.782  16.515  1.00 288.14 ? 57   TYR X O   1 
ATOM   12994 C  CB  . TYR B 2 57   ? -94.712  23.302  19.518  1.00 291.21 ? 57   TYR X CB  1 
ATOM   12995 C  CG  . TYR B 2 57   ? -94.044  21.967  19.764  1.00 290.68 ? 57   TYR X CG  1 
ATOM   12996 C  CD1 . TYR B 2 57   ? -94.320  21.231  20.906  1.00 290.86 ? 57   TYR X CD1 1 
ATOM   12997 C  CD2 . TYR B 2 57   ? -93.124  21.451  18.862  1.00 290.23 ? 57   TYR X CD2 1 
ATOM   12998 C  CE1 . TYR B 2 57   ? -93.713  20.010  21.130  1.00 291.60 ? 57   TYR X CE1 1 
ATOM   12999 C  CE2 . TYR B 2 57   ? -92.510  20.235  19.078  1.00 290.72 ? 57   TYR X CE2 1 
ATOM   13000 C  CZ  . TYR B 2 57   ? -92.807  19.519  20.213  1.00 291.37 ? 57   TYR X CZ  1 
ATOM   13001 O  OH  . TYR B 2 57   ? -92.192  18.308  20.429  1.00 292.22 ? 57   TYR X OH  1 
ATOM   13002 N  N   . SER B 2 58   ? -93.874  22.855  16.570  1.00 282.21 ? 58   SER X N   1 
ATOM   13003 C  CA  . SER B 2 58   ? -94.153  22.468  15.185  1.00 275.44 ? 58   SER X CA  1 
ATOM   13004 C  C   . SER B 2 58   ? -94.053  20.953  14.987  1.00 269.55 ? 58   SER X C   1 
ATOM   13005 O  O   . SER B 2 58   ? -93.673  20.218  15.900  1.00 268.15 ? 58   SER X O   1 
ATOM   13006 C  CB  . SER B 2 58   ? -93.193  23.174  14.225  1.00 275.15 ? 58   SER X CB  1 
ATOM   13007 O  OG  . SER B 2 58   ? -91.847  22.826  14.502  1.00 275.39 ? 58   SER X OG  1 
ATOM   13008 N  N   . ASN B 2 59   ? -94.392  20.495  13.786  1.00 264.97 ? 59   ASN X N   1 
ATOM   13009 C  CA  . ASN B 2 59   ? -94.413  19.069  13.494  1.00 261.34 ? 59   ASN X CA  1 
ATOM   13010 C  C   . ASN B 2 59   ? -95.479  18.349  14.307  1.00 263.20 ? 59   ASN X C   1 
ATOM   13011 O  O   . ASN B 2 59   ? -95.488  17.121  14.379  1.00 265.27 ? 59   ASN X O   1 
ATOM   13012 C  CB  . ASN B 2 59   ? -93.047  18.434  13.755  1.00 254.72 ? 59   ASN X CB  1 
ATOM   13013 C  CG  . ASN B 2 59   ? -91.947  19.056  12.924  1.00 247.11 ? 59   ASN X CG  1 
ATOM   13014 O  OD1 . ASN B 2 59   ? -91.332  18.393  12.087  1.00 245.53 ? 59   ASN X OD1 1 
ATOM   13015 N  ND2 . ASN B 2 59   ? -91.696  20.340  13.145  1.00 243.09 ? 59   ASN X ND2 1 
ATOM   13016 N  N   . VAL B 2 60   ? -96.368  19.122  14.926  1.00 263.52 ? 60   VAL X N   1 
ATOM   13017 C  CA  . VAL B 2 60   ? -97.444  18.563  15.744  1.00 267.14 ? 60   VAL X CA  1 
ATOM   13018 C  C   . VAL B 2 60   ? -98.752  18.338  14.964  1.00 273.11 ? 60   VAL X C   1 
ATOM   13019 O  O   . VAL B 2 60   ? -99.437  19.294  14.593  1.00 272.18 ? 60   VAL X O   1 
ATOM   13020 C  CB  . VAL B 2 60   ? -97.727  19.432  17.010  1.00 238.36 ? 60   VAL X CB  1 
ATOM   13021 C  CG1 . VAL B 2 60   ? -96.583  19.328  18.010  1.00 238.12 ? 60   VAL X CG1 1 
ATOM   13022 C  CG2 . VAL B 2 60   ? -97.988  20.882  16.635  1.00 236.48 ? 60   VAL X CG2 1 
ATOM   13023 N  N   . SER B 2 61   ? -99.091  17.071  14.722  1.00 280.25 ? 61   SER X N   1 
ATOM   13024 C  CA  . SER B 2 61   ? -100.371 16.708  14.103  1.00 287.17 ? 61   SER X CA  1 
ATOM   13025 C  C   . SER B 2 61   ? -101.320 15.982  15.063  1.00 294.79 ? 61   SER X C   1 
ATOM   13026 O  O   . SER B 2 61   ? -100.918 15.041  15.748  1.00 295.35 ? 61   SER X O   1 
ATOM   13027 C  CB  . SER B 2 61   ? -100.146 15.847  12.860  1.00 288.14 ? 61   SER X CB  1 
ATOM   13028 O  OG  . SER B 2 61   ? -101.378 15.349  12.368  1.00 289.30 ? 61   SER X OG  1 
ATOM   13029 N  N   . GLY B 2 62   ? -102.585 16.401  15.088  1.00 302.25 ? 62   GLY X N   1 
ATOM   13030 C  CA  . GLY B 2 62   ? -103.570 15.814  15.985  1.00 310.96 ? 62   GLY X CA  1 
ATOM   13031 C  C   . GLY B 2 62   ? -104.955 15.634  15.378  1.00 319.58 ? 62   GLY X C   1 
ATOM   13032 O  O   . GLY B 2 62   ? -105.190 16.021  14.233  1.00 318.61 ? 62   GLY X O   1 
ATOM   13033 N  N   . LYS B 2 63   ? -105.877 15.055  16.149  1.00 328.10 ? 63   LYS X N   1 
ATOM   13034 C  CA  . LYS B 2 63   ? -107.229 14.766  15.661  1.00 335.92 ? 63   LYS X CA  1 
ATOM   13035 C  C   . LYS B 2 63   ? -108.333 15.180  16.645  1.00 339.27 ? 63   LYS X C   1 
ATOM   13036 O  O   . LYS B 2 63   ? -108.429 14.658  17.758  1.00 342.30 ? 63   LYS X O   1 
ATOM   13037 C  CB  . LYS B 2 63   ? -107.362 13.283  15.307  1.00 339.92 ? 63   LYS X CB  1 
ATOM   13038 C  CG  . LYS B 2 63   ? -106.890 12.347  16.400  1.00 342.64 ? 63   LYS X CG  1 
ATOM   13039 C  CD  . LYS B 2 63   ? -107.022 10.899  15.978  1.00 347.19 ? 63   LYS X CD  1 
ATOM   13040 C  CE  . LYS B 2 63   ? -106.796 9.978   17.157  1.00 350.69 ? 63   LYS X CE  1 
ATOM   13041 N  NZ  . LYS B 2 63   ? -107.625 10.399  18.317  1.00 352.13 ? 63   LYS X NZ  1 
ATOM   13042 N  N   . VAL B 2 64   ? -109.179 16.097  16.185  1.00 338.76 ? 64   VAL X N   1 
ATOM   13043 C  CA  . VAL B 2 64   ? -110.189 16.795  16.990  1.00 338.00 ? 64   VAL X CA  1 
ATOM   13044 C  C   . VAL B 2 64   ? -110.986 16.013  18.051  1.00 335.64 ? 64   VAL X C   1 
ATOM   13045 O  O   . VAL B 2 64   ? -111.280 14.830  17.881  1.00 337.85 ? 64   VAL X O   1 
ATOM   13046 C  CB  . VAL B 2 64   ? -111.222 17.464  16.049  1.00 341.24 ? 64   VAL X CB  1 
ATOM   13047 C  CG1 . VAL B 2 64   ? -111.844 16.417  15.134  1.00 344.71 ? 64   VAL X CG1 1 
ATOM   13048 C  CG2 . VAL B 2 64   ? -112.297 18.191  16.844  1.00 341.90 ? 64   VAL X CG2 1 
ATOM   13049 N  N   . GLU B 2 65   ? -111.309 16.707  19.146  1.00 330.52 ? 65   GLU X N   1 
ATOM   13050 C  CA  . GLU B 2 65   ? -112.403 16.350  20.057  1.00 326.83 ? 65   GLU X CA  1 
ATOM   13051 C  C   . GLU B 2 65   ? -112.968 17.642  20.654  1.00 320.52 ? 65   GLU X C   1 
ATOM   13052 O  O   . GLU B 2 65   ? -112.211 18.488  21.130  1.00 317.96 ? 65   GLU X O   1 
ATOM   13053 C  CB  . GLU B 2 65   ? -111.999 15.466  21.256  1.00 326.59 ? 65   GLU X CB  1 
ATOM   13054 C  CG  . GLU B 2 65   ? -110.612 14.788  21.386  1.00 324.57 ? 65   GLU X CG  1 
ATOM   13055 C  CD  . GLU B 2 65   ? -109.389 15.581  20.939  1.00 320.87 ? 65   GLU X CD  1 
ATOM   13056 O  OE1 . GLU B 2 65   ? -109.506 16.727  20.465  1.00 318.28 ? 65   GLU X OE1 1 
ATOM   13057 O  OE2 . GLU B 2 65   ? -108.283 15.009  21.058  1.00 320.70 ? 65   GLU X OE2 1 
ATOM   13058 N  N   . ASN B 2 66   ? -114.288 17.793  20.662  1.00 316.58 ? 66   ASN X N   1 
ATOM   13059 C  CA  . ASN B 2 66   ? -114.886 18.961  21.303  1.00 309.72 ? 66   ASN X CA  1 
ATOM   13060 C  C   . ASN B 2 66   ? -115.208 18.766  22.801  1.00 307.30 ? 66   ASN X C   1 
ATOM   13061 O  O   . ASN B 2 66   ? -116.066 17.961  23.165  1.00 308.29 ? 66   ASN X O   1 
ATOM   13062 C  CB  . ASN B 2 66   ? -116.091 19.496  20.503  1.00 306.18 ? 66   ASN X CB  1 
ATOM   13063 C  CG  . ASN B 2 66   ? -116.798 18.422  19.698  1.00 304.84 ? 66   ASN X CG  1 
ATOM   13064 O  OD1 . ASN B 2 66   ? -116.168 17.580  19.057  1.00 304.75 ? 66   ASN X OD1 1 
ATOM   13065 N  ND2 . ASN B 2 66   ? -118.124 18.460  19.716  1.00 304.37 ? 66   ASN X ND2 1 
ATOM   13066 N  N   . TYR B 2 67   ? -114.479 19.494  23.652  1.00 303.66 ? 67   TYR X N   1 
ATOM   13067 C  CA  . TYR B 2 67   ? -114.738 19.572  25.095  1.00 301.22 ? 67   TYR X CA  1 
ATOM   13068 C  C   . TYR B 2 67   ? -116.160 20.086  25.368  1.00 298.89 ? 67   TYR X C   1 
ATOM   13069 O  O   . TYR B 2 67   ? -117.038 19.299  25.715  1.00 302.93 ? 67   TYR X O   1 
ATOM   13070 C  CB  . TYR B 2 67   ? -113.647 20.411  25.804  1.00 298.65 ? 67   TYR X CB  1 
ATOM   13071 C  CG  . TYR B 2 67   ? -114.161 21.492  26.744  1.00 296.01 ? 67   TYR X CG  1 
ATOM   13072 C  CD1 . TYR B 2 67   ? -114.783 21.162  27.948  1.00 296.11 ? 67   TYR X CD1 1 
ATOM   13073 C  CD2 . TYR B 2 67   ? -114.006 22.844  26.431  1.00 291.87 ? 67   TYR X CD2 1 
ATOM   13074 C  CE1 . TYR B 2 67   ? -115.254 22.143  28.807  1.00 293.08 ? 67   TYR X CE1 1 
ATOM   13075 C  CE2 . TYR B 2 67   ? -114.469 23.836  27.284  1.00 288.90 ? 67   TYR X CE2 1 
ATOM   13076 C  CZ  . TYR B 2 67   ? -115.094 23.477  28.471  1.00 288.87 ? 67   TYR X CZ  1 
ATOM   13077 O  OH  . TYR B 2 67   ? -115.562 24.444  29.330  1.00 286.01 ? 67   TYR X OH  1 
ATOM   13078 N  N   . ASN B 2 68   ? -116.389 21.391  25.207  1.00 292.81 ? 68   ASN X N   1 
ATOM   13079 C  CA  . ASN B 2 68   ? -117.763 21.929  25.139  1.00 295.43 ? 68   ASN X CA  1 
ATOM   13080 C  C   . ASN B 2 68   ? -118.204 22.475  23.762  1.00 302.14 ? 68   ASN X C   1 
ATOM   13081 O  O   . ASN B 2 68   ? -118.681 21.713  22.920  1.00 308.67 ? 68   ASN X O   1 
ATOM   13082 C  CB  . ASN B 2 68   ? -118.088 22.912  26.290  1.00 293.26 ? 68   ASN X CB  1 
ATOM   13083 C  CG  . ASN B 2 68   ? -117.299 24.230  26.196  1.00 295.64 ? 68   ASN X CG  1 
ATOM   13084 O  OD1 . ASN B 2 68   ? -116.615 24.512  25.196  1.00 296.63 ? 68   ASN X OD1 1 
ATOM   13085 N  ND2 . ASN B 2 68   ? -117.400 25.042  27.235  1.00 295.56 ? 68   ASN X ND2 1 
ATOM   13086 N  N   . GLY B 2 69   ? -118.022 23.775  23.537  1.00 301.12 ? 69   GLY X N   1 
ATOM   13087 C  CA  . GLY B 2 69   ? -118.580 24.470  22.388  1.00 298.36 ? 69   GLY X CA  1 
ATOM   13088 C  C   . GLY B 2 69   ? -118.325 23.896  20.998  1.00 297.09 ? 69   GLY X C   1 
ATOM   13089 O  O   . GLY B 2 69   ? -119.277 23.635  20.254  1.00 298.14 ? 69   GLY X O   1 
ATOM   13090 N  N   . SER B 2 70   ? -117.055 23.692  20.649  1.00 292.43 ? 70   SER X N   1 
ATOM   13091 C  CA  . SER B 2 70   ? -116.687 23.364  19.279  1.00 287.30 ? 70   SER X CA  1 
ATOM   13092 C  C   . SER B 2 70   ? -115.387 22.585  19.128  1.00 280.95 ? 70   SER X C   1 
ATOM   13093 O  O   . SER B 2 70   ? -115.121 22.046  18.059  1.00 280.01 ? 70   SER X O   1 
ATOM   13094 C  CB  . SER B 2 70   ? -116.606 24.636  18.436  1.00 285.77 ? 70   SER X CB  1 
ATOM   13095 O  OG  . SER B 2 70   ? -117.859 25.202  18.187  1.00 285.53 ? 70   SER X OG  1 
ATOM   13096 N  N   . ASN B 2 71   ? -114.568 22.544  20.171  1.00 275.06 ? 71   ASN X N   1 
ATOM   13097 C  CA  . ASN B 2 71   ? -113.218 22.029  19.991  1.00 270.15 ? 71   ASN X CA  1 
ATOM   13098 C  C   . ASN B 2 71   ? -112.397 21.898  21.270  1.00 267.42 ? 71   ASN X C   1 
ATOM   13099 O  O   . ASN B 2 71   ? -112.778 22.413  22.319  1.00 268.18 ? 71   ASN X O   1 
ATOM   13100 C  CB  . ASN B 2 71   ? -112.469 22.940  19.008  1.00 265.23 ? 71   ASN X CB  1 
ATOM   13101 C  CG  . ASN B 2 71   ? -111.889 22.190  17.824  1.00 262.36 ? 71   ASN X CG  1 
ATOM   13102 O  OD1 . ASN B 2 71   ? -111.845 20.963  17.806  1.00 262.92 ? 71   ASN X OD1 1 
ATOM   13103 N  ND2 . ASN B 2 71   ? -111.446 22.938  16.816  1.00 259.92 ? 71   ASN X ND2 1 
ATOM   13104 N  N   . VAL B 2 72   ? -111.269 21.199  21.149  1.00 265.06 ? 72   VAL X N   1 
ATOM   13105 C  CA  . VAL B 2 72   ? -110.252 21.043  22.198  1.00 264.15 ? 72   VAL X CA  1 
ATOM   13106 C  C   . VAL B 2 72   ? -109.239 20.013  21.712  1.00 264.94 ? 72   VAL X C   1 
ATOM   13107 O  O   . VAL B 2 72   ? -109.605 19.059  21.025  1.00 264.28 ? 72   VAL X O   1 
ATOM   13108 C  CB  . VAL B 2 72   ? -110.831 20.602  23.564  1.00 265.84 ? 72   VAL X CB  1 
ATOM   13109 C  CG1 . VAL B 2 72   ? -109.965 19.512  24.194  1.00 268.09 ? 72   VAL X CG1 1 
ATOM   13110 C  CG2 . VAL B 2 72   ? -110.946 21.797  24.499  1.00 264.81 ? 72   VAL X CG2 1 
ATOM   13111 N  N   . VAL B 2 73   ? -107.968 20.200  22.055  1.00 266.40 ? 73   VAL X N   1 
ATOM   13112 C  CA  . VAL B 2 73   ? -106.923 19.332  21.517  1.00 268.28 ? 73   VAL X CA  1 
ATOM   13113 C  C   . VAL B 2 73   ? -105.906 18.923  22.584  1.00 266.54 ? 73   VAL X C   1 
ATOM   13114 O  O   . VAL B 2 73   ? -106.132 19.154  23.771  1.00 266.00 ? 73   VAL X O   1 
ATOM   13115 C  CB  . VAL B 2 73   ? -106.262 19.908  20.201  1.00 206.05 ? 73   VAL X CB  1 
ATOM   13116 C  CG1 . VAL B 2 73   ? -107.095 21.013  19.531  1.00 204.34 ? 73   VAL X CG1 1 
ATOM   13117 C  CG2 . VAL B 2 73   ? -104.763 20.174  20.299  1.00 205.32 ? 73   VAL X CG2 1 
ATOM   13118 N  N   . ARG B 2 74   ? -104.826 18.268  22.168  1.00 266.99 ? 74   ARG X N   1 
ATOM   13119 C  CA  . ARG B 2 74   ? -103.753 17.887  23.085  1.00 267.29 ? 74   ARG X CA  1 
ATOM   13120 C  C   . ARG B 2 74   ? -102.472 17.477  22.347  1.00 269.27 ? 74   ARG X C   1 
ATOM   13121 O  O   . ARG B 2 74   ? -102.511 17.126  21.165  1.00 270.36 ? 74   ARG X O   1 
ATOM   13122 C  CB  . ARG B 2 74   ? -104.216 16.767  24.024  1.00 269.27 ? 74   ARG X CB  1 
ATOM   13123 C  CG  . ARG B 2 74   ? -104.364 15.411  23.357  1.00 272.13 ? 74   ARG X CG  1 
ATOM   13124 C  CD  . ARG B 2 74   ? -104.947 14.391  24.315  1.00 275.00 ? 74   ARG X CD  1 
ATOM   13125 N  NE  . ARG B 2 74   ? -106.297 14.751  24.739  1.00 275.59 ? 74   ARG X NE  1 
ATOM   13126 C  CZ  . ARG B 2 74   ? -107.408 14.298  24.167  1.00 276.90 ? 74   ARG X CZ  1 
ATOM   13127 N  NH1 . ARG B 2 74   ? -107.338 13.460  23.141  1.00 278.14 ? 74   ARG X NH1 1 
ATOM   13128 N  NH2 . ARG B 2 74   ? -108.594 14.680  24.621  1.00 276.96 ? 74   ARG X NH2 1 
ATOM   13129 N  N   . PHE B 2 75   ? -101.343 17.527  23.055  1.00 270.10 ? 75   PHE X N   1 
ATOM   13130 C  CA  . PHE B 2 75   ? -100.043 17.152  22.489  1.00 271.54 ? 75   PHE X CA  1 
ATOM   13131 C  C   . PHE B 2 75   ? -98.962  16.824  23.520  1.00 266.81 ? 75   PHE X C   1 
ATOM   13132 O  O   . PHE B 2 75   ? -98.852  17.484  24.552  1.00 265.36 ? 75   PHE X O   1 
ATOM   13133 C  CB  . PHE B 2 75   ? -99.528  18.221  21.520  1.00 276.47 ? 75   PHE X CB  1 
ATOM   13134 C  CG  . PHE B 2 75   ? -99.624  17.811  20.093  1.00 283.14 ? 75   PHE X CG  1 
ATOM   13135 C  CD1 . PHE B 2 75   ? -98.673  16.973  19.547  1.00 286.26 ? 75   PHE X CD1 1 
ATOM   13136 C  CD2 . PHE B 2 75   ? -100.680 18.230  19.306  1.00 285.58 ? 75   PHE X CD2 1 
ATOM   13137 C  CE1 . PHE B 2 75   ? -98.765  16.572  18.242  1.00 288.29 ? 75   PHE X CE1 1 
ATOM   13138 C  CE2 . PHE B 2 75   ? -100.775 17.833  17.998  1.00 287.56 ? 75   PHE X CE2 1 
ATOM   13139 C  CZ  . PHE B 2 75   ? -99.817  17.001  17.468  1.00 288.68 ? 75   PHE X CZ  1 
ATOM   13140 N  N   . ASN B 2 76   ? -98.170  15.796  23.214  1.00 263.26 ? 76   ASN X N   1 
ATOM   13141 C  CA  . ASN B 2 76   ? -97.079  15.338  24.072  1.00 258.59 ? 76   ASN X CA  1 
ATOM   13142 C  C   . ASN B 2 76   ? -95.753  15.987  23.662  1.00 253.27 ? 76   ASN X C   1 
ATOM   13143 O  O   . ASN B 2 76   ? -95.061  15.492  22.774  1.00 252.44 ? 76   ASN X O   1 
ATOM   13144 C  CB  . ASN B 2 76   ? -96.983  13.806  24.012  1.00 260.29 ? 76   ASN X CB  1 
ATOM   13145 C  CG  . ASN B 2 76   ? -96.237  13.209  25.196  1.00 259.87 ? 76   ASN X CG  1 
ATOM   13146 O  OD1 . ASN B 2 76   ? -95.061  13.497  25.413  1.00 258.20 ? 76   ASN X OD1 1 
ATOM   13147 N  ND2 . ASN B 2 76   ? -96.918  12.355  25.955  1.00 261.65 ? 76   ASN X ND2 1 
ATOM   13148 N  N   . PRO B 2 77   ? -95.405  17.108  24.315  1.00 248.14 ? 77   PRO X N   1 
ATOM   13149 C  CA  . PRO B 2 77   ? -94.265  17.987  24.011  1.00 246.09 ? 77   PRO X CA  1 
ATOM   13150 C  C   . PRO B 2 77   ? -92.863  17.443  24.334  1.00 246.98 ? 77   PRO X C   1 
ATOM   13151 O  O   . PRO B 2 77   ? -91.901  18.081  23.910  1.00 245.35 ? 77   PRO X O   1 
ATOM   13152 C  CB  . PRO B 2 77   ? -94.547  19.211  24.892  1.00 243.22 ? 77   PRO X CB  1 
ATOM   13153 C  CG  . PRO B 2 77   ? -95.365  18.659  26.016  1.00 244.07 ? 77   PRO X CG  1 
ATOM   13154 C  CD  . PRO B 2 77   ? -96.284  17.720  25.325  1.00 246.43 ? 77   PRO X CD  1 
ATOM   13155 N  N   . LYS B 2 78   ? -92.770  16.323  25.058  1.00 250.87 ? 78   LYS X N   1 
ATOM   13156 C  CA  . LYS B 2 78   ? -91.508  15.671  25.493  1.00 253.94 ? 78   LYS X CA  1 
ATOM   13157 C  C   . LYS B 2 78   ? -91.290  15.657  27.022  1.00 263.17 ? 78   LYS X C   1 
ATOM   13158 O  O   . LYS B 2 78   ? -90.284  15.125  27.508  1.00 265.18 ? 78   LYS X O   1 
ATOM   13159 C  CB  . LYS B 2 78   ? -90.252  16.193  24.752  1.00 246.15 ? 78   LYS X CB  1 
ATOM   13160 C  CG  . LYS B 2 78   ? -89.739  17.575  25.163  1.00 238.86 ? 78   LYS X CG  1 
ATOM   13161 C  CD  . LYS B 2 78   ? -89.068  17.573  26.514  1.00 235.72 ? 78   LYS X CD  1 
ATOM   13162 C  CE  . LYS B 2 78   ? -89.206  18.927  27.172  1.00 231.85 ? 78   LYS X CE  1 
ATOM   13163 N  NZ  . LYS B 2 78   ? -88.862  18.864  28.614  1.00 231.46 ? 78   LYS X NZ  1 
ATOM   13164 N  N   . ASP B 2 79   ? -92.250  16.211  27.766  1.00 270.14 ? 79   ASP X N   1 
ATOM   13165 C  CA  . ASP B 2 79   ? -92.136  16.367  29.221  1.00 276.69 ? 79   ASP X CA  1 
ATOM   13166 C  C   . ASP B 2 79   ? -93.497  16.238  29.937  1.00 283.48 ? 79   ASP X C   1 
ATOM   13167 O  O   . ASP B 2 79   ? -93.552  15.937  31.131  1.00 284.41 ? 79   ASP X O   1 
ATOM   13168 C  CB  . ASP B 2 79   ? -91.471  17.714  29.548  1.00 274.55 ? 79   ASP X CB  1 
ATOM   13169 C  CG  . ASP B 2 79   ? -90.953  17.791  30.974  1.00 274.91 ? 79   ASP X CG  1 
ATOM   13170 O  OD1 . ASP B 2 79   ? -91.767  17.685  31.913  1.00 275.73 ? 79   ASP X OD1 1 
ATOM   13171 O  OD2 . ASP B 2 79   ? -89.730  17.983  31.153  1.00 274.45 ? 79   ASP X OD2 1 
ATOM   13172 N  N   . GLN B 2 80   ? -94.587  16.459  29.202  1.00 289.18 ? 80   GLN X N   1 
ATOM   13173 C  CA  . GLN B 2 80   ? -95.942  16.319  29.745  1.00 295.20 ? 80   GLN X CA  1 
ATOM   13174 C  C   . GLN B 2 80   ? -96.971  16.071  28.642  1.00 299.18 ? 80   GLN X C   1 
ATOM   13175 O  O   . GLN B 2 80   ? -96.671  15.431  27.635  1.00 299.37 ? 80   GLN X O   1 
ATOM   13176 C  CB  . GLN B 2 80   ? -96.344  17.553  30.559  1.00 295.17 ? 80   GLN X CB  1 
ATOM   13177 C  CG  . GLN B 2 80   ? -96.408  18.843  29.760  1.00 293.56 ? 80   GLN X CG  1 
ATOM   13178 C  CD  . GLN B 2 80   ? -95.099  19.605  29.779  1.00 292.56 ? 80   GLN X CD  1 
ATOM   13179 O  OE1 . GLN B 2 80   ? -95.025  20.746  29.327  1.00 291.21 ? 80   GLN X OE1 1 
ATOM   13180 N  NE2 . GLN B 2 80   ? -94.061  18.982  30.318  1.00 293.46 ? 80   GLN X NE2 1 
ATOM   13181 N  N   . ASN B 2 81   ? -98.187  16.575  28.841  1.00 301.98 ? 81   ASN X N   1 
ATOM   13182 C  CA  . ASN B 2 81   ? -99.250  16.452  27.847  1.00 305.16 ? 81   ASN X CA  1 
ATOM   13183 C  C   . ASN B 2 81   ? -100.204 17.639  27.908  1.00 308.07 ? 81   ASN X C   1 
ATOM   13184 O  O   . ASN B 2 81   ? -101.038 17.728  28.806  1.00 308.97 ? 81   ASN X O   1 
ATOM   13185 C  CB  . ASN B 2 81   ? -100.022 15.144  28.036  1.00 305.52 ? 81   ASN X CB  1 
ATOM   13186 C  CG  . ASN B 2 81   ? -99.331  13.960  27.390  1.00 304.49 ? 81   ASN X CG  1 
ATOM   13187 O  OD1 . ASN B 2 81   ? -99.425  13.758  26.179  1.00 303.70 ? 81   ASN X OD1 1 
ATOM   13188 N  ND2 . ASN B 2 81   ? -98.640  13.164  28.197  1.00 304.97 ? 81   ASN X ND2 1 
ATOM   13189 N  N   . HIS B 2 82   ? -100.084 18.536  26.934  1.00 310.21 ? 82   HIS X N   1 
ATOM   13190 C  CA  . HIS B 2 82   ? -100.771 19.826  26.965  1.00 312.06 ? 82   HIS X CA  1 
ATOM   13191 C  C   . HIS B 2 82   ? -102.211 19.817  26.456  1.00 309.47 ? 82   HIS X C   1 
ATOM   13192 O  O   . HIS B 2 82   ? -102.841 18.768  26.331  1.00 309.79 ? 82   HIS X O   1 
ATOM   13193 C  CB  . HIS B 2 82   ? -99.976  20.859  26.166  1.00 316.68 ? 82   HIS X CB  1 
ATOM   13194 C  CG  . HIS B 2 82   ? -98.689  21.266  26.812  1.00 321.28 ? 82   HIS X CG  1 
ATOM   13195 N  ND1 . HIS B 2 82   ? -98.640  22.071  27.929  1.00 322.12 ? 82   HIS X ND1 1 
ATOM   13196 C  CD2 . HIS B 2 82   ? -97.403  20.992  26.487  1.00 322.89 ? 82   HIS X CD2 1 
ATOM   13197 C  CE1 . HIS B 2 82   ? -97.379  22.270  28.270  1.00 322.38 ? 82   HIS X CE1 1 
ATOM   13198 N  NE2 . HIS B 2 82   ? -96.609  21.627  27.411  1.00 322.90 ? 82   HIS X NE2 1 
ATOM   13199 N  N   . GLN B 2 83   ? -102.711 21.014  26.164  1.00 305.94 ? 83   GLN X N   1 
ATOM   13200 C  CA  . GLN B 2 83   ? -104.042 21.203  25.604  1.00 304.44 ? 83   GLN X CA  1 
ATOM   13201 C  C   . GLN B 2 83   ? -104.058 22.463  24.742  1.00 302.54 ? 83   GLN X C   1 
ATOM   13202 O  O   . GLN B 2 83   ? -103.241 23.359  24.935  1.00 301.40 ? 83   GLN X O   1 
ATOM   13203 C  CB  . GLN B 2 83   ? -105.076 21.321  26.721  1.00 302.22 ? 83   GLN X CB  1 
ATOM   13204 C  CG  . GLN B 2 83   ? -106.508 21.408  26.227  1.00 300.52 ? 83   GLN X CG  1 
ATOM   13205 C  CD  . GLN B 2 83   ? -107.513 21.315  27.353  1.00 299.83 ? 83   GLN X CD  1 
ATOM   13206 O  OE1 . GLN B 2 83   ? -107.153 21.414  28.524  1.00 299.80 ? 83   GLN X OE1 1 
ATOM   13207 N  NE2 . GLN B 2 83   ? -108.781 21.123  27.007  1.00 299.66 ? 83   GLN X NE2 1 
ATOM   13208 N  N   . LEU B 2 84   ? -104.988 22.533  23.795  1.00 302.07 ? 84   LEU X N   1 
ATOM   13209 C  CA  . LEU B 2 84   ? -105.079 23.679  22.893  1.00 299.02 ? 84   LEU X CA  1 
ATOM   13210 C  C   . LEU B 2 84   ? -106.521 23.932  22.461  1.00 294.55 ? 84   LEU X C   1 
ATOM   13211 O  O   . LEU B 2 84   ? -107.201 23.034  21.966  1.00 298.05 ? 84   LEU X O   1 
ATOM   13212 C  CB  . LEU B 2 84   ? -104.181 23.471  21.669  1.00 301.03 ? 84   LEU X CB  1 
ATOM   13213 C  CG  . LEU B 2 84   ? -104.342 24.431  20.487  1.00 301.61 ? 84   LEU X CG  1 
ATOM   13214 C  CD1 . LEU B 2 84   ? -104.163 25.878  20.919  1.00 300.35 ? 84   LEU X CD1 1 
ATOM   13215 C  CD2 . LEU B 2 84   ? -103.365 24.079  19.374  1.00 302.72 ? 84   LEU X CD2 1 
ATOM   13216 N  N   . PHE B 2 85   ? -106.985 25.161  22.657  1.00 287.08 ? 85   PHE X N   1 
ATOM   13217 C  CA  . PHE B 2 85   ? -108.359 25.523  22.323  1.00 280.76 ? 85   PHE X CA  1 
ATOM   13218 C  C   . PHE B 2 85   ? -108.450 26.314  21.016  1.00 275.05 ? 85   PHE X C   1 
ATOM   13219 O  O   . PHE B 2 85   ? -108.085 27.490  20.960  1.00 274.00 ? 85   PHE X O   1 
ATOM   13220 C  CB  . PHE B 2 85   ? -108.997 26.311  23.472  1.00 279.86 ? 85   PHE X CB  1 
ATOM   13221 C  CG  . PHE B 2 85   ? -109.218 25.498  24.721  1.00 281.99 ? 85   PHE X CG  1 
ATOM   13222 C  CD1 . PHE B 2 85   ? -108.153 24.908  25.381  1.00 282.87 ? 85   PHE X CD1 1 
ATOM   13223 C  CD2 . PHE B 2 85   ? -110.492 25.337  25.243  1.00 283.63 ? 85   PHE X CD2 1 
ATOM   13224 C  CE1 . PHE B 2 85   ? -108.354 24.169  26.530  1.00 285.18 ? 85   PHE X CE1 1 
ATOM   13225 C  CE2 . PHE B 2 85   ? -110.700 24.596  26.395  1.00 285.89 ? 85   PHE X CE2 1 
ATOM   13226 C  CZ  . PHE B 2 85   ? -109.629 24.011  27.037  1.00 286.62 ? 85   PHE X CZ  1 
ATOM   13227 N  N   . LEU B 2 86   ? -108.935 25.651  19.970  1.00 269.68 ? 86   LEU X N   1 
ATOM   13228 C  CA  . LEU B 2 86   ? -109.178 26.291  18.683  1.00 262.49 ? 86   LEU X CA  1 
ATOM   13229 C  C   . LEU B 2 86   ? -110.587 26.887  18.706  1.00 257.87 ? 86   LEU X C   1 
ATOM   13230 O  O   . LEU B 2 86   ? -111.549 26.180  19.000  1.00 257.99 ? 86   LEU X O   1 
ATOM   13231 C  CB  . LEU B 2 86   ? -109.044 25.252  17.561  1.00 262.16 ? 86   LEU X CB  1 
ATOM   13232 C  CG  . LEU B 2 86   ? -108.649 25.688  16.147  1.00 260.13 ? 86   LEU X CG  1 
ATOM   13233 C  CD1 . LEU B 2 86   ? -107.471 26.634  16.187  1.00 257.44 ? 86   LEU X CD1 1 
ATOM   13234 C  CD2 . LEU B 2 86   ? -108.341 24.475  15.276  1.00 261.14 ? 86   LEU X CD2 1 
ATOM   13235 N  N   . LEU B 2 87   ? -110.714 28.180  18.417  1.00 252.20 ? 87   LEU X N   1 
ATOM   13236 C  CA  . LEU B 2 87   ? -112.033 28.816  18.382  1.00 248.56 ? 87   LEU X CA  1 
ATOM   13237 C  C   . LEU B 2 87   ? -112.030 30.153  17.642  1.00 249.95 ? 87   LEU X C   1 
ATOM   13238 O  O   . LEU B 2 87   ? -112.841 31.039  17.924  1.00 249.89 ? 87   LEU X O   1 
ATOM   13239 C  CB  . LEU B 2 87   ? -112.644 28.942  19.790  1.00 240.24 ? 87   LEU X CB  1 
ATOM   13240 C  CG  . LEU B 2 87   ? -111.854 29.523  20.966  1.00 231.03 ? 87   LEU X CG  1 
ATOM   13241 C  CD1 . LEU B 2 87   ? -111.934 31.036  20.964  1.00 226.66 ? 87   LEU X CD1 1 
ATOM   13242 C  CD2 . LEU B 2 87   ? -112.382 28.984  22.285  1.00 229.04 ? 87   LEU X CD2 1 
ATOM   13243 N  N   . GLY B 2 88   ? -111.109 30.287  16.691  1.00 253.80 ? 88   GLY X N   1 
ATOM   13244 C  CA  . GLY B 2 88   ? -111.037 31.468  15.849  1.00 257.84 ? 88   GLY X CA  1 
ATOM   13245 C  C   . GLY B 2 88   ? -111.841 31.266  14.583  1.00 266.38 ? 88   GLY X C   1 
ATOM   13246 O  O   . GLY B 2 88   ? -112.275 30.150  14.306  1.00 268.77 ? 88   GLY X O   1 
ATOM   13247 N  N   . LYS B 2 89   ? -112.044 32.330  13.812  1.00 272.40 ? 89   LYS X N   1 
ATOM   13248 C  CA  . LYS B 2 89   ? -112.785 32.211  12.561  1.00 280.59 ? 89   LYS X CA  1 
ATOM   13249 C  C   . LYS B 2 89   ? -112.092 31.224  11.622  1.00 290.31 ? 89   LYS X C   1 
ATOM   13250 O  O   . LYS B 2 89   ? -112.703 30.713  10.678  1.00 292.52 ? 89   LYS X O   1 
ATOM   13251 C  CB  . LYS B 2 89   ? -112.948 33.572  11.885  1.00 278.67 ? 89   LYS X CB  1 
ATOM   13252 C  CG  . LYS B 2 89   ? -113.775 33.525  10.615  1.00 279.62 ? 89   LYS X CG  1 
ATOM   13253 C  CD  . LYS B 2 89   ? -115.148 32.950  10.884  1.00 281.57 ? 89   LYS X CD  1 
ATOM   13254 C  CE  . LYS B 2 89   ? -115.948 32.845  9.606   1.00 284.37 ? 89   LYS X CE  1 
ATOM   13255 N  NZ  . LYS B 2 89   ? -117.327 32.376  9.886   1.00 286.46 ? 89   LYS X NZ  1 
ATOM   13256 N  N   . ASP B 2 90   ? -110.813 30.965  11.897  1.00 295.49 ? 90   ASP X N   1 
ATOM   13257 C  CA  . ASP B 2 90   ? -110.023 29.983  11.155  1.00 300.70 ? 90   ASP X CA  1 
ATOM   13258 C  C   . ASP B 2 90   ? -110.255 28.553  11.650  1.00 302.00 ? 90   ASP X C   1 
ATOM   13259 O  O   . ASP B 2 90   ? -109.838 27.594  10.997  1.00 303.62 ? 90   ASP X O   1 
ATOM   13260 C  CB  . ASP B 2 90   ? -108.531 30.316  11.236  1.00 301.99 ? 90   ASP X CB  1 
ATOM   13261 C  CG  . ASP B 2 90   ? -108.152 31.516  10.392  1.00 302.36 ? 90   ASP X CG  1 
ATOM   13262 O  OD1 . ASP B 2 90   ? -109.003 31.996  9.614   1.00 302.90 ? 90   ASP X OD1 1 
ATOM   13263 O  OD2 . ASP B 2 90   ? -106.999 31.979  10.502  1.00 301.62 ? 90   ASP X OD2 1 
ATOM   13264 N  N   . LYS B 2 91   ? -110.904 28.417  12.807  1.00 300.43 ? 91   LYS X N   1 
ATOM   13265 C  CA  . LYS B 2 91   ? -111.233 27.100  13.360  1.00 300.72 ? 91   LYS X CA  1 
ATOM   13266 C  C   . LYS B 2 91   ? -112.429 26.445  12.676  1.00 297.48 ? 91   LYS X C   1 
ATOM   13267 O  O   . LYS B 2 91   ? -112.487 25.219  12.559  1.00 299.96 ? 91   LYS X O   1 
ATOM   13268 C  CB  . LYS B 2 91   ? -111.525 27.177  14.858  1.00 303.15 ? 91   LYS X CB  1 
ATOM   13269 C  CG  . LYS B 2 91   ? -111.841 25.809  15.462  1.00 308.26 ? 91   LYS X CG  1 
ATOM   13270 C  CD  . LYS B 2 91   ? -112.880 25.880  16.568  1.00 311.36 ? 91   LYS X CD  1 
ATOM   13271 C  CE  . LYS B 2 91   ? -114.233 25.355  16.114  1.00 315.06 ? 91   LYS X CE  1 
ATOM   13272 N  NZ  . LYS B 2 91   ? -114.965 26.325  15.258  1.00 315.55 ? 91   LYS X NZ  1 
ATOM   13273 N  N   . GLU B 2 92   ? -113.397 27.258  12.258  1.00 291.46 ? 92   GLU X N   1 
ATOM   13274 C  CA  . GLU B 2 92   ? -114.570 26.741  11.558  1.00 286.07 ? 92   GLU X CA  1 
ATOM   13275 C  C   . GLU B 2 92   ? -114.138 26.116  10.231  1.00 286.82 ? 92   GLU X C   1 
ATOM   13276 O  O   . GLU B 2 92   ? -114.923 25.446  9.554   1.00 288.00 ? 92   GLU X O   1 
ATOM   13277 C  CB  . GLU B 2 92   ? -115.618 27.842  11.348  1.00 278.70 ? 92   GLU X CB  1 
ATOM   13278 C  CG  . GLU B 2 92   ? -116.966 27.326  10.858  1.00 274.63 ? 92   GLU X CG  1 
ATOM   13279 C  CD  . GLU B 2 92   ? -117.403 26.057  11.572  1.00 271.67 ? 92   GLU X CD  1 
ATOM   13280 O  OE1 . GLU B 2 92   ? -117.289 25.997  12.813  1.00 269.51 ? 92   GLU X OE1 1 
ATOM   13281 O  OE2 . GLU B 2 92   ? -117.865 25.119  10.890  1.00 272.31 ? 92   GLU X OE2 1 
ATOM   13282 N  N   . GLN B 2 93   ? -112.877 26.347  9.874   1.00 285.73 ? 93   GLN X N   1 
ATOM   13283 C  CA  . GLN B 2 93   ? -112.248 25.719  8.718   1.00 285.92 ? 93   GLN X CA  1 
ATOM   13284 C  C   . GLN B 2 93   ? -111.323 24.574  9.152   1.00 289.20 ? 93   GLN X C   1 
ATOM   13285 O  O   . GLN B 2 93   ? -110.665 23.951  8.318   1.00 290.39 ? 93   GLN X O   1 
ATOM   13286 C  CB  . GLN B 2 93   ? -111.460 26.760  7.916   1.00 281.60 ? 93   GLN X CB  1 
ATOM   13287 C  CG  . GLN B 2 93   ? -112.230 28.047  7.640   1.00 277.24 ? 93   GLN X CG  1 
ATOM   13288 C  CD  . GLN B 2 93   ? -111.354 29.146  7.067   1.00 272.75 ? 93   GLN X CD  1 
ATOM   13289 O  OE1 . GLN B 2 93   ? -110.139 28.986  6.940   1.00 271.13 ? 93   GLN X OE1 1 
ATOM   13290 N  NE2 . GLN B 2 93   ? -111.969 30.272  6.720   1.00 270.94 ? 93   GLN X NE2 1 
ATOM   13291 N  N   . TYR B 2 94   ? -111.282 24.299  10.457  1.00 290.56 ? 94   TYR X N   1 
ATOM   13292 C  CA  . TYR B 2 94   ? -110.367 23.299  11.019  1.00 293.39 ? 94   TYR X CA  1 
ATOM   13293 C  C   . TYR B 2 94   ? -110.895 22.556  12.249  1.00 290.13 ? 94   TYR X C   1 
ATOM   13294 O  O   . TYR B 2 94   ? -110.168 22.386  13.230  1.00 288.97 ? 94   TYR X O   1 
ATOM   13295 C  CB  . TYR B 2 94   ? -109.020 23.934  11.375  1.00 298.14 ? 94   TYR X CB  1 
ATOM   13296 C  CG  . TYR B 2 94   ? -107.920 23.632  10.391  1.00 304.50 ? 94   TYR X CG  1 
ATOM   13297 C  CD1 . TYR B 2 94   ? -107.504 22.327  10.168  1.00 308.45 ? 94   TYR X CD1 1 
ATOM   13298 C  CD2 . TYR B 2 94   ? -107.288 24.652  9.695   1.00 305.80 ? 94   TYR X CD2 1 
ATOM   13299 C  CE1 . TYR B 2 94   ? -106.498 22.044  9.273   1.00 309.97 ? 94   TYR X CE1 1 
ATOM   13300 C  CE2 . TYR B 2 94   ? -106.279 24.380  8.798   1.00 307.34 ? 94   TYR X CE2 1 
ATOM   13301 C  CZ  . TYR B 2 94   ? -105.887 23.074  8.591   1.00 309.03 ? 94   TYR X CZ  1 
ATOM   13302 O  OH  . TYR B 2 94   ? -104.880 22.799  7.696   1.00 309.30 ? 94   TYR X OH  1 
ATOM   13303 N  N   . LYS B 2 95   ? -112.151 22.123  12.204  1.00 288.05 ? 95   LYS X N   1 
ATOM   13304 C  CA  . LYS B 2 95   ? -112.681 21.242  13.239  1.00 285.31 ? 95   LYS X CA  1 
ATOM   13305 C  C   . LYS B 2 95   ? -112.190 19.818  13.011  1.00 285.54 ? 95   LYS X C   1 
ATOM   13306 O  O   . LYS B 2 95   ? -112.516 18.916  13.776  1.00 288.24 ? 95   LYS X O   1 
ATOM   13307 C  CB  . LYS B 2 95   ? -114.209 21.257  13.248  1.00 283.75 ? 95   LYS X CB  1 
ATOM   13308 C  CG  . LYS B 2 95   ? -114.830 22.476  13.897  1.00 280.04 ? 95   LYS X CG  1 
ATOM   13309 C  CD  . LYS B 2 95   ? -116.317 22.258  14.126  1.00 279.42 ? 95   LYS X CD  1 
ATOM   13310 C  CE  . LYS B 2 95   ? -116.950 23.434  14.848  1.00 276.78 ? 95   LYS X CE  1 
ATOM   13311 N  NZ  . LYS B 2 95   ? -118.356 23.148  15.251  1.00 277.35 ? 95   LYS X NZ  1 
ATOM   13312 N  N   . GLU B 2 96   ? -111.417 19.626  11.945  1.00 282.13 ? 96   GLU X N   1 
ATOM   13313 C  CA  . GLU B 2 96   ? -110.922 18.307  11.551  1.00 280.00 ? 96   GLU X CA  1 
ATOM   13314 C  C   . GLU B 2 96   ? -109.696 17.873  12.356  1.00 277.89 ? 96   GLU X C   1 
ATOM   13315 O  O   . GLU B 2 96   ? -109.651 16.761  12.887  1.00 279.25 ? 96   GLU X O   1 
ATOM   13316 C  CB  . GLU B 2 96   ? -110.596 18.301  10.053  1.00 278.68 ? 96   GLU X CB  1 
ATOM   13317 C  CG  . GLU B 2 96   ? -109.547 19.334  9.645   1.00 275.60 ? 96   GLU X CG  1 
ATOM   13318 C  CD  . GLU B 2 96   ? -109.605 19.689  8.172   1.00 275.18 ? 96   GLU X CD  1 
ATOM   13319 O  OE1 . GLU B 2 96   ? -110.724 19.749  7.619   1.00 276.02 ? 96   GLU X OE1 1 
ATOM   13320 O  OE2 . GLU B 2 96   ? -108.530 19.917  7.574   1.00 274.06 ? 96   GLU X OE2 1 
ATOM   13321 N  N   . GLY B 2 97   ? -108.703 18.754  12.432  1.00 274.10 ? 97   GLY X N   1 
ATOM   13322 C  CA  . GLY B 2 97   ? -107.476 18.472  13.155  1.00 271.35 ? 97   GLY X CA  1 
ATOM   13323 C  C   . GLY B 2 97   ? -106.289 19.266  12.639  1.00 267.45 ? 97   GLY X C   1 
ATOM   13324 O  O   . GLY B 2 97   ? -106.396 19.979  11.638  1.00 266.44 ? 97   GLY X O   1 
ATOM   13325 N  N   . LEU B 2 98   ? -105.157 19.145  13.333  1.00 264.99 ? 98   LEU X N   1 
ATOM   13326 C  CA  . LEU B 2 98   ? -103.916 19.809  12.935  1.00 262.04 ? 98   LEU X CA  1 
ATOM   13327 C  C   . LEU B 2 98   ? -102.989 18.897  12.134  1.00 261.86 ? 98   LEU X C   1 
ATOM   13328 O  O   . LEU B 2 98   ? -102.691 17.782  12.559  1.00 263.12 ? 98   LEU X O   1 
ATOM   13329 C  CB  . LEU B 2 98   ? -103.150 20.312  14.165  1.00 259.98 ? 98   LEU X CB  1 
ATOM   13330 C  CG  . LEU B 2 98   ? -103.652 21.507  14.978  1.00 257.98 ? 98   LEU X CG  1 
ATOM   13331 C  CD1 . LEU B 2 98   ? -102.540 21.979  15.907  1.00 256.60 ? 98   LEU X CD1 1 
ATOM   13332 C  CD2 . LEU B 2 98   ? -104.129 22.648  14.085  1.00 256.79 ? 98   LEU X CD2 1 
ATOM   13333 N  N   . GLN B 2 99   ? -102.537 19.373  10.977  1.00 260.93 ? 99   GLN X N   1 
ATOM   13334 C  CA  . GLN B 2 99   ? -101.409 18.758  10.286  1.00 261.47 ? 99   GLN X CA  1 
ATOM   13335 C  C   . GLN B 2 99   ? -100.159 19.579  10.611  1.00 261.25 ? 99   GLN X C   1 
ATOM   13336 O  O   . GLN B 2 99   ? -100.080 20.757  10.258  1.00 259.20 ? 99   GLN X O   1 
ATOM   13337 C  CB  . GLN B 2 99   ? -101.638 18.701  8.770   1.00 261.21 ? 99   GLN X CB  1 
ATOM   13338 C  CG  . GLN B 2 99   ? -102.983 18.128  8.336   1.00 261.96 ? 99   GLN X CG  1 
ATOM   13339 C  CD  . GLN B 2 99   ? -104.021 19.206  8.092   1.00 260.95 ? 99   GLN X CD  1 
ATOM   13340 O  OE1 . GLN B 2 99   ? -103.736 20.394  8.232   1.00 259.34 ? 99   GLN X OE1 1 
ATOM   13341 N  NE2 . GLN B 2 99   ? -105.232 18.798  7.718   1.00 261.97 ? 99   GLN X NE2 1 
ATOM   13342 N  N   . GLY B 2 100  ? -99.187  18.950  11.267  1.00 263.62 ? 100  GLY X N   1 
ATOM   13343 C  CA  . GLY B 2 100  ? -98.016  19.633  11.805  1.00 262.99 ? 100  GLY X CA  1 
ATOM   13344 C  C   . GLY B 2 100  ? -97.838  21.110  11.483  1.00 261.26 ? 100  GLY X C   1 
ATOM   13345 O  O   . GLY B 2 100  ? -97.056  21.474  10.606  1.00 259.97 ? 100  GLY X O   1 
ATOM   13346 N  N   . GLN B 2 101  ? -98.564  21.962  12.206  1.00 261.21 ? 101  GLN X N   1 
ATOM   13347 C  CA  . GLN B 2 101  ? -98.419  23.412  12.081  1.00 261.82 ? 101  GLN X CA  1 
ATOM   13348 C  C   . GLN B 2 101  ? -97.486  23.983  13.148  1.00 263.01 ? 101  GLN X C   1 
ATOM   13349 O  O   . GLN B 2 101  ? -96.960  23.247  13.987  1.00 262.18 ? 101  GLN X O   1 
ATOM   13350 C  CB  . GLN B 2 101  ? -99.776  24.115  12.189  1.00 261.92 ? 101  GLN X CB  1 
ATOM   13351 C  CG  . GLN B 2 101  ? -100.707 23.909  11.015  1.00 264.87 ? 101  GLN X CG  1 
ATOM   13352 C  CD  . GLN B 2 101  ? -101.698 22.799  11.261  1.00 268.53 ? 101  GLN X CD  1 
ATOM   13353 O  OE1 . GLN B 2 101  ? -101.579 22.054  12.234  1.00 269.76 ? 101  GLN X OE1 1 
ATOM   13354 N  NE2 . GLN B 2 101  ? -102.687 22.681  10.382  1.00 270.28 ? 101  GLN X NE2 1 
ATOM   13355 N  N   . ASN B 2 102  ? -97.283  25.298  13.103  1.00 265.71 ? 102  ASN X N   1 
ATOM   13356 C  CA  . ASN B 2 102  ? -96.598  26.021  14.173  1.00 267.82 ? 102  ASN X CA  1 
ATOM   13357 C  C   . ASN B 2 102  ? -97.592  26.560  15.197  1.00 275.77 ? 102  ASN X C   1 
ATOM   13358 O  O   . ASN B 2 102  ? -98.536  27.263  14.843  1.00 275.82 ? 102  ASN X O   1 
ATOM   13359 C  CB  . ASN B 2 102  ? -95.783  27.182  13.601  1.00 260.55 ? 102  ASN X CB  1 
ATOM   13360 C  CG  . ASN B 2 102  ? -94.553  26.722  12.864  1.00 255.10 ? 102  ASN X CG  1 
ATOM   13361 O  OD1 . ASN B 2 102  ? -94.440  26.897  11.654  1.00 252.93 ? 102  ASN X OD1 1 
ATOM   13362 N  ND2 . ASN B 2 102  ? -93.621  26.125  13.591  1.00 253.33 ? 102  ASN X ND2 1 
ATOM   13363 N  N   . VAL B 2 103  ? -97.369  26.238  16.465  1.00 283.69 ? 103  VAL X N   1 
ATOM   13364 C  CA  . VAL B 2 103  ? -98.258  26.690  17.519  1.00 292.22 ? 103  VAL X CA  1 
ATOM   13365 C  C   . VAL B 2 103  ? -97.501  27.460  18.579  1.00 300.10 ? 103  VAL X C   1 
ATOM   13366 O  O   . VAL B 2 103  ? -96.758  26.886  19.381  1.00 300.78 ? 103  VAL X O   1 
ATOM   13367 C  CB  . VAL B 2 103  ? -99.022  25.517  18.189  1.00 301.90 ? 103  VAL X CB  1 
ATOM   13368 C  CG1 . VAL B 2 103  ? -99.787  26.012  19.411  1.00 301.33 ? 103  VAL X CG1 1 
ATOM   13369 C  CG2 . VAL B 2 103  ? -99.968  24.855  17.199  1.00 303.58 ? 103  VAL X CG2 1 
ATOM   13370 N  N   . PHE B 2 104  ? -97.677  28.776  18.551  1.00 308.18 ? 104  PHE X N   1 
ATOM   13371 C  CA  . PHE B 2 104  ? -97.139  29.655  19.584  1.00 315.26 ? 104  PHE X CA  1 
ATOM   13372 C  C   . PHE B 2 104  ? -97.810  29.308  20.904  1.00 315.39 ? 104  PHE X C   1 
ATOM   13373 O  O   . PHE B 2 104  ? -98.757  29.966  21.329  1.00 314.90 ? 104  PHE X O   1 
ATOM   13374 C  CB  . PHE B 2 104  ? -97.435  31.109  19.206  1.00 320.97 ? 104  PHE X CB  1 
ATOM   13375 C  CG  . PHE B 2 104  ? -96.710  32.122  20.034  1.00 324.62 ? 104  PHE X CG  1 
ATOM   13376 C  CD1 . PHE B 2 104  ? -95.331  32.217  19.980  1.00 325.80 ? 104  PHE X CD1 1 
ATOM   13377 C  CD2 . PHE B 2 104  ? -97.408  32.988  20.861  1.00 325.29 ? 104  PHE X CD2 1 
ATOM   13378 C  CE1 . PHE B 2 104  ? -94.657  33.153  20.739  1.00 325.10 ? 104  PHE X CE1 1 
ATOM   13379 C  CE2 . PHE B 2 104  ? -96.738  33.928  21.618  1.00 324.50 ? 104  PHE X CE2 1 
ATOM   13380 C  CZ  . PHE B 2 104  ? -95.366  34.009  21.559  1.00 324.21 ? 104  PHE X CZ  1 
ATOM   13381 N  N   . VAL B 2 105  ? -97.319  28.254  21.543  1.00 315.02 ? 105  VAL X N   1 
ATOM   13382 C  CA  . VAL B 2 105  ? -97.922  27.768  22.780  1.00 313.03 ? 105  VAL X CA  1 
ATOM   13383 C  C   . VAL B 2 105  ? -97.432  28.540  24.007  1.00 307.24 ? 105  VAL X C   1 
ATOM   13384 O  O   . VAL B 2 105  ? -96.444  28.165  24.644  1.00 308.18 ? 105  VAL X O   1 
ATOM   13385 C  CB  . VAL B 2 105  ? -97.707  26.255  22.968  1.00 316.50 ? 105  VAL X CB  1 
ATOM   13386 C  CG1 . VAL B 2 105  ? -96.263  25.877  22.680  1.00 317.13 ? 105  VAL X CG1 1 
ATOM   13387 C  CG2 . VAL B 2 105  ? -98.126  25.813  24.360  1.00 317.51 ? 105  VAL X CG2 1 
ATOM   13388 N  N   . VAL B 2 106  ? -98.118  29.637  24.318  1.00 299.88 ? 106  VAL X N   1 
ATOM   13389 C  CA  . VAL B 2 106  ? -97.893  30.350  25.568  1.00 292.24 ? 106  VAL X CA  1 
ATOM   13390 C  C   . VAL B 2 106  ? -99.046  30.022  26.505  1.00 286.43 ? 106  VAL X C   1 
ATOM   13391 O  O   . VAL B 2 106  ? -100.193 29.932  26.071  1.00 286.43 ? 106  VAL X O   1 
ATOM   13392 C  CB  . VAL B 2 106  ? -97.809  31.867  25.348  1.00 290.57 ? 106  VAL X CB  1 
ATOM   13393 C  CG1 . VAL B 2 106  ? -96.850  32.178  24.222  1.00 290.03 ? 106  VAL X CG1 1 
ATOM   13394 C  CG2 . VAL B 2 106  ? -99.180  32.442  25.049  1.00 289.98 ? 106  VAL X CG2 1 
ATOM   13395 N  N   . GLN B 2 107  ? -98.747  29.832  27.783  1.00 280.09 ? 107  GLN X N   1 
ATOM   13396 C  CA  . GLN B 2 107  ? -99.773  29.424  28.735  1.00 274.31 ? 107  GLN X CA  1 
ATOM   13397 C  C   . GLN B 2 107  ? -100.702 30.578  29.135  1.00 268.98 ? 107  GLN X C   1 
ATOM   13398 O  O   . GLN B 2 107  ? -100.245 31.693  29.403  1.00 267.23 ? 107  GLN X O   1 
ATOM   13399 C  CB  . GLN B 2 107  ? -99.134  28.770  29.967  1.00 272.59 ? 107  GLN X CB  1 
ATOM   13400 C  CG  . GLN B 2 107  ? -97.983  29.555  30.580  1.00 268.87 ? 107  GLN X CG  1 
ATOM   13401 C  CD  . GLN B 2 107  ? -97.176  28.740  31.573  1.00 267.67 ? 107  GLN X CD  1 
ATOM   13402 O  OE1 . GLN B 2 107  ? -96.896  27.567  31.343  1.00 268.84 ? 107  GLN X OE1 1 
ATOM   13403 N  NE2 . GLN B 2 107  ? -96.801  29.361  32.687  1.00 265.88 ? 107  GLN X NE2 1 
ATOM   13404 N  N   . GLU B 2 108  ? -102.008 30.309  29.143  1.00 265.53 ? 108  GLU X N   1 
ATOM   13405 C  CA  . GLU B 2 108  ? -103.007 31.272  29.613  1.00 260.25 ? 108  GLU X CA  1 
ATOM   13406 C  C   . GLU B 2 108  ? -103.490 30.860  31.013  1.00 259.28 ? 108  GLU X C   1 
ATOM   13407 O  O   . GLU B 2 108  ? -103.854 31.705  31.834  1.00 257.82 ? 108  GLU X O   1 
ATOM   13408 C  CB  . GLU B 2 108  ? -104.199 31.329  28.650  1.00 258.06 ? 108  GLU X CB  1 
ATOM   13409 C  CG  . GLU B 2 108  ? -103.822 31.403  27.170  1.00 255.04 ? 108  GLU X CG  1 
ATOM   13410 C  CD  . GLU B 2 108  ? -103.467 32.804  26.721  1.00 250.47 ? 108  GLU X CD  1 
ATOM   13411 O  OE1 . GLU B 2 108  ? -104.162 33.753  27.130  1.00 248.33 ? 108  GLU X OE1 1 
ATOM   13412 O  OE2 . GLU B 2 108  ? -102.498 32.952  25.950  1.00 249.16 ? 108  GLU X OE2 1 
ATOM   13413 N  N   . LEU B 2 109  ? -103.483 29.551  31.256  1.00 260.14 ? 109  LEU X N   1 
ATOM   13414 C  CA  . LEU B 2 109  ? -103.806 28.956  32.538  1.00 262.13 ? 109  LEU X CA  1 
ATOM   13415 C  C   . LEU B 2 109  ? -103.190 27.560  32.504  1.00 271.45 ? 109  LEU X C   1 
ATOM   13416 O  O   . LEU B 2 109  ? -102.822 27.087  31.433  1.00 273.00 ? 109  LEU X O   1 
ATOM   13417 C  CB  . LEU B 2 109  ? -105.297 28.928  32.795  1.00 258.83 ? 109  LEU X CB  1 
ATOM   13418 C  CG  . LEU B 2 109  ? -105.975 30.145  33.351  1.00 253.85 ? 109  LEU X CG  1 
ATOM   13419 C  CD1 . LEU B 2 109  ? -107.495 29.975  33.442  1.00 256.00 ? 109  LEU X CD1 1 
ATOM   13420 C  CD2 . LEU B 2 109  ? -105.415 30.544  34.725  1.00 252.48 ? 109  LEU X CD2 1 
ATOM   13421 N  N   . ILE B 2 110  ? -103.109 26.882  33.646  1.00 280.30 ? 110  ILE X N   1 
ATOM   13422 C  CA  . ILE B 2 110  ? -102.385 25.612  33.700  1.00 290.17 ? 110  ILE X CA  1 
ATOM   13423 C  C   . ILE B 2 110  ? -103.018 24.550  34.600  1.00 301.08 ? 110  ILE X C   1 
ATOM   13424 O  O   . ILE B 2 110  ? -103.844 24.854  35.460  1.00 301.17 ? 110  ILE X O   1 
ATOM   13425 C  CB  . ILE B 2 110  ? -100.918 25.830  34.143  1.00 290.28 ? 110  ILE X CB  1 
ATOM   13426 C  CG1 . ILE B 2 110  ? -100.241 26.901  33.288  1.00 286.82 ? 110  ILE X CG1 1 
ATOM   13427 C  CG2 . ILE B 2 110  ? -100.122 24.535  34.072  1.00 293.09 ? 110  ILE X CG2 1 
ATOM   13428 C  CD1 . ILE B 2 110  ? -98.748  26.922  33.447  1.00 285.84 ? 110  ILE X CD1 1 
ATOM   13429 N  N   . ASP B 2 111  ? -102.636 23.297  34.366  1.00 310.73 ? 111  ASP X N   1 
ATOM   13430 C  CA  . ASP B 2 111  ? -102.973 22.185  35.253  1.00 320.48 ? 111  ASP X CA  1 
ATOM   13431 C  C   . ASP B 2 111  ? -101.708 21.774  36.015  1.00 324.26 ? 111  ASP X C   1 
ATOM   13432 O  O   . ASP B 2 111  ? -100.596 21.980  35.524  1.00 323.90 ? 111  ASP X O   1 
ATOM   13433 C  CB  . ASP B 2 111  ? -103.526 21.015  34.430  1.00 325.41 ? 111  ASP X CB  1 
ATOM   13434 C  CG  . ASP B 2 111  ? -104.095 19.902  35.290  1.00 330.01 ? 111  ASP X CG  1 
ATOM   13435 O  OD1 . ASP B 2 111  ? -103.304 19.095  35.818  1.00 332.80 ? 111  ASP X OD1 1 
ATOM   13436 O  OD2 . ASP B 2 111  ? -105.333 19.827  35.427  1.00 330.66 ? 111  ASP X OD2 1 
ATOM   13437 N  N   . PRO B 2 112  ? -101.866 21.211  37.225  1.00 327.29 ? 112  PRO X N   1 
ATOM   13438 C  CA  . PRO B 2 112  ? -100.711 20.822  38.046  1.00 328.08 ? 112  PRO X CA  1 
ATOM   13439 C  C   . PRO B 2 112  ? -99.681  19.942  37.327  1.00 327.56 ? 112  PRO X C   1 
ATOM   13440 O  O   . PRO B 2 112  ? -98.501  19.998  37.672  1.00 327.81 ? 112  PRO X O   1 
ATOM   13441 C  CB  . PRO B 2 112  ? -101.359 20.057  39.217  1.00 330.79 ? 112  PRO X CB  1 
ATOM   13442 C  CG  . PRO B 2 112  ? -102.798 19.822  38.788  1.00 331.58 ? 112  PRO X CG  1 
ATOM   13443 C  CD  . PRO B 2 112  ? -103.117 21.027  37.976  1.00 329.12 ? 112  PRO X CD  1 
ATOM   13444 N  N   . ASN B 2 113  ? -100.115 19.151  36.348  1.00 326.66 ? 113  ASN X N   1 
ATOM   13445 C  CA  . ASN B 2 113  ? -99.207  18.255  35.629  1.00 325.35 ? 113  ASN X CA  1 
ATOM   13446 C  C   . ASN B 2 113  ? -98.285  18.978  34.647  1.00 319.42 ? 113  ASN X C   1 
ATOM   13447 O  O   . ASN B 2 113  ? -97.484  18.348  33.956  1.00 319.37 ? 113  ASN X O   1 
ATOM   13448 C  CB  . ASN B 2 113  ? -99.984  17.147  34.905  1.00 328.77 ? 113  ASN X CB  1 
ATOM   13449 C  CG  . ASN B 2 113  ? -100.637 17.630  33.622  1.00 329.18 ? 113  ASN X CG  1 
ATOM   13450 O  OD1 . ASN B 2 113  ? -100.640 16.928  32.609  1.00 330.32 ? 113  ASN X OD1 1 
ATOM   13451 N  ND2 . ASN B 2 113  ? -101.194 18.834  33.658  1.00 328.10 ? 113  ASN X ND2 1 
ATOM   13452 N  N   . GLY B 2 114  ? -98.401  20.300  34.590  1.00 313.85 ? 114  GLY X N   1 
ATOM   13453 C  CA  . GLY B 2 114  ? -97.580  21.095  33.698  1.00 308.52 ? 114  GLY X CA  1 
ATOM   13454 C  C   . GLY B 2 114  ? -98.261  21.427  32.385  1.00 303.97 ? 114  GLY X C   1 
ATOM   13455 O  O   . GLY B 2 114  ? -97.860  22.367  31.695  1.00 302.37 ? 114  GLY X O   1 
ATOM   13456 N  N   . ARG B 2 115  ? -99.288  20.658  32.031  1.00 302.05 ? 115  ARG X N   1 
ATOM   13457 C  CA  . ARG B 2 115  ? -100.044 20.935  30.816  1.00 298.81 ? 115  ARG X CA  1 
ATOM   13458 C  C   . ARG B 2 115  ? -100.749 22.267  30.965  1.00 296.31 ? 115  ARG X C   1 
ATOM   13459 O  O   . ARG B 2 115  ? -101.235 22.608  32.041  1.00 295.02 ? 115  ARG X O   1 
ATOM   13460 C  CB  . ARG B 2 115  ? -101.057 19.830  30.519  1.00 299.70 ? 115  ARG X CB  1 
ATOM   13461 C  CG  . ARG B 2 115  ? -102.417 20.044  31.154  1.00 299.92 ? 115  ARG X CG  1 
ATOM   13462 C  CD  . ARG B 2 115  ? -103.384 18.949  30.739  1.00 302.08 ? 115  ARG X CD  1 
ATOM   13463 N  NE  . ARG B 2 115  ? -104.498 18.836  31.674  1.00 303.10 ? 115  ARG X NE  1 
ATOM   13464 C  CZ  . ARG B 2 115  ? -104.568 17.929  32.644  1.00 304.81 ? 115  ARG X CZ  1 
ATOM   13465 N  NH1 . ARG B 2 115  ? -103.585 17.049  32.804  1.00 305.91 ? 115  ARG X NH1 1 
ATOM   13466 N  NH2 . ARG B 2 115  ? -105.623 17.898  33.450  1.00 305.34 ? 115  ARG X NH2 1 
ATOM   13467 N  N   . LEU B 2 116  ? -100.817 23.013  29.873  1.00 296.30 ? 116  LEU X N   1 
ATOM   13468 C  CA  . LEU B 2 116  ? -101.312 24.373  29.938  1.00 295.54 ? 116  LEU X CA  1 
ATOM   13469 C  C   . LEU B 2 116  ? -102.293 24.656  28.811  1.00 299.26 ? 116  LEU X C   1 
ATOM   13470 O  O   . LEU B 2 116  ? -102.057 24.288  27.661  1.00 299.96 ? 116  LEU X O   1 
ATOM   13471 C  CB  . LEU B 2 116  ? -100.137 25.357  29.893  1.00 290.16 ? 116  LEU X CB  1 
ATOM   13472 C  CG  . LEU B 2 116  ? -99.127  25.169  28.757  1.00 285.71 ? 116  LEU X CG  1 
ATOM   13473 C  CD1 . LEU B 2 116  ? -99.497  26.037  27.567  1.00 283.10 ? 116  LEU X CD1 1 
ATOM   13474 C  CD2 . LEU B 2 116  ? -97.725  25.494  29.231  1.00 283.32 ? 116  LEU X CD2 1 
ATOM   13475 N  N   . SER B 2 117  ? -103.407 25.294  29.158  1.00 301.52 ? 117  SER X N   1 
ATOM   13476 C  CA  . SER B 2 117  ? -104.386 25.728  28.170  1.00 303.26 ? 117  SER X CA  1 
ATOM   13477 C  C   . SER B 2 117  ? -103.878 26.955  27.404  1.00 301.02 ? 117  SER X C   1 
ATOM   13478 O  O   . SER B 2 117  ? -103.099 27.749  27.935  1.00 300.64 ? 117  SER X O   1 
ATOM   13479 C  CB  . SER B 2 117  ? -105.729 26.023  28.844  1.00 305.44 ? 117  SER X CB  1 
ATOM   13480 O  OG  . SER B 2 117  ? -105.568 26.873  29.966  1.00 305.57 ? 117  SER X OG  1 
ATOM   13481 N  N   . THR B 2 118  ? -104.324 27.101  26.157  1.00 298.90 ? 118  THR X N   1 
ATOM   13482 C  CA  . THR B 2 118  ? -103.895 28.195  25.280  1.00 295.52 ? 118  THR X CA  1 
ATOM   13483 C  C   . THR B 2 118  ? -104.930 28.433  24.175  1.00 293.60 ? 118  THR X C   1 
ATOM   13484 O  O   . THR B 2 118  ? -105.764 27.570  23.903  1.00 295.53 ? 118  THR X O   1 
ATOM   13485 C  CB  . THR B 2 118  ? -102.505 27.910  24.652  1.00 311.68 ? 118  THR X CB  1 
ATOM   13486 O  OG1 . THR B 2 118  ? -102.160 28.954  23.731  1.00 309.93 ? 118  THR X OG1 1 
ATOM   13487 C  CG2 . THR B 2 118  ? -102.504 26.578  23.917  1.00 313.81 ? 118  THR X CG2 1 
ATOM   13488 N  N   . VAL B 2 119  ? -104.881 29.597  23.536  1.00 289.92 ? 119  VAL X N   1 
ATOM   13489 C  CA  . VAL B 2 119  ? -105.872 29.924  22.516  1.00 286.74 ? 119  VAL X CA  1 
ATOM   13490 C  C   . VAL B 2 119  ? -105.249 30.572  21.283  1.00 283.74 ? 119  VAL X C   1 
ATOM   13491 O  O   . VAL B 2 119  ? -104.608 31.618  21.370  1.00 281.85 ? 119  VAL X O   1 
ATOM   13492 C  CB  . VAL B 2 119  ? -106.984 30.838  23.081  1.00 284.33 ? 119  VAL X CB  1 
ATOM   13493 C  CG1 . VAL B 2 119  ? -106.383 31.984  23.878  1.00 281.54 ? 119  VAL X CG1 1 
ATOM   13494 C  CG2 . VAL B 2 119  ? -107.870 31.357  21.960  1.00 284.05 ? 119  VAL X CG2 1 
ATOM   13495 N  N   . GLY B 2 120  ? -105.450 29.939  20.133  1.00 282.39 ? 120  GLY X N   1 
ATOM   13496 C  CA  . GLY B 2 120  ? -104.908 30.432  18.883  1.00 279.23 ? 120  GLY X CA  1 
ATOM   13497 C  C   . GLY B 2 120  ? -103.410 30.229  18.791  1.00 276.03 ? 120  GLY X C   1 
ATOM   13498 O  O   . GLY B 2 120  ? -102.859 29.295  19.378  1.00 278.29 ? 120  GLY X O   1 
ATOM   13499 N  N   . GLY B 2 121  ? -102.752 31.106  18.040  1.00 271.57 ? 121  GLY X N   1 
ATOM   13500 C  CA  . GLY B 2 121  ? -101.305 31.084  17.921  1.00 268.70 ? 121  GLY X CA  1 
ATOM   13501 C  C   . GLY B 2 121  ? -100.773 30.183  16.822  1.00 268.73 ? 121  GLY X C   1 
ATOM   13502 O  O   . GLY B 2 121  ? -99.561  30.068  16.631  1.00 268.08 ? 121  GLY X O   1 
ATOM   13503 N  N   . VAL B 2 122  ? -101.680 29.545  16.093  1.00 268.58 ? 122  VAL X N   1 
ATOM   13504 C  CA  . VAL B 2 122  ? -101.283 28.601  15.056  1.00 266.73 ? 122  VAL X CA  1 
ATOM   13505 C  C   . VAL B 2 122  ? -100.929 29.278  13.731  1.00 259.90 ? 122  VAL X C   1 
ATOM   13506 O  O   . VAL B 2 122  ? -101.540 30.276  13.336  1.00 260.02 ? 122  VAL X O   1 
ATOM   13507 C  CB  . VAL B 2 122  ? -102.361 27.531  14.832  1.00 269.60 ? 122  VAL X CB  1 
ATOM   13508 C  CG1 . VAL B 2 122  ? -101.836 26.431  13.921  1.00 271.20 ? 122  VAL X CG1 1 
ATOM   13509 C  CG2 . VAL B 2 122  ? -102.805 26.955  16.166  1.00 270.35 ? 122  VAL X CG2 1 
ATOM   13510 N  N   . THR B 2 123  ? -99.940  28.707  13.052  1.00 252.56 ? 123  THR X N   1 
ATOM   13511 C  CA  . THR B 2 123  ? -99.436  29.231  11.789  1.00 246.20 ? 123  THR X CA  1 
ATOM   13512 C  C   . THR B 2 123  ? -99.135  28.070  10.829  1.00 242.29 ? 123  THR X C   1 
ATOM   13513 O  O   . THR B 2 123  ? -99.277  26.907  11.210  1.00 243.85 ? 123  THR X O   1 
ATOM   13514 C  CB  . THR B 2 123  ? -98.201  30.147  12.013  1.00 262.69 ? 123  THR X CB  1 
ATOM   13515 O  OG1 . THR B 2 123  ? -97.213  29.907  11.003  1.00 263.17 ? 123  THR X OG1 1 
ATOM   13516 C  CG2 . THR B 2 123  ? -97.586  29.898  13.384  1.00 262.27 ? 123  THR X CG2 1 
ATOM   13517 N  N   . LYS B 2 124  ? -98.730  28.384  9.596   1.00 237.99 ? 124  LYS X N   1 
ATOM   13518 C  CA  . LYS B 2 124  ? -98.673  27.393  8.506   1.00 233.08 ? 124  LYS X CA  1 
ATOM   13519 C  C   . LYS B 2 124  ? -97.791  26.143  8.715   1.00 232.86 ? 124  LYS X C   1 
ATOM   13520 O  O   . LYS B 2 124  ? -98.313  25.052  8.970   1.00 235.24 ? 124  LYS X O   1 
ATOM   13521 C  CB  . LYS B 2 124  ? -98.373  28.064  7.150   1.00 227.15 ? 124  LYS X CB  1 
ATOM   13522 C  CG  . LYS B 2 124  ? -97.118  28.918  7.100   1.00 219.76 ? 124  LYS X CG  1 
ATOM   13523 C  CD  . LYS B 2 124  ? -97.133  29.837  5.882   1.00 214.95 ? 124  LYS X CD  1 
ATOM   13524 C  CE  . LYS B 2 124  ? -97.046  29.060  4.579   1.00 213.69 ? 124  LYS X CE  1 
ATOM   13525 N  NZ  . LYS B 2 124  ? -95.666  28.572  4.322   1.00 213.03 ? 124  LYS X NZ  1 
ATOM   13526 N  N   . LYS B 2 125  ? -96.473  26.296  8.600   1.00 228.66 ? 125  LYS X N   1 
ATOM   13527 C  CA  . LYS B 2 125  ? -95.561  25.149  8.628   1.00 227.37 ? 125  LYS X CA  1 
ATOM   13528 C  C   . LYS B 2 125  ? -95.847  24.216  7.452   1.00 229.03 ? 125  LYS X C   1 
ATOM   13529 O  O   . LYS B 2 125  ? -96.917  23.606  7.391   1.00 229.39 ? 125  LYS X O   1 
ATOM   13530 C  CB  . LYS B 2 125  ? -95.670  24.389  9.958   1.00 225.60 ? 125  LYS X CB  1 
ATOM   13531 C  CG  . LYS B 2 125  ? -94.744  23.175  10.088  1.00 225.16 ? 125  LYS X CG  1 
ATOM   13532 C  CD  . LYS B 2 125  ? -93.312  23.586  10.392  1.00 222.59 ? 125  LYS X CD  1 
ATOM   13533 C  CE  . LYS B 2 125  ? -92.420  22.378  10.626  1.00 221.76 ? 125  LYS X CE  1 
ATOM   13534 N  NZ  . LYS B 2 125  ? -92.225  21.591  9.385   1.00 222.28 ? 125  LYS X NZ  1 
ATOM   13535 N  N   . ASN B 2 126  ? -94.899  24.091  6.522   1.00 230.62 ? 126  ASN X N   1 
ATOM   13536 C  CA  . ASN B 2 126  ? -93.590  24.735  6.609   1.00 230.57 ? 126  ASN X CA  1 
ATOM   13537 C  C   . ASN B 2 126  ? -93.626  26.263  6.621   1.00 236.85 ? 126  ASN X C   1 
ATOM   13538 O  O   . ASN B 2 126  ? -93.940  26.907  5.617   1.00 238.88 ? 126  ASN X O   1 
ATOM   13539 C  CB  . ASN B 2 126  ? -92.681  24.236  5.483   1.00 225.58 ? 126  ASN X CB  1 
ATOM   13540 C  CG  . ASN B 2 126  ? -92.456  22.740  5.540   1.00 218.72 ? 126  ASN X CG  1 
ATOM   13541 O  OD1 . ASN B 2 126  ? -92.502  22.138  6.612   1.00 216.23 ? 126  ASN X OD1 1 
ATOM   13542 N  ND2 . ASN B 2 126  ? -92.213  22.130  4.385   1.00 222.75 ? 126  ASN X ND2 1 
ATOM   13543 N  N   . ASN B 2 127  ? -93.295  26.824  7.781   1.00 242.43 ? 127  ASN X N   1 
ATOM   13544 C  CA  . ASN B 2 127  ? -93.298  28.264  8.000   1.00 247.45 ? 127  ASN X CA  1 
ATOM   13545 C  C   . ASN B 2 127  ? -91.929  28.865  7.705   1.00 251.84 ? 127  ASN X C   1 
ATOM   13546 O  O   . ASN B 2 127  ? -90.967  28.622  8.439   1.00 250.76 ? 127  ASN X O   1 
ATOM   13547 C  CB  . ASN B 2 127  ? -93.702  28.570  9.446   1.00 250.95 ? 127  ASN X CB  1 
ATOM   13548 C  CG  . ASN B 2 127  ? -94.137  30.012  9.646   1.00 254.33 ? 127  ASN X CG  1 
ATOM   13549 O  OD1 . ASN B 2 127  ? -94.190  30.799  8.698   1.00 255.84 ? 127  ASN X OD1 1 
ATOM   13550 N  ND2 . ASN B 2 127  ? -94.457  30.364  10.888  1.00 255.21 ? 127  ASN X ND2 1 
ATOM   13551 N  N   . LYS B 2 128  ? -91.852  29.651  6.634   1.00 255.38 ? 128  LYS X N   1 
ATOM   13552 C  CA  . LYS B 2 128  ? -90.603  30.287  6.223   1.00 257.69 ? 128  LYS X CA  1 
ATOM   13553 C  C   . LYS B 2 128  ? -89.932  30.984  7.413   1.00 260.49 ? 128  LYS X C   1 
ATOM   13554 O  O   . LYS B 2 128  ? -90.600  31.677  8.181   1.00 260.18 ? 128  LYS X O   1 
ATOM   13555 C  CB  . LYS B 2 128  ? -90.869  31.292  5.092   1.00 253.93 ? 128  LYS X CB  1 
ATOM   13556 C  CG  . LYS B 2 128  ? -91.734  30.758  3.952   1.00 250.38 ? 128  LYS X CG  1 
ATOM   13557 C  CD  . LYS B 2 128  ? -91.960  31.818  2.887   1.00 245.55 ? 128  LYS X CD  1 
ATOM   13558 C  CE  . LYS B 2 128  ? -90.665  32.531  2.542   1.00 241.64 ? 128  LYS X CE  1 
ATOM   13559 N  NZ  . LYS B 2 128  ? -89.600  31.573  2.149   1.00 240.91 ? 128  LYS X NZ  1 
ATOM   13560 N  N   . THR B 2 129  ? -88.622  30.792  7.576   1.00 211.09 ? 129  THR X N   1 
ATOM   13561 C  CA  . THR B 2 129  ? -87.889  31.420  8.682   1.00 211.26 ? 129  THR X CA  1 
ATOM   13562 C  C   . THR B 2 129  ? -87.397  32.828  8.328   1.00 211.82 ? 129  THR X C   1 
ATOM   13563 O  O   . THR B 2 129  ? -86.267  33.204  8.640   1.00 210.58 ? 129  THR X O   1 
ATOM   13564 C  CB  . THR B 2 129  ? -86.716  30.543  9.181   1.00 212.05 ? 129  THR X CB  1 
ATOM   13565 O  OG1 . THR B 2 129  ? -87.153  29.186  9.301   1.00 213.83 ? 129  THR X OG1 1 
ATOM   13566 C  CG2 . THR B 2 129  ? -86.224  31.020  10.543  1.00 210.49 ? 129  THR X CG2 1 
ATOM   13567 N  N   . SER B 2 130  ? -88.258  33.593  7.661   1.00 213.94 ? 130  SER X N   1 
ATOM   13568 C  CA  . SER B 2 130  ? -88.003  35.002  7.382   1.00 215.06 ? 130  SER X CA  1 
ATOM   13569 C  C   . SER B 2 130  ? -87.918  35.833  8.667   1.00 216.59 ? 130  SER X C   1 
ATOM   13570 O  O   . SER B 2 130  ? -88.536  35.494  9.677   1.00 216.19 ? 130  SER X O   1 
ATOM   13571 C  CB  . SER B 2 130  ? -89.096  35.563  6.476   1.00 213.98 ? 130  SER X CB  1 
ATOM   13572 O  OG  . SER B 2 130  ? -89.265  36.948  6.706   1.00 211.89 ? 130  SER X OG  1 
ATOM   13573 N  N   . GLU B 2 131  ? -87.164  36.931  8.609   1.00 217.83 ? 131  GLU X N   1 
ATOM   13574 C  CA  . GLU B 2 131  ? -86.891  37.783  9.770   1.00 216.55 ? 131  GLU X CA  1 
ATOM   13575 C  C   . GLU B 2 131  ? -87.022  39.250  9.388   1.00 215.98 ? 131  GLU X C   1 
ATOM   13576 O  O   . GLU B 2 131  ? -86.076  39.841  8.867   1.00 216.98 ? 131  GLU X O   1 
ATOM   13577 C  CB  . GLU B 2 131  ? -85.467  37.532  10.289  1.00 215.69 ? 131  GLU X CB  1 
ATOM   13578 C  CG  . GLU B 2 131  ? -84.831  38.731  11.012  1.00 213.69 ? 131  GLU X CG  1 
ATOM   13579 C  CD  . GLU B 2 131  ? -83.322  38.585  11.239  1.00 212.73 ? 131  GLU X CD  1 
ATOM   13580 O  OE1 . GLU B 2 131  ? -82.889  37.546  11.777  1.00 212.61 ? 131  GLU X OE1 1 
ATOM   13581 O  OE2 . GLU B 2 131  ? -82.561  39.518  10.898  1.00 211.99 ? 131  GLU X OE2 1 
ATOM   13582 N  N   . THR B 2 132  ? -88.185  39.843  9.637   1.00 214.20 ? 132  THR X N   1 
ATOM   13583 C  CA  . THR B 2 132  ? -88.378  41.245  9.277   1.00 212.80 ? 132  THR X CA  1 
ATOM   13584 C  C   . THR B 2 132  ? -88.123  42.220  10.433  1.00 209.34 ? 132  THR X C   1 
ATOM   13585 O  O   . THR B 2 132  ? -88.475  41.961  11.589  1.00 208.17 ? 132  THR X O   1 
ATOM   13586 C  CB  . THR B 2 132  ? -89.757  41.504  8.638   1.00 213.73 ? 132  THR X CB  1 
ATOM   13587 O  OG1 . THR B 2 132  ? -89.902  42.904  8.372   1.00 214.29 ? 132  THR X OG1 1 
ATOM   13588 C  CG2 . THR B 2 132  ? -90.864  41.050  9.557   1.00 212.82 ? 132  THR X CG2 1 
ATOM   13589 N  N   . ASN B 2 133  ? -87.479  43.332  10.101  1.00 207.01 ? 133  ASN X N   1 
ATOM   13590 C  CA  . ASN B 2 133  ? -87.243  44.416  11.043  1.00 201.90 ? 133  ASN X CA  1 
ATOM   13591 C  C   . ASN B 2 133  ? -88.276  45.518  10.805  1.00 197.64 ? 133  ASN X C   1 
ATOM   13592 O  O   . ASN B 2 133  ? -88.075  46.377  9.945   1.00 200.63 ? 133  ASN X O   1 
ATOM   13593 C  CB  . ASN B 2 133  ? -85.831  44.963  10.837  1.00 200.87 ? 133  ASN X CB  1 
ATOM   13594 C  CG  . ASN B 2 133  ? -85.335  45.749  12.017  1.00 197.77 ? 133  ASN X CG  1 
ATOM   13595 O  OD1 . ASN B 2 133  ? -85.414  45.292  13.152  1.00 196.07 ? 133  ASN X OD1 1 
ATOM   13596 N  ND2 . ASN B 2 133  ? -84.812  46.939  11.756  1.00 197.26 ? 133  ASN X ND2 1 
ATOM   13597 N  N   . THR B 2 134  ? -89.378  45.491  11.557  1.00 190.54 ? 134  THR X N   1 
ATOM   13598 C  CA  . THR B 2 134  ? -90.521  46.382  11.295  1.00 184.29 ? 134  THR X CA  1 
ATOM   13599 C  C   . THR B 2 134  ? -90.541  47.701  12.068  1.00 179.26 ? 134  THR X C   1 
ATOM   13600 O  O   . THR B 2 134  ? -90.366  47.715  13.289  1.00 176.31 ? 134  THR X O   1 
ATOM   13601 C  CB  . THR B 2 134  ? -91.886  45.679  11.542  1.00 206.59 ? 134  THR X CB  1 
ATOM   13602 O  OG1 . THR B 2 134  ? -92.935  46.656  11.510  1.00 207.12 ? 134  THR X OG1 1 
ATOM   13603 C  CG2 . THR B 2 134  ? -91.917  44.993  12.893  1.00 204.86 ? 134  THR X CG2 1 
ATOM   13604 N  N   . PRO B 2 135  ? -90.787  48.814  11.352  1.00 177.12 ? 135  PRO X N   1 
ATOM   13605 C  CA  . PRO B 2 135  ? -91.075  50.083  12.023  1.00 176.53 ? 135  PRO X CA  1 
ATOM   13606 C  C   . PRO B 2 135  ? -92.167  49.882  13.087  1.00 174.14 ? 135  PRO X C   1 
ATOM   13607 O  O   . PRO B 2 135  ? -92.799  48.821  13.115  1.00 174.28 ? 135  PRO X O   1 
ATOM   13608 C  CB  . PRO B 2 135  ? -91.550  50.984  10.869  1.00 177.89 ? 135  PRO X CB  1 
ATOM   13609 C  CG  . PRO B 2 135  ? -91.783  50.036  9.693   1.00 178.16 ? 135  PRO X CG  1 
ATOM   13610 C  CD  . PRO B 2 135  ? -90.758  48.984  9.890   1.00 177.84 ? 135  PRO X CD  1 
ATOM   13611 N  N   . LEU B 2 136  ? -92.377  50.877  13.946  1.00 172.00 ? 136  LEU X N   1 
ATOM   13612 C  CA  . LEU B 2 136  ? -93.173  50.690  15.158  1.00 168.82 ? 136  LEU X CA  1 
ATOM   13613 C  C   . LEU B 2 136  ? -92.967  51.856  16.110  1.00 170.12 ? 136  LEU X C   1 
ATOM   13614 O  O   . LEU B 2 136  ? -91.904  51.982  16.730  1.00 169.80 ? 136  LEU X O   1 
ATOM   13615 C  CB  . LEU B 2 136  ? -92.747  49.403  15.869  1.00 165.39 ? 136  LEU X CB  1 
ATOM   13616 C  CG  . LEU B 2 136  ? -92.840  49.443  17.395  1.00 161.55 ? 136  LEU X CG  1 
ATOM   13617 C  CD1 . LEU B 2 136  ? -94.297  49.503  17.826  1.00 160.91 ? 136  LEU X CD1 1 
ATOM   13618 C  CD2 . LEU B 2 136  ? -92.114  48.267  18.036  1.00 159.94 ? 136  LEU X CD2 1 
ATOM   13619 N  N   . PHE B 2 137  ? -93.978  52.708  16.239  1.00 172.06 ? 137  PHE X N   1 
ATOM   13620 C  CA  . PHE B 2 137  ? -93.819  53.911  17.056  1.00 174.01 ? 137  PHE X CA  1 
ATOM   13621 C  C   . PHE B 2 137  ? -94.473  53.763  18.424  1.00 173.80 ? 137  PHE X C   1 
ATOM   13622 O  O   . PHE B 2 137  ? -95.212  52.807  18.675  1.00 172.11 ? 137  PHE X O   1 
ATOM   13623 C  CB  . PHE B 2 137  ? -94.352  55.152  16.337  1.00 177.19 ? 137  PHE X CB  1 
ATOM   13624 C  CG  . PHE B 2 137  ? -93.970  55.222  14.886  1.00 180.74 ? 137  PHE X CG  1 
ATOM   13625 C  CD1 . PHE B 2 137  ? -93.146  54.257  14.316  1.00 179.77 ? 137  PHE X CD1 1 
ATOM   13626 C  CD2 . PHE B 2 137  ? -94.411  56.264  14.097  1.00 182.50 ? 137  PHE X CD2 1 
ATOM   13627 C  CE1 . PHE B 2 137  ? -92.793  54.318  12.992  1.00 181.15 ? 137  PHE X CE1 1 
ATOM   13628 C  CE2 . PHE B 2 137  ? -94.055  56.336  12.771  1.00 184.27 ? 137  PHE X CE2 1 
ATOM   13629 C  CZ  . PHE B 2 137  ? -93.241  55.360  12.216  1.00 183.02 ? 137  PHE X CZ  1 
ATOM   13630 N  N   . VAL B 2 138  ? -94.194  54.712  19.307  1.00 173.20 ? 138  VAL X N   1 
ATOM   13631 C  CA  . VAL B 2 138  ? -94.758  54.678  20.643  1.00 170.69 ? 138  VAL X CA  1 
ATOM   13632 C  C   . VAL B 2 138  ? -94.826  56.086  21.205  1.00 173.99 ? 138  VAL X C   1 
ATOM   13633 O  O   . VAL B 2 138  ? -93.803  56.720  21.471  1.00 175.59 ? 138  VAL X O   1 
ATOM   13634 C  CB  . VAL B 2 138  ? -93.966  53.735  21.572  1.00 167.10 ? 138  VAL X CB  1 
ATOM   13635 C  CG1 . VAL B 2 138  ? -93.836  54.324  22.960  1.00 166.46 ? 138  VAL X CG1 1 
ATOM   13636 C  CG2 . VAL B 2 138  ? -94.632  52.369  21.627  1.00 163.56 ? 138  VAL X CG2 1 
ATOM   13637 N  N   . ASN B 2 139  ? -96.054  56.578  21.341  1.00 173.67 ? 139  ASN X N   1 
ATOM   13638 C  CA  . ASN B 2 139  ? -96.317  57.887  21.917  1.00 174.43 ? 139  ASN X CA  1 
ATOM   13639 C  C   . ASN B 2 139  ? -96.985  57.735  23.283  1.00 174.08 ? 139  ASN X C   1 
ATOM   13640 O  O   . ASN B 2 139  ? -98.040  57.111  23.395  1.00 173.54 ? 139  ASN X O   1 
ATOM   13641 C  CB  . ASN B 2 139  ? -97.217  58.694  20.979  1.00 174.29 ? 139  ASN X CB  1 
ATOM   13642 C  CG  . ASN B 2 139  ? -96.995  58.347  19.520  1.00 175.51 ? 139  ASN X CG  1 
ATOM   13643 O  OD1 . ASN B 2 139  ? -97.788  57.624  18.921  1.00 175.52 ? 139  ASN X OD1 1 
ATOM   13644 N  ND2 . ASN B 2 139  ? -95.906  58.847  18.945  1.00 176.51 ? 139  ASN X ND2 1 
ATOM   13645 N  N   . LYS B 2 140  ? -96.373  58.280  24.328  1.00 175.82 ? 140  LYS X N   1 
ATOM   13646 C  CA  . LYS B 2 140  ? -97.031  58.272  25.625  1.00 175.65 ? 140  LYS X CA  1 
ATOM   13647 C  C   . LYS B 2 140  ? -97.834  59.555  25.791  1.00 176.17 ? 140  LYS X C   1 
ATOM   13648 O  O   . LYS B 2 140  ? -97.305  60.655  25.664  1.00 176.43 ? 140  LYS X O   1 
ATOM   13649 C  CB  . LYS B 2 140  ? -96.020  58.076  26.761  1.00 176.17 ? 140  LYS X CB  1 
ATOM   13650 C  CG  . LYS B 2 140  ? -95.167  56.809  26.616  1.00 174.47 ? 140  LYS X CG  1 
ATOM   13651 C  CD  . LYS B 2 140  ? -94.564  56.342  27.941  1.00 172.87 ? 140  LYS X CD  1 
ATOM   13652 C  CE  . LYS B 2 140  ? -95.524  55.446  28.711  1.00 171.23 ? 140  LYS X CE  1 
ATOM   13653 N  NZ  . LYS B 2 140  ? -94.854  54.846  29.892  1.00 170.59 ? 140  LYS X NZ  1 
ATOM   13654 N  N   . VAL B 2 141  ? -99.128  59.405  26.031  1.00 177.17 ? 141  VAL X N   1 
ATOM   13655 C  CA  . VAL B 2 141  ? -99.971  60.553  26.316  1.00 181.27 ? 141  VAL X CA  1 
ATOM   13656 C  C   . VAL B 2 141  ? -99.894  60.876  27.811  1.00 184.73 ? 141  VAL X C   1 
ATOM   13657 O  O   . VAL B 2 141  ? -99.767  59.983  28.653  1.00 182.53 ? 141  VAL X O   1 
ATOM   13658 C  CB  . VAL B 2 141  ? -101.458 60.296  25.947  1.00 183.14 ? 141  VAL X CB  1 
ATOM   13659 C  CG1 . VAL B 2 141  ? -102.209 61.614  25.784  1.00 185.28 ? 141  VAL X CG1 1 
ATOM   13660 C  CG2 . VAL B 2 141  ? -101.579 59.457  24.688  1.00 182.33 ? 141  VAL X CG2 1 
ATOM   13661 N  N   . ASN B 2 142  ? -99.972  62.160  28.133  1.00 188.79 ? 142  ASN X N   1 
ATOM   13662 C  CA  . ASN B 2 142  ? -100.098 62.607  29.509  1.00 190.23 ? 142  ASN X CA  1 
ATOM   13663 C  C   . ASN B 2 142  ? -100.927 63.870  29.464  1.00 193.54 ? 142  ASN X C   1 
ATOM   13664 O  O   . ASN B 2 142  ? -100.490 64.945  29.876  1.00 195.74 ? 142  ASN X O   1 
ATOM   13665 C  CB  . ASN B 2 142  ? -98.733  62.862  30.141  1.00 189.55 ? 142  ASN X CB  1 
ATOM   13666 C  CG  . ASN B 2 142  ? -98.819  63.059  31.641  1.00 187.88 ? 142  ASN X CG  1 
ATOM   13667 O  OD1 . ASN B 2 142  ? -99.035  64.173  32.126  1.00 188.73 ? 142  ASN X OD1 1 
ATOM   13668 N  ND2 . ASN B 2 142  ? -98.643  61.973  32.388  1.00 185.44 ? 142  ASN X ND2 1 
ATOM   13669 N  N   . GLY B 2 143  ? -102.132 63.719  28.924  1.00 194.02 ? 143  GLY X N   1 
ATOM   13670 C  CA  . GLY B 2 143  ? -103.006 64.840  28.659  1.00 197.57 ? 143  GLY X CA  1 
ATOM   13671 C  C   . GLY B 2 143  ? -102.436 65.706  27.556  1.00 201.20 ? 143  GLY X C   1 
ATOM   13672 O  O   . GLY B 2 143  ? -102.589 65.403  26.372  1.00 201.78 ? 143  GLY X O   1 
ATOM   13673 N  N   . GLU B 2 144  ? -101.769 66.786  27.945  1.00 204.44 ? 144  GLU X N   1 
ATOM   13674 C  CA  . GLU B 2 144  ? -101.161 67.689  26.979  1.00 207.25 ? 144  GLU X CA  1 
ATOM   13675 C  C   . GLU B 2 144  ? -99.757  67.227  26.631  1.00 203.81 ? 144  GLU X C   1 
ATOM   13676 O  O   . GLU B 2 144  ? -99.159  67.699  25.664  1.00 203.97 ? 144  GLU X O   1 
ATOM   13677 C  CB  . GLU B 2 144  ? -101.143 69.120  27.519  1.00 212.84 ? 144  GLU X CB  1 
ATOM   13678 C  CG  . GLU B 2 144  ? -102.507 69.786  27.486  1.00 216.87 ? 144  GLU X CG  1 
ATOM   13679 C  CD  . GLU B 2 144  ? -103.170 69.674  26.120  1.00 219.10 ? 144  GLU X CD  1 
ATOM   13680 O  OE1 . GLU B 2 144  ? -102.438 69.554  25.112  1.00 219.95 ? 144  GLU X OE1 1 
ATOM   13681 O  OE2 . GLU B 2 144  ? -104.419 69.704  26.052  1.00 219.70 ? 144  GLU X OE2 1 
ATOM   13682 N  N   . ASP B 2 145  ? -99.245  66.297  27.433  1.00 199.89 ? 145  ASP X N   1 
ATOM   13683 C  CA  . ASP B 2 145  ? -97.881  65.800  27.281  1.00 196.48 ? 145  ASP X CA  1 
ATOM   13684 C  C   . ASP B 2 145  ? -97.801  64.576  26.351  1.00 190.09 ? 145  ASP X C   1 
ATOM   13685 O  O   . ASP B 2 145  ? -98.760  63.804  26.231  1.00 187.90 ? 145  ASP X O   1 
ATOM   13686 C  CB  . ASP B 2 145  ? -97.256  65.494  28.658  1.00 197.08 ? 145  ASP X CB  1 
ATOM   13687 C  CG  . ASP B 2 145  ? -96.899  66.762  29.456  1.00 200.41 ? 145  ASP X CG  1 
ATOM   13688 O  OD1 . ASP B 2 145  ? -97.027  67.886  28.923  1.00 203.27 ? 145  ASP X OD1 1 
ATOM   13689 O  OD2 . ASP B 2 145  ? -96.481  66.631  30.628  1.00 199.69 ? 145  ASP X OD2 1 
ATOM   13690 N  N   . LEU B 2 146  ? -96.652  64.423  25.688  1.00 186.35 ? 146  LEU X N   1 
ATOM   13691 C  CA  . LEU B 2 146  ? -96.378  63.269  24.828  1.00 181.15 ? 146  LEU X CA  1 
ATOM   13692 C  C   . LEU B 2 146  ? -94.889  62.964  24.761  1.00 178.85 ? 146  LEU X C   1 
ATOM   13693 O  O   . LEU B 2 146  ? -94.112  63.723  24.171  1.00 177.62 ? 146  LEU X O   1 
ATOM   13694 C  CB  . LEU B 2 146  ? -96.869  63.506  23.402  1.00 181.34 ? 146  LEU X CB  1 
ATOM   13695 C  CG  . LEU B 2 146  ? -96.928  62.281  22.476  1.00 178.94 ? 146  LEU X CG  1 
ATOM   13696 C  CD1 . LEU B 2 146  ? -96.438  62.662  21.096  1.00 179.89 ? 146  LEU X CD1 1 
ATOM   13697 C  CD2 . LEU B 2 146  ? -96.132  61.097  22.993  1.00 176.58 ? 146  LEU X CD2 1 
ATOM   13698 N  N   . ASP B 2 147  ? -94.510  61.837  25.357  1.00 178.28 ? 147  ASP X N   1 
ATOM   13699 C  CA  . ASP B 2 147  ? -93.164  61.303  25.222  1.00 177.13 ? 147  ASP X CA  1 
ATOM   13700 C  C   . ASP B 2 147  ? -93.177  60.162  24.216  1.00 180.44 ? 147  ASP X C   1 
ATOM   13701 O  O   . ASP B 2 147  ? -93.533  59.024  24.542  1.00 179.86 ? 147  ASP X O   1 
ATOM   13702 C  CB  . ASP B 2 147  ? -92.616  60.844  26.573  1.00 169.81 ? 147  ASP X CB  1 
ATOM   13703 C  CG  . ASP B 2 147  ? -92.376  62.003  27.531  1.00 164.60 ? 147  ASP X CG  1 
ATOM   13704 O  OD1 . ASP B 2 147  ? -92.083  63.128  27.073  1.00 163.85 ? 147  ASP X OD1 1 
ATOM   13705 O  OD2 . ASP B 2 147  ? -92.484  61.785  28.752  1.00 161.78 ? 147  ASP X OD2 1 
ATOM   13706 N  N   . ALA B 2 148  ? -92.800  60.495  22.986  1.00 183.60 ? 148  ALA X N   1 
ATOM   13707 C  CA  . ALA B 2 148  ? -92.839  59.555  21.875  1.00 184.95 ? 148  ALA X CA  1 
ATOM   13708 C  C   . ALA B 2 148  ? -91.457  59.024  21.501  1.00 186.80 ? 148  ALA X C   1 
ATOM   13709 O  O   . ALA B 2 148  ? -90.433  59.626  21.826  1.00 190.49 ? 148  ALA X O   1 
ATOM   13710 C  CB  . ALA B 2 148  ? -93.508  60.200  20.660  1.00 186.26 ? 148  ALA X CB  1 
ATOM   13711 N  N   . SER B 2 149  ? -91.450  57.901  20.793  1.00 184.02 ? 149  SER X N   1 
ATOM   13712 C  CA  . SER B 2 149  ? -90.222  57.225  20.410  1.00 181.89 ? 149  SER X CA  1 
ATOM   13713 C  C   . SER B 2 149  ? -90.494  56.379  19.168  1.00 174.95 ? 149  SER X C   1 
ATOM   13714 O  O   . SER B 2 149  ? -91.497  55.658  19.118  1.00 172.39 ? 149  SER X O   1 
ATOM   13715 C  CB  . SER B 2 149  ? -89.757  56.316  21.551  1.00 183.69 ? 149  SER X CB  1 
ATOM   13716 O  OG  . SER B 2 149  ? -89.921  56.943  22.814  1.00 185.72 ? 149  SER X OG  1 
ATOM   13717 N  N   . ILE B 2 150  ? -89.628  56.481  18.157  1.00 170.84 ? 150  ILE X N   1 
ATOM   13718 C  CA  . ILE B 2 150  ? -89.700  55.578  17.006  1.00 161.60 ? 150  ILE X CA  1 
ATOM   13719 C  C   . ILE B 2 150  ? -88.920  54.327  17.391  1.00 158.33 ? 150  ILE X C   1 
ATOM   13720 O  O   . ILE B 2 150  ? -87.917  54.421  18.105  1.00 159.05 ? 150  ILE X O   1 
ATOM   13721 C  CB  . ILE B 2 150  ? -89.075  56.188  15.731  1.00 146.39 ? 150  ILE X CB  1 
ATOM   13722 C  CG1 . ILE B 2 150  ? -87.679  55.627  15.513  1.00 141.84 ? 150  ILE X CG1 1 
ATOM   13723 C  CG2 . ILE B 2 150  ? -89.035  57.698  15.800  1.00 152.98 ? 150  ILE X CG2 1 
ATOM   13724 C  CD1 . ILE B 2 150  ? -87.661  54.269  14.865  1.00 129.61 ? 150  ILE X CD1 1 
ATOM   13725 N  N   . ASP B 2 151  ? -89.350  53.158  16.926  1.00 155.31 ? 151  ASP X N   1 
ATOM   13726 C  CA  . ASP B 2 151  ? -88.685  51.937  17.366  1.00 153.92 ? 151  ASP X CA  1 
ATOM   13727 C  C   . ASP B 2 151  ? -88.739  50.836  16.326  1.00 159.69 ? 151  ASP X C   1 
ATOM   13728 O  O   . ASP B 2 151  ? -88.671  51.105  15.130  1.00 159.44 ? 151  ASP X O   1 
ATOM   13729 C  CB  . ASP B 2 151  ? -89.267  51.444  18.702  1.00 147.90 ? 151  ASP X CB  1 
ATOM   13730 C  CG  . ASP B 2 151  ? -88.222  50.759  19.590  1.00 141.90 ? 151  ASP X CG  1 
ATOM   13731 O  OD1 . ASP B 2 151  ? -87.080  50.543  19.124  1.00 141.38 ? 151  ASP X OD1 1 
ATOM   13732 O  OD2 . ASP B 2 151  ? -88.548  50.439  20.755  1.00 138.31 ? 151  ASP X OD2 1 
ATOM   13733 N  N   . SER B 2 152  ? -88.844  49.594  16.794  1.00 167.78 ? 152  SER X N   1 
ATOM   13734 C  CA  . SER B 2 152  ? -88.785  48.428  15.915  1.00 177.09 ? 152  SER X CA  1 
ATOM   13735 C  C   . SER B 2 152  ? -89.339  47.162  16.574  1.00 187.30 ? 152  SER X C   1 
ATOM   13736 O  O   . SER B 2 152  ? -89.309  47.009  17.801  1.00 186.48 ? 152  SER X O   1 
ATOM   13737 C  CB  . SER B 2 152  ? -87.340  48.167  15.451  1.00 177.83 ? 152  SER X CB  1 
ATOM   13738 O  OG  . SER B 2 152  ? -86.860  49.196  14.598  1.00 178.59 ? 152  SER X OG  1 
ATOM   13739 N  N   . PHE B 2 153  ? -89.841  46.261  15.731  1.00 198.03 ? 153  PHE X N   1 
ATOM   13740 C  CA  . PHE B 2 153  ? -90.251  44.919  16.147  1.00 208.39 ? 153  PHE X CA  1 
ATOM   13741 C  C   . PHE B 2 153  ? -89.699  43.848  15.190  1.00 213.69 ? 153  PHE X C   1 
ATOM   13742 O  O   . PHE B 2 153  ? -89.629  44.044  13.974  1.00 213.99 ? 153  PHE X O   1 
ATOM   13743 C  CB  . PHE B 2 153  ? -91.780  44.798  16.244  1.00 215.42 ? 153  PHE X CB  1 
ATOM   13744 C  CG  . PHE B 2 153  ? -92.251  43.436  16.702  1.00 222.25 ? 153  PHE X CG  1 
ATOM   13745 C  CD1 . PHE B 2 153  ? -92.716  43.247  17.993  1.00 223.85 ? 153  PHE X CD1 1 
ATOM   13746 C  CD2 . PHE B 2 153  ? -92.212  42.343  15.843  1.00 226.00 ? 153  PHE X CD2 1 
ATOM   13747 C  CE1 . PHE B 2 153  ? -93.138  42.000  18.416  1.00 225.88 ? 153  PHE X CE1 1 
ATOM   13748 C  CE2 . PHE B 2 153  ? -92.628  41.090  16.261  1.00 227.79 ? 153  PHE X CE2 1 
ATOM   13749 C  CZ  . PHE B 2 153  ? -93.093  40.918  17.548  1.00 227.46 ? 153  PHE X CZ  1 
ATOM   13750 N  N   . LEU B 2 154  ? -89.308  42.710  15.754  1.00 216.05 ? 154  LEU X N   1 
ATOM   13751 C  CA  . LEU B 2 154  ? -88.729  41.631  14.967  1.00 218.18 ? 154  LEU X CA  1 
ATOM   13752 C  C   . LEU B 2 154  ? -89.692  40.461  14.779  1.00 220.29 ? 154  LEU X C   1 
ATOM   13753 O  O   . LEU B 2 154  ? -89.916  39.662  15.692  1.00 219.09 ? 154  LEU X O   1 
ATOM   13754 C  CB  . LEU B 2 154  ? -87.413  41.178  15.603  1.00 216.82 ? 154  LEU X CB  1 
ATOM   13755 C  CG  . LEU B 2 154  ? -86.430  42.342  15.776  1.00 214.42 ? 154  LEU X CG  1 
ATOM   13756 C  CD1 . LEU B 2 154  ? -85.380  42.042  16.826  1.00 213.18 ? 154  LEU X CD1 1 
ATOM   13757 C  CD2 . LEU B 2 154  ? -85.789  42.717  14.445  1.00 214.91 ? 154  LEU X CD2 1 
ATOM   13758 N  N   . ILE B 2 155  ? -90.267  40.380  13.585  1.00 223.23 ? 155  ILE X N   1 
ATOM   13759 C  CA  . ILE B 2 155  ? -91.111  39.256  13.207  1.00 226.66 ? 155  ILE X CA  1 
ATOM   13760 C  C   . ILE B 2 155  ? -90.245  38.130  12.659  1.00 230.74 ? 155  ILE X C   1 
ATOM   13761 O  O   . ILE B 2 155  ? -89.587  38.283  11.629  1.00 231.03 ? 155  ILE X O   1 
ATOM   13762 C  CB  . ILE B 2 155  ? -92.122  39.664  12.132  1.00 224.44 ? 155  ILE X CB  1 
ATOM   13763 C  CG1 . ILE B 2 155  ? -92.654  41.064  12.421  1.00 222.61 ? 155  ILE X CG1 1 
ATOM   13764 C  CG2 . ILE B 2 155  ? -93.251  38.646  12.035  1.00 225.75 ? 155  ILE X CG2 1 
ATOM   13765 C  CD1 . ILE B 2 155  ? -93.669  41.531  11.419  1.00 222.63 ? 155  ILE X CD1 1 
ATOM   13766 N  N   . GLN B 2 156  ? -90.256  36.996  13.349  1.00 235.83 ? 156  GLN X N   1 
ATOM   13767 C  CA  . GLN B 2 156  ? -89.354  35.899  13.025  1.00 242.28 ? 156  GLN X CA  1 
ATOM   13768 C  C   . GLN B 2 156  ? -89.967  34.839  12.110  1.00 247.04 ? 156  GLN X C   1 
ATOM   13769 O  O   . GLN B 2 156  ? -89.487  33.707  12.057  1.00 247.95 ? 156  GLN X O   1 
ATOM   13770 C  CB  . GLN B 2 156  ? -88.827  35.259  14.312  1.00 243.71 ? 156  GLN X CB  1 
ATOM   13771 C  CG  . GLN B 2 156  ? -87.722  34.240  14.087  1.00 245.96 ? 156  GLN X CG  1 
ATOM   13772 C  CD  . GLN B 2 156  ? -86.778  34.647  12.971  1.00 246.65 ? 156  GLN X CD  1 
ATOM   13773 O  OE1 . GLN B 2 156  ? -86.200  35.734  12.997  1.00 245.60 ? 156  GLN X OE1 1 
ATOM   13774 N  NE2 . GLN B 2 156  ? -86.618  33.774  11.983  1.00 247.76 ? 156  GLN X NE2 1 
ATOM   13775 N  N   . LYS B 2 157  ? -91.015  35.203  11.376  1.00 252.02 ? 157  LYS X N   1 
ATOM   13776 C  CA  . LYS B 2 157  ? -91.699  34.231  10.519  1.00 257.18 ? 157  LYS X CA  1 
ATOM   13777 C  C   . LYS B 2 157  ? -92.317  34.828  9.245   1.00 260.42 ? 157  LYS X C   1 
ATOM   13778 O  O   . LYS B 2 157  ? -92.247  36.035  9.006   1.00 260.17 ? 157  LYS X O   1 
ATOM   13779 C  CB  . LYS B 2 157  ? -92.758  33.459  11.320  1.00 258.28 ? 157  LYS X CB  1 
ATOM   13780 C  CG  . LYS B 2 157  ? -92.195  32.575  12.442  1.00 258.77 ? 157  LYS X CG  1 
ATOM   13781 C  CD  . LYS B 2 157  ? -91.333  31.436  11.897  1.00 260.43 ? 157  LYS X CD  1 
ATOM   13782 C  CE  . LYS B 2 157  ? -90.663  30.652  13.017  1.00 260.59 ? 157  LYS X CE  1 
ATOM   13783 N  NZ  . LYS B 2 157  ? -89.791  29.571  12.486  1.00 262.16 ? 157  LYS X NZ  1 
ATOM   13784 N  N   . GLU B 2 158  ? -92.896  33.955  8.424   1.00 263.83 ? 158  GLU X N   1 
ATOM   13785 C  CA  . GLU B 2 158  ? -93.537  34.346  7.173   1.00 266.64 ? 158  GLU X CA  1 
ATOM   13786 C  C   . GLU B 2 158  ? -95.005  34.671  7.414   1.00 265.55 ? 158  GLU X C   1 
ATOM   13787 O  O   . GLU B 2 158  ? -95.518  35.671  6.915   1.00 265.93 ? 158  GLU X O   1 
ATOM   13788 C  CB  . GLU B 2 158  ? -93.399  33.224  6.140   1.00 272.31 ? 158  GLU X CB  1 
ATOM   13789 C  CG  . GLU B 2 158  ? -94.279  33.372  4.909   1.00 277.03 ? 158  GLU X CG  1 
ATOM   13790 C  CD  . GLU B 2 158  ? -93.897  34.558  4.043   1.00 279.95 ? 158  GLU X CD  1 
ATOM   13791 O  OE1 . GLU B 2 158  ? -92.857  35.196  4.314   1.00 279.79 ? 158  GLU X OE1 1 
ATOM   13792 O  OE2 . GLU B 2 158  ? -94.644  34.850  3.085   1.00 282.09 ? 158  GLU X OE2 1 
ATOM   13793 N  N   . GLU B 2 159  ? -95.670  33.814  8.185   1.00 263.21 ? 159  GLU X N   1 
ATOM   13794 C  CA  . GLU B 2 159  ? -97.039  34.061  8.632   1.00 260.13 ? 159  GLU X CA  1 
ATOM   13795 C  C   . GLU B 2 159  ? -97.044  34.049  10.150  1.00 255.03 ? 159  GLU X C   1 
ATOM   13796 O  O   . GLU B 2 159  ? -96.392  33.209  10.773  1.00 254.63 ? 159  GLU X O   1 
ATOM   13797 C  CB  . GLU B 2 159  ? -98.008  32.997  8.101   1.00 262.70 ? 159  GLU X CB  1 
ATOM   13798 C  CG  . GLU B 2 159  ? -99.428  33.092  8.679   1.00 262.76 ? 159  GLU X CG  1 
ATOM   13799 C  CD  . GLU B 2 159  ? -100.331 31.947  8.238   1.00 264.53 ? 159  GLU X CD  1 
ATOM   13800 O  OE1 . GLU B 2 159  ? -101.218 31.548  9.022   1.00 265.07 ? 159  GLU X OE1 1 
ATOM   13801 O  OE2 . GLU B 2 159  ? -100.153 31.442  7.111   1.00 265.66 ? 159  GLU X OE2 1 
ATOM   13802 N  N   . ILE B 2 160  ? -97.781  34.973  10.751  1.00 249.32 ? 160  ILE X N   1 
ATOM   13803 C  CA  . ILE B 2 160  ? -97.709  35.125  12.193  1.00 243.27 ? 160  ILE X CA  1 
ATOM   13804 C  C   . ILE B 2 160  ? -99.077  35.333  12.839  1.00 242.96 ? 160  ILE X C   1 
ATOM   13805 O  O   . ILE B 2 160  ? -99.885  36.146  12.384  1.00 242.99 ? 160  ILE X O   1 
ATOM   13806 C  CB  . ILE B 2 160  ? -96.711  36.243  12.582  1.00 233.71 ? 160  ILE X CB  1 
ATOM   13807 C  CG1 . ILE B 2 160  ? -96.600  36.366  14.100  1.00 229.05 ? 160  ILE X CG1 1 
ATOM   13808 C  CG2 . ILE B 2 160  ? -97.092  37.567  11.928  1.00 232.43 ? 160  ILE X CG2 1 
ATOM   13809 C  CD1 . ILE B 2 160  ? -95.506  37.302  14.539  1.00 226.22 ? 160  ILE X CD1 1 
ATOM   13810 N  N   . SER B 2 161  ? -99.319  34.561  13.895  1.00 243.03 ? 161  SER X N   1 
ATOM   13811 C  CA  . SER B 2 161  ? -100.588 34.568  14.612  1.00 243.21 ? 161  SER X CA  1 
ATOM   13812 C  C   . SER B 2 161  ? -100.774 35.856  15.402  1.00 241.84 ? 161  SER X C   1 
ATOM   13813 O  O   . SER B 2 161  ? -99.853  36.312  16.080  1.00 240.89 ? 161  SER X O   1 
ATOM   13814 C  CB  . SER B 2 161  ? -100.662 33.368  15.559  1.00 242.92 ? 161  SER X CB  1 
ATOM   13815 O  OG  . SER B 2 161  ? -99.522  33.307  16.402  1.00 241.07 ? 161  SER X OG  1 
ATOM   13816 N  N   . LEU B 2 162  ? -101.973 36.429  15.318  1.00 243.02 ? 162  LEU X N   1 
ATOM   13817 C  CA  . LEU B 2 162  ? -102.286 37.672  16.023  1.00 241.74 ? 162  LEU X CA  1 
ATOM   13818 C  C   . LEU B 2 162  ? -102.160 37.519  17.542  1.00 240.28 ? 162  LEU X C   1 
ATOM   13819 O  O   . LEU B 2 162  ? -101.942 38.496  18.257  1.00 237.86 ? 162  LEU X O   1 
ATOM   13820 C  CB  . LEU B 2 162  ? -103.686 38.174  15.641  1.00 243.40 ? 162  LEU X CB  1 
ATOM   13821 C  CG  . LEU B 2 162  ? -104.099 39.573  16.114  1.00 243.11 ? 162  LEU X CG  1 
ATOM   13822 C  CD1 . LEU B 2 162  ? -103.076 40.615  15.692  1.00 241.79 ? 162  LEU X CD1 1 
ATOM   13823 C  CD2 . LEU B 2 162  ? -105.484 39.935  15.590  1.00 244.77 ? 162  LEU X CD2 1 
ATOM   13824 N  N   . LYS B 2 163  ? -102.302 36.292  18.033  1.00 240.94 ? 163  LYS X N   1 
ATOM   13825 C  CA  . LYS B 2 163  ? -102.052 36.026  19.439  1.00 239.91 ? 163  LYS X CA  1 
ATOM   13826 C  C   . LYS B 2 163  ? -100.592 36.302  19.725  1.00 239.58 ? 163  LYS X C   1 
ATOM   13827 O  O   . LYS B 2 163  ? -100.261 37.120  20.579  1.00 240.27 ? 163  LYS X O   1 
ATOM   13828 C  CB  . LYS B 2 163  ? -102.354 34.573  19.779  1.00 239.72 ? 163  LYS X CB  1 
ATOM   13829 C  CG  . LYS B 2 163  ? -101.754 34.129  21.103  1.00 237.12 ? 163  LYS X CG  1 
ATOM   13830 C  CD  . LYS B 2 163  ? -101.477 32.637  21.102  1.00 236.75 ? 163  LYS X CD  1 
ATOM   13831 C  CE  . LYS B 2 163  ? -101.054 32.155  22.474  1.00 234.86 ? 163  LYS X CE  1 
ATOM   13832 N  NZ  . LYS B 2 163  ? -102.128 32.380  23.473  1.00 234.50 ? 163  LYS X NZ  1 
ATOM   13833 N  N   . GLU B 2 164  ? -99.720  35.612  18.995  1.00 239.63 ? 164  GLU X N   1 
ATOM   13834 C  CA  . GLU B 2 164  ? -98.280  35.778  19.148  1.00 239.11 ? 164  GLU X CA  1 
ATOM   13835 C  C   . GLU B 2 164  ? -97.847  37.197  18.805  1.00 231.44 ? 164  GLU X C   1 
ATOM   13836 O  O   . GLU B 2 164  ? -96.900  37.723  19.389  1.00 227.75 ? 164  GLU X O   1 
ATOM   13837 C  CB  . GLU B 2 164  ? -97.526  34.788  18.260  1.00 247.41 ? 164  GLU X CB  1 
ATOM   13838 C  CG  . GLU B 2 164  ? -96.020  34.963  18.306  1.00 253.21 ? 164  GLU X CG  1 
ATOM   13839 C  CD  . GLU B 2 164  ? -95.315  34.215  17.197  1.00 259.70 ? 164  GLU X CD  1 
ATOM   13840 O  OE1 . GLU B 2 164  ? -96.004  33.527  16.409  1.00 263.06 ? 164  GLU X OE1 1 
ATOM   13841 O  OE2 . GLU B 2 164  ? -94.072  34.320  17.113  1.00 260.94 ? 164  GLU X OE2 1 
ATOM   13842 N  N   . LEU B 2 165  ? -98.538  37.805  17.847  1.00 228.47 ? 165  LEU X N   1 
ATOM   13843 C  CA  . LEU B 2 165  ? -98.269  39.182  17.467  1.00 223.35 ? 165  LEU X CA  1 
ATOM   13844 C  C   . LEU B 2 165  ? -98.562  40.092  18.654  1.00 222.81 ? 165  LEU X C   1 
ATOM   13845 O  O   . LEU B 2 165  ? -97.818  41.026  18.941  1.00 221.64 ? 165  LEU X O   1 
ATOM   13846 C  CB  . LEU B 2 165  ? -99.141  39.581  16.273  1.00 219.27 ? 165  LEU X CB  1 
ATOM   13847 C  CG  . LEU B 2 165  ? -98.664  40.707  15.348  1.00 213.40 ? 165  LEU X CG  1 
ATOM   13848 C  CD1 . LEU B 2 165  ? -97.598  40.197  14.390  1.00 211.66 ? 165  LEU X CD1 1 
ATOM   13849 C  CD2 . LEU B 2 165  ? -99.820  41.303  14.562  1.00 211.73 ? 165  LEU X CD2 1 
ATOM   13850 N  N   . ASP B 2 166  ? -99.653  39.796  19.351  1.00 223.05 ? 166  ASP X N   1 
ATOM   13851 C  CA  . ASP B 2 166  ? -100.116 40.621  20.459  1.00 223.52 ? 166  ASP X CA  1 
ATOM   13852 C  C   . ASP B 2 166  ? -99.310  40.384  21.732  1.00 224.16 ? 166  ASP X C   1 
ATOM   13853 O  O   . ASP B 2 166  ? -99.129  41.294  22.538  1.00 222.92 ? 166  ASP X O   1 
ATOM   13854 C  CB  . ASP B 2 166  ? -101.597 40.352  20.725  1.00 225.68 ? 166  ASP X CB  1 
ATOM   13855 C  CG  . ASP B 2 166  ? -102.295 41.532  21.358  1.00 227.57 ? 166  ASP X CG  1 
ATOM   13856 O  OD1 . ASP B 2 166  ? -101.651 42.592  21.494  1.00 228.20 ? 166  ASP X OD1 1 
ATOM   13857 O  OD2 . ASP B 2 166  ? -103.487 41.406  21.711  1.00 229.33 ? 166  ASP X OD2 1 
ATOM   13858 N  N   . PHE B 2 167  ? -98.833  39.156  21.906  1.00 227.41 ? 167  PHE X N   1 
ATOM   13859 C  CA  . PHE B 2 167  ? -98.041  38.780  23.080  1.00 230.23 ? 167  PHE X CA  1 
ATOM   13860 C  C   . PHE B 2 167  ? -96.671  39.472  23.102  1.00 226.04 ? 167  PHE X C   1 
ATOM   13861 O  O   . PHE B 2 167  ? -96.228  39.940  24.155  1.00 227.07 ? 167  PHE X O   1 
ATOM   13862 C  CB  . PHE B 2 167  ? -97.871  37.252  23.150  1.00 236.24 ? 167  PHE X CB  1 
ATOM   13863 C  CG  . PHE B 2 167  ? -97.227  36.757  24.425  1.00 240.28 ? 167  PHE X CG  1 
ATOM   13864 C  CD1 . PHE B 2 167  ? -95.870  36.475  24.471  1.00 241.40 ? 167  PHE X CD1 1 
ATOM   13865 C  CD2 . PHE B 2 167  ? -97.981  36.559  25.570  1.00 242.14 ? 167  PHE X CD2 1 
ATOM   13866 C  CE1 . PHE B 2 167  ? -95.276  36.015  25.638  1.00 242.34 ? 167  PHE X CE1 1 
ATOM   13867 C  CE2 . PHE B 2 167  ? -97.392  36.099  26.738  1.00 243.14 ? 167  PHE X CE2 1 
ATOM   13868 C  CZ  . PHE B 2 167  ? -96.039  35.827  26.771  1.00 242.97 ? 167  PHE X CZ  1 
ATOM   13869 N  N   . LYS B 2 168  ? -96.005  39.532  21.946  1.00 220.41 ? 168  LYS X N   1 
ATOM   13870 C  CA  . LYS B 2 168  ? -94.692  40.181  21.836  1.00 212.93 ? 168  LYS X CA  1 
ATOM   13871 C  C   . LYS B 2 168  ? -94.803  41.718  21.736  1.00 207.96 ? 168  LYS X C   1 
ATOM   13872 O  O   . LYS B 2 168  ? -93.909  42.437  22.201  1.00 205.80 ? 168  LYS X O   1 
ATOM   13873 C  CB  . LYS B 2 168  ? -93.877  39.589  20.666  1.00 211.68 ? 168  LYS X CB  1 
ATOM   13874 C  CG  . LYS B 2 168  ? -93.453  38.116  20.855  1.00 210.31 ? 168  LYS X CG  1 
ATOM   13875 C  CD  . LYS B 2 168  ? -92.731  37.537  19.631  1.00 209.21 ? 168  LYS X CD  1 
ATOM   13876 C  CE  . LYS B 2 168  ? -92.200  36.139  19.918  1.00 208.79 ? 168  LYS X CE  1 
ATOM   13877 N  NZ  . LYS B 2 168  ? -91.361  35.613  18.812  1.00 209.14 ? 168  LYS X NZ  1 
ATOM   13878 N  N   . ILE B 2 169  ? -95.903  42.201  21.142  1.00 204.54 ? 169  ILE X N   1 
ATOM   13879 C  CA  . ILE B 2 169  ? -96.225  43.635  21.068  1.00 199.49 ? 169  ILE X CA  1 
ATOM   13880 C  C   . ILE B 2 169  ? -96.467  44.254  22.444  1.00 199.62 ? 169  ILE X C   1 
ATOM   13881 O  O   . ILE B 2 169  ? -96.254  45.451  22.649  1.00 200.39 ? 169  ILE X O   1 
ATOM   13882 C  CB  . ILE B 2 169  ? -97.486  43.902  20.214  1.00 192.79 ? 169  ILE X CB  1 
ATOM   13883 C  CG1 . ILE B 2 169  ? -97.178  43.765  18.721  1.00 189.26 ? 169  ILE X CG1 1 
ATOM   13884 C  CG2 . ILE B 2 169  ? -98.044  45.286  20.509  1.00 191.18 ? 169  ILE X CG2 1 
ATOM   13885 C  CD1 . ILE B 2 169  ? -95.891  44.413  18.303  1.00 186.24 ? 169  ILE X CD1 1 
ATOM   13886 N  N   . ARG B 2 170  ? -96.931  43.432  23.378  1.00 199.33 ? 170  ARG X N   1 
ATOM   13887 C  CA  . ARG B 2 170  ? -97.160  43.881  24.744  1.00 200.28 ? 170  ARG X CA  1 
ATOM   13888 C  C   . ARG B 2 170  ? -96.020  43.488  25.708  1.00 197.45 ? 170  ARG X C   1 
ATOM   13889 O  O   . ARG B 2 170  ? -95.728  44.214  26.659  1.00 196.26 ? 170  ARG X O   1 
ATOM   13890 C  CB  . ARG B 2 170  ? -98.519  43.386  25.250  1.00 205.15 ? 170  ARG X CB  1 
ATOM   13891 C  CG  . ARG B 2 170  ? -99.716  43.803  24.383  1.00 211.26 ? 170  ARG X CG  1 
ATOM   13892 C  CD  . ARG B 2 170  ? -100.996 43.897  25.225  1.00 216.90 ? 170  ARG X CD  1 
ATOM   13893 N  NE  . ARG B 2 170  ? -102.221 43.650  24.460  1.00 221.69 ? 170  ARG X NE  1 
ATOM   13894 C  CZ  . ARG B 2 170  ? -103.449 43.699  24.974  1.00 224.29 ? 170  ARG X CZ  1 
ATOM   13895 N  NH1 . ARG B 2 170  ? -103.619 43.993  26.258  1.00 225.09 ? 170  ARG X NH1 1 
ATOM   13896 N  NH2 . ARG B 2 170  ? -104.509 43.458  24.210  1.00 225.10 ? 170  ARG X NH2 1 
ATOM   13897 N  N   . GLN B 2 171  ? -95.380  42.346  25.459  1.00 197.08 ? 171  GLN X N   1 
ATOM   13898 C  CA  . GLN B 2 171  ? -94.212  41.929  26.235  1.00 195.92 ? 171  GLN X CA  1 
ATOM   13899 C  C   . GLN B 2 171  ? -93.159  43.025  26.184  1.00 194.65 ? 171  GLN X C   1 
ATOM   13900 O  O   . GLN B 2 171  ? -92.489  43.314  27.183  1.00 193.15 ? 171  GLN X O   1 
ATOM   13901 C  CB  . GLN B 2 171  ? -93.612  40.646  25.656  1.00 194.96 ? 171  GLN X CB  1 
ATOM   13902 C  CG  . GLN B 2 171  ? -92.343  40.174  26.353  1.00 193.01 ? 171  GLN X CG  1 
ATOM   13903 C  CD  . GLN B 2 171  ? -91.436  39.370  25.438  1.00 190.99 ? 171  GLN X CD  1 
ATOM   13904 O  OE1 . GLN B 2 171  ? -91.247  39.723  24.274  1.00 190.09 ? 171  GLN X OE1 1 
ATOM   13905 N  NE2 . GLN B 2 171  ? -90.863  38.290  25.963  1.00 190.15 ? 171  GLN X NE2 1 
ATOM   13906 N  N   . GLN B 2 172  ? -93.027  43.624  25.000  1.00 195.15 ? 172  GLN X N   1 
ATOM   13907 C  CA  . GLN B 2 172  ? -92.066  44.696  24.747  1.00 193.44 ? 172  GLN X CA  1 
ATOM   13908 C  C   . GLN B 2 172  ? -92.416  46.010  25.453  1.00 195.64 ? 172  GLN X C   1 
ATOM   13909 O  O   . GLN B 2 172  ? -91.545  46.660  26.040  1.00 195.93 ? 172  GLN X O   1 
ATOM   13910 C  CB  . GLN B 2 172  ? -91.925  44.929  23.244  1.00 188.59 ? 172  GLN X CB  1 
ATOM   13911 C  CG  . GLN B 2 172  ? -91.141  43.853  22.537  1.00 183.75 ? 172  GLN X CG  1 
ATOM   13912 C  CD  . GLN B 2 172  ? -90.248  44.424  21.467  1.00 180.24 ? 172  GLN X CD  1 
ATOM   13913 O  OE1 . GLN B 2 172  ? -90.678  45.231  20.644  1.00 179.47 ? 172  GLN X OE1 1 
ATOM   13914 N  NE2 . GLN B 2 172  ? -88.989  44.022  21.480  1.00 179.00 ? 172  GLN X NE2 1 
ATOM   13915 N  N   . LEU B 2 173  ? -93.688  46.397  25.386  1.00 196.61 ? 173  LEU X N   1 
ATOM   13916 C  CA  . LEU B 2 173  ? -94.171  47.583  26.085  1.00 197.61 ? 173  LEU X CA  1 
ATOM   13917 C  C   . LEU B 2 173  ? -94.014  47.436  27.605  1.00 198.53 ? 173  LEU X C   1 
ATOM   13918 O  O   . LEU B 2 173  ? -93.682  48.403  28.299  1.00 199.74 ? 173  LEU X O   1 
ATOM   13919 C  CB  . LEU B 2 173  ? -95.634  47.849  25.727  1.00 198.03 ? 173  LEU X CB  1 
ATOM   13920 C  CG  . LEU B 2 173  ? -95.961  48.091  24.252  1.00 199.13 ? 173  LEU X CG  1 
ATOM   13921 C  CD1 . LEU B 2 173  ? -97.466  48.068  24.000  1.00 200.36 ? 173  LEU X CD1 1 
ATOM   13922 C  CD2 . LEU B 2 173  ? -95.360  49.404  23.785  1.00 199.83 ? 173  LEU X CD2 1 
ATOM   13923 N  N   . VAL B 2 174  ? -94.251  46.220  28.106  1.00 198.33 ? 174  VAL X N   1 
ATOM   13924 C  CA  . VAL B 2 174  ? -94.153  45.905  29.536  1.00 196.79 ? 174  VAL X CA  1 
ATOM   13925 C  C   . VAL B 2 174  ? -92.737  46.060  30.083  1.00 196.72 ? 174  VAL X C   1 
ATOM   13926 O  O   . VAL B 2 174  ? -92.547  46.398  31.252  1.00 196.14 ? 174  VAL X O   1 
ATOM   13927 C  CB  . VAL B 2 174  ? -94.603  44.451  29.835  1.00 203.49 ? 174  VAL X CB  1 
ATOM   13928 C  CG1 . VAL B 2 174  ? -94.344  44.103  31.293  1.00 204.18 ? 174  VAL X CG1 1 
ATOM   13929 C  CG2 . VAL B 2 174  ? -96.067  44.256  29.503  1.00 203.29 ? 174  VAL X CG2 1 
ATOM   13930 N  N   . ASN B 2 175  ? -91.750  45.799  29.232  1.00 193.99 ? 175  ASN X N   1 
ATOM   13931 C  CA  . ASN B 2 175  ? -90.358  45.754  29.657  1.00 191.93 ? 175  ASN X CA  1 
ATOM   13932 C  C   . ASN B 2 175  ? -89.520  46.942  29.214  1.00 188.82 ? 175  ASN X C   1 
ATOM   13933 O  O   . ASN B 2 175  ? -88.357  47.072  29.617  1.00 188.99 ? 175  ASN X O   1 
ATOM   13934 C  CB  . ASN B 2 175  ? -89.719  44.471  29.149  1.00 191.45 ? 175  ASN X CB  1 
ATOM   13935 C  CG  . ASN B 2 175  ? -90.579  43.271  29.409  1.00 190.02 ? 175  ASN X CG  1 
ATOM   13936 O  OD1 . ASN B 2 175  ? -90.479  42.262  28.719  1.00 189.99 ? 175  ASN X OD1 1 
ATOM   13937 N  ND2 . ASN B 2 175  ? -91.446  43.377  30.406  1.00 189.04 ? 175  ASN X ND2 1 
ATOM   13938 N  N   . ASN B 2 176  ? -90.102  47.804  28.385  1.00 184.61 ? 176  ASN X N   1 
ATOM   13939 C  CA  . ASN B 2 176  ? -89.338  48.904  27.813  1.00 181.72 ? 176  ASN X CA  1 
ATOM   13940 C  C   . ASN B 2 176  ? -90.077  50.243  27.692  1.00 177.02 ? 176  ASN X C   1 
ATOM   13941 O  O   . ASN B 2 176  ? -89.454  51.274  27.438  1.00 176.57 ? 176  ASN X O   1 
ATOM   13942 C  CB  . ASN B 2 176  ? -88.741  48.492  26.460  1.00 182.16 ? 176  ASN X CB  1 
ATOM   13943 C  CG  . ASN B 2 176  ? -87.850  47.252  26.557  1.00 182.06 ? 176  ASN X CG  1 
ATOM   13944 O  OD1 . ASN B 2 176  ? -86.619  47.346  26.502  1.00 182.45 ? 176  ASN X OD1 1 
ATOM   13945 N  ND2 . ASN B 2 176  ? -88.472  46.087  26.698  1.00 181.46 ? 176  ASN X ND2 1 
ATOM   13946 N  N   . TYR B 2 177  ? -91.391  50.243  27.894  1.00 175.12 ? 177  TYR X N   1 
ATOM   13947 C  CA  . TYR B 2 177  ? -92.148  51.493  27.800  1.00 174.31 ? 177  TYR X CA  1 
ATOM   13948 C  C   . TYR B 2 177  ? -93.023  51.772  29.009  1.00 178.62 ? 177  TYR X C   1 
ATOM   13949 O  O   . TYR B 2 177  ? -93.940  52.591  28.947  1.00 180.83 ? 177  TYR X O   1 
ATOM   13950 C  CB  . TYR B 2 177  ? -92.954  51.553  26.499  1.00 168.33 ? 177  TYR X CB  1 
ATOM   13951 C  CG  . TYR B 2 177  ? -92.041  51.694  25.314  1.00 163.53 ? 177  TYR X CG  1 
ATOM   13952 C  CD1 . TYR B 2 177  ? -91.554  50.571  24.652  1.00 161.03 ? 177  TYR X CD1 1 
ATOM   13953 C  CD2 . TYR B 2 177  ? -91.609  52.944  24.893  1.00 161.64 ? 177  TYR X CD2 1 
ATOM   13954 C  CE1 . TYR B 2 177  ? -90.682  50.688  23.578  1.00 159.13 ? 177  TYR X CE1 1 
ATOM   13955 C  CE2 . TYR B 2 177  ? -90.741  53.075  23.820  1.00 160.30 ? 177  TYR X CE2 1 
ATOM   13956 C  CZ  . TYR B 2 177  ? -90.280  51.941  23.167  1.00 158.38 ? 177  TYR X CZ  1 
ATOM   13957 O  OH  . TYR B 2 177  ? -89.416  52.051  22.105  1.00 156.70 ? 177  TYR X OH  1 
ATOM   13958 N  N   . GLY B 2 178  ? -92.718  51.095  30.110  1.00 181.71 ? 178  GLY X N   1 
ATOM   13959 C  CA  . GLY B 2 178  ? -93.442  51.286  31.352  1.00 185.82 ? 178  GLY X CA  1 
ATOM   13960 C  C   . GLY B 2 178  ? -94.903  50.885  31.275  1.00 190.91 ? 178  GLY X C   1 
ATOM   13961 O  O   . GLY B 2 178  ? -95.769  51.596  31.782  1.00 190.17 ? 178  GLY X O   1 
ATOM   13962 N  N   . LEU B 2 179  ? -95.180  49.752  30.636  1.00 196.06 ? 179  LEU X N   1 
ATOM   13963 C  CA  . LEU B 2 179  ? -96.549  49.266  30.527  1.00 202.58 ? 179  LEU X CA  1 
ATOM   13964 C  C   . LEU B 2 179  ? -96.944  48.391  31.710  1.00 208.81 ? 179  LEU X C   1 
ATOM   13965 O  O   . LEU B 2 179  ? -96.126  47.637  32.240  1.00 208.44 ? 179  LEU X O   1 
ATOM   13966 C  CB  . LEU B 2 179  ? -96.761  48.505  29.216  1.00 201.78 ? 179  LEU X CB  1 
ATOM   13967 C  CG  . LEU B 2 179  ? -98.204  48.055  28.934  1.00 200.49 ? 179  LEU X CG  1 
ATOM   13968 C  CD1 . LEU B 2 179  ? -99.163  49.243  28.950  1.00 201.03 ? 179  LEU X CD1 1 
ATOM   13969 C  CD2 . LEU B 2 179  ? -98.311  47.291  27.617  1.00 199.23 ? 179  LEU X CD2 1 
ATOM   13970 N  N   . TYR B 2 180  ? -98.211  48.502  32.105  1.00 216.28 ? 180  TYR X N   1 
ATOM   13971 C  CA  . TYR B 2 180  ? -98.775  47.737  33.219  1.00 223.22 ? 180  TYR X CA  1 
ATOM   13972 C  C   . TYR B 2 180  ? -98.057  47.980  34.545  1.00 229.02 ? 180  TYR X C   1 
ATOM   13973 O  O   . TYR B 2 180  ? -97.892  47.064  35.349  1.00 230.56 ? 180  TYR X O   1 
ATOM   13974 C  CB  . TYR B 2 180  ? -98.833  46.243  32.887  1.00 224.21 ? 180  TYR X CB  1 
ATOM   13975 C  CG  . TYR B 2 180  ? -99.786  45.929  31.758  1.00 226.03 ? 180  TYR X CG  1 
ATOM   13976 C  CD1 . TYR B 2 180  ? -100.992 46.613  31.632  1.00 227.08 ? 180  TYR X CD1 1 
ATOM   13977 C  CD2 . TYR B 2 180  ? -99.489  44.947  30.824  1.00 226.27 ? 180  TYR X CD2 1 
ATOM   13978 C  CE1 . TYR B 2 180  ? -101.869 46.335  30.601  1.00 227.46 ? 180  TYR X CE1 1 
ATOM   13979 C  CE2 . TYR B 2 180  ? -100.362 44.656  29.790  1.00 226.63 ? 180  TYR X CE2 1 
ATOM   13980 C  CZ  . TYR B 2 180  ? -101.549 45.353  29.683  1.00 226.88 ? 180  TYR X CZ  1 
ATOM   13981 O  OH  . TYR B 2 180  ? -102.418 45.065  28.655  1.00 226.79 ? 180  TYR X OH  1 
ATOM   13982 N  N   . LYS B 2 181  ? -97.651  49.226  34.771  1.00 233.08 ? 181  LYS X N   1 
ATOM   13983 C  CA  . LYS B 2 181  ? -96.920  49.604  35.975  1.00 236.71 ? 181  LYS X CA  1 
ATOM   13984 C  C   . LYS B 2 181  ? -97.260  51.046  36.349  1.00 236.90 ? 181  LYS X C   1 
ATOM   13985 O  O   . LYS B 2 181  ? -96.599  51.986  35.901  1.00 236.55 ? 181  LYS X O   1 
ATOM   13986 C  CB  . LYS B 2 181  ? -95.413  49.455  35.739  1.00 241.00 ? 181  LYS X CB  1 
ATOM   13987 C  CG  . LYS B 2 181  ? -94.544  49.761  36.948  1.00 245.61 ? 181  LYS X CG  1 
ATOM   13988 C  CD  . LYS B 2 181  ? -93.072  49.530  36.640  1.00 248.48 ? 181  LYS X CD  1 
ATOM   13989 C  CE  . LYS B 2 181  ? -92.218  49.692  37.885  1.00 250.39 ? 181  LYS X CE  1 
ATOM   13990 N  NZ  . LYS B 2 181  ? -90.786  49.427  37.596  1.00 250.95 ? 181  LYS X NZ  1 
ATOM   13991 N  N   . GLY B 2 182  ? -98.289  51.214  37.177  1.00 236.61 ? 182  GLY X N   1 
ATOM   13992 C  CA  . GLY B 2 182  ? -98.791  52.534  37.518  1.00 236.06 ? 182  GLY X CA  1 
ATOM   13993 C  C   . GLY B 2 182  ? -99.964  52.958  36.651  1.00 233.40 ? 182  GLY X C   1 
ATOM   13994 O  O   . GLY B 2 182  ? -100.868 52.171  36.381  1.00 231.77 ? 182  GLY X O   1 
ATOM   13995 N  N   . THR B 2 183  ? -99.962  54.215  36.222  1.00 233.62 ? 183  THR X N   1 
ATOM   13996 C  CA  . THR B 2 183  ? -101.034 54.713  35.371  1.00 233.81 ? 183  THR X CA  1 
ATOM   13997 C  C   . THR B 2 183  ? -100.991 54.108  33.965  1.00 236.28 ? 183  THR X C   1 
ATOM   13998 O  O   . THR B 2 183  ? -101.801 54.474  33.115  1.00 237.54 ? 183  THR X O   1 
ATOM   13999 C  CB  . THR B 2 183  ? -101.036 56.261  35.273  1.00 226.78 ? 183  THR X CB  1 
ATOM   14000 O  OG1 . THR B 2 183  ? -99.691  56.750  35.322  1.00 226.05 ? 183  THR X OG1 1 
ATOM   14001 C  CG2 . THR B 2 183  ? -101.835 56.874  36.415  1.00 227.55 ? 183  THR X CG2 1 
ATOM   14002 N  N   . SER B 2 184  ? -100.052 53.190  33.717  1.00 236.79 ? 184  SER X N   1 
ATOM   14003 C  CA  . SER B 2 184  ? -99.911  52.561  32.393  1.00 238.12 ? 184  SER X CA  1 
ATOM   14004 C  C   . SER B 2 184  ? -100.741 51.279  32.233  1.00 239.51 ? 184  SER X C   1 
ATOM   14005 O  O   . SER B 2 184  ? -100.425 50.253  32.836  1.00 238.99 ? 184  SER X O   1 
ATOM   14006 C  CB  . SER B 2 184  ? -98.437  52.264  32.083  1.00 237.41 ? 184  SER X CB  1 
ATOM   14007 O  OG  . SER B 2 184  ? -97.683  53.451  31.893  1.00 237.87 ? 184  SER X OG  1 
ATOM   14008 N  N   . LYS B 2 185  ? -101.784 51.335  31.403  1.00 241.07 ? 185  LYS X N   1 
ATOM   14009 C  CA  . LYS B 2 185  ? -102.688 50.195  31.225  1.00 241.92 ? 185  LYS X CA  1 
ATOM   14010 C  C   . LYS B 2 185  ? -103.738 50.368  30.115  1.00 238.61 ? 185  LYS X C   1 
ATOM   14011 O  O   . LYS B 2 185  ? -104.292 49.379  29.638  1.00 238.65 ? 185  LYS X O   1 
ATOM   14012 C  CB  . LYS B 2 185  ? -103.397 49.859  32.541  1.00 246.03 ? 185  LYS X CB  1 
ATOM   14013 C  CG  . LYS B 2 185  ? -104.627 50.714  32.818  1.00 249.99 ? 185  LYS X CG  1 
ATOM   14014 C  CD  . LYS B 2 185  ? -105.273 50.355  34.149  1.00 252.31 ? 185  LYS X CD  1 
ATOM   14015 C  CE  . LYS B 2 185  ? -104.520 50.965  35.319  1.00 253.55 ? 185  LYS X CE  1 
ATOM   14016 N  NZ  . LYS B 2 185  ? -105.029 50.463  36.624  1.00 254.69 ? 185  LYS X NZ  1 
ATOM   14017 N  N   . TYR B 2 186  ? -104.028 51.610  29.722  1.00 235.38 ? 186  TYR X N   1 
ATOM   14018 C  CA  . TYR B 2 186  ? -104.976 51.875  28.630  1.00 232.61 ? 186  TYR X CA  1 
ATOM   14019 C  C   . TYR B 2 186  ? -104.302 52.342  27.335  1.00 228.90 ? 186  TYR X C   1 
ATOM   14020 O  O   . TYR B 2 186  ? -103.386 53.164  27.371  1.00 227.76 ? 186  TYR X O   1 
ATOM   14021 C  CB  . TYR B 2 186  ? -106.007 52.920  29.048  1.00 233.20 ? 186  TYR X CB  1 
ATOM   14022 C  CG  . TYR B 2 186  ? -106.642 52.649  30.378  1.00 232.81 ? 186  TYR X CG  1 
ATOM   14023 C  CD1 . TYR B 2 186  ? -106.578 53.582  31.395  1.00 233.39 ? 186  TYR X CD1 1 
ATOM   14024 C  CD2 . TYR B 2 186  ? -107.302 51.456  30.621  1.00 232.99 ? 186  TYR X CD2 1 
ATOM   14025 C  CE1 . TYR B 2 186  ? -107.158 53.342  32.617  1.00 233.77 ? 186  TYR X CE1 1 
ATOM   14026 C  CE2 . TYR B 2 186  ? -107.885 51.203  31.841  1.00 233.43 ? 186  TYR X CE2 1 
ATOM   14027 C  CZ  . TYR B 2 186  ? -107.810 52.151  32.838  1.00 233.87 ? 186  TYR X CZ  1 
ATOM   14028 O  OH  . TYR B 2 186  ? -108.387 51.912  34.066  1.00 234.14 ? 186  TYR X OH  1 
ATOM   14029 N  N   . GLY B 2 187  ? -104.771 51.839  26.193  1.00 227.15 ? 187  GLY X N   1 
ATOM   14030 C  CA  . GLY B 2 187  ? -104.221 52.245  24.909  1.00 224.17 ? 187  GLY X CA  1 
ATOM   14031 C  C   . GLY B 2 187  ? -104.687 51.410  23.733  1.00 221.30 ? 187  GLY X C   1 
ATOM   14032 O  O   . GLY B 2 187  ? -105.473 50.481  23.894  1.00 220.39 ? 187  GLY X O   1 
ATOM   14033 N  N   . LYS B 2 188  ? -104.178 51.733  22.548  1.00 219.18 ? 188  LYS X N   1 
ATOM   14034 C  CA  . LYS B 2 188  ? -104.631 51.093  21.317  1.00 220.13 ? 188  LYS X CA  1 
ATOM   14035 C  C   . LYS B 2 188  ? -103.492 50.884  20.309  1.00 218.71 ? 188  LYS X C   1 
ATOM   14036 O  O   . LYS B 2 188  ? -102.859 51.847  19.871  1.00 220.37 ? 188  LYS X O   1 
ATOM   14037 C  CB  . LYS B 2 188  ? -105.731 51.943  20.673  1.00 221.80 ? 188  LYS X CB  1 
ATOM   14038 C  CG  . LYS B 2 188  ? -107.052 51.974  21.435  1.00 222.92 ? 188  LYS X CG  1 
ATOM   14039 C  CD  . LYS B 2 188  ? -107.921 50.776  21.083  1.00 223.25 ? 188  LYS X CD  1 
ATOM   14040 C  CE  . LYS B 2 188  ? -109.328 50.929  21.628  1.00 223.48 ? 188  LYS X CE  1 
ATOM   14041 N  NZ  . LYS B 2 188  ? -109.331 51.035  23.106  1.00 222.20 ? 188  LYS X NZ  1 
ATOM   14042 N  N   . ILE B 2 189  ? -103.242 49.628  19.935  1.00 216.91 ? 189  ILE X N   1 
ATOM   14043 C  CA  . ILE B 2 189  ? -102.196 49.301  18.963  1.00 214.95 ? 189  ILE X CA  1 
ATOM   14044 C  C   . ILE B 2 189  ? -102.728 49.306  17.535  1.00 215.74 ? 189  ILE X C   1 
ATOM   14045 O  O   . ILE B 2 189  ? -103.497 48.423  17.160  1.00 216.46 ? 189  ILE X O   1 
ATOM   14046 C  CB  . ILE B 2 189  ? -101.618 47.896  19.205  1.00 212.59 ? 189  ILE X CB  1 
ATOM   14047 C  CG1 . ILE B 2 189  ? -101.542 47.580  20.699  1.00 211.14 ? 189  ILE X CG1 1 
ATOM   14048 C  CG2 . ILE B 2 189  ? -100.260 47.760  18.536  1.00 212.13 ? 189  ILE X CG2 1 
ATOM   14049 C  CD1 . ILE B 2 189  ? -101.197 46.134  20.993  1.00 210.28 ? 189  ILE X CD1 1 
ATOM   14050 N  N   . ILE B 2 190  ? -102.312 50.278  16.730  1.00 217.89 ? 190  ILE X N   1 
ATOM   14051 C  CA  . ILE B 2 190  ? -102.758 50.334  15.336  1.00 220.36 ? 190  ILE X CA  1 
ATOM   14052 C  C   . ILE B 2 190  ? -101.760 49.688  14.352  1.00 222.18 ? 190  ILE X C   1 
ATOM   14053 O  O   . ILE B 2 190  ? -100.844 50.343  13.843  1.00 221.72 ? 190  ILE X O   1 
ATOM   14054 C  CB  . ILE B 2 190  ? -103.194 51.789  14.919  1.00 147.02 ? 190  ILE X CB  1 
ATOM   14055 C  CG1 . ILE B 2 190  ? -102.763 52.119  13.476  1.00 147.67 ? 190  ILE X CG1 1 
ATOM   14056 C  CG2 . ILE B 2 190  ? -102.693 52.819  15.940  1.00 146.06 ? 190  ILE X CG2 1 
ATOM   14057 C  CD1 . ILE B 2 190  ? -102.942 53.580  13.062  1.00 148.39 ? 190  ILE X CD1 1 
ATOM   14058 N  N   . ILE B 2 191  ? -101.936 48.390  14.105  1.00 224.03 ? 191  ILE X N   1 
ATOM   14059 C  CA  . ILE B 2 191  ? -101.110 47.693  13.122  1.00 227.60 ? 191  ILE X CA  1 
ATOM   14060 C  C   . ILE B 2 191  ? -101.497 48.175  11.742  1.00 233.32 ? 191  ILE X C   1 
ATOM   14061 O  O   . ILE B 2 191  ? -102.673 48.156  11.386  1.00 236.07 ? 191  ILE X O   1 
ATOM   14062 C  CB  . ILE B 2 191  ? -101.320 46.152  13.118  1.00 174.38 ? 191  ILE X CB  1 
ATOM   14063 C  CG1 . ILE B 2 191  ? -101.600 45.615  14.520  1.00 169.35 ? 191  ILE X CG1 1 
ATOM   14064 C  CG2 . ILE B 2 191  ? -100.123 45.440  12.468  1.00 176.04 ? 191  ILE X CG2 1 
ATOM   14065 C  CD1 . ILE B 2 191  ? -101.703 44.108  14.572  1.00 165.84 ? 191  ILE X CD1 1 
ATOM   14066 N  N   . ASN B 2 192  ? -100.521 48.604  10.957  1.00 235.80 ? 192  ASN X N   1 
ATOM   14067 C  CA  . ASN B 2 192  ? -100.793 48.889  9.557   1.00 240.99 ? 192  ASN X CA  1 
ATOM   14068 C  C   . ASN B 2 192  ? -100.613 47.627  8.706   1.00 245.06 ? 192  ASN X C   1 
ATOM   14069 O  O   . ASN B 2 192  ? -99.794  46.764  9.027   1.00 243.36 ? 192  ASN X O   1 
ATOM   14070 C  CB  . ASN B 2 192  ? -99.934  50.055  9.065   1.00 241.74 ? 192  ASN X CB  1 
ATOM   14071 C  CG  . ASN B 2 192  ? -100.291 51.363  9.752   1.00 242.52 ? 192  ASN X CG  1 
ATOM   14072 O  OD1 . ASN B 2 192  ? -101.462 51.738  9.822   1.00 243.37 ? 192  ASN X OD1 1 
ATOM   14073 N  ND2 . ASN B 2 192  ? -99.285  52.061  10.264  1.00 241.99 ? 192  ASN X ND2 1 
ATOM   14074 N  N   . LEU B 2 193  ? -101.394 47.513  7.636   1.00 250.20 ? 193  LEU X N   1 
ATOM   14075 C  CA  . LEU B 2 193  ? -101.369 46.324  6.792   1.00 253.82 ? 193  LEU X CA  1 
ATOM   14076 C  C   . LEU B 2 193  ? -101.480 46.716  5.326   1.00 259.35 ? 193  LEU X C   1 
ATOM   14077 O  O   . LEU B 2 193  ? -100.992 46.014  4.438   1.00 260.93 ? 193  LEU X O   1 
ATOM   14078 C  CB  . LEU B 2 193  ? -102.507 45.379  7.174   1.00 252.17 ? 193  LEU X CB  1 
ATOM   14079 C  CG  . LEU B 2 193  ? -102.387 44.749  8.561   1.00 247.83 ? 193  LEU X CG  1 
ATOM   14080 C  CD1 . LEU B 2 193  ? -103.657 44.008  8.934   1.00 247.35 ? 193  LEU X CD1 1 
ATOM   14081 C  CD2 . LEU B 2 193  ? -101.185 43.821  8.614   1.00 246.19 ? 193  LEU X CD2 1 
ATOM   14082 N  N   . LYS B 2 194  ? -102.132 47.847  5.087   1.00 263.19 ? 194  LYS X N   1 
ATOM   14083 C  CA  . LYS B 2 194  ? -102.190 48.444  3.761   1.00 268.39 ? 194  LYS X CA  1 
ATOM   14084 C  C   . LYS B 2 194  ? -102.718 49.870  3.858   1.00 269.37 ? 194  LYS X C   1 
ATOM   14085 O  O   . LYS B 2 194  ? -103.149 50.311  4.928   1.00 266.51 ? 194  LYS X O   1 
ATOM   14086 C  CB  . LYS B 2 194  ? -103.038 47.605  2.805   1.00 273.41 ? 194  LYS X CB  1 
ATOM   14087 C  CG  . LYS B 2 194  ? -104.393 47.225  3.345   1.00 277.91 ? 194  LYS X CG  1 
ATOM   14088 C  CD  . LYS B 2 194  ? -105.089 46.271  2.399   1.00 283.84 ? 194  LYS X CD  1 
ATOM   14089 C  CE  . LYS B 2 194  ? -106.455 45.880  2.927   1.00 287.77 ? 194  LYS X CE  1 
ATOM   14090 N  NZ  . LYS B 2 194  ? -107.357 47.058  3.050   1.00 290.41 ? 194  LYS X NZ  1 
ATOM   14091 N  N   . ASP B 2 195  ? -102.675 50.582  2.736   1.00 273.46 ? 195  ASP X N   1 
ATOM   14092 C  CA  . ASP B 2 195  ? -102.969 52.011  2.702   1.00 274.63 ? 195  ASP X CA  1 
ATOM   14093 C  C   . ASP B 2 195  ? -104.201 52.395  3.516   1.00 281.07 ? 195  ASP X C   1 
ATOM   14094 O  O   . ASP B 2 195  ? -104.330 53.537  3.959   1.00 283.38 ? 195  ASP X O   1 
ATOM   14095 C  CB  . ASP B 2 195  ? -103.131 52.485  1.253   1.00 269.36 ? 195  ASP X CB  1 
ATOM   14096 C  CG  . ASP B 2 195  ? -101.812 52.843  0.601   1.00 260.62 ? 195  ASP X CG  1 
ATOM   14097 O  OD1 . ASP B 2 195  ? -101.093 53.707  1.141   1.00 256.67 ? 195  ASP X OD1 1 
ATOM   14098 O  OD2 . ASP B 2 195  ? -101.499 52.270  -0.460  1.00 258.70 ? 195  ASP X OD2 1 
ATOM   14099 N  N   . GLU B 2 196  ? -105.094 51.436  3.734   1.00 284.55 ? 196  GLU X N   1 
ATOM   14100 C  CA  . GLU B 2 196  ? -106.407 51.754  4.277   1.00 290.18 ? 196  GLU X CA  1 
ATOM   14101 C  C   . GLU B 2 196  ? -106.909 50.771  5.330   1.00 283.48 ? 196  GLU X C   1 
ATOM   14102 O  O   . GLU B 2 196  ? -108.092 50.781  5.666   1.00 284.01 ? 196  GLU X O   1 
ATOM   14103 C  CB  . GLU B 2 196  ? -107.437 51.859  3.142   1.00 304.80 ? 196  GLU X CB  1 
ATOM   14104 C  CG  . GLU B 2 196  ? -107.845 50.525  2.508   1.00 316.83 ? 196  GLU X CG  1 
ATOM   14105 C  CD  . GLU B 2 196  ? -106.825 49.990  1.514   1.00 326.57 ? 196  GLU X CD  1 
ATOM   14106 O  OE1 . GLU B 2 196  ? -105.760 50.621  1.343   1.00 329.88 ? 196  GLU X OE1 1 
ATOM   14107 O  OE2 . GLU B 2 196  ? -107.093 48.936  0.897   1.00 330.71 ? 196  GLU X OE2 1 
ATOM   14108 N  N   . ASN B 2 197  ? -106.028 49.933  5.865   1.00 275.46 ? 197  ASN X N   1 
ATOM   14109 C  CA  . ASN B 2 197  ? -106.475 48.934  6.829   1.00 267.44 ? 197  ASN X CA  1 
ATOM   14110 C  C   . ASN B 2 197  ? -105.655 48.942  8.106   1.00 256.30 ? 197  ASN X C   1 
ATOM   14111 O  O   . ASN B 2 197  ? -104.485 49.320  8.102   1.00 254.64 ? 197  ASN X O   1 
ATOM   14112 C  CB  . ASN B 2 197  ? -106.482 47.534  6.203   1.00 267.72 ? 197  ASN X CB  1 
ATOM   14113 C  CG  . ASN B 2 197  ? -107.236 46.518  7.046   1.00 265.54 ? 197  ASN X CG  1 
ATOM   14114 O  OD1 . ASN B 2 197  ? -106.870 46.250  8.190   1.00 263.23 ? 197  ASN X OD1 1 
ATOM   14115 N  ND2 . ASN B 2 197  ? -108.287 45.937  6.476   1.00 266.44 ? 197  ASN X ND2 1 
ATOM   14116 N  N   . LYS B 2 198  ? -106.288 48.531  9.199   1.00 247.57 ? 198  LYS X N   1 
ATOM   14117 C  CA  . LYS B 2 198  ? -105.616 48.442  10.484  1.00 237.78 ? 198  LYS X CA  1 
ATOM   14118 C  C   . LYS B 2 198  ? -106.350 47.530  11.470  1.00 234.63 ? 198  LYS X C   1 
ATOM   14119 O  O   . LYS B 2 198  ? -107.576 47.580  11.578  1.00 236.29 ? 198  LYS X O   1 
ATOM   14120 C  CB  . LYS B 2 198  ? -105.413 49.840  11.085  1.00 232.35 ? 198  LYS X CB  1 
ATOM   14121 C  CG  . LYS B 2 198  ? -106.667 50.523  11.646  1.00 228.74 ? 198  LYS X CG  1 
ATOM   14122 C  CD  . LYS B 2 198  ? -106.267 51.636  12.635  1.00 224.20 ? 198  LYS X CD  1 
ATOM   14123 C  CE  . LYS B 2 198  ? -107.415 52.586  12.976  1.00 222.38 ? 198  LYS X CE  1 
ATOM   14124 N  NZ  . LYS B 2 198  ? -106.973 53.695  13.880  1.00 219.79 ? 198  LYS X NZ  1 
ATOM   14125 N  N   . VAL B 2 199  ? -105.586 46.693  12.173  1.00 230.68 ? 199  VAL X N   1 
ATOM   14126 C  CA  . VAL B 2 199  ? -106.121 45.819  13.224  1.00 227.96 ? 199  VAL X CA  1 
ATOM   14127 C  C   . VAL B 2 199  ? -105.733 46.289  14.632  1.00 224.07 ? 199  VAL X C   1 
ATOM   14128 O  O   . VAL B 2 199  ? -104.573 46.167  15.035  1.00 223.54 ? 199  VAL X O   1 
ATOM   14129 C  CB  . VAL B 2 199  ? -105.631 44.372  13.052  1.00 227.95 ? 199  VAL X CB  1 
ATOM   14130 C  CG1 . VAL B 2 199  ? -106.292 43.464  14.083  1.00 227.93 ? 199  VAL X CG1 1 
ATOM   14131 C  CG2 . VAL B 2 199  ? -105.911 43.886  11.644  1.00 229.97 ? 199  VAL X CG2 1 
ATOM   14132 N  N   . GLU B 2 200  ? -106.710 46.803  15.380  1.00 220.79 ? 200  GLU X N   1 
ATOM   14133 C  CA  . GLU B 2 200  ? -106.455 47.385  16.702  1.00 215.79 ? 200  GLU X CA  1 
ATOM   14134 C  C   . GLU B 2 200  ? -106.539 46.374  17.847  1.00 213.60 ? 200  GLU X C   1 
ATOM   14135 O  O   . GLU B 2 200  ? -107.164 45.320  17.715  1.00 212.46 ? 200  GLU X O   1 
ATOM   14136 C  CB  . GLU B 2 200  ? -107.413 48.552  16.971  1.00 215.41 ? 200  GLU X CB  1 
ATOM   14137 C  CG  . GLU B 2 200  ? -107.293 49.706  15.987  1.00 215.81 ? 200  GLU X CG  1 
ATOM   14138 C  CD  . GLU B 2 200  ? -108.022 50.949  16.460  1.00 217.12 ? 200  GLU X CD  1 
ATOM   14139 O  OE1 . GLU B 2 200  ? -108.576 50.923  17.580  1.00 217.04 ? 200  GLU X OE1 1 
ATOM   14140 O  OE2 . GLU B 2 200  ? -108.040 51.953  15.716  1.00 218.54 ? 200  GLU X OE2 1 
ATOM   14141 N  N   . ILE B 2 201  ? -105.910 46.710  18.973  1.00 212.04 ? 201  ILE X N   1 
ATOM   14142 C  CA  . ILE B 2 201  ? -105.975 45.885  20.179  1.00 210.99 ? 201  ILE X CA  1 
ATOM   14143 C  C   . ILE B 2 201  ? -106.023 46.740  21.436  1.00 213.66 ? 201  ILE X C   1 
ATOM   14144 O  O   . ILE B 2 201  ? -105.002 47.286  21.851  1.00 212.89 ? 201  ILE X O   1 
ATOM   14145 C  CB  . ILE B 2 201  ? -104.747 44.977  20.329  1.00 204.89 ? 201  ILE X CB  1 
ATOM   14146 C  CG1 . ILE B 2 201  ? -104.398 44.300  19.006  1.00 202.36 ? 201  ILE X CG1 1 
ATOM   14147 C  CG2 . ILE B 2 201  ? -104.990 43.953  21.426  1.00 203.58 ? 201  ILE X CG2 1 
ATOM   14148 C  CD1 . ILE B 2 201  ? -103.113 43.517  19.054  1.00 199.31 ? 201  ILE X CD1 1 
ATOM   14149 N  N   . ASP B 2 202  ? -107.198 46.845  22.050  1.00 218.00 ? 202  ASP X N   1 
ATOM   14150 C  CA  . ASP B 2 202  ? -107.309 47.574  23.305  1.00 222.23 ? 202  ASP X CA  1 
ATOM   14151 C  C   . ASP B 2 202  ? -106.317 46.939  24.259  1.00 225.13 ? 202  ASP X C   1 
ATOM   14152 O  O   . ASP B 2 202  ? -106.079 45.729  24.209  1.00 223.69 ? 202  ASP X O   1 
ATOM   14153 C  CB  . ASP B 2 202  ? -108.736 47.517  23.877  1.00 224.57 ? 202  ASP X CB  1 
ATOM   14154 C  CG  . ASP B 2 202  ? -108.921 48.403  25.120  1.00 226.31 ? 202  ASP X CG  1 
ATOM   14155 O  OD1 . ASP B 2 202  ? -109.939 48.240  25.828  1.00 227.29 ? 202  ASP X OD1 1 
ATOM   14156 O  OD2 . ASP B 2 202  ? -108.054 49.263  25.392  1.00 226.86 ? 202  ASP X OD2 1 
ATOM   14157 N  N   . LEU B 2 203  ? -105.718 47.769  25.102  1.00 230.54 ? 203  LEU X N   1 
ATOM   14158 C  CA  . LEU B 2 203  ? -104.759 47.297  26.082  1.00 235.11 ? 203  LEU X CA  1 
ATOM   14159 C  C   . LEU B 2 203  ? -105.422 47.149  27.444  1.00 243.74 ? 203  LEU X C   1 
ATOM   14160 O  O   . LEU B 2 203  ? -104.837 46.591  28.372  1.00 243.49 ? 203  LEU X O   1 
ATOM   14161 C  CB  . LEU B 2 203  ? -103.585 48.261  26.148  1.00 231.15 ? 203  LEU X CB  1 
ATOM   14162 C  CG  . LEU B 2 203  ? -103.004 48.485  24.757  1.00 228.04 ? 203  LEU X CG  1 
ATOM   14163 C  CD1 . LEU B 2 203  ? -101.947 49.569  24.765  1.00 226.72 ? 203  LEU X CD1 1 
ATOM   14164 C  CD2 . LEU B 2 203  ? -102.432 47.183  24.242  1.00 226.41 ? 203  LEU X CD2 1 
ATOM   14165 N  N   . GLY B 2 204  ? -106.651 47.645  27.549  1.00 252.30 ? 204  GLY X N   1 
ATOM   14166 C  CA  . GLY B 2 204  ? -107.398 47.599  28.795  1.00 260.35 ? 204  GLY X CA  1 
ATOM   14167 C  C   . GLY B 2 204  ? -107.865 46.214  29.210  1.00 268.23 ? 204  GLY X C   1 
ATOM   14168 O  O   . GLY B 2 204  ? -108.321 46.023  30.338  1.00 269.46 ? 204  GLY X O   1 
ATOM   14169 N  N   . ASP B 2 205  ? -107.749 45.248  28.301  1.00 274.66 ? 205  ASP X N   1 
ATOM   14170 C  CA  . ASP B 2 205  ? -108.214 43.884  28.552  1.00 281.42 ? 205  ASP X CA  1 
ATOM   14171 C  C   . ASP B 2 205  ? -107.705 42.931  27.472  1.00 281.76 ? 205  ASP X C   1 
ATOM   14172 O  O   . ASP B 2 205  ? -107.510 43.325  26.321  1.00 282.28 ? 205  ASP X O   1 
ATOM   14173 C  CB  . ASP B 2 205  ? -109.747 43.846  28.601  1.00 288.26 ? 205  ASP X CB  1 
ATOM   14174 C  CG  . ASP B 2 205  ? -110.298 42.470  28.960  1.00 293.80 ? 205  ASP X CG  1 
ATOM   14175 O  OD1 . ASP B 2 205  ? -109.549 41.647  29.529  1.00 295.01 ? 205  ASP X OD1 1 
ATOM   14176 O  OD2 . ASP B 2 205  ? -111.493 42.219  28.680  1.00 296.71 ? 205  ASP X OD2 1 
ATOM   14177 N  N   . LYS B 2 206  ? -107.483 41.678  27.848  1.00 281.39 ? 206  LYS X N   1 
ATOM   14178 C  CA  . LYS B 2 206  ? -107.061 40.661  26.896  1.00 279.92 ? 206  LYS X CA  1 
ATOM   14179 C  C   . LYS B 2 206  ? -108.225 39.743  26.541  1.00 278.64 ? 206  LYS X C   1 
ATOM   14180 O  O   . LYS B 2 206  ? -108.077 38.524  26.549  1.00 280.20 ? 206  LYS X O   1 
ATOM   14181 C  CB  . LYS B 2 206  ? -105.902 39.854  27.475  1.00 279.99 ? 206  LYS X CB  1 
ATOM   14182 C  CG  . LYS B 2 206  ? -104.859 40.731  28.128  1.00 279.05 ? 206  LYS X CG  1 
ATOM   14183 C  CD  . LYS B 2 206  ? -103.805 39.928  28.859  1.00 279.00 ? 206  LYS X CD  1 
ATOM   14184 C  CE  . LYS B 2 206  ? -102.887 40.861  29.637  1.00 278.17 ? 206  LYS X CE  1 
ATOM   14185 N  NZ  . LYS B 2 206  ? -101.688 40.182  30.203  1.00 278.00 ? 206  LYS X NZ  1 
ATOM   14186 N  N   . LEU B 2 207  ? -109.379 40.334  26.238  1.00 274.89 ? 207  LEU X N   1 
ATOM   14187 C  CA  . LEU B 2 207  ? -110.610 39.577  25.986  1.00 271.74 ? 207  LEU X CA  1 
ATOM   14188 C  C   . LEU B 2 207  ? -110.745 39.061  24.544  1.00 268.34 ? 207  LEU X C   1 
ATOM   14189 O  O   . LEU B 2 207  ? -111.826 38.624  24.137  1.00 269.70 ? 207  LEU X O   1 
ATOM   14190 C  CB  . LEU B 2 207  ? -111.834 40.427  26.360  1.00 272.12 ? 207  LEU X CB  1 
ATOM   14191 C  CG  . LEU B 2 207  ? -113.212 39.768  26.445  1.00 273.81 ? 207  LEU X CG  1 
ATOM   14192 C  CD1 . LEU B 2 207  ? -113.231 38.707  27.528  1.00 274.67 ? 207  LEU X CD1 1 
ATOM   14193 C  CD2 . LEU B 2 207  ? -114.279 40.814  26.704  1.00 273.97 ? 207  LEU X CD2 1 
ATOM   14194 N  N   . GLN B 2 208  ? -109.654 39.106  23.778  1.00 262.75 ? 208  GLN X N   1 
ATOM   14195 C  CA  . GLN B 2 208  ? -109.683 38.736  22.357  1.00 258.95 ? 208  GLN X CA  1 
ATOM   14196 C  C   . GLN B 2 208  ? -109.335 37.268  22.081  1.00 257.19 ? 208  GLN X C   1 
ATOM   14197 O  O   . GLN B 2 208  ? -108.456 36.967  21.275  1.00 255.54 ? 208  GLN X O   1 
ATOM   14198 C  CB  . GLN B 2 208  ? -108.770 39.659  21.541  1.00 255.31 ? 208  GLN X CB  1 
ATOM   14199 C  CG  . GLN B 2 208  ? -108.927 39.519  20.028  1.00 254.12 ? 208  GLN X CG  1 
ATOM   14200 C  CD  . GLN B 2 208  ? -110.230 40.098  19.508  1.00 253.75 ? 208  GLN X CD  1 
ATOM   14201 O  OE1 . GLN B 2 208  ? -111.099 39.369  19.030  1.00 254.50 ? 208  GLN X OE1 1 
ATOM   14202 N  NE2 . GLN B 2 208  ? -110.371 41.416  19.596  1.00 253.05 ? 208  GLN X NE2 1 
ATOM   14203 N  N   . PHE B 2 209  ? -110.038 36.360  22.743  1.00 257.30 ? 209  PHE X N   1 
ATOM   14204 C  CA  . PHE B 2 209  ? -109.796 34.933  22.576  1.00 257.64 ? 209  PHE X CA  1 
ATOM   14205 C  C   . PHE B 2 209  ? -110.054 34.440  21.147  1.00 262.69 ? 209  PHE X C   1 
ATOM   14206 O  O   . PHE B 2 209  ? -109.304 33.611  20.630  1.00 263.88 ? 209  PHE X O   1 
ATOM   14207 C  CB  . PHE B 2 209  ? -110.650 34.140  23.573  1.00 254.11 ? 209  PHE X CB  1 
ATOM   14208 C  CG  . PHE B 2 209  ? -112.084 34.605  23.654  1.00 250.48 ? 209  PHE X CG  1 
ATOM   14209 C  CD1 . PHE B 2 209  ? -113.063 34.014  22.872  1.00 250.75 ? 209  PHE X CD1 1 
ATOM   14210 C  CD2 . PHE B 2 209  ? -112.451 35.633  24.512  1.00 246.95 ? 209  PHE X CD2 1 
ATOM   14211 C  CE1 . PHE B 2 209  ? -114.374 34.438  22.942  1.00 250.41 ? 209  PHE X CE1 1 
ATOM   14212 C  CE2 . PHE B 2 209  ? -113.761 36.061  24.586  1.00 246.56 ? 209  PHE X CE2 1 
ATOM   14213 C  CZ  . PHE B 2 209  ? -114.723 35.462  23.800  1.00 248.77 ? 209  PHE X CZ  1 
ATOM   14214 N  N   . GLU B 2 210  ? -111.103 34.968  20.513  1.00 267.41 ? 210  GLU X N   1 
ATOM   14215 C  CA  . GLU B 2 210  ? -111.612 34.419  19.245  1.00 272.64 ? 210  GLU X CA  1 
ATOM   14216 C  C   . GLU B 2 210  ? -110.864 34.856  17.971  1.00 270.84 ? 210  GLU X C   1 
ATOM   14217 O  O   . GLU B 2 210  ? -110.859 34.127  16.975  1.00 273.32 ? 210  GLU X O   1 
ATOM   14218 C  CB  . GLU B 2 210  ? -113.125 34.675  19.097  1.00 279.39 ? 210  GLU X CB  1 
ATOM   14219 C  CG  . GLU B 2 210  ? -113.526 35.591  17.941  1.00 284.31 ? 210  GLU X CG  1 
ATOM   14220 C  CD  . GLU B 2 210  ? -113.380 37.066  18.263  1.00 286.54 ? 210  GLU X CD  1 
ATOM   14221 O  OE1 . GLU B 2 210  ? -113.418 37.426  19.458  1.00 286.71 ? 210  GLU X OE1 1 
ATOM   14222 O  OE2 . GLU B 2 210  ? -113.237 37.866  17.316  1.00 287.87 ? 210  GLU X OE2 1 
ATOM   14223 N  N   . ARG B 2 211  ? -110.250 36.039  17.989  1.00 265.58 ? 211  ARG X N   1 
ATOM   14224 C  CA  . ARG B 2 211  ? -109.445 36.481  16.847  1.00 259.50 ? 211  ARG X CA  1 
ATOM   14225 C  C   . ARG B 2 211  ? -108.010 35.982  16.983  1.00 257.94 ? 211  ARG X C   1 
ATOM   14226 O  O   . ARG B 2 211  ? -107.222 36.063  16.040  1.00 255.79 ? 211  ARG X O   1 
ATOM   14227 C  CB  . ARG B 2 211  ? -109.483 38.005  16.684  1.00 252.85 ? 211  ARG X CB  1 
ATOM   14228 C  CG  . ARG B 2 211  ? -108.822 38.507  15.404  1.00 246.56 ? 211  ARG X CG  1 
ATOM   14229 C  CD  . ARG B 2 211  ? -109.261 39.922  15.073  1.00 241.42 ? 211  ARG X CD  1 
ATOM   14230 N  NE  . ARG B 2 211  ? -109.082 40.830  16.201  1.00 236.11 ? 211  ARG X NE  1 
ATOM   14231 C  CZ  . ARG B 2 211  ? -109.561 42.068  16.248  1.00 233.28 ? 211  ARG X CZ  1 
ATOM   14232 N  NH1 . ARG B 2 211  ? -110.253 42.549  15.228  1.00 233.93 ? 211  ARG X NH1 1 
ATOM   14233 N  NH2 . ARG B 2 211  ? -109.352 42.827  17.316  1.00 231.10 ? 211  ARG X NH2 1 
ATOM   14234 N  N   . MET B 2 212  ? -107.687 35.457  18.164  1.00 257.07 ? 212  MET X N   1 
ATOM   14235 C  CA  . MET B 2 212  ? -106.380 34.863  18.421  1.00 255.48 ? 212  MET X CA  1 
ATOM   14236 C  C   . MET B 2 212  ? -106.125 33.715  17.460  1.00 254.47 ? 212  MET X C   1 
ATOM   14237 O  O   . MET B 2 212  ? -105.070 33.080  17.489  1.00 256.06 ? 212  MET X O   1 
ATOM   14238 C  CB  . MET B 2 212  ? -106.279 34.391  19.872  1.00 254.74 ? 212  MET X CB  1 
ATOM   14239 C  CG  . MET B 2 212  ? -105.991 35.528  20.836  1.00 252.93 ? 212  MET X CG  1 
ATOM   14240 S  SD  . MET B 2 212  ? -105.865 35.075  22.576  1.00 230.99 ? 212  MET X SD  1 
ATOM   14241 C  CE  . MET B 2 212  ? -105.264 36.622  23.266  1.00 131.38 ? 212  MET X CE  1 
ATOM   14242 N  N   . GLY B 2 213  ? -107.116 33.458  16.614  1.00 253.01 ? 213  GLY X N   1 
ATOM   14243 C  CA  . GLY B 2 213  ? -107.002 32.487  15.545  1.00 252.20 ? 213  GLY X CA  1 
ATOM   14244 C  C   . GLY B 2 213  ? -106.562 33.129  14.243  1.00 251.04 ? 213  GLY X C   1 
ATOM   14245 O  O   . GLY B 2 213  ? -105.826 32.516  13.466  1.00 250.78 ? 213  GLY X O   1 
ATOM   14246 N  N   . ASP B 2 214  ? -107.015 34.361  14.008  1.00 250.45 ? 214  ASP X N   1 
ATOM   14247 C  CA  . ASP B 2 214  ? -106.610 35.141  12.838  1.00 247.78 ? 214  ASP X CA  1 
ATOM   14248 C  C   . ASP B 2 214  ? -105.102 34.952  12.584  1.00 248.49 ? 214  ASP X C   1 
ATOM   14249 O  O   . ASP B 2 214  ? -104.341 34.709  13.526  1.00 250.11 ? 214  ASP X O   1 
ATOM   14250 C  CB  . ASP B 2 214  ? -106.958 36.624  13.063  1.00 241.05 ? 214  ASP X CB  1 
ATOM   14251 C  CG  . ASP B 2 214  ? -107.156 37.401  11.763  1.00 234.61 ? 214  ASP X CG  1 
ATOM   14252 O  OD1 . ASP B 2 214  ? -106.364 37.232  10.816  1.00 231.67 ? 214  ASP X OD1 1 
ATOM   14253 O  OD2 . ASP B 2 214  ? -108.102 38.208  11.694  1.00 232.63 ? 214  ASP X OD2 1 
ATOM   14254 N  N   . VAL B 2 215  ? -104.675 35.044  11.321  1.00 244.62 ? 215  VAL X N   1 
ATOM   14255 C  CA  . VAL B 2 215  ? -103.251 34.927  10.962  1.00 239.69 ? 215  VAL X CA  1 
ATOM   14256 C  C   . VAL B 2 215  ? -102.809 36.072  10.032  1.00 236.25 ? 215  VAL X C   1 
ATOM   14257 O  O   . VAL B 2 215  ? -103.641 36.693  9.362   1.00 235.64 ? 215  VAL X O   1 
ATOM   14258 C  CB  . VAL B 2 215  ? -102.901 33.548  10.326  1.00 278.55 ? 215  VAL X CB  1 
ATOM   14259 C  CG1 . VAL B 2 215  ? -103.004 32.429  11.362  1.00 278.69 ? 215  VAL X CG1 1 
ATOM   14260 C  CG2 . VAL B 2 215  ? -103.785 33.258  9.122   1.00 280.89 ? 215  VAL X CG2 1 
ATOM   14261 N  N   . LEU B 2 216  ? -101.504 36.348  9.994   1.00 232.89 ? 216  LEU X N   1 
ATOM   14262 C  CA  . LEU B 2 216  ? -100.998 37.523  9.281   1.00 228.63 ? 216  LEU X CA  1 
ATOM   14263 C  C   . LEU B 2 216  ? -99.808  37.250  8.359   1.00 225.59 ? 216  LEU X C   1 
ATOM   14264 O  O   . LEU B 2 216  ? -98.911  36.474  8.688   1.00 224.41 ? 216  LEU X O   1 
ATOM   14265 C  CB  . LEU B 2 216  ? -100.621 38.631  10.271  1.00 224.22 ? 216  LEU X CB  1 
ATOM   14266 C  CG  . LEU B 2 216  ? -101.749 39.298  11.054  1.00 220.07 ? 216  LEU X CG  1 
ATOM   14267 C  CD1 . LEU B 2 216  ? -102.952 39.551  10.146  1.00 220.69 ? 216  LEU X CD1 1 
ATOM   14268 C  CD2 . LEU B 2 216  ? -102.137 38.458  12.261  1.00 217.70 ? 216  LEU X CD2 1 
ATOM   14269 N  N   . ASN B 2 217  ? -99.819  37.910  7.203   1.00 223.77 ? 217  ASN X N   1 
ATOM   14270 C  CA  . ASN B 2 217  ? -98.716  37.855  6.252   1.00 222.94 ? 217  ASN X CA  1 
ATOM   14271 C  C   . ASN B 2 217  ? -97.589  38.782  6.686   1.00 221.23 ? 217  ASN X C   1 
ATOM   14272 O  O   . ASN B 2 217  ? -97.773  39.993  6.742   1.00 218.98 ? 217  ASN X O   1 
ATOM   14273 C  CB  . ASN B 2 217  ? -99.198  38.271  4.859   1.00 224.81 ? 217  ASN X CB  1 
ATOM   14274 C  CG  . ASN B 2 217  ? -100.529 37.649  4.490   1.00 227.94 ? 217  ASN X CG  1 
ATOM   14275 O  OD1 . ASN B 2 217  ? -100.960 36.671  5.099   1.00 229.36 ? 217  ASN X OD1 1 
ATOM   14276 N  ND2 . ASN B 2 217  ? -101.190 38.214  3.484   1.00 229.04 ? 217  ASN X ND2 1 
ATOM   14277 N  N   . SER B 2 218  ? -96.422  38.220  6.974   1.00 223.46 ? 218  SER X N   1 
ATOM   14278 C  CA  . SER B 2 218  ? -95.308  39.006  7.488   1.00 225.23 ? 218  SER X CA  1 
ATOM   14279 C  C   . SER B 2 218  ? -94.966  40.219  6.624   1.00 229.75 ? 218  SER X C   1 
ATOM   14280 O  O   . SER B 2 218  ? -94.956  41.346  7.110   1.00 227.68 ? 218  SER X O   1 
ATOM   14281 C  CB  . SER B 2 218  ? -94.075  38.124  7.667   1.00 222.90 ? 218  SER X CB  1 
ATOM   14282 O  OG  . SER B 2 218  ? -94.304  37.157  8.671   1.00 220.87 ? 218  SER X OG  1 
ATOM   14283 N  N   . LYS B 2 219  ? -94.691  39.987  5.345   1.00 236.85 ? 219  LYS X N   1 
ATOM   14284 C  CA  . LYS B 2 219  ? -94.250  41.055  4.449   1.00 244.23 ? 219  LYS X CA  1 
ATOM   14285 C  C   . LYS B 2 219  ? -95.293  42.150  4.219   1.00 238.05 ? 219  LYS X C   1 
ATOM   14286 O  O   . LYS B 2 219  ? -94.969  43.229  3.722   1.00 240.52 ? 219  LYS X O   1 
ATOM   14287 C  CB  . LYS B 2 219  ? -93.821  40.475  3.102   1.00 261.18 ? 219  LYS X CB  1 
ATOM   14288 C  CG  . LYS B 2 219  ? -92.654  39.515  3.183   1.00 283.06 ? 219  LYS X CG  1 
ATOM   14289 C  CD  . LYS B 2 219  ? -92.263  39.043  1.799   1.00 286.03 ? 219  LYS X CD  1 
ATOM   14290 C  CE  . LYS B 2 219  ? -93.370  38.216  1.172   1.00 292.44 ? 219  LYS X CE  1 
ATOM   14291 N  NZ  . LYS B 2 219  ? -93.590  36.958  1.931   1.00 296.68 ? 219  LYS X NZ  1 
ATOM   14292 N  N   . ASP B 2 220  ? -96.543  41.869  4.566   1.00 231.29 ? 220  ASP X N   1 
ATOM   14293 C  CA  . ASP B 2 220  ? -97.621  42.825  4.335   1.00 225.73 ? 220  ASP X CA  1 
ATOM   14294 C  C   . ASP B 2 220  ? -97.560  44.023  5.288   1.00 220.58 ? 220  ASP X C   1 
ATOM   14295 O  O   . ASP B 2 220  ? -97.785  45.159  4.862   1.00 222.01 ? 220  ASP X O   1 
ATOM   14296 C  CB  . ASP B 2 220  ? -98.992  42.139  4.430   1.00 224.93 ? 220  ASP X CB  1 
ATOM   14297 C  CG  . ASP B 2 220  ? -99.371  41.387  3.158   1.00 226.83 ? 220  ASP X CG  1 
ATOM   14298 O  OD1 . ASP B 2 220  ? -98.751  41.627  2.102   1.00 228.15 ? 220  ASP X OD1 1 
ATOM   14299 O  OD2 . ASP B 2 220  ? -100.303 40.558  3.213   1.00 227.44 ? 220  ASP X OD2 1 
ATOM   14300 N  N   . ILE B 2 221  ? -97.250  43.763  6.564   1.00 213.97 ? 221  ILE X N   1 
ATOM   14301 C  CA  . ILE B 2 221  ? -97.288  44.788  7.624   1.00 207.15 ? 221  ILE X CA  1 
ATOM   14302 C  C   . ILE B 2 221  ? -96.384  45.987  7.341   1.00 201.70 ? 221  ILE X C   1 
ATOM   14303 O  O   . ILE B 2 221  ? -95.157  45.873  7.363   1.00 203.18 ? 221  ILE X O   1 
ATOM   14304 C  CB  . ILE B 2 221  ? -96.898  44.230  9.026   1.00 164.79 ? 221  ILE X CB  1 
ATOM   14305 C  CG1 . ILE B 2 221  ? -97.495  42.845  9.283   1.00 162.13 ? 221  ILE X CG1 1 
ATOM   14306 C  CG2 . ILE B 2 221  ? -97.333  45.194  10.118  1.00 166.04 ? 221  ILE X CG2 1 
ATOM   14307 C  CD1 . ILE B 2 221  ? -97.221  42.303  10.688  1.00 158.12 ? 221  ILE X CD1 1 
ATOM   14308 N  N   . ARG B 2 222  ? -96.999  47.141  7.103   1.00 197.30 ? 222  ARG X N   1 
ATOM   14309 C  CA  . ARG B 2 222  ? -96.264  48.353  6.751   1.00 194.34 ? 222  ARG X CA  1 
ATOM   14310 C  C   . ARG B 2 222  ? -95.587  49.023  7.954   1.00 191.61 ? 222  ARG X C   1 
ATOM   14311 O  O   . ARG B 2 222  ? -94.442  49.474  7.851   1.00 188.24 ? 222  ARG X O   1 
ATOM   14312 C  CB  . ARG B 2 222  ? -97.188  49.338  6.039   1.00 198.76 ? 222  ARG X CB  1 
ATOM   14313 C  CG  . ARG B 2 222  ? -96.568  50.684  5.745   1.00 203.49 ? 222  ARG X CG  1 
ATOM   14314 C  CD  . ARG B 2 222  ? -97.607  51.579  5.121   1.00 209.15 ? 222  ARG X CD  1 
ATOM   14315 N  NE  . ARG B 2 222  ? -98.262  50.891  4.016   1.00 213.25 ? 222  ARG X NE  1 
ATOM   14316 C  CZ  . ARG B 2 222  ? -99.230  51.415  3.275   1.00 216.09 ? 222  ARG X CZ  1 
ATOM   14317 N  NH1 . ARG B 2 222  ? -99.666  52.644  3.524   1.00 217.01 ? 222  ARG X NH1 1 
ATOM   14318 N  NH2 . ARG B 2 222  ? -99.759  50.710  2.283   1.00 217.76 ? 222  ARG X NH2 1 
ATOM   14319 N  N   . GLY B 2 223  ? -96.288  49.092  9.087   1.00 189.15 ? 223  GLY X N   1 
ATOM   14320 C  CA  . GLY B 2 223  ? -95.718  49.649  10.301  1.00 185.22 ? 223  GLY X CA  1 
ATOM   14321 C  C   . GLY B 2 223  ? -96.693  49.803  11.447  1.00 176.50 ? 223  GLY X C   1 
ATOM   14322 O  O   . GLY B 2 223  ? -97.748  50.410  11.290  1.00 176.95 ? 223  GLY X O   1 
ATOM   14323 N  N   . ILE B 2 224  ? -96.327  49.253  12.605  1.00 174.06 ? 224  ILE X N   1 
ATOM   14324 C  CA  . ILE B 2 224  ? -97.094  49.430  13.851  1.00 173.58 ? 224  ILE X CA  1 
ATOM   14325 C  C   . ILE B 2 224  ? -96.991  50.846  14.448  1.00 179.03 ? 224  ILE X C   1 
ATOM   14326 O  O   . ILE B 2 224  ? -96.002  51.565  14.247  1.00 179.44 ? 224  ILE X O   1 
ATOM   14327 C  CB  . ILE B 2 224  ? -96.662  48.445  14.986  1.00 156.16 ? 224  ILE X CB  1 
ATOM   14328 C  CG1 . ILE B 2 224  ? -96.507  47.015  14.488  1.00 154.72 ? 224  ILE X CG1 1 
ATOM   14329 C  CG2 . ILE B 2 224  ? -97.672  48.449  16.122  1.00 155.82 ? 224  ILE X CG2 1 
ATOM   14330 C  CD1 . ILE B 2 224  ? -96.386  46.034  15.638  1.00 152.34 ? 224  ILE X CD1 1 
ATOM   14331 N  N   . SER B 2 225  ? -98.008  51.217  15.220  1.00 183.81 ? 225  SER X N   1 
ATOM   14332 C  CA  . SER B 2 225  ? -98.042  52.510  15.883  1.00 188.64 ? 225  SER X CA  1 
ATOM   14333 C  C   . SER B 2 225  ? -98.937  52.426  17.132  1.00 192.60 ? 225  SER X C   1 
ATOM   14334 O  O   . SER B 2 225  ? -100.150 52.225  17.026  1.00 194.18 ? 225  SER X O   1 
ATOM   14335 C  CB  . SER B 2 225  ? -98.548  53.582  14.910  1.00 190.02 ? 225  SER X CB  1 
ATOM   14336 O  OG  . SER B 2 225  ? -97.768  54.767  14.978  1.00 189.35 ? 225  SER X OG  1 
ATOM   14337 N  N   . VAL B 2 226  ? -98.323  52.556  18.311  1.00 192.82 ? 226  VAL X N   1 
ATOM   14338 C  CA  . VAL B 2 226  ? -99.042  52.518  19.591  1.00 193.91 ? 226  VAL X CA  1 
ATOM   14339 C  C   . VAL B 2 226  ? -99.226  53.914  20.192  1.00 197.17 ? 226  VAL X C   1 
ATOM   14340 O  O   . VAL B 2 226  ? -98.431  54.822  19.941  1.00 195.74 ? 226  VAL X O   1 
ATOM   14341 C  CB  . VAL B 2 226  ? -98.322  51.613  20.631  1.00 228.02 ? 226  VAL X CB  1 
ATOM   14342 C  CG1 . VAL B 2 226  ? -99.102  51.558  21.949  1.00 227.32 ? 226  VAL X CG1 1 
ATOM   14343 C  CG2 . VAL B 2 226  ? -98.123  50.214  20.075  1.00 227.58 ? 226  VAL X CG2 1 
ATOM   14344 N  N   . THR B 2 227  ? -100.279 54.074  20.988  1.00 201.11 ? 227  THR X N   1 
ATOM   14345 C  CA  . THR B 2 227  ? -100.503 55.305  21.730  1.00 204.86 ? 227  THR X CA  1 
ATOM   14346 C  C   . THR B 2 227  ? -100.981 54.944  23.132  1.00 209.20 ? 227  THR X C   1 
ATOM   14347 O  O   . THR B 2 227  ? -102.039 54.333  23.293  1.00 210.40 ? 227  THR X O   1 
ATOM   14348 C  CB  . THR B 2 227  ? -101.540 56.210  21.039  1.00 202.65 ? 227  THR X CB  1 
ATOM   14349 O  OG1 . THR B 2 227  ? -101.167 56.413  19.673  1.00 201.87 ? 227  THR X OG1 1 
ATOM   14350 C  CG2 . THR B 2 227  ? -101.629 57.559  21.735  1.00 202.27 ? 227  THR X CG2 1 
ATOM   14351 N  N   . ILE B 2 228  ? -100.182 55.306  24.137  1.00 212.29 ? 228  ILE X N   1 
ATOM   14352 C  CA  . ILE B 2 228  ? -100.488 55.018  25.541  1.00 214.98 ? 228  ILE X CA  1 
ATOM   14353 C  C   . ILE B 2 228  ? -101.080 56.207  26.292  1.00 218.01 ? 228  ILE X C   1 
ATOM   14354 O  O   . ILE B 2 228  ? -100.426 57.241  26.448  1.00 219.26 ? 228  ILE X O   1 
ATOM   14355 C  CB  . ILE B 2 228  ? -99.245  54.524  26.310  1.00 216.19 ? 228  ILE X CB  1 
ATOM   14356 C  CG1 . ILE B 2 228  ? -99.143  53.001  26.231  1.00 215.56 ? 228  ILE X CG1 1 
ATOM   14357 C  CG2 . ILE B 2 228  ? -99.305  54.953  27.770  1.00 217.29 ? 228  ILE X CG2 1 
ATOM   14358 C  CD1 . ILE B 2 228  ? -98.206  52.404  27.258  1.00 215.33 ? 228  ILE X CD1 1 
ATOM   14359 N  N   . ASN B 2 229  ? -102.322 56.044  26.751  1.00 219.35 ? 229  ASN X N   1 
ATOM   14360 C  CA  . ASN B 2 229  ? -102.973 57.020  27.628  1.00 220.21 ? 229  ASN X CA  1 
ATOM   14361 C  C   . ASN B 2 229  ? -103.004 56.593  29.109  1.00 213.05 ? 229  ASN X C   1 
ATOM   14362 O  O   . ASN B 2 229  ? -103.663 55.621  29.480  1.00 210.83 ? 229  ASN X O   1 
ATOM   14363 C  CB  . ASN B 2 229  ? -104.374 57.426  27.105  1.00 226.55 ? 229  ASN X CB  1 
ATOM   14364 C  CG  . ASN B 2 229  ? -105.237 56.232  26.670  1.00 229.47 ? 229  ASN X CG  1 
ATOM   14365 O  OD1 . ASN B 2 229  ? -104.731 55.195  26.237  1.00 229.14 ? 229  ASN X OD1 1 
ATOM   14366 N  ND2 . ASN B 2 229  ? -106.557 56.396  26.766  1.00 231.37 ? 229  ASN X ND2 1 
ATOM   14367 N  N   . GLN B 2 230  ? -102.277 57.329  29.943  1.00 208.44 ? 230  GLN X N   1 
ATOM   14368 C  CA  . GLN B 2 230  ? -102.149 56.992  31.357  1.00 202.87 ? 230  GLN X CA  1 
ATOM   14369 C  C   . GLN B 2 230  ? -103.183 57.718  32.218  1.00 202.59 ? 230  GLN X C   1 
ATOM   14370 O  O   . GLN B 2 230  ? -102.925 58.053  33.378  1.00 201.52 ? 230  GLN X O   1 
ATOM   14371 C  CB  . GLN B 2 230  ? -100.729 57.295  31.848  1.00 198.93 ? 230  GLN X CB  1 
ATOM   14372 C  CG  . GLN B 2 230  ? -99.631  56.811  30.899  1.00 194.40 ? 230  GLN X CG  1 
ATOM   14373 C  CD  . GLN B 2 230  ? -98.232  56.985  31.461  1.00 190.89 ? 230  GLN X CD  1 
ATOM   14374 O  OE1 . GLN B 2 230  ? -97.443  57.781  30.955  1.00 190.50 ? 230  GLN X OE1 1 
ATOM   14375 N  NE2 . GLN B 2 230  ? -97.917  56.238  32.512  1.00 189.20 ? 230  GLN X NE2 1 
ATOM   14376 N  N   . THR C 1 22   ? -18.476  122.259 68.596  1.00 166.69 ? 22   THR B N   1 
ATOM   14377 C  CA  . THR C 1 22   ? -18.698  121.165 69.535  1.00 164.49 ? 22   THR B CA  1 
ATOM   14378 C  C   . THR C 1 22   ? -17.530  120.180 69.506  1.00 160.56 ? 22   THR B C   1 
ATOM   14379 O  O   . THR C 1 22   ? -16.718  120.200 68.583  1.00 158.12 ? 22   THR B O   1 
ATOM   14380 C  CB  . THR C 1 22   ? -20.042  120.447 69.249  1.00 164.06 ? 22   THR B CB  1 
ATOM   14381 O  OG1 . THR C 1 22   ? -20.381  120.585 67.853  1.00 161.66 ? 22   THR B OG1 1 
ATOM   14382 C  CG2 . THR C 1 22   ? -21.161  121.039 70.137  1.00 164.91 ? 22   THR B CG2 1 
ATOM   14383 N  N   . TYR C 1 23   ? -17.431  119.348 70.535  1.00 159.93 ? 23   TYR B N   1 
ATOM   14384 C  CA  . TYR C 1 23   ? -16.419  118.308 70.566  1.00 162.71 ? 23   TYR B CA  1 
ATOM   14385 C  C   . TYR C 1 23   ? -16.996  116.917 70.382  1.00 161.08 ? 23   TYR B C   1 
ATOM   14386 O  O   . TYR C 1 23   ? -18.140  116.651 70.755  1.00 159.02 ? 23   TYR B O   1 
ATOM   14387 C  CB  . TYR C 1 23   ? -15.632  118.337 71.866  1.00 169.96 ? 23   TYR B CB  1 
ATOM   14388 C  CG  . TYR C 1 23   ? -16.464  118.613 73.102  1.00 177.95 ? 23   TYR B CG  1 
ATOM   14389 C  CD1 . TYR C 1 23   ? -17.833  118.320 73.140  1.00 179.27 ? 23   TYR B CD1 1 
ATOM   14390 C  CD2 . TYR C 1 23   ? -15.868  119.165 74.249  1.00 182.94 ? 23   TYR B CD2 1 
ATOM   14391 C  CE1 . TYR C 1 23   ? -18.578  118.583 74.281  1.00 182.51 ? 23   TYR B CE1 1 
ATOM   14392 C  CE2 . TYR C 1 23   ? -16.596  119.428 75.388  1.00 185.02 ? 23   TYR B CE2 1 
ATOM   14393 C  CZ  . TYR C 1 23   ? -17.947  119.137 75.406  1.00 185.69 ? 23   TYR B CZ  1 
ATOM   14394 O  OH  . TYR C 1 23   ? -18.651  119.409 76.560  1.00 187.42 ? 23   TYR B OH  1 
ATOM   14395 N  N   . VAL C 1 24   ? -16.168  116.036 69.820  1.00 160.34 ? 24   VAL B N   1 
ATOM   14396 C  CA  . VAL C 1 24   ? -16.461  114.618 69.660  1.00 156.96 ? 24   VAL B CA  1 
ATOM   14397 C  C   . VAL C 1 24   ? -15.263  113.829 70.153  1.00 153.67 ? 24   VAL B C   1 
ATOM   14398 O  O   . VAL C 1 24   ? -14.114  114.106 69.809  1.00 153.44 ? 24   VAL B O   1 
ATOM   14399 C  CB  . VAL C 1 24   ? -16.774  114.246 68.193  1.00 157.46 ? 24   VAL B CB  1 
ATOM   14400 C  CG1 . VAL C 1 24   ? -16.517  112.755 67.921  1.00 157.05 ? 24   VAL B CG1 1 
ATOM   14401 C  CG2 . VAL C 1 24   ? -18.211  114.637 67.837  1.00 156.64 ? 24   VAL B CG2 1 
ATOM   14402 N  N   . ILE C 1 25   ? -15.555  112.843 70.979  1.00 153.57 ? 25   ILE B N   1 
ATOM   14403 C  CA  . ILE C 1 25   ? -14.537  112.029 71.600  1.00 158.07 ? 25   ILE B CA  1 
ATOM   14404 C  C   . ILE C 1 25   ? -15.031  110.603 71.506  1.00 155.85 ? 25   ILE B C   1 
ATOM   14405 O  O   . ILE C 1 25   ? -15.814  110.141 72.335  1.00 156.66 ? 25   ILE B O   1 
ATOM   14406 C  CB  . ILE C 1 25   ? -14.388  112.393 73.082  1.00 165.21 ? 25   ILE B CB  1 
ATOM   14407 C  CG1 . ILE C 1 25   ? -13.901  113.840 73.239  1.00 169.66 ? 25   ILE B CG1 1 
ATOM   14408 C  CG2 . ILE C 1 25   ? -13.467  111.398 73.790  1.00 166.81 ? 25   ILE B CG2 1 
ATOM   14409 C  CD1 . ILE C 1 25   ? -12.412  113.980 73.402  1.00 172.54 ? 25   ILE B CD1 1 
ATOM   14410 N  N   . SER C 1 26   ? -14.595  109.900 70.479  1.00 153.05 ? 26   SER B N   1 
ATOM   14411 C  CA  . SER C 1 26   ? -15.143  108.590 70.233  1.00 149.70 ? 26   SER B CA  1 
ATOM   14412 C  C   . SER C 1 26   ? -14.427  107.563 71.079  1.00 144.09 ? 26   SER B C   1 
ATOM   14413 O  O   . SER C 1 26   ? -13.282  107.773 71.476  1.00 145.00 ? 26   SER B O   1 
ATOM   14414 C  CB  . SER C 1 26   ? -15.021  108.257 68.750  1.00 152.06 ? 26   SER B CB  1 
ATOM   14415 O  OG  . SER C 1 26   ? -15.614  109.279 67.970  1.00 153.72 ? 26   SER B OG  1 
ATOM   14416 N  N   . ALA C 1 27   ? -15.109  106.461 71.362  1.00 138.41 ? 27   ALA B N   1 
ATOM   14417 C  CA  . ALA C 1 27   ? -14.456  105.320 71.981  1.00 134.35 ? 27   ALA B CA  1 
ATOM   14418 C  C   . ALA C 1 27   ? -15.373  104.108 72.041  1.00 130.37 ? 27   ALA B C   1 
ATOM   14419 O  O   . ALA C 1 27   ? -16.595  104.247 71.972  1.00 126.52 ? 27   ALA B O   1 
ATOM   14420 C  CB  . ALA C 1 27   ? -13.956  105.672 73.353  1.00 136.96 ? 27   ALA B CB  1 
ATOM   14421 N  N   . PRO C 1 28   ? -14.774  102.911 72.179  1.00 128.74 ? 28   PRO B N   1 
ATOM   14422 C  CA  . PRO C 1 28   ? -15.486  101.635 72.176  1.00 129.94 ? 28   PRO B CA  1 
ATOM   14423 C  C   . PRO C 1 28   ? -16.727  101.632 73.054  1.00 135.01 ? 28   PRO B C   1 
ATOM   14424 O  O   . PRO C 1 28   ? -16.898  102.502 73.894  1.00 137.39 ? 28   PRO B O   1 
ATOM   14425 C  CB  . PRO C 1 28   ? -14.442  100.678 72.733  1.00 127.76 ? 28   PRO B CB  1 
ATOM   14426 C  CG  . PRO C 1 28   ? -13.165  101.228 72.233  1.00 127.19 ? 28   PRO B CG  1 
ATOM   14427 C  CD  . PRO C 1 28   ? -13.318  102.711 72.298  1.00 128.38 ? 28   PRO B CD  1 
ATOM   14428 N  N   . LYS C 1 29   ? -17.602  100.662 72.832  1.00 136.19 ? 29   LYS B N   1 
ATOM   14429 C  CA  . LYS C 1 29   ? -18.774  100.478 73.676  1.00 138.50 ? 29   LYS B CA  1 
ATOM   14430 C  C   . LYS C 1 29   ? -18.332  99.907  75.045  1.00 138.25 ? 29   LYS B C   1 
ATOM   14431 O  O   . LYS C 1 29   ? -18.951  100.177 76.086  1.00 138.61 ? 29   LYS B O   1 
ATOM   14432 C  CB  . LYS C 1 29   ? -19.814  99.590  72.952  1.00 137.22 ? 29   LYS B CB  1 
ATOM   14433 C  CG  . LYS C 1 29   ? -21.073  99.181  73.750  1.00 137.57 ? 29   LYS B CG  1 
ATOM   14434 C  CD  . LYS C 1 29   ? -21.771  100.346 74.505  1.00 185.19 ? 29   LYS B CD  1 
ATOM   14435 C  CE  . LYS C 1 29   ? -22.186  99.919  75.945  1.00 178.14 ? 29   LYS B CE  1 
ATOM   14436 N  NZ  . LYS C 1 29   ? -23.064  100.866 76.703  1.00 177.66 ? 29   LYS B NZ  1 
ATOM   14437 N  N   . ILE C 1 30   ? -17.234  99.153  75.046  1.00 138.11 ? 30   ILE B N   1 
ATOM   14438 C  CA  . ILE C 1 30   ? -16.711  98.544  76.273  1.00 137.40 ? 30   ILE B CA  1 
ATOM   14439 C  C   . ILE C 1 30   ? -15.211  98.789  76.364  1.00 136.65 ? 30   ILE B C   1 
ATOM   14440 O  O   . ILE C 1 30   ? -14.570  99.043  75.349  1.00 136.21 ? 30   ILE B O   1 
ATOM   14441 C  CB  . ILE C 1 30   ? -16.954  97.000  76.310  1.00 129.34 ? 30   ILE B CB  1 
ATOM   14442 C  CG1 . ILE C 1 30   ? -18.440  96.680  76.229  1.00 128.79 ? 30   ILE B CG1 1 
ATOM   14443 C  CG2 . ILE C 1 30   ? -16.377  96.361  77.579  1.00 128.91 ? 30   ILE B CG2 1 
ATOM   14444 C  CD1 . ILE C 1 30   ? -19.234  97.210  77.394  1.00 130.58 ? 30   ILE B CD1 1 
ATOM   14445 N  N   . PHE C 1 31   ? -14.653  98.748  77.573  1.00 134.34 ? 31   PHE B N   1 
ATOM   14446 C  CA  . PHE C 1 31   ? -13.205  98.629  77.707  1.00 132.51 ? 31   PHE B CA  1 
ATOM   14447 C  C   . PHE C 1 31   ? -12.791  97.202  78.071  1.00 131.27 ? 31   PHE B C   1 
ATOM   14448 O  O   . PHE C 1 31   ? -13.606  96.319  78.412  1.00 128.13 ? 31   PHE B O   1 
ATOM   14449 C  CB  . PHE C 1 31   ? -12.597  99.617  78.707  1.00 132.26 ? 31   PHE B CB  1 
ATOM   14450 C  CG  . PHE C 1 31   ? -12.902  101.067 78.413  1.00 133.57 ? 31   PHE B CG  1 
ATOM   14451 C  CD1 . PHE C 1 31   ? -13.697  101.819 79.283  1.00 134.32 ? 31   PHE B CD1 1 
ATOM   14452 C  CD2 . PHE C 1 31   ? -12.385  101.694 77.295  1.00 132.95 ? 31   PHE B CD2 1 
ATOM   14453 C  CE1 . PHE C 1 31   ? -13.982  103.156 79.035  1.00 132.94 ? 31   PHE B CE1 1 
ATOM   14454 C  CE2 . PHE C 1 31   ? -12.671  103.035 77.044  1.00 132.82 ? 31   PHE B CE2 1 
ATOM   14455 C  CZ  . PHE C 1 31   ? -13.471  103.759 77.915  1.00 132.76 ? 31   PHE B CZ  1 
ATOM   14456 N  N   . ARG C 1 32   ? -11.489  96.994  77.994  1.00 132.32 ? 32   ARG B N   1 
ATOM   14457 C  CA  . ARG C 1 32   ? -10.906  95.722  78.340  1.00 131.07 ? 32   ARG B CA  1 
ATOM   14458 C  C   . ARG C 1 32   ? -9.653   95.981  79.131  1.00 126.90 ? 32   ARG B C   1 
ATOM   14459 O  O   . ARG C 1 32   ? -8.879   96.909  78.859  1.00 126.36 ? 32   ARG B O   1 
ATOM   14460 C  CB  . ARG C 1 32   ? -10.532  94.929  77.089  1.00 134.36 ? 32   ARG B CB  1 
ATOM   14461 C  CG  . ARG C 1 32   ? -11.692  94.329  76.319  1.00 136.00 ? 32   ARG B CG  1 
ATOM   14462 C  CD  . ARG C 1 32   ? -11.194  93.493  75.109  1.00 136.95 ? 32   ARG B CD  1 
ATOM   14463 N  NE  . ARG C 1 32   ? -12.228  92.583  74.621  1.00 134.46 ? 32   ARG B NE  1 
ATOM   14464 C  CZ  . ARG C 1 32   ? -12.833  92.673  73.446  1.00 132.81 ? 32   ARG B CZ  1 
ATOM   14465 N  NH1 . ARG C 1 32   ? -12.503  93.621  72.571  1.00 133.29 ? 32   ARG B NH1 1 
ATOM   14466 N  NH2 . ARG C 1 32   ? -13.770  91.789  73.157  1.00 131.84 ? 32   ARG B NH2 1 
ATOM   14467 N  N   . VAL C 1 33   ? -9.479   95.136  80.124  1.00 125.22 ? 33   VAL B N   1 
ATOM   14468 C  CA  . VAL C 1 33   ? -8.298   95.117  80.928  1.00 126.91 ? 33   VAL B CA  1 
ATOM   14469 C  C   . VAL C 1 33   ? -7.127   94.676  80.080  1.00 129.07 ? 33   VAL B C   1 
ATOM   14470 O  O   . VAL C 1 33   ? -7.279   93.838  79.208  1.00 128.81 ? 33   VAL B O   1 
ATOM   14471 C  CB  . VAL C 1 33   ? -8.540   94.131  82.024  1.00 126.84 ? 33   VAL B CB  1 
ATOM   14472 C  CG1 . VAL C 1 33   ? -7.490   94.270  83.119  1.00 129.87 ? 33   VAL B CG1 1 
ATOM   14473 C  CG2 . VAL C 1 33   ? -9.953   94.360  82.551  1.00 126.12 ? 33   VAL B CG2 1 
ATOM   14474 N  N   . GLY C 1 34   ? -5.958   95.254  80.315  1.00 134.32 ? 34   GLY B N   1 
ATOM   14475 C  CA  . GLY C 1 34   ? -4.791   94.940  79.509  1.00 139.12 ? 34   GLY B CA  1 
ATOM   14476 C  C   . GLY C 1 34   ? -4.982   95.374  78.070  1.00 142.81 ? 34   GLY B C   1 
ATOM   14477 O  O   . GLY C 1 34   ? -4.186   95.061  77.180  1.00 143.70 ? 34   GLY B O   1 
ATOM   14478 N  N   . ALA C 1 35   ? -6.062   96.098  77.838  1.00 143.98 ? 35   ALA B N   1 
ATOM   14479 C  CA  . ALA C 1 35   ? -6.371   96.509  76.494  1.00 146.05 ? 35   ALA B CA  1 
ATOM   14480 C  C   . ALA C 1 35   ? -5.974   97.945  76.272  1.00 149.93 ? 35   ALA B C   1 
ATOM   14481 O  O   . ALA C 1 35   ? -6.327   98.822  77.067  1.00 148.32 ? 35   ALA B O   1 
ATOM   14482 C  CB  . ALA C 1 35   ? -7.830   96.317  76.215  1.00 144.91 ? 35   ALA B CB  1 
ATOM   14483 N  N   . SER C 1 36   ? -5.241   98.162  75.180  1.00 154.17 ? 36   SER B N   1 
ATOM   14484 C  CA  . SER C 1 36   ? -4.856   99.492  74.734  1.00 156.59 ? 36   SER B CA  1 
ATOM   14485 C  C   . SER C 1 36   ? -6.085   100.120 74.141  1.00 156.66 ? 36   SER B C   1 
ATOM   14486 O  O   . SER C 1 36   ? -6.381   99.909  72.974  1.00 156.78 ? 36   SER B O   1 
ATOM   14487 C  CB  . SER C 1 36   ? -3.797   99.394  73.642  1.00 155.63 ? 36   SER B CB  1 
ATOM   14488 O  OG  . SER C 1 36   ? -3.306   98.071  73.541  1.00 154.24 ? 36   SER B OG  1 
ATOM   14489 N  N   . GLU C 1 37   ? -6.815   100.883 74.937  1.00 157.57 ? 37   GLU B N   1 
ATOM   14490 C  CA  . GLU C 1 37   ? -8.076   101.414 74.456  1.00 158.90 ? 37   GLU B CA  1 
ATOM   14491 C  C   . GLU C 1 37   ? -7.894   102.677 73.611  1.00 157.76 ? 37   GLU B C   1 
ATOM   14492 O  O   . GLU C 1 37   ? -7.477   103.727 74.114  1.00 157.78 ? 37   GLU B O   1 
ATOM   14493 C  CB  . GLU C 1 37   ? -9.068   101.605 75.610  1.00 163.57 ? 37   GLU B CB  1 
ATOM   14494 C  CG  . GLU C 1 37   ? -9.365   100.312 76.400  1.00 168.05 ? 37   GLU B CG  1 
ATOM   14495 C  CD  . GLU C 1 37   ? -10.051  99.234  75.567  1.00 171.74 ? 37   GLU B CD  1 
ATOM   14496 O  OE1 . GLU C 1 37   ? -9.628   98.964  74.414  1.00 172.89 ? 37   GLU B OE1 1 
ATOM   14497 O  OE2 . GLU C 1 37   ? -11.024  98.646  76.076  1.00 172.40 ? 37   GLU B OE2 1 
ATOM   14498 N  N   . ASN C 1 38   ? -8.198   102.541 72.318  1.00 155.74 ? 38   ASN B N   1 
ATOM   14499 C  CA  . ASN C 1 38   ? -8.098   103.636 71.364  1.00 153.79 ? 38   ASN B CA  1 
ATOM   14500 C  C   . ASN C 1 38   ? -9.233   104.645 71.492  1.00 152.50 ? 38   ASN B C   1 
ATOM   14501 O  O   . ASN C 1 38   ? -10.403  104.268 71.488  1.00 151.60 ? 38   ASN B O   1 
ATOM   14502 C  CB  . ASN C 1 38   ? -8.075   103.081 69.951  1.00 151.85 ? 38   ASN B CB  1 
ATOM   14503 C  CG  . ASN C 1 38   ? -6.678   102.832 69.452  1.00 151.50 ? 38   ASN B CG  1 
ATOM   14504 O  OD1 . ASN C 1 38   ? -5.865   102.205 70.128  1.00 151.29 ? 38   ASN B OD1 1 
ATOM   14505 N  ND2 . ASN C 1 38   ? -6.387   103.328 68.257  1.00 150.17 ? 38   ASN B ND2 1 
ATOM   14506 N  N   . ILE C 1 39   ? -8.871   105.927 71.585  1.00 150.99 ? 39   ILE B N   1 
ATOM   14507 C  CA  . ILE C 1 39   ? -9.814   107.028 71.783  1.00 147.57 ? 39   ILE B CA  1 
ATOM   14508 C  C   . ILE C 1 39   ? -9.413   108.253 70.974  1.00 147.13 ? 39   ILE B C   1 
ATOM   14509 O  O   . ILE C 1 39   ? -8.517   108.996 71.378  1.00 146.50 ? 39   ILE B O   1 
ATOM   14510 C  CB  . ILE C 1 39   ? -9.818   107.487 73.249  1.00 148.12 ? 39   ILE B CB  1 
ATOM   14511 C  CG1 . ILE C 1 39   ? -9.748   106.284 74.193  1.00 145.64 ? 39   ILE B CG1 1 
ATOM   14512 C  CG2 . ILE C 1 39   ? -11.016  108.384 73.534  1.00 147.54 ? 39   ILE B CG2 1 
ATOM   14513 C  CD1 . ILE C 1 39   ? -10.887  105.296 74.050  1.00 141.48 ? 39   ILE B CD1 1 
ATOM   14514 N  N   . VAL C 1 40   ? -10.071  108.468 69.835  1.00 148.28 ? 40   VAL B N   1 
ATOM   14515 C  CA  . VAL C 1 40   ? -9.839   109.694 69.070  1.00 151.86 ? 40   VAL B CA  1 
ATOM   14516 C  C   . VAL C 1 40   ? -10.560  110.861 69.716  1.00 155.55 ? 40   VAL B C   1 
ATOM   14517 O  O   . VAL C 1 40   ? -11.606  110.710 70.361  1.00 154.37 ? 40   VAL B O   1 
ATOM   14518 C  CB  . VAL C 1 40   ? -10.239  109.641 67.539  1.00 156.12 ? 40   VAL B CB  1 
ATOM   14519 C  CG1 . VAL C 1 40   ? -9.848   108.321 66.889  1.00 155.63 ? 40   VAL B CG1 1 
ATOM   14520 C  CG2 . VAL C 1 40   ? -11.720  109.969 67.314  1.00 154.61 ? 40   VAL B CG2 1 
ATOM   14521 N  N   . ILE C 1 41   ? -9.967   112.030 69.531  1.00 160.28 ? 41   ILE B N   1 
ATOM   14522 C  CA  . ILE C 1 41   ? -10.589  113.281 69.892  1.00 163.84 ? 41   ILE B CA  1 
ATOM   14523 C  C   . ILE C 1 41   ? -10.358  114.195 68.731  1.00 161.88 ? 41   ILE B C   1 
ATOM   14524 O  O   . ILE C 1 41   ? -9.297   114.206 68.123  1.00 160.50 ? 41   ILE B O   1 
ATOM   14525 C  CB  . ILE C 1 41   ? -9.934   113.929 71.087  1.00 169.49 ? 41   ILE B CB  1 
ATOM   14526 C  CG1 . ILE C 1 41   ? -10.449  115.363 71.234  1.00 172.87 ? 41   ILE B CG1 1 
ATOM   14527 C  CG2 . ILE C 1 41   ? -8.423   113.929 70.914  1.00 172.11 ? 41   ILE B CG2 1 
ATOM   14528 C  CD1 . ILE C 1 41   ? -9.725   116.167 72.289  1.00 175.64 ? 41   ILE B CD1 1 
ATOM   14529 N  N   . GLN C 1 42   ? -11.368  114.981 68.444  1.00 163.56 ? 42   GLN B N   1 
ATOM   14530 C  CA  . GLN C 1 42   ? -11.383  115.787 67.259  1.00 169.34 ? 42   GLN B CA  1 
ATOM   14531 C  C   . GLN C 1 42   ? -12.490  116.746 67.583  1.00 173.41 ? 42   GLN B C   1 
ATOM   14532 O  O   . GLN C 1 42   ? -13.418  116.357 68.293  1.00 172.32 ? 42   GLN B O   1 
ATOM   14533 C  CB  . GLN C 1 42   ? -11.744  114.902 66.069  1.00 170.23 ? 42   GLN B CB  1 
ATOM   14534 C  CG  . GLN C 1 42   ? -12.772  115.481 65.136  1.00 170.94 ? 42   GLN B CG  1 
ATOM   14535 C  CD  . GLN C 1 42   ? -13.757  114.436 64.702  1.00 170.81 ? 42   GLN B CD  1 
ATOM   14536 O  OE1 . GLN C 1 42   ? -14.686  114.736 63.964  1.00 171.47 ? 42   GLN B OE1 1 
ATOM   14537 N  NE2 . GLN C 1 42   ? -13.572  113.198 65.174  1.00 169.17 ? 42   GLN B NE2 1 
ATOM   14538 N  N   . VAL C 1 43   ? -12.405  117.989 67.103  1.00 177.18 ? 43   VAL B N   1 
ATOM   14539 C  CA  . VAL C 1 43   ? -13.359  119.003 67.542  1.00 177.00 ? 43   VAL B CA  1 
ATOM   14540 C  C   . VAL C 1 43   ? -13.441  120.210 66.621  1.00 180.89 ? 43   VAL B C   1 
ATOM   14541 O  O   . VAL C 1 43   ? -12.549  120.429 65.809  1.00 182.48 ? 43   VAL B O   1 
ATOM   14542 C  CB  . VAL C 1 43   ? -13.046  119.439 68.978  1.00 170.84 ? 43   VAL B CB  1 
ATOM   14543 C  CG1 . VAL C 1 43   ? -11.716  120.157 69.021  1.00 170.40 ? 43   VAL B CG1 1 
ATOM   14544 C  CG2 . VAL C 1 43   ? -14.159  120.283 69.527  1.00 168.40 ? 43   VAL B CG2 1 
ATOM   14545 N  N   . TYR C 1 44   ? -14.534  120.963 66.751  1.00 184.21 ? 44   TYR B N   1 
ATOM   14546 C  CA  . TYR C 1 44   ? -14.825  122.133 65.914  1.00 190.47 ? 44   TYR B CA  1 
ATOM   14547 C  C   . TYR C 1 44   ? -14.388  123.504 66.521  1.00 209.53 ? 44   TYR B C   1 
ATOM   14548 O  O   . TYR C 1 44   ? -14.830  124.573 66.075  1.00 206.15 ? 44   TYR B O   1 
ATOM   14549 C  CB  . TYR C 1 44   ? -16.319  122.134 65.535  1.00 199.12 ? 44   TYR B CB  1 
ATOM   14550 C  CG  . TYR C 1 44   ? -16.697  123.064 64.387  1.00 211.19 ? 44   TYR B CG  1 
ATOM   14551 C  CD1 . TYR C 1 44   ? -16.474  122.697 63.056  1.00 215.23 ? 44   TYR B CD1 1 
ATOM   14552 C  CD2 . TYR C 1 44   ? -17.288  124.307 64.633  1.00 217.34 ? 44   TYR B CD2 1 
ATOM   14553 C  CE1 . TYR C 1 44   ? -16.817  123.547 62.010  1.00 217.53 ? 44   TYR B CE1 1 
ATOM   14554 C  CE2 . TYR C 1 44   ? -17.637  125.161 63.588  1.00 219.78 ? 44   TYR B CE2 1 
ATOM   14555 C  CZ  . TYR C 1 44   ? -17.401  124.773 62.281  1.00 219.36 ? 44   TYR B CZ  1 
ATOM   14556 O  OH  . TYR C 1 44   ? -17.748  125.617 61.248  1.00 219.01 ? 44   TYR B OH  1 
ATOM   14557 N  N   . GLY C 1 45   ? -13.511  123.469 67.524  1.00 214.17 ? 45   GLY B N   1 
ATOM   14558 C  CA  . GLY C 1 45   ? -13.037  124.679 68.177  1.00 216.80 ? 45   GLY B CA  1 
ATOM   14559 C  C   . GLY C 1 45   ? -12.384  125.645 67.209  1.00 216.67 ? 45   GLY B C   1 
ATOM   14560 O  O   . GLY C 1 45   ? -11.704  125.242 66.272  1.00 214.02 ? 45   GLY B O   1 
ATOM   14561 N  N   . TYR C 1 46   ? -12.602  126.931 67.446  1.00 221.24 ? 46   TYR B N   1 
ATOM   14562 C  CA  . TYR C 1 46   ? -11.989  128.004 66.661  1.00 224.94 ? 46   TYR B CA  1 
ATOM   14563 C  C   . TYR C 1 46   ? -10.453  127.944 66.621  1.00 225.46 ? 46   TYR B C   1 
ATOM   14564 O  O   . TYR C 1 46   ? -9.856   126.917 66.950  1.00 229.76 ? 46   TYR B O   1 
ATOM   14565 C  CB  . TYR C 1 46   ? -12.438  129.359 67.206  1.00 229.56 ? 46   TYR B CB  1 
ATOM   14566 C  CG  . TYR C 1 46   ? -12.558  129.364 68.711  1.00 234.37 ? 46   TYR B CG  1 
ATOM   14567 C  CD1 . TYR C 1 46   ? -11.440  129.547 69.517  1.00 237.18 ? 46   TYR B CD1 1 
ATOM   14568 C  CD2 . TYR C 1 46   ? -13.787  129.164 69.329  1.00 235.46 ? 46   TYR B CD2 1 
ATOM   14569 C  CE1 . TYR C 1 46   ? -11.545  129.542 70.898  1.00 239.57 ? 46   TYR B CE1 1 
ATOM   14570 C  CE2 . TYR C 1 46   ? -13.903  129.156 70.709  1.00 237.72 ? 46   TYR B CE2 1 
ATOM   14571 C  CZ  . TYR C 1 46   ? -12.779  129.346 71.490  1.00 240.01 ? 46   TYR B CZ  1 
ATOM   14572 O  OH  . TYR C 1 46   ? -12.892  129.337 72.865  1.00 242.23 ? 46   TYR B OH  1 
ATOM   14573 N  N   . THR C 1 47   ? -9.836   129.062 66.226  1.00 220.54 ? 47   THR B N   1 
ATOM   14574 C  CA  . THR C 1 47   ? -8.395   129.153 65.933  1.00 216.98 ? 47   THR B CA  1 
ATOM   14575 C  C   . THR C 1 47   ? -7.506   128.790 67.111  1.00 215.15 ? 47   THR B C   1 
ATOM   14576 O  O   . THR C 1 47   ? -6.459   128.156 66.959  1.00 214.99 ? 47   THR B O   1 
ATOM   14577 C  CB  . THR C 1 47   ? -7.994   130.592 65.499  1.00 268.13 ? 47   THR B CB  1 
ATOM   14578 O  OG1 . THR C 1 47   ? -8.877   131.060 64.471  1.00 266.52 ? 47   THR B OG1 1 
ATOM   14579 C  CG2 . THR C 1 47   ? -6.549   130.629 64.992  1.00 268.81 ? 47   THR B CG2 1 
ATOM   14580 N  N   . GLU C 1 48   ? -7.926   129.217 68.289  1.00 214.16 ? 48   GLU B N   1 
ATOM   14581 C  CA  . GLU C 1 48   ? -7.120   129.036 69.471  1.00 213.54 ? 48   GLU B CA  1 
ATOM   14582 C  C   . GLU C 1 48   ? -6.788   127.571 69.674  1.00 209.38 ? 48   GLU B C   1 
ATOM   14583 O  O   . GLU C 1 48   ? -7.643   126.811 70.107  1.00 208.09 ? 48   GLU B O   1 
ATOM   14584 C  CB  . GLU C 1 48   ? -7.892   129.537 70.684  1.00 215.82 ? 48   GLU B CB  1 
ATOM   14585 C  CG  . GLU C 1 48   ? -7.064   129.594 71.945  1.00 217.76 ? 48   GLU B CG  1 
ATOM   14586 C  CD  . GLU C 1 48   ? -6.134   130.789 71.962  1.00 218.46 ? 48   GLU B CD  1 
ATOM   14587 O  OE1 . GLU C 1 48   ? -6.286   131.673 71.093  1.00 217.71 ? 48   GLU B OE1 1 
ATOM   14588 O  OE2 . GLU C 1 48   ? -5.257   130.850 72.848  1.00 220.30 ? 48   GLU B OE2 1 
ATOM   14589 N  N   . ALA C 1 49   ? -5.555   127.168 69.381  1.00 205.41 ? 49   ALA B N   1 
ATOM   14590 C  CA  . ALA C 1 49   ? -5.106   125.830 69.759  1.00 202.21 ? 49   ALA B CA  1 
ATOM   14591 C  C   . ALA C 1 49   ? -5.564   125.554 71.193  1.00 200.25 ? 49   ALA B C   1 
ATOM   14592 O  O   . ALA C 1 49   ? -5.989   126.477 71.884  1.00 202.71 ? 49   ALA B O   1 
ATOM   14593 C  CB  . ALA C 1 49   ? -3.598   125.730 69.652  1.00 201.85 ? 49   ALA B CB  1 
ATOM   14594 N  N   . PHE C 1 50   ? -5.502   124.301 71.648  1.00 198.29 ? 50   PHE B N   1 
ATOM   14595 C  CA  . PHE C 1 50   ? -5.829   124.002 73.057  1.00 199.58 ? 50   PHE B CA  1 
ATOM   14596 C  C   . PHE C 1 50   ? -5.598   122.558 73.547  1.00 193.79 ? 50   PHE B C   1 
ATOM   14597 O  O   . PHE C 1 50   ? -6.081   121.604 72.948  1.00 190.83 ? 50   PHE B O   1 
ATOM   14598 C  CB  . PHE C 1 50   ? -7.251   124.470 73.402  1.00 206.29 ? 50   PHE B CB  1 
ATOM   14599 C  CG  . PHE C 1 50   ? -8.336   123.568 72.892  1.00 214.17 ? 50   PHE B CG  1 
ATOM   14600 C  CD1 . PHE C 1 50   ? -9.039   122.751 73.766  1.00 217.18 ? 50   PHE B CD1 1 
ATOM   14601 C  CD2 . PHE C 1 50   ? -8.664   123.547 71.539  1.00 216.68 ? 50   PHE B CD2 1 
ATOM   14602 C  CE1 . PHE C 1 50   ? -10.047  121.924 73.300  1.00 218.31 ? 50   PHE B CE1 1 
ATOM   14603 C  CE2 . PHE C 1 50   ? -9.672   122.724 71.061  1.00 217.22 ? 50   PHE B CE2 1 
ATOM   14604 C  CZ  . PHE C 1 50   ? -10.363  121.910 71.942  1.00 217.63 ? 50   PHE B CZ  1 
ATOM   14605 N  N   . ASP C 1 51   ? -4.876   122.424 74.658  1.00 193.09 ? 51   ASP B N   1 
ATOM   14606 C  CA  . ASP C 1 51   ? -4.506   121.122 75.207  1.00 191.40 ? 51   ASP B CA  1 
ATOM   14607 C  C   . ASP C 1 51   ? -5.691   120.205 75.469  1.00 189.52 ? 51   ASP B C   1 
ATOM   14608 O  O   . ASP C 1 51   ? -6.820   120.671 75.650  1.00 189.83 ? 51   ASP B O   1 
ATOM   14609 C  CB  . ASP C 1 51   ? -3.713   121.284 76.506  1.00 191.82 ? 51   ASP B CB  1 
ATOM   14610 C  CG  . ASP C 1 51   ? -2.210   121.243 76.295  1.00 189.53 ? 51   ASP B CG  1 
ATOM   14611 O  OD1 . ASP C 1 51   ? -1.760   121.169 75.137  1.00 187.15 ? 51   ASP B OD1 1 
ATOM   14612 O  OD2 . ASP C 1 51   ? -1.477   121.287 77.307  1.00 190.92 ? 51   ASP B OD2 1 
ATOM   14613 N  N   . ALA C 1 52   ? -5.392   118.901 75.515  1.00 187.38 ? 52   ALA B N   1 
ATOM   14614 C  CA  . ALA C 1 52   ? -6.370   117.819 75.690  1.00 182.17 ? 52   ALA B CA  1 
ATOM   14615 C  C   . ALA C 1 52   ? -5.748   116.602 76.396  1.00 181.48 ? 52   ALA B C   1 
ATOM   14616 O  O   . ALA C 1 52   ? -4.927   115.897 75.810  1.00 181.07 ? 52   ALA B O   1 
ATOM   14617 C  CB  . ALA C 1 52   ? -6.935   117.396 74.336  1.00 178.38 ? 52   ALA B CB  1 
ATOM   14618 N  N   . THR C 1 53   ? -6.141   116.364 77.648  1.00 180.28 ? 53   THR B N   1 
ATOM   14619 C  CA  . THR C 1 53   ? -5.687   115.201 78.419  1.00 179.57 ? 53   THR B CA  1 
ATOM   14620 C  C   . THR C 1 53   ? -6.843   114.264 78.750  1.00 174.17 ? 53   THR B C   1 
ATOM   14621 O  O   . THR C 1 53   ? -7.929   114.703 79.116  1.00 174.00 ? 53   THR B O   1 
ATOM   14622 C  CB  . THR C 1 53   ? -5.009   115.620 79.743  1.00 184.29 ? 53   THR B CB  1 
ATOM   14623 O  OG1 . THR C 1 53   ? -3.616   115.863 79.517  1.00 186.73 ? 53   THR B OG1 1 
ATOM   14624 C  CG2 . THR C 1 53   ? -5.160   114.529 80.799  1.00 184.60 ? 53   THR B CG2 1 
ATOM   14625 N  N   . ILE C 1 54   ? -6.610   112.966 78.646  1.00 171.43 ? 54   ILE B N   1 
ATOM   14626 C  CA  . ILE C 1 54   ? -7.669   112.012 78.910  1.00 167.84 ? 54   ILE B CA  1 
ATOM   14627 C  C   . ILE C 1 54   ? -7.134   111.056 79.948  1.00 166.50 ? 54   ILE B C   1 
ATOM   14628 O  O   . ILE C 1 54   ? -5.946   111.083 80.246  1.00 163.34 ? 54   ILE B O   1 
ATOM   14629 C  CB  . ILE C 1 54   ? -8.047   111.221 77.638  1.00 168.76 ? 54   ILE B CB  1 
ATOM   14630 C  CG1 . ILE C 1 54   ? -8.431   112.154 76.487  1.00 168.54 ? 54   ILE B CG1 1 
ATOM   14631 C  CG2 . ILE C 1 54   ? -9.187   110.255 77.911  1.00 167.41 ? 54   ILE B CG2 1 
ATOM   14632 C  CD1 . ILE C 1 54   ? -8.653   111.411 75.169  1.00 166.99 ? 54   ILE B CD1 1 
ATOM   14633 N  N   . SER C 1 55   ? -8.007   110.218 80.496  1.00 167.44 ? 55   SER B N   1 
ATOM   14634 C  CA  . SER C 1 55   ? -7.604   109.253 81.504  1.00 171.37 ? 55   SER B CA  1 
ATOM   14635 C  C   . SER C 1 55   ? -8.768   108.413 82.008  1.00 172.31 ? 55   SER B C   1 
ATOM   14636 O  O   . SER C 1 55   ? -9.930   108.689 81.707  1.00 170.29 ? 55   SER B O   1 
ATOM   14637 C  CB  . SER C 1 55   ? -6.936   109.973 82.664  1.00 174.13 ? 55   SER B CB  1 
ATOM   14638 O  OG  . SER C 1 55   ? -7.381   111.316 82.726  1.00 175.62 ? 55   SER B OG  1 
ATOM   14639 N  N   . ILE C 1 56   ? -8.436   107.392 82.790  1.00 177.93 ? 56   ILE B N   1 
ATOM   14640 C  CA  . ILE C 1 56   ? -9.409   106.403 83.239  1.00 184.82 ? 56   ILE B CA  1 
ATOM   14641 C  C   . ILE C 1 56   ? -9.597   106.430 84.757  1.00 189.81 ? 56   ILE B C   1 
ATOM   14642 O  O   . ILE C 1 56   ? -8.657   106.137 85.496  1.00 189.62 ? 56   ILE B O   1 
ATOM   14643 C  CB  . ILE C 1 56   ? -8.918   105.018 82.852  1.00 188.79 ? 56   ILE B CB  1 
ATOM   14644 C  CG1 . ILE C 1 56   ? -7.415   104.934 83.141  1.00 192.37 ? 56   ILE B CG1 1 
ATOM   14645 C  CG2 . ILE C 1 56   ? -9.226   104.721 81.363  1.00 191.39 ? 56   ILE B CG2 1 
ATOM   14646 C  CD1 . ILE C 1 56   ? -6.714   103.810 82.408  1.00 193.75 ? 56   ILE B CD1 1 
ATOM   14647 N  N   . LYS C 1 57   ? -10.820  106.735 85.209  1.00 195.06 ? 57   LYS B N   1 
ATOM   14648 C  CA  . LYS C 1 57   ? -11.106  106.978 86.635  1.00 198.97 ? 57   LYS B CA  1 
ATOM   14649 C  C   . LYS C 1 57   ? -12.369  106.280 87.167  1.00 200.43 ? 57   LYS B C   1 
ATOM   14650 O  O   . LYS C 1 57   ? -13.369  106.164 86.469  1.00 200.20 ? 57   LYS B O   1 
ATOM   14651 C  CB  . LYS C 1 57   ? -11.160  108.481 86.928  1.00 200.36 ? 57   LYS B CB  1 
ATOM   14652 C  CG  . LYS C 1 57   ? -9.829   109.190 86.690  1.00 200.80 ? 57   LYS B CG  1 
ATOM   14653 C  CD  . LYS C 1 57   ? -9.922   110.704 86.849  1.00 201.14 ? 57   LYS B CD  1 
ATOM   14654 C  CE  . LYS C 1 57   ? -8.583   111.363 86.533  1.00 202.02 ? 57   LYS B CE  1 
ATOM   14655 N  NZ  . LYS C 1 57   ? -8.520   112.779 86.972  1.00 203.36 ? 57   LYS B NZ  1 
ATOM   14656 N  N   . SER C 1 58   ? -12.311  105.876 88.435  1.00 201.67 ? 58   SER B N   1 
ATOM   14657 C  CA  . SER C 1 58   ? -13.092  104.753 88.981  1.00 201.06 ? 58   SER B CA  1 
ATOM   14658 C  C   . SER C 1 58   ? -14.481  105.031 89.566  1.00 200.82 ? 58   SER B C   1 
ATOM   14659 O  O   . SER C 1 58   ? -14.598  105.661 90.611  1.00 202.14 ? 58   SER B O   1 
ATOM   14660 C  CB  . SER C 1 58   ? -12.250  104.076 90.063  1.00 204.29 ? 58   SER B CB  1 
ATOM   14661 O  OG  . SER C 1 58   ? -11.715  105.042 90.964  1.00 207.06 ? 58   SER B OG  1 
ATOM   14662 N  N   . TYR C 1 59   ? -15.514  104.481 88.937  1.00 197.38 ? 59   TYR B N   1 
ATOM   14663 C  CA  . TYR C 1 59   ? -16.908  104.762 89.303  1.00 196.67 ? 59   TYR B CA  1 
ATOM   14664 C  C   . TYR C 1 59   ? -17.158  106.152 89.961  1.00 227.30 ? 59   TYR B C   1 
ATOM   14665 O  O   . TYR C 1 59   ? -16.687  107.154 89.420  1.00 229.27 ? 59   TYR B O   1 
ATOM   14666 C  CB  . TYR C 1 59   ? -17.579  103.580 90.007  1.00 193.69 ? 59   TYR B CB  1 
ATOM   14667 C  CG  . TYR C 1 59   ? -19.046  103.511 89.653  1.00 190.41 ? 59   TYR B CG  1 
ATOM   14668 C  CD1 . TYR C 1 59   ? -19.545  104.248 88.586  1.00 188.89 ? 59   TYR B CD1 1 
ATOM   14669 C  CD2 . TYR C 1 59   ? -19.926  102.717 90.365  1.00 188.49 ? 59   TYR B CD2 1 
ATOM   14670 C  CE1 . TYR C 1 59   ? -20.878  104.212 88.242  1.00 186.83 ? 59   TYR B CE1 1 
ATOM   14671 C  CE2 . TYR C 1 59   ? -21.269  102.663 90.021  1.00 186.42 ? 59   TYR B CE2 1 
ATOM   14672 C  CZ  . TYR C 1 59   ? -21.738  103.415 88.958  1.00 185.70 ? 59   TYR B CZ  1 
ATOM   14673 O  OH  . TYR C 1 59   ? -23.071  103.368 88.617  1.00 183.89 ? 59   TYR B OH  1 
ATOM   14674 N  N   . PRO C 1 60   ? -17.896  106.243 91.098  1.00 225.22 ? 60   PRO B N   1 
ATOM   14675 C  CA  . PRO C 1 60   ? -18.266  107.630 91.453  1.00 223.64 ? 60   PRO B CA  1 
ATOM   14676 C  C   . PRO C 1 60   ? -17.169  108.509 92.098  1.00 220.35 ? 60   PRO B C   1 
ATOM   14677 O  O   . PRO C 1 60   ? -17.366  109.711 92.222  1.00 220.69 ? 60   PRO B O   1 
ATOM   14678 C  CB  . PRO C 1 60   ? -19.454  107.444 92.414  1.00 224.14 ? 60   PRO B CB  1 
ATOM   14679 C  CG  . PRO C 1 60   ? -19.829  105.957 92.320  1.00 222.91 ? 60   PRO B CG  1 
ATOM   14680 C  CD  . PRO C 1 60   ? -18.537  105.277 92.008  1.00 223.59 ? 60   PRO B CD  1 
ATOM   14681 N  N   . ASP C 1 61   ? -16.050  107.921 92.504  1.00 217.84 ? 61   ASP B N   1 
ATOM   14682 C  CA  . ASP C 1 61   ? -14.926  108.677 93.045  1.00 217.31 ? 61   ASP B CA  1 
ATOM   14683 C  C   . ASP C 1 61   ? -13.845  108.843 91.991  1.00 215.19 ? 61   ASP B C   1 
ATOM   14684 O  O   . ASP C 1 61   ? -13.200  107.873 91.608  1.00 214.16 ? 61   ASP B O   1 
ATOM   14685 C  CB  . ASP C 1 61   ? -14.319  107.938 94.237  1.00 218.94 ? 61   ASP B CB  1 
ATOM   14686 C  CG  . ASP C 1 61   ? -13.618  106.636 93.830  1.00 218.58 ? 61   ASP B CG  1 
ATOM   14687 O  OD1 . ASP C 1 61   ? -12.382  106.543 94.003  1.00 220.63 ? 61   ASP B OD1 1 
ATOM   14688 O  OD2 . ASP C 1 61   ? -14.294  105.710 93.321  1.00 216.22 ? 61   ASP B OD2 1 
ATOM   14689 N  N   . LYS C 1 62   ? -13.624  110.064 91.525  1.00 216.23 ? 62   LYS B N   1 
ATOM   14690 C  CA  . LYS C 1 62   ? -12.574  110.293 90.530  1.00 215.19 ? 62   LYS B CA  1 
ATOM   14691 C  C   . LYS C 1 62   ? -11.168  110.274 91.149  1.00 217.96 ? 62   LYS B C   1 
ATOM   14692 O  O   . LYS C 1 62   ? -10.309  111.086 90.792  1.00 220.72 ? 62   LYS B O   1 
ATOM   14693 C  CB  . LYS C 1 62   ? -12.835  111.582 89.727  1.00 213.05 ? 62   LYS B CB  1 
ATOM   14694 C  CG  . LYS C 1 62   ? -13.729  111.361 88.500  1.00 206.33 ? 62   LYS B CG  1 
ATOM   14695 C  CD  . LYS C 1 62   ? -14.530  112.595 88.089  1.00 201.86 ? 62   LYS B CD  1 
ATOM   14696 C  CE  . LYS C 1 62   ? -15.658  112.183 87.148  1.00 196.12 ? 62   LYS B CE  1 
ATOM   14697 N  NZ  . LYS C 1 62   ? -16.567  113.290 86.762  1.00 193.97 ? 62   LYS B NZ  1 
ATOM   14698 N  N   . LYS C 1 63   ? -10.943  109.338 92.074  1.00 215.59 ? 63   LYS B N   1 
ATOM   14699 C  CA  . LYS C 1 63   ? -9.654   109.218 92.764  1.00 215.63 ? 63   LYS B CA  1 
ATOM   14700 C  C   . LYS C 1 63   ? -8.599   108.435 91.974  1.00 213.34 ? 63   LYS B C   1 
ATOM   14701 O  O   . LYS C 1 63   ? -7.576   108.995 91.578  1.00 213.98 ? 63   LYS B O   1 
ATOM   14702 C  CB  . LYS C 1 63   ? -9.829   108.618 94.164  1.00 217.27 ? 63   LYS B CB  1 
ATOM   14703 C  CG  . LYS C 1 63   ? -10.640  109.490 95.126  1.00 220.78 ? 63   LYS B CG  1 
ATOM   14704 C  CD  . LYS C 1 63   ? -10.065  110.902 95.266  1.00 225.38 ? 63   LYS B CD  1 
ATOM   14705 C  CE  . LYS C 1 63   ? -8.766   110.914 96.053  1.00 228.74 ? 63   LYS B CE  1 
ATOM   14706 N  NZ  . LYS C 1 63   ? -8.074   112.224 95.934  1.00 231.16 ? 63   LYS B NZ  1 
ATOM   14707 N  N   . PHE C 1 64   ? -8.833   107.145 91.750  1.00 209.04 ? 64   PHE B N   1 
ATOM   14708 C  CA  . PHE C 1 64   ? -7.883   106.355 90.975  1.00 205.76 ? 64   PHE B CA  1 
ATOM   14709 C  C   . PHE C 1 64   ? -7.901   106.798 89.522  1.00 204.07 ? 64   PHE B C   1 
ATOM   14710 O  O   . PHE C 1 64   ? -8.971   106.931 88.935  1.00 203.81 ? 64   PHE B O   1 
ATOM   14711 C  CB  . PHE C 1 64   ? -8.200   104.864 91.075  1.00 200.07 ? 64   PHE B CB  1 
ATOM   14712 C  CG  . PHE C 1 64   ? -7.250   104.090 91.960  1.00 197.47 ? 64   PHE B CG  1 
ATOM   14713 C  CD1 . PHE C 1 64   ? -7.659   103.617 93.205  1.00 195.82 ? 64   PHE B CD1 1 
ATOM   14714 C  CD2 . PHE C 1 64   ? -5.951   103.823 91.541  1.00 196.36 ? 64   PHE B CD2 1 
ATOM   14715 C  CE1 . PHE C 1 64   ? -6.788   102.898 94.014  1.00 194.73 ? 64   PHE B CE1 1 
ATOM   14716 C  CE2 . PHE C 1 64   ? -5.076   103.105 92.345  1.00 195.39 ? 64   PHE B CE2 1 
ATOM   14717 C  CZ  . PHE C 1 64   ? -5.495   102.643 93.583  1.00 195.01 ? 64   PHE B CZ  1 
ATOM   14718 N  N   . SER C 1 65   ? -6.719   107.040 88.952  1.00 205.56 ? 65   SER B N   1 
ATOM   14719 C  CA  . SER C 1 65   ? -6.588   107.301 87.509  1.00 206.14 ? 65   SER B CA  1 
ATOM   14720 C  C   . SER C 1 65   ? -5.431   106.476 86.929  1.00 205.43 ? 65   SER B C   1 
ATOM   14721 O  O   . SER C 1 65   ? -4.257   106.862 87.000  1.00 208.14 ? 65   SER B O   1 
ATOM   14722 C  CB  . SER C 1 65   ? -6.409   108.795 87.198  1.00 209.97 ? 65   SER B CB  1 
ATOM   14723 O  OG  . SER C 1 65   ? -5.162   109.068 86.575  1.00 212.86 ? 65   SER B OG  1 
ATOM   14724 N  N   . TYR C 1 66   ? -5.788   105.334 86.347  1.00 200.72 ? 66   TYR B N   1 
ATOM   14725 C  CA  . TYR C 1 66   ? -4.820   104.299 86.002  1.00 194.88 ? 66   TYR B CA  1 
ATOM   14726 C  C   . TYR C 1 66   ? -3.819   104.860 85.002  1.00 196.35 ? 66   TYR B C   1 
ATOM   14727 O  O   . TYR C 1 66   ? -2.601   104.754 85.192  1.00 196.27 ? 66   TYR B O   1 
ATOM   14728 C  CB  . TYR C 1 66   ? -5.551   103.052 85.483  1.00 185.28 ? 66   TYR B CB  1 
ATOM   14729 C  CG  . TYR C 1 66   ? -6.831   102.755 86.258  1.00 177.55 ? 66   TYR B CG  1 
ATOM   14730 C  CD1 . TYR C 1 66   ? -6.847   101.823 87.306  1.00 174.02 ? 66   TYR B CD1 1 
ATOM   14731 C  CD2 . TYR C 1 66   ? -8.018   103.423 85.960  1.00 173.10 ? 66   TYR B CD2 1 
ATOM   14732 C  CE1 . TYR C 1 66   ? -8.018   101.558 88.026  1.00 170.24 ? 66   TYR B CE1 1 
ATOM   14733 C  CE2 . TYR C 1 66   ? -9.189   103.163 86.671  1.00 170.00 ? 66   TYR B CE2 1 
ATOM   14734 C  CZ  . TYR C 1 66   ? -9.185   102.228 87.702  1.00 167.55 ? 66   TYR B CZ  1 
ATOM   14735 O  OH  . TYR C 1 66   ? -10.345  101.966 88.409  1.00 163.21 ? 66   TYR B OH  1 
ATOM   14736 N  N   . SER C 1 67   ? -4.342   105.513 83.970  1.00 195.76 ? 67   SER B N   1 
ATOM   14737 C  CA  . SER C 1 67   ? -3.497   106.174 82.990  1.00 194.63 ? 67   SER B CA  1 
ATOM   14738 C  C   . SER C 1 67   ? -4.235   107.276 82.257  1.00 191.74 ? 67   SER B C   1 
ATOM   14739 O  O   . SER C 1 67   ? -5.431   107.489 82.461  1.00 189.76 ? 67   SER B O   1 
ATOM   14740 C  CB  . SER C 1 67   ? -2.903   105.167 82.000  1.00 193.40 ? 67   SER B CB  1 
ATOM   14741 O  OG  . SER C 1 67   ? -3.896   104.321 81.446  1.00 190.71 ? 67   SER B OG  1 
ATOM   14742 N  N   . SER C 1 68   ? -3.494   107.955 81.390  1.00 192.52 ? 68   SER B N   1 
ATOM   14743 C  CA  . SER C 1 68   ? -3.931   109.202 80.784  1.00 194.91 ? 68   SER B CA  1 
ATOM   14744 C  C   . SER C 1 68   ? -3.095   109.527 79.547  1.00 197.63 ? 68   SER B C   1 
ATOM   14745 O  O   . SER C 1 68   ? -2.345   108.681 79.057  1.00 194.40 ? 68   SER B O   1 
ATOM   14746 C  CB  . SER C 1 68   ? -3.811   110.337 81.803  1.00 198.70 ? 68   SER B CB  1 
ATOM   14747 O  OG  . SER C 1 68   ? -2.558   110.306 82.469  1.00 202.02 ? 68   SER B OG  1 
ATOM   14748 N  N   . GLY C 1 69   ? -3.224   110.751 79.043  1.00 203.04 ? 69   GLY B N   1 
ATOM   14749 C  CA  . GLY C 1 69   ? -2.454   111.161 77.885  1.00 208.12 ? 69   GLY B CA  1 
ATOM   14750 C  C   . GLY C 1 69   ? -2.566   112.634 77.559  1.00 210.37 ? 69   GLY B C   1 
ATOM   14751 O  O   . GLY C 1 69   ? -3.664   113.171 77.443  1.00 210.49 ? 69   GLY B O   1 
ATOM   14752 N  N   . HIS C 1 70   ? -1.416   113.280 77.407  1.00 214.12 ? 70   HIS B N   1 
ATOM   14753 C  CA  . HIS C 1 70   ? -1.348   114.710 77.123  1.00 216.89 ? 70   HIS B CA  1 
ATOM   14754 C  C   . HIS C 1 70   ? -1.218   114.928 75.621  1.00 212.96 ? 70   HIS B C   1 
ATOM   14755 O  O   . HIS C 1 70   ? -0.120   115.117 75.103  1.00 211.42 ? 70   HIS B O   1 
ATOM   14756 C  CB  . HIS C 1 70   ? -0.145   115.320 77.845  1.00 225.84 ? 70   HIS B CB  1 
ATOM   14757 C  CG  . HIS C 1 70   ? -0.348   116.737 78.286  1.00 235.02 ? 70   HIS B CG  1 
ATOM   14758 N  ND1 . HIS C 1 70   ? -1.093   117.073 79.396  1.00 238.49 ? 70   HIS B ND1 1 
ATOM   14759 C  CD2 . HIS C 1 70   ? 0.124    117.903 77.783  1.00 238.96 ? 70   HIS B CD2 1 
ATOM   14760 C  CE1 . HIS C 1 70   ? -1.085   118.386 79.551  1.00 241.66 ? 70   HIS B CE1 1 
ATOM   14761 N  NE2 . HIS C 1 70   ? -0.352   118.912 78.587  1.00 242.16 ? 70   HIS B NE2 1 
ATOM   14762 N  N   . VAL C 1 71   ? -2.348   114.910 74.927  1.00 210.69 ? 71   VAL B N   1 
ATOM   14763 C  CA  . VAL C 1 71   ? -2.359   114.971 73.472  1.00 208.06 ? 71   VAL B CA  1 
ATOM   14764 C  C   . VAL C 1 71   ? -2.938   116.291 72.944  1.00 209.08 ? 71   VAL B C   1 
ATOM   14765 O  O   . VAL C 1 71   ? -4.153   116.480 72.873  1.00 206.97 ? 71   VAL B O   1 
ATOM   14766 C  CB  . VAL C 1 71   ? -3.107   113.760 72.913  1.00 204.23 ? 71   VAL B CB  1 
ATOM   14767 C  CG1 . VAL C 1 71   ? -2.587   112.488 73.583  1.00 202.57 ? 71   VAL B CG1 1 
ATOM   14768 C  CG2 . VAL C 1 71   ? -4.597   113.894 73.162  1.00 202.02 ? 71   VAL B CG2 1 
ATOM   14769 N  N   . HIS C 1 72   ? -2.049   117.200 72.565  1.00 213.19 ? 72   HIS B N   1 
ATOM   14770 C  CA  . HIS C 1 72   ? -2.436   118.583 72.297  1.00 218.11 ? 72   HIS B CA  1 
ATOM   14771 C  C   . HIS C 1 72   ? -2.779   118.877 70.853  1.00 216.35 ? 72   HIS B C   1 
ATOM   14772 O  O   . HIS C 1 72   ? -1.889   119.069 70.033  1.00 216.47 ? 72   HIS B O   1 
ATOM   14773 C  CB  . HIS C 1 72   ? -1.319   119.539 72.714  1.00 225.93 ? 72   HIS B CB  1 
ATOM   14774 C  CG  . HIS C 1 72   ? -1.474   120.918 72.155  1.00 232.63 ? 72   HIS B CG  1 
ATOM   14775 N  ND1 . HIS C 1 72   ? -2.241   121.886 72.767  1.00 236.04 ? 72   HIS B ND1 1 
ATOM   14776 C  CD2 . HIS C 1 72   ? -0.976   121.489 71.033  1.00 234.82 ? 72   HIS B CD2 1 
ATOM   14777 C  CE1 . HIS C 1 72   ? -2.201   122.996 72.051  1.00 237.58 ? 72   HIS B CE1 1 
ATOM   14778 N  NE2 . HIS C 1 72   ? -1.440   122.781 70.993  1.00 236.86 ? 72   HIS B NE2 1 
ATOM   14779 N  N   . LEU C 1 73   ? -4.066   118.960 70.547  1.00 216.79 ? 73   LEU B N   1 
ATOM   14780 C  CA  . LEU C 1 73   ? -4.491   119.310 69.196  1.00 217.06 ? 73   LEU B CA  1 
ATOM   14781 C  C   . LEU C 1 73   ? -4.241   120.787 68.898  1.00 223.02 ? 73   LEU B C   1 
ATOM   14782 O  O   . LEU C 1 73   ? -3.714   121.519 69.735  1.00 223.23 ? 73   LEU B O   1 
ATOM   14783 C  CB  . LEU C 1 73   ? -5.965   118.972 68.995  1.00 212.90 ? 73   LEU B CB  1 
ATOM   14784 C  CG  . LEU C 1 73   ? -6.778   119.036 70.286  1.00 210.89 ? 73   LEU B CG  1 
ATOM   14785 C  CD1 . LEU C 1 73   ? -8.238   119.343 69.994  1.00 208.56 ? 73   LEU B CD1 1 
ATOM   14786 C  CD2 . LEU C 1 73   ? -6.621   117.734 71.063  1.00 210.19 ? 73   LEU B CD2 1 
ATOM   14787 N  N   . SER C 1 74   ? -4.619   121.205 67.693  1.00 226.91 ? 74   SER B N   1 
ATOM   14788 C  CA  . SER C 1 74   ? -4.421   122.568 67.217  1.00 231.54 ? 74   SER B CA  1 
ATOM   14789 C  C   . SER C 1 74   ? -4.988   122.640 65.812  1.00 234.45 ? 74   SER B C   1 
ATOM   14790 O  O   . SER C 1 74   ? -5.436   121.629 65.287  1.00 235.57 ? 74   SER B O   1 
ATOM   14791 C  CB  . SER C 1 74   ? -2.935   122.921 67.192  1.00 232.08 ? 74   SER B CB  1 
ATOM   14792 O  OG  . SER C 1 74   ? -2.247   122.185 66.197  1.00 229.75 ? 74   SER B OG  1 
ATOM   14793 N  N   . SER C 1 75   ? -4.972   123.819 65.198  1.00 236.81 ? 75   SER B N   1 
ATOM   14794 C  CA  . SER C 1 75   ? -5.397   123.962 63.799  1.00 239.94 ? 75   SER B CA  1 
ATOM   14795 C  C   . SER C 1 75   ? -4.467   123.201 62.848  1.00 239.03 ? 75   SER B C   1 
ATOM   14796 O  O   . SER C 1 75   ? -4.761   123.046 61.659  1.00 237.27 ? 75   SER B O   1 
ATOM   14797 C  CB  . SER C 1 75   ? -5.462   125.439 63.385  1.00 244.12 ? 75   SER B CB  1 
ATOM   14798 O  OG  . SER C 1 75   ? -6.726   126.018 63.669  1.00 246.52 ? 75   SER B OG  1 
ATOM   14799 N  N   . GLU C 1 76   ? -3.341   122.740 63.386  1.00 240.58 ? 76   GLU B N   1 
ATOM   14800 C  CA  . GLU C 1 76   ? -2.334   122.007 62.622  1.00 237.86 ? 76   GLU B CA  1 
ATOM   14801 C  C   . GLU C 1 76   ? -2.683   120.525 62.529  1.00 229.88 ? 76   GLU B C   1 
ATOM   14802 O  O   . GLU C 1 76   ? -2.440   119.875 61.515  1.00 230.11 ? 76   GLU B O   1 
ATOM   14803 C  CB  . GLU C 1 76   ? -0.977   122.175 63.301  1.00 241.61 ? 76   GLU B CB  1 
ATOM   14804 C  CG  . GLU C 1 76   ? 0.122    121.287 62.770  1.00 241.95 ? 76   GLU B CG  1 
ATOM   14805 C  CD  . GLU C 1 76   ? 1.356    121.344 63.643  1.00 243.51 ? 76   GLU B CD  1 
ATOM   14806 O  OE1 . GLU C 1 76   ? 1.237    121.758 64.821  1.00 244.60 ? 76   GLU B OE1 1 
ATOM   14807 O  OE2 . GLU C 1 76   ? 2.442    120.976 63.150  1.00 243.48 ? 76   GLU B OE2 1 
ATOM   14808 N  N   . ASN C 1 77   ? -3.235   120.011 63.622  1.00 221.92 ? 77   ASN B N   1 
ATOM   14809 C  CA  . ASN C 1 77   ? -3.720   118.646 63.732  1.00 211.32 ? 77   ASN B CA  1 
ATOM   14810 C  C   . ASN C 1 77   ? -5.229   118.639 63.490  1.00 198.97 ? 77   ASN B C   1 
ATOM   14811 O  O   . ASN C 1 77   ? -5.938   117.767 63.980  1.00 193.32 ? 77   ASN B O   1 
ATOM   14812 C  CB  . ASN C 1 77   ? -3.412   118.118 65.144  1.00 218.49 ? 77   ASN B CB  1 
ATOM   14813 C  CG  . ASN C 1 77   ? -3.286   116.598 65.205  1.00 224.33 ? 77   ASN B CG  1 
ATOM   14814 O  OD1 . ASN C 1 77   ? -3.653   115.885 64.269  1.00 226.01 ? 77   ASN B OD1 1 
ATOM   14815 N  ND2 . ASN C 1 77   ? -2.767   116.098 66.323  1.00 227.13 ? 77   ASN B ND2 1 
ATOM   14816 N  N   . LYS C 1 78   ? -5.716   119.634 62.756  1.00 191.97 ? 78   LYS B N   1 
ATOM   14817 C  CA  . LYS C 1 78   ? -7.151   119.818 62.546  1.00 181.47 ? 78   LYS B CA  1 
ATOM   14818 C  C   . LYS C 1 78   ? -7.965   119.550 63.800  1.00 177.13 ? 78   LYS B C   1 
ATOM   14819 O  O   . LYS C 1 78   ? -9.140   119.185 63.738  1.00 173.90 ? 78   LYS B O   1 
ATOM   14820 C  CB  . LYS C 1 78   ? -7.642   118.950 61.409  1.00 174.21 ? 78   LYS B CB  1 
ATOM   14821 C  CG  . LYS C 1 78   ? -6.931   119.228 60.121  1.00 162.34 ? 78   LYS B CG  1 
ATOM   14822 C  CD  . LYS C 1 78   ? -7.012   120.687 59.797  1.00 154.53 ? 78   LYS B CD  1 
ATOM   14823 C  CE  . LYS C 1 78   ? -6.314   120.962 58.495  1.00 147.44 ? 78   LYS B CE  1 
ATOM   14824 N  NZ  . LYS C 1 78   ? -5.946   122.398 58.361  1.00 146.33 ? 78   LYS B NZ  1 
ATOM   14825 N  N   . PHE C 1 79   ? -7.323   119.740 64.942  1.00 175.24 ? 79   PHE B N   1 
ATOM   14826 C  CA  . PHE C 1 79   ? -7.970   119.546 66.223  1.00 174.04 ? 79   PHE B CA  1 
ATOM   14827 C  C   . PHE C 1 79   ? -8.483   118.140 66.260  1.00 175.70 ? 79   PHE B C   1 
ATOM   14828 O  O   . PHE C 1 79   ? -9.691   117.923 66.225  1.00 175.73 ? 79   PHE B O   1 
ATOM   14829 C  CB  . PHE C 1 79   ? -9.111   120.541 66.414  1.00 173.65 ? 79   PHE B CB  1 
ATOM   14830 C  CG  . PHE C 1 79   ? -8.639   121.962 66.612  1.00 176.52 ? 79   PHE B CG  1 
ATOM   14831 C  CD1 . PHE C 1 79   ? -8.924   122.942 65.676  1.00 176.52 ? 79   PHE B CD1 1 
ATOM   14832 C  CD2 . PHE C 1 79   ? -7.895   122.311 67.728  1.00 179.33 ? 79   PHE B CD2 1 
ATOM   14833 C  CE1 . PHE C 1 79   ? -8.494   124.227 65.854  1.00 177.22 ? 79   PHE B CE1 1 
ATOM   14834 C  CE2 . PHE C 1 79   ? -7.464   123.595 67.902  1.00 180.23 ? 79   PHE B CE2 1 
ATOM   14835 C  CZ  . PHE C 1 79   ? -7.762   124.553 66.964  1.00 179.46 ? 79   PHE B CZ  1 
ATOM   14836 N  N   . GLN C 1 80   ? -7.542   117.194 66.307  1.00 178.58 ? 80   GLN B N   1 
ATOM   14837 C  CA  . GLN C 1 80   ? -7.818   115.753 66.339  1.00 179.28 ? 80   GLN B CA  1 
ATOM   14838 C  C   . GLN C 1 80   ? -6.602   115.008 66.891  1.00 179.80 ? 80   GLN B C   1 
ATOM   14839 O  O   . GLN C 1 80   ? -5.466   115.380 66.608  1.00 180.88 ? 80   GLN B O   1 
ATOM   14840 C  CB  . GLN C 1 80   ? -8.112   115.227 64.935  1.00 180.32 ? 80   GLN B CB  1 
ATOM   14841 C  CG  . GLN C 1 80   ? -9.143   116.027 64.163  1.00 180.97 ? 80   GLN B CG  1 
ATOM   14842 C  CD  . GLN C 1 80   ? -9.741   115.238 63.024  1.00 179.84 ? 80   GLN B CD  1 
ATOM   14843 O  OE1 . GLN C 1 80   ? -9.056   114.455 62.368  1.00 179.92 ? 80   GLN B OE1 1 
ATOM   14844 N  NE2 . GLN C 1 80   ? -11.028  115.439 62.782  1.00 179.07 ? 80   GLN B NE2 1 
ATOM   14845 N  N   . ASN C 1 81   ? -6.822   113.950 67.662  1.00 178.77 ? 81   ASN B N   1 
ATOM   14846 C  CA  . ASN C 1 81   ? -5.693   113.272 68.298  1.00 180.21 ? 81   ASN B CA  1 
ATOM   14847 C  C   . ASN C 1 81   ? -6.055   111.926 68.925  1.00 176.27 ? 81   ASN B C   1 
ATOM   14848 O  O   . ASN C 1 81   ? -7.211   111.524 68.948  1.00 172.62 ? 81   ASN B O   1 
ATOM   14849 C  CB  . ASN C 1 81   ? -5.053   114.198 69.338  1.00 186.03 ? 81   ASN B CB  1 
ATOM   14850 C  CG  . ASN C 1 81   ? -3.541   114.256 69.222  1.00 189.92 ? 81   ASN B CG  1 
ATOM   14851 O  OD1 . ASN C 1 81   ? -2.879   113.249 68.960  1.00 189.94 ? 81   ASN B OD1 1 
ATOM   14852 N  ND2 . ASN C 1 81   ? -2.986   115.445 69.420  1.00 192.80 ? 81   ASN B ND2 1 
ATOM   14853 N  N   . SER C 1 82   ? -5.065   111.225 69.443  1.00 176.12 ? 82   SER B N   1 
ATOM   14854 C  CA  . SER C 1 82   ? -5.323   109.894 69.928  1.00 176.84 ? 82   SER B CA  1 
ATOM   14855 C  C   . SER C 1 82   ? -4.504   109.532 71.141  1.00 179.45 ? 82   SER B C   1 
ATOM   14856 O  O   . SER C 1 82   ? -3.414   110.052 71.335  1.00 182.74 ? 82   SER B O   1 
ATOM   14857 C  CB  . SER C 1 82   ? -5.089   108.899 68.812  1.00 175.98 ? 82   SER B CB  1 
ATOM   14858 O  OG  . SER C 1 82   ? -6.291   108.235 68.480  1.00 175.33 ? 82   SER B OG  1 
ATOM   14859 N  N   . ALA C 1 83   ? -5.032   108.635 71.964  1.00 179.12 ? 83   ALA B N   1 
ATOM   14860 C  CA  . ALA C 1 83   ? -4.358   108.283 73.202  1.00 180.90 ? 83   ALA B CA  1 
ATOM   14861 C  C   . ALA C 1 83   ? -4.556   106.814 73.541  1.00 180.01 ? 83   ALA B C   1 
ATOM   14862 O  O   . ALA C 1 83   ? -5.642   106.266 73.363  1.00 181.86 ? 83   ALA B O   1 
ATOM   14863 C  CB  . ALA C 1 83   ? -4.861   109.163 74.334  1.00 180.48 ? 83   ALA B CB  1 
ATOM   14864 N  N   . ILE C 1 84   ? -3.495   106.173 74.020  1.00 179.74 ? 84   ILE B N   1 
ATOM   14865 C  CA  . ILE C 1 84   ? -3.611   104.813 74.532  1.00 176.87 ? 84   ILE B CA  1 
ATOM   14866 C  C   . ILE C 1 84   ? -3.746   104.787 76.069  1.00 176.86 ? 84   ILE B C   1 
ATOM   14867 O  O   . ILE C 1 84   ? -2.765   104.587 76.798  1.00 177.58 ? 84   ILE B O   1 
ATOM   14868 C  CB  . ILE C 1 84   ? -2.457   103.894 74.045  1.00 235.80 ? 84   ILE B CB  1 
ATOM   14869 C  CG1 . ILE C 1 84   ? -1.092   104.485 74.406  1.00 237.23 ? 84   ILE B CG1 1 
ATOM   14870 C  CG2 . ILE C 1 84   ? -2.556   103.658 72.540  1.00 234.37 ? 84   ILE B CG2 1 
ATOM   14871 C  CD1 . ILE C 1 84   ? 0.045    103.507 74.262  1.00 236.90 ? 84   ILE B CD1 1 
ATOM   14872 N  N   . LEU C 1 85   ? -4.973   105.012 76.544  1.00 174.97 ? 85   LEU B N   1 
ATOM   14873 C  CA  . LEU C 1 85   ? -5.334   104.777 77.938  1.00 171.52 ? 85   LEU B CA  1 
ATOM   14874 C  C   . LEU C 1 85   ? -5.162   103.300 78.150  1.00 166.26 ? 85   LEU B C   1 
ATOM   14875 O  O   . LEU C 1 85   ? -4.745   102.588 77.235  1.00 164.89 ? 85   LEU B O   1 
ATOM   14876 C  CB  . LEU C 1 85   ? -6.793   105.150 78.199  1.00 170.73 ? 85   LEU B CB  1 
ATOM   14877 C  CG  . LEU C 1 85   ? -7.056   106.617 77.894  1.00 171.39 ? 85   LEU B CG  1 
ATOM   14878 C  CD1 . LEU C 1 85   ? -5.844   107.400 78.350  1.00 173.79 ? 85   LEU B CD1 1 
ATOM   14879 C  CD2 . LEU C 1 85   ? -7.300   106.857 76.412  1.00 169.66 ? 85   LEU B CD2 1 
ATOM   14880 N  N   . THR C 1 86   ? -5.492   102.817 79.335  1.00 160.68 ? 86   THR B N   1 
ATOM   14881 C  CA  . THR C 1 86   ? -5.364   101.391 79.536  1.00 157.66 ? 86   THR B CA  1 
ATOM   14882 C  C   . THR C 1 86   ? -5.529   100.971 80.996  1.00 155.06 ? 86   THR B C   1 
ATOM   14883 O  O   . THR C 1 86   ? -4.655   101.201 81.841  1.00 156.57 ? 86   THR B O   1 
ATOM   14884 C  CB  . THR C 1 86   ? -4.043   100.866 78.889  1.00 142.50 ? 86   THR B CB  1 
ATOM   14885 O  OG1 . THR C 1 86   ? -4.214   99.517  78.445  1.00 141.67 ? 86   THR B OG1 1 
ATOM   14886 C  CG2 . THR C 1 86   ? -2.860   100.983 79.837  1.00 144.49 ? 86   THR B CG2 1 
ATOM   14887 N  N   . ILE C 1 87   ? -6.682   100.367 81.272  1.00 154.04 ? 87   ILE B N   1 
ATOM   14888 C  CA  . ILE C 1 87   ? -7.021   99.875  82.592  1.00 154.52 ? 87   ILE B CA  1 
ATOM   14889 C  C   . ILE C 1 87   ? -6.328   98.561  82.851  1.00 167.99 ? 87   ILE B C   1 
ATOM   14890 O  O   . ILE C 1 87   ? -6.740   97.544  82.314  1.00 172.25 ? 87   ILE B O   1 
ATOM   14891 C  CB  . ILE C 1 87   ? -8.510   99.586  82.684  1.00 139.49 ? 87   ILE B CB  1 
ATOM   14892 C  CG1 . ILE C 1 87   ? -9.311   100.776 82.178  1.00 135.22 ? 87   ILE B CG1 1 
ATOM   14893 C  CG2 . ILE C 1 87   ? -8.889   99.220  84.101  1.00 134.50 ? 87   ILE B CG2 1 
ATOM   14894 C  CD1 . ILE C 1 87   ? -10.778  100.671 82.473  1.00 132.46 ? 87   ILE B CD1 1 
ATOM   14895 N  N   . GLN C 1 88   ? -5.278   98.573  83.664  1.00 179.43 ? 88   GLN B N   1 
ATOM   14896 C  CA  . GLN C 1 88   ? -4.617   97.338  84.051  1.00 188.08 ? 88   GLN B CA  1 
ATOM   14897 C  C   . GLN C 1 88   ? -5.370   96.728  85.225  1.00 194.87 ? 88   GLN B C   1 
ATOM   14898 O  O   . GLN C 1 88   ? -6.437   97.220  85.585  1.00 196.94 ? 88   GLN B O   1 
ATOM   14899 C  CB  . GLN C 1 88   ? -3.171   97.610  84.436  1.00 189.40 ? 88   GLN B CB  1 
ATOM   14900 C  CG  . GLN C 1 88   ? -2.411   98.414  83.430  1.00 191.43 ? 88   GLN B CG  1 
ATOM   14901 C  CD  . GLN C 1 88   ? -1.038   97.848  83.199  1.00 192.33 ? 88   GLN B CD  1 
ATOM   14902 O  OE1 . GLN C 1 88   ? -0.136   98.540  82.726  1.00 194.73 ? 88   GLN B OE1 1 
ATOM   14903 N  NE2 . GLN C 1 88   ? -0.868   96.571  83.528  1.00 191.04 ? 88   GLN B NE2 1 
ATOM   14904 N  N   . PRO C 1 89   ? -4.834   95.637  85.804  1.00 202.78 ? 89   PRO B N   1 
ATOM   14905 C  CA  . PRO C 1 89   ? -5.261   95.038  87.091  1.00 204.53 ? 89   PRO B CA  1 
ATOM   14906 C  C   . PRO C 1 89   ? -5.207   95.917  88.390  1.00 202.78 ? 89   PRO B C   1 
ATOM   14907 O  O   . PRO C 1 89   ? -4.148   96.387  88.821  1.00 200.54 ? 89   PRO B O   1 
ATOM   14908 C  CB  . PRO C 1 89   ? -4.337   93.820  87.213  1.00 205.56 ? 89   PRO B CB  1 
ATOM   14909 C  CG  . PRO C 1 89   ? -4.115   93.409  85.765  1.00 203.93 ? 89   PRO B CG  1 
ATOM   14910 C  CD  . PRO C 1 89   ? -4.045   94.689  84.989  1.00 202.64 ? 89   PRO B CD  1 
ATOM   14911 N  N   . LYS C 1 90   ? -6.371   96.095  89.018  1.00 208.48 ? 90   LYS B N   1 
ATOM   14912 C  CA  . LYS C 1 90   ? -6.503   96.851  90.262  1.00 213.07 ? 90   LYS B CA  1 
ATOM   14913 C  C   . LYS C 1 90   ? -7.293   96.054  91.280  1.00 224.85 ? 90   LYS B C   1 
ATOM   14914 O  O   . LYS C 1 90   ? -6.721   95.414  92.151  1.00 224.28 ? 90   LYS B O   1 
ATOM   14915 C  CB  . LYS C 1 90   ? -7.221   98.169  90.015  1.00 202.98 ? 90   LYS B CB  1 
ATOM   14916 C  CG  . LYS C 1 90   ? -6.516   99.049  89.037  1.00 193.69 ? 90   LYS B CG  1 
ATOM   14917 C  CD  . LYS C 1 90   ? -5.149   99.425  89.539  1.00 188.27 ? 90   LYS B CD  1 
ATOM   14918 C  CE  . LYS C 1 90   ? -4.345   100.071 88.437  1.00 185.40 ? 90   LYS B CE  1 
ATOM   14919 N  NZ  . LYS C 1 90   ? -3.564   101.235 88.925  1.00 187.43 ? 90   LYS B NZ  1 
ATOM   14920 N  N   . GLN C 1 91   ? -8.616   96.090  91.170  1.00 237.94 ? 91   GLN B N   1 
ATOM   14921 C  CA  . GLN C 1 91   ? -9.464   95.281  92.040  1.00 253.77 ? 91   GLN B CA  1 
ATOM   14922 C  C   . GLN C 1 91   ? -9.353   93.785  91.743  1.00 268.56 ? 91   GLN B C   1 
ATOM   14923 O  O   . GLN C 1 91   ? -9.843   93.305  90.717  1.00 268.15 ? 91   GLN B O   1 
ATOM   14924 C  CB  . GLN C 1 91   ? -10.922  95.723  91.940  1.00 255.51 ? 91   GLN B CB  1 
ATOM   14925 C  CG  . GLN C 1 91   ? -11.238  96.938  92.771  1.00 260.33 ? 91   GLN B CG  1 
ATOM   14926 C  CD  . GLN C 1 91   ? -10.400  96.994  94.025  1.00 264.91 ? 91   GLN B CD  1 
ATOM   14927 O  OE1 . GLN C 1 91   ? -9.295   97.536  94.019  1.00 267.59 ? 91   GLN B OE1 1 
ATOM   14928 N  NE2 . GLN C 1 91   ? -10.919  96.435  95.112  1.00 265.30 ? 91   GLN B NE2 1 
ATOM   14929 N  N   . LEU C 1 92   ? -8.710   93.056  92.653  1.00 283.95 ? 92   LEU B N   1 
ATOM   14930 C  CA  . LEU C 1 92   ? -8.570   91.602  92.541  1.00 297.69 ? 92   LEU B CA  1 
ATOM   14931 C  C   . LEU C 1 92   ? -9.476   90.770  93.469  1.00 306.35 ? 92   LEU B C   1 
ATOM   14932 O  O   . LEU C 1 92   ? -9.469   89.542  93.381  1.00 305.93 ? 92   LEU B O   1 
ATOM   14933 C  CB  . LEU C 1 92   ? -7.107   91.181  92.756  1.00 302.50 ? 92   LEU B CB  1 
ATOM   14934 C  CG  . LEU C 1 92   ? -6.056   91.532  91.697  1.00 306.66 ? 92   LEU B CG  1 
ATOM   14935 C  CD1 . LEU C 1 92   ? -4.659   91.172  92.192  1.00 308.86 ? 92   LEU B CD1 1 
ATOM   14936 C  CD2 . LEU C 1 92   ? -6.350   90.844  90.370  1.00 305.78 ? 92   LEU B CD2 1 
ATOM   14937 N  N   . PRO C 1 93   ? -10.255  91.419  94.358  1.00 315.97 ? 93   PRO B N   1 
ATOM   14938 C  CA  . PRO C 1 93   ? -10.976  90.591  95.333  1.00 320.11 ? 93   PRO B CA  1 
ATOM   14939 C  C   . PRO C 1 93   ? -12.010  89.687  94.674  1.00 323.82 ? 93   PRO B C   1 
ATOM   14940 O  O   . PRO C 1 93   ? -13.001  90.175  94.129  1.00 324.35 ? 93   PRO B O   1 
ATOM   14941 C  CB  . PRO C 1 93   ? -11.682  91.625  96.225  1.00 320.49 ? 93   PRO B CB  1 
ATOM   14942 C  CG  . PRO C 1 93   ? -11.015  92.930  95.933  1.00 321.50 ? 93   PRO B CG  1 
ATOM   14943 C  CD  . PRO C 1 93   ? -10.605  92.841  94.502  1.00 319.49 ? 93   PRO B CD  1 
ATOM   14944 N  N   . GLY C 1 94   ? -11.777  88.380  94.727  1.00 325.88 ? 94   GLY B N   1 
ATOM   14945 C  CA  . GLY C 1 94   ? -12.744  87.425  94.226  1.00 326.45 ? 94   GLY B CA  1 
ATOM   14946 C  C   . GLY C 1 94   ? -14.011  87.530  95.045  1.00 328.34 ? 94   GLY B C   1 
ATOM   14947 O  O   . GLY C 1 94   ? -13.958  87.603  96.271  1.00 329.78 ? 94   GLY B O   1 
ATOM   14948 N  N   . GLY C 1 95   ? -15.154  87.534  94.370  1.00 328.26 ? 95   GLY B N   1 
ATOM   14949 C  CA  . GLY C 1 95   ? -16.426  87.695  95.047  1.00 328.40 ? 95   GLY B CA  1 
ATOM   14950 C  C   . GLY C 1 95   ? -16.965  89.106  94.928  1.00 329.66 ? 95   GLY B C   1 
ATOM   14951 O  O   . GLY C 1 95   ? -18.076  89.306  94.431  1.00 328.72 ? 95   GLY B O   1 
ATOM   14952 N  N   . GLN C 1 96   ? -16.193  90.091  95.383  1.00 331.20 ? 96   GLN B N   1 
ATOM   14953 C  CA  . GLN C 1 96   ? -16.592  91.468  95.160  1.00 330.76 ? 96   GLN B CA  1 
ATOM   14954 C  C   . GLN C 1 96   ? -16.869  91.528  93.682  1.00 332.55 ? 96   GLN B C   1 
ATOM   14955 O  O   . GLN C 1 96   ? -16.117  90.965  92.895  1.00 334.31 ? 96   GLN B O   1 
ATOM   14956 C  CB  . GLN C 1 96   ? -15.482  92.460  95.515  1.00 329.15 ? 96   GLN B CB  1 
ATOM   14957 C  CG  . GLN C 1 96   ? -15.765  93.874  95.013  1.00 327.40 ? 96   GLN B CG  1 
ATOM   14958 C  CD  . GLN C 1 96   ? -14.795  94.905  95.547  1.00 328.85 ? 96   GLN B CD  1 
ATOM   14959 O  OE1 . GLN C 1 96   ? -13.834  94.573  96.238  1.00 329.32 ? 96   GLN B OE1 1 
ATOM   14960 N  NE2 . GLN C 1 96   ? -15.045  96.170  95.228  1.00 329.96 ? 96   GLN B NE2 1 
ATOM   14961 N  N   . ASN C 1 97   ? -17.974  92.153  93.304  1.00 331.46 ? 97   ASN B N   1 
ATOM   14962 C  CA  . ASN C 1 97   ? -18.228  92.407  91.901  1.00 329.51 ? 97   ASN B CA  1 
ATOM   14963 C  C   . ASN C 1 97   ? -17.383  93.604  91.508  1.00 324.49 ? 97   ASN B C   1 
ATOM   14964 O  O   . ASN C 1 97   ? -17.887  94.722  91.407  1.00 326.14 ? 97   ASN B O   1 
ATOM   14965 C  CB  . ASN C 1 97   ? -19.712  92.678  91.671  1.00 332.26 ? 97   ASN B CB  1 
ATOM   14966 C  CG  . ASN C 1 97   ? -20.588  91.541  92.159  1.00 333.48 ? 97   ASN B CG  1 
ATOM   14967 O  OD1 . ASN C 1 97   ? -20.132  90.405  92.283  1.00 333.77 ? 97   ASN B OD1 1 
ATOM   14968 N  ND2 . ASN C 1 97   ? -21.850  91.841  92.443  1.00 333.60 ? 97   ASN B ND2 1 
ATOM   14969 N  N   . PRO C 1 98   ? -16.083  93.371  91.282  1.00 317.32 ? 98   PRO B N   1 
ATOM   14970 C  CA  . PRO C 1 98   ? -15.165  94.497  91.181  1.00 310.41 ? 98   PRO B CA  1 
ATOM   14971 C  C   . PRO C 1 98   ? -15.300  95.056  89.793  1.00 296.06 ? 98   PRO B C   1 
ATOM   14972 O  O   . PRO C 1 98   ? -15.972  94.442  88.969  1.00 295.65 ? 98   PRO B O   1 
ATOM   14973 C  CB  . PRO C 1 98   ? -13.787  93.830  91.307  1.00 315.18 ? 98   PRO B CB  1 
ATOM   14974 C  CG  . PRO C 1 98   ? -14.039  92.316  91.225  1.00 315.94 ? 98   PRO B CG  1 
ATOM   14975 C  CD  . PRO C 1 98   ? -15.454  92.145  90.772  1.00 315.53 ? 98   PRO B CD  1 
ATOM   14976 N  N   . VAL C 1 99   ? -14.693  96.202  89.532  1.00 281.98 ? 99   VAL B N   1 
ATOM   14977 C  CA  . VAL C 1 99   ? -14.424  96.553  88.159  1.00 266.88 ? 99   VAL B CA  1 
ATOM   14978 C  C   . VAL C 1 99   ? -15.694  96.871  87.352  1.00 247.28 ? 99   VAL B C   1 
ATOM   14979 O  O   . VAL C 1 99   ? -15.641  97.625  86.379  1.00 247.92 ? 99   VAL B O   1 
ATOM   14980 C  CB  . VAL C 1 99   ? -13.648  95.383  87.513  1.00 269.46 ? 99   VAL B CB  1 
ATOM   14981 C  CG1 . VAL C 1 99   ? -13.415  95.613  86.036  1.00 271.38 ? 99   VAL B CG1 1 
ATOM   14982 C  CG2 . VAL C 1 99   ? -12.332  95.140  88.258  1.00 271.58 ? 99   VAL B CG2 1 
ATOM   14983 N  N   . SER C 1 100  ? -16.834  96.312  87.749  1.00 227.31 ? 100  SER B N   1 
ATOM   14984 C  CA  . SER C 1 100  ? -18.069  96.543  87.006  1.00 207.38 ? 100  SER B CA  1 
ATOM   14985 C  C   . SER C 1 100  ? -18.306  98.040  86.920  1.00 194.30 ? 100  SER B C   1 
ATOM   14986 O  O   . SER C 1 100  ? -18.658  98.660  87.919  1.00 197.11 ? 100  SER B O   1 
ATOM   14987 C  CB  . SER C 1 100  ? -19.244  95.889  87.721  1.00 201.89 ? 100  SER B CB  1 
ATOM   14988 O  OG  . SER C 1 100  ? -18.772  94.988  88.696  1.00 199.19 ? 100  SER B OG  1 
ATOM   14989 N  N   . TYR C 1 101  ? -18.099  98.623  85.743  1.00 177.71 ? 101  TYR B N   1 
ATOM   14990 C  CA  . TYR C 1 101  ? -18.285  100.065 85.561  1.00 164.31 ? 101  TYR B CA  1 
ATOM   14991 C  C   . TYR C 1 101  ? -17.059  100.910 85.891  1.00 158.87 ? 101  TYR B C   1 
ATOM   14992 O  O   . TYR C 1 101  ? -16.427  100.717 86.916  1.00 158.21 ? 101  TYR B O   1 
ATOM   14993 C  CB  . TYR C 1 101  ? -19.465  100.557 86.396  1.00 160.19 ? 101  TYR B CB  1 
ATOM   14994 C  CG  . TYR C 1 101  ? -20.803  100.200 85.820  1.00 156.75 ? 101  TYR B CG  1 
ATOM   14995 C  CD1 . TYR C 1 101  ? -21.581  101.175 85.217  1.00 157.40 ? 101  TYR B CD1 1 
ATOM   14996 C  CD2 . TYR C 1 101  ? -21.286  98.889  85.857  1.00 153.68 ? 101  TYR B CD2 1 
ATOM   14997 C  CE1 . TYR C 1 101  ? -22.802  100.872 84.677  1.00 156.87 ? 101  TYR B CE1 1 
ATOM   14998 C  CE2 . TYR C 1 101  ? -22.525  98.572  85.315  1.00 153.24 ? 101  TYR B CE2 1 
ATOM   14999 C  CZ  . TYR C 1 101  ? -23.281  99.582  84.724  1.00 155.19 ? 101  TYR B CZ  1 
ATOM   15000 O  OH  . TYR C 1 101  ? -24.519  99.342  84.155  1.00 154.48 ? 101  TYR B OH  1 
ATOM   15001 N  N   . VAL C 1 102  ? -16.735  101.850 85.011  1.00 154.39 ? 102  VAL B N   1 
ATOM   15002 C  CA  . VAL C 1 102  ? -15.690  102.826 85.275  1.00 153.11 ? 102  VAL B CA  1 
ATOM   15003 C  C   . VAL C 1 102  ? -16.048  104.106 84.580  1.00 155.68 ? 102  VAL B C   1 
ATOM   15004 O  O   . VAL C 1 102  ? -17.105  104.203 83.943  1.00 153.58 ? 102  VAL B O   1 
ATOM   15005 C  CB  . VAL C 1 102  ? -14.311  102.441 84.730  1.00 148.95 ? 102  VAL B CB  1 
ATOM   15006 C  CG1 . VAL C 1 102  ? -13.972  101.011 85.067  1.00 146.15 ? 102  VAL B CG1 1 
ATOM   15007 C  CG2 . VAL C 1 102  ? -14.254  102.694 83.225  1.00 147.78 ? 102  VAL B CG2 1 
ATOM   15008 N  N   . TYR C 1 103  ? -15.135  105.072 84.687  1.00 159.34 ? 103  TYR B N   1 
ATOM   15009 C  CA  . TYR C 1 103  ? -15.364  106.432 84.207  1.00 162.34 ? 103  TYR B CA  1 
ATOM   15010 C  C   . TYR C 1 103  ? -14.285  106.876 83.216  1.00 160.26 ? 103  TYR B C   1 
ATOM   15011 O  O   . TYR C 1 103  ? -13.083  106.848 83.513  1.00 158.00 ? 103  TYR B O   1 
ATOM   15012 C  CB  . TYR C 1 103  ? -15.513  107.432 85.386  1.00 176.47 ? 103  TYR B CB  1 
ATOM   15013 C  CG  . TYR C 1 103  ? -16.939  107.544 85.947  1.00 183.59 ? 103  TYR B CG  1 
ATOM   15014 C  CD1 . TYR C 1 103  ? -17.513  106.498 86.669  1.00 186.10 ? 103  TYR B CD1 1 
ATOM   15015 C  CD2 . TYR C 1 103  ? -17.706  108.694 85.754  1.00 187.00 ? 103  TYR B CD2 1 
ATOM   15016 C  CE1 . TYR C 1 103  ? -18.811  106.586 87.174  1.00 189.24 ? 103  TYR B CE1 1 
ATOM   15017 C  CE2 . TYR C 1 103  ? -19.011  108.790 86.260  1.00 190.23 ? 103  TYR B CE2 1 
ATOM   15018 C  CZ  . TYR C 1 103  ? -19.552  107.724 86.969  1.00 191.55 ? 103  TYR B CZ  1 
ATOM   15019 O  OH  . TYR C 1 103  ? -20.830  107.770 87.479  1.00 192.77 ? 103  TYR B OH  1 
ATOM   15020 N  N   . LEU C 1 104  ? -14.746  107.239 82.018  1.00 162.89 ? 104  LEU B N   1 
ATOM   15021 C  CA  . LEU C 1 104  ? -13.892  107.806 80.980  1.00 164.61 ? 104  LEU B CA  1 
ATOM   15022 C  C   . LEU C 1 104  ? -13.888  109.284 81.243  1.00 165.30 ? 104  LEU B C   1 
ATOM   15023 O  O   . LEU C 1 104  ? -14.921  109.842 81.585  1.00 163.66 ? 104  LEU B O   1 
ATOM   15024 C  CB  . LEU C 1 104  ? -14.449  107.522 79.568  1.00 161.20 ? 104  LEU B CB  1 
ATOM   15025 C  CG  . LEU C 1 104  ? -13.602  107.832 78.311  1.00 158.87 ? 104  LEU B CG  1 
ATOM   15026 C  CD1 . LEU C 1 104  ? -12.234  107.158 78.325  1.00 158.54 ? 104  LEU B CD1 1 
ATOM   15027 C  CD2 . LEU C 1 104  ? -14.338  107.452 77.049  1.00 155.79 ? 104  LEU B CD2 1 
ATOM   15028 N  N   . GLU C 1 105  ? -12.730  109.914 81.093  1.00 170.13 ? 105  GLU B N   1 
ATOM   15029 C  CA  . GLU C 1 105  ? -12.628  111.338 81.334  1.00 175.16 ? 105  GLU B CA  1 
ATOM   15030 C  C   . GLU C 1 105  ? -11.738  112.003 80.310  1.00 176.33 ? 105  GLU B C   1 
ATOM   15031 O  O   . GLU C 1 105  ? -10.750  111.436 79.854  1.00 176.51 ? 105  GLU B O   1 
ATOM   15032 C  CB  . GLU C 1 105  ? -12.083  111.607 82.737  1.00 179.54 ? 105  GLU B CB  1 
ATOM   15033 C  CG  . GLU C 1 105  ? -12.299  113.035 83.242  1.00 182.40 ? 105  GLU B CG  1 
ATOM   15034 C  CD  . GLU C 1 105  ? -12.058  113.154 84.739  1.00 185.58 ? 105  GLU B CD  1 
ATOM   15035 O  OE1 . GLU C 1 105  ? -10.890  113.050 85.177  1.00 187.31 ? 105  GLU B OE1 1 
ATOM   15036 O  OE2 . GLU C 1 105  ? -13.044  113.346 85.481  1.00 186.21 ? 105  GLU B OE2 1 
ATOM   15037 N  N   . VAL C 1 106  ? -12.099  113.227 79.968  1.00 177.43 ? 106  VAL B N   1 
ATOM   15038 C  CA  . VAL C 1 106  ? -11.292  114.031 79.083  1.00 178.55 ? 106  VAL B CA  1 
ATOM   15039 C  C   . VAL C 1 106  ? -11.176  115.416 79.690  1.00 181.33 ? 106  VAL B C   1 
ATOM   15040 O  O   . VAL C 1 106  ? -12.035  115.825 80.465  1.00 181.83 ? 106  VAL B O   1 
ATOM   15041 C  CB  . VAL C 1 106  ? -11.936  114.121 77.719  1.00 177.75 ? 106  VAL B CB  1 
ATOM   15042 C  CG1 . VAL C 1 106  ? -11.152  115.066 76.838  1.00 179.44 ? 106  VAL B CG1 1 
ATOM   15043 C  CG2 . VAL C 1 106  ? -11.994  112.748 77.104  1.00 176.05 ? 106  VAL B CG2 1 
ATOM   15044 N  N   . VAL C 1 107  ? -10.113  116.133 79.346  1.00 182.76 ? 107  VAL B N   1 
ATOM   15045 C  CA  . VAL C 1 107  ? -9.804   117.404 79.990  1.00 184.34 ? 107  VAL B CA  1 
ATOM   15046 C  C   . VAL C 1 107  ? -9.286   118.396 78.946  1.00 184.28 ? 107  VAL B C   1 
ATOM   15047 O  O   . VAL C 1 107  ? -8.645   118.000 77.981  1.00 182.21 ? 107  VAL B O   1 
ATOM   15048 C  CB  . VAL C 1 107  ? -8.746   117.203 81.120  1.00 192.19 ? 107  VAL B CB  1 
ATOM   15049 C  CG1 . VAL C 1 107  ? -8.618   118.449 81.978  1.00 194.12 ? 107  VAL B CG1 1 
ATOM   15050 C  CG2 . VAL C 1 107  ? -9.091   115.992 81.994  1.00 191.47 ? 107  VAL B CG2 1 
ATOM   15051 N  N   . SER C 1 108  ? -9.575   119.679 79.132  1.00 185.53 ? 108  SER B N   1 
ATOM   15052 C  CA  . SER C 1 108  ? -9.102   120.713 78.218  1.00 190.01 ? 108  SER B CA  1 
ATOM   15053 C  C   . SER C 1 108  ? -9.075   122.058 78.933  1.00 196.87 ? 108  SER B C   1 
ATOM   15054 O  O   . SER C 1 108  ? -9.088   122.100 80.161  1.00 199.44 ? 108  SER B O   1 
ATOM   15055 C  CB  . SER C 1 108  ? -10.008  120.791 76.995  1.00 187.34 ? 108  SER B CB  1 
ATOM   15056 O  OG  . SER C 1 108  ? -11.366  120.908 77.373  1.00 186.72 ? 108  SER B OG  1 
ATOM   15057 N  N   . LYS C 1 109  ? -9.019   123.158 78.181  1.00 203.27 ? 109  LYS B N   1 
ATOM   15058 C  CA  . LYS C 1 109  ? -9.201   124.493 78.775  1.00 209.93 ? 109  LYS B CA  1 
ATOM   15059 C  C   . LYS C 1 109  ? -10.667  124.930 78.760  1.00 213.50 ? 109  LYS B C   1 
ATOM   15060 O  O   . LYS C 1 109  ? -11.091  125.728 79.602  1.00 215.05 ? 109  LYS B O   1 
ATOM   15061 C  CB  . LYS C 1 109  ? -8.320   125.574 78.107  1.00 210.93 ? 109  LYS B CB  1 
ATOM   15062 C  CG  . LYS C 1 109  ? -8.398   125.706 76.553  1.00 212.24 ? 109  LYS B CG  1 
ATOM   15063 C  CD  . LYS C 1 109  ? -9.825   125.676 75.966  1.00 209.39 ? 109  LYS B CD  1 
ATOM   15064 C  CE  . LYS C 1 109  ? -9.884   126.016 74.480  1.00 206.62 ? 109  LYS B CE  1 
ATOM   15065 N  NZ  . LYS C 1 109  ? -10.228  127.438 74.243  1.00 207.09 ? 109  LYS B NZ  1 
ATOM   15066 N  N   . HIS C 1 110  ? -11.429  124.390 77.803  1.00 215.32 ? 110  HIS B N   1 
ATOM   15067 C  CA  . HIS C 1 110  ? -12.774  124.881 77.488  1.00 217.26 ? 110  HIS B CA  1 
ATOM   15068 C  C   . HIS C 1 110  ? -13.944  124.074 78.047  1.00 213.00 ? 110  HIS B C   1 
ATOM   15069 O  O   . HIS C 1 110  ? -15.018  124.626 78.307  1.00 213.40 ? 110  HIS B O   1 
ATOM   15070 C  CB  . HIS C 1 110  ? -12.968  125.037 75.985  1.00 222.73 ? 110  HIS B CB  1 
ATOM   15071 C  CG  . HIS C 1 110  ? -14.335  125.514 75.624  1.00 229.62 ? 110  HIS B CG  1 
ATOM   15072 N  ND1 . HIS C 1 110  ? -15.077  124.961 74.605  1.00 231.92 ? 110  HIS B ND1 1 
ATOM   15073 C  CD2 . HIS C 1 110  ? -15.115  126.468 76.183  1.00 233.76 ? 110  HIS B CD2 1 
ATOM   15074 C  CE1 . HIS C 1 110  ? -16.245  125.574 74.533  1.00 233.29 ? 110  HIS B CE1 1 
ATOM   15075 N  NE2 . HIS C 1 110  ? -16.295  126.491 75.483  1.00 234.38 ? 110  HIS B NE2 1 
ATOM   15076 N  N   . PHE C 1 111  ? -13.754  122.770 78.203  1.00 208.16 ? 111  PHE B N   1 
ATOM   15077 C  CA  . PHE C 1 111  ? -14.757  121.949 78.875  1.00 202.05 ? 111  PHE B CA  1 
ATOM   15078 C  C   . PHE C 1 111  ? -14.109  120.755 79.571  1.00 192.47 ? 111  PHE B C   1 
ATOM   15079 O  O   . PHE C 1 111  ? -12.921  120.469 79.398  1.00 189.24 ? 111  PHE B O   1 
ATOM   15080 C  CB  . PHE C 1 111  ? -15.858  121.484 77.894  1.00 202.71 ? 111  PHE B CB  1 
ATOM   15081 C  CG  . PHE C 1 111  ? -17.207  121.223 78.553  1.00 204.47 ? 111  PHE B CG  1 
ATOM   15082 C  CD1 . PHE C 1 111  ? -18.170  122.220 78.615  1.00 205.93 ? 111  PHE B CD1 1 
ATOM   15083 C  CD2 . PHE C 1 111  ? -17.507  119.981 79.103  1.00 203.76 ? 111  PHE B CD2 1 
ATOM   15084 C  CE1 . PHE C 1 111  ? -19.397  121.979 79.215  1.00 206.20 ? 111  PHE B CE1 1 
ATOM   15085 C  CE2 . PHE C 1 111  ? -18.734  119.737 79.705  1.00 203.42 ? 111  PHE B CE2 1 
ATOM   15086 C  CZ  . PHE C 1 111  ? -19.676  120.730 79.759  1.00 204.70 ? 111  PHE B CZ  1 
ATOM   15087 N  N   . SER C 1 112  ? -14.896  120.073 80.382  1.00 186.16 ? 112  SER B N   1 
ATOM   15088 C  CA  . SER C 1 112  ? -14.500  118.769 80.833  1.00 180.41 ? 112  SER B CA  1 
ATOM   15089 C  C   . SER C 1 112  ? -15.740  117.892 80.897  1.00 178.72 ? 112  SER B C   1 
ATOM   15090 O  O   . SER C 1 112  ? -16.815  118.349 81.317  1.00 179.27 ? 112  SER B O   1 
ATOM   15091 C  CB  . SER C 1 112  ? -13.803  118.848 82.176  1.00 178.00 ? 112  SER B CB  1 
ATOM   15092 O  OG  . SER C 1 112  ? -12.834  117.825 82.277  1.00 175.62 ? 112  SER B OG  1 
ATOM   15093 N  N   . LYS C 1 113  ? -15.581  116.643 80.443  1.00 175.75 ? 113  LYS B N   1 
ATOM   15094 C  CA  . LYS C 1 113  ? -16.664  115.660 80.393  1.00 170.50 ? 113  LYS B CA  1 
ATOM   15095 C  C   . LYS C 1 113  ? -16.175  114.216 80.474  1.00 165.38 ? 113  LYS B C   1 
ATOM   15096 O  O   . LYS C 1 113  ? -15.054  113.885 80.087  1.00 163.49 ? 113  LYS B O   1 
ATOM   15097 C  CB  . LYS C 1 113  ? -17.520  115.852 79.138  1.00 171.18 ? 113  LYS B CB  1 
ATOM   15098 C  CG  . LYS C 1 113  ? -18.781  114.986 79.117  1.00 172.78 ? 113  LYS B CG  1 
ATOM   15099 C  CD  . LYS C 1 113  ? -19.999  115.684 79.726  1.00 175.96 ? 113  LYS B CD  1 
ATOM   15100 C  CE  . LYS C 1 113  ? -21.262  114.832 79.565  1.00 175.53 ? 113  LYS B CE  1 
ATOM   15101 N  NZ  . LYS C 1 113  ? -22.544  115.601 79.624  1.00 175.52 ? 113  LYS B NZ  1 
ATOM   15102 N  N   . SER C 1 114  ? -17.057  113.360 80.963  1.00 164.76 ? 114  SER B N   1 
ATOM   15103 C  CA  . SER C 1 114  ? -16.707  111.988 81.271  1.00 168.72 ? 114  SER B CA  1 
ATOM   15104 C  C   . SER C 1 114  ? -17.912  111.060 81.031  1.00 168.59 ? 114  SER B C   1 
ATOM   15105 O  O   . SER C 1 114  ? -18.938  111.514 80.504  1.00 166.84 ? 114  SER B O   1 
ATOM   15106 C  CB  . SER C 1 114  ? -16.193  111.901 82.713  1.00 172.50 ? 114  SER B CB  1 
ATOM   15107 O  OG  . SER C 1 114  ? -16.550  113.048 83.465  1.00 174.86 ? 114  SER B OG  1 
ATOM   15108 N  N   . LYS C 1 115  ? -17.796  109.775 81.391  1.00 168.84 ? 115  LYS B N   1 
ATOM   15109 C  CA  . LYS C 1 115  ? -18.866  108.813 81.096  1.00 167.13 ? 115  LYS B CA  1 
ATOM   15110 C  C   . LYS C 1 115  ? -18.853  107.578 81.974  1.00 165.33 ? 115  LYS B C   1 
ATOM   15111 O  O   . LYS C 1 115  ? -17.790  107.078 82.314  1.00 164.47 ? 115  LYS B O   1 
ATOM   15112 C  CB  . LYS C 1 115  ? -18.787  108.373 79.630  1.00 165.58 ? 115  LYS B CB  1 
ATOM   15113 C  CG  . LYS C 1 115  ? -19.872  107.380 79.184  1.00 161.86 ? 115  LYS B CG  1 
ATOM   15114 C  CD  . LYS C 1 115  ? -21.117  108.071 78.608  1.00 158.81 ? 115  LYS B CD  1 
ATOM   15115 C  CE  . LYS C 1 115  ? -22.001  107.075 77.843  1.00 154.58 ? 115  LYS B CE  1 
ATOM   15116 N  NZ  . LYS C 1 115  ? -23.308  107.666 77.424  1.00 152.72 ? 115  LYS B NZ  1 
ATOM   15117 N  N   . ARG C 1 116  ? -20.046  107.095 82.328  1.00 166.95 ? 116  ARG B N   1 
ATOM   15118 C  CA  . ARG C 1 116  ? -20.215  105.788 82.976  1.00 170.63 ? 116  ARG B CA  1 
ATOM   15119 C  C   . ARG C 1 116  ? -20.447  104.715 81.921  1.00 170.94 ? 116  ARG B C   1 
ATOM   15120 O  O   . ARG C 1 116  ? -21.418  104.783 81.170  1.00 171.88 ? 116  ARG B O   1 
ATOM   15121 C  CB  . ARG C 1 116  ? -21.397  105.808 83.954  1.00 174.44 ? 116  ARG B CB  1 
ATOM   15122 C  CG  . ARG C 1 116  ? -21.799  104.444 84.534  1.00 177.29 ? 116  ARG B CG  1 
ATOM   15123 C  CD  . ARG C 1 116  ? -23.097  103.929 83.905  1.00 180.59 ? 116  ARG B CD  1 
ATOM   15124 N  NE  . ARG C 1 116  ? -24.043  103.416 84.901  1.00 184.46 ? 116  ARG B NE  1 
ATOM   15125 C  CZ  . ARG C 1 116  ? -25.057  102.588 84.636  1.00 186.06 ? 116  ARG B CZ  1 
ATOM   15126 N  NH1 . ARG C 1 116  ? -25.260  102.143 83.398  1.00 185.95 ? 116  ARG B NH1 1 
ATOM   15127 N  NH2 . ARG C 1 116  ? -25.861  102.179 85.615  1.00 186.55 ? 116  ARG B NH2 1 
ATOM   15128 N  N   . MET C 1 117  ? -19.578  103.713 81.860  1.00 168.95 ? 117  MET B N   1 
ATOM   15129 C  CA  . MET C 1 117  ? -19.661  102.755 80.763  1.00 165.32 ? 117  MET B CA  1 
ATOM   15130 C  C   . MET C 1 117  ? -18.970  101.428 81.081  1.00 161.95 ? 117  MET B C   1 
ATOM   15131 O  O   . MET C 1 117  ? -17.760  101.395 81.339  1.00 159.95 ? 117  MET B O   1 
ATOM   15132 C  CB  . MET C 1 117  ? -19.066  103.364 79.497  1.00 166.44 ? 117  MET B CB  1 
ATOM   15133 C  CG  . MET C 1 117  ? -17.660  103.894 79.699  1.00 168.60 ? 117  MET B CG  1 
ATOM   15134 S  SD  . MET C 1 117  ? -16.913  104.349 78.140  1.00 170.88 ? 117  MET B SD  1 
ATOM   15135 C  CE  . MET C 1 117  ? -18.322  105.134 77.376  1.00 131.84 ? 117  MET B CE  1 
ATOM   15136 N  N   . PRO C 1 118  ? -19.746  100.325 81.043  1.00 159.17 ? 118  PRO B N   1 
ATOM   15137 C  CA  . PRO C 1 118  ? -19.314  98.986  81.467  1.00 156.13 ? 118  PRO B CA  1 
ATOM   15138 C  C   . PRO C 1 118  ? -17.999  98.517  80.854  1.00 154.61 ? 118  PRO B C   1 
ATOM   15139 O  O   . PRO C 1 118  ? -17.625  98.955  79.762  1.00 152.66 ? 118  PRO B O   1 
ATOM   15140 C  CB  . PRO C 1 118  ? -20.475  98.095  81.027  1.00 154.56 ? 118  PRO B CB  1 
ATOM   15141 C  CG  . PRO C 1 118  ? -21.668  98.989  81.110  1.00 155.44 ? 118  PRO B CG  1 
ATOM   15142 C  CD  . PRO C 1 118  ? -21.177  100.346 80.675  1.00 158.27 ? 118  PRO B CD  1 
ATOM   15143 N  N   . ILE C 1 119  ? -17.311  97.627  81.575  1.00 154.31 ? 119  ILE B N   1 
ATOM   15144 C  CA  . ILE C 1 119  ? -16.027  97.078  81.133  1.00 153.21 ? 119  ILE B CA  1 
ATOM   15145 C  C   . ILE C 1 119  ? -15.899  95.585  81.409  1.00 151.13 ? 119  ILE B C   1 
ATOM   15146 O  O   . ILE C 1 119  ? -16.696  95.023  82.159  1.00 149.12 ? 119  ILE B O   1 
ATOM   15147 C  CB  . ILE C 1 119  ? -14.845  97.770  81.810  1.00 152.14 ? 119  ILE B CB  1 
ATOM   15148 C  CG1 . ILE C 1 119  ? -14.631  97.219  83.210  1.00 149.52 ? 119  ILE B CG1 1 
ATOM   15149 C  CG2 . ILE C 1 119  ? -15.032  99.279  81.831  1.00 153.29 ? 119  ILE B CG2 1 
ATOM   15150 C  CD1 . ILE C 1 119  ? -13.382  97.757  83.808  1.00 150.73 ? 119  ILE B CD1 1 
ATOM   15151 N  N   . THR C 1 120  ? -14.886  94.958  80.808  1.00 152.01 ? 120  THR B N   1 
ATOM   15152 C  CA  . THR C 1 120  ? -14.762  93.508  80.885  1.00 153.02 ? 120  THR B CA  1 
ATOM   15153 C  C   . THR C 1 120  ? -13.349  92.960  80.933  1.00 153.95 ? 120  THR B C   1 
ATOM   15154 O  O   . THR C 1 120  ? -12.371  93.670  80.671  1.00 154.27 ? 120  THR B O   1 
ATOM   15155 C  CB  . THR C 1 120  ? -15.483  92.821  79.735  1.00 153.79 ? 120  THR B CB  1 
ATOM   15156 O  OG1 . THR C 1 120  ? -16.677  93.553  79.442  1.00 154.69 ? 120  THR B OG1 1 
ATOM   15157 C  CG2 . THR C 1 120  ? -15.808  91.324  80.086  1.00 116.07 ? 120  THR B CG2 1 
ATOM   15158 N  N   . TYR C 1 121  ? -13.294  91.666  81.251  1.00 173.17 ? 121  TYR B N   1 
ATOM   15159 C  CA  . TYR C 1 121  ? -12.082  90.959  81.601  1.00 174.13 ? 121  TYR B CA  1 
ATOM   15160 C  C   . TYR C 1 121  ? -11.623  90.055  80.496  1.00 166.69 ? 121  TYR B C   1 
ATOM   15161 O  O   . TYR C 1 121  ? -10.654  89.330  80.658  1.00 167.59 ? 121  TYR B O   1 
ATOM   15162 C  CB  . TYR C 1 121  ? -12.340  90.066  82.797  1.00 180.22 ? 121  TYR B CB  1 
ATOM   15163 C  CG  . TYR C 1 121  ? -12.854  90.763  84.029  1.00 186.20 ? 121  TYR B CG  1 
ATOM   15164 C  CD1 . TYR C 1 121  ? -12.074  91.686  84.706  1.00 189.72 ? 121  TYR B CD1 1 
ATOM   15165 C  CD2 . TYR C 1 121  ? -14.114  90.464  84.534  1.00 186.18 ? 121  TYR B CD2 1 
ATOM   15166 C  CE1 . TYR C 1 121  ? -12.542  92.303  85.828  1.00 193.26 ? 121  TYR B CE1 1 
ATOM   15167 C  CE2 . TYR C 1 121  ? -14.586  91.073  85.657  1.00 189.00 ? 121  TYR B CE2 1 
ATOM   15168 C  CZ  . TYR C 1 121  ? -13.798  91.992  86.300  1.00 193.70 ? 121  TYR B CZ  1 
ATOM   15169 O  OH  . TYR C 1 121  ? -14.272  92.600  87.436  1.00 199.27 ? 121  TYR B OH  1 
ATOM   15170 N  N   . ASP C 1 122  ? -12.350  90.056  79.394  1.00 158.40 ? 122  ASP B N   1 
ATOM   15171 C  CA  . ASP C 1 122  ? -11.927  89.341  78.203  1.00 150.85 ? 122  ASP B CA  1 
ATOM   15172 C  C   . ASP C 1 122  ? -10.804  90.047  77.476  1.00 145.69 ? 122  ASP B C   1 
ATOM   15173 O  O   . ASP C 1 122  ? -11.066  90.986  76.743  1.00 146.79 ? 122  ASP B O   1 
ATOM   15174 C  CB  . ASP C 1 122  ? -13.095  89.281  77.242  1.00 150.49 ? 122  ASP B CB  1 
ATOM   15175 C  CG  . ASP C 1 122  ? -13.605  87.889  77.045  1.00 150.74 ? 122  ASP B CG  1 
ATOM   15176 O  OD1 . ASP C 1 122  ? -14.845  87.723  77.003  1.00 150.44 ? 122  ASP B OD1 1 
ATOM   15177 O  OD2 . ASP C 1 122  ? -12.766  86.966  76.921  1.00 151.06 ? 122  ASP B OD2 1 
ATOM   15178 N  N   . ASN C 1 123  ? -9.564   89.600  77.622  1.00 140.93 ? 123  ASN B N   1 
ATOM   15179 C  CA  . ASN C 1 123  ? -8.496   90.194  76.818  1.00 140.25 ? 123  ASN B CA  1 
ATOM   15180 C  C   . ASN C 1 123  ? -7.784   89.148  76.000  1.00 140.02 ? 123  ASN B C   1 
ATOM   15181 O  O   . ASN C 1 123  ? -7.109   88.279  76.561  1.00 138.60 ? 123  ASN B O   1 
ATOM   15182 C  CB  . ASN C 1 123  ? -7.488   90.970  77.671  1.00 140.60 ? 123  ASN B CB  1 
ATOM   15183 C  CG  . ASN C 1 123  ? -6.317   91.534  76.857  1.00 140.74 ? 123  ASN B CG  1 
ATOM   15184 O  OD1 . ASN C 1 123  ? -5.638   92.469  77.291  1.00 142.37 ? 123  ASN B OD1 1 
ATOM   15185 N  ND2 . ASN C 1 123  ? -6.068   90.959  75.690  1.00 139.20 ? 123  ASN B ND2 1 
ATOM   15186 N  N   . GLY C 1 124  ? -7.945   89.256  74.675  1.00 141.22 ? 124  GLY B N   1 
ATOM   15187 C  CA  . GLY C 1 124  ? -7.284   88.392  73.713  1.00 140.00 ? 124  GLY B CA  1 
ATOM   15188 C  C   . GLY C 1 124  ? -8.057   87.156  73.307  1.00 126.44 ? 124  GLY B C   1 
ATOM   15189 O  O   . GLY C 1 124  ? -9.275   87.132  73.372  1.00 125.28 ? 124  GLY B O   1 
ATOM   15190 N  N   . PHE C 1 125  ? -7.318   86.123  72.918  1.00 125.62 ? 125  PHE B N   1 
ATOM   15191 C  CA  . PHE C 1 125  ? -7.873   84.949  72.275  1.00 123.14 ? 125  PHE B CA  1 
ATOM   15192 C  C   . PHE C 1 125  ? -7.056   83.700  72.575  1.00 123.01 ? 125  PHE B C   1 
ATOM   15193 O  O   . PHE C 1 125  ? -5.848   83.708  72.371  1.00 124.03 ? 125  PHE B O   1 
ATOM   15194 C  CB  . PHE C 1 125  ? -7.799   85.144  70.763  1.00 121.91 ? 125  PHE B CB  1 
ATOM   15195 C  CG  . PHE C 1 125  ? -8.499   86.367  70.265  1.00 122.05 ? 125  PHE B CG  1 
ATOM   15196 C  CD1 . PHE C 1 125  ? -7.779   87.507  69.934  1.00 123.68 ? 125  PHE B CD1 1 
ATOM   15197 C  CD2 . PHE C 1 125  ? -9.880   86.368  70.102  1.00 120.61 ? 125  PHE B CD2 1 
ATOM   15198 C  CE1 . PHE C 1 125  ? -8.420   88.636  69.459  1.00 123.90 ? 125  PHE B CE1 1 
ATOM   15199 C  CE2 . PHE C 1 125  ? -10.530  87.488  69.646  1.00 120.83 ? 125  PHE B CE2 1 
ATOM   15200 C  CZ  . PHE C 1 125  ? -9.796   88.634  69.315  1.00 122.49 ? 125  PHE B CZ  1 
ATOM   15201 N  N   . LEU C 1 126  ? -7.697   82.617  73.010  1.00 121.77 ? 126  LEU B N   1 
ATOM   15202 C  CA  . LEU C 1 126  ? -6.975   81.350  73.178  1.00 121.49 ? 126  LEU B CA  1 
ATOM   15203 C  C   . LEU C 1 126  ? -7.268   80.357  72.037  1.00 119.75 ? 126  LEU B C   1 
ATOM   15204 O  O   . LEU C 1 126  ? -8.427   80.016  71.783  1.00 121.30 ? 126  LEU B O   1 
ATOM   15205 C  CB  . LEU C 1 126  ? -7.259   80.711  74.549  1.00 122.13 ? 126  LEU B CB  1 
ATOM   15206 C  CG  . LEU C 1 126  ? -6.554   81.139  75.855  1.00 124.76 ? 126  LEU B CG  1 
ATOM   15207 C  CD1 . LEU C 1 126  ? -5.150   81.701  75.618  1.00 126.49 ? 126  LEU B CD1 1 
ATOM   15208 C  CD2 . LEU C 1 126  ? -7.397   82.120  76.663  1.00 125.79 ? 126  LEU B CD2 1 
ATOM   15209 N  N   . PHE C 1 127  ? -6.224   79.895  71.347  1.00 119.10 ? 127  PHE B N   1 
ATOM   15210 C  CA  . PHE C 1 127  ? -6.388   79.035  70.164  1.00 117.11 ? 127  PHE B CA  1 
ATOM   15211 C  C   . PHE C 1 127  ? -5.809   77.650  70.390  1.00 116.81 ? 127  PHE B C   1 
ATOM   15212 O  O   . PHE C 1 127  ? -4.598   77.499  70.332  1.00 117.86 ? 127  PHE B O   1 
ATOM   15213 C  CB  . PHE C 1 127  ? -5.656   79.646  68.965  1.00 117.76 ? 127  PHE B CB  1 
ATOM   15214 C  CG  . PHE C 1 127  ? -6.407   80.775  68.282  1.00 118.02 ? 127  PHE B CG  1 
ATOM   15215 C  CD1 . PHE C 1 127  ? -7.778   80.715  68.103  1.00 116.61 ? 127  PHE B CD1 1 
ATOM   15216 C  CD2 . PHE C 1 127  ? -5.727   81.880  67.791  1.00 118.13 ? 127  PHE B CD2 1 
ATOM   15217 C  CE1 . PHE C 1 127  ? -8.445   81.732  67.484  1.00 115.19 ? 127  PHE B CE1 1 
ATOM   15218 C  CE2 . PHE C 1 127  ? -6.394   82.902  67.174  1.00 117.92 ? 127  PHE B CE2 1 
ATOM   15219 C  CZ  . PHE C 1 127  ? -7.755   82.827  67.023  1.00 116.45 ? 127  PHE B CZ  1 
ATOM   15220 N  N   . ILE C 1 128  ? -6.646   76.634  70.595  1.00 115.42 ? 128  ILE B N   1 
ATOM   15221 C  CA  . ILE C 1 128  ? -6.143   75.303  71.000  1.00 115.36 ? 128  ILE B CA  1 
ATOM   15222 C  C   . ILE C 1 128  ? -5.872   74.296  69.875  1.00 113.96 ? 128  ILE B C   1 
ATOM   15223 O  O   . ILE C 1 128  ? -6.778   73.622  69.362  1.00 112.23 ? 128  ILE B O   1 
ATOM   15224 C  CB  . ILE C 1 128  ? -7.063   74.627  72.018  1.00 114.98 ? 128  ILE B CB  1 
ATOM   15225 C  CG1 . ILE C 1 128  ? -7.894   75.663  72.766  1.00 115.60 ? 128  ILE B CG1 1 
ATOM   15226 C  CG2 . ILE C 1 128  ? -6.245   73.837  72.977  1.00 116.23 ? 128  ILE B CG2 1 
ATOM   15227 C  CD1 . ILE C 1 128  ? -8.836   75.054  73.762  1.00 115.28 ? 128  ILE B CD1 1 
ATOM   15228 N  N   . HIS C 1 129  ? -4.602   74.159  69.530  1.00 114.83 ? 129  HIS B N   1 
ATOM   15229 C  CA  . HIS C 1 129  ? -4.206   73.351  68.377  1.00 117.14 ? 129  HIS B CA  1 
ATOM   15230 C  C   . HIS C 1 129  ? -3.860   71.902  68.734  1.00 119.42 ? 129  HIS B C   1 
ATOM   15231 O  O   . HIS C 1 129  ? -2.697   71.539  68.945  1.00 122.09 ? 129  HIS B O   1 
ATOM   15232 C  CB  . HIS C 1 129  ? -3.038   74.043  67.665  1.00 115.03 ? 129  HIS B CB  1 
ATOM   15233 C  CG  . HIS C 1 129  ? -2.580   73.352  66.422  1.00 113.89 ? 129  HIS B CG  1 
ATOM   15234 N  ND1 . HIS C 1 129  ? -1.532   73.821  65.658  1.00 114.68 ? 129  HIS B ND1 1 
ATOM   15235 C  CD2 . HIS C 1 129  ? -3.014   72.220  65.821  1.00 112.40 ? 129  HIS B CD2 1 
ATOM   15236 C  CE1 . HIS C 1 129  ? -1.349   73.015  64.630  1.00 113.69 ? 129  HIS B CE1 1 
ATOM   15237 N  NE2 . HIS C 1 129  ? -2.232   72.033  64.708  1.00 112.33 ? 129  HIS B NE2 1 
ATOM   15238 N  N   . THR C 1 130  ? -4.878   71.068  68.814  1.00 118.53 ? 130  THR B N   1 
ATOM   15239 C  CA  . THR C 1 130  ? -4.625   69.667  69.035  1.00 118.67 ? 130  THR B CA  1 
ATOM   15240 C  C   . THR C 1 130  ? -4.112   69.190  67.692  1.00 119.23 ? 130  THR B C   1 
ATOM   15241 O  O   . THR C 1 130  ? -4.481   69.760  66.660  1.00 120.21 ? 130  THR B O   1 
ATOM   15242 C  CB  . THR C 1 130  ? -5.904   68.957  69.412  1.00 117.36 ? 130  THR B CB  1 
ATOM   15243 O  OG1 . THR C 1 130  ? -5.767   67.569  69.105  1.00 115.93 ? 130  THR B OG1 1 
ATOM   15244 C  CG2 . THR C 1 130  ? -7.086   69.549  68.627  1.00 116.55 ? 130  THR B CG2 1 
ATOM   15245 N  N   . ASP C 1 131  ? -3.250   68.180  67.671  1.00 118.35 ? 131  ASP B N   1 
ATOM   15246 C  CA  . ASP C 1 131  ? -2.643   67.808  66.397  1.00 118.94 ? 131  ASP B CA  1 
ATOM   15247 C  C   . ASP C 1 131  ? -3.659   67.236  65.403  1.00 119.97 ? 131  ASP B C   1 
ATOM   15248 O  O   . ASP C 1 131  ? -3.747   67.703  64.267  1.00 120.46 ? 131  ASP B O   1 
ATOM   15249 C  CB  . ASP C 1 131  ? -1.459   66.868  66.581  1.00 118.19 ? 131  ASP B CB  1 
ATOM   15250 C  CG  . ASP C 1 131  ? -1.888   65.476  66.863  1.00 117.24 ? 131  ASP B CG  1 
ATOM   15251 O  OD1 . ASP C 1 131  ? -2.950   65.339  67.485  1.00 115.89 ? 131  ASP B OD1 1 
ATOM   15252 O  OD2 . ASP C 1 131  ? -1.180   64.526  66.470  1.00 118.24 ? 131  ASP B OD2 1 
ATOM   15253 N  N   . LYS C 1 132  ? -4.441   66.252  65.829  1.00 120.38 ? 132  LYS B N   1 
ATOM   15254 C  CA  . LYS C 1 132  ? -5.514   65.747  64.980  1.00 119.93 ? 132  LYS B CA  1 
ATOM   15255 C  C   . LYS C 1 132  ? -6.817   65.611  65.772  1.00 123.67 ? 132  LYS B C   1 
ATOM   15256 O  O   . LYS C 1 132  ? -6.807   65.800  66.977  1.00 128.66 ? 132  LYS B O   1 
ATOM   15257 C  CB  . LYS C 1 132  ? -5.086   64.476  64.245  1.00 115.37 ? 132  LYS B CB  1 
ATOM   15258 C  CG  . LYS C 1 132  ? -5.225   63.179  64.968  1.00 112.58 ? 132  LYS B CG  1 
ATOM   15259 C  CD  . LYS C 1 132  ? -4.170   62.213  64.430  1.00 106.98 ? 132  LYS B CD  1 
ATOM   15260 C  CE  . LYS C 1 132  ? -4.264   60.840  65.066  1.00 107.07 ? 132  LYS B CE  1 
ATOM   15261 N  NZ  . LYS C 1 132  ? -2.882   60.382  65.331  1.00 108.89 ? 132  LYS B NZ  1 
ATOM   15262 N  N   . PRO C 1 133  ? -7.954   65.350  65.107  1.00 118.20 ? 133  PRO B N   1 
ATOM   15263 C  CA  . PRO C 1 133  ? -9.144   65.594  65.903  1.00 113.05 ? 133  PRO B CA  1 
ATOM   15264 C  C   . PRO C 1 133  ? -9.786   64.266  66.214  1.00 108.65 ? 133  PRO B C   1 
ATOM   15265 O  O   . PRO C 1 133  ? -10.960  64.282  66.573  1.00 110.37 ? 133  PRO B O   1 
ATOM   15266 C  CB  . PRO C 1 133  ? -10.052  66.303  64.918  1.00 108.69 ? 133  PRO B CB  1 
ATOM   15267 C  CG  . PRO C 1 133  ? -9.655   65.657  63.542  1.00 117.24 ? 133  PRO B CG  1 
ATOM   15268 C  CD  . PRO C 1 133  ? -8.347   64.870  63.776  1.00 118.56 ? 133  PRO B CD  1 
ATOM   15269 N  N   . VAL C 1 134  ? -9.089   63.146  66.043  1.00 107.83 ? 134  VAL B N   1 
ATOM   15270 C  CA  . VAL C 1 134  ? -9.664   61.897  66.502  1.00 103.58 ? 134  VAL B CA  1 
ATOM   15271 C  C   . VAL C 1 134  ? -8.613   60.910  66.945  1.00 111.16 ? 134  VAL B C   1 
ATOM   15272 O  O   . VAL C 1 134  ? -7.640   60.641  66.224  1.00 109.15 ? 134  VAL B O   1 
ATOM   15273 C  CB  . VAL C 1 134  ? -10.598  61.247  65.475  1.00 101.86 ? 134  VAL B CB  1 
ATOM   15274 C  CG1 . VAL C 1 134  ? -10.663  59.775  65.686  1.00 101.80 ? 134  VAL B CG1 1 
ATOM   15275 C  CG2 . VAL C 1 134  ? -11.983  61.780  65.634  1.00 100.93 ? 134  VAL B CG2 1 
ATOM   15276 N  N   . TYR C 1 135  ? -8.836   60.353  68.140  1.00 108.66 ? 135  TYR B N   1 
ATOM   15277 C  CA  . TYR C 1 135  ? -7.908   59.405  68.759  1.00 111.88 ? 135  TYR B CA  1 
ATOM   15278 C  C   . TYR C 1 135  ? -8.511   58.079  69.160  1.00 106.67 ? 135  TYR B C   1 
ATOM   15279 O  O   . TYR C 1 135  ? -9.715   57.941  69.404  1.00 104.79 ? 135  TYR B O   1 
ATOM   15280 C  CB  . TYR C 1 135  ? -7.253   60.020  69.978  1.00 107.52 ? 135  TYR B CB  1 
ATOM   15281 C  CG  . TYR C 1 135  ? -6.578   61.297  69.648  1.00 108.05 ? 135  TYR B CG  1 
ATOM   15282 C  CD1 . TYR C 1 135  ? -5.228   61.327  69.364  1.00 109.11 ? 135  TYR B CD1 1 
ATOM   15283 C  CD2 . TYR C 1 135  ? -7.301   62.478  69.582  1.00 107.52 ? 135  TYR B CD2 1 
ATOM   15284 C  CE1 . TYR C 1 135  ? -4.609   62.501  69.049  1.00 109.67 ? 135  TYR B CE1 1 
ATOM   15285 C  CE2 . TYR C 1 135  ? -6.697   63.655  69.271  1.00 108.09 ? 135  TYR B CE2 1 
ATOM   15286 C  CZ  . TYR C 1 135  ? -5.350   63.669  69.005  1.00 109.17 ? 135  TYR B CZ  1 
ATOM   15287 O  OH  . TYR C 1 135  ? -4.751   64.868  68.694  1.00 109.81 ? 135  TYR B OH  1 
ATOM   15288 N  N   . THR C 1 136  ? -7.621   57.108  69.259  1.00 108.14 ? 136  THR B N   1 
ATOM   15289 C  CA  . THR C 1 136  ? -7.995   55.771  69.638  1.00 109.21 ? 136  THR B CA  1 
ATOM   15290 C  C   . THR C 1 136  ? -7.197   55.407  70.876  1.00 111.04 ? 136  THR B C   1 
ATOM   15291 O  O   . THR C 1 136  ? -6.060   55.846  71.031  1.00 111.23 ? 136  THR B O   1 
ATOM   15292 C  CB  . THR C 1 136  ? -7.602   54.798  68.549  1.00 109.97 ? 136  THR B CB  1 
ATOM   15293 O  OG1 . THR C 1 136  ? -6.561   55.391  67.753  1.00 111.97 ? 136  THR B OG1 1 
ATOM   15294 C  CG2 . THR C 1 136  ? -8.805   54.493  67.687  1.00 108.68 ? 136  THR B CG2 1 
ATOM   15295 N  N   . PRO C 1 137  ? -7.792   54.598  71.760  1.00 108.41 ? 137  PRO B N   1 
ATOM   15296 C  CA  . PRO C 1 137  ? -7.141   54.188  72.993  1.00 110.11 ? 137  PRO B CA  1 
ATOM   15297 C  C   . PRO C 1 137  ? -5.629   54.151  72.857  1.00 111.44 ? 137  PRO B C   1 
ATOM   15298 O  O   . PRO C 1 137  ? -5.114   53.454  71.973  1.00 111.25 ? 137  PRO B O   1 
ATOM   15299 C  CB  . PRO C 1 137  ? -7.674   52.779  73.178  1.00 109.94 ? 137  PRO B CB  1 
ATOM   15300 C  CG  . PRO C 1 137  ? -9.051   52.828  72.610  1.00 108.19 ? 137  PRO B CG  1 
ATOM   15301 C  CD  . PRO C 1 137  ? -9.075   53.902  71.566  1.00 109.01 ? 137  PRO B CD  1 
ATOM   15302 N  N   . ASP C 1 138  ? -4.957   54.926  73.709  1.00 112.83 ? 138  ASP B N   1 
ATOM   15303 C  CA  . ASP C 1 138  ? -3.514   54.852  73.933  1.00 114.53 ? 138  ASP B CA  1 
ATOM   15304 C  C   . ASP C 1 138  ? -2.652   55.746  73.070  1.00 114.56 ? 138  ASP B C   1 
ATOM   15305 O  O   . ASP C 1 138  ? -1.446   55.796  73.268  1.00 118.66 ? 138  ASP B O   1 
ATOM   15306 C  CB  . ASP C 1 138  ? -3.018   53.407  73.865  1.00 122.56 ? 138  ASP B CB  1 
ATOM   15307 C  CG  . ASP C 1 138  ? -3.378   52.619  75.116  1.00 128.13 ? 138  ASP B CG  1 
ATOM   15308 O  OD1 . ASP C 1 138  ? -3.347   53.233  76.206  1.00 133.14 ? 138  ASP B OD1 1 
ATOM   15309 O  OD2 . ASP C 1 138  ? -3.699   51.408  75.024  1.00 130.05 ? 138  ASP B OD2 1 
ATOM   15310 N  N   . GLN C 1 139  ? -3.257   56.448  72.113  1.00 121.69 ? 139  GLN B N   1 
ATOM   15311 C  CA  . GLN C 1 139  ? -2.501   57.403  71.299  1.00 120.49 ? 139  GLN B CA  1 
ATOM   15312 C  C   . GLN C 1 139  ? -2.127   58.529  72.253  1.00 122.33 ? 139  GLN B C   1 
ATOM   15313 O  O   . GLN C 1 139  ? -2.703   58.641  73.341  1.00 123.20 ? 139  GLN B O   1 
ATOM   15314 C  CB  . GLN C 1 139  ? -3.306   57.966  70.099  1.00 120.30 ? 139  GLN B CB  1 
ATOM   15315 C  CG  . GLN C 1 139  ? -4.090   56.975  69.204  1.00 119.12 ? 139  GLN B CG  1 
ATOM   15316 C  CD  . GLN C 1 139  ? -4.210   57.471  67.762  1.00 118.84 ? 139  GLN B CD  1 
ATOM   15317 O  OE1 . GLN C 1 139  ? -5.313   57.678  67.222  1.00 115.97 ? 139  GLN B OE1 1 
ATOM   15318 N  NE2 . GLN C 1 139  ? -3.056   57.684  67.136  1.00 120.56 ? 139  GLN B NE2 1 
ATOM   15319 N  N   . SER C 1 140  ? -1.158   59.351  71.875  1.00 123.18 ? 140  SER B N   1 
ATOM   15320 C  CA  . SER C 1 140  ? -0.846   60.506  72.704  1.00 123.69 ? 140  SER B CA  1 
ATOM   15321 C  C   . SER C 1 140  ? -1.221   61.784  71.990  1.00 121.85 ? 140  SER B C   1 
ATOM   15322 O  O   . SER C 1 140  ? -0.660   62.112  70.953  1.00 119.38 ? 140  SER B O   1 
ATOM   15323 C  CB  . SER C 1 140  ? 0.623    60.520  73.142  1.00 126.41 ? 140  SER B CB  1 
ATOM   15324 O  OG  . SER C 1 140  ? 0.758    59.971  74.454  1.00 126.98 ? 140  SER B OG  1 
ATOM   15325 N  N   . VAL C 1 141  ? -2.186   62.494  72.555  1.00 119.95 ? 141  VAL B N   1 
ATOM   15326 C  CA  . VAL C 1 141  ? -2.667   63.741  71.979  1.00 117.76 ? 141  VAL B CA  1 
ATOM   15327 C  C   . VAL C 1 141  ? -1.569   64.781  71.980  1.00 117.83 ? 141  VAL B C   1 
ATOM   15328 O  O   . VAL C 1 141  ? -1.116   65.193  73.035  1.00 121.74 ? 141  VAL B O   1 
ATOM   15329 C  CB  . VAL C 1 141  ? -3.829   64.324  72.809  1.00 114.18 ? 141  VAL B CB  1 
ATOM   15330 C  CG1 . VAL C 1 141  ? -4.315   65.601  72.193  1.00 113.47 ? 141  VAL B CG1 1 
ATOM   15331 C  CG2 . VAL C 1 141  ? -4.972   63.322  72.945  1.00 112.87 ? 141  VAL B CG2 1 
ATOM   15332 N  N   . LYS C 1 142  ? -1.125   65.206  70.808  1.00 119.10 ? 142  LYS B N   1 
ATOM   15333 C  CA  . LYS C 1 142  ? -0.221   66.340  70.758  1.00 121.86 ? 142  LYS B CA  1 
ATOM   15334 C  C   . LYS C 1 142  ? -1.052   67.602  70.976  1.00 125.89 ? 142  LYS B C   1 
ATOM   15335 O  O   . LYS C 1 142  ? -2.199   67.656  70.537  1.00 126.92 ? 142  LYS B O   1 
ATOM   15336 C  CB  . LYS C 1 142  ? 0.532    66.391  69.427  1.00 121.89 ? 142  LYS B CB  1 
ATOM   15337 C  CG  . LYS C 1 142  ? 1.683    65.404  69.346  1.00 123.72 ? 142  LYS B CG  1 
ATOM   15338 C  CD  . LYS C 1 142  ? 2.822    65.958  68.501  1.00 125.53 ? 142  LYS B CD  1 
ATOM   15339 C  CE  . LYS C 1 142  ? 4.108    65.133  68.651  1.00 128.00 ? 142  LYS B CE  1 
ATOM   15340 N  NZ  . LYS C 1 142  ? 3.949    63.701  68.210  1.00 127.07 ? 142  LYS B NZ  1 
ATOM   15341 N  N   . VAL C 1 143  ? -0.505   68.602  71.671  1.00 127.08 ? 143  VAL B N   1 
ATOM   15342 C  CA  . VAL C 1 143  ? -1.233   69.868  71.859  1.00 125.93 ? 143  VAL B CA  1 
ATOM   15343 C  C   . VAL C 1 143  ? -0.360   71.115  72.052  1.00 125.47 ? 143  VAL B C   1 
ATOM   15344 O  O   . VAL C 1 143  ? 0.728    71.064  72.634  1.00 126.98 ? 143  VAL B O   1 
ATOM   15345 C  CB  . VAL C 1 143  ? -2.321   69.772  72.982  1.00 118.06 ? 143  VAL B CB  1 
ATOM   15346 C  CG1 . VAL C 1 143  ? -2.126   68.537  73.811  1.00 118.57 ? 143  VAL B CG1 1 
ATOM   15347 C  CG2 . VAL C 1 143  ? -2.332   71.020  73.847  1.00 119.61 ? 143  VAL B CG2 1 
ATOM   15348 N  N   . ARG C 1 144  ? -0.846   72.231  71.522  1.00 122.05 ? 144  ARG B N   1 
ATOM   15349 C  CA  . ARG C 1 144  ? -0.270   73.525  71.828  1.00 123.58 ? 144  ARG B CA  1 
ATOM   15350 C  C   . ARG C 1 144  ? -1.365   74.597  71.780  1.00 122.17 ? 144  ARG B C   1 
ATOM   15351 O  O   . ARG C 1 144  ? -2.515   74.306  71.418  1.00 118.85 ? 144  ARG B O   1 
ATOM   15352 C  CB  . ARG C 1 144  ? 0.901    73.861  70.898  1.00 125.18 ? 144  ARG B CB  1 
ATOM   15353 C  CG  . ARG C 1 144  ? 0.634    73.654  69.425  1.00 125.67 ? 144  ARG B CG  1 
ATOM   15354 C  CD  . ARG C 1 144  ? 1.602    74.453  68.548  1.00 128.15 ? 144  ARG B CD  1 
ATOM   15355 N  NE  . ARG C 1 144  ? 1.588    73.923  67.195  1.00 128.20 ? 144  ARG B NE  1 
ATOM   15356 C  CZ  . ARG C 1 144  ? 2.247    72.830  66.823  1.00 130.18 ? 144  ARG B CZ  1 
ATOM   15357 N  NH1 . ARG C 1 144  ? 2.990    72.174  67.703  1.00 131.62 ? 144  ARG B NH1 1 
ATOM   15358 N  NH2 . ARG C 1 144  ? 2.168    72.393  65.573  1.00 129.85 ? 144  ARG B NH2 1 
ATOM   15359 N  N   . VAL C 1 145  ? -1.010   75.822  72.176  1.00 124.14 ? 145  VAL B N   1 
ATOM   15360 C  CA  . VAL C 1 145  ? -1.957   76.917  72.267  1.00 122.14 ? 145  VAL B CA  1 
ATOM   15361 C  C   . VAL C 1 145  ? -1.326   78.114  71.621  1.00 123.08 ? 145  VAL B C   1 
ATOM   15362 O  O   . VAL C 1 145  ? -0.209   78.474  71.969  1.00 124.99 ? 145  VAL B O   1 
ATOM   15363 C  CB  . VAL C 1 145  ? -2.246   77.314  73.719  1.00 123.70 ? 145  VAL B CB  1 
ATOM   15364 C  CG1 . VAL C 1 145  ? -2.893   78.661  73.741  1.00 124.08 ? 145  VAL B CG1 1 
ATOM   15365 C  CG2 . VAL C 1 145  ? -3.153   76.314  74.386  1.00 122.70 ? 145  VAL B CG2 1 
ATOM   15366 N  N   . TYR C 1 146  ? -2.028   78.695  70.647  1.00 123.16 ? 146  TYR B N   1 
ATOM   15367 C  CA  . TYR C 1 146  ? -1.691   80.013  70.108  1.00 125.38 ? 146  TYR B CA  1 
ATOM   15368 C  C   . TYR C 1 146  ? -2.544   81.000  70.864  1.00 128.67 ? 146  TYR B C   1 
ATOM   15369 O  O   . TYR C 1 146  ? -3.767   80.862  70.883  1.00 127.40 ? 146  TYR B O   1 
ATOM   15370 C  CB  . TYR C 1 146  ? -1.964   80.110  68.606  1.00 121.12 ? 146  TYR B CB  1 
ATOM   15371 C  CG  . TYR C 1 146  ? -1.379   78.955  67.850  1.00 125.94 ? 146  TYR B CG  1 
ATOM   15372 C  CD1 . TYR C 1 146  ? -0.012   78.734  67.825  1.00 128.13 ? 146  TYR B CD1 1 
ATOM   15373 C  CD2 . TYR C 1 146  ? -2.193   78.057  67.180  1.00 124.33 ? 146  TYR B CD2 1 
ATOM   15374 C  CE1 . TYR C 1 146  ? 0.530    77.641  67.140  1.00 127.28 ? 146  TYR B CE1 1 
ATOM   15375 C  CE2 . TYR C 1 146  ? -1.664   76.973  66.486  1.00 122.94 ? 146  TYR B CE2 1 
ATOM   15376 C  CZ  . TYR C 1 146  ? -0.308   76.769  66.472  1.00 123.95 ? 146  TYR B CZ  1 
ATOM   15377 O  OH  . TYR C 1 146  ? 0.210    75.691  65.791  1.00 122.36 ? 146  TYR B OH  1 
ATOM   15378 N  N   . SER C 1 147  ? -1.904   81.975  71.507  1.00 131.98 ? 147  SER B N   1 
ATOM   15379 C  CA  . SER C 1 147  ? -2.639   82.942  72.310  1.00 135.53 ? 147  SER B CA  1 
ATOM   15380 C  C   . SER C 1 147  ? -2.248   84.369  71.950  1.00 137.81 ? 147  SER B C   1 
ATOM   15381 O  O   . SER C 1 147  ? -1.065   84.690  71.842  1.00 139.99 ? 147  SER B O   1 
ATOM   15382 C  CB  . SER C 1 147  ? -2.448   82.682  73.816  1.00 138.94 ? 147  SER B CB  1 
ATOM   15383 O  OG  . SER C 1 147  ? -1.264   83.275  74.336  1.00 143.01 ? 147  SER B OG  1 
ATOM   15384 N  N   . LEU C 1 148  ? -3.255   85.218  71.769  1.00 137.35 ? 148  LEU B N   1 
ATOM   15385 C  CA  . LEU C 1 148  ? -3.049   86.607  71.402  1.00 140.27 ? 148  LEU B CA  1 
ATOM   15386 C  C   . LEU C 1 148  ? -3.804   87.489  72.370  1.00 143.47 ? 148  LEU B C   1 
ATOM   15387 O  O   . LEU C 1 148  ? -4.745   87.036  73.008  1.00 149.06 ? 148  LEU B O   1 
ATOM   15388 C  CB  . LEU C 1 148  ? -3.585   86.840  70.000  1.00 134.51 ? 148  LEU B CB  1 
ATOM   15389 C  CG  . LEU C 1 148  ? -2.638   86.498  68.856  1.00 133.49 ? 148  LEU B CG  1 
ATOM   15390 C  CD1 . LEU C 1 148  ? -1.656   85.415  69.222  1.00 133.36 ? 148  LEU B CD1 1 
ATOM   15391 C  CD2 . LEU C 1 148  ? -3.437   86.085  67.657  1.00 132.36 ? 148  LEU B CD2 1 
ATOM   15392 N  N   . ASN C 1 149  ? -3.384   88.746  72.480  1.00 144.11 ? 149  ASN B N   1 
ATOM   15393 C  CA  . ASN C 1 149  ? -4.081   89.754  73.275  1.00 143.14 ? 149  ASN B CA  1 
ATOM   15394 C  C   . ASN C 1 149  ? -4.859   90.732  72.389  1.00 139.06 ? 149  ASN B C   1 
ATOM   15395 O  O   . ASN C 1 149  ? -4.573   90.846  71.195  1.00 137.91 ? 149  ASN B O   1 
ATOM   15396 C  CB  . ASN C 1 149  ? -3.052   90.562  74.025  1.00 148.57 ? 149  ASN B CB  1 
ATOM   15397 C  CG  . ASN C 1 149  ? -2.147   91.322  73.083  1.00 152.68 ? 149  ASN B CG  1 
ATOM   15398 O  OD1 . ASN C 1 149  ? -1.824   90.834  71.995  1.00 152.42 ? 149  ASN B OD1 1 
ATOM   15399 N  ND2 . ASN C 1 149  ? -1.750   92.530  73.476  1.00 157.00 ? 149  ASN B ND2 1 
ATOM   15400 N  N   . ASP C 1 150  ? -5.797   91.466  72.986  1.00 140.74 ? 150  ASP B N   1 
ATOM   15401 C  CA  . ASP C 1 150  ? -6.577   92.492  72.289  1.00 138.48 ? 150  ASP B CA  1 
ATOM   15402 C  C   . ASP C 1 150  ? -5.930   93.042  71.031  1.00 139.50 ? 150  ASP B C   1 
ATOM   15403 O  O   . ASP C 1 150  ? -6.621   93.466  70.124  1.00 136.03 ? 150  ASP B O   1 
ATOM   15404 C  CB  . ASP C 1 150  ? -6.897   93.677  73.226  1.00 145.22 ? 150  ASP B CB  1 
ATOM   15405 C  CG  . ASP C 1 150  ? -5.632   94.381  73.802  1.00 161.41 ? 150  ASP B CG  1 
ATOM   15406 O  OD1 . ASP C 1 150  ? -5.440   95.598  73.562  1.00 161.31 ? 150  ASP B OD1 1 
ATOM   15407 O  OD2 . ASP C 1 150  ? -4.845   93.723  74.516  1.00 163.32 ? 150  ASP B OD2 1 
ATOM   15408 N  N   . ASP C 1 151  ? -4.605   93.046  70.985  1.00 141.36 ? 151  ASP B N   1 
ATOM   15409 C  CA  . ASP C 1 151  ? -3.864   93.671  69.900  1.00 145.01 ? 151  ASP B CA  1 
ATOM   15410 C  C   . ASP C 1 151  ? -3.278   92.634  68.968  1.00 144.63 ? 151  ASP B C   1 
ATOM   15411 O  O   . ASP C 1 151  ? -2.351   92.932  68.224  1.00 145.28 ? 151  ASP B O   1 
ATOM   15412 C  CB  . ASP C 1 151  ? -2.736   94.538  70.469  1.00 152.11 ? 151  ASP B CB  1 
ATOM   15413 C  CG  . ASP C 1 151  ? -2.530   95.838  69.694  1.00 155.01 ? 151  ASP B CG  1 
ATOM   15414 O  OD1 . ASP C 1 151  ? -1.574   96.577  70.032  1.00 157.96 ? 151  ASP B OD1 1 
ATOM   15415 O  OD2 . ASP C 1 151  ? -3.321   96.130  68.767  1.00 154.85 ? 151  ASP B OD2 1 
ATOM   15416 N  N   . LEU C 1 152  ? -3.806   91.416  69.025  1.00 143.58 ? 152  LEU B N   1 
ATOM   15417 C  CA  . LEU C 1 152  ? -3.365   90.328  68.146  1.00 145.18 ? 152  LEU B CA  1 
ATOM   15418 C  C   . LEU C 1 152  ? -1.844   90.216  68.027  1.00 149.27 ? 152  LEU B C   1 
ATOM   15419 O  O   . LEU C 1 152  ? -1.328   89.946  66.930  1.00 147.65 ? 152  LEU B O   1 
ATOM   15420 C  CB  . LEU C 1 152  ? -3.961   90.466  66.738  1.00 144.26 ? 152  LEU B CB  1 
ATOM   15421 C  CG  . LEU C 1 152  ? -5.478   90.461  66.613  1.00 143.54 ? 152  LEU B CG  1 
ATOM   15422 C  CD1 . LEU C 1 152  ? -6.079   89.539  67.655  1.00 142.30 ? 152  LEU B CD1 1 
ATOM   15423 C  CD2 . LEU C 1 152  ? -6.002   91.876  66.776  1.00 146.22 ? 152  LEU B CD2 1 
ATOM   15424 N  N   . LYS C 1 153  ? -1.137   90.461  69.133  1.00 152.86 ? 153  LYS B N   1 
ATOM   15425 C  CA  . LYS C 1 153  ? 0.307    90.229  69.207  1.00 155.75 ? 153  LYS B CA  1 
ATOM   15426 C  C   . LYS C 1 153  ? 0.622    89.170  70.265  1.00 155.43 ? 153  LYS B C   1 
ATOM   15427 O  O   . LYS C 1 153  ? -0.218   88.878  71.117  1.00 153.33 ? 153  LYS B O   1 
ATOM   15428 C  CB  . LYS C 1 153  ? 1.057    91.532  69.479  1.00 159.24 ? 153  LYS B CB  1 
ATOM   15429 C  CG  . LYS C 1 153  ? 1.500    92.273  68.227  1.00 160.34 ? 153  LYS B CG  1 
ATOM   15430 C  CD  . LYS C 1 153  ? 2.026    93.670  68.560  1.00 164.12 ? 153  LYS B CD  1 
ATOM   15431 C  CE  . LYS C 1 153  ? 2.299    94.493  67.289  1.00 165.83 ? 153  LYS B CE  1 
ATOM   15432 N  NZ  . LYS C 1 153  ? 1.181    94.459  66.274  1.00 163.72 ? 153  LYS B NZ  1 
ATOM   15433 N  N   . PRO C 1 154  ? 1.838    88.599  70.217  1.00 160.86 ? 154  PRO B N   1 
ATOM   15434 C  CA  . PRO C 1 154  ? 2.221    87.421  70.999  1.00 162.44 ? 154  PRO B CA  1 
ATOM   15435 C  C   . PRO C 1 154  ? 1.369    87.217  72.239  1.00 167.83 ? 154  PRO B C   1 
ATOM   15436 O  O   . PRO C 1 154  ? 0.868    86.119  72.446  1.00 166.96 ? 154  PRO B O   1 
ATOM   15437 C  CB  . PRO C 1 154  ? 3.666    87.731  71.379  1.00 165.75 ? 154  PRO B CB  1 
ATOM   15438 C  CG  . PRO C 1 154  ? 4.190    88.505  70.199  1.00 165.33 ? 154  PRO B CG  1 
ATOM   15439 C  CD  . PRO C 1 154  ? 2.995    89.140  69.482  1.00 162.64 ? 154  PRO B CD  1 
ATOM   15440 N  N   . ALA C 1 155  ? 1.217    88.260  73.046  1.00 171.92 ? 155  ALA B N   1 
ATOM   15441 C  CA  . ALA C 1 155  ? 0.352    88.210  74.225  1.00 175.52 ? 155  ALA B CA  1 
ATOM   15442 C  C   . ALA C 1 155  ? 0.912    87.371  75.386  1.00 179.88 ? 155  ALA B C   1 
ATOM   15443 O  O   . ALA C 1 155  ? 0.144    86.741  76.120  1.00 180.07 ? 155  ALA B O   1 
ATOM   15444 C  CB  . ALA C 1 155  ? -1.024   87.699  73.833  1.00 171.08 ? 155  ALA B CB  1 
ATOM   15445 N  N   . LYS C 1 156  ? 2.233    87.367  75.559  1.00 183.27 ? 156  LYS B N   1 
ATOM   15446 C  CA  . LYS C 1 156  ? 2.867    86.463  76.515  1.00 184.15 ? 156  LYS B CA  1 
ATOM   15447 C  C   . LYS C 1 156  ? 2.139    86.509  77.843  1.00 181.82 ? 156  LYS B C   1 
ATOM   15448 O  O   . LYS C 1 156  ? 1.792    87.578  78.324  1.00 182.84 ? 156  LYS B O   1 
ATOM   15449 C  CB  . LYS C 1 156  ? 4.338    86.823  76.702  1.00 188.99 ? 156  LYS B CB  1 
ATOM   15450 C  CG  . LYS C 1 156  ? 5.179    86.617  75.465  1.00 189.70 ? 156  LYS B CG  1 
ATOM   15451 C  CD  . LYS C 1 156  ? 6.281    87.650  75.370  1.00 194.22 ? 156  LYS B CD  1 
ATOM   15452 C  CE  . LYS C 1 156  ? 6.604    87.956  73.917  1.00 195.08 ? 156  LYS B CE  1 
ATOM   15453 N  NZ  . LYS C 1 156  ? 7.409    89.196  73.762  1.00 199.28 ? 156  LYS B NZ  1 
ATOM   15454 N  N   . ARG C 1 157  ? 1.904    85.341  78.423  1.00 178.78 ? 157  ARG B N   1 
ATOM   15455 C  CA  . ARG C 1 157  ? 1.157    85.220  79.662  1.00 176.72 ? 157  ARG B CA  1 
ATOM   15456 C  C   . ARG C 1 157  ? 1.282    83.780  80.091  1.00 179.32 ? 157  ARG B C   1 
ATOM   15457 O  O   . ARG C 1 157  ? 1.762    82.958  79.327  1.00 179.12 ? 157  ARG B O   1 
ATOM   15458 C  CB  . ARG C 1 157  ? -0.315   85.534  79.417  1.00 169.64 ? 157  ARG B CB  1 
ATOM   15459 C  CG  . ARG C 1 157  ? -0.589   86.955  79.003  1.00 165.01 ? 157  ARG B CG  1 
ATOM   15460 C  CD  . ARG C 1 157  ? -1.986   87.146  78.482  1.00 159.05 ? 157  ARG B CD  1 
ATOM   15461 N  NE  . ARG C 1 157  ? -2.206   88.535  78.103  1.00 157.97 ? 157  ARG B NE  1 
ATOM   15462 C  CZ  . ARG C 1 157  ? -3.382   89.037  77.741  1.00 155.68 ? 157  ARG B CZ  1 
ATOM   15463 N  NH1 . ARG C 1 157  ? -4.454   88.256  77.712  1.00 153.24 ? 157  ARG B NH1 1 
ATOM   15464 N  NH2 . ARG C 1 157  ? -3.484   90.323  77.416  1.00 156.20 ? 157  ARG B NH2 1 
ATOM   15465 N  N   . GLU C 1 158  ? 0.854    83.448  81.299  1.00 181.54 ? 158  GLU B N   1 
ATOM   15466 C  CA  . GLU C 1 158  ? 0.765    82.032  81.636  1.00 182.92 ? 158  GLU B CA  1 
ATOM   15467 C  C   . GLU C 1 158  ? -0.674   81.510  81.589  1.00 178.05 ? 158  GLU B C   1 
ATOM   15468 O  O   . GLU C 1 158  ? -1.573   82.071  82.223  1.00 179.31 ? 158  GLU B O   1 
ATOM   15469 C  CB  . GLU C 1 158  ? 1.430    81.729  82.972  1.00 190.45 ? 158  GLU B CB  1 
ATOM   15470 C  CG  . GLU C 1 158  ? 2.940    81.810  82.914  1.00 197.18 ? 158  GLU B CG  1 
ATOM   15471 C  CD  . GLU C 1 158  ? 3.587    81.196  84.129  1.00 203.64 ? 158  GLU B CD  1 
ATOM   15472 O  OE1 . GLU C 1 158  ? 3.334    80.000  84.387  1.00 203.51 ? 158  GLU B OE1 1 
ATOM   15473 O  OE2 . GLU C 1 158  ? 4.349    81.906  84.821  1.00 208.06 ? 158  GLU B OE2 1 
ATOM   15474 N  N   . THR C 1 159  ? -0.868   80.433  80.827  1.00 171.35 ? 159  THR B N   1 
ATOM   15475 C  CA  . THR C 1 159  ? -2.192   79.902  80.506  1.00 163.39 ? 159  THR B CA  1 
ATOM   15476 C  C   . THR C 1 159  ? -2.425   78.516  81.096  1.00 153.67 ? 159  THR B C   1 
ATOM   15477 O  O   . THR C 1 159  ? -1.475   77.784  81.365  1.00 153.21 ? 159  THR B O   1 
ATOM   15478 C  CB  . THR C 1 159  ? -2.375   79.809  78.985  1.00 164.16 ? 159  THR B CB  1 
ATOM   15479 O  OG1 . THR C 1 159  ? -2.067   81.077  78.383  1.00 166.30 ? 159  THR B OG1 1 
ATOM   15480 C  CG2 . THR C 1 159  ? -3.801   79.407  78.644  1.00 163.21 ? 159  THR B CG2 1 
ATOM   15481 N  N   . VAL C 1 160  ? -3.687   78.143  81.276  1.00 145.87 ? 160  VAL B N   1 
ATOM   15482 C  CA  . VAL C 1 160  ? -3.983   76.871  81.912  1.00 141.63 ? 160  VAL B CA  1 
ATOM   15483 C  C   . VAL C 1 160  ? -5.180   76.117  81.395  1.00 138.45 ? 160  VAL B C   1 
ATOM   15484 O  O   . VAL C 1 160  ? -6.324   76.550  81.549  1.00 136.63 ? 160  VAL B O   1 
ATOM   15485 C  CB  . VAL C 1 160  ? -4.223   77.040  83.375  1.00 142.44 ? 160  VAL B CB  1 
ATOM   15486 C  CG1 . VAL C 1 160  ? -5.434   76.234  83.785  1.00 141.49 ? 160  VAL B CG1 1 
ATOM   15487 C  CG2 . VAL C 1 160  ? -3.024   76.575  84.125  1.00 145.23 ? 160  VAL B CG2 1 
ATOM   15488 N  N   . LEU C 1 161  ? -4.906   74.955  80.816  1.00 138.14 ? 161  LEU B N   1 
ATOM   15489 C  CA  . LEU C 1 161  ? -5.973   74.124  80.283  1.00 136.94 ? 161  LEU B CA  1 
ATOM   15490 C  C   . LEU C 1 161  ? -6.311   72.958  81.185  1.00 136.45 ? 161  LEU B C   1 
ATOM   15491 O  O   . LEU C 1 161  ? -5.620   72.689  82.170  1.00 139.32 ? 161  LEU B O   1 
ATOM   15492 C  CB  . LEU C 1 161  ? -5.697   73.667  78.845  1.00 133.29 ? 161  LEU B CB  1 
ATOM   15493 C  CG  . LEU C 1 161  ? -4.237   73.563  78.444  1.00 132.44 ? 161  LEU B CG  1 
ATOM   15494 C  CD1 . LEU C 1 161  ? -3.628   72.412  79.173  1.00 133.75 ? 161  LEU B CD1 1 
ATOM   15495 C  CD2 . LEU C 1 161  ? -4.114   73.379  76.955  1.00 129.62 ? 161  LEU B CD2 1 
ATOM   15496 N  N   . THR C 1 162  ? -7.382   72.266  80.816  1.00 133.49 ? 162  THR B N   1 
ATOM   15497 C  CA  . THR C 1 162  ? -8.052   71.334  81.703  1.00 131.29 ? 162  THR B CA  1 
ATOM   15498 C  C   . THR C 1 162  ? -8.967   70.412  80.896  1.00 129.37 ? 162  THR B C   1 
ATOM   15499 O  O   . THR C 1 162  ? -10.145  70.708  80.707  1.00 128.35 ? 162  THR B O   1 
ATOM   15500 C  CB  . THR C 1 162  ? -8.864   72.104  82.798  1.00 156.83 ? 162  THR B CB  1 
ATOM   15501 O  OG1 . THR C 1 162  ? -10.068  71.391  83.120  1.00 155.34 ? 162  THR B OG1 1 
ATOM   15502 C  CG2 . THR C 1 162  ? -9.222   73.550  82.345  1.00 153.64 ? 162  THR B CG2 1 
ATOM   15503 N  N   . PHE C 1 163  ? -8.417   69.294  80.424  1.00 128.44 ? 163  PHE B N   1 
ATOM   15504 C  CA  . PHE C 1 163  ? -9.167   68.285  79.660  1.00 126.08 ? 163  PHE B CA  1 
ATOM   15505 C  C   . PHE C 1 163  ? -10.430  67.782  80.340  1.00 126.28 ? 163  PHE B C   1 
ATOM   15506 O  O   . PHE C 1 163  ? -10.433  67.502  81.532  1.00 129.02 ? 163  PHE B O   1 
ATOM   15507 C  CB  . PHE C 1 163  ? -8.288   67.071  79.421  1.00 125.00 ? 163  PHE B CB  1 
ATOM   15508 C  CG  . PHE C 1 163  ? -6.988   67.394  78.808  1.00 124.24 ? 163  PHE B CG  1 
ATOM   15509 C  CD1 . PHE C 1 163  ? -6.084   68.186  79.477  1.00 126.95 ? 163  PHE B CD1 1 
ATOM   15510 C  CD2 . PHE C 1 163  ? -6.664   66.900  77.558  1.00 122.16 ? 163  PHE B CD2 1 
ATOM   15511 C  CE1 . PHE C 1 163  ? -4.883   68.480  78.913  1.00 128.89 ? 163  PHE B CE1 1 
ATOM   15512 C  CE2 . PHE C 1 163  ? -5.467   67.189  76.976  1.00 122.93 ? 163  PHE B CE2 1 
ATOM   15513 C  CZ  . PHE C 1 163  ? -4.570   67.978  77.647  1.00 127.18 ? 163  PHE B CZ  1 
ATOM   15514 N  N   . ILE C 1 164  ? -11.493  67.596  79.582  1.00 124.34 ? 164  ILE B N   1 
ATOM   15515 C  CA  . ILE C 1 164  ? -12.733  67.223  80.210  1.00 127.38 ? 164  ILE B CA  1 
ATOM   15516 C  C   . ILE C 1 164  ? -13.363  66.041  79.543  1.00 128.02 ? 164  ILE B C   1 
ATOM   15517 O  O   . ILE C 1 164  ? -13.802  66.121  78.409  1.00 126.88 ? 164  ILE B O   1 
ATOM   15518 C  CB  . ILE C 1 164  ? -13.724  68.346  80.130  1.00 130.12 ? 164  ILE B CB  1 
ATOM   15519 C  CG1 . ILE C 1 164  ? -13.110  69.640  80.679  1.00 134.58 ? 164  ILE B CG1 1 
ATOM   15520 C  CG2 . ILE C 1 164  ? -14.978  67.961  80.873  1.00 131.29 ? 164  ILE B CG2 1 
ATOM   15521 C  CD1 . ILE C 1 164  ? -14.077  70.831  80.705  1.00 135.23 ? 164  ILE B CD1 1 
ATOM   15522 N  N   . ASP C 1 165  ? -13.441  64.937  80.263  1.00 132.60 ? 165  ASP B N   1 
ATOM   15523 C  CA  . ASP C 1 165  ? -13.889  63.693  79.654  1.00 134.82 ? 165  ASP B CA  1 
ATOM   15524 C  C   . ASP C 1 165  ? -15.276  63.847  79.064  1.00 128.95 ? 165  ASP B C   1 
ATOM   15525 O  O   . ASP C 1 165  ? -16.000  64.771  79.392  1.00 125.28 ? 165  ASP B O   1 
ATOM   15526 C  CB  . ASP C 1 165  ? -13.814  62.515  80.643  1.00 145.56 ? 165  ASP B CB  1 
ATOM   15527 C  CG  . ASP C 1 165  ? -15.031  62.429  81.567  1.00 154.96 ? 165  ASP B CG  1 
ATOM   15528 O  OD1 . ASP C 1 165  ? -15.910  63.338  81.525  1.00 157.54 ? 165  ASP B OD1 1 
ATOM   15529 O  OD2 . ASP C 1 165  ? -15.093  61.439  82.345  1.00 158.84 ? 165  ASP B OD2 1 
ATOM   15530 N  N   . PRO C 1 166  ? -15.646  62.919  78.194  1.00 128.76 ? 166  PRO B N   1 
ATOM   15531 C  CA  . PRO C 1 166  ? -16.899  62.969  77.445  1.00 127.88 ? 166  PRO B CA  1 
ATOM   15532 C  C   . PRO C 1 166  ? -18.120  62.963  78.337  1.00 126.03 ? 166  PRO B C   1 
ATOM   15533 O  O   . PRO C 1 166  ? -19.225  62.824  77.832  1.00 124.19 ? 166  PRO B O   1 
ATOM   15534 C  CB  . PRO C 1 166  ? -16.868  61.677  76.624  1.00 128.63 ? 166  PRO B CB  1 
ATOM   15535 C  CG  . PRO C 1 166  ? -15.437  61.295  76.550  1.00 130.55 ? 166  PRO B CG  1 
ATOM   15536 C  CD  . PRO C 1 166  ? -14.823  61.754  77.833  1.00 131.53 ? 166  PRO B CD  1 
ATOM   15537 N  N   . GLU C 1 167  ? -17.946  63.087  79.639  1.00 127.54 ? 167  GLU B N   1 
ATOM   15538 C  CA  . GLU C 1 167  ? -19.112  63.097  80.492  1.00 129.33 ? 167  GLU B CA  1 
ATOM   15539 C  C   . GLU C 1 167  ? -19.146  64.389  81.245  1.00 130.94 ? 167  GLU B C   1 
ATOM   15540 O  O   . GLU C 1 167  ? -20.145  64.735  81.859  1.00 132.75 ? 167  GLU B O   1 
ATOM   15541 C  CB  . GLU C 1 167  ? -19.107  61.927  81.455  1.00 133.49 ? 167  GLU B CB  1 
ATOM   15542 C  CG  . GLU C 1 167  ? -19.661  60.649  80.876  1.00 135.49 ? 167  GLU B CG  1 
ATOM   15543 C  CD  . GLU C 1 167  ? -19.707  59.540  81.911  1.00 140.35 ? 167  GLU B CD  1 
ATOM   15544 O  OE1 . GLU C 1 167  ? -20.584  59.604  82.805  1.00 141.49 ? 167  GLU B OE1 1 
ATOM   15545 O  OE2 . GLU C 1 167  ? -18.867  58.608  81.836  1.00 142.28 ? 167  GLU B OE2 1 
ATOM   15546 N  N   . GLY C 1 168  ? -18.052  65.124  81.177  1.00 130.72 ? 168  GLY B N   1 
ATOM   15547 C  CA  . GLY C 1 168  ? -18.068  66.470  81.696  1.00 132.86 ? 168  GLY B CA  1 
ATOM   15548 C  C   . GLY C 1 168  ? -17.541  66.559  83.101  1.00 137.55 ? 168  GLY B C   1 
ATOM   15549 O  O   . GLY C 1 168  ? -17.904  67.471  83.855  1.00 139.43 ? 168  GLY B O   1 
ATOM   15550 N  N   . SER C 1 169  ? -16.704  65.600  83.475  1.00 140.31 ? 169  SER B N   1 
ATOM   15551 C  CA  . SER C 1 169  ? -15.881  65.812  84.647  1.00 145.39 ? 169  SER B CA  1 
ATOM   15552 C  C   . SER C 1 169  ? -14.465  66.102  84.197  1.00 143.93 ? 169  SER B C   1 
ATOM   15553 O  O   . SER C 1 169  ? -13.999  65.561  83.200  1.00 141.72 ? 169  SER B O   1 
ATOM   15554 C  CB  . SER C 1 169  ? -15.914  64.626  85.606  1.00 150.87 ? 169  SER B CB  1 
ATOM   15555 O  OG  . SER C 1 169  ? -15.380  65.010  86.870  1.00 154.87 ? 169  SER B OG  1 
ATOM   15556 N  N   . GLU C 1 170  ? -13.788  66.977  84.925  1.00 144.38 ? 170  GLU B N   1 
ATOM   15557 C  CA  . GLU C 1 170  ? -12.405  67.286  84.619  1.00 145.63 ? 170  GLU B CA  1 
ATOM   15558 C  C   . GLU C 1 170  ? -11.643  65.981  84.687  1.00 140.87 ? 170  GLU B C   1 
ATOM   15559 O  O   . GLU C 1 170  ? -12.192  64.972  85.120  1.00 138.25 ? 170  GLU B O   1 
ATOM   15560 C  CB  . GLU C 1 170  ? -11.841  68.284  85.635  1.00 154.55 ? 170  GLU B CB  1 
ATOM   15561 C  CG  . GLU C 1 170  ? -12.588  69.629  85.720  1.00 160.57 ? 170  GLU B CG  1 
ATOM   15562 C  CD  . GLU C 1 170  ? -11.941  70.600  86.703  1.00 169.10 ? 170  GLU B CD  1 
ATOM   15563 O  OE1 . GLU C 1 170  ? -11.656  70.185  87.858  1.00 173.21 ? 170  GLU B OE1 1 
ATOM   15564 O  OE2 . GLU C 1 170  ? -11.719  71.773  86.315  1.00 170.53 ? 170  GLU B OE2 1 
ATOM   15565 N  N   . VAL C 1 171  ? -10.387  65.981  84.263  1.00 139.90 ? 171  VAL B N   1 
ATOM   15566 C  CA  . VAL C 1 171  ? -9.589   64.770  84.373  1.00 141.23 ? 171  VAL B CA  1 
ATOM   15567 C  C   . VAL C 1 171  ? -8.115   65.090  84.489  1.00 137.80 ? 171  VAL B C   1 
ATOM   15568 O  O   . VAL C 1 171  ? -7.317   64.234  84.848  1.00 139.20 ? 171  VAL B O   1 
ATOM   15569 C  CB  . VAL C 1 171  ? -9.811   63.797  83.189  1.00 143.10 ? 171  VAL B CB  1 
ATOM   15570 C  CG1 . VAL C 1 171  ? -8.794   62.661  83.220  1.00 145.17 ? 171  VAL B CG1 1 
ATOM   15571 C  CG2 . VAL C 1 171  ? -11.226  63.225  83.197  1.00 143.08 ? 171  VAL B CG2 1 
ATOM   15572 N  N   . ASP C 1 172  ? -7.747   66.325  84.198  1.00 135.62 ? 172  ASP B N   1 
ATOM   15573 C  CA  . ASP C 1 172  ? -6.341   66.713  84.275  1.00 138.36 ? 172  ASP B CA  1 
ATOM   15574 C  C   . ASP C 1 172  ? -6.264   68.238  84.357  1.00 139.76 ? 172  ASP B C   1 
ATOM   15575 O  O   . ASP C 1 172  ? -7.281   68.918  84.533  1.00 139.00 ? 172  ASP B O   1 
ATOM   15576 C  CB  . ASP C 1 172  ? -5.574   66.172  83.054  1.00 139.27 ? 172  ASP B CB  1 
ATOM   15577 C  CG  . ASP C 1 172  ? -4.059   66.095  83.266  1.00 143.63 ? 172  ASP B CG  1 
ATOM   15578 O  OD1 . ASP C 1 172  ? -3.434   65.171  82.687  1.00 143.82 ? 172  ASP B OD1 1 
ATOM   15579 O  OD2 . ASP C 1 172  ? -3.494   66.951  83.984  1.00 146.73 ? 172  ASP B OD2 1 
ATOM   15580 N  N   . MET C 1 173  ? -5.061   68.776  84.235  1.00 141.73 ? 173  MET B N   1 
ATOM   15581 C  CA  . MET C 1 173  ? -4.880   70.204  84.282  1.00 142.01 ? 173  MET B CA  1 
ATOM   15582 C  C   . MET C 1 173  ? -3.405   70.416  84.107  1.00 141.25 ? 173  MET B C   1 
ATOM   15583 O  O   . MET C 1 173  ? -2.619   69.523  84.402  1.00 143.05 ? 173  MET B O   1 
ATOM   15584 C  CB  . MET C 1 173  ? -5.343   70.738  85.636  1.00 145.85 ? 173  MET B CB  1 
ATOM   15585 C  CG  . MET C 1 173  ? -5.864   72.162  85.589  1.00 148.00 ? 173  MET B CG  1 
ATOM   15586 S  SD  . MET C 1 173  ? -6.960   72.657  86.945  1.00 165.11 ? 173  MET B SD  1 
ATOM   15587 C  CE  . MET C 1 173  ? -7.933   71.162  87.147  1.00 156.22 ? 173  MET B CE  1 
ATOM   15588 N  N   . VAL C 1 174  ? -3.029   71.577  83.593  1.00 139.09 ? 174  VAL B N   1 
ATOM   15589 C  CA  . VAL C 1 174  ? -1.622   71.975  83.564  1.00 140.83 ? 174  VAL B CA  1 
ATOM   15590 C  C   . VAL C 1 174  ? -1.398   73.391  83.015  1.00 141.68 ? 174  VAL B C   1 
ATOM   15591 O  O   . VAL C 1 174  ? -2.029   73.788  82.039  1.00 142.08 ? 174  VAL B O   1 
ATOM   15592 C  CB  . VAL C 1 174  ? -0.735   70.950  82.808  1.00 145.45 ? 174  VAL B CB  1 
ATOM   15593 C  CG1 . VAL C 1 174  ? -1.501   70.296  81.670  1.00 142.39 ? 174  VAL B CG1 1 
ATOM   15594 C  CG2 . VAL C 1 174  ? 0.543    71.615  82.310  1.00 146.58 ? 174  VAL B CG2 1 
ATOM   15595 N  N   . GLU C 1 175  ? -0.520   74.152  83.664  1.00 141.35 ? 175  GLU B N   1 
ATOM   15596 C  CA  . GLU C 1 175  ? -0.149   75.483  83.214  1.00 141.71 ? 175  GLU B CA  1 
ATOM   15597 C  C   . GLU C 1 175  ? 1.183    75.415  82.487  1.00 141.06 ? 175  GLU B C   1 
ATOM   15598 O  O   . GLU C 1 175  ? 1.813    74.368  82.490  1.00 138.85 ? 175  GLU B O   1 
ATOM   15599 C  CB  . GLU C 1 175  ? -0.079   76.416  84.416  1.00 148.93 ? 175  GLU B CB  1 
ATOM   15600 C  CG  . GLU C 1 175  ? 0.017    75.684  85.759  1.00 153.92 ? 175  GLU B CG  1 
ATOM   15601 C  CD  . GLU C 1 175  ? -0.635   76.428  86.936  1.00 156.35 ? 175  GLU B CD  1 
ATOM   15602 O  OE1 . GLU C 1 175  ? -0.325   77.620  87.175  1.00 157.67 ? 175  GLU B OE1 1 
ATOM   15603 O  OE2 . GLU C 1 175  ? -1.461   75.799  87.632  1.00 156.29 ? 175  GLU B OE2 1 
ATOM   15604 N  N   . GLU C 1 176  ? 1.595    76.508  81.843  1.00 142.99 ? 176  GLU B N   1 
ATOM   15605 C  CA  . GLU C 1 176  ? 2.890    76.584  81.139  1.00 147.00 ? 176  GLU B CA  1 
ATOM   15606 C  C   . GLU C 1 176  ? 3.178    78.041  80.758  1.00 151.46 ? 176  GLU B C   1 
ATOM   15607 O  O   . GLU C 1 176  ? 2.262    78.864  80.710  1.00 150.98 ? 176  GLU B O   1 
ATOM   15608 C  CB  . GLU C 1 176  ? 2.919    75.669  79.898  1.00 142.75 ? 176  GLU B CB  1 
ATOM   15609 C  CG  . GLU C 1 176  ? 4.320    75.182  79.431  1.00 159.72 ? 176  GLU B CG  1 
ATOM   15610 C  CD  . GLU C 1 176  ? 4.668    73.728  79.856  1.00 173.39 ? 176  GLU B CD  1 
ATOM   15611 O  OE1 . GLU C 1 176  ? 4.554    73.390  81.060  1.00 174.58 ? 176  GLU B OE1 1 
ATOM   15612 O  OE2 . GLU C 1 176  ? 5.079    72.921  78.982  1.00 171.75 ? 176  GLU B OE2 1 
ATOM   15613 N  N   . ILE C 1 177  ? 4.447    78.360  80.505  1.00 157.90 ? 177  ILE B N   1 
ATOM   15614 C  CA  . ILE C 1 177  ? 4.878    79.754  80.318  1.00 163.22 ? 177  ILE B CA  1 
ATOM   15615 C  C   . ILE C 1 177  ? 4.865    80.179  78.856  1.00 164.00 ? 177  ILE B C   1 
ATOM   15616 O  O   . ILE C 1 177  ? 5.129    79.360  77.979  1.00 161.76 ? 177  ILE B O   1 
ATOM   15617 C  CB  . ILE C 1 177  ? 6.289    80.001  80.922  1.00 167.11 ? 177  ILE B CB  1 
ATOM   15618 C  CG1 . ILE C 1 177  ? 7.394    79.423  80.024  1.00 166.25 ? 177  ILE B CG1 1 
ATOM   15619 C  CG2 . ILE C 1 177  ? 6.371    79.402  82.312  1.00 169.13 ? 177  ILE B CG2 1 
ATOM   15620 C  CD1 . ILE C 1 177  ? 7.859    80.346  78.893  1.00 165.08 ? 177  ILE B CD1 1 
ATOM   15621 N  N   . ASP C 1 178  ? 4.572    81.456  78.600  1.00 168.89 ? 178  ASP B N   1 
ATOM   15622 C  CA  . ASP C 1 178  ? 4.430    81.952  77.224  1.00 170.45 ? 178  ASP B CA  1 
ATOM   15623 C  C   . ASP C 1 178  ? 5.625    82.745  76.716  1.00 175.94 ? 178  ASP B C   1 
ATOM   15624 O  O   . ASP C 1 178  ? 5.639    83.975  76.765  1.00 178.30 ? 178  ASP B O   1 
ATOM   15625 C  CB  . ASP C 1 178  ? 3.166    82.799  77.064  1.00 167.41 ? 178  ASP B CB  1 
ATOM   15626 C  CG  . ASP C 1 178  ? 2.707    82.889  75.624  1.00 161.22 ? 178  ASP B CG  1 
ATOM   15627 O  OD1 . ASP C 1 178  ? 1.566    83.355  75.401  1.00 158.54 ? 178  ASP B OD1 1 
ATOM   15628 O  OD2 . ASP C 1 178  ? 3.487    82.481  74.728  1.00 158.40 ? 178  ASP B OD2 1 
ATOM   15629 N  N   . HIS C 1 179  ? 6.606    82.032  76.186  1.00 177.22 ? 179  HIS B N   1 
ATOM   15630 C  CA  . HIS C 1 179  ? 7.829    82.663  75.729  1.00 181.06 ? 179  HIS B CA  1 
ATOM   15631 C  C   . HIS C 1 179  ? 7.626    83.415  74.419  1.00 176.16 ? 179  HIS B C   1 
ATOM   15632 O  O   . HIS C 1 179  ? 8.261    84.447  74.194  1.00 176.90 ? 179  HIS B O   1 
ATOM   15633 C  CB  . HIS C 1 179  ? 8.951    81.633  75.589  1.00 187.22 ? 179  HIS B CB  1 
ATOM   15634 C  CG  . HIS C 1 179  ? 10.312   82.179  75.891  1.00 196.17 ? 179  HIS B CG  1 
ATOM   15635 N  ND1 . HIS C 1 179  ? 11.011   81.840  77.028  1.00 201.40 ? 179  HIS B ND1 1 
ATOM   15636 C  CD2 . HIS C 1 179  ? 11.098   83.048  75.210  1.00 200.46 ? 179  HIS B CD2 1 
ATOM   15637 C  CE1 . HIS C 1 179  ? 12.173   82.471  77.032  1.00 205.42 ? 179  HIS B CE1 1 
ATOM   15638 N  NE2 . HIS C 1 179  ? 12.250   83.210  75.939  1.00 204.70 ? 179  HIS B NE2 1 
ATOM   15639 N  N   . ILE C 1 180  ? 6.744    82.918  73.555  1.00 172.04 ? 180  ILE B N   1 
ATOM   15640 C  CA  . ILE C 1 180  ? 6.547    83.599  72.270  1.00 168.72 ? 180  ILE B CA  1 
ATOM   15641 C  C   . ILE C 1 180  ? 5.093    83.774  71.786  1.00 161.07 ? 180  ILE B C   1 
ATOM   15642 O  O   . ILE C 1 180  ? 4.786    84.703  71.030  1.00 156.67 ? 180  ILE B O   1 
ATOM   15643 C  CB  . ILE C 1 180  ? 7.454    83.019  71.147  1.00 151.15 ? 180  ILE B CB  1 
ATOM   15644 C  CG1 . ILE C 1 180  ? 7.203    81.541  70.917  1.00 147.87 ? 180  ILE B CG1 1 
ATOM   15645 C  CG2 . ILE C 1 180  ? 8.915    83.175  71.506  1.00 154.23 ? 180  ILE B CG2 1 
ATOM   15646 C  CD1 . ILE C 1 180  ? 8.148    80.985  69.883  1.00 146.09 ? 180  ILE B CD1 1 
ATOM   15647 N  N   . GLY C 1 181  ? 4.203    82.904  72.241  1.00 158.20 ? 181  GLY B N   1 
ATOM   15648 C  CA  . GLY C 1 181  ? 2.809    83.006  71.866  1.00 153.23 ? 181  GLY B CA  1 
ATOM   15649 C  C   . GLY C 1 181  ? 2.343    81.636  71.451  1.00 148.66 ? 181  GLY B C   1 
ATOM   15650 O  O   . GLY C 1 181  ? 1.149    81.408  71.261  1.00 147.30 ? 181  GLY B O   1 
ATOM   15651 N  N   . ILE C 1 182  ? 3.311    80.733  71.299  1.00 145.94 ? 182  ILE B N   1 
ATOM   15652 C  CA  . ILE C 1 182  ? 3.057    79.336  70.959  1.00 141.93 ? 182  ILE B CA  1 
ATOM   15653 C  C   . ILE C 1 182  ? 3.298    78.435  72.165  1.00 143.08 ? 182  ILE B C   1 
ATOM   15654 O  O   . ILE C 1 182  ? 4.149    77.550  72.131  1.00 143.30 ? 182  ILE B O   1 
ATOM   15655 C  CB  . ILE C 1 182  ? 3.951    78.874  69.802  1.00 141.16 ? 182  ILE B CB  1 
ATOM   15656 C  CG1 . ILE C 1 182  ? 3.979    79.959  68.724  1.00 141.07 ? 182  ILE B CG1 1 
ATOM   15657 C  CG2 . ILE C 1 182  ? 3.461    77.533  69.260  1.00 138.12 ? 182  ILE B CG2 1 
ATOM   15658 C  CD1 . ILE C 1 182  ? 5.228    79.986  67.873  1.00 142.12 ? 182  ILE B CD1 1 
ATOM   15659 N  N   . ILE C 1 183  ? 2.562    78.686  73.237  1.00 141.18 ? 183  ILE B N   1 
ATOM   15660 C  CA  . ILE C 1 183  ? 2.587    77.839  74.414  1.00 140.29 ? 183  ILE B CA  1 
ATOM   15661 C  C   . ILE C 1 183  ? 2.562    76.361  74.057  1.00 138.49 ? 183  ILE B C   1 
ATOM   15662 O  O   . ILE C 1 183  ? 1.633    75.896  73.406  1.00 137.13 ? 183  ILE B O   1 
ATOM   15663 C  CB  . ILE C 1 183  ? 1.353    78.103  75.242  1.00 138.57 ? 183  ILE B CB  1 
ATOM   15664 C  CG1 . ILE C 1 183  ? 1.362    79.536  75.757  1.00 140.62 ? 183  ILE B CG1 1 
ATOM   15665 C  CG2 . ILE C 1 183  ? 1.286    77.146  76.384  1.00 140.65 ? 183  ILE B CG2 1 
ATOM   15666 C  CD1 . ILE C 1 183  ? 0.158    79.861  76.617  1.00 140.29 ? 183  ILE B CD1 1 
ATOM   15667 N  N   . SER C 1 184  ? 3.574    75.621  74.502  1.00 137.42 ? 184  SER B N   1 
ATOM   15668 C  CA  . SER C 1 184  ? 3.708    74.200  74.167  1.00 136.68 ? 184  SER B CA  1 
ATOM   15669 C  C   . SER C 1 184  ? 3.495    73.230  75.358  1.00 143.74 ? 184  SER B C   1 
ATOM   15670 O  O   . SER C 1 184  ? 4.398    72.993  76.176  1.00 146.89 ? 184  SER B O   1 
ATOM   15671 C  CB  . SER C 1 184  ? 5.073    73.965  73.514  1.00 135.53 ? 184  SER B CB  1 
ATOM   15672 O  OG  . SER C 1 184  ? 5.511    75.127  72.811  1.00 135.88 ? 184  SER B OG  1 
ATOM   15673 N  N   . PHE C 1 185  ? 2.297    72.655  75.426  1.00 142.70 ? 185  PHE B N   1 
ATOM   15674 C  CA  . PHE C 1 185  ? 1.902    71.784  76.529  1.00 141.36 ? 185  PHE B CA  1 
ATOM   15675 C  C   . PHE C 1 185  ? 2.350    70.349  76.353  1.00 139.72 ? 185  PHE B C   1 
ATOM   15676 O  O   . PHE C 1 185  ? 2.821    69.966  75.289  1.00 136.92 ? 185  PHE B O   1 
ATOM   15677 C  CB  . PHE C 1 185  ? 0.394    71.770  76.646  1.00 140.86 ? 185  PHE B CB  1 
ATOM   15678 C  CG  . PHE C 1 185  ? -0.187   73.049  77.105  1.00 141.81 ? 185  PHE B CG  1 
ATOM   15679 C  CD1 . PHE C 1 185  ? -0.390   73.281  78.445  1.00 143.13 ? 185  PHE B CD1 1 
ATOM   15680 C  CD2 . PHE C 1 185  ? -0.556   74.009  76.193  1.00 140.75 ? 185  PHE B CD2 1 
ATOM   15681 C  CE1 . PHE C 1 185  ? -0.947   74.450  78.871  1.00 145.12 ? 185  PHE B CE1 1 
ATOM   15682 C  CE2 . PHE C 1 185  ? -1.113   75.182  76.610  1.00 142.99 ? 185  PHE B CE2 1 
ATOM   15683 C  CZ  . PHE C 1 185  ? -1.309   75.408  77.956  1.00 145.16 ? 185  PHE B CZ  1 
ATOM   15684 N  N   . PRO C 1 186  ? 2.149    69.529  77.388  1.00 142.89 ? 186  PRO B N   1 
ATOM   15685 C  CA  . PRO C 1 186  ? 2.684    68.180  77.346  1.00 144.79 ? 186  PRO B CA  1 
ATOM   15686 C  C   . PRO C 1 186  ? 1.608    67.244  76.828  1.00 145.08 ? 186  PRO B C   1 
ATOM   15687 O  O   . PRO C 1 186  ? 0.443    67.405  77.208  1.00 145.16 ? 186  PRO B O   1 
ATOM   15688 C  CB  . PRO C 1 186  ? 2.948    67.885  78.822  1.00 148.43 ? 186  PRO B CB  1 
ATOM   15689 C  CG  . PRO C 1 186  ? 2.110    68.914  79.599  1.00 149.04 ? 186  PRO B CG  1 
ATOM   15690 C  CD  . PRO C 1 186  ? 1.335    69.713  78.593  1.00 145.11 ? 186  PRO B CD  1 
ATOM   15691 N  N   . ASP C 1 187  ? 2.009    66.283  75.990  1.00 143.44 ? 187  ASP B N   1 
ATOM   15692 C  CA  . ASP C 1 187  ? 1.104    65.289  75.400  1.00 141.58 ? 187  ASP B CA  1 
ATOM   15693 C  C   . ASP C 1 187  ? 0.206    64.632  76.466  1.00 138.65 ? 187  ASP B C   1 
ATOM   15694 O  O   . ASP C 1 187  ? 0.624    64.434  77.621  1.00 138.87 ? 187  ASP B O   1 
ATOM   15695 C  CB  . ASP C 1 187  ? 1.894    64.222  74.608  1.00 143.18 ? 187  ASP B CB  1 
ATOM   15696 C  CG  . ASP C 1 187  ? 2.582    64.788  73.360  1.00 145.45 ? 187  ASP B CG  1 
ATOM   15697 O  OD1 . ASP C 1 187  ? 2.817    66.016  73.294  1.00 147.18 ? 187  ASP B OD1 1 
ATOM   15698 O  OD2 . ASP C 1 187  ? 2.899    63.997  72.444  1.00 145.83 ? 187  ASP B OD2 1 
ATOM   15699 N  N   . PHE C 1 188  ? -1.028   64.320  76.063  1.00 134.85 ? 188  PHE B N   1 
ATOM   15700 C  CA  . PHE C 1 188  ? -2.047   63.761  76.940  1.00 132.08 ? 188  PHE B CA  1 
ATOM   15701 C  C   . PHE C 1 188  ? -2.398   62.369  76.460  1.00 131.23 ? 188  PHE B C   1 
ATOM   15702 O  O   . PHE C 1 188  ? -3.093   62.211  75.476  1.00 129.65 ? 188  PHE B O   1 
ATOM   15703 C  CB  . PHE C 1 188  ? -3.272   64.652  76.900  1.00 126.92 ? 188  PHE B CB  1 
ATOM   15704 C  CG  . PHE C 1 188  ? -4.471   64.103  77.616  1.00 125.80 ? 188  PHE B CG  1 
ATOM   15705 C  CD1 . PHE C 1 188  ? -5.462   63.437  76.929  1.00 123.18 ? 188  PHE B CD1 1 
ATOM   15706 C  CD2 . PHE C 1 188  ? -4.644   64.306  78.964  1.00 127.15 ? 188  PHE B CD2 1 
ATOM   15707 C  CE1 . PHE C 1 188  ? -6.600   62.959  77.572  1.00 123.02 ? 188  PHE B CE1 1 
ATOM   15708 C  CE2 . PHE C 1 188  ? -5.777   63.826  79.614  1.00 127.46 ? 188  PHE B CE2 1 
ATOM   15709 C  CZ  . PHE C 1 188  ? -6.757   63.152  78.904  1.00 124.74 ? 188  PHE B CZ  1 
ATOM   15710 N  N   . LYS C 1 189  ? -1.893   61.361  77.158  1.00 132.45 ? 189  LYS B N   1 
ATOM   15711 C  CA  . LYS C 1 189  ? -2.025   59.972  76.743  1.00 131.75 ? 189  LYS B CA  1 
ATOM   15712 C  C   . LYS C 1 189  ? -3.445   59.460  76.959  1.00 126.98 ? 189  LYS B C   1 
ATOM   15713 O  O   . LYS C 1 189  ? -3.939   59.412  78.083  1.00 129.62 ? 189  LYS B O   1 
ATOM   15714 C  CB  . LYS C 1 189  ? -1.012   59.121  77.519  1.00 133.90 ? 189  LYS B CB  1 
ATOM   15715 C  CG  . LYS C 1 189  ? -1.417   57.689  77.793  1.00 136.97 ? 189  LYS B CG  1 
ATOM   15716 C  CD  . LYS C 1 189  ? -0.991   56.770  76.671  1.00 138.54 ? 189  LYS B CD  1 
ATOM   15717 C  CE  . LYS C 1 189  ? -0.928   55.341  77.166  1.00 140.56 ? 189  LYS B CE  1 
ATOM   15718 N  NZ  . LYS C 1 189  ? -1.985   55.089  78.194  1.00 141.07 ? 189  LYS B NZ  1 
ATOM   15719 N  N   . ILE C 1 190  ? -4.100   59.080  75.874  1.00 124.75 ? 190  ILE B N   1 
ATOM   15720 C  CA  . ILE C 1 190  ? -5.413   58.481  75.961  1.00 122.68 ? 190  ILE B CA  1 
ATOM   15721 C  C   . ILE C 1 190  ? -5.318   57.155  76.736  1.00 129.28 ? 190  ILE B C   1 
ATOM   15722 O  O   . ILE C 1 190  ? -4.473   56.313  76.423  1.00 133.86 ? 190  ILE B O   1 
ATOM   15723 C  CB  . ILE C 1 190  ? -5.934   58.243  74.543  1.00 121.74 ? 190  ILE B CB  1 
ATOM   15724 C  CG1 . ILE C 1 190  ? -5.559   59.440  73.655  1.00 112.28 ? 190  ILE B CG1 1 
ATOM   15725 C  CG2 . ILE C 1 190  ? -7.434   57.973  74.547  1.00 111.20 ? 190  ILE B CG2 1 
ATOM   15726 C  CD1 . ILE C 1 190  ? -6.621   60.539  73.545  1.00 111.27 ? 190  ILE B CD1 1 
ATOM   15727 N  N   . PRO C 1 191  ? -6.173   56.972  77.762  1.00 127.72 ? 191  PRO B N   1 
ATOM   15728 C  CA  . PRO C 1 191  ? -6.252   55.770  78.608  1.00 131.14 ? 191  PRO B CA  1 
ATOM   15729 C  C   . PRO C 1 191  ? -6.224   54.440  77.844  1.00 131.20 ? 191  PRO B C   1 
ATOM   15730 O  O   . PRO C 1 191  ? -6.657   54.360  76.690  1.00 130.31 ? 191  PRO B O   1 
ATOM   15731 C  CB  . PRO C 1 191  ? -7.611   55.928  79.291  1.00 126.82 ? 191  PRO B CB  1 
ATOM   15732 C  CG  . PRO C 1 191  ? -7.748   57.380  79.458  1.00 127.08 ? 191  PRO B CG  1 
ATOM   15733 C  CD  . PRO C 1 191  ? -7.098   58.014  78.234  1.00 126.92 ? 191  PRO B CD  1 
ATOM   15734 N  N   . SER C 1 192  ? -5.724   53.399  78.511  1.00 136.01 ? 192  SER B N   1 
ATOM   15735 C  CA  . SER C 1 192  ? -5.659   52.053  77.938  1.00 133.27 ? 192  SER B CA  1 
ATOM   15736 C  C   . SER C 1 192  ? -7.030   51.645  77.425  1.00 127.28 ? 192  SER B C   1 
ATOM   15737 O  O   . SER C 1 192  ? -7.163   51.036  76.373  1.00 122.37 ? 192  SER B O   1 
ATOM   15738 C  CB  . SER C 1 192  ? -5.188   51.053  79.000  1.00 138.10 ? 192  SER B CB  1 
ATOM   15739 O  OG  . SER C 1 192  ? -4.172   51.600  79.824  1.00 141.08 ? 192  SER B OG  1 
ATOM   15740 N  N   . ASN C 1 193  ? -8.040   52.005  78.206  1.00 127.67 ? 193  ASN B N   1 
ATOM   15741 C  CA  . ASN C 1 193  ? -9.432   51.753  77.893  1.00 126.87 ? 193  ASN B CA  1 
ATOM   15742 C  C   . ASN C 1 193  ? -10.260  52.957  78.356  1.00 129.16 ? 193  ASN B C   1 
ATOM   15743 O  O   . ASN C 1 193  ? -10.831  52.945  79.454  1.00 129.73 ? 193  ASN B O   1 
ATOM   15744 C  CB  . ASN C 1 193  ? -9.882   50.489  78.613  1.00 129.58 ? 193  ASN B CB  1 
ATOM   15745 C  CG  . ASN C 1 193  ? -11.364  50.456  78.843  1.00 129.87 ? 193  ASN B CG  1 
ATOM   15746 O  OD1 . ASN C 1 193  ? -12.113  51.186  78.193  1.00 128.12 ? 193  ASN B OD1 1 
ATOM   15747 N  ND2 . ASN C 1 193  ? -11.804  49.611  79.775  1.00 131.76 ? 193  ASN B ND2 1 
ATOM   15748 N  N   . PRO C 1 194  ? -10.311  54.007  77.519  1.00 127.25 ? 194  PRO B N   1 
ATOM   15749 C  CA  . PRO C 1 194  ? -10.837  55.320  77.884  1.00 126.07 ? 194  PRO B CA  1 
ATOM   15750 C  C   . PRO C 1 194  ? -12.341  55.372  77.928  1.00 123.65 ? 194  PRO B C   1 
ATOM   15751 O  O   . PRO C 1 194  ? -13.024  54.388  77.643  1.00 119.79 ? 194  PRO B O   1 
ATOM   15752 C  CB  . PRO C 1 194  ? -10.350  56.224  76.749  1.00 127.24 ? 194  PRO B CB  1 
ATOM   15753 C  CG  . PRO C 1 194  ? -9.358   55.424  75.992  1.00 128.66 ? 194  PRO B CG  1 
ATOM   15754 C  CD  . PRO C 1 194  ? -9.769   54.012  76.156  1.00 128.87 ? 194  PRO B CD  1 
ATOM   15755 N  N   . ARG C 1 195  ? -12.821  56.551  78.313  1.00 125.77 ? 195  ARG B N   1 
ATOM   15756 C  CA  . ARG C 1 195  ? -14.227  56.921  78.320  1.00 128.23 ? 195  ARG B CA  1 
ATOM   15757 C  C   . ARG C 1 195  ? -14.507  57.448  76.915  1.00 126.65 ? 195  ARG B C   1 
ATOM   15758 O  O   . ARG C 1 195  ? -14.117  58.569  76.585  1.00 126.92 ? 195  ARG B O   1 
ATOM   15759 C  CB  . ARG C 1 195  ? -14.436  58.044  79.343  1.00 131.46 ? 195  ARG B CB  1 
ATOM   15760 C  CG  . ARG C 1 195  ? -15.646  57.901  80.258  1.00 135.20 ? 195  ARG B CG  1 
ATOM   15761 C  CD  . ARG C 1 195  ? -15.239  57.358  81.612  1.00 141.31 ? 195  ARG B CD  1 
ATOM   15762 N  NE  . ARG C 1 195  ? -15.920  58.051  82.698  1.00 145.65 ? 195  ARG B NE  1 
ATOM   15763 C  CZ  . ARG C 1 195  ? -16.871  57.517  83.454  1.00 148.03 ? 195  ARG B CZ  1 
ATOM   15764 N  NH1 . ARG C 1 195  ? -17.270  56.264  83.260  1.00 146.85 ? 195  ARG B NH1 1 
ATOM   15765 N  NH2 . ARG C 1 195  ? -17.423  58.248  84.412  1.00 150.46 ? 195  ARG B NH2 1 
ATOM   15766 N  N   . TYR C 1 196  ? -15.169  56.649  76.085  1.00 123.72 ? 196  TYR B N   1 
ATOM   15767 C  CA  . TYR C 1 196  ? -15.158  56.896  74.657  1.00 120.59 ? 196  TYR B CA  1 
ATOM   15768 C  C   . TYR C 1 196  ? -16.142  57.963  74.292  1.00 114.76 ? 196  TYR B C   1 
ATOM   15769 O  O   . TYR C 1 196  ? -17.303  57.879  74.678  1.00 115.32 ? 196  TYR B O   1 
ATOM   15770 C  CB  . TYR C 1 196  ? -15.521  55.620  73.920  1.00 121.40 ? 196  TYR B CB  1 
ATOM   15771 C  CG  . TYR C 1 196  ? -14.419  54.578  73.877  1.00 122.83 ? 196  TYR B CG  1 
ATOM   15772 C  CD1 . TYR C 1 196  ? -13.219  54.840  73.231  1.00 122.88 ? 196  TYR B CD1 1 
ATOM   15773 C  CD2 . TYR C 1 196  ? -14.590  53.327  74.464  1.00 123.37 ? 196  TYR B CD2 1 
ATOM   15774 C  CE1 . TYR C 1 196  ? -12.220  53.897  73.183  1.00 122.83 ? 196  TYR B CE1 1 
ATOM   15775 C  CE2 . TYR C 1 196  ? -13.596  52.379  74.420  1.00 122.92 ? 196  TYR B CE2 1 
ATOM   15776 C  CZ  . TYR C 1 196  ? -12.415  52.671  73.775  1.00 122.92 ? 196  TYR B CZ  1 
ATOM   15777 O  OH  . TYR C 1 196  ? -11.417  51.738  73.714  1.00 122.70 ? 196  TYR B OH  1 
ATOM   15778 N  N   . GLY C 1 197  ? -15.688  58.962  73.543  1.00 114.31 ? 197  GLY B N   1 
ATOM   15779 C  CA  . GLY C 1 197  ? -16.590  60.006  73.078  1.00 112.82 ? 197  GLY B CA  1 
ATOM   15780 C  C   . GLY C 1 197  ? -16.039  61.423  72.950  1.00 114.53 ? 197  GLY B C   1 
ATOM   15781 O  O   . GLY C 1 197  ? -14.859  61.645  72.695  1.00 114.91 ? 197  GLY B O   1 
ATOM   15782 N  N   . MET C 1 198  ? -16.910  62.401  73.130  1.00 111.78 ? 198  MET B N   1 
ATOM   15783 C  CA  . MET C 1 198  ? -16.544  63.778  72.861  1.00 112.69 ? 198  MET B CA  1 
ATOM   15784 C  C   . MET C 1 198  ? -15.705  64.436  73.967  1.00 110.67 ? 198  MET B C   1 
ATOM   15785 O  O   . MET C 1 198  ? -16.235  64.871  74.992  1.00 105.09 ? 198  MET B O   1 
ATOM   15786 C  CB  . MET C 1 198  ? -17.830  64.572  72.567  1.00 116.40 ? 198  MET B CB  1 
ATOM   15787 C  CG  . MET C 1 198  ? -17.679  65.995  71.942  1.00 141.25 ? 198  MET B CG  1 
ATOM   15788 S  SD  . MET C 1 198  ? -16.349  66.231  70.742  1.00 154.49 ? 198  MET B SD  1 
ATOM   15789 C  CE  . MET C 1 198  ? -16.337  64.651  69.886  1.00 100.78 ? 198  MET B CE  1 
ATOM   15790 N  N   . TRP C 1 199  ? -14.397  64.525  73.757  1.00 108.82 ? 199  TRP B N   1 
ATOM   15791 C  CA  . TRP C 1 199  ? -13.546  65.231  74.717  1.00 112.00 ? 199  TRP B CA  1 
ATOM   15792 C  C   . TRP C 1 199  ? -13.645  66.747  74.561  1.00 111.66 ? 199  TRP B C   1 
ATOM   15793 O  O   . TRP C 1 199  ? -14.119  67.227  73.546  1.00 114.25 ? 199  TRP B O   1 
ATOM   15794 C  CB  . TRP C 1 199  ? -12.102  64.727  74.618  1.00 114.39 ? 199  TRP B CB  1 
ATOM   15795 C  CG  . TRP C 1 199  ? -12.008  63.377  75.213  1.00 117.93 ? 199  TRP B CG  1 
ATOM   15796 C  CD1 . TRP C 1 199  ? -12.651  62.266  74.775  1.00 119.10 ? 199  TRP B CD1 1 
ATOM   15797 C  CD2 . TRP C 1 199  ? -11.289  62.986  76.405  1.00 121.33 ? 199  TRP B CD2 1 
ATOM   15798 N  NE1 . TRP C 1 199  ? -12.372  61.199  75.602  1.00 121.83 ? 199  TRP B NE1 1 
ATOM   15799 C  CE2 . TRP C 1 199  ? -11.539  61.616  76.608  1.00 122.19 ? 199  TRP B CE2 1 
ATOM   15800 C  CE3 . TRP C 1 199  ? -10.450  63.654  77.303  1.00 121.87 ? 199  TRP B CE3 1 
ATOM   15801 C  CZ2 . TRP C 1 199  ? -10.980  60.907  77.664  1.00 122.42 ? 199  TRP B CZ2 1 
ATOM   15802 C  CZ3 . TRP C 1 199  ? -9.901   62.949  78.349  1.00 122.74 ? 199  TRP B CZ3 1 
ATOM   15803 C  CH2 . TRP C 1 199  ? -10.168  61.595  78.521  1.00 123.46 ? 199  TRP B CH2 1 
ATOM   15804 N  N   . THR C 1 200  ? -13.218  67.508  75.556  1.00 110.56 ? 200  THR B N   1 
ATOM   15805 C  CA  . THR C 1 200  ? -13.264  68.954  75.447  1.00 109.53 ? 200  THR B CA  1 
ATOM   15806 C  C   . THR C 1 200  ? -12.015  69.457  76.107  1.00 111.56 ? 200  THR B C   1 
ATOM   15807 O  O   . THR C 1 200  ? -11.723  69.065  77.223  1.00 114.18 ? 200  THR B O   1 
ATOM   15808 C  CB  . THR C 1 200  ? -14.444  69.545  76.246  1.00 109.62 ? 200  THR B CB  1 
ATOM   15809 O  OG1 . THR C 1 200  ? -15.637  68.799  76.005  1.00 108.02 ? 200  THR B OG1 1 
ATOM   15810 C  CG2 . THR C 1 200  ? -14.665  70.977  75.878  1.00 109.76 ? 200  THR B CG2 1 
ATOM   15811 N  N   . ILE C 1 201  ? -11.246  70.302  75.447  1.00 111.97 ? 201  ILE B N   1 
ATOM   15812 C  CA  . ILE C 1 201  ? -10.153  70.952  76.154  1.00 114.10 ? 201  ILE B CA  1 
ATOM   15813 C  C   . ILE C 1 201  ? -10.460  72.443  76.323  1.00 117.61 ? 201  ILE B C   1 
ATOM   15814 O  O   . ILE C 1 201  ? -10.489  73.170  75.332  1.00 120.62 ? 201  ILE B O   1 
ATOM   15815 C  CB  . ILE C 1 201  ? -8.806   70.842  75.409  1.00 114.52 ? 201  ILE B CB  1 
ATOM   15816 C  CG1 . ILE C 1 201  ? -8.300   69.414  75.300  1.00 114.17 ? 201  ILE B CG1 1 
ATOM   15817 C  CG2 . ILE C 1 201  ? -7.749   71.583  76.160  1.00 118.43 ? 201  ILE B CG2 1 
ATOM   15818 C  CD1 . ILE C 1 201  ? -6.792   69.376  75.077  1.00 115.41 ? 201  ILE B CD1 1 
ATOM   15819 N  N   . LYS C 1 202  ? -10.682  72.915  77.550  1.00 120.46 ? 202  LYS B N   1 
ATOM   15820 C  CA  . LYS C 1 202  ? -10.839  74.359  77.771  1.00 124.50 ? 202  LYS B CA  1 
ATOM   15821 C  C   . LYS C 1 202  ? -9.509   75.004  78.169  1.00 122.15 ? 202  LYS B C   1 
ATOM   15822 O  O   . LYS C 1 202  ? -8.597   74.316  78.617  1.00 123.29 ? 202  LYS B O   1 
ATOM   15823 C  CB  . LYS C 1 202  ? -11.899  74.645  78.836  1.00 128.03 ? 202  LYS B CB  1 
ATOM   15824 C  CG  . LYS C 1 202  ? -13.337  74.279  78.467  1.00 131.48 ? 202  LYS B CG  1 
ATOM   15825 C  CD  . LYS C 1 202  ? -14.286  74.598  79.623  1.00 137.15 ? 202  LYS B CD  1 
ATOM   15826 C  CE  . LYS C 1 202  ? -15.551  73.752  79.579  1.00 138.55 ? 202  LYS B CE  1 
ATOM   15827 N  NZ  . LYS C 1 202  ? -15.949  73.292  80.944  1.00 141.39 ? 202  LYS B NZ  1 
ATOM   15828 N  N   . ALA C 1 203  ? -9.393   76.320  78.016  1.00 122.54 ? 203  ALA B N   1 
ATOM   15829 C  CA  . ALA C 1 203  ? -8.174   77.013  78.437  1.00 125.82 ? 203  ALA B CA  1 
ATOM   15830 C  C   . ALA C 1 203  ? -8.443   78.441  78.915  1.00 128.74 ? 203  ALA B C   1 
ATOM   15831 O  O   . ALA C 1 203  ? -9.154   79.196  78.248  1.00 126.35 ? 203  ALA B O   1 
ATOM   15832 C  CB  . ALA C 1 203  ? -7.139   77.001  77.324  1.00 122.44 ? 203  ALA B CB  1 
ATOM   15833 N  N   . LYS C 1 204  ? -7.863   78.800  80.066  1.00 134.25 ? 204  LYS B N   1 
ATOM   15834 C  CA  . LYS C 1 204  ? -8.060   80.121  80.692  1.00 139.06 ? 204  LYS B CA  1 
ATOM   15835 C  C   . LYS C 1 204  ? -6.746   80.750  81.104  1.00 140.45 ? 204  LYS B C   1 
ATOM   15836 O  O   . LYS C 1 204  ? -5.747   80.056  81.297  1.00 138.51 ? 204  LYS B O   1 
ATOM   15837 C  CB  . LYS C 1 204  ? -8.959   80.024  81.918  1.00 144.70 ? 204  LYS B CB  1 
ATOM   15838 C  CG  . LYS C 1 204  ? -8.567   78.882  82.817  1.00 151.33 ? 204  LYS B CG  1 
ATOM   15839 C  CD  . LYS C 1 204  ? -9.646   78.590  83.825  1.00 156.30 ? 204  LYS B CD  1 
ATOM   15840 C  CE  . LYS C 1 204  ? -9.587   77.149  84.293  1.00 159.14 ? 204  LYS B CE  1 
ATOM   15841 N  NZ  . LYS C 1 204  ? -10.366  77.016  85.556  1.00 162.27 ? 204  LYS B NZ  1 
ATOM   15842 N  N   . TYR C 1 205  ? -6.735   82.069  81.219  1.00 143.84 ? 205  TYR B N   1 
ATOM   15843 C  CA  . TYR C 1 205  ? -5.489   82.728  81.531  1.00 151.70 ? 205  TYR B CA  1 
ATOM   15844 C  C   . TYR C 1 205  ? -5.238   82.538  83.017  1.00 161.99 ? 205  TYR B C   1 
ATOM   15845 O  O   . TYR C 1 205  ? -6.137   82.795  83.814  1.00 165.22 ? 205  TYR B O   1 
ATOM   15846 C  CB  . TYR C 1 205  ? -5.536   84.199  81.110  1.00 152.00 ? 205  TYR B CB  1 
ATOM   15847 C  CG  . TYR C 1 205  ? -5.022   84.397  79.700  1.00 151.32 ? 205  TYR B CG  1 
ATOM   15848 C  CD1 . TYR C 1 205  ? -5.855   84.844  78.676  1.00 148.90 ? 205  TYR B CD1 1 
ATOM   15849 C  CD2 . TYR C 1 205  ? -3.700   84.095  79.380  1.00 152.37 ? 205  TYR B CD2 1 
ATOM   15850 C  CE1 . TYR C 1 205  ? -5.375   85.003  77.373  1.00 147.76 ? 205  TYR B CE1 1 
ATOM   15851 C  CE2 . TYR C 1 205  ? -3.215   84.249  78.082  1.00 151.13 ? 205  TYR B CE2 1 
ATOM   15852 C  CZ  . TYR C 1 205  ? -4.056   84.704  77.089  1.00 148.19 ? 205  TYR B CZ  1 
ATOM   15853 O  OH  . TYR C 1 205  ? -3.558   84.855  75.821  1.00 145.83 ? 205  TYR B OH  1 
ATOM   15854 N  N   . LYS C 1 206  ? -4.053   82.053  83.405  1.00 165.65 ? 206  LYS B N   1 
ATOM   15855 C  CA  . LYS C 1 206  ? -3.822   81.759  84.821  1.00 170.33 ? 206  LYS B CA  1 
ATOM   15856 C  C   . LYS C 1 206  ? -4.203   82.983  85.623  1.00 172.69 ? 206  LYS B C   1 
ATOM   15857 O  O   . LYS C 1 206  ? -5.165   82.975  86.392  1.00 173.08 ? 206  LYS B O   1 
ATOM   15858 C  CB  . LYS C 1 206  ? -2.366   81.378  85.120  1.00 172.62 ? 206  LYS B CB  1 
ATOM   15859 C  CG  . LYS C 1 206  ? -2.144   80.968  86.590  1.00 176.24 ? 206  LYS B CG  1 
ATOM   15860 C  CD  . LYS C 1 206  ? -0.764   80.374  86.855  1.00 178.80 ? 206  LYS B CD  1 
ATOM   15861 C  CE  . LYS C 1 206  ? 0.335    81.422  86.756  1.00 182.56 ? 206  LYS B CE  1 
ATOM   15862 N  NZ  . LYS C 1 206  ? 1.605    81.007  87.427  1.00 185.68 ? 206  LYS B NZ  1 
ATOM   15863 N  N   . GLU C 1 207  ? -3.453   84.049  85.397  1.00 175.21 ? 207  GLU B N   1 
ATOM   15864 C  CA  . GLU C 1 207  ? -3.709   85.323  86.039  1.00 178.61 ? 207  GLU B CA  1 
ATOM   15865 C  C   . GLU C 1 207  ? -5.080   85.908  85.683  1.00 173.54 ? 207  GLU B C   1 
ATOM   15866 O  O   . GLU C 1 207  ? -5.972   85.185  85.265  1.00 171.45 ? 207  GLU B O   1 
ATOM   15867 C  CB  . GLU C 1 207  ? -2.576   86.282  85.701  1.00 183.24 ? 207  GLU B CB  1 
ATOM   15868 C  CG  . GLU C 1 207  ? -1.304   85.974  86.484  1.00 188.04 ? 207  GLU B CG  1 
ATOM   15869 C  CD  . GLU C 1 207  ? -1.345   86.542  87.892  1.00 192.24 ? 207  GLU B CD  1 
ATOM   15870 O  OE1 . GLU C 1 207  ? -2.449   86.621  88.471  1.00 192.19 ? 207  GLU B OE1 1 
ATOM   15871 O  OE2 . GLU C 1 207  ? -0.277   86.920  88.414  1.00 195.36 ? 207  GLU B OE2 1 
ATOM   15872 N  N   . ASP C 1 208  ? -5.260   87.208  85.886  1.00 172.46 ? 208  ASP B N   1 
ATOM   15873 C  CA  . ASP C 1 208  ? -6.539   87.854  85.612  1.00 166.10 ? 208  ASP B CA  1 
ATOM   15874 C  C   . ASP C 1 208  ? -6.750   87.866  84.129  1.00 161.37 ? 208  ASP B C   1 
ATOM   15875 O  O   . ASP C 1 208  ? -5.785   87.707  83.378  1.00 161.59 ? 208  ASP B O   1 
ATOM   15876 C  CB  . ASP C 1 208  ? -6.467   89.275  86.085  1.00 165.61 ? 208  ASP B CB  1 
ATOM   15877 C  CG  . ASP C 1 208  ? -5.070   89.770  86.088  1.00 164.33 ? 208  ASP B CG  1 
ATOM   15878 O  OD1 . ASP C 1 208  ? -4.526   90.001  84.984  1.00 160.08 ? 208  ASP B OD1 1 
ATOM   15879 O  OD2 . ASP C 1 208  ? -4.514   89.886  87.203  1.00 167.33 ? 208  ASP B OD2 1 
ATOM   15880 N  N   . PHE C 1 209  ? -7.999   88.121  83.731  1.00 156.28 ? 209  PHE B N   1 
ATOM   15881 C  CA  . PHE C 1 209  ? -8.468   87.974  82.354  1.00 149.98 ? 209  PHE B CA  1 
ATOM   15882 C  C   . PHE C 1 209  ? -9.432   86.778  82.239  1.00 148.42 ? 209  PHE B C   1 
ATOM   15883 O  O   . PHE C 1 209  ? -9.065   85.648  82.575  1.00 148.45 ? 209  PHE B O   1 
ATOM   15884 C  CB  . PHE C 1 209  ? -7.298   87.781  81.388  1.00 146.32 ? 209  PHE B CB  1 
ATOM   15885 C  CG  . PHE C 1 209  ? -6.512   89.029  81.112  1.00 145.40 ? 209  PHE B CG  1 
ATOM   15886 C  CD1 . PHE C 1 209  ? -5.180   88.945  80.724  1.00 145.16 ? 209  PHE B CD1 1 
ATOM   15887 C  CD2 . PHE C 1 209  ? -7.099   90.279  81.226  1.00 141.54 ? 209  PHE B CD2 1 
ATOM   15888 C  CE1 . PHE C 1 209  ? -4.444   90.089  80.445  1.00 143.15 ? 209  PHE B CE1 1 
ATOM   15889 C  CE2 . PHE C 1 209  ? -6.368   91.431  80.948  1.00 143.48 ? 209  PHE B CE2 1 
ATOM   15890 C  CZ  . PHE C 1 209  ? -5.038   91.333  80.555  1.00 144.25 ? 209  PHE B CZ  1 
ATOM   15891 N  N   . SER C 1 210  ? -10.653  87.026  81.758  1.00 145.76 ? 210  SER B N   1 
ATOM   15892 C  CA  . SER C 1 210  ? -11.681  85.983  81.670  1.00 143.64 ? 210  SER B CA  1 
ATOM   15893 C  C   . SER C 1 210  ? -11.613  85.149  80.382  1.00 140.14 ? 210  SER B C   1 
ATOM   15894 O  O   . SER C 1 210  ? -12.355  84.163  80.199  1.00 136.83 ? 210  SER B O   1 
ATOM   15895 C  CB  . SER C 1 210  ? -13.072  86.592  81.802  1.00 143.33 ? 210  SER B CB  1 
ATOM   15896 O  OG  . SER C 1 210  ? -14.045  85.564  81.772  1.00 142.40 ? 210  SER B OG  1 
ATOM   15897 N  N   . THR C 1 211  ? -10.710  85.552  79.497  1.00 140.59 ? 211  THR B N   1 
ATOM   15898 C  CA  . THR C 1 211  ? -10.642  85.008  78.152  1.00 138.52 ? 211  THR B CA  1 
ATOM   15899 C  C   . THR C 1 211  ? -10.562  83.482  78.131  1.00 135.85 ? 211  THR B C   1 
ATOM   15900 O  O   . THR C 1 211  ? -9.814   82.887  78.887  1.00 135.69 ? 211  THR B O   1 
ATOM   15901 C  CB  . THR C 1 211  ? -9.493   85.672  77.358  1.00 139.20 ? 211  THR B CB  1 
ATOM   15902 O  OG1 . THR C 1 211  ? -8.359   85.869  78.213  1.00 141.96 ? 211  THR B OG1 1 
ATOM   15903 C  CG2 . THR C 1 211  ? -9.941   87.017  76.854  1.00 138.42 ? 211  THR B CG2 1 
ATOM   15904 N  N   . THR C 1 212  ? -11.335  82.877  77.232  1.00 135.20 ? 212  THR B N   1 
ATOM   15905 C  CA  . THR C 1 212  ? -11.559  81.436  77.190  1.00 133.89 ? 212  THR B CA  1 
ATOM   15906 C  C   . THR C 1 212  ? -11.198  80.808  75.863  1.00 133.18 ? 212  THR B C   1 
ATOM   15907 O  O   . THR C 1 212  ? -11.621  81.261  74.802  1.00 134.95 ? 212  THR B O   1 
ATOM   15908 C  CB  . THR C 1 212  ? -13.045  81.147  77.317  1.00 132.67 ? 212  THR B CB  1 
ATOM   15909 O  OG1 . THR C 1 212  ? -13.613  82.009  78.316  1.00 134.57 ? 212  THR B OG1 1 
ATOM   15910 C  CG2 . THR C 1 212  ? -13.289  79.661  77.622  1.00 131.15 ? 212  THR B CG2 1 
ATOM   15911 N  N   . GLY C 1 213  ? -10.426  79.741  75.921  1.00 132.49 ? 213  GLY B N   1 
ATOM   15912 C  CA  . GLY C 1 213  ? -10.262  78.910  74.750  1.00 130.01 ? 213  GLY B CA  1 
ATOM   15913 C  C   . GLY C 1 213  ? -11.051  77.628  74.919  1.00 129.55 ? 213  GLY B C   1 
ATOM   15914 O  O   . GLY C 1 213  ? -11.233  77.129  76.026  1.00 130.42 ? 213  GLY B O   1 
ATOM   15915 N  N   . THR C 1 214  ? -11.528  77.081  73.818  1.00 125.27 ? 214  THR B N   1 
ATOM   15916 C  CA  . THR C 1 214  ? -12.121  75.766  73.872  1.00 122.82 ? 214  THR B CA  1 
ATOM   15917 C  C   . THR C 1 214  ? -11.791  75.063  72.585  1.00 116.86 ? 214  THR B C   1 
ATOM   15918 O  O   . THR C 1 214  ? -11.593  75.692  71.552  1.00 116.03 ? 214  THR B O   1 
ATOM   15919 C  CB  . THR C 1 214  ? -13.639  75.813  74.099  1.00 123.77 ? 214  THR B CB  1 
ATOM   15920 O  OG1 . THR C 1 214  ? -13.914  76.005  75.498  1.00 126.05 ? 214  THR B OG1 1 
ATOM   15921 C  CG2 . THR C 1 214  ? -14.299  74.512  73.625  1.00 121.09 ? 214  THR B CG2 1 
ATOM   15922 N  N   . ALA C 1 215  ? -11.705  73.750  72.664  1.00 114.28 ? 215  ALA B N   1 
ATOM   15923 C  CA  . ALA C 1 215  ? -11.356  72.945  71.522  1.00 109.50 ? 215  ALA B CA  1 
ATOM   15924 C  C   . ALA C 1 215  ? -12.058  71.619  71.725  1.00 109.31 ? 215  ALA B C   1 
ATOM   15925 O  O   . ALA C 1 215  ? -12.686  71.422  72.764  1.00 108.63 ? 215  ALA B O   1 
ATOM   15926 C  CB  . ALA C 1 215  ? -9.860   72.766  71.479  1.00 110.69 ? 215  ALA B CB  1 
ATOM   15927 N  N   . TYR C 1 216  ? -11.998  70.717  70.752  1.00 107.10 ? 216  TYR B N   1 
ATOM   15928 C  CA  . TYR C 1 216  ? -12.457  69.371  71.043  1.00 112.95 ? 216  TYR B CA  1 
ATOM   15929 C  C   . TYR C 1 216  ? -11.619  68.349  70.337  1.00 106.04 ? 216  TYR B C   1 
ATOM   15930 O  O   . TYR C 1 216  ? -10.819  68.705  69.462  1.00 106.18 ? 216  TYR B O   1 
ATOM   15931 C  CB  . TYR C 1 216  ? -13.916  69.162  70.668  1.00 115.02 ? 216  TYR B CB  1 
ATOM   15932 C  CG  . TYR C 1 216  ? -14.849  70.212  71.195  1.00 122.41 ? 216  TYR B CG  1 
ATOM   15933 C  CD1 . TYR C 1 216  ? -15.921  69.879  72.017  1.00 124.63 ? 216  TYR B CD1 1 
ATOM   15934 C  CD2 . TYR C 1 216  ? -14.676  71.540  70.854  1.00 126.34 ? 216  TYR B CD2 1 
ATOM   15935 C  CE1 . TYR C 1 216  ? -16.788  70.858  72.495  1.00 127.88 ? 216  TYR B CE1 1 
ATOM   15936 C  CE2 . TYR C 1 216  ? -15.517  72.512  71.329  1.00 130.08 ? 216  TYR B CE2 1 
ATOM   15937 C  CZ  . TYR C 1 216  ? -16.572  72.172  72.147  1.00 131.01 ? 216  TYR B CZ  1 
ATOM   15938 O  OH  . TYR C 1 216  ? -17.405  73.165  72.605  1.00 133.49 ? 216  TYR B OH  1 
ATOM   15939 N  N   . PHE C 1 217  ? -11.790  67.098  70.776  1.00 105.77 ? 217  PHE B N   1 
ATOM   15940 C  CA  . PHE C 1 217  ? -11.350  65.904  70.067  1.00 105.18 ? 217  PHE B CA  1 
ATOM   15941 C  C   . PHE C 1 217  ? -12.241  64.733  70.447  1.00 108.36 ? 217  PHE B C   1 
ATOM   15942 O  O   . PHE C 1 217  ? -12.897  64.750  71.486  1.00 108.47 ? 217  PHE B O   1 
ATOM   15943 C  CB  . PHE C 1 217  ? -9.853   65.604  70.244  1.00 106.52 ? 217  PHE B CB  1 
ATOM   15944 C  CG  . PHE C 1 217  ? -9.441   65.242  71.631  1.00 107.92 ? 217  PHE B CG  1 
ATOM   15945 C  CD1 . PHE C 1 217  ? -8.984   63.960  71.917  1.00 109.55 ? 217  PHE B CD1 1 
ATOM   15946 C  CD2 . PHE C 1 217  ? -9.455   66.172  72.646  1.00 109.11 ? 217  PHE B CD2 1 
ATOM   15947 C  CE1 . PHE C 1 217  ? -8.565   63.594  73.211  1.00 110.88 ? 217  PHE B CE1 1 
ATOM   15948 C  CE2 . PHE C 1 217  ? -9.043   65.815  73.934  1.00 112.13 ? 217  PHE B CE2 1 
ATOM   15949 C  CZ  . PHE C 1 217  ? -8.593   64.520  74.209  1.00 112.33 ? 217  PHE B CZ  1 
ATOM   15950 N  N   . GLU C 1 218  ? -12.333  63.747  69.567  1.00 109.99 ? 218  GLU B N   1 
ATOM   15951 C  CA  . GLU C 1 218  ? -13.185  62.603  69.836  1.00 114.09 ? 218  GLU B CA  1 
ATOM   15952 C  C   . GLU C 1 218  ? -12.336  61.356  70.020  1.00 113.97 ? 218  GLU B C   1 
ATOM   15953 O  O   . GLU C 1 218  ? -11.465  61.050  69.215  1.00 111.71 ? 218  GLU B O   1 
ATOM   15954 C  CB  . GLU C 1 218  ? -14.231  62.411  68.736  1.00 119.96 ? 218  GLU B CB  1 
ATOM   15955 C  CG  . GLU C 1 218  ? -15.407  61.534  69.158  1.00 126.84 ? 218  GLU B CG  1 
ATOM   15956 C  CD  . GLU C 1 218  ? -16.525  61.469  68.117  1.00 132.99 ? 218  GLU B CD  1 
ATOM   15957 O  OE1 . GLU C 1 218  ? -17.273  60.455  68.123  1.00 135.49 ? 218  GLU B OE1 1 
ATOM   15958 O  OE2 . GLU C 1 218  ? -16.655  62.420  67.300  1.00 134.58 ? 218  GLU B OE2 1 
ATOM   15959 N  N   . VAL C 1 219  ? -12.570  60.665  71.124  1.00 114.16 ? 219  VAL B N   1 
ATOM   15960 C  CA  . VAL C 1 219  ? -11.902  59.419  71.394  1.00 111.96 ? 219  VAL B CA  1 
ATOM   15961 C  C   . VAL C 1 219  ? -12.847  58.357  70.950  1.00 112.59 ? 219  VAL B C   1 
ATOM   15962 O  O   . VAL C 1 219  ? -13.929  58.201  71.524  1.00 111.86 ? 219  VAL B O   1 
ATOM   15963 C  CB  . VAL C 1 219  ? -11.628  59.234  72.885  1.00 111.27 ? 219  VAL B CB  1 
ATOM   15964 C  CG1 . VAL C 1 219  ? -11.753  57.760  73.269  1.00 108.34 ? 219  VAL B CG1 1 
ATOM   15965 C  CG2 . VAL C 1 219  ? -10.257  59.811  73.247  1.00 107.50 ? 219  VAL B CG2 1 
ATOM   15966 N  N   . LYS C 1 220  ? -12.448  57.659  69.895  1.00 114.00 ? 220  LYS B N   1 
ATOM   15967 C  CA  . LYS C 1 220  ? -13.197  56.516  69.408  1.00 111.50 ? 220  LYS B CA  1 
ATOM   15968 C  C   . LYS C 1 220  ? -12.393  55.227  69.557  1.00 112.50 ? 220  LYS B C   1 
ATOM   15969 O  O   . LYS C 1 220  ? -11.160  55.240  69.587  1.00 103.80 ? 220  LYS B O   1 
ATOM   15970 C  CB  . LYS C 1 220  ? -13.656  56.738  67.966  1.00 110.82 ? 220  LYS B CB  1 
ATOM   15971 C  CG  . LYS C 1 220  ? -14.658  57.877  67.791  1.00 110.70 ? 220  LYS B CG  1 
ATOM   15972 C  CD  . LYS C 1 220  ? -14.566  58.450  66.375  1.00 113.46 ? 220  LYS B CD  1 
ATOM   15973 C  CE  . LYS C 1 220  ? -15.788  59.288  65.960  1.00 113.98 ? 220  LYS B CE  1 
ATOM   15974 N  NZ  . LYS C 1 220  ? -16.850  58.537  65.218  1.00 113.03 ? 220  LYS B NZ  1 
ATOM   15975 N  N   . GLU C 1 221  ? -13.131  54.128  69.662  1.00 116.77 ? 221  GLU B N   1 
ATOM   15976 C  CA  . GLU C 1 221  ? -12.580  52.802  69.926  1.00 128.44 ? 221  GLU B CA  1 
ATOM   15977 C  C   . GLU C 1 221  ? -12.239  51.998  68.676  1.00 126.58 ? 221  GLU B C   1 
ATOM   15978 O  O   . GLU C 1 221  ? -13.131  51.474  68.002  1.00 124.40 ? 221  GLU B O   1 
ATOM   15979 C  CB  . GLU C 1 221  ? -13.563  51.980  70.758  1.00 139.17 ? 221  GLU B CB  1 
ATOM   15980 C  CG  . GLU C 1 221  ? -13.191  50.506  70.818  1.00 149.58 ? 221  GLU B CG  1 
ATOM   15981 C  CD  . GLU C 1 221  ? -14.409  49.627  70.899  1.00 156.81 ? 221  GLU B CD  1 
ATOM   15982 O  OE1 . GLU C 1 221  ? -15.532  50.199  70.900  1.00 157.66 ? 221  GLU B OE1 1 
ATOM   15983 O  OE2 . GLU C 1 221  ? -14.236  48.380  70.959  1.00 159.69 ? 221  GLU B OE2 1 
ATOM   15984 N  N   . TYR C 1 222  ? -10.948  51.859  68.396  1.00 126.27 ? 222  TYR B N   1 
ATOM   15985 C  CA  . TYR C 1 222  ? -10.533  51.208  67.173  1.00 124.40 ? 222  TYR B CA  1 
ATOM   15986 C  C   . TYR C 1 222  ? -10.871  49.722  67.180  1.00 126.20 ? 222  TYR B C   1 
ATOM   15987 O  O   . TYR C 1 222  ? -10.687  49.047  68.191  1.00 127.55 ? 222  TYR B O   1 
ATOM   15988 C  CB  . TYR C 1 222  ? -9.046   51.403  66.925  1.00 123.80 ? 222  TYR B CB  1 
ATOM   15989 C  CG  . TYR C 1 222  ? -8.619   50.616  65.736  1.00 123.00 ? 222  TYR B CG  1 
ATOM   15990 C  CD1 . TYR C 1 222  ? -8.374   51.228  64.523  1.00 121.66 ? 222  TYR B CD1 1 
ATOM   15991 C  CD2 . TYR C 1 222  ? -8.520   49.241  65.810  1.00 124.44 ? 222  TYR B CD2 1 
ATOM   15992 C  CE1 . TYR C 1 222  ? -8.011   50.486  63.421  1.00 122.02 ? 222  TYR B CE1 1 
ATOM   15993 C  CE2 . TYR C 1 222  ? -8.168   48.499  64.727  1.00 124.73 ? 222  TYR B CE2 1 
ATOM   15994 C  CZ  . TYR C 1 222  ? -7.911   49.118  63.535  1.00 123.27 ? 222  TYR B CZ  1 
ATOM   15995 O  OH  . TYR C 1 222  ? -7.555   48.347  62.462  1.00 123.73 ? 222  TYR B OH  1 
ATOM   15996 N  N   . VAL C 1 223  ? -11.357  49.227  66.040  1.00 124.55 ? 223  VAL B N   1 
ATOM   15997 C  CA  . VAL C 1 223  ? -11.648  47.810  65.842  1.00 123.07 ? 223  VAL B CA  1 
ATOM   15998 C  C   . VAL C 1 223  ? -11.046  47.369  64.542  1.00 123.43 ? 223  VAL B C   1 
ATOM   15999 O  O   . VAL C 1 223  ? -11.142  48.069  63.536  1.00 122.38 ? 223  VAL B O   1 
ATOM   16000 C  CB  . VAL C 1 223  ? -13.129  47.528  65.627  1.00 119.57 ? 223  VAL B CB  1 
ATOM   16001 C  CG1 . VAL C 1 223  ? -13.363  46.023  65.600  1.00 118.44 ? 223  VAL B CG1 1 
ATOM   16002 C  CG2 . VAL C 1 223  ? -13.991  48.221  66.672  1.00 119.56 ? 223  VAL B CG2 1 
ATOM   16003 N  N   . LEU C 1 224  ? -10.471  46.177  64.553  1.00 126.37 ? 224  LEU B N   1 
ATOM   16004 C  CA  . LEU C 1 224  ? -9.883   45.597  63.359  1.00 127.83 ? 224  LEU B CA  1 
ATOM   16005 C  C   . LEU C 1 224  ? -10.987  45.219  62.384  1.00 132.21 ? 224  LEU B C   1 
ATOM   16006 O  O   . LEU C 1 224  ? -11.987  44.598  62.769  1.00 131.06 ? 224  LEU B O   1 
ATOM   16007 C  CB  . LEU C 1 224  ? -9.042   44.374  63.725  1.00 128.78 ? 224  LEU B CB  1 
ATOM   16008 C  CG  . LEU C 1 224  ? -7.753   44.221  62.933  1.00 129.16 ? 224  LEU B CG  1 
ATOM   16009 C  CD1 . LEU C 1 224  ? -8.028   43.536  61.626  1.00 130.62 ? 224  LEU B CD1 1 
ATOM   16010 C  CD2 . LEU C 1 224  ? -7.131   45.575  62.696  1.00 129.01 ? 224  LEU B CD2 1 
ATOM   16011 N  N   . PRO C 1 225  ? -10.814  45.604  61.112  1.00 143.22 ? 225  PRO B N   1 
ATOM   16012 C  CA  . PRO C 1 225  ? -11.842  45.380  60.095  1.00 141.75 ? 225  PRO B CA  1 
ATOM   16013 C  C   . PRO C 1 225  ? -11.645  44.035  59.417  1.00 138.97 ? 225  PRO B C   1 
ATOM   16014 O  O   . PRO C 1 225  ? -10.513  43.651  59.123  1.00 139.44 ? 225  PRO B O   1 
ATOM   16015 C  CB  . PRO C 1 225  ? -11.600  46.528  59.097  1.00 139.11 ? 225  PRO B CB  1 
ATOM   16016 C  CG  . PRO C 1 225  ? -10.394  47.328  59.645  1.00 142.42 ? 225  PRO B CG  1 
ATOM   16017 C  CD  . PRO C 1 225  ? -9.690   46.385  60.574  1.00 146.16 ? 225  PRO B CD  1 
ATOM   16018 N  N   . HIS C 1 226  ? -12.740  43.326  59.182  1.00 140.40 ? 226  HIS B N   1 
ATOM   16019 C  CA  . HIS C 1 226  ? -12.668  42.024  58.532  1.00 144.36 ? 226  HIS B CA  1 
ATOM   16020 C  C   . HIS C 1 226  ? -12.719  42.123  57.002  1.00 139.53 ? 226  HIS B C   1 
ATOM   16021 O  O   . HIS C 1 226  ? -12.098  41.339  56.269  1.00 137.59 ? 226  HIS B O   1 
ATOM   16022 C  CB  . HIS C 1 226  ? -13.792  41.118  59.038  1.00 150.38 ? 226  HIS B CB  1 
ATOM   16023 C  CG  . HIS C 1 226  ? -13.554  40.562  60.410  1.00 158.51 ? 226  HIS B CG  1 
ATOM   16024 N  ND1 . HIS C 1 226  ? -14.391  40.823  61.477  1.00 162.28 ? 226  HIS B ND1 1 
ATOM   16025 C  CD2 . HIS C 1 226  ? -12.574  39.758  60.891  1.00 163.11 ? 226  HIS B CD2 1 
ATOM   16026 C  CE1 . HIS C 1 226  ? -13.938  40.205  62.553  1.00 166.07 ? 226  HIS B CE1 1 
ATOM   16027 N  NE2 . HIS C 1 226  ? -12.837  39.550  62.224  1.00 166.75 ? 226  HIS B NE2 1 
ATOM   16028 N  N   . PHE C 1 227  ? -13.480  43.096  56.524  1.00 137.25 ? 227  PHE B N   1 
ATOM   16029 C  CA  . PHE C 1 227  ? -13.650  43.292  55.090  1.00 134.00 ? 227  PHE B CA  1 
ATOM   16030 C  C   . PHE C 1 227  ? -14.254  44.637  54.861  1.00 133.57 ? 227  PHE B C   1 
ATOM   16031 O  O   . PHE C 1 227  ? -15.140  45.048  55.596  1.00 136.38 ? 227  PHE B O   1 
ATOM   16032 C  CB  . PHE C 1 227  ? -14.582  42.242  54.487  1.00 128.39 ? 227  PHE B CB  1 
ATOM   16033 C  CG  . PHE C 1 227  ? -15.884  42.126  55.189  1.00 121.73 ? 227  PHE B CG  1 
ATOM   16034 C  CD1 . PHE C 1 227  ? -16.891  42.998  54.926  1.00 116.93 ? 227  PHE B CD1 1 
ATOM   16035 C  CD2 . PHE C 1 227  ? -16.090  41.133  56.123  1.00 121.93 ? 227  PHE B CD2 1 
ATOM   16036 C  CE1 . PHE C 1 227  ? -18.079  42.881  55.586  1.00 116.99 ? 227  PHE B CE1 1 
ATOM   16037 C  CE2 . PHE C 1 227  ? -17.279  41.009  56.783  1.00 120.70 ? 227  PHE B CE2 1 
ATOM   16038 C  CZ  . PHE C 1 227  ? -18.271  41.878  56.520  1.00 118.52 ? 227  PHE B CZ  1 
ATOM   16039 N  N   . SER C 1 228  ? -13.795  45.301  53.817  1.00 131.45 ? 228  SER B N   1 
ATOM   16040 C  CA  . SER C 1 228  ? -14.207  46.657  53.564  1.00 132.04 ? 228  SER B CA  1 
ATOM   16041 C  C   . SER C 1 228  ? -15.716  46.784  53.265  1.00 127.28 ? 228  SER B C   1 
ATOM   16042 O  O   . SER C 1 228  ? -16.187  46.286  52.251  1.00 124.56 ? 228  SER B O   1 
ATOM   16043 C  CB  . SER C 1 228  ? -13.351  47.217  52.422  1.00 136.60 ? 228  SER B CB  1 
ATOM   16044 O  OG  . SER C 1 228  ? -13.784  48.511  52.028  1.00 137.94 ? 228  SER B OG  1 
ATOM   16045 N  N   . VAL C 1 229  ? -16.476  47.422  54.157  1.00 123.31 ? 229  VAL B N   1 
ATOM   16046 C  CA  . VAL C 1 229  ? -17.859  47.756  53.846  1.00 118.38 ? 229  VAL B CA  1 
ATOM   16047 C  C   . VAL C 1 229  ? -17.939  49.239  53.498  1.00 113.33 ? 229  VAL B C   1 
ATOM   16048 O  O   . VAL C 1 229  ? -17.493  50.093  54.271  1.00 113.71 ? 229  VAL B O   1 
ATOM   16049 C  CB  . VAL C 1 229  ? -18.837  47.375  54.987  1.00 94.02  ? 229  VAL B CB  1 
ATOM   16050 C  CG1 . VAL C 1 229  ? -20.075  48.227  54.931  1.00 86.48  ? 229  VAL B CG1 1 
ATOM   16051 C  CG2 . VAL C 1 229  ? -19.220  45.926  54.870  1.00 89.51  ? 229  VAL B CG2 1 
ATOM   16052 N  N   . SER C 1 230  ? -18.449  49.524  52.296  1.00 112.13 ? 230  SER B N   1 
ATOM   16053 C  CA  . SER C 1 230  ? -18.697  50.893  51.815  1.00 109.32 ? 230  SER B CA  1 
ATOM   16054 C  C   . SER C 1 230  ? -20.173  51.191  51.773  1.00 106.71 ? 230  SER B C   1 
ATOM   16055 O  O   . SER C 1 230  ? -20.988  50.280  51.577  1.00 106.84 ? 230  SER B O   1 
ATOM   16056 C  CB  . SER C 1 230  ? -18.135  51.109  50.400  1.00 107.59 ? 230  SER B CB  1 
ATOM   16057 O  OG  . SER C 1 230  ? -18.875  50.425  49.413  1.00 104.16 ? 230  SER B OG  1 
ATOM   16058 N  N   . ILE C 1 231  ? -20.524  52.465  51.885  1.00 103.97 ? 231  ILE B N   1 
ATOM   16059 C  CA  . ILE C 1 231  ? -21.922  52.823  51.811  1.00 102.91 ? 231  ILE B CA  1 
ATOM   16060 C  C   . ILE C 1 231  ? -22.119  54.186  51.162  1.00 108.67 ? 231  ILE B C   1 
ATOM   16061 O  O   . ILE C 1 231  ? -21.618  55.197  51.650  1.00 110.85 ? 231  ILE B O   1 
ATOM   16062 C  CB  . ILE C 1 231  ? -22.587  52.742  53.189  1.00 100.39 ? 231  ILE B CB  1 
ATOM   16063 C  CG1 . ILE C 1 231  ? -23.780  53.667  53.262  1.00 97.89  ? 231  ILE B CG1 1 
ATOM   16064 C  CG2 . ILE C 1 231  ? -21.622  53.099  54.282  1.00 100.95 ? 231  ILE B CG2 1 
ATOM   16065 C  CD1 . ILE C 1 231  ? -24.380  53.647  54.615  1.00 99.69  ? 231  ILE B CD1 1 
ATOM   16066 N  N   . GLU C 1 232  ? -22.833  54.191  50.035  1.00 112.85 ? 232  GLU B N   1 
ATOM   16067 C  CA  . GLU C 1 232  ? -22.994  55.382  49.191  1.00 116.00 ? 232  GLU B CA  1 
ATOM   16068 C  C   . GLU C 1 232  ? -24.473  55.718  48.951  1.00 114.19 ? 232  GLU B C   1 
ATOM   16069 O  O   . GLU C 1 232  ? -25.290  54.863  48.604  1.00 112.02 ? 232  GLU B O   1 
ATOM   16070 C  CB  . GLU C 1 232  ? -22.276  55.183  47.852  1.00 122.26 ? 232  GLU B CB  1 
ATOM   16071 C  CG  . GLU C 1 232  ? -20.939  54.461  47.971  1.00 131.18 ? 232  GLU B CG  1 
ATOM   16072 C  CD  . GLU C 1 232  ? -20.576  53.590  46.757  1.00 137.51 ? 232  GLU B CD  1 
ATOM   16073 O  OE1 . GLU C 1 232  ? -21.033  53.856  45.616  1.00 138.92 ? 232  GLU B OE1 1 
ATOM   16074 O  OE2 . GLU C 1 232  ? -19.799  52.630  46.956  1.00 140.72 ? 232  GLU B OE2 1 
ATOM   16075 N  N   . PRO C 1 233  ? -24.817  56.983  49.125  1.00 114.81 ? 233  PRO B N   1 
ATOM   16076 C  CA  . PRO C 1 233  ? -26.202  57.420  49.223  1.00 116.00 ? 233  PRO B CA  1 
ATOM   16077 C  C   . PRO C 1 233  ? -26.627  58.014  47.894  1.00 116.22 ? 233  PRO B C   1 
ATOM   16078 O  O   . PRO C 1 233  ? -25.752  58.536  47.202  1.00 117.80 ? 233  PRO B O   1 
ATOM   16079 C  CB  . PRO C 1 233  ? -26.112  58.526  50.268  1.00 117.79 ? 233  PRO B CB  1 
ATOM   16080 C  CG  . PRO C 1 233  ? -24.579  58.848  50.398  1.00 115.96 ? 233  PRO B CG  1 
ATOM   16081 C  CD  . PRO C 1 233  ? -23.900  58.110  49.292  1.00 115.21 ? 233  PRO B CD  1 
ATOM   16082 N  N   . GLU C 1 234  ? -27.916  57.980  47.549  1.00 112.53 ? 234  GLU B N   1 
ATOM   16083 C  CA  . GLU C 1 234  ? -28.313  58.431  46.222  1.00 109.36 ? 234  GLU B CA  1 
ATOM   16084 C  C   . GLU C 1 234  ? -27.701  59.780  45.890  1.00 104.48 ? 234  GLU B C   1 
ATOM   16085 O  O   . GLU C 1 234  ? -27.001  59.901  44.902  1.00 106.44 ? 234  GLU B O   1 
ATOM   16086 C  CB  . GLU C 1 234  ? -29.828  58.421  45.985  1.00 112.03 ? 234  GLU B CB  1 
ATOM   16087 C  CG  . GLU C 1 234  ? -30.107  58.340  44.465  1.00 121.05 ? 234  GLU B CG  1 
ATOM   16088 C  CD  . GLU C 1 234  ? -31.572  58.339  44.052  1.00 125.25 ? 234  GLU B CD  1 
ATOM   16089 O  OE1 . GLU C 1 234  ? -32.435  58.028  44.906  1.00 127.45 ? 234  GLU B OE1 1 
ATOM   16090 O  OE2 . GLU C 1 234  ? -31.840  58.634  42.854  1.00 125.19 ? 234  GLU B OE2 1 
ATOM   16091 N  N   . TYR C 1 235  ? -27.940  60.789  46.714  1.00 99.27  ? 235  TYR B N   1 
ATOM   16092 C  CA  . TYR C 1 235  ? -27.235  62.059  46.559  1.00 96.38  ? 235  TYR B CA  1 
ATOM   16093 C  C   . TYR C 1 235  ? -26.824  62.581  47.939  1.00 93.34  ? 235  TYR B C   1 
ATOM   16094 O  O   . TYR C 1 235  ? -27.106  61.963  48.949  1.00 94.06  ? 235  TYR B O   1 
ATOM   16095 C  CB  . TYR C 1 235  ? -28.083  63.140  45.866  1.00 96.91  ? 235  TYR B CB  1 
ATOM   16096 C  CG  . TYR C 1 235  ? -28.950  62.766  44.668  1.00 99.18  ? 235  TYR B CG  1 
ATOM   16097 C  CD1 . TYR C 1 235  ? -29.192  63.697  43.672  1.00 103.07 ? 235  TYR B CD1 1 
ATOM   16098 C  CD2 . TYR C 1 235  ? -29.567  61.527  44.551  1.00 101.15 ? 235  TYR B CD2 1 
ATOM   16099 C  CE1 . TYR C 1 235  ? -30.004  63.407  42.564  1.00 106.07 ? 235  TYR B CE1 1 
ATOM   16100 C  CE2 . TYR C 1 235  ? -30.379  61.220  43.446  1.00 103.86 ? 235  TYR B CE2 1 
ATOM   16101 C  CZ  . TYR C 1 235  ? -30.591  62.167  42.456  1.00 106.67 ? 235  TYR B CZ  1 
ATOM   16102 O  OH  . TYR C 1 235  ? -31.387  61.899  41.358  1.00 108.21 ? 235  TYR B OH  1 
ATOM   16103 N  N   . ASN C 1 236  ? -26.200  63.750  47.973  1.00 91.51  ? 236  ASN B N   1 
ATOM   16104 C  CA  . ASN C 1 236  ? -25.608  64.273  49.196  1.00 90.85  ? 236  ASN B CA  1 
ATOM   16105 C  C   . ASN C 1 236  ? -26.515  65.118  50.078  1.00 87.93  ? 236  ASN B C   1 
ATOM   16106 O  O   . ASN C 1 236  ? -26.141  65.506  51.207  1.00 92.84  ? 236  ASN B O   1 
ATOM   16107 C  CB  . ASN C 1 236  ? -24.381  65.087  48.859  1.00 95.86  ? 236  ASN B CB  1 
ATOM   16108 C  CG  . ASN C 1 236  ? -23.179  64.227  48.636  1.00 103.12 ? 236  ASN B CG  1 
ATOM   16109 O  OD1 . ASN C 1 236  ? -23.269  62.990  48.607  1.00 104.07 ? 236  ASN B OD1 1 
ATOM   16110 N  ND2 . ASN C 1 236  ? -22.032  64.868  48.469  1.00 107.49 ? 236  ASN B ND2 1 
ATOM   16111 N  N   . PHE C 1 237  ? -27.684  65.464  49.563  1.00 79.52  ? 237  PHE B N   1 
ATOM   16112 C  CA  . PHE C 1 237  ? -28.680  66.079  50.411  1.00 79.18  ? 237  PHE B CA  1 
ATOM   16113 C  C   . PHE C 1 237  ? -29.963  65.470  49.978  1.00 75.83  ? 237  PHE B C   1 
ATOM   16114 O  O   . PHE C 1 237  ? -30.042  64.929  48.903  1.00 71.43  ? 237  PHE B O   1 
ATOM   16115 C  CB  . PHE C 1 237  ? -28.804  67.565  50.183  1.00 67.54  ? 237  PHE B CB  1 
ATOM   16116 C  CG  . PHE C 1 237  ? -27.521  68.287  50.161  1.00 68.16  ? 237  PHE B CG  1 
ATOM   16117 C  CD1 . PHE C 1 237  ? -27.404  69.502  50.768  1.00 69.92  ? 237  PHE B CD1 1 
ATOM   16118 C  CD2 . PHE C 1 237  ? -26.447  67.802  49.490  1.00 68.95  ? 237  PHE B CD2 1 
ATOM   16119 C  CE1 . PHE C 1 237  ? -26.231  70.206  50.722  1.00 75.75  ? 237  PHE B CE1 1 
ATOM   16120 C  CE2 . PHE C 1 237  ? -25.268  68.503  49.448  1.00 76.67  ? 237  PHE B CE2 1 
ATOM   16121 C  CZ  . PHE C 1 237  ? -25.166  69.702  50.066  1.00 76.40  ? 237  PHE B CZ  1 
ATOM   16122 N  N   . ILE C 1 238  ? -30.974  65.572  50.819  1.00 78.59  ? 238  ILE B N   1 
ATOM   16123 C  CA  . ILE C 1 238  ? -32.302  65.206  50.406  1.00 79.85  ? 238  ILE B CA  1 
ATOM   16124 C  C   . ILE C 1 238  ? -33.181  66.436  50.147  1.00 85.25  ? 238  ILE B C   1 
ATOM   16125 O  O   . ILE C 1 238  ? -33.159  67.412  50.908  1.00 87.57  ? 238  ILE B O   1 
ATOM   16126 C  CB  . ILE C 1 238  ? -32.889  64.245  51.356  1.00 73.31  ? 238  ILE B CB  1 
ATOM   16127 C  CG1 . ILE C 1 238  ? -31.785  63.331  51.845  1.00 69.12  ? 238  ILE B CG1 1 
ATOM   16128 C  CG2 . ILE C 1 238  ? -33.893  63.440  50.637  1.00 77.63  ? 238  ILE B CG2 1 
ATOM   16129 C  CD1 . ILE C 1 238  ? -32.281  62.009  52.374  1.00 70.14  ? 238  ILE B CD1 1 
ATOM   16130 N  N   . GLY C 1 239  ? -33.915  66.368  49.035  1.00 89.68  ? 239  GLY B N   1 
ATOM   16131 C  CA  . GLY C 1 239  ? -34.573  67.518  48.425  1.00 92.35  ? 239  GLY B CA  1 
ATOM   16132 C  C   . GLY C 1 239  ? -35.918  67.067  47.891  1.00 95.88  ? 239  GLY B C   1 
ATOM   16133 O  O   . GLY C 1 239  ? -36.129  65.861  47.700  1.00 95.92  ? 239  GLY B O   1 
ATOM   16134 N  N   . TYR C 1 240  ? -36.846  67.996  47.673  1.00 98.17  ? 240  TYR B N   1 
ATOM   16135 C  CA  . TYR C 1 240  ? -38.232  67.547  47.590  1.00 101.68 ? 240  TYR B CA  1 
ATOM   16136 C  C   . TYR C 1 240  ? -38.311  66.428  46.599  1.00 102.95 ? 240  TYR B C   1 
ATOM   16137 O  O   . TYR C 1 240  ? -39.116  65.539  46.752  1.00 101.75 ? 240  TYR B O   1 
ATOM   16138 C  CB  . TYR C 1 240  ? -39.195  68.653  47.168  1.00 101.73 ? 240  TYR B CB  1 
ATOM   16139 C  CG  . TYR C 1 240  ? -39.046  69.000  45.722  1.00 97.37  ? 240  TYR B CG  1 
ATOM   16140 C  CD1 . TYR C 1 240  ? -39.806  68.388  44.747  1.00 93.75  ? 240  TYR B CD1 1 
ATOM   16141 C  CD2 . TYR C 1 240  ? -38.103  69.906  45.334  1.00 96.79  ? 240  TYR B CD2 1 
ATOM   16142 C  CE1 . TYR C 1 240  ? -39.626  68.695  43.434  1.00 91.58  ? 240  TYR B CE1 1 
ATOM   16143 C  CE2 . TYR C 1 240  ? -37.930  70.221  44.033  1.00 95.62  ? 240  TYR B CE2 1 
ATOM   16144 C  CZ  . TYR C 1 240  ? -38.679  69.617  43.085  1.00 93.46  ? 240  TYR B CZ  1 
ATOM   16145 O  OH  . TYR C 1 240  ? -38.438  69.984  41.786  1.00 95.43  ? 240  TYR B OH  1 
ATOM   16146 N  N   . LYS C 1 241  ? -37.450  66.492  45.588  1.00 107.09 ? 241  LYS B N   1 
ATOM   16147 C  CA  . LYS C 1 241  ? -37.471  65.542  44.478  1.00 112.48 ? 241  LYS B CA  1 
ATOM   16148 C  C   . LYS C 1 241  ? -37.542  64.096  45.000  1.00 117.17 ? 241  LYS B C   1 
ATOM   16149 O  O   . LYS C 1 241  ? -38.527  63.378  44.743  1.00 119.56 ? 241  LYS B O   1 
ATOM   16150 C  CB  . LYS C 1 241  ? -36.287  65.761  43.495  1.00 95.37  ? 241  LYS B CB  1 
ATOM   16151 C  CG  . LYS C 1 241  ? -36.566  66.751  42.321  1.00 79.13  ? 241  LYS B CG  1 
ATOM   16152 C  CD  . LYS C 1 241  ? -35.306  67.102  41.480  1.00 91.62  ? 241  LYS B CD  1 
ATOM   16153 C  CE  . LYS C 1 241  ? -35.585  68.062  40.255  1.00 123.38 ? 241  LYS B CE  1 
ATOM   16154 N  NZ  . LYS C 1 241  ? -35.392  69.554  40.447  1.00 122.42 ? 241  LYS B NZ  1 
ATOM   16155 N  N   . ASN C 1 242  ? -36.514  63.668  45.734  1.00 118.46 ? 242  ASN B N   1 
ATOM   16156 C  CA  . ASN C 1 242  ? -36.560  62.376  46.426  1.00 117.93 ? 242  ASN B CA  1 
ATOM   16157 C  C   . ASN C 1 242  ? -36.798  62.569  47.908  1.00 121.69 ? 242  ASN B C   1 
ATOM   16158 O  O   . ASN C 1 242  ? -36.166  63.406  48.539  1.00 120.01 ? 242  ASN B O   1 
ATOM   16159 C  CB  . ASN C 1 242  ? -35.319  61.516  46.171  1.00 111.79 ? 242  ASN B CB  1 
ATOM   16160 C  CG  . ASN C 1 242  ? -34.173  62.286  45.550  1.00 105.61 ? 242  ASN B CG  1 
ATOM   16161 O  OD1 . ASN C 1 242  ? -33.325  61.692  44.897  1.00 104.05 ? 242  ASN B OD1 1 
ATOM   16162 N  ND2 . ASN C 1 242  ? -34.135  63.602  45.745  1.00 102.09 ? 242  ASN B ND2 1 
ATOM   16163 N  N   . PHE C 1 243  ? -37.733  61.798  48.442  1.00 127.97 ? 243  PHE B N   1 
ATOM   16164 C  CA  . PHE C 1 243  ? -38.241  61.992  49.786  1.00 134.83 ? 243  PHE B CA  1 
ATOM   16165 C  C   . PHE C 1 243  ? -39.384  61.040  49.883  1.00 142.07 ? 243  PHE B C   1 
ATOM   16166 O  O   . PHE C 1 243  ? -39.996  60.883  50.928  1.00 142.45 ? 243  PHE B O   1 
ATOM   16167 C  CB  . PHE C 1 243  ? -38.776  63.402  49.981  1.00 136.75 ? 243  PHE B CB  1 
ATOM   16168 C  CG  . PHE C 1 243  ? -39.320  63.662  51.366  1.00 140.10 ? 243  PHE B CG  1 
ATOM   16169 C  CD1 . PHE C 1 243  ? -38.463  63.958  52.416  1.00 140.24 ? 243  PHE B CD1 1 
ATOM   16170 C  CD2 . PHE C 1 243  ? -40.681  63.637  51.611  1.00 142.18 ? 243  PHE B CD2 1 
ATOM   16171 C  CE1 . PHE C 1 243  ? -38.945  64.211  53.674  1.00 141.50 ? 243  PHE B CE1 1 
ATOM   16172 C  CE2 . PHE C 1 243  ? -41.165  63.897  52.875  1.00 143.75 ? 243  PHE B CE2 1 
ATOM   16173 C  CZ  . PHE C 1 243  ? -40.295  64.184  53.902  1.00 143.23 ? 243  PHE B CZ  1 
ATOM   16174 N  N   . LYS C 1 244  ? -39.707  60.448  48.747  1.00 148.26 ? 244  LYS B N   1 
ATOM   16175 C  CA  . LYS C 1 244  ? -40.438  59.209  48.755  1.00 156.40 ? 244  LYS B CA  1 
ATOM   16176 C  C   . LYS C 1 244  ? -39.449  58.123  48.360  1.00 157.59 ? 244  LYS B C   1 
ATOM   16177 O  O   . LYS C 1 244  ? -39.783  56.945  48.379  1.00 163.22 ? 244  LYS B O   1 
ATOM   16178 C  CB  . LYS C 1 244  ? -41.667  59.267  47.847  1.00 161.42 ? 244  LYS B CB  1 
ATOM   16179 C  CG  . LYS C 1 244  ? -42.825  60.083  48.434  1.00 165.79 ? 244  LYS B CG  1 
ATOM   16180 C  CD  . LYS C 1 244  ? -44.179  59.609  47.896  1.00 169.45 ? 244  LYS B CD  1 
ATOM   16181 C  CE  . LYS C 1 244  ? -45.338  60.518  48.314  1.00 171.12 ? 244  LYS B CE  1 
ATOM   16182 N  NZ  . LYS C 1 244  ? -45.450  61.739  47.478  1.00 169.73 ? 244  LYS B NZ  1 
ATOM   16183 N  N   . ASN C 1 245  ? -38.221  58.527  48.036  1.00 150.90 ? 245  ASN B N   1 
ATOM   16184 C  CA  . ASN C 1 245  ? -37.152  57.557  47.776  1.00 149.73 ? 245  ASN B CA  1 
ATOM   16185 C  C   . ASN C 1 245  ? -35.716  58.136  47.743  1.00 141.71 ? 245  ASN B C   1 
ATOM   16186 O  O   . ASN C 1 245  ? -35.533  59.331  47.488  1.00 142.88 ? 245  ASN B O   1 
ATOM   16187 C  CB  . ASN C 1 245  ? -37.436  56.804  46.486  1.00 150.45 ? 245  ASN B CB  1 
ATOM   16188 C  CG  . ASN C 1 245  ? -37.269  57.667  45.291  1.00 153.87 ? 245  ASN B CG  1 
ATOM   16189 O  OD1 . ASN C 1 245  ? -37.282  58.894  45.392  1.00 154.01 ? 245  ASN B OD1 1 
ATOM   16190 N  ND2 . ASN C 1 245  ? -37.096  57.044  44.144  1.00 156.16 ? 245  ASN B ND2 1 
ATOM   16191 N  N   . PHE C 1 246  ? -34.721  57.257  47.981  1.00 134.04 ? 246  PHE B N   1 
ATOM   16192 C  CA  . PHE C 1 246  ? -33.290  57.595  48.144  1.00 117.88 ? 246  PHE B CA  1 
ATOM   16193 C  C   . PHE C 1 246  ? -32.417  56.355  47.971  1.00 111.09 ? 246  PHE B C   1 
ATOM   16194 O  O   . PHE C 1 246  ? -32.184  55.683  48.957  1.00 109.78 ? 246  PHE B O   1 
ATOM   16195 C  CB  . PHE C 1 246  ? -33.065  58.066  49.576  1.00 107.99 ? 246  PHE B CB  1 
ATOM   16196 C  CG  . PHE C 1 246  ? -31.890  58.975  49.745  1.00 96.35  ? 246  PHE B CG  1 
ATOM   16197 C  CD1 . PHE C 1 246  ? -31.873  60.209  49.168  1.00 89.56  ? 246  PHE B CD1 1 
ATOM   16198 C  CD2 . PHE C 1 246  ? -30.825  58.610  50.520  1.00 92.76  ? 246  PHE B CD2 1 
ATOM   16199 C  CE1 . PHE C 1 246  ? -30.811  61.032  49.339  1.00 85.75  ? 246  PHE B CE1 1 
ATOM   16200 C  CE2 . PHE C 1 246  ? -29.769  59.450  50.688  1.00 89.19  ? 246  PHE B CE2 1 
ATOM   16201 C  CZ  . PHE C 1 246  ? -29.766  60.655  50.097  1.00 86.16  ? 246  PHE B CZ  1 
ATOM   16202 N  N   . GLU C 1 247  ? -31.919  56.067  46.760  1.00 108.99 ? 247  GLU B N   1 
ATOM   16203 C  CA  . GLU C 1 247  ? -31.229  54.781  46.436  1.00 109.04 ? 247  GLU B CA  1 
ATOM   16204 C  C   . GLU C 1 247  ? -29.845  54.696  47.179  1.00 114.37 ? 247  GLU B C   1 
ATOM   16205 O  O   . GLU C 1 247  ? -28.833  55.205  46.688  1.00 115.31 ? 247  GLU B O   1 
ATOM   16206 C  CB  . GLU C 1 247  ? -31.130  54.569  44.862  1.00 153.91 ? 247  GLU B CB  1 
ATOM   16207 C  CG  . GLU C 1 247  ? -31.506  53.127  44.211  1.00 135.64 ? 247  GLU B CG  1 
ATOM   16208 C  CD  . GLU C 1 247  ? -32.585  53.134  43.029  1.00 88.08  ? 247  GLU B CD  1 
ATOM   16209 O  OE1 . GLU C 1 247  ? -33.616  53.824  43.180  1.00 80.64  ? 247  GLU B OE1 1 
ATOM   16210 O  OE2 . GLU C 1 247  ? -32.417  52.444  41.963  1.00 72.31  ? 247  GLU B OE2 1 
ATOM   16211 N  N   . ILE C 1 248  ? -29.821  54.092  48.376  1.00 111.97 ? 248  ILE B N   1 
ATOM   16212 C  CA  . ILE C 1 248  ? -28.590  53.895  49.157  1.00 106.48 ? 248  ILE B CA  1 
ATOM   16213 C  C   . ILE C 1 248  ? -27.933  52.601  48.758  1.00 104.60 ? 248  ILE B C   1 
ATOM   16214 O  O   . ILE C 1 248  ? -28.484  51.537  49.027  1.00 105.81 ? 248  ILE B O   1 
ATOM   16215 C  CB  . ILE C 1 248  ? -28.871  53.728  50.671  1.00 105.79 ? 248  ILE B CB  1 
ATOM   16216 C  CG1 . ILE C 1 248  ? -29.769  54.831  51.207  1.00 105.00 ? 248  ILE B CG1 1 
ATOM   16217 C  CG2 . ILE C 1 248  ? -27.575  53.721  51.464  1.00 106.04 ? 248  ILE B CG2 1 
ATOM   16218 C  CD1 . ILE C 1 248  ? -29.778  54.904  52.706  1.00 105.64 ? 248  ILE B CD1 1 
ATOM   16219 N  N   . THR C 1 249  ? -26.762  52.677  48.128  1.00 102.42 ? 249  THR B N   1 
ATOM   16220 C  CA  . THR C 1 249  ? -26.062  51.466  47.650  1.00 103.91 ? 249  THR B CA  1 
ATOM   16221 C  C   . THR C 1 249  ? -24.874  51.035  48.547  1.00 106.38 ? 249  THR B C   1 
ATOM   16222 O  O   . THR C 1 249  ? -23.879  51.767  48.660  1.00 104.62 ? 249  THR B O   1 
ATOM   16223 C  CB  . THR C 1 249  ? -25.494  51.661  46.218  1.00 109.11 ? 249  THR B CB  1 
ATOM   16224 O  OG1 . THR C 1 249  ? -26.182  52.732  45.547  1.00 107.61 ? 249  THR B OG1 1 
ATOM   16225 C  CG2 . THR C 1 249  ? -25.553  50.346  45.423  1.00 108.70 ? 249  THR B CG2 1 
ATOM   16226 N  N   . ILE C 1 250  ? -24.944  49.847  49.148  1.00 108.78 ? 250  ILE B N   1 
ATOM   16227 C  CA  . ILE C 1 250  ? -23.835  49.390  49.977  1.00 111.86 ? 250  ILE B CA  1 
ATOM   16228 C  C   . ILE C 1 250  ? -23.048  48.281  49.284  1.00 115.61 ? 250  ILE B C   1 
ATOM   16229 O  O   . ILE C 1 250  ? -23.636  47.435  48.633  1.00 115.48 ? 250  ILE B O   1 
ATOM   16230 C  CB  . ILE C 1 250  ? -24.339  48.953  51.325  1.00 111.52 ? 250  ILE B CB  1 
ATOM   16231 C  CG1 . ILE C 1 250  ? -25.000  47.607  51.217  1.00 113.66 ? 250  ILE B CG1 1 
ATOM   16232 C  CG2 . ILE C 1 250  ? -25.411  49.881  51.793  1.00 108.62 ? 250  ILE B CG2 1 
ATOM   16233 C  CD1 . ILE C 1 250  ? -25.719  47.248  52.459  1.00 115.83 ? 250  ILE B CD1 1 
ATOM   16234 N  N   . LYS C 1 251  ? -21.723  48.283  49.420  1.00 121.60 ? 251  LYS B N   1 
ATOM   16235 C  CA  . LYS C 1 251  ? -20.876  47.369  48.634  1.00 129.95 ? 251  LYS B CA  1 
ATOM   16236 C  C   . LYS C 1 251  ? -19.743  46.708  49.457  1.00 138.35 ? 251  LYS B C   1 
ATOM   16237 O  O   . LYS C 1 251  ? -18.786  47.372  49.887  1.00 140.47 ? 251  LYS B O   1 
ATOM   16238 C  CB  . LYS C 1 251  ? -20.280  48.091  47.413  1.00 130.40 ? 251  LYS B CB  1 
ATOM   16239 C  CG  . LYS C 1 251  ? -21.278  48.894  46.589  1.00 130.33 ? 251  LYS B CG  1 
ATOM   16240 C  CD  . LYS C 1 251  ? -20.692  49.363  45.242  1.00 131.44 ? 251  LYS B CD  1 
ATOM   16241 C  CE  . LYS C 1 251  ? -19.690  50.499  45.396  1.00 132.34 ? 251  LYS B CE  1 
ATOM   16242 N  NZ  . LYS C 1 251  ? -19.327  51.187  44.118  1.00 131.36 ? 251  LYS B NZ  1 
ATOM   16243 N  N   . ALA C 1 252  ? -19.854  45.392  49.649  1.00 143.39 ? 252  ALA B N   1 
ATOM   16244 C  CA  . ALA C 1 252  ? -18.983  44.646  50.562  1.00 146.75 ? 252  ALA B CA  1 
ATOM   16245 C  C   . ALA C 1 252  ? -17.952  43.780  49.849  1.00 148.81 ? 252  ALA B C   1 
ATOM   16246 O  O   . ALA C 1 252  ? -18.254  43.156  48.846  1.00 149.59 ? 252  ALA B O   1 
ATOM   16247 C  CB  . ALA C 1 252  ? -19.828  43.794  51.509  1.00 148.26 ? 252  ALA B CB  1 
ATOM   16248 N  N   . ARG C 1 253  ? -16.747  43.705  50.401  1.00 150.90 ? 253  ARG B N   1 
ATOM   16249 C  CA  . ARG C 1 253  ? -15.641  43.059  49.712  1.00 152.67 ? 253  ARG B CA  1 
ATOM   16250 C  C   . ARG C 1 253  ? -14.432  42.824  50.624  1.00 150.29 ? 253  ARG B C   1 
ATOM   16251 O  O   . ARG C 1 253  ? -14.053  43.707  51.406  1.00 150.36 ? 253  ARG B O   1 
ATOM   16252 C  CB  . ARG C 1 253  ? -15.200  43.966  48.585  1.00 159.19 ? 253  ARG B CB  1 
ATOM   16253 C  CG  . ARG C 1 253  ? -14.665  45.290  49.089  1.00 166.48 ? 253  ARG B CG  1 
ATOM   16254 C  CD  . ARG C 1 253  ? -13.662  45.846  48.116  1.00 174.83 ? 253  ARG B CD  1 
ATOM   16255 N  NE  . ARG C 1 253  ? -12.777  44.798  47.601  1.00 183.58 ? 253  ARG B NE  1 
ATOM   16256 C  CZ  . ARG C 1 253  ? -12.996  44.091  46.486  1.00 187.61 ? 253  ARG B CZ  1 
ATOM   16257 N  NH1 . ARG C 1 253  ? -14.080  44.302  45.749  1.00 187.31 ? 253  ARG B NH1 1 
ATOM   16258 N  NH2 . ARG C 1 253  ? -12.133  43.163  46.098  1.00 190.27 ? 253  ARG B NH2 1 
ATOM   16259 N  N   . TYR C 1 254  ? -13.812  41.647  50.504  1.00 144.95 ? 254  TYR B N   1 
ATOM   16260 C  CA  . TYR C 1 254  ? -12.617  41.323  51.291  1.00 139.84 ? 254  TYR B CA  1 
ATOM   16261 C  C   . TYR C 1 254  ? -11.362  42.004  50.751  1.00 135.67 ? 254  TYR B C   1 
ATOM   16262 O  O   . TYR C 1 254  ? -11.330  42.444  49.618  1.00 132.19 ? 254  TYR B O   1 
ATOM   16263 C  CB  . TYR C 1 254  ? -12.406  39.815  51.379  1.00 140.07 ? 254  TYR B CB  1 
ATOM   16264 C  CG  . TYR C 1 254  ? -13.649  39.034  51.728  1.00 139.41 ? 254  TYR B CG  1 
ATOM   16265 C  CD1 . TYR C 1 254  ? -14.141  38.075  50.877  1.00 140.30 ? 254  TYR B CD1 1 
ATOM   16266 C  CD2 . TYR C 1 254  ? -14.333  39.264  52.902  1.00 139.53 ? 254  TYR B CD2 1 
ATOM   16267 C  CE1 . TYR C 1 254  ? -15.273  37.357  51.185  1.00 140.45 ? 254  TYR B CE1 1 
ATOM   16268 C  CE2 . TYR C 1 254  ? -15.473  38.552  53.221  1.00 139.68 ? 254  TYR B CE2 1 
ATOM   16269 C  CZ  . TYR C 1 254  ? -15.935  37.599  52.358  1.00 139.84 ? 254  TYR B CZ  1 
ATOM   16270 O  OH  . TYR C 1 254  ? -17.068  36.890  52.665  1.00 140.23 ? 254  TYR B OH  1 
ATOM   16271 N  N   . PHE C 1 255  ? -10.335  42.106  51.578  1.00 137.03 ? 255  PHE B N   1 
ATOM   16272 C  CA  . PHE C 1 255  ? -9.149   42.859  51.215  1.00 140.63 ? 255  PHE B CA  1 
ATOM   16273 C  C   . PHE C 1 255  ? -8.378   42.150  50.142  1.00 147.87 ? 255  PHE B C   1 
ATOM   16274 O  O   . PHE C 1 255  ? -7.443   42.715  49.578  1.00 147.17 ? 255  PHE B O   1 
ATOM   16275 C  CB  . PHE C 1 255  ? -8.240   43.001  52.424  1.00 141.54 ? 255  PHE B CB  1 
ATOM   16276 C  CG  . PHE C 1 255  ? -8.761   43.935  53.460  1.00 138.75 ? 255  PHE B CG  1 
ATOM   16277 C  CD1 . PHE C 1 255  ? -8.058   45.081  53.789  1.00 138.13 ? 255  PHE B CD1 1 
ATOM   16278 C  CD2 . PHE C 1 255  ? -9.960   43.673  54.101  1.00 137.08 ? 255  PHE B CD2 1 
ATOM   16279 C  CE1 . PHE C 1 255  ? -8.537   45.941  54.729  1.00 137.03 ? 255  PHE B CE1 1 
ATOM   16280 C  CE2 . PHE C 1 255  ? -10.449  44.540  55.047  1.00 135.52 ? 255  PHE B CE2 1 
ATOM   16281 C  CZ  . PHE C 1 255  ? -9.739   45.673  55.358  1.00 136.18 ? 255  PHE B CZ  1 
ATOM   16282 N  N   . TYR C 1 256  ? -8.749   40.893  49.900  1.00 157.90 ? 256  TYR B N   1 
ATOM   16283 C  CA  . TYR C 1 256  ? -8.074   40.059  48.904  1.00 169.35 ? 256  TYR B CA  1 
ATOM   16284 C  C   . TYR C 1 256  ? -8.673   40.173  47.496  1.00 180.46 ? 256  TYR B C   1 
ATOM   16285 O  O   . TYR C 1 256  ? -8.716   39.194  46.751  1.00 186.69 ? 256  TYR B O   1 
ATOM   16286 C  CB  . TYR C 1 256  ? -7.934   38.589  49.362  1.00 165.89 ? 256  TYR B CB  1 
ATOM   16287 C  CG  . TYR C 1 256  ? -9.120   37.926  50.070  1.00 160.89 ? 256  TYR B CG  1 
ATOM   16288 C  CD1 . TYR C 1 256  ? -9.946   37.026  49.399  1.00 159.13 ? 256  TYR B CD1 1 
ATOM   16289 C  CD2 . TYR C 1 256  ? -9.369   38.139  51.420  1.00 158.68 ? 256  TYR B CD2 1 
ATOM   16290 C  CE1 . TYR C 1 256  ? -11.009  36.391  50.048  1.00 156.72 ? 256  TYR B CE1 1 
ATOM   16291 C  CE2 . TYR C 1 256  ? -10.426  37.508  52.072  1.00 156.26 ? 256  TYR B CE2 1 
ATOM   16292 C  CZ  . TYR C 1 256  ? -11.241  36.641  51.385  1.00 154.55 ? 256  TYR B CZ  1 
ATOM   16293 O  OH  . TYR C 1 256  ? -12.289  36.021  52.035  1.00 152.42 ? 256  TYR B OH  1 
ATOM   16294 N  N   . ASN C 1 257  ? -9.123   41.380  47.148  1.00 185.88 ? 257  ASN B N   1 
ATOM   16295 C  CA  . ASN C 1 257  ? -9.732   41.699  45.845  1.00 190.25 ? 257  ASN B CA  1 
ATOM   16296 C  C   . ASN C 1 257  ? -10.853  40.767  45.371  1.00 185.66 ? 257  ASN B C   1 
ATOM   16297 O  O   . ASN C 1 257  ? -10.945  40.435  44.193  1.00 184.92 ? 257  ASN B O   1 
ATOM   16298 C  CB  . ASN C 1 257  ? -8.667   41.905  44.753  1.00 202.68 ? 257  ASN B CB  1 
ATOM   16299 C  CG  . ASN C 1 257  ? -7.733   40.711  44.597  1.00 215.33 ? 257  ASN B CG  1 
ATOM   16300 O  OD1 . ASN C 1 257  ? -6.888   40.456  45.457  1.00 220.94 ? 257  ASN B OD1 1 
ATOM   16301 N  ND2 . ASN C 1 257  ? -7.867   39.990  43.482  1.00 219.03 ? 257  ASN B ND2 1 
ATOM   16302 N  N   . LYS C 1 258  ? -11.719  40.376  46.294  1.00 183.68 ? 258  LYS B N   1 
ATOM   16303 C  CA  . LYS C 1 258  ? -12.745  39.397  45.998  1.00 180.81 ? 258  LYS B CA  1 
ATOM   16304 C  C   . LYS C 1 258  ? -13.996  39.670  46.801  1.00 174.91 ? 258  LYS B C   1 
ATOM   16305 O  O   . LYS C 1 258  ? -14.033  39.425  48.001  1.00 175.02 ? 258  LYS B O   1 
ATOM   16306 C  CB  . LYS C 1 258  ? -12.229  37.999  46.312  1.00 188.54 ? 258  LYS B CB  1 
ATOM   16307 C  CG  . LYS C 1 258  ? -11.943  37.187  45.075  1.00 193.52 ? 258  LYS B CG  1 
ATOM   16308 C  CD  . LYS C 1 258  ? -13.229  37.060  44.268  1.00 194.94 ? 258  LYS B CD  1 
ATOM   16309 C  CE  . LYS C 1 258  ? -13.045  36.310  42.958  1.00 198.41 ? 258  LYS B CE  1 
ATOM   16310 N  NZ  . LYS C 1 258  ? -14.281  36.408  42.128  1.00 197.55 ? 258  LYS B NZ  1 
ATOM   16311 N  N   . VAL C 1 259  ? -15.030  40.155  46.128  1.00 166.38 ? 259  VAL B N   1 
ATOM   16312 C  CA  . VAL C 1 259  ? -16.218  40.664  46.810  1.00 160.02 ? 259  VAL B CA  1 
ATOM   16313 C  C   . VAL C 1 259  ? -16.896  39.647  47.716  1.00 155.66 ? 259  VAL B C   1 
ATOM   16314 O  O   . VAL C 1 259  ? -16.822  38.442  47.486  1.00 156.20 ? 259  VAL B O   1 
ATOM   16315 C  CB  . VAL C 1 259  ? -17.273  41.225  45.817  1.00 152.79 ? 259  VAL B CB  1 
ATOM   16316 C  CG1 . VAL C 1 259  ? -16.605  42.035  44.700  1.00 152.14 ? 259  VAL B CG1 1 
ATOM   16317 C  CG2 . VAL C 1 259  ? -18.126  40.109  45.245  1.00 153.69 ? 259  VAL B CG2 1 
ATOM   16318 N  N   . VAL C 1 260  ? -17.547  40.150  48.756  1.00 153.74 ? 260  VAL B N   1 
ATOM   16319 C  CA  . VAL C 1 260  ? -18.401  39.322  49.584  1.00 155.18 ? 260  VAL B CA  1 
ATOM   16320 C  C   . VAL C 1 260  ? -19.401  38.631  48.680  1.00 157.35 ? 260  VAL B C   1 
ATOM   16321 O  O   . VAL C 1 260  ? -19.706  39.149  47.619  1.00 156.48 ? 260  VAL B O   1 
ATOM   16322 C  CB  . VAL C 1 260  ? -19.165  40.189  50.576  1.00 151.61 ? 260  VAL B CB  1 
ATOM   16323 C  CG1 . VAL C 1 260  ? -20.207  39.358  51.315  1.00 152.70 ? 260  VAL B CG1 1 
ATOM   16324 C  CG2 . VAL C 1 260  ? -18.191  40.840  51.532  1.00 151.32 ? 260  VAL B CG2 1 
ATOM   16325 N  N   . THR C 1 261  ? -19.897  37.460  49.067  1.00 162.16 ? 261  THR B N   1 
ATOM   16326 C  CA  . THR C 1 261  ? -20.956  36.831  48.287  1.00 165.26 ? 261  THR B CA  1 
ATOM   16327 C  C   . THR C 1 261  ? -22.306  37.007  48.966  1.00 167.31 ? 261  THR B C   1 
ATOM   16328 O  O   . THR C 1 261  ? -22.927  38.052  48.847  1.00 166.94 ? 261  THR B O   1 
ATOM   16329 C  CB  . THR C 1 261  ? -20.685  35.351  48.009  1.00 170.24 ? 261  THR B CB  1 
ATOM   16330 O  OG1 . THR C 1 261  ? -19.554  35.224  47.137  1.00 171.84 ? 261  THR B OG1 1 
ATOM   16331 C  CG2 . THR C 1 261  ? -21.883  34.728  47.332  1.00 171.19 ? 261  THR B CG2 1 
ATOM   16332 N  N   . GLU C 1 262  ? -22.771  35.995  49.679  1.00 170.98 ? 262  GLU B N   1 
ATOM   16333 C  CA  . GLU C 1 262  ? -23.956  36.191  50.487  1.00 174.96 ? 262  GLU B CA  1 
ATOM   16334 C  C   . GLU C 1 262  ? -23.502  36.951  51.720  1.00 174.07 ? 262  GLU B C   1 
ATOM   16335 O  O   . GLU C 1 262  ? -22.352  36.824  52.150  1.00 172.79 ? 262  GLU B O   1 
ATOM   16336 C  CB  . GLU C 1 262  ? -24.594  34.858  50.876  1.00 184.89 ? 262  GLU B CB  1 
ATOM   16337 C  CG  . GLU C 1 262  ? -25.862  34.996  51.717  1.00 192.54 ? 262  GLU B CG  1 
ATOM   16338 C  CD  . GLU C 1 262  ? -26.390  33.655  52.208  1.00 202.07 ? 262  GLU B CD  1 
ATOM   16339 O  OE1 . GLU C 1 262  ? -26.673  33.524  53.421  1.00 205.97 ? 262  GLU B OE1 1 
ATOM   16340 O  OE2 . GLU C 1 262  ? -26.513  32.728  51.379  1.00 205.90 ? 262  GLU B OE2 1 
ATOM   16341 N  N   . ALA C 1 263  ? -24.400  37.751  52.277  1.00 173.54 ? 263  ALA B N   1 
ATOM   16342 C  CA  . ALA C 1 263  ? -24.105  38.489  53.488  1.00 174.66 ? 263  ALA B CA  1 
ATOM   16343 C  C   . ALA C 1 263  ? -25.416  38.919  54.083  1.00 171.32 ? 263  ALA B C   1 
ATOM   16344 O  O   . ALA C 1 263  ? -26.423  38.985  53.388  1.00 172.53 ? 263  ALA B O   1 
ATOM   16345 C  CB  . ALA C 1 263  ? -23.252  39.686  53.181  1.00 174.46 ? 263  ALA B CB  1 
ATOM   16346 N  N   . ASP C 1 264  ? -25.414  39.180  55.380  1.00 169.12 ? 264  ASP B N   1 
ATOM   16347 C  CA  . ASP C 1 264  ? -26.610  39.685  56.036  1.00 169.16 ? 264  ASP B CA  1 
ATOM   16348 C  C   . ASP C 1 264  ? -26.432  41.194  56.317  1.00 165.93 ? 264  ASP B C   1 
ATOM   16349 O  O   . ASP C 1 264  ? -25.500  41.579  57.029  1.00 163.63 ? 264  ASP B O   1 
ATOM   16350 C  CB  . ASP C 1 264  ? -26.894  38.881  57.320  1.00 176.10 ? 264  ASP B CB  1 
ATOM   16351 C  CG  . ASP C 1 264  ? -28.364  38.435  57.431  1.00 184.46 ? 264  ASP B CG  1 
ATOM   16352 O  OD1 . ASP C 1 264  ? -29.227  39.105  56.800  1.00 185.10 ? 264  ASP B OD1 1 
ATOM   16353 O  OD2 . ASP C 1 264  ? -28.651  37.417  58.136  1.00 189.91 ? 264  ASP B OD2 1 
ATOM   16354 N  N   . VAL C 1 265  ? -27.300  42.038  55.734  1.00 166.07 ? 265  VAL B N   1 
ATOM   16355 C  CA  . VAL C 1 265  ? -27.212  43.504  55.890  1.00 160.34 ? 265  VAL B CA  1 
ATOM   16356 C  C   . VAL C 1 265  ? -28.229  44.094  56.835  1.00 163.79 ? 265  VAL B C   1 
ATOM   16357 O  O   . VAL C 1 265  ? -29.415  43.821  56.706  1.00 166.11 ? 265  VAL B O   1 
ATOM   16358 C  CB  . VAL C 1 265  ? -27.474  44.268  54.605  1.00 150.80 ? 265  VAL B CB  1 
ATOM   16359 C  CG1 . VAL C 1 265  ? -27.220  45.713  54.895  1.00 146.01 ? 265  VAL B CG1 1 
ATOM   16360 C  CG2 . VAL C 1 265  ? -26.591  43.789  53.476  1.00 148.06 ? 265  VAL B CG2 1 
ATOM   16361 N  N   . TYR C 1 266  ? -27.777  44.962  57.733  1.00 164.04 ? 266  TYR B N   1 
ATOM   16362 C  CA  . TYR C 1 266  ? -28.680  45.595  58.691  1.00 167.05 ? 266  TYR B CA  1 
ATOM   16363 C  C   . TYR C 1 266  ? -28.521  47.117  58.773  1.00 162.07 ? 266  TYR B C   1 
ATOM   16364 O  O   . TYR C 1 266  ? -27.658  47.628  59.502  1.00 161.47 ? 266  TYR B O   1 
ATOM   16365 C  CB  . TYR C 1 266  ? -28.482  45.013  60.087  1.00 177.17 ? 266  TYR B CB  1 
ATOM   16366 C  CG  . TYR C 1 266  ? -29.066  43.639  60.280  1.00 189.39 ? 266  TYR B CG  1 
ATOM   16367 C  CD1 . TYR C 1 266  ? -28.559  42.544  59.593  1.00 193.57 ? 266  TYR B CD1 1 
ATOM   16368 C  CD2 . TYR C 1 266  ? -30.105  43.427  61.178  1.00 196.07 ? 266  TYR B CD2 1 
ATOM   16369 C  CE1 . TYR C 1 266  ? -29.079  41.277  59.782  1.00 199.75 ? 266  TYR B CE1 1 
ATOM   16370 C  CE2 . TYR C 1 266  ? -30.634  42.161  61.372  1.00 202.41 ? 266  TYR B CE2 1 
ATOM   16371 C  CZ  . TYR C 1 266  ? -30.116  41.089  60.674  1.00 203.57 ? 266  TYR B CZ  1 
ATOM   16372 O  OH  . TYR C 1 266  ? -30.637  39.827  60.865  1.00 207.26 ? 266  TYR B OH  1 
ATOM   16373 N  N   . ILE C 1 267  ? -29.390  47.835  58.062  1.00 155.11 ? 267  ILE B N   1 
ATOM   16374 C  CA  . ILE C 1 267  ? -29.339  49.287  58.030  1.00 146.85 ? 267  ILE B CA  1 
ATOM   16375 C  C   . ILE C 1 267  ? -30.414  49.979  58.843  1.00 147.87 ? 267  ILE B C   1 
ATOM   16376 O  O   . ILE C 1 267  ? -31.603  49.725  58.663  1.00 150.29 ? 267  ILE B O   1 
ATOM   16377 C  CB  . ILE C 1 267  ? -29.496  49.772  56.636  1.00 139.97 ? 267  ILE B CB  1 
ATOM   16378 C  CG1 . ILE C 1 267  ? -28.515  49.045  55.735  1.00 134.85 ? 267  ILE B CG1 1 
ATOM   16379 C  CG2 . ILE C 1 267  ? -29.251  51.252  56.601  1.00 137.69 ? 267  ILE B CG2 1 
ATOM   16380 C  CD1 . ILE C 1 267  ? -28.768  49.283  54.273  1.00 131.17 ? 267  ILE B CD1 1 
ATOM   16381 N  N   . THR C 1 268  ? -29.982  50.877  59.719  1.00 146.55 ? 268  THR B N   1 
ATOM   16382 C  CA  . THR C 1 268  ? -30.883  51.597  60.605  1.00 148.07 ? 268  THR B CA  1 
ATOM   16383 C  C   . THR C 1 268  ? -30.634  53.077  60.423  1.00 145.66 ? 268  THR B C   1 
ATOM   16384 O  O   . THR C 1 268  ? -29.482  53.503  60.384  1.00 146.46 ? 268  THR B O   1 
ATOM   16385 C  CB  . THR C 1 268  ? -30.579  51.292  62.079  1.00 151.66 ? 268  THR B CB  1 
ATOM   16386 O  OG1 . THR C 1 268  ? -29.167  51.404  62.303  1.00 153.01 ? 268  THR B OG1 1 
ATOM   16387 C  CG2 . THR C 1 268  ? -31.028  49.886  62.448  1.00 155.23 ? 268  THR B CG2 1 
ATOM   16388 N  N   . PHE C 1 269  ? -31.706  53.864  60.330  1.00 144.61 ? 269  PHE B N   1 
ATOM   16389 C  CA  . PHE C 1 269  ? -31.594  55.310  60.104  1.00 139.02 ? 269  PHE B CA  1 
ATOM   16390 C  C   . PHE C 1 269  ? -31.874  56.143  61.321  1.00 133.31 ? 269  PHE B C   1 
ATOM   16391 O  O   . PHE C 1 269  ? -32.247  55.631  62.371  1.00 136.13 ? 269  PHE B O   1 
ATOM   16392 C  CB  . PHE C 1 269  ? -32.560  55.741  59.028  1.00 139.55 ? 269  PHE B CB  1 
ATOM   16393 C  CG  . PHE C 1 269  ? -32.489  54.909  57.822  1.00 138.20 ? 269  PHE B CG  1 
ATOM   16394 C  CD1 . PHE C 1 269  ? -33.495  54.018  57.526  1.00 139.09 ? 269  PHE B CD1 1 
ATOM   16395 C  CD2 . PHE C 1 269  ? -31.395  54.997  56.998  1.00 136.59 ? 269  PHE B CD2 1 
ATOM   16396 C  CE1 . PHE C 1 269  ? -33.419  53.254  56.413  1.00 138.60 ? 269  PHE B CE1 1 
ATOM   16397 C  CE2 . PHE C 1 269  ? -31.309  54.237  55.889  1.00 135.98 ? 269  PHE B CE2 1 
ATOM   16398 C  CZ  . PHE C 1 269  ? -32.320  53.360  55.587  1.00 137.34 ? 269  PHE B CZ  1 
ATOM   16399 N  N   . GLY C 1 270  ? -31.720  57.448  61.163  1.00 125.85 ? 270  GLY B N   1 
ATOM   16400 C  CA  . GLY C 1 270  ? -31.969  58.354  62.266  1.00 124.33 ? 270  GLY B CA  1 
ATOM   16401 C  C   . GLY C 1 270  ? -31.771  59.813  61.914  1.00 120.49 ? 270  GLY B C   1 
ATOM   16402 O  O   . GLY C 1 270  ? -31.009  60.128  60.999  1.00 120.94 ? 270  GLY B O   1 
ATOM   16403 N  N   . ILE C 1 271  ? -32.457  60.702  62.633  1.00 113.74 ? 271  ILE B N   1 
ATOM   16404 C  CA  . ILE C 1 271  ? -32.361  62.137  62.382  1.00 104.87 ? 271  ILE B CA  1 
ATOM   16405 C  C   . ILE C 1 271  ? -31.167  62.680  63.102  1.00 107.68 ? 271  ILE B C   1 
ATOM   16406 O  O   . ILE C 1 271  ? -30.405  61.917  63.655  1.00 109.31 ? 271  ILE B O   1 
ATOM   16407 C  CB  . ILE C 1 271  ? -33.576  62.847  62.876  1.00 100.66 ? 271  ILE B CB  1 
ATOM   16408 C  CG1 . ILE C 1 271  ? -34.795  62.007  62.513  1.00 97.56  ? 271  ILE B CG1 1 
ATOM   16409 C  CG2 . ILE C 1 271  ? -33.648  64.233  62.263  1.00 97.92  ? 271  ILE B CG2 1 
ATOM   16410 C  CD1 . ILE C 1 271  ? -34.895  61.690  61.028  1.00 92.11  ? 271  ILE B CD1 1 
ATOM   16411 N  N   . ARG C 1 272  ? -30.992  63.992  63.106  1.00 111.26 ? 272  ARG B N   1 
ATOM   16412 C  CA  . ARG C 1 272  ? -29.779  64.561  63.677  1.00 119.26 ? 272  ARG B CA  1 
ATOM   16413 C  C   . ARG C 1 272  ? -29.778  66.077  63.630  1.00 127.54 ? 272  ARG B C   1 
ATOM   16414 O  O   . ARG C 1 272  ? -29.984  66.673  62.582  1.00 125.65 ? 272  ARG B O   1 
ATOM   16415 C  CB  . ARG C 1 272  ? -28.561  64.033  62.922  1.00 116.03 ? 272  ARG B CB  1 
ATOM   16416 C  CG  . ARG C 1 272  ? -27.222  64.336  63.550  1.00 115.97 ? 272  ARG B CG  1 
ATOM   16417 C  CD  . ARG C 1 272  ? -26.285  63.226  63.169  1.00 114.25 ? 272  ARG B CD  1 
ATOM   16418 N  NE  . ARG C 1 272  ? -24.884  63.580  63.312  1.00 115.89 ? 272  ARG B NE  1 
ATOM   16419 C  CZ  . ARG C 1 272  ? -23.916  62.675  63.440  1.00 117.34 ? 272  ARG B CZ  1 
ATOM   16420 N  NH1 . ARG C 1 272  ? -24.220  61.381  63.465  1.00 117.17 ? 272  ARG B NH1 1 
ATOM   16421 N  NH2 . ARG C 1 272  ? -22.648  63.055  63.559  1.00 118.20 ? 272  ARG B NH2 1 
ATOM   16422 N  N   . GLU C 1 273  ? -29.536  66.701  64.771  1.00 136.55 ? 273  GLU B N   1 
ATOM   16423 C  CA  . GLU C 1 273  ? -29.460  68.146  64.810  1.00 143.78 ? 273  GLU B CA  1 
ATOM   16424 C  C   . GLU C 1 273  ? -28.287  68.637  63.970  1.00 142.78 ? 273  GLU B C   1 
ATOM   16425 O  O   . GLU C 1 273  ? -28.445  69.518  63.131  1.00 141.98 ? 273  GLU B O   1 
ATOM   16426 C  CB  . GLU C 1 273  ? -29.336  68.653  66.255  1.00 154.14 ? 273  GLU B CB  1 
ATOM   16427 C  CG  . GLU C 1 273  ? -30.663  69.043  66.903  1.00 160.37 ? 273  GLU B CG  1 
ATOM   16428 C  CD  . GLU C 1 273  ? -31.614  69.726  65.926  1.00 160.82 ? 273  GLU B CD  1 
ATOM   16429 O  OE1 . GLU C 1 273  ? -31.228  70.745  65.304  1.00 159.70 ? 273  GLU B OE1 1 
ATOM   16430 O  OE2 . GLU C 1 273  ? -32.752  69.229  65.777  1.00 161.61 ? 273  GLU B OE2 1 
ATOM   16431 N  N   . ASP C 1 274  ? -27.115  68.051  64.192  1.00 144.03 ? 274  ASP B N   1 
ATOM   16432 C  CA  . ASP C 1 274  ? -25.879  68.540  63.581  1.00 144.34 ? 274  ASP B CA  1 
ATOM   16433 C  C   . ASP C 1 274  ? -24.791  67.478  63.504  1.00 144.29 ? 274  ASP B C   1 
ATOM   16434 O  O   . ASP C 1 274  ? -25.039  66.286  63.707  1.00 143.28 ? 274  ASP B O   1 
ATOM   16435 C  CB  . ASP C 1 274  ? -25.343  69.796  64.313  1.00 146.80 ? 274  ASP B CB  1 
ATOM   16436 C  CG  . ASP C 1 274  ? -25.157  69.598  65.849  1.00 181.47 ? 274  ASP B CG  1 
ATOM   16437 O  OD1 . ASP C 1 274  ? -24.069  69.958  66.376  1.00 183.65 ? 274  ASP B OD1 1 
ATOM   16438 O  OD2 . ASP C 1 274  ? -26.094  69.118  66.540  1.00 182.59 ? 274  ASP B OD2 1 
ATOM   16439 N  N   . LEU C 1 275  ? -23.579  67.917  63.203  1.00 147.61 ? 275  LEU B N   1 
ATOM   16440 C  CA  . LEU C 1 275  ? -22.447  67.006  63.222  1.00 151.73 ? 275  LEU B CA  1 
ATOM   16441 C  C   . LEU C 1 275  ? -21.459  67.234  64.393  1.00 162.34 ? 275  LEU B C   1 
ATOM   16442 O  O   . LEU C 1 275  ? -20.317  66.781  64.345  1.00 163.80 ? 275  LEU B O   1 
ATOM   16443 C  CB  . LEU C 1 275  ? -21.755  66.980  61.853  1.00 145.60 ? 275  LEU B CB  1 
ATOM   16444 C  CG  . LEU C 1 275  ? -22.639  66.427  60.728  1.00 138.89 ? 275  LEU B CG  1 
ATOM   16445 C  CD1 . LEU C 1 275  ? -21.950  66.617  59.415  1.00 136.35 ? 275  LEU B CD1 1 
ATOM   16446 C  CD2 . LEU C 1 275  ? -22.983  64.958  60.927  1.00 137.35 ? 275  LEU B CD2 1 
ATOM   16447 N  N   . LYS C 1 276  ? -21.896  67.944  65.433  1.00 170.73 ? 276  LYS B N   1 
ATOM   16448 C  CA  . LYS C 1 276  ? -21.171  67.986  66.708  1.00 179.19 ? 276  LYS B CA  1 
ATOM   16449 C  C   . LYS C 1 276  ? -22.008  67.283  67.782  1.00 190.61 ? 276  LYS B C   1 
ATOM   16450 O  O   . LYS C 1 276  ? -21.691  67.317  68.971  1.00 197.19 ? 276  LYS B O   1 
ATOM   16451 C  CB  . LYS C 1 276  ? -20.837  69.429  67.122  1.00 175.97 ? 276  LYS B CB  1 
ATOM   16452 C  CG  . LYS C 1 276  ? -19.993  69.547  68.406  1.00 174.40 ? 276  LYS B CG  1 
ATOM   16453 C  CD  . LYS C 1 276  ? -19.572  70.994  68.720  1.00 170.11 ? 276  LYS B CD  1 
ATOM   16454 C  CE  . LYS C 1 276  ? -20.725  71.851  69.237  1.00 164.52 ? 276  LYS B CE  1 
ATOM   16455 N  NZ  . LYS C 1 276  ? -20.955  71.664  70.685  1.00 165.60 ? 276  LYS B NZ  1 
ATOM   16456 N  N   . ASP C 1 277  ? -23.090  66.654  67.333  1.00 194.42 ? 277  ASP B N   1 
ATOM   16457 C  CA  . ASP C 1 277  ? -24.051  65.972  68.198  1.00 204.12 ? 277  ASP B CA  1 
ATOM   16458 C  C   . ASP C 1 277  ? -23.753  64.473  68.224  1.00 206.84 ? 277  ASP B C   1 
ATOM   16459 O  O   . ASP C 1 277  ? -24.038  63.756  67.267  1.00 205.42 ? 277  ASP B O   1 
ATOM   16460 C  CB  . ASP C 1 277  ? -25.481  66.250  67.688  1.00 208.60 ? 277  ASP B CB  1 
ATOM   16461 C  CG  . ASP C 1 277  ? -26.572  65.569  68.514  1.00 217.63 ? 277  ASP B CG  1 
ATOM   16462 O  OD1 . ASP C 1 277  ? -26.275  64.991  69.580  1.00 224.21 ? 277  ASP B OD1 1 
ATOM   16463 O  OD2 . ASP C 1 277  ? -27.746  65.616  68.080  1.00 218.22 ? 277  ASP B OD2 1 
ATOM   16464 N  N   . ASP C 1 278  ? -23.166  64.011  69.324  1.00 211.27 ? 278  ASP B N   1 
ATOM   16465 C  CA  . ASP C 1 278  ? -22.866  62.593  69.506  1.00 210.18 ? 278  ASP B CA  1 
ATOM   16466 C  C   . ASP C 1 278  ? -24.131  61.743  69.477  1.00 206.62 ? 278  ASP B C   1 
ATOM   16467 O  O   . ASP C 1 278  ? -24.059  60.524  69.336  1.00 205.70 ? 278  ASP B O   1 
ATOM   16468 C  CB  . ASP C 1 278  ? -22.048  62.336  70.798  1.00 246.71 ? 278  ASP B CB  1 
ATOM   16469 C  CG  . ASP C 1 278  ? -22.537  63.154  72.021  1.00 248.24 ? 278  ASP B CG  1 
ATOM   16470 O  OD1 . ASP C 1 278  ? -23.686  63.650  72.021  1.00 246.10 ? 278  ASP B OD1 1 
ATOM   16471 O  OD2 . ASP C 1 278  ? -21.758  63.289  72.999  1.00 251.13 ? 278  ASP B OD2 1 
ATOM   16472 N  N   . GLN C 1 279  ? -25.286  62.401  69.583  1.00 202.05 ? 279  GLN B N   1 
ATOM   16473 C  CA  . GLN C 1 279  ? -26.557  61.702  69.725  1.00 197.99 ? 279  GLN B CA  1 
ATOM   16474 C  C   . GLN C 1 279  ? -27.579  62.086  68.687  1.00 185.17 ? 279  GLN B C   1 
ATOM   16475 O  O   . GLN C 1 279  ? -27.665  63.225  68.248  1.00 180.83 ? 279  GLN B O   1 
ATOM   16476 C  CB  . GLN C 1 279  ? -27.176  61.929  71.102  1.00 206.10 ? 279  GLN B CB  1 
ATOM   16477 C  CG  . GLN C 1 279  ? -28.454  61.119  71.321  1.00 210.00 ? 279  GLN B CG  1 
ATOM   16478 C  CD  . GLN C 1 279  ? -28.219  59.608  71.241  1.00 212.84 ? 279  GLN B CD  1 
ATOM   16479 O  OE1 . GLN C 1 279  ? -28.749  58.930  70.358  1.00 210.76 ? 279  GLN B OE1 1 
ATOM   16480 N  NE2 . GLN C 1 279  ? -27.419  59.081  72.167  1.00 217.04 ? 279  GLN B NE2 1 
ATOM   16481 N  N   . LYS C 1 280  ? -28.389  61.109  68.334  1.00 179.73 ? 280  LYS B N   1 
ATOM   16482 C  CA  . LYS C 1 280  ? -29.321  61.272  67.255  1.00 171.64 ? 280  LYS B CA  1 
ATOM   16483 C  C   . LYS C 1 280  ? -30.456  60.275  67.413  1.00 171.29 ? 280  LYS B C   1 
ATOM   16484 O  O   . LYS C 1 280  ? -30.237  59.079  67.571  1.00 174.13 ? 280  LYS B O   1 
ATOM   16485 C  CB  . LYS C 1 280  ? -28.596  61.088  65.917  1.00 163.81 ? 280  LYS B CB  1 
ATOM   16486 C  CG  . LYS C 1 280  ? -27.839  59.770  65.746  1.00 158.98 ? 280  LYS B CG  1 
ATOM   16487 C  CD  . LYS C 1 280  ? -26.332  59.870  66.008  1.00 157.23 ? 280  LYS B CD  1 
ATOM   16488 C  CE  . LYS C 1 280  ? -25.669  58.487  65.862  1.00 155.78 ? 280  LYS B CE  1 
ATOM   16489 N  NZ  . LYS C 1 280  ? -24.179  58.455  66.024  1.00 156.02 ? 280  LYS B NZ  1 
ATOM   16490 N  N   . GLU C 1 281  ? -31.675  60.784  67.379  1.00 169.42 ? 281  GLU B N   1 
ATOM   16491 C  CA  . GLU C 1 281  ? -32.851  59.962  67.589  1.00 170.76 ? 281  GLU B CA  1 
ATOM   16492 C  C   . GLU C 1 281  ? -33.063  58.972  66.456  1.00 162.81 ? 281  GLU B C   1 
ATOM   16493 O  O   . GLU C 1 281  ? -33.640  59.322  65.431  1.00 157.06 ? 281  GLU B O   1 
ATOM   16494 C  CB  . GLU C 1 281  ? -34.076  60.865  67.724  1.00 180.13 ? 281  GLU B CB  1 
ATOM   16495 C  CG  . GLU C 1 281  ? -33.859  62.060  68.657  1.00 192.73 ? 281  GLU B CG  1 
ATOM   16496 C  CD  . GLU C 1 281  ? -33.267  61.674  70.024  1.00 207.01 ? 281  GLU B CD  1 
ATOM   16497 O  OE1 . GLU C 1 281  ? -33.161  60.462  70.340  1.00 211.68 ? 281  GLU B OE1 1 
ATOM   16498 O  OE2 . GLU C 1 281  ? -32.904  62.595  70.791  1.00 212.84 ? 281  GLU B OE2 1 
ATOM   16499 N  N   . MET C 1 282  ? -32.622  57.733  66.642  1.00 162.35 ? 282  MET B N   1 
ATOM   16500 C  CA  . MET C 1 282  ? -32.852  56.712  65.632  1.00 160.70 ? 282  MET B CA  1 
ATOM   16501 C  C   . MET C 1 282  ? -34.325  56.600  65.320  1.00 162.48 ? 282  MET B C   1 
ATOM   16502 O  O   . MET C 1 282  ? -35.127  57.386  65.797  1.00 163.89 ? 282  MET B O   1 
ATOM   16503 C  CB  . MET C 1 282  ? -32.347  55.359  66.094  1.00 162.51 ? 282  MET B CB  1 
ATOM   16504 C  CG  . MET C 1 282  ? -30.842  55.235  66.206  1.00 162.50 ? 282  MET B CG  1 
ATOM   16505 S  SD  . MET C 1 282  ? -29.973  55.602  64.674  1.00 165.77 ? 282  MET B SD  1 
ATOM   16506 C  CE  . MET C 1 282  ? -29.782  57.373  64.885  1.00 122.22 ? 282  MET B CE  1 
ATOM   16507 N  N   . MET C 1 283  ? -34.689  55.616  64.517  1.00 164.51 ? 283  MET B N   1 
ATOM   16508 C  CA  . MET C 1 283  ? -36.066  55.506  64.076  1.00 171.93 ? 283  MET B CA  1 
ATOM   16509 C  C   . MET C 1 283  ? -36.397  54.044  63.831  1.00 182.71 ? 283  MET B C   1 
ATOM   16510 O  O   . MET C 1 283  ? -35.676  53.355  63.111  1.00 183.02 ? 283  MET B O   1 
ATOM   16511 C  CB  . MET C 1 283  ? -36.295  56.312  62.781  1.00 167.01 ? 283  MET B CB  1 
ATOM   16512 C  CG  . MET C 1 283  ? -36.014  57.835  62.859  1.00 180.02 ? 283  MET B CG  1 
ATOM   16513 S  SD  . MET C 1 283  ? -35.959  58.717  61.250  1.00 114.30 ? 283  MET B SD  1 
ATOM   16514 C  CE  . MET C 1 283  ? -34.569  57.925  60.459  1.00 109.55 ? 283  MET B CE  1 
ATOM   16515 N  N   . GLN C 1 284  ? -37.488  53.576  64.429  1.00 194.34 ? 284  GLN B N   1 
ATOM   16516 C  CA  . GLN C 1 284  ? -37.985  52.220  64.226  1.00 202.42 ? 284  GLN B CA  1 
ATOM   16517 C  C   . GLN C 1 284  ? -38.188  51.918  62.755  1.00 205.01 ? 284  GLN B C   1 
ATOM   16518 O  O   . GLN C 1 284  ? -38.048  52.792  61.893  1.00 203.65 ? 284  GLN B O   1 
ATOM   16519 C  CB  . GLN C 1 284  ? -39.332  52.060  64.916  1.00 206.72 ? 284  GLN B CB  1 
ATOM   16520 C  CG  . GLN C 1 284  ? -40.410  52.966  64.341  1.00 205.29 ? 284  GLN B CG  1 
ATOM   16521 C  CD  . GLN C 1 284  ? -40.260  54.408  64.796  1.00 204.39 ? 284  GLN B CD  1 
ATOM   16522 O  OE1 . GLN C 1 284  ? -39.294  55.088  64.456  1.00 201.60 ? 284  GLN B OE1 1 
ATOM   16523 N  NE2 . GLN C 1 284  ? -41.225  54.882  65.567  1.00 207.16 ? 284  GLN B NE2 1 
ATOM   16524 N  N   . THR C 1 285  ? -38.547  50.674  62.471  1.00 208.50 ? 285  THR B N   1 
ATOM   16525 C  CA  . THR C 1 285  ? -38.862  50.300  61.108  1.00 208.71 ? 285  THR B CA  1 
ATOM   16526 C  C   . THR C 1 285  ? -37.762  50.862  60.198  1.00 204.30 ? 285  THR B C   1 
ATOM   16527 O  O   . THR C 1 285  ? -38.021  51.584  59.226  1.00 200.60 ? 285  THR B O   1 
ATOM   16528 C  CB  . THR C 1 285  ? -40.263  50.809  60.709  1.00 211.97 ? 285  THR B CB  1 
ATOM   16529 O  OG1 . THR C 1 285  ? -41.126  50.771  61.854  1.00 216.07 ? 285  THR B OG1 1 
ATOM   16530 C  CG2 . THR C 1 285  ? -40.857  49.949  59.602  1.00 213.60 ? 285  THR B CG2 1 
ATOM   16531 N  N   . ALA C 1 286  ? -36.522  50.566  60.582  1.00 202.50 ? 286  ALA B N   1 
ATOM   16532 C  CA  . ALA C 1 286  ? -35.362  50.780  59.729  1.00 197.25 ? 286  ALA B CA  1 
ATOM   16533 C  C   . ALA C 1 286  ? -35.021  49.463  59.035  1.00 194.69 ? 286  ALA B C   1 
ATOM   16534 O  O   . ALA C 1 286  ? -34.482  48.543  59.653  1.00 192.69 ? 286  ALA B O   1 
ATOM   16535 C  CB  . ALA C 1 286  ? -34.188  51.271  60.540  1.00 197.19 ? 286  ALA B CB  1 
ATOM   16536 N  N   . MET C 1 287  ? -35.335  49.400  57.742  1.00 193.17 ? 287  MET B N   1 
ATOM   16537 C  CA  . MET C 1 287  ? -35.257  48.177  56.948  1.00 191.11 ? 287  MET B CA  1 
ATOM   16538 C  C   . MET C 1 287  ? -34.198  47.196  57.387  1.00 192.33 ? 287  MET B C   1 
ATOM   16539 O  O   . MET C 1 287  ? -33.072  47.569  57.712  1.00 190.85 ? 287  MET B O   1 
ATOM   16540 C  CB  . MET C 1 287  ? -35.037  48.504  55.478  1.00 185.57 ? 287  MET B CB  1 
ATOM   16541 C  CG  . MET C 1 287  ? -36.297  48.795  54.721  1.00 183.47 ? 287  MET B CG  1 
ATOM   16542 S  SD  . MET C 1 287  ? -35.897  49.266  53.038  1.00 221.87 ? 287  MET B SD  1 
ATOM   16543 C  CE  . MET C 1 287  ? -35.109  50.842  53.338  1.00 182.94 ? 287  MET B CE  1 
ATOM   16544 N  N   . GLN C 1 288  ? -34.589  45.929  57.381  1.00 196.54 ? 288  GLN B N   1 
ATOM   16545 C  CA  . GLN C 1 288  ? -33.687  44.833  57.679  1.00 202.15 ? 288  GLN B CA  1 
ATOM   16546 C  C   . GLN C 1 288  ? -33.448  43.983  56.443  1.00 202.35 ? 288  GLN B C   1 
ATOM   16547 O  O   . GLN C 1 288  ? -34.297  43.879  55.563  1.00 201.51 ? 288  GLN B O   1 
ATOM   16548 C  CB  . GLN C 1 288  ? -34.221  43.975  58.841  1.00 210.16 ? 288  GLN B CB  1 
ATOM   16549 C  CG  . GLN C 1 288  ? -35.705  43.601  58.744  1.00 217.43 ? 288  GLN B CG  1 
ATOM   16550 C  CD  . GLN C 1 288  ? -36.260  42.921  60.006  1.00 226.48 ? 288  GLN B CD  1 
ATOM   16551 O  OE1 . GLN C 1 288  ? -35.534  42.252  60.748  1.00 229.95 ? 288  GLN B OE1 1 
ATOM   16552 N  NE2 . GLN C 1 288  ? -37.562  43.081  60.235  1.00 230.67 ? 288  GLN B NE2 1 
ATOM   16553 N  N   . ASN C 1 289  ? -32.263  43.399  56.381  1.00 205.06 ? 289  ASN B N   1 
ATOM   16554 C  CA  . ASN C 1 289  ? -31.933  42.419  55.362  1.00 207.96 ? 289  ASN B CA  1 
ATOM   16555 C  C   . ASN C 1 289  ? -32.424  42.761  53.969  1.00 200.86 ? 289  ASN B C   1 
ATOM   16556 O  O   . ASN C 1 289  ? -33.611  42.693  53.675  1.00 198.62 ? 289  ASN B O   1 
ATOM   16557 C  CB  . ASN C 1 289  ? -32.495  41.046  55.742  1.00 217.34 ? 289  ASN B CB  1 
ATOM   16558 C  CG  . ASN C 1 289  ? -32.315  40.718  57.213  1.00 224.53 ? 289  ASN B CG  1 
ATOM   16559 O  OD1 . ASN C 1 289  ? -31.579  41.396  57.928  1.00 225.99 ? 289  ASN B OD1 1 
ATOM   16560 N  ND2 . ASN C 1 289  ? -32.993  39.667  57.672  1.00 228.64 ? 289  ASN B ND2 1 
ATOM   16561 N  N   . THR C 1 290  ? -31.497  43.152  53.119  1.00 197.58 ? 290  THR B N   1 
ATOM   16562 C  CA  . THR C 1 290  ? -31.649  42.934  51.695  1.00 195.00 ? 290  THR B CA  1 
ATOM   16563 C  C   . THR C 1 290  ? -30.345  42.242  51.413  1.00 191.00 ? 290  THR B C   1 
ATOM   16564 O  O   . THR C 1 290  ? -29.529  42.700  50.616  1.00 191.99 ? 290  THR B O   1 
ATOM   16565 C  CB  . THR C 1 290  ? -31.850  44.232  50.858  1.00 162.37 ? 290  THR B CB  1 
ATOM   16566 O  OG1 . THR C 1 290  ? -33.246  44.545  50.803  1.00 162.75 ? 290  THR B OG1 1 
ATOM   16567 C  CG2 . THR C 1 290  ? -31.361  44.055  49.424  1.00 160.77 ? 290  THR B CG2 1 
ATOM   16568 N  N   . MET C 1 291  ? -30.149  41.151  52.148  1.00 187.18 ? 291  MET B N   1 
ATOM   16569 C  CA  . MET C 1 291  ? -28.925  40.375  52.102  1.00 183.12 ? 291  MET B CA  1 
ATOM   16570 C  C   . MET C 1 291  ? -28.031  40.829  50.957  1.00 176.28 ? 291  MET B C   1 
ATOM   16571 O  O   . MET C 1 291  ? -28.405  40.729  49.785  1.00 175.33 ? 291  MET B O   1 
ATOM   16572 C  CB  . MET C 1 291  ? -29.234  38.890  51.907  1.00 187.55 ? 291  MET B CB  1 
ATOM   16573 C  CG  . MET C 1 291  ? -30.209  38.265  52.886  1.00 191.02 ? 291  MET B CG  1 
ATOM   16574 S  SD  . MET C 1 291  ? -30.405  36.517  52.463  1.00 217.79 ? 291  MET B SD  1 
ATOM   16575 C  CE  . MET C 1 291  ? -30.717  36.640  50.702  1.00 212.85 ? 291  MET B CE  1 
ATOM   16576 N  N   . LEU C 1 292  ? -26.849  41.327  51.304  1.00 170.50 ? 292  LEU B N   1 
ATOM   16577 C  CA  . LEU C 1 292  ? -25.839  41.650  50.311  1.00 163.63 ? 292  LEU B CA  1 
ATOM   16578 C  C   . LEU C 1 292  ? -25.741  40.458  49.378  1.00 159.52 ? 292  LEU B C   1 
ATOM   16579 O  O   . LEU C 1 292  ? -25.895  39.313  49.795  1.00 161.27 ? 292  LEU B O   1 
ATOM   16580 C  CB  . LEU C 1 292  ? -24.491  41.901  50.992  1.00 163.89 ? 292  LEU B CB  1 
ATOM   16581 C  CG  . LEU C 1 292  ? -23.420  42.737  50.287  1.00 161.76 ? 292  LEU B CG  1 
ATOM   16582 C  CD1 . LEU C 1 292  ? -22.901  42.065  49.029  1.00 161.98 ? 292  LEU B CD1 1 
ATOM   16583 C  CD2 . LEU C 1 292  ? -23.962  44.110  49.977  1.00 159.21 ? 292  LEU B CD2 1 
ATOM   16584 N  N   . ILE C 1 293  ? -25.482  40.720  48.111  1.00 152.67 ? 293  ILE B N   1 
ATOM   16585 C  CA  . ILE C 1 293  ? -25.478  39.651  47.145  1.00 148.81 ? 293  ILE B CA  1 
ATOM   16586 C  C   . ILE C 1 293  ? -24.531  40.006  46.028  1.00 144.85 ? 293  ILE B C   1 
ATOM   16587 O  O   . ILE C 1 293  ? -24.773  40.919  45.256  1.00 143.86 ? 293  ILE B O   1 
ATOM   16588 C  CB  . ILE C 1 293  ? -26.894  39.407  46.624  1.00 147.19 ? 293  ILE B CB  1 
ATOM   16589 C  CG1 . ILE C 1 293  ? -27.636  38.447  47.568  1.00 146.92 ? 293  ILE B CG1 1 
ATOM   16590 C  CG2 . ILE C 1 293  ? -26.865  38.900  45.187  1.00 148.69 ? 293  ILE B CG2 1 
ATOM   16591 C  CD1 . ILE C 1 293  ? -29.092  38.192  47.204  1.00 146.29 ? 293  ILE B CD1 1 
ATOM   16592 N  N   . ASN C 1 294  ? -23.424  39.290  45.972  1.00 144.42 ? 294  ASN B N   1 
ATOM   16593 C  CA  . ASN C 1 294  ? -22.389  39.557  44.987  1.00 144.37 ? 294  ASN B CA  1 
ATOM   16594 C  C   . ASN C 1 294  ? -21.722  40.943  45.067  1.00 136.64 ? 294  ASN B C   1 
ATOM   16595 O  O   . ASN C 1 294  ? -21.249  41.491  44.069  1.00 135.08 ? 294  ASN B O   1 
ATOM   16596 C  CB  . ASN C 1 294  ? -22.917  39.301  43.589  1.00 151.01 ? 294  ASN B CB  1 
ATOM   16597 C  CG  . ASN C 1 294  ? -21.811  39.223  42.573  1.00 157.35 ? 294  ASN B CG  1 
ATOM   16598 O  OD1 . ASN C 1 294  ? -21.585  40.178  41.827  1.00 158.71 ? 294  ASN B OD1 1 
ATOM   16599 N  ND2 . ASN C 1 294  ? -21.082  38.098  42.559  1.00 160.52 ? 294  ASN B ND2 1 
ATOM   16600 N  N   . GLY C 1 295  ? -21.663  41.492  46.271  1.00 132.42 ? 295  GLY B N   1 
ATOM   16601 C  CA  . GLY C 1 295  ? -20.865  42.671  46.522  1.00 129.03 ? 295  GLY B CA  1 
ATOM   16602 C  C   . GLY C 1 295  ? -21.705  43.919  46.559  1.00 126.22 ? 295  GLY B C   1 
ATOM   16603 O  O   . GLY C 1 295  ? -21.175  45.030  46.704  1.00 124.55 ? 295  GLY B O   1 
ATOM   16604 N  N   . ILE C 1 296  ? -23.019  43.729  46.422  1.00 124.43 ? 296  ILE B N   1 
ATOM   16605 C  CA  . ILE C 1 296  ? -23.978  44.838  46.436  1.00 119.30 ? 296  ILE B CA  1 
ATOM   16606 C  C   . ILE C 1 296  ? -25.319  44.481  47.076  1.00 122.44 ? 296  ILE B C   1 
ATOM   16607 O  O   . ILE C 1 296  ? -25.752  43.326  47.063  1.00 125.25 ? 296  ILE B O   1 
ATOM   16608 C  CB  . ILE C 1 296  ? -24.272  45.400  45.023  1.00 108.84 ? 296  ILE B CB  1 
ATOM   16609 C  CG1 . ILE C 1 296  ? -22.990  45.524  44.200  1.00 106.82 ? 296  ILE B CG1 1 
ATOM   16610 C  CG2 . ILE C 1 296  ? -24.962  46.744  45.130  1.00 102.54 ? 296  ILE B CG2 1 
ATOM   16611 C  CD1 . ILE C 1 296  ? -22.464  46.912  44.110  1.00 104.34 ? 296  ILE B CD1 1 
ATOM   16612 N  N   . ALA C 1 297  ? -25.940  45.497  47.667  1.00 121.82 ? 297  ALA B N   1 
ATOM   16613 C  CA  . ALA C 1 297  ? -27.350  45.486  48.024  1.00 121.48 ? 297  ALA B CA  1 
ATOM   16614 C  C   . ALA C 1 297  ? -27.775  46.937  47.988  1.00 121.90 ? 297  ALA B C   1 
ATOM   16615 O  O   . ALA C 1 297  ? -26.932  47.844  47.952  1.00 122.52 ? 297  ALA B O   1 
ATOM   16616 C  CB  . ALA C 1 297  ? -27.583  44.892  49.382  1.00 120.40 ? 297  ALA B CB  1 
ATOM   16617 N  N   . GLN C 1 298  ? -29.081  47.153  47.987  1.00 123.07 ? 298  GLN B N   1 
ATOM   16618 C  CA  . GLN C 1 298  ? -29.637  48.474  47.777  1.00 121.57 ? 298  GLN B CA  1 
ATOM   16619 C  C   . GLN C 1 298  ? -30.984  48.514  48.470  1.00 120.34 ? 298  GLN B C   1 
ATOM   16620 O  O   . GLN C 1 298  ? -31.634  47.488  48.620  1.00 121.65 ? 298  GLN B O   1 
ATOM   16621 C  CB  . GLN C 1 298  ? -29.821  48.737  46.282  1.00 125.17 ? 298  GLN B CB  1 
ATOM   16622 C  CG  . GLN C 1 298  ? -28.666  49.495  45.622  1.00 130.14 ? 298  GLN B CG  1 
ATOM   16623 C  CD  . GLN C 1 298  ? -29.141  50.540  44.599  1.00 135.67 ? 298  GLN B CD  1 
ATOM   16624 O  OE1 . GLN C 1 298  ? -30.338  50.770  44.440  1.00 138.96 ? 298  GLN B OE1 1 
ATOM   16625 N  NE2 . GLN C 1 298  ? -28.198  51.180  43.915  1.00 136.62 ? 298  GLN B NE2 1 
ATOM   16626 N  N   . VAL C 1 299  ? -31.393  49.685  48.927  1.00 117.89 ? 299  VAL B N   1 
ATOM   16627 C  CA  . VAL C 1 299  ? -32.778  49.883  49.308  1.00 119.90 ? 299  VAL B CA  1 
ATOM   16628 C  C   . VAL C 1 299  ? -32.989  51.341  49.148  1.00 122.54 ? 299  VAL B C   1 
ATOM   16629 O  O   . VAL C 1 299  ? -32.048  52.104  49.344  1.00 126.55 ? 299  VAL B O   1 
ATOM   16630 C  CB  . VAL C 1 299  ? -33.032  49.566  50.762  1.00 120.63 ? 299  VAL B CB  1 
ATOM   16631 C  CG1 . VAL C 1 299  ? -33.272  48.087  50.945  1.00 122.60 ? 299  VAL B CG1 1 
ATOM   16632 C  CG2 . VAL C 1 299  ? -31.880  50.077  51.612  1.00 120.79 ? 299  VAL B CG2 1 
ATOM   16633 N  N   . THR C 1 300  ? -34.204  51.730  48.769  1.00 120.44 ? 300  THR B N   1 
ATOM   16634 C  CA  . THR C 1 300  ? -34.576  53.138  48.745  1.00 119.19 ? 300  THR B CA  1 
ATOM   16635 C  C   . THR C 1 300  ? -35.338  53.475  50.019  1.00 123.00 ? 300  THR B C   1 
ATOM   16636 O  O   . THR C 1 300  ? -36.006  52.624  50.603  1.00 123.69 ? 300  THR B O   1 
ATOM   16637 C  CB  . THR C 1 300  ? -35.354  53.542  47.458  1.00 157.13 ? 300  THR B CB  1 
ATOM   16638 O  OG1 . THR C 1 300  ? -36.317  52.536  47.114  1.00 159.25 ? 300  THR B OG1 1 
ATOM   16639 C  CG2 . THR C 1 300  ? -34.393  53.713  46.289  1.00 156.14 ? 300  THR B CG2 1 
ATOM   16640 N  N   . PHE C 1 301  ? -35.204  54.710  50.469  1.00 128.92 ? 301  PHE B N   1 
ATOM   16641 C  CA  . PHE C 1 301  ? -35.659  55.053  51.803  1.00 137.35 ? 301  PHE B CA  1 
ATOM   16642 C  C   . PHE C 1 301  ? -36.743  56.129  51.714  1.00 147.10 ? 301  PHE B C   1 
ATOM   16643 O  O   . PHE C 1 301  ? -36.453  57.285  51.408  1.00 150.48 ? 301  PHE B O   1 
ATOM   16644 C  CB  . PHE C 1 301  ? -34.428  55.482  52.613  1.00 134.25 ? 301  PHE B CB  1 
ATOM   16645 C  CG  . PHE C 1 301  ? -34.731  56.130  53.926  1.00 131.26 ? 301  PHE B CG  1 
ATOM   16646 C  CD1 . PHE C 1 301  ? -35.466  55.481  54.880  1.00 130.87 ? 301  PHE B CD1 1 
ATOM   16647 C  CD2 . PHE C 1 301  ? -34.232  57.398  54.220  1.00 129.04 ? 301  PHE B CD2 1 
ATOM   16648 C  CE1 . PHE C 1 301  ? -35.721  56.096  56.098  1.00 131.28 ? 301  PHE B CE1 1 
ATOM   16649 C  CE2 . PHE C 1 301  ? -34.491  58.023  55.428  1.00 128.16 ? 301  PHE B CE2 1 
ATOM   16650 C  CZ  . PHE C 1 301  ? -35.235  57.365  56.370  1.00 129.89 ? 301  PHE B CZ  1 
ATOM   16651 N  N   . ASP C 1 302  ? -38.001  55.737  51.928  1.00 151.36 ? 302  ASP B N   1 
ATOM   16652 C  CA  . ASP C 1 302  ? -39.128  56.683  51.905  1.00 153.53 ? 302  ASP B CA  1 
ATOM   16653 C  C   . ASP C 1 302  ? -39.080  57.494  53.198  1.00 152.00 ? 302  ASP B C   1 
ATOM   16654 O  O   . ASP C 1 302  ? -39.507  57.028  54.261  1.00 151.13 ? 302  ASP B O   1 
ATOM   16655 C  CB  . ASP C 1 302  ? -40.477  55.945  51.734  1.00 160.81 ? 302  ASP B CB  1 
ATOM   16656 C  CG  . ASP C 1 302  ? -41.671  56.897  51.499  1.00 168.41 ? 302  ASP B CG  1 
ATOM   16657 O  OD1 . ASP C 1 302  ? -42.680  56.443  50.920  1.00 172.96 ? 302  ASP B OD1 1 
ATOM   16658 O  OD2 . ASP C 1 302  ? -41.628  58.082  51.895  1.00 169.52 ? 302  ASP B OD2 1 
ATOM   16659 N  N   . SER C 1 303  ? -38.527  58.698  53.094  1.00 150.30 ? 303  SER B N   1 
ATOM   16660 C  CA  . SER C 1 303  ? -38.327  59.560  54.241  1.00 150.22 ? 303  SER B CA  1 
ATOM   16661 C  C   . SER C 1 303  ? -39.659  60.027  54.847  1.00 151.30 ? 303  SER B C   1 
ATOM   16662 O  O   . SER C 1 303  ? -39.778  60.238  56.056  1.00 153.91 ? 303  SER B O   1 
ATOM   16663 C  CB  . SER C 1 303  ? -37.450  60.746  53.839  1.00 144.89 ? 303  SER B CB  1 
ATOM   16664 O  OG  . SER C 1 303  ? -36.268  60.307  53.208  1.00 140.26 ? 303  SER B OG  1 
ATOM   16665 N  N   . GLU C 1 304  ? -40.669  60.176  54.001  1.00 149.52 ? 304  GLU B N   1 
ATOM   16666 C  CA  . GLU C 1 304  ? -41.959  60.699  54.445  1.00 147.79 ? 304  GLU B CA  1 
ATOM   16667 C  C   . GLU C 1 304  ? -42.543  59.795  55.508  1.00 145.05 ? 304  GLU B C   1 
ATOM   16668 O  O   . GLU C 1 304  ? -42.787  60.217  56.633  1.00 143.01 ? 304  GLU B O   1 
ATOM   16669 C  CB  . GLU C 1 304  ? -42.922  60.795  53.264  1.00 149.47 ? 304  GLU B CB  1 
ATOM   16670 C  CG  . GLU C 1 304  ? -44.013  61.820  53.431  1.00 152.79 ? 304  GLU B CG  1 
ATOM   16671 C  CD  . GLU C 1 304  ? -45.055  61.655  52.375  1.00 156.16 ? 304  GLU B CD  1 
ATOM   16672 O  OE1 . GLU C 1 304  ? -45.033  60.573  51.742  1.00 158.14 ? 304  GLU B OE1 1 
ATOM   16673 O  OE2 . GLU C 1 304  ? -45.880  62.582  52.182  1.00 156.95 ? 304  GLU B OE2 1 
ATOM   16674 N  N   . THR C 1 305  ? -42.774  58.549  55.116  1.00 147.01 ? 305  THR B N   1 
ATOM   16675 C  CA  . THR C 1 305  ? -43.151  57.487  56.027  1.00 150.24 ? 305  THR B CA  1 
ATOM   16676 C  C   . THR C 1 305  ? -42.250  57.519  57.240  1.00 152.69 ? 305  THR B C   1 
ATOM   16677 O  O   . THR C 1 305  ? -42.659  57.839  58.363  1.00 150.60 ? 305  THR B O   1 
ATOM   16678 C  CB  . THR C 1 305  ? -42.890  56.143  55.337  1.00 149.64 ? 305  THR B CB  1 
ATOM   16679 O  OG1 . THR C 1 305  ? -43.682  56.058  54.147  1.00 149.80 ? 305  THR B OG1 1 
ATOM   16680 C  CG2 . THR C 1 305  ? -43.194  54.975  56.261  1.00 151.46 ? 305  THR B CG2 1 
ATOM   16681 N  N   . ALA C 1 306  ? -40.995  57.213  56.960  1.00 157.05 ? 306  ALA B N   1 
ATOM   16682 C  CA  . ALA C 1 306  ? -39.994  56.893  57.958  1.00 164.18 ? 306  ALA B CA  1 
ATOM   16683 C  C   . ALA C 1 306  ? -39.643  57.990  58.959  1.00 175.45 ? 306  ALA B C   1 
ATOM   16684 O  O   . ALA C 1 306  ? -38.570  57.951  59.557  1.00 173.76 ? 306  ALA B O   1 
ATOM   16685 C  CB  . ALA C 1 306  ? -38.741  56.428  57.257  1.00 162.34 ? 306  ALA B CB  1 
ATOM   16686 N  N   . VAL C 1 307  ? -40.526  58.958  59.158  1.00 184.82 ? 307  VAL B N   1 
ATOM   16687 C  CA  . VAL C 1 307  ? -40.249  60.019  60.119  1.00 200.99 ? 307  VAL B CA  1 
ATOM   16688 C  C   . VAL C 1 307  ? -41.538  60.369  60.835  1.00 218.45 ? 307  VAL B C   1 
ATOM   16689 O  O   . VAL C 1 307  ? -41.563  60.537  62.055  1.00 220.60 ? 307  VAL B O   1 
ATOM   16690 C  CB  . VAL C 1 307  ? -39.651  61.292  59.440  1.00 136.48 ? 307  VAL B CB  1 
ATOM   16691 C  CG1 . VAL C 1 307  ? -39.685  62.463  60.372  1.00 137.77 ? 307  VAL B CG1 1 
ATOM   16692 C  CG2 . VAL C 1 307  ? -38.228  61.071  59.007  1.00 134.10 ? 307  VAL B CG2 1 
ATOM   16693 N  N   . LYS C 1 308  ? -42.614  60.444  60.061  1.00 238.41 ? 308  LYS B N   1 
ATOM   16694 C  CA  . LYS C 1 308  ? -43.878  60.946  60.568  1.00 258.68 ? 308  LYS B CA  1 
ATOM   16695 C  C   . LYS C 1 308  ? -44.113  60.431  61.986  1.00 279.42 ? 308  LYS B C   1 
ATOM   16696 O  O   . LYS C 1 308  ? -43.632  61.029  62.949  1.00 282.84 ? 308  LYS B O   1 
ATOM   16697 C  CB  . LYS C 1 308  ? -45.041  60.599  59.621  1.00 259.36 ? 308  LYS B CB  1 
ATOM   16698 C  CG  . LYS C 1 308  ? -45.093  61.448  58.336  1.00 254.77 ? 308  LYS B CG  1 
ATOM   16699 C  CD  . LYS C 1 308  ? -46.442  61.331  57.618  1.00 255.03 ? 308  LYS B CD  1 
ATOM   16700 C  CE  . LYS C 1 308  ? -46.760  59.890  57.235  1.00 254.81 ? 308  LYS B CE  1 
ATOM   16701 N  NZ  . LYS C 1 308  ? -48.078  59.756  56.555  1.00 256.30 ? 308  LYS B NZ  1 
ATOM   16702 N  N   . GLU C 1 309  ? -44.814  59.311  62.120  1.00 295.24 ? 309  GLU B N   1 
ATOM   16703 C  CA  . GLU C 1 309  ? -45.156  58.798  63.445  1.00 308.43 ? 309  GLU B CA  1 
ATOM   16704 C  C   . GLU C 1 309  ? -43.896  58.455  64.224  1.00 299.96 ? 309  GLU B C   1 
ATOM   16705 O  O   . GLU C 1 309  ? -43.942  58.201  65.426  1.00 314.61 ? 309  GLU B O   1 
ATOM   16706 C  CB  . GLU C 1 309  ? -46.079  57.575  63.342  1.00 332.80 ? 309  GLU B CB  1 
ATOM   16707 C  CG  . GLU C 1 309  ? -46.409  56.893  64.677  1.00 360.90 ? 309  GLU B CG  1 
ATOM   16708 C  CD  . GLU C 1 309  ? -47.358  57.698  65.555  1.00 379.32 ? 309  GLU B CD  1 
ATOM   16709 O  OE1 . GLU C 1 309  ? -48.058  58.589  65.032  1.00 385.17 ? 309  GLU B OE1 1 
ATOM   16710 O  OE2 . GLU C 1 309  ? -47.408  57.429  66.775  1.00 385.18 ? 309  GLU B OE2 1 
ATOM   16711 N  N   . LEU C 1 310  ? -42.765  58.460  63.535  1.00 280.91 ? 310  LEU B N   1 
ATOM   16712 C  CA  . LEU C 1 310  ? -41.526  58.032  64.154  1.00 269.56 ? 310  LEU B CA  1 
ATOM   16713 C  C   . LEU C 1 310  ? -40.727  59.195  64.749  1.00 252.36 ? 310  LEU B C   1 
ATOM   16714 O  O   . LEU C 1 310  ? -39.598  59.011  65.181  1.00 249.42 ? 310  LEU B O   1 
ATOM   16715 C  CB  . LEU C 1 310  ? -40.690  57.220  63.161  1.00 270.02 ? 310  LEU B CB  1 
ATOM   16716 C  CG  . LEU C 1 310  ? -41.450  56.232  62.258  1.00 270.28 ? 310  LEU B CG  1 
ATOM   16717 C  CD1 . LEU C 1 310  ? -40.508  55.185  61.662  1.00 267.99 ? 310  LEU B CD1 1 
ATOM   16718 C  CD2 . LEU C 1 310  ? -42.611  55.550  62.980  1.00 274.30 ? 310  LEU B CD2 1 
ATOM   16719 N  N   . SER C 1 311  ? -41.320  60.384  64.773  1.00 238.80 ? 311  SER B N   1 
ATOM   16720 C  CA  . SER C 1 311  ? -40.697  61.551  65.398  1.00 226.67 ? 311  SER B CA  1 
ATOM   16721 C  C   . SER C 1 311  ? -41.623  62.764  65.288  1.00 220.04 ? 311  SER B C   1 
ATOM   16722 O  O   . SER C 1 311  ? -42.697  62.663  64.707  1.00 218.92 ? 311  SER B O   1 
ATOM   16723 C  CB  . SER C 1 311  ? -39.335  61.857  64.763  1.00 217.19 ? 311  SER B CB  1 
ATOM   16724 O  OG  . SER C 1 311  ? -38.306  61.024  65.271  1.00 214.07 ? 311  SER B OG  1 
ATOM   16725 N  N   . TYR C 1 312  ? -41.216  63.903  65.848  1.00 218.20 ? 312  TYR B N   1 
ATOM   16726 C  CA  . TYR C 1 312  ? -41.984  65.153  65.713  1.00 217.49 ? 312  TYR B CA  1 
ATOM   16727 C  C   . TYR C 1 312  ? -42.112  65.653  64.246  1.00 172.06 ? 312  TYR B C   1 
ATOM   16728 O  O   . TYR C 1 312  ? -42.725  66.703  63.991  1.00 170.04 ? 312  TYR B O   1 
ATOM   16729 C  CB  . TYR C 1 312  ? -41.369  66.276  66.577  1.00 220.13 ? 312  TYR B CB  1 
ATOM   16730 C  CG  . TYR C 1 312  ? -41.946  66.458  67.974  1.00 226.16 ? 312  TYR B CG  1 
ATOM   16731 C  CD1 . TYR C 1 312  ? -41.111  66.618  69.075  1.00 229.29 ? 312  TYR B CD1 1 
ATOM   16732 C  CD2 . TYR C 1 312  ? -43.321  66.500  68.191  1.00 229.02 ? 312  TYR B CD2 1 
ATOM   16733 C  CE1 . TYR C 1 312  ? -41.628  66.800  70.354  1.00 233.81 ? 312  TYR B CE1 1 
ATOM   16734 C  CE2 . TYR C 1 312  ? -43.844  66.682  69.472  1.00 233.33 ? 312  TYR B CE2 1 
ATOM   16735 C  CZ  . TYR C 1 312  ? -42.990  66.829  70.547  1.00 235.17 ? 312  TYR B CZ  1 
ATOM   16736 O  OH  . TYR C 1 312  ? -43.493  67.003  71.817  1.00 239.46 ? 312  TYR B OH  1 
ATOM   16737 N  N   . TYR C 1 313  ? -41.531  64.909  63.298  1.00 168.41 ? 313  TYR B N   1 
ATOM   16738 C  CA  . TYR C 1 313  ? -41.421  65.356  61.905  1.00 161.62 ? 313  TYR B CA  1 
ATOM   16739 C  C   . TYR C 1 313  ? -42.466  64.808  60.909  1.00 164.45 ? 313  TYR B C   1 
ATOM   16740 O  O   . TYR C 1 313  ? -42.337  63.702  60.375  1.00 165.64 ? 313  TYR B O   1 
ATOM   16741 C  CB  . TYR C 1 313  ? -40.024  65.081  61.373  1.00 149.87 ? 313  TYR B CB  1 
ATOM   16742 C  CG  . TYR C 1 313  ? -38.906  65.397  62.318  1.00 142.69 ? 313  TYR B CG  1 
ATOM   16743 C  CD1 . TYR C 1 313  ? -38.117  64.390  62.826  1.00 142.10 ? 313  TYR B CD1 1 
ATOM   16744 C  CD2 . TYR C 1 313  ? -38.619  66.699  62.687  1.00 139.93 ? 313  TYR B CD2 1 
ATOM   16745 C  CE1 . TYR C 1 313  ? -37.064  64.658  63.702  1.00 142.19 ? 313  TYR B CE1 1 
ATOM   16746 C  CE2 . TYR C 1 313  ? -37.565  66.993  63.553  1.00 139.89 ? 313  TYR B CE2 1 
ATOM   16747 C  CZ  . TYR C 1 313  ? -36.783  65.965  64.065  1.00 140.96 ? 313  TYR B CZ  1 
ATOM   16748 O  OH  . TYR C 1 313  ? -35.729  66.223  64.938  1.00 141.03 ? 313  TYR B OH  1 
ATOM   16749 N  N   . SER C 1 314  ? -43.469  65.640  60.637  1.00 165.96 ? 314  SER B N   1 
ATOM   16750 C  CA  . SER C 1 314  ? -44.625  65.291  59.806  1.00 165.16 ? 314  SER B CA  1 
ATOM   16751 C  C   . SER C 1 314  ? -44.656  66.034  58.459  1.00 156.24 ? 314  SER B C   1 
ATOM   16752 O  O   . SER C 1 314  ? -45.120  65.499  57.448  1.00 152.92 ? 314  SER B O   1 
ATOM   16753 C  CB  . SER C 1 314  ? -45.891  65.617  60.589  1.00 173.72 ? 314  SER B CB  1 
ATOM   16754 O  OG  . SER C 1 314  ? -45.754  66.894  61.203  1.00 177.82 ? 314  SER B OG  1 
ATOM   16755 N  N   . LEU C 1 315  ? -44.198  67.280  58.460  1.00 151.22 ? 315  LEU B N   1 
ATOM   16756 C  CA  . LEU C 1 315  ? -43.943  67.972  57.212  1.00 147.59 ? 315  LEU B CA  1 
ATOM   16757 C  C   . LEU C 1 315  ? -42.434  67.905  56.947  1.00 136.31 ? 315  LEU B C   1 
ATOM   16758 O  O   . LEU C 1 315  ? -41.647  68.062  57.887  1.00 135.33 ? 315  LEU B O   1 
ATOM   16759 C  CB  . LEU C 1 315  ? -44.424  69.433  57.302  1.00 153.89 ? 315  LEU B CB  1 
ATOM   16760 C  CG  . LEU C 1 315  ? -45.899  69.886  57.135  1.00 161.62 ? 315  LEU B CG  1 
ATOM   16761 C  CD1 . LEU C 1 315  ? -46.243  71.040  58.088  1.00 163.12 ? 315  LEU B CD1 1 
ATOM   16762 C  CD2 . LEU C 1 315  ? -46.268  70.267  55.680  1.00 159.08 ? 315  LEU B CD2 1 
ATOM   16763 N  N   . GLU C 1 316  ? -42.035  67.658  55.692  1.00 127.72 ? 316  GLU B N   1 
ATOM   16764 C  CA  . GLU C 1 316  ? -40.616  67.663  55.315  1.00 120.99 ? 316  GLU B CA  1 
ATOM   16765 C  C   . GLU C 1 316  ? -40.063  69.058  55.540  1.00 115.09 ? 316  GLU B C   1 
ATOM   16766 O  O   . GLU C 1 316  ? -38.937  69.226  55.989  1.00 112.35 ? 316  GLU B O   1 
ATOM   16767 C  CB  . GLU C 1 316  ? -40.433  67.258  53.859  1.00 121.69 ? 316  GLU B CB  1 
ATOM   16768 C  CG  . GLU C 1 316  ? -38.969  67.133  53.433  1.00 125.41 ? 316  GLU B CG  1 
ATOM   16769 C  CD  . GLU C 1 316  ? -38.419  68.355  52.675  1.00 130.61 ? 316  GLU B CD  1 
ATOM   16770 O  OE1 . GLU C 1 316  ? -39.178  69.049  51.952  1.00 132.99 ? 316  GLU B OE1 1 
ATOM   16771 O  OE2 . GLU C 1 316  ? -37.202  68.614  52.782  1.00 131.39 ? 316  GLU B OE2 1 
ATOM   16772 N  N   . ASP C 1 317  ? -40.885  70.046  55.195  1.00 114.96 ? 317  ASP B N   1 
ATOM   16773 C  CA  . ASP C 1 317  ? -40.759  71.433  55.633  1.00 117.39 ? 317  ASP B CA  1 
ATOM   16774 C  C   . ASP C 1 317  ? -39.933  71.456  56.917  1.00 120.78 ? 317  ASP B C   1 
ATOM   16775 O  O   . ASP C 1 317  ? -38.736  71.779  56.900  1.00 118.07 ? 317  ASP B O   1 
ATOM   16776 C  CB  . ASP C 1 317  ? -42.191  71.953  55.907  1.00 123.15 ? 317  ASP B CB  1 
ATOM   16777 C  CG  . ASP C 1 317  ? -42.340  73.487  55.802  1.00 132.17 ? 317  ASP B CG  1 
ATOM   16778 O  OD1 . ASP C 1 317  ? -41.367  74.244  56.043  1.00 135.29 ? 317  ASP B OD1 1 
ATOM   16779 O  OD2 . ASP C 1 317  ? -43.474  73.943  55.498  1.00 134.42 ? 317  ASP B OD2 1 
ATOM   16780 N  N   . LEU C 1 318  ? -40.622  71.091  58.011  1.00 127.77 ? 318  LEU B N   1 
ATOM   16781 C  CA  . LEU C 1 318  ? -40.098  70.778  59.361  1.00 131.06 ? 318  LEU B CA  1 
ATOM   16782 C  C   . LEU C 1 318  ? -38.926  69.804  59.331  1.00 127.54 ? 318  LEU B C   1 
ATOM   16783 O  O   . LEU C 1 318  ? -39.071  68.657  59.723  1.00 126.57 ? 318  LEU B O   1 
ATOM   16784 C  CB  . LEU C 1 318  ? -41.186  70.063  60.181  1.00 136.15 ? 318  LEU B CB  1 
ATOM   16785 C  CG  . LEU C 1 318  ? -42.376  70.762  60.822  1.00 142.57 ? 318  LEU B CG  1 
ATOM   16786 C  CD1 . LEU C 1 318  ? -43.416  69.728  61.182  1.00 146.65 ? 318  LEU B CD1 1 
ATOM   16787 C  CD2 . LEU C 1 318  ? -41.931  71.505  62.049  1.00 147.26 ? 318  LEU B CD2 1 
ATOM   16788 N  N   . ASN C 1 319  ? -37.760  70.260  58.906  1.00 123.43 ? 319  ASN B N   1 
ATOM   16789 C  CA  . ASN C 1 319  ? -36.652  69.357  58.737  1.00 115.65 ? 319  ASN B CA  1 
ATOM   16790 C  C   . ASN C 1 319  ? -35.604  69.965  57.840  1.00 108.77 ? 319  ASN B C   1 
ATOM   16791 O  O   . ASN C 1 319  ? -35.673  69.779  56.647  1.00 107.19 ? 319  ASN B O   1 
ATOM   16792 C  CB  . ASN C 1 319  ? -37.160  68.073  58.096  1.00 114.66 ? 319  ASN B CB  1 
ATOM   16793 C  CG  . ASN C 1 319  ? -36.351  66.893  58.503  1.00 120.09 ? 319  ASN B CG  1 
ATOM   16794 O  OD1 . ASN C 1 319  ? -35.350  67.054  59.196  1.00 122.86 ? 319  ASN B OD1 1 
ATOM   16795 N  ND2 . ASN C 1 319  ? -36.768  65.690  58.098  1.00 121.40 ? 319  ASN B ND2 1 
ATOM   16796 N  N   . ASN C 1 320  ? -34.653  70.710  58.389  1.00 105.60 ? 320  ASN B N   1 
ATOM   16797 C  CA  . ASN C 1 320  ? -33.501  71.146  57.604  1.00 103.69 ? 320  ASN B CA  1 
ATOM   16798 C  C   . ASN C 1 320  ? -32.231  70.789  58.319  1.00 105.84 ? 320  ASN B C   1 
ATOM   16799 O  O   . ASN C 1 320  ? -31.212  71.495  58.218  1.00 105.82 ? 320  ASN B O   1 
ATOM   16800 C  CB  . ASN C 1 320  ? -33.550  72.616  57.244  1.00 104.83 ? 320  ASN B CB  1 
ATOM   16801 C  CG  . ASN C 1 320  ? -34.602  72.897  56.186  1.00 107.21 ? 320  ASN B CG  1 
ATOM   16802 O  OD1 . ASN C 1 320  ? -34.291  73.211  55.020  1.00 106.05 ? 320  ASN B OD1 1 
ATOM   16803 N  ND2 . ASN C 1 320  ? -35.870  72.744  56.577  1.00 109.85 ? 320  ASN B ND2 1 
ATOM   16804 N  N   . LYS C 1 321  ? -32.361  69.665  59.039  1.00 107.57 ? 321  LYS B N   1 
ATOM   16805 C  CA  . LYS C 1 321  ? -31.329  68.943  59.784  1.00 110.13 ? 321  LYS B CA  1 
ATOM   16806 C  C   . LYS C 1 321  ? -30.904  67.682  59.050  1.00 105.38 ? 321  LYS B C   1 
ATOM   16807 O  O   . LYS C 1 321  ? -31.216  67.521  57.884  1.00 103.87 ? 321  LYS B O   1 
ATOM   16808 C  CB  . LYS C 1 321  ? -31.886  68.518  61.133  1.00 118.47 ? 321  LYS B CB  1 
ATOM   16809 C  CG  . LYS C 1 321  ? -33.361  68.135  61.110  1.00 124.14 ? 321  LYS B CG  1 
ATOM   16810 C  CD  . LYS C 1 321  ? -33.951  68.189  62.533  1.00 133.50 ? 321  LYS B CD  1 
ATOM   16811 C  CE  . LYS C 1 321  ? -35.126  69.187  62.683  1.00 136.61 ? 321  LYS B CE  1 
ATOM   16812 N  NZ  . LYS C 1 321  ? -35.603  69.251  64.106  1.00 141.21 ? 321  LYS B NZ  1 
ATOM   16813 N  N   . TYR C 1 322  ? -30.229  66.764  59.738  1.00 104.38 ? 322  TYR B N   1 
ATOM   16814 C  CA  . TYR C 1 322  ? -29.525  65.672  59.052  1.00 102.01 ? 322  TYR B CA  1 
ATOM   16815 C  C   . TYR C 1 322  ? -30.236  64.323  58.995  1.00 104.44 ? 322  TYR B C   1 
ATOM   16816 O  O   . TYR C 1 322  ? -31.125  64.051  59.790  1.00 107.90 ? 322  TYR B O   1 
ATOM   16817 C  CB  . TYR C 1 322  ? -28.114  65.522  59.612  1.00 101.10 ? 322  TYR B CB  1 
ATOM   16818 C  CG  . TYR C 1 322  ? -27.280  66.687  59.216  1.00 101.24 ? 322  TYR B CG  1 
ATOM   16819 C  CD1 . TYR C 1 322  ? -26.137  66.523  58.460  1.00 99.46  ? 322  TYR B CD1 1 
ATOM   16820 C  CD2 . TYR C 1 322  ? -27.681  67.982  59.553  1.00 105.76 ? 322  TYR B CD2 1 
ATOM   16821 C  CE1 . TYR C 1 322  ? -25.387  67.615  58.073  1.00 103.20 ? 322  TYR B CE1 1 
ATOM   16822 C  CE2 . TYR C 1 322  ? -26.948  69.090  59.182  1.00 108.81 ? 322  TYR B CE2 1 
ATOM   16823 C  CZ  . TYR C 1 322  ? -25.800  68.906  58.437  1.00 109.23 ? 322  TYR B CZ  1 
ATOM   16824 O  OH  . TYR C 1 322  ? -25.083  70.034  58.069  1.00 112.35 ? 322  TYR B OH  1 
ATOM   16825 N  N   . LEU C 1 323  ? -29.852  63.492  58.030  1.00 103.80 ? 323  LEU B N   1 
ATOM   16826 C  CA  . LEU C 1 323  ? -30.296  62.103  57.989  1.00 105.98 ? 323  LEU B CA  1 
ATOM   16827 C  C   . LEU C 1 323  ? -29.103  61.170  58.214  1.00 110.17 ? 323  LEU B C   1 
ATOM   16828 O  O   . LEU C 1 323  ? -28.136  61.232  57.472  1.00 109.63 ? 323  LEU B O   1 
ATOM   16829 C  CB  . LEU C 1 323  ? -30.948  61.801  56.649  1.00 104.01 ? 323  LEU B CB  1 
ATOM   16830 C  CG  . LEU C 1 323  ? -31.549  60.406  56.554  1.00 104.00 ? 323  LEU B CG  1 
ATOM   16831 C  CD1 . LEU C 1 323  ? -30.474  59.362  56.382  1.00 102.84 ? 323  LEU B CD1 1 
ATOM   16832 C  CD2 . LEU C 1 323  ? -32.320  60.154  57.812  1.00 106.93 ? 323  LEU B CD2 1 
ATOM   16833 N  N   . TYR C 1 324  ? -29.172  60.309  59.230  1.00 115.13 ? 324  TYR B N   1 
ATOM   16834 C  CA  . TYR C 1 324  ? -28.051  59.427  59.612  1.00 120.64 ? 324  TYR B CA  1 
ATOM   16835 C  C   . TYR C 1 324  ? -28.249  57.985  59.153  1.00 120.19 ? 324  TYR B C   1 
ATOM   16836 O  O   . TYR C 1 324  ? -29.275  57.363  59.465  1.00 120.27 ? 324  TYR B O   1 
ATOM   16837 C  CB  . TYR C 1 324  ? -27.832  59.449  61.132  1.00 127.51 ? 324  TYR B CB  1 
ATOM   16838 C  CG  . TYR C 1 324  ? -26.928  58.355  61.705  1.00 134.61 ? 324  TYR B CG  1 
ATOM   16839 C  CD1 . TYR C 1 324  ? -25.617  58.638  62.084  1.00 138.36 ? 324  TYR B CD1 1 
ATOM   16840 C  CD2 . TYR C 1 324  ? -27.389  57.049  61.908  1.00 136.47 ? 324  TYR B CD2 1 
ATOM   16841 C  CE1 . TYR C 1 324  ? -24.777  57.649  62.632  1.00 140.74 ? 324  TYR B CE1 1 
ATOM   16842 C  CE2 . TYR C 1 324  ? -26.547  56.054  62.457  1.00 139.05 ? 324  TYR B CE2 1 
ATOM   16843 C  CZ  . TYR C 1 324  ? -25.245  56.370  62.813  1.00 140.00 ? 324  TYR B CZ  1 
ATOM   16844 O  OH  . TYR C 1 324  ? -24.402  55.429  63.355  1.00 140.74 ? 324  TYR B OH  1 
ATOM   16845 N  N   . ILE C 1 325  ? -27.246  57.453  58.445  1.00 118.85 ? 325  ILE B N   1 
ATOM   16846 C  CA  . ILE C 1 325  ? -27.297  56.090  57.917  1.00 114.31 ? 325  ILE B CA  1 
ATOM   16847 C  C   . ILE C 1 325  ? -26.104  55.317  58.400  1.00 115.05 ? 325  ILE B C   1 
ATOM   16848 O  O   . ILE C 1 325  ? -24.988  55.833  58.444  1.00 115.46 ? 325  ILE B O   1 
ATOM   16849 C  CB  . ILE C 1 325  ? -27.240  56.024  56.383  1.00 111.51 ? 325  ILE B CB  1 
ATOM   16850 C  CG1 . ILE C 1 325  ? -27.805  57.289  55.737  1.00 109.24 ? 325  ILE B CG1 1 
ATOM   16851 C  CG2 . ILE C 1 325  ? -27.971  54.792  55.889  1.00 109.26 ? 325  ILE B CG2 1 
ATOM   16852 C  CD1 . ILE C 1 325  ? -27.842  57.220  54.232  1.00 107.05 ? 325  ILE B CD1 1 
ATOM   16853 N  N   . ALA C 1 326  ? -26.353  54.062  58.743  1.00 116.54 ? 326  ALA B N   1 
ATOM   16854 C  CA  . ALA C 1 326  ? -25.322  53.186  59.278  1.00 116.51 ? 326  ALA B CA  1 
ATOM   16855 C  C   . ALA C 1 326  ? -25.719  51.724  59.068  1.00 117.72 ? 326  ALA B C   1 
ATOM   16856 O  O   . ALA C 1 326  ? -26.725  51.230  59.595  1.00 116.52 ? 326  ALA B O   1 
ATOM   16857 C  CB  . ALA C 1 326  ? -25.071  53.480  60.739  1.00 118.15 ? 326  ALA B CB  1 
ATOM   16858 N  N   . VAL C 1 327  ? -24.909  51.049  58.271  1.00 117.78 ? 327  VAL B N   1 
ATOM   16859 C  CA  . VAL C 1 327  ? -25.170  49.697  57.880  1.00 117.70 ? 327  VAL B CA  1 
ATOM   16860 C  C   . VAL C 1 327  ? -24.373  48.793  58.783  1.00 123.76 ? 327  VAL B C   1 
ATOM   16861 O  O   . VAL C 1 327  ? -23.346  49.218  59.311  1.00 125.36 ? 327  VAL B O   1 
ATOM   16862 C  CB  . VAL C 1 327  ? -24.677  49.500  56.456  1.00 114.61 ? 327  VAL B CB  1 
ATOM   16863 C  CG1 . VAL C 1 327  ? -25.140  48.144  55.901  1.00 113.76 ? 327  VAL B CG1 1 
ATOM   16864 C  CG2 . VAL C 1 327  ? -25.129  50.655  55.597  1.00 108.95 ? 327  VAL B CG2 1 
ATOM   16865 N  N   . THR C 1 328  ? -24.852  47.555  58.952  1.00 126.06 ? 328  THR B N   1 
ATOM   16866 C  CA  . THR C 1 328  ? -24.041  46.450  59.490  1.00 130.64 ? 328  THR B CA  1 
ATOM   16867 C  C   . THR C 1 328  ? -24.148  45.212  58.586  1.00 129.76 ? 328  THR B C   1 
ATOM   16868 O  O   . THR C 1 328  ? -25.219  44.626  58.438  1.00 126.88 ? 328  THR B O   1 
ATOM   16869 C  CB  . THR C 1 328  ? -24.404  46.076  60.935  1.00 133.97 ? 328  THR B CB  1 
ATOM   16870 O  OG1 . THR C 1 328  ? -24.379  47.250  61.757  1.00 137.65 ? 328  THR B OG1 1 
ATOM   16871 C  CG2 . THR C 1 328  ? -23.399  45.083  61.472  1.00 135.90 ? 328  THR B CG2 1 
ATOM   16872 N  N   . VAL C 1 329  ? -23.022  44.847  57.974  1.00 133.47 ? 329  VAL B N   1 
ATOM   16873 C  CA  . VAL C 1 329  ? -22.945  43.782  56.982  1.00 135.14 ? 329  VAL B CA  1 
ATOM   16874 C  C   . VAL C 1 329  ? -22.258  42.596  57.586  1.00 145.61 ? 329  VAL B C   1 
ATOM   16875 O  O   . VAL C 1 329  ? -21.034  42.599  57.696  1.00 149.87 ? 329  VAL B O   1 
ATOM   16876 C  CB  . VAL C 1 329  ? -22.049  44.192  55.820  1.00 128.81 ? 329  VAL B CB  1 
ATOM   16877 C  CG1 . VAL C 1 329  ? -22.072  43.127  54.730  1.00 124.47 ? 329  VAL B CG1 1 
ATOM   16878 C  CG2 . VAL C 1 329  ? -22.449  45.563  55.296  1.00 125.61 ? 329  VAL B CG2 1 
ATOM   16879 N  N   . ILE C 1 330  ? -23.021  41.580  57.977  1.00 150.61 ? 330  ILE B N   1 
ATOM   16880 C  CA  . ILE C 1 330  ? -22.419  40.375  58.557  1.00 158.58 ? 330  ILE B CA  1 
ATOM   16881 C  C   . ILE C 1 330  ? -22.212  39.261  57.518  1.00 165.68 ? 330  ILE B C   1 
ATOM   16882 O  O   . ILE C 1 330  ? -23.163  38.764  56.902  1.00 162.71 ? 330  ILE B O   1 
ATOM   16883 C  CB  . ILE C 1 330  ? -23.165  39.879  59.838  1.00 171.47 ? 330  ILE B CB  1 
ATOM   16884 C  CG1 . ILE C 1 330  ? -24.657  39.664  59.579  1.00 171.05 ? 330  ILE B CG1 1 
ATOM   16885 C  CG2 . ILE C 1 330  ? -22.987  40.868  60.983  1.00 171.46 ? 330  ILE B CG2 1 
ATOM   16886 C  CD1 . ILE C 1 330  ? -25.456  39.409  60.859  1.00 173.54 ? 330  ILE B CD1 1 
ATOM   16887 N  N   . GLU C 1 331  ? -20.954  38.888  57.320  1.00 176.30 ? 331  GLU B N   1 
ATOM   16888 C  CA  . GLU C 1 331  ? -20.613  37.974  56.254  1.00 185.80 ? 331  GLU B CA  1 
ATOM   16889 C  C   . GLU C 1 331  ? -21.237  36.616  56.486  1.00 196.12 ? 331  GLU B C   1 
ATOM   16890 O  O   . GLU C 1 331  ? -21.143  36.067  57.579  1.00 199.27 ? 331  GLU B O   1 
ATOM   16891 C  CB  . GLU C 1 331  ? -19.115  37.828  56.157  1.00 187.25 ? 331  GLU B CB  1 
ATOM   16892 C  CG  . GLU C 1 331  ? -18.724  36.639  55.341  1.00 188.79 ? 331  GLU B CG  1 
ATOM   16893 C  CD  . GLU C 1 331  ? -17.351  36.172  55.698  1.00 191.08 ? 331  GLU B CD  1 
ATOM   16894 O  OE1 . GLU C 1 331  ? -16.658  36.956  56.368  1.00 191.19 ? 331  GLU B OE1 1 
ATOM   16895 O  OE2 . GLU C 1 331  ? -16.962  35.041  55.327  1.00 192.84 ? 331  GLU B OE2 1 
ATOM   16896 N  N   . SER C 1 332  ? -21.858  36.071  55.445  1.00 202.63 ? 332  SER B N   1 
ATOM   16897 C  CA  . SER C 1 332  ? -22.611  34.825  55.561  1.00 212.19 ? 332  SER B CA  1 
ATOM   16898 C  C   . SER C 1 332  ? -21.740  33.587  55.740  1.00 220.82 ? 332  SER B C   1 
ATOM   16899 O  O   . SER C 1 332  ? -22.076  32.688  56.510  1.00 222.93 ? 332  SER B O   1 
ATOM   16900 C  CB  . SER C 1 332  ? -23.515  34.635  54.347  1.00 213.11 ? 332  SER B CB  1 
ATOM   16901 O  OG  . SER C 1 332  ? -24.335  33.491  54.513  1.00 216.92 ? 332  SER B OG  1 
ATOM   16902 N  N   . THR C 1 333  ? -20.629  33.534  55.016  1.00 226.37 ? 333  THR B N   1 
ATOM   16903 C  CA  . THR C 1 333  ? -19.729  32.389  55.098  1.00 233.27 ? 333  THR B CA  1 
ATOM   16904 C  C   . THR C 1 333  ? -19.041  32.253  56.459  1.00 236.50 ? 333  THR B C   1 
ATOM   16905 O  O   . THR C 1 333  ? -19.350  31.346  57.224  1.00 239.66 ? 333  THR B O   1 
ATOM   16906 C  CB  . THR C 1 333  ? -18.686  32.412  53.965  1.00 234.01 ? 333  THR B CB  1 
ATOM   16907 O  OG1 . THR C 1 333  ? -17.370  32.279  54.517  1.00 235.90 ? 333  THR B OG1 1 
ATOM   16908 C  CG2 . THR C 1 333  ? -18.777  33.718  53.191  1.00 231.03 ? 333  THR B CG2 1 
ATOM   16909 N  N   . GLY C 1 334  ? -18.120  33.157  56.763  1.00 235.32 ? 334  GLY B N   1 
ATOM   16910 C  CA  . GLY C 1 334  ? -17.371  33.082  58.005  1.00 236.32 ? 334  GLY B CA  1 
ATOM   16911 C  C   . GLY C 1 334  ? -18.164  33.393  59.266  1.00 233.58 ? 334  GLY B C   1 
ATOM   16912 O  O   . GLY C 1 334  ? -17.814  32.935  60.354  1.00 239.66 ? 334  GLY B O   1 
ATOM   16913 N  N   . GLY C 1 335  ? -19.233  34.172  59.124  1.00 224.14 ? 335  GLY B N   1 
ATOM   16914 C  CA  . GLY C 1 335  ? -20.019  34.611  60.265  1.00 217.38 ? 335  GLY B CA  1 
ATOM   16915 C  C   . GLY C 1 335  ? -19.438  35.838  60.943  1.00 210.97 ? 335  GLY B C   1 
ATOM   16916 O  O   . GLY C 1 335  ? -19.876  36.229  62.027  1.00 214.36 ? 335  GLY B O   1 
ATOM   16917 N  N   . PHE C 1 336  ? -18.444  36.442  60.301  1.00 197.99 ? 336  PHE B N   1 
ATOM   16918 C  CA  . PHE C 1 336  ? -17.788  37.629  60.826  1.00 188.43 ? 336  PHE B CA  1 
ATOM   16919 C  C   . PHE C 1 336  ? -18.814  38.702  61.083  1.00 178.76 ? 336  PHE B C   1 
ATOM   16920 O  O   . PHE C 1 336  ? -19.989  38.418  61.249  1.00 177.61 ? 336  PHE B O   1 
ATOM   16921 C  CB  . PHE C 1 336  ? -16.793  38.177  59.810  1.00 181.37 ? 336  PHE B CB  1 
ATOM   16922 C  CG  . PHE C 1 336  ? -15.443  37.512  59.836  1.00 176.64 ? 336  PHE B CG  1 
ATOM   16923 C  CD1 . PHE C 1 336  ? -14.923  36.929  58.692  1.00 172.90 ? 336  PHE B CD1 1 
ATOM   16924 C  CD2 . PHE C 1 336  ? -14.683  37.497  60.981  1.00 177.38 ? 336  PHE B CD2 1 
ATOM   16925 C  CE1 . PHE C 1 336  ? -13.678  36.340  58.689  1.00 173.45 ? 336  PHE B CE1 1 
ATOM   16926 C  CE2 . PHE C 1 336  ? -13.439  36.908  60.983  1.00 178.58 ? 336  PHE B CE2 1 
ATOM   16927 C  CZ  . PHE C 1 336  ? -12.938  36.331  59.833  1.00 177.18 ? 336  PHE B CZ  1 
ATOM   16928 N  N   . SER C 1 337  ? -18.351  39.944  61.116  1.00 171.19 ? 337  SER B N   1 
ATOM   16929 C  CA  . SER C 1 337  ? -19.249  41.088  61.113  1.00 164.34 ? 337  SER B CA  1 
ATOM   16930 C  C   . SER C 1 337  ? -18.524  42.401  60.907  1.00 161.68 ? 337  SER B C   1 
ATOM   16931 O  O   . SER C 1 337  ? -17.418  42.614  61.405  1.00 163.95 ? 337  SER B O   1 
ATOM   16932 C  CB  . SER C 1 337  ? -20.080  41.171  62.389  1.00 161.27 ? 337  SER B CB  1 
ATOM   16933 O  OG  . SER C 1 337  ? -20.840  42.376  62.406  1.00 155.24 ? 337  SER B OG  1 
ATOM   16934 N  N   . GLU C 1 338  ? -19.185  43.290  60.182  1.00 159.02 ? 338  GLU B N   1 
ATOM   16935 C  CA  . GLU C 1 338  ? -18.590  44.551  59.812  1.00 157.94 ? 338  GLU B CA  1 
ATOM   16936 C  C   . GLU C 1 338  ? -19.648  45.631  59.804  1.00 153.47 ? 338  GLU B C   1 
ATOM   16937 O  O   . GLU C 1 338  ? -20.744  45.430  59.290  1.00 150.74 ? 338  GLU B O   1 
ATOM   16938 C  CB  . GLU C 1 338  ? -17.945  44.438  58.442  1.00 160.04 ? 338  GLU B CB  1 
ATOM   16939 C  CG  . GLU C 1 338  ? -16.770  45.359  58.272  1.00 164.60 ? 338  GLU B CG  1 
ATOM   16940 C  CD  . GLU C 1 338  ? -15.869  45.361  59.490  1.00 171.98 ? 338  GLU B CD  1 
ATOM   16941 O  OE1 . GLU C 1 338  ? -15.447  44.268  59.942  1.00 174.22 ? 338  GLU B OE1 1 
ATOM   16942 O  OE2 . GLU C 1 338  ? -15.586  46.471  59.994  1.00 174.76 ? 338  GLU B OE2 1 
ATOM   16943 N  N   . GLU C 1 339  ? -19.308  46.766  60.410  1.00 154.29 ? 339  GLU B N   1 
ATOM   16944 C  CA  . GLU C 1 339  ? -20.194  47.916  60.511  1.00 152.86 ? 339  GLU B CA  1 
ATOM   16945 C  C   . GLU C 1 339  ? -19.615  49.078  59.719  1.00 145.73 ? 339  GLU B C   1 
ATOM   16946 O  O   . GLU C 1 339  ? -18.395  49.143  59.510  1.00 142.61 ? 339  GLU B O   1 
ATOM   16947 C  CB  . GLU C 1 339  ? -20.371  48.334  61.969  1.00 163.38 ? 339  GLU B CB  1 
ATOM   16948 C  CG  . GLU C 1 339  ? -21.365  47.480  62.738  1.00 173.40 ? 339  GLU B CG  1 
ATOM   16949 C  CD  . GLU C 1 339  ? -20.957  47.263  64.196  1.00 185.56 ? 339  GLU B CD  1 
ATOM   16950 O  OE1 . GLU C 1 339  ? -20.390  48.189  64.813  1.00 190.11 ? 339  GLU B OE1 1 
ATOM   16951 O  OE2 . GLU C 1 339  ? -21.199  46.156  64.727  1.00 190.62 ? 339  GLU B OE2 1 
ATOM   16952 N  N   . ALA C 1 340  ? -20.509  49.974  59.281  1.00 141.55 ? 340  ALA B N   1 
ATOM   16953 C  CA  . ALA C 1 340  ? -20.171  51.202  58.555  1.00 140.38 ? 340  ALA B CA  1 
ATOM   16954 C  C   . ALA C 1 340  ? -21.276  52.219  58.749  1.00 135.86 ? 340  ALA B C   1 
ATOM   16955 O  O   . ALA C 1 340  ? -22.431  51.835  58.899  1.00 136.17 ? 340  ALA B O   1 
ATOM   16956 C  CB  . ALA C 1 340  ? -20.004  50.916  57.078  1.00 139.61 ? 340  ALA B CB  1 
ATOM   16957 N  N   . GLU C 1 341  ? -20.933  53.508  58.721  1.00 135.24 ? 341  GLU B N   1 
ATOM   16958 C  CA  . GLU C 1 341  ? -21.945  54.567  58.877  1.00 135.34 ? 341  GLU B CA  1 
ATOM   16959 C  C   . GLU C 1 341  ? -21.737  55.835  58.000  1.00 110.97 ? 341  GLU B C   1 
ATOM   16960 O  O   . GLU C 1 341  ? -20.612  56.157  57.616  1.00 112.43 ? 341  GLU B O   1 
ATOM   16961 C  CB  . GLU C 1 341  ? -22.042  54.984  60.348  1.00 139.75 ? 341  GLU B CB  1 
ATOM   16962 C  CG  . GLU C 1 341  ? -20.713  55.429  60.951  1.00 144.13 ? 341  GLU B CG  1 
ATOM   16963 C  CD  . GLU C 1 341  ? -20.885  56.374  62.132  1.00 148.01 ? 341  GLU B CD  1 
ATOM   16964 O  OE1 . GLU C 1 341  ? -22.040  56.648  62.528  1.00 148.13 ? 341  GLU B OE1 1 
ATOM   16965 O  OE2 . GLU C 1 341  ? -19.856  56.839  62.667  1.00 150.97 ? 341  GLU B OE2 1 
ATOM   16966 N  N   . ILE C 1 342  ? -22.823  56.539  57.671  1.00 108.01 ? 342  ILE B N   1 
ATOM   16967 C  CA  . ILE C 1 342  ? -22.729  57.893  57.137  1.00 104.14 ? 342  ILE B CA  1 
ATOM   16968 C  C   . ILE C 1 342  ? -23.234  58.843  58.190  1.00 107.00 ? 342  ILE B C   1 
ATOM   16969 O  O   . ILE C 1 342  ? -24.377  58.732  58.626  1.00 108.62 ? 342  ILE B O   1 
ATOM   16970 C  CB  . ILE C 1 342  ? -23.609  58.089  55.932  1.00 97.65  ? 342  ILE B CB  1 
ATOM   16971 C  CG1 . ILE C 1 342  ? -23.058  57.309  54.755  1.00 97.41  ? 342  ILE B CG1 1 
ATOM   16972 C  CG2 . ILE C 1 342  ? -23.672  59.548  55.574  1.00 91.80  ? 342  ILE B CG2 1 
ATOM   16973 C  CD1 . ILE C 1 342  ? -24.074  57.100  53.646  1.00 96.44  ? 342  ILE B CD1 1 
ATOM   16974 N  N   . PRO C 1 343  ? -22.403  59.818  58.572  1.00 108.96 ? 343  PRO B N   1 
ATOM   16975 C  CA  . PRO C 1 343  ? -22.686  60.604  59.775  1.00 109.26 ? 343  PRO B CA  1 
ATOM   16976 C  C   . PRO C 1 343  ? -24.033  61.276  59.621  1.00 109.35 ? 343  PRO B C   1 
ATOM   16977 O  O   . PRO C 1 343  ? -24.934  61.110  60.442  1.00 111.06 ? 343  PRO B O   1 
ATOM   16978 C  CB  . PRO C 1 343  ? -21.586  61.678  59.769  1.00 109.63 ? 343  PRO B CB  1 
ATOM   16979 C  CG  . PRO C 1 343  ? -20.667  61.335  58.633  1.00 109.10 ? 343  PRO B CG  1 
ATOM   16980 C  CD  . PRO C 1 343  ? -21.448  60.500  57.687  1.00 106.92 ? 343  PRO B CD  1 
ATOM   16981 N  N   . GLY C 1 344  ? -24.161  62.022  58.528  1.00 110.76 ? 344  GLY B N   1 
ATOM   16982 C  CA  . GLY C 1 344  ? -25.380  62.750  58.221  1.00 110.41 ? 344  GLY B CA  1 
ATOM   16983 C  C   . GLY C 1 344  ? -25.450  63.176  56.764  1.00 99.29  ? 344  GLY B C   1 
ATOM   16984 O  O   . GLY C 1 344  ? -24.450  63.138  56.056  1.00 100.09 ? 344  GLY B O   1 
ATOM   16985 N  N   . ILE C 1 345  ? -26.636  63.593  56.338  1.00 93.02  ? 345  ILE B N   1 
ATOM   16986 C  CA  . ILE C 1 345  ? -26.937  63.914  54.960  1.00 89.49  ? 345  ILE B CA  1 
ATOM   16987 C  C   . ILE C 1 345  ? -27.953  65.003  55.155  1.00 89.31  ? 345  ILE B C   1 
ATOM   16988 O  O   . ILE C 1 345  ? -29.040  64.725  55.648  1.00 91.78  ? 345  ILE B O   1 
ATOM   16989 C  CB  . ILE C 1 345  ? -27.661  62.719  54.293  1.00 86.33  ? 345  ILE B CB  1 
ATOM   16990 C  CG1 . ILE C 1 345  ? -26.695  61.620  53.904  1.00 78.50  ? 345  ILE B CG1 1 
ATOM   16991 C  CG2 . ILE C 1 345  ? -28.334  63.113  53.037  1.00 87.19  ? 345  ILE B CG2 1 
ATOM   16992 C  CD1 . ILE C 1 345  ? -27.342  60.585  53.069  1.00 71.87  ? 345  ILE B CD1 1 
ATOM   16993 N  N   . LYS C 1 346  ? -27.615  66.244  54.826  1.00 84.63  ? 346  LYS B N   1 
ATOM   16994 C  CA  . LYS C 1 346  ? -28.497  67.352  55.182  1.00 75.95  ? 346  LYS B CA  1 
ATOM   16995 C  C   . LYS C 1 346  ? -29.832  67.230  54.439  1.00 72.52  ? 346  LYS B C   1 
ATOM   16996 O  O   . LYS C 1 346  ? -29.827  66.911  53.267  1.00 82.35  ? 346  LYS B O   1 
ATOM   16997 C  CB  . LYS C 1 346  ? -27.803  68.679  54.868  1.00 75.10  ? 346  LYS B CB  1 
ATOM   16998 C  CG  . LYS C 1 346  ? -28.466  69.895  55.489  1.00 79.84  ? 346  LYS B CG  1 
ATOM   16999 C  CD  . LYS C 1 346  ? -27.842  71.225  55.015  1.00 84.22  ? 346  LYS B CD  1 
ATOM   17000 C  CE  . LYS C 1 346  ? -26.452  71.510  55.617  1.00 88.41  ? 346  LYS B CE  1 
ATOM   17001 N  NZ  . LYS C 1 346  ? -26.108  72.975  55.611  1.00 90.40  ? 346  LYS B NZ  1 
ATOM   17002 N  N   . TYR C 1 347  ? -30.975  67.436  55.094  1.00 77.80  ? 347  TYR B N   1 
ATOM   17003 C  CA  . TYR C 1 347  ? -32.252  67.537  54.360  1.00 79.05  ? 347  TYR B CA  1 
ATOM   17004 C  C   . TYR C 1 347  ? -32.348  68.957  53.837  1.00 78.99  ? 347  TYR B C   1 
ATOM   17005 O  O   . TYR C 1 347  ? -31.816  69.876  54.449  1.00 78.53  ? 347  TYR B O   1 
ATOM   17006 C  CB  . TYR C 1 347  ? -33.482  67.246  55.242  1.00 78.69  ? 347  TYR B CB  1 
ATOM   17007 C  CG  . TYR C 1 347  ? -33.921  65.794  55.297  1.00 82.00  ? 347  TYR B CG  1 
ATOM   17008 C  CD1 . TYR C 1 347  ? -34.787  65.275  54.336  1.00 82.45  ? 347  TYR B CD1 1 
ATOM   17009 C  CD2 . TYR C 1 347  ? -33.476  64.930  56.325  1.00 84.92  ? 347  TYR B CD2 1 
ATOM   17010 C  CE1 . TYR C 1 347  ? -35.191  63.923  54.383  1.00 84.09  ? 347  TYR B CE1 1 
ATOM   17011 C  CE2 . TYR C 1 347  ? -33.874  63.588  56.386  1.00 85.55  ? 347  TYR B CE2 1 
ATOM   17012 C  CZ  . TYR C 1 347  ? -34.729  63.083  55.407  1.00 86.46  ? 347  TYR B CZ  1 
ATOM   17013 O  OH  . TYR C 1 347  ? -35.113  61.744  55.423  1.00 88.55  ? 347  TYR B OH  1 
ATOM   17014 N  N   . VAL C 1 348  ? -33.022  69.160  52.715  1.00 81.99  ? 348  VAL B N   1 
ATOM   17015 C  CA  . VAL C 1 348  ? -33.169  70.520  52.202  1.00 86.42  ? 348  VAL B CA  1 
ATOM   17016 C  C   . VAL C 1 348  ? -34.558  70.830  51.668  1.00 87.34  ? 348  VAL B C   1 
ATOM   17017 O  O   . VAL C 1 348  ? -35.094  70.096  50.844  1.00 88.90  ? 348  VAL B O   1 
ATOM   17018 C  CB  . VAL C 1 348  ? -32.124  70.838  51.099  1.00 92.15  ? 348  VAL B CB  1 
ATOM   17019 C  CG1 . VAL C 1 348  ? -32.493  72.128  50.365  1.00 91.65  ? 348  VAL B CG1 1 
ATOM   17020 C  CG2 . VAL C 1 348  ? -30.754  70.984  51.696  1.00 93.54  ? 348  VAL B CG2 1 
ATOM   17021 N  N   . LEU C 1 349  ? -35.137  71.930  52.120  1.00 87.53  ? 349  LEU B N   1 
ATOM   17022 C  CA  . LEU C 1 349  ? -36.387  72.369  51.519  1.00 88.81  ? 349  LEU B CA  1 
ATOM   17023 C  C   . LEU C 1 349  ? -36.151  72.869  50.089  1.00 82.67  ? 349  LEU B C   1 
ATOM   17024 O  O   . LEU C 1 349  ? -36.760  72.407  49.133  1.00 80.83  ? 349  LEU B O   1 
ATOM   17025 C  CB  . LEU C 1 349  ? -37.006  73.483  52.369  1.00 93.85  ? 349  LEU B CB  1 
ATOM   17026 C  CG  . LEU C 1 349  ? -38.511  73.778  52.250  1.00 95.55  ? 349  LEU B CG  1 
ATOM   17027 C  CD1 . LEU C 1 349  ? -38.765  75.078  51.520  1.00 96.00  ? 349  LEU B CD1 1 
ATOM   17028 C  CD2 . LEU C 1 349  ? -39.283  72.602  51.629  1.00 95.15  ? 349  LEU B CD2 1 
ATOM   17029 N  N   . SER C 1 350  ? -35.234  73.806  49.960  1.00 77.74  ? 350  SER B N   1 
ATOM   17030 C  CA  . SER C 1 350  ? -35.053  74.512  48.723  1.00 75.94  ? 350  SER B CA  1 
ATOM   17031 C  C   . SER C 1 350  ? -33.587  74.603  48.397  1.00 76.67  ? 350  SER B C   1 
ATOM   17032 O  O   . SER C 1 350  ? -32.790  75.041  49.198  1.00 80.09  ? 350  SER B O   1 
ATOM   17033 C  CB  . SER C 1 350  ? -35.611  75.915  48.862  1.00 76.16  ? 350  SER B CB  1 
ATOM   17034 O  OG  . SER C 1 350  ? -35.161  76.765  47.819  1.00 76.61  ? 350  SER B OG  1 
ATOM   17035 N  N   . PRO C 1 351  ? -33.220  74.232  47.186  1.00 74.51  ? 351  PRO B N   1 
ATOM   17036 C  CA  . PRO C 1 351  ? -31.794  74.053  46.986  1.00 74.50  ? 351  PRO B CA  1 
ATOM   17037 C  C   . PRO C 1 351  ? -31.044  75.360  46.827  1.00 76.56  ? 351  PRO B C   1 
ATOM   17038 O  O   . PRO C 1 351  ? -29.847  75.288  46.584  1.00 79.70  ? 351  PRO B O   1 
ATOM   17039 C  CB  . PRO C 1 351  ? -31.743  73.250  45.703  1.00 73.45  ? 351  PRO B CB  1 
ATOM   17040 C  CG  . PRO C 1 351  ? -33.190  72.776  45.485  1.00 71.81  ? 351  PRO B CG  1 
ATOM   17041 C  CD  . PRO C 1 351  ? -34.000  73.832  46.011  1.00 71.84  ? 351  PRO B CD  1 
ATOM   17042 N  N   . TYR C 1 352  ? -31.700  76.515  46.936  1.00 75.15  ? 352  TYR B N   1 
ATOM   17043 C  CA  . TYR C 1 352  ? -30.959  77.777  47.007  1.00 76.54  ? 352  TYR B CA  1 
ATOM   17044 C  C   . TYR C 1 352  ? -31.122  78.351  48.407  1.00 76.69  ? 352  TYR B C   1 
ATOM   17045 O  O   . TYR C 1 352  ? -31.979  77.892  49.156  1.00 73.97  ? 352  TYR B O   1 
ATOM   17046 C  CB  . TYR C 1 352  ? -31.400  78.815  45.943  1.00 81.01  ? 352  TYR B CB  1 
ATOM   17047 C  CG  . TYR C 1 352  ? -31.468  78.325  44.497  1.00 82.13  ? 352  TYR B CG  1 
ATOM   17048 C  CD1 . TYR C 1 352  ? -30.355  78.367  43.669  1.00 82.83  ? 352  TYR B CD1 1 
ATOM   17049 C  CD2 . TYR C 1 352  ? -32.656  77.844  43.961  1.00 83.02  ? 352  TYR B CD2 1 
ATOM   17050 C  CE1 . TYR C 1 352  ? -30.411  77.916  42.356  1.00 83.72  ? 352  TYR B CE1 1 
ATOM   17051 C  CE2 . TYR C 1 352  ? -32.726  77.397  42.661  1.00 84.09  ? 352  TYR B CE2 1 
ATOM   17052 C  CZ  . TYR C 1 352  ? -31.602  77.430  41.861  1.00 84.90  ? 352  TYR B CZ  1 
ATOM   17053 O  OH  . TYR C 1 352  ? -31.686  76.966  40.568  1.00 86.50  ? 352  TYR B OH  1 
ATOM   17054 N  N   . LYS C 1 353  ? -30.302  79.349  48.746  1.00 80.83  ? 353  LYS B N   1 
ATOM   17055 C  CA  . LYS C 1 353  ? -30.436  80.100  49.999  1.00 82.65  ? 353  LYS B CA  1 
ATOM   17056 C  C   . LYS C 1 353  ? -30.037  81.571  49.812  1.00 77.41  ? 353  LYS B C   1 
ATOM   17057 O  O   . LYS C 1 353  ? -28.870  81.902  49.522  1.00 72.61  ? 353  LYS B O   1 
ATOM   17058 C  CB  . LYS C 1 353  ? -29.600  79.451  51.103  1.00 89.81  ? 353  LYS B CB  1 
ATOM   17059 C  CG  . LYS C 1 353  ? -28.419  78.646  50.538  1.00 97.19  ? 353  LYS B CG  1 
ATOM   17060 C  CD  . LYS C 1 353  ? -28.000  77.444  51.411  1.00 102.71 ? 353  LYS B CD  1 
ATOM   17061 C  CE  . LYS C 1 353  ? -26.850  77.790  52.355  1.00 106.63 ? 353  LYS B CE  1 
ATOM   17062 N  NZ  . LYS C 1 353  ? -26.539  76.657  53.277  1.00 109.24 ? 353  LYS B NZ  1 
ATOM   17063 N  N   . LEU C 1 354  ? -31.033  82.440  49.973  1.00 76.64  ? 354  LEU B N   1 
ATOM   17064 C  CA  . LEU C 1 354  ? -30.853  83.887  49.859  1.00 77.47  ? 354  LEU B CA  1 
ATOM   17065 C  C   . LEU C 1 354  ? -30.300  84.489  51.131  1.00 76.22  ? 354  LEU B C   1 
ATOM   17066 O  O   . LEU C 1 354  ? -30.655  84.067  52.229  1.00 77.32  ? 354  LEU B O   1 
ATOM   17067 C  CB  . LEU C 1 354  ? -32.189  84.590  49.648  1.00 78.54  ? 354  LEU B CB  1 
ATOM   17068 C  CG  . LEU C 1 354  ? -33.358  84.026  48.859  1.00 77.92  ? 354  LEU B CG  1 
ATOM   17069 C  CD1 . LEU C 1 354  ? -32.882  83.905  47.439  1.00 78.87  ? 354  LEU B CD1 1 
ATOM   17070 C  CD2 . LEU C 1 354  ? -33.853  82.710  49.417  1.00 75.09  ? 354  LEU B CD2 1 
ATOM   17071 N  N   . ASN C 1 355  ? -29.495  85.525  50.977  1.00 74.05  ? 355  ASN B N   1 
ATOM   17072 C  CA  . ASN C 1 355  ? -29.056  86.297  52.103  1.00 78.40  ? 355  ASN B CA  1 
ATOM   17073 C  C   . ASN C 1 355  ? -28.620  87.641  51.620  1.00 75.84  ? 355  ASN B C   1 
ATOM   17074 O  O   . ASN C 1 355  ? -27.789  87.728  50.718  1.00 73.42  ? 355  ASN B O   1 
ATOM   17075 C  CB  . ASN C 1 355  ? -27.887  85.633  52.797  1.00 86.25  ? 355  ASN B CB  1 
ATOM   17076 C  CG  . ASN C 1 355  ? -26.742  85.364  51.868  1.00 92.65  ? 355  ASN B CG  1 
ATOM   17077 O  OD1 . ASN C 1 355  ? -26.711  84.330  51.182  1.00 94.28  ? 355  ASN B OD1 1 
ATOM   17078 N  ND2 . ASN C 1 355  ? -25.764  86.272  51.862  1.00 94.77  ? 355  ASN B ND2 1 
ATOM   17079 N  N   . LEU C 1 356  ? -29.190  88.687  52.211  1.00 75.16  ? 356  LEU B N   1 
ATOM   17080 C  CA  . LEU C 1 356  ? -28.897  90.050  51.821  1.00 75.11  ? 356  LEU B CA  1 
ATOM   17081 C  C   . LEU C 1 356  ? -27.395  90.228  51.882  1.00 80.24  ? 356  LEU B C   1 
ATOM   17082 O  O   . LEU C 1 356  ? -26.732  89.477  52.594  1.00 80.20  ? 356  LEU B O   1 
ATOM   17083 C  CB  . LEU C 1 356  ? -29.594  90.982  52.794  1.00 77.91  ? 356  LEU B CB  1 
ATOM   17084 C  CG  . LEU C 1 356  ? -31.121  90.920  52.745  1.00 76.85  ? 356  LEU B CG  1 
ATOM   17085 C  CD1 . LEU C 1 356  ? -31.767  92.045  53.565  1.00 77.16  ? 356  LEU B CD1 1 
ATOM   17086 C  CD2 . LEU C 1 356  ? -31.514  91.030  51.305  1.00 76.70  ? 356  LEU B CD2 1 
ATOM   17087 N  N   . VAL C 1 357  ? -26.849  91.196  51.145  1.00 82.62  ? 357  VAL B N   1 
ATOM   17088 C  CA  . VAL C 1 357  ? -25.397  91.394  51.093  1.00 78.14  ? 357  VAL B CA  1 
ATOM   17089 C  C   . VAL C 1 357  ? -25.026  92.853  51.226  1.00 89.30  ? 357  VAL B C   1 
ATOM   17090 O  O   . VAL C 1 357  ? -25.343  93.657  50.352  1.00 84.50  ? 357  VAL B O   1 
ATOM   17091 C  CB  . VAL C 1 357  ? -24.816  90.977  49.774  1.00 77.63  ? 357  VAL B CB  1 
ATOM   17092 C  CG1 . VAL C 1 357  ? -23.459  91.590  49.626  1.00 79.29  ? 357  VAL B CG1 1 
ATOM   17093 C  CG2 . VAL C 1 357  ? -24.740  89.497  49.702  1.00 76.41  ? 357  VAL B CG2 1 
ATOM   17094 N  N   . ALA C 1 358  ? -24.333  93.200  52.305  1.00 91.28  ? 358  ALA B N   1 
ATOM   17095 C  CA  . ALA C 1 358  ? -24.017  94.601  52.562  1.00 95.07  ? 358  ALA B CA  1 
ATOM   17096 C  C   . ALA C 1 358  ? -25.152  95.520  52.057  1.00 91.32  ? 358  ALA B C   1 
ATOM   17097 O  O   . ALA C 1 358  ? -24.957  96.403  51.203  1.00 88.84  ? 358  ALA B O   1 
ATOM   17098 C  CB  . ALA C 1 358  ? -22.651  94.978  52.004  1.00 95.86  ? 358  ALA B CB  1 
ATOM   17099 N  N   . THR C 1 359  ? -26.350  95.252  52.589  1.00 92.68  ? 359  THR B N   1 
ATOM   17100 C  CA  . THR C 1 359  ? -27.514  96.118  52.395  1.00 93.33  ? 359  THR B CA  1 
ATOM   17101 C  C   . THR C 1 359  ? -28.254  96.441  53.700  1.00 89.42  ? 359  THR B C   1 
ATOM   17102 O  O   . THR C 1 359  ? -29.197  95.740  54.064  1.00 86.15  ? 359  THR B O   1 
ATOM   17103 C  CB  . THR C 1 359  ? -28.493  95.530  51.380  1.00 94.27  ? 359  THR B CB  1 
ATOM   17104 O  OG1 . THR C 1 359  ? -28.933  94.250  51.835  1.00 94.63  ? 359  THR B OG1 1 
ATOM   17105 C  CG2 . THR C 1 359  ? -27.803  95.404  50.030  1.00 94.10  ? 359  THR B CG2 1 
ATOM   17106 N  N   . PRO C 1 360  ? -27.831  97.534  54.368  1.00 89.77  ? 360  PRO B N   1 
ATOM   17107 C  CA  . PRO C 1 360  ? -28.225  98.077  55.666  1.00 89.85  ? 360  PRO B CA  1 
ATOM   17108 C  C   . PRO C 1 360  ? -29.708  98.111  55.777  1.00 89.39  ? 360  PRO B C   1 
ATOM   17109 O  O   . PRO C 1 360  ? -30.363  98.370  54.775  1.00 85.54  ? 360  PRO B O   1 
ATOM   17110 C  CB  . PRO C 1 360  ? -27.712  99.498  55.599  1.00 93.36  ? 360  PRO B CB  1 
ATOM   17111 C  CG  . PRO C 1 360  ? -26.523  99.422  54.722  1.00 93.54  ? 360  PRO B CG  1 
ATOM   17112 C  CD  . PRO C 1 360  ? -26.800  98.368  53.726  1.00 91.70  ? 360  PRO B CD  1 
ATOM   17113 N  N   . LEU C 1 361  ? -30.225  97.870  56.972  1.00 90.53  ? 361  LEU B N   1 
ATOM   17114 C  CA  . LEU C 1 361  ? -31.656  97.674  57.127  1.00 94.83  ? 361  LEU B CA  1 
ATOM   17115 C  C   . LEU C 1 361  ? -32.432  98.866  57.650  1.00 103.69 ? 361  LEU B C   1 
ATOM   17116 O  O   . LEU C 1 361  ? -33.476  98.724  58.297  1.00 104.68 ? 361  LEU B O   1 
ATOM   17117 C  CB  . LEU C 1 361  ? -31.925  96.459  57.968  1.00 91.31  ? 361  LEU B CB  1 
ATOM   17118 C  CG  . LEU C 1 361  ? -32.111  95.309  56.992  1.00 89.66  ? 361  LEU B CG  1 
ATOM   17119 C  CD1 . LEU C 1 361  ? -30.783  94.685  56.482  1.00 83.59  ? 361  LEU B CD1 1 
ATOM   17120 C  CD2 . LEU C 1 361  ? -32.969  94.284  57.687  1.00 91.47  ? 361  LEU B CD2 1 
ATOM   17121 N  N   . PHE C 1 362  ? -31.919  100.042 57.325  1.00 111.85 ? 362  PHE B N   1 
ATOM   17122 C  CA  . PHE C 1 362  ? -32.499  101.287 57.762  1.00 118.48 ? 362  PHE B CA  1 
ATOM   17123 C  C   . PHE C 1 362  ? -32.578  102.170 56.558  1.00 110.73 ? 362  PHE B C   1 
ATOM   17124 O  O   . PHE C 1 362  ? -31.607  102.306 55.813  1.00 108.58 ? 362  PHE B O   1 
ATOM   17125 C  CB  . PHE C 1 362  ? -31.600  101.954 58.798  1.00 133.01 ? 362  PHE B CB  1 
ATOM   17126 C  CG  . PHE C 1 362  ? -31.401  101.137 60.021  1.00 143.42 ? 362  PHE B CG  1 
ATOM   17127 C  CD1 . PHE C 1 362  ? -30.135  100.844 60.474  1.00 147.99 ? 362  PHE B CD1 1 
ATOM   17128 C  CD2 . PHE C 1 362  ? -32.498  100.637 60.707  1.00 148.92 ? 362  PHE B CD2 1 
ATOM   17129 C  CE1 . PHE C 1 362  ? -29.969  100.089 61.605  1.00 151.72 ? 362  PHE B CE1 1 
ATOM   17130 C  CE2 . PHE C 1 362  ? -32.340  99.877  61.832  1.00 151.89 ? 362  PHE B CE2 1 
ATOM   17131 C  CZ  . PHE C 1 362  ? -31.075  99.600  62.283  1.00 153.43 ? 362  PHE B CZ  1 
ATOM   17132 N  N   . LEU C 1 363  ? -33.736  102.773 56.358  1.00 106.40 ? 363  LEU B N   1 
ATOM   17133 C  CA  . LEU C 1 363  ? -33.869  103.712 55.273  1.00 98.97  ? 363  LEU B CA  1 
ATOM   17134 C  C   . LEU C 1 363  ? -33.649  105.123 55.741  1.00 99.09  ? 363  LEU B C   1 
ATOM   17135 O  O   . LEU C 1 363  ? -34.234  105.541 56.723  1.00 97.69  ? 363  LEU B O   1 
ATOM   17136 C  CB  . LEU C 1 363  ? -35.222  103.563 54.583  1.00 96.10  ? 363  LEU B CB  1 
ATOM   17137 C  CG  . LEU C 1 363  ? -36.274  102.791 55.353  1.00 92.02  ? 363  LEU B CG  1 
ATOM   17138 C  CD1 . LEU C 1 363  ? -37.016  103.744 56.227  1.00 93.55  ? 363  LEU B CD1 1 
ATOM   17139 C  CD2 . LEU C 1 363  ? -37.217  102.131 54.399  1.00 89.24  ? 363  LEU B CD2 1 
ATOM   17140 N  N   . LYS C 1 364  ? -32.751  105.822 55.057  1.00 100.01 ? 364  LYS B N   1 
ATOM   17141 C  CA  . LYS C 1 364  ? -32.702  107.272 55.080  1.00 107.05 ? 364  LYS B CA  1 
ATOM   17142 C  C   . LYS C 1 364  ? -33.797  107.674 54.104  1.00 110.60 ? 364  LYS B C   1 
ATOM   17143 O  O   . LYS C 1 364  ? -33.990  106.965 53.112  1.00 108.38 ? 364  LYS B O   1 
ATOM   17144 C  CB  . LYS C 1 364  ? -31.353  107.751 54.569  1.00 109.83 ? 364  LYS B CB  1 
ATOM   17145 C  CG  . LYS C 1 364  ? -30.163  107.166 55.313  1.00 113.57 ? 364  LYS B CG  1 
ATOM   17146 C  CD  . LYS C 1 364  ? -29.949  105.656 55.059  1.00 113.66 ? 364  LYS B CD  1 
ATOM   17147 C  CE  . LYS C 1 364  ? -28.640  105.146 55.710  1.00 116.00 ? 364  LYS B CE  1 
ATOM   17148 N  NZ  . LYS C 1 364  ? -28.282  105.894 56.986  1.00 119.85 ? 364  LYS B NZ  1 
ATOM   17149 N  N   . PRO C 1 365  ? -34.548  108.765 54.384  1.00 115.69 ? 365  PRO B N   1 
ATOM   17150 C  CA  . PRO C 1 365  ? -35.639  109.129 53.477  1.00 117.18 ? 365  PRO B CA  1 
ATOM   17151 C  C   . PRO C 1 365  ? -35.190  110.087 52.381  1.00 120.85 ? 365  PRO B C   1 
ATOM   17152 O  O   . PRO C 1 365  ? -34.180  110.774 52.502  1.00 125.59 ? 365  PRO B O   1 
ATOM   17153 C  CB  . PRO C 1 365  ? -36.653  109.803 54.400  1.00 118.72 ? 365  PRO B CB  1 
ATOM   17154 C  CG  . PRO C 1 365  ? -36.098  109.712 55.772  1.00 118.51 ? 365  PRO B CG  1 
ATOM   17155 C  CD  . PRO C 1 365  ? -34.624  109.556 55.615  1.00 117.55 ? 365  PRO B CD  1 
ATOM   17156 N  N   . GLY C 1 366  ? -35.957  110.127 51.305  1.00 122.38 ? 366  GLY B N   1 
ATOM   17157 C  CA  . GLY C 1 366  ? -35.514  110.835 50.125  1.00 128.22 ? 366  GLY B CA  1 
ATOM   17158 C  C   . GLY C 1 366  ? -34.419  110.075 49.373  1.00 124.34 ? 366  GLY B C   1 
ATOM   17159 O  O   . GLY C 1 366  ? -34.227  110.260 48.162  1.00 128.87 ? 366  GLY B O   1 
ATOM   17160 N  N   . ILE C 1 367  ? -33.680  109.222 50.068  1.00 118.64 ? 367  ILE B N   1 
ATOM   17161 C  CA  . ILE C 1 367  ? -32.696  108.425 49.375  1.00 116.48 ? 367  ILE B CA  1 
ATOM   17162 C  C   . ILE C 1 367  ? -33.357  107.134 48.920  1.00 111.81 ? 367  ILE B C   1 
ATOM   17163 O  O   . ILE C 1 367  ? -34.280  106.656 49.578  1.00 112.97 ? 367  ILE B O   1 
ATOM   17164 C  CB  . ILE C 1 367  ? -31.472  108.211 50.244  1.00 115.37 ? 367  ILE B CB  1 
ATOM   17165 C  CG1 . ILE C 1 367  ? -30.623  109.472 50.227  1.00 117.23 ? 367  ILE B CG1 1 
ATOM   17166 C  CG2 . ILE C 1 367  ? -30.658  107.067 49.728  1.00 114.10 ? 367  ILE B CG2 1 
ATOM   17167 C  CD1 . ILE C 1 367  ? -29.583  109.503 51.283  1.00 117.90 ? 367  ILE B CD1 1 
ATOM   17168 N  N   . PRO C 1 368  ? -32.932  106.585 47.766  1.00 107.12 ? 368  PRO B N   1 
ATOM   17169 C  CA  . PRO C 1 368  ? -33.607  105.375 47.313  1.00 101.08 ? 368  PRO B CA  1 
ATOM   17170 C  C   . PRO C 1 368  ? -32.970  104.179 47.997  1.00 100.14 ? 368  PRO B C   1 
ATOM   17171 O  O   . PRO C 1 368  ? -31.744  104.092 48.033  1.00 99.36  ? 368  PRO B O   1 
ATOM   17172 C  CB  . PRO C 1 368  ? -33.302  105.350 45.816  1.00 99.95  ? 368  PRO B CB  1 
ATOM   17173 C  CG  . PRO C 1 368  ? -32.343  106.504 45.570  1.00 102.22 ? 368  PRO B CG  1 
ATOM   17174 C  CD  . PRO C 1 368  ? -31.815  106.916 46.872  1.00 105.00 ? 368  PRO B CD  1 
ATOM   17175 N  N   . TYR C 1 369  ? -33.786  103.288 48.550  1.00 97.94  ? 369  TYR B N   1 
ATOM   17176 C  CA  . TYR C 1 369  ? -33.286  102.143 49.298  1.00 95.37  ? 369  TYR B CA  1 
ATOM   17177 C  C   . TYR C 1 369  ? -32.909  101.011 48.333  1.00 95.45  ? 369  TYR B C   1 
ATOM   17178 O  O   . TYR C 1 369  ? -33.728  100.612 47.530  1.00 97.38  ? 369  TYR B O   1 
ATOM   17179 C  CB  . TYR C 1 369  ? -34.358  101.703 50.304  1.00 99.81  ? 369  TYR B CB  1 
ATOM   17180 C  CG  . TYR C 1 369  ? -33.950  100.587 51.236  1.00 102.76 ? 369  TYR B CG  1 
ATOM   17181 C  CD1 . TYR C 1 369  ? -32.724  100.604 51.889  1.00 104.64 ? 369  TYR B CD1 1 
ATOM   17182 C  CD2 . TYR C 1 369  ? -34.799  99.533  51.480  1.00 102.11 ? 369  TYR B CD2 1 
ATOM   17183 C  CE1 . TYR C 1 369  ? -32.353  99.586  52.734  1.00 105.92 ? 369  TYR B CE1 1 
ATOM   17184 C  CE2 . TYR C 1 369  ? -34.440  98.518  52.318  1.00 104.45 ? 369  TYR B CE2 1 
ATOM   17185 C  CZ  . TYR C 1 369  ? -33.221  98.548  52.941  1.00 106.69 ? 369  TYR B CZ  1 
ATOM   17186 O  OH  . TYR C 1 369  ? -32.877  97.525  53.784  1.00 109.42 ? 369  TYR B OH  1 
ATOM   17187 N  N   . PRO C 1 370  ? -31.651  100.543 48.386  1.00 83.97  ? 370  PRO B N   1 
ATOM   17188 C  CA  . PRO C 1 370  ? -30.972  99.416  47.723  1.00 82.39  ? 370  PRO B CA  1 
ATOM   17189 C  C   . PRO C 1 370  ? -31.149  98.067  48.418  1.00 88.86  ? 370  PRO B C   1 
ATOM   17190 O  O   . PRO C 1 370  ? -31.102  98.064  49.627  1.00 87.89  ? 370  PRO B O   1 
ATOM   17191 C  CB  . PRO C 1 370  ? -29.508  99.783  47.879  1.00 83.71  ? 370  PRO B CB  1 
ATOM   17192 C  CG  . PRO C 1 370  ? -29.496  101.217 48.268  1.00 85.96  ? 370  PRO B CG  1 
ATOM   17193 C  CD  . PRO C 1 370  ? -30.693  101.436 49.045  1.00 86.03  ? 370  PRO B CD  1 
ATOM   17194 N  N   . ILE C 1 371  ? -31.279  96.946  47.717  1.00 79.09  ? 371  ILE B N   1 
ATOM   17195 C  CA  . ILE C 1 371  ? -31.492  95.670  48.403  1.00 77.80  ? 371  ILE B CA  1 
ATOM   17196 C  C   . ILE C 1 371  ? -30.777  94.499  47.717  1.00 78.86  ? 371  ILE B C   1 
ATOM   17197 O  O   . ILE C 1 371  ? -31.456  93.549  47.362  1.00 78.31  ? 371  ILE B O   1 
ATOM   17198 C  CB  . ILE C 1 371  ? -33.030  95.237  48.479  1.00 76.83  ? 371  ILE B CB  1 
ATOM   17199 C  CG1 . ILE C 1 371  ? -33.910  96.130  49.353  1.00 78.01  ? 371  ILE B CG1 1 
ATOM   17200 C  CG2 . ILE C 1 371  ? -33.200  93.860  49.071  1.00 75.60  ? 371  ILE B CG2 1 
ATOM   17201 C  CD1 . ILE C 1 371  ? -35.371  95.668  49.366  1.00 77.25  ? 371  ILE B CD1 1 
ATOM   17202 N  N   . LYS C 1 372  ? -29.446  94.507  47.529  1.00 77.13  ? 372  LYS B N   1 
ATOM   17203 C  CA  . LYS C 1 372  ? -28.739  93.364  46.869  1.00 76.14  ? 372  LYS B CA  1 
ATOM   17204 C  C   . LYS C 1 372  ? -28.892  92.023  47.577  1.00 75.00  ? 372  LYS B C   1 
ATOM   17205 O  O   . LYS C 1 372  ? -28.141  91.770  48.480  1.00 79.05  ? 372  LYS B O   1 
ATOM   17206 C  CB  . LYS C 1 372  ? -27.229  93.610  46.785  1.00 77.31  ? 372  LYS B CB  1 
ATOM   17207 C  CG  . LYS C 1 372  ? -26.808  95.054  46.946  1.00 79.19  ? 372  LYS B CG  1 
ATOM   17208 C  CD  . LYS C 1 372  ? -25.311  95.213  47.309  1.00 95.94  ? 372  LYS B CD  1 
ATOM   17209 C  CE  . LYS C 1 372  ? -24.980  96.606  47.935  1.00 117.13 ? 372  LYS B CE  1 
ATOM   17210 N  NZ  . LYS C 1 372  ? -24.050  97.489  47.135  1.00 117.70 ? 372  LYS B NZ  1 
ATOM   17211 N  N   . VAL C 1 373  ? -29.822  91.153  47.178  1.00 73.63  ? 373  VAL B N   1 
ATOM   17212 C  CA  . VAL C 1 373  ? -29.889  89.787  47.736  1.00 79.50  ? 373  VAL B CA  1 
ATOM   17213 C  C   . VAL C 1 373  ? -28.847  88.866  47.074  1.00 76.70  ? 373  VAL B C   1 
ATOM   17214 O  O   . VAL C 1 373  ? -28.228  89.252  46.081  1.00 79.86  ? 373  VAL B O   1 
ATOM   17215 C  CB  . VAL C 1 373  ? -31.287  89.175  47.645  1.00 71.60  ? 373  VAL B CB  1 
ATOM   17216 C  CG1 . VAL C 1 373  ? -32.325  90.260  47.846  1.00 72.13  ? 373  VAL B CG1 1 
ATOM   17217 C  CG2 . VAL C 1 373  ? -31.508  88.499  46.333  1.00 70.68  ? 373  VAL B CG2 1 
ATOM   17218 N  N   . GLN C 1 374  ? -28.623  87.665  47.585  1.00 72.92  ? 374  GLN B N   1 
ATOM   17219 C  CA  . GLN C 1 374  ? -27.529  86.877  47.021  1.00 75.10  ? 374  GLN B CA  1 
ATOM   17220 C  C   . GLN C 1 374  ? -27.780  85.372  47.103  1.00 81.77  ? 374  GLN B C   1 
ATOM   17221 O  O   . GLN C 1 374  ? -27.812  84.812  48.196  1.00 87.67  ? 374  GLN B O   1 
ATOM   17222 C  CB  . GLN C 1 374  ? -26.239  87.235  47.731  1.00 74.96  ? 374  GLN B CB  1 
ATOM   17223 C  CG  . GLN C 1 374  ? -25.220  86.124  47.752  1.00 78.86  ? 374  GLN B CG  1 
ATOM   17224 C  CD  . GLN C 1 374  ? -23.893  86.573  48.376  1.00 85.50  ? 374  GLN B CD  1 
ATOM   17225 O  OE1 . GLN C 1 374  ? -23.615  86.312  49.563  1.00 87.30  ? 374  GLN B OE1 1 
ATOM   17226 N  NE2 . GLN C 1 374  ? -23.065  87.266  47.577  1.00 87.44  ? 374  GLN B NE2 1 
ATOM   17227 N  N   . VAL C 1 375  ? -27.964  84.706  45.961  1.00 81.15  ? 375  VAL B N   1 
ATOM   17228 C  CA  . VAL C 1 375  ? -28.392  83.303  45.977  1.00 78.19  ? 375  VAL B CA  1 
ATOM   17229 C  C   . VAL C 1 375  ? -27.231  82.355  46.101  1.00 81.74  ? 375  VAL B C   1 
ATOM   17230 O  O   . VAL C 1 375  ? -26.163  82.605  45.547  1.00 82.69  ? 375  VAL B O   1 
ATOM   17231 C  CB  . VAL C 1 375  ? -29.159  82.885  44.729  1.00 71.62  ? 375  VAL B CB  1 
ATOM   17232 C  CG1 . VAL C 1 375  ? -29.457  81.407  44.804  1.00 68.80  ? 375  VAL B CG1 1 
ATOM   17233 C  CG2 . VAL C 1 375  ? -30.446  83.682  44.597  1.00 69.53  ? 375  VAL B CG2 1 
ATOM   17234 N  N   . LYS C 1 376  ? -27.460  81.255  46.821  1.00 83.23  ? 376  LYS B N   1 
ATOM   17235 C  CA  . LYS C 1 376  ? -26.435  80.243  47.078  1.00 81.33  ? 376  LYS B CA  1 
ATOM   17236 C  C   . LYS C 1 376  ? -27.067  78.875  47.035  1.00 76.06  ? 376  LYS B C   1 
ATOM   17237 O  O   . LYS C 1 376  ? -28.259  78.737  47.287  1.00 71.02  ? 376  LYS B O   1 
ATOM   17238 C  CB  . LYS C 1 376  ? -25.792  80.460  48.447  1.00 84.97  ? 376  LYS B CB  1 
ATOM   17239 C  CG  . LYS C 1 376  ? -24.499  81.286  48.422  1.00 88.44  ? 376  LYS B CG  1 
ATOM   17240 C  CD  . LYS C 1 376  ? -24.152  81.874  49.786  1.00 89.50  ? 376  LYS B CD  1 
ATOM   17241 C  CE  . LYS C 1 376  ? -22.862  82.651  49.743  1.00 90.68  ? 376  LYS B CE  1 
ATOM   17242 N  NZ  . LYS C 1 376  ? -23.003  83.778  50.698  1.00 93.37  ? 376  LYS B NZ  1 
ATOM   17243 N  N   . ASP C 1 377  ? -26.278  77.865  46.697  1.00 78.81  ? 377  ASP B N   1 
ATOM   17244 C  CA  . ASP C 1 377  ? -26.808  76.510  46.622  1.00 82.84  ? 377  ASP B CA  1 
ATOM   17245 C  C   . ASP C 1 377  ? -26.540  75.753  47.871  1.00 88.50  ? 377  ASP B C   1 
ATOM   17246 O  O   . ASP C 1 377  ? -25.673  76.108  48.678  1.00 89.93  ? 377  ASP B O   1 
ATOM   17247 C  CB  . ASP C 1 377  ? -26.161  75.707  45.518  1.00 84.22  ? 377  ASP B CB  1 
ATOM   17248 C  CG  . ASP C 1 377  ? -24.682  75.785  45.576  1.00 88.15  ? 377  ASP B CG  1 
ATOM   17249 O  OD1 . ASP C 1 377  ? -24.182  76.696  46.260  1.00 89.78  ? 377  ASP B OD1 1 
ATOM   17250 O  OD2 . ASP C 1 377  ? -24.021  74.958  44.938  1.00 90.82  ? 377  ASP B OD2 1 
ATOM   17251 N  N   . SER C 1 378  ? -27.276  74.664  47.995  1.00 91.75  ? 378  SER B N   1 
ATOM   17252 C  CA  . SER C 1 378  ? -27.134  73.758  49.112  1.00 95.99  ? 378  SER B CA  1 
ATOM   17253 C  C   . SER C 1 378  ? -25.648  73.411  49.412  1.00 71.68  ? 378  SER B C   1 
ATOM   17254 O  O   . SER C 1 378  ? -25.357  72.629  50.306  1.00 71.51  ? 378  SER B O   1 
ATOM   17255 C  CB  . SER C 1 378  ? -28.035  72.518  48.881  1.00 97.45  ? 378  SER B CB  1 
ATOM   17256 O  OG  . SER C 1 378  ? -28.421  72.339  47.498  1.00 96.88  ? 378  SER B OG  1 
ATOM   17257 N  N   . LEU C 1 379  ? -24.722  74.042  48.693  1.00 73.97  ? 379  LEU B N   1 
ATOM   17258 C  CA  . LEU C 1 379  ? -23.295  73.866  48.930  1.00 80.49  ? 379  LEU B CA  1 
ATOM   17259 C  C   . LEU C 1 379  ? -22.614  75.185  49.142  1.00 88.58  ? 379  LEU B C   1 
ATOM   17260 O  O   . LEU C 1 379  ? -21.394  75.279  49.020  1.00 93.11  ? 379  LEU B O   1 
ATOM   17261 C  CB  . LEU C 1 379  ? -22.607  73.155  47.764  1.00 79.31  ? 379  LEU B CB  1 
ATOM   17262 C  CG  . LEU C 1 379  ? -22.357  71.681  48.058  1.00 82.14  ? 379  LEU B CG  1 
ATOM   17263 C  CD1 . LEU C 1 379  ? -22.144  70.812  46.799  1.00 81.84  ? 379  LEU B CD1 1 
ATOM   17264 C  CD2 . LEU C 1 379  ? -21.215  71.558  49.062  1.00 83.93  ? 379  LEU B CD2 1 
ATOM   17265 N  N   . ASP C 1 380  ? -23.394  76.209  49.443  1.00 90.33  ? 380  ASP B N   1 
ATOM   17266 C  CA  . ASP C 1 380  ? -22.836  77.527  49.677  1.00 96.71  ? 380  ASP B CA  1 
ATOM   17267 C  C   . ASP C 1 380  ? -21.832  78.062  48.649  1.00 98.69  ? 380  ASP B C   1 
ATOM   17268 O  O   . ASP C 1 380  ? -20.931  78.794  49.030  1.00 100.23 ? 380  ASP B O   1 
ATOM   17269 C  CB  . ASP C 1 380  ? -22.194  77.584  51.063  1.00 103.38 ? 380  ASP B CB  1 
ATOM   17270 C  CG  . ASP C 1 380  ? -23.218  77.550  52.183  1.00 110.07 ? 380  ASP B CG  1 
ATOM   17271 O  OD1 . ASP C 1 380  ? -23.868  78.591  52.473  1.00 109.68 ? 380  ASP B OD1 1 
ATOM   17272 O  OD2 . ASP C 1 380  ? -23.349  76.466  52.787  1.00 115.31 ? 380  ASP B OD2 1 
ATOM   17273 N  N   . GLN C 1 381  ? -21.946  77.693  47.372  1.00 100.91 ? 381  GLN B N   1 
ATOM   17274 C  CA  . GLN C 1 381  ? -21.304  78.505  46.325  1.00 102.61 ? 381  GLN B CA  1 
ATOM   17275 C  C   . GLN C 1 381  ? -22.327  79.505  45.801  1.00 98.31  ? 381  GLN B C   1 
ATOM   17276 O  O   . GLN C 1 381  ? -23.546  79.337  45.986  1.00 96.24  ? 381  GLN B O   1 
ATOM   17277 C  CB  . GLN C 1 381  ? -20.738  77.721  45.139  1.00 106.23 ? 381  GLN B CB  1 
ATOM   17278 C  CG  . GLN C 1 381  ? -19.745  76.641  45.470  1.00 113.37 ? 381  GLN B CG  1 
ATOM   17279 C  CD  . GLN C 1 381  ? -20.386  75.265  45.372  1.00 118.62 ? 381  GLN B CD  1 
ATOM   17280 O  OE1 . GLN C 1 381  ? -19.845  74.340  44.748  1.00 121.63 ? 381  GLN B OE1 1 
ATOM   17281 N  NE2 . GLN C 1 381  ? -21.568  75.134  45.962  1.00 118.66 ? 381  GLN B NE2 1 
ATOM   17282 N  N   . LEU C 1 382  ? -21.831  80.557  45.162  1.00 94.75  ? 382  LEU B N   1 
ATOM   17283 C  CA  . LEU C 1 382  ? -22.712  81.561  44.633  1.00 89.74  ? 382  LEU B CA  1 
ATOM   17284 C  C   . LEU C 1 382  ? -23.340  80.970  43.407  1.00 89.59  ? 382  LEU B C   1 
ATOM   17285 O  O   . LEU C 1 382  ? -22.705  80.202  42.715  1.00 94.75  ? 382  LEU B O   1 
ATOM   17286 C  CB  . LEU C 1 382  ? -21.893  82.793  44.319  1.00 89.35  ? 382  LEU B CB  1 
ATOM   17287 C  CG  . LEU C 1 382  ? -21.765  83.593  45.609  1.00 89.95  ? 382  LEU B CG  1 
ATOM   17288 C  CD1 . LEU C 1 382  ? -20.970  84.872  45.404  1.00 92.11  ? 382  LEU B CD1 1 
ATOM   17289 C  CD2 . LEU C 1 382  ? -23.168  83.897  46.136  1.00 87.72  ? 382  LEU B CD2 1 
ATOM   17290 N  N   . VAL C 1 383  ? -24.593  81.279  43.132  1.00 86.08  ? 383  VAL B N   1 
ATOM   17291 C  CA  . VAL C 1 383  ? -25.194  80.792  41.892  1.00 83.06  ? 383  VAL B CA  1 
ATOM   17292 C  C   . VAL C 1 383  ? -25.920  81.904  41.164  1.00 84.24  ? 383  VAL B C   1 
ATOM   17293 O  O   . VAL C 1 383  ? -26.797  82.566  41.702  1.00 83.74  ? 383  VAL B O   1 
ATOM   17294 C  CB  . VAL C 1 383  ? -26.078  79.549  42.107  1.00 77.65  ? 383  VAL B CB  1 
ATOM   17295 C  CG1 . VAL C 1 383  ? -26.031  79.164  43.546  1.00 79.47  ? 383  VAL B CG1 1 
ATOM   17296 C  CG2 . VAL C 1 383  ? -27.508  79.780  41.634  1.00 71.47  ? 383  VAL B CG2 1 
ATOM   17297 N  N   . GLY C 1 384  ? -25.494  82.133  39.934  1.00 86.09  ? 384  GLY B N   1 
ATOM   17298 C  CA  . GLY C 1 384  ? -26.018  83.229  39.153  1.00 86.97  ? 384  GLY B CA  1 
ATOM   17299 C  C   . GLY C 1 384  ? -27.133  82.791  38.234  1.00 88.37  ? 384  GLY B C   1 
ATOM   17300 O  O   . GLY C 1 384  ? -27.349  81.596  38.018  1.00 90.28  ? 384  GLY B O   1 
ATOM   17301 N  N   . GLY C 1 385  ? -27.848  83.770  37.695  1.00 88.72  ? 385  GLY B N   1 
ATOM   17302 C  CA  . GLY C 1 385  ? -28.897  83.510  36.732  1.00 88.29  ? 385  GLY B CA  1 
ATOM   17303 C  C   . GLY C 1 385  ? -30.151  82.921  37.339  1.00 86.60  ? 385  GLY B C   1 
ATOM   17304 O  O   . GLY C 1 385  ? -30.913  82.232  36.660  1.00 87.91  ? 385  GLY B O   1 
ATOM   17305 N  N   . VAL C 1 386  ? -30.367  83.163  38.623  1.00 83.74  ? 386  VAL B N   1 
ATOM   17306 C  CA  . VAL C 1 386  ? -31.625  82.771  39.225  1.00 80.54  ? 386  VAL B CA  1 
ATOM   17307 C  C   . VAL C 1 386  ? -32.503  84.000  39.251  1.00 76.00  ? 386  VAL B C   1 
ATOM   17308 O  O   . VAL C 1 386  ? -32.054  85.099  39.549  1.00 76.57  ? 386  VAL B O   1 
ATOM   17309 C  CB  . VAL C 1 386  ? -31.470  82.140  40.644  1.00 71.74  ? 386  VAL B CB  1 
ATOM   17310 C  CG1 . VAL C 1 386  ? -32.548  81.107  40.870  1.00 70.71  ? 386  VAL B CG1 1 
ATOM   17311 C  CG2 . VAL C 1 386  ? -30.122  81.459  40.808  1.00 72.09  ? 386  VAL B CG2 1 
ATOM   17312 N  N   . PRO C 1 387  ? -33.761  83.832  38.897  1.00 72.11  ? 387  PRO B N   1 
ATOM   17313 C  CA  . PRO C 1 387  ? -34.601  85.008  39.025  1.00 75.13  ? 387  PRO B CA  1 
ATOM   17314 C  C   . PRO C 1 387  ? -35.009  85.136  40.499  1.00 79.05  ? 387  PRO B C   1 
ATOM   17315 O  O   . PRO C 1 387  ? -35.209  84.117  41.167  1.00 79.83  ? 387  PRO B O   1 
ATOM   17316 C  CB  . PRO C 1 387  ? -35.807  84.666  38.131  1.00 73.78  ? 387  PRO B CB  1 
ATOM   17317 C  CG  . PRO C 1 387  ? -35.569  83.223  37.652  1.00 69.73  ? 387  PRO B CG  1 
ATOM   17318 C  CD  . PRO C 1 387  ? -34.526  82.646  38.513  1.00 68.95  ? 387  PRO B CD  1 
ATOM   17319 N  N   . VAL C 1 388  ? -35.153  86.365  40.987  1.00 78.90  ? 388  VAL B N   1 
ATOM   17320 C  CA  . VAL C 1 388  ? -35.482  86.602  42.393  1.00 78.24  ? 388  VAL B CA  1 
ATOM   17321 C  C   . VAL C 1 388  ? -36.561  87.692  42.558  1.00 79.51  ? 388  VAL B C   1 
ATOM   17322 O  O   . VAL C 1 388  ? -36.273  88.873  42.328  1.00 81.33  ? 388  VAL B O   1 
ATOM   17323 C  CB  . VAL C 1 388  ? -34.191  87.033  43.148  1.00 78.94  ? 388  VAL B CB  1 
ATOM   17324 C  CG1 . VAL C 1 388  ? -34.471  88.048  44.251  1.00 79.96  ? 388  VAL B CG1 1 
ATOM   17325 C  CG2 . VAL C 1 388  ? -33.428  85.806  43.676  1.00 78.01  ? 388  VAL B CG2 1 
ATOM   17326 N  N   . THR C 1 389  ? -37.794  87.335  42.939  1.00 79.25  ? 389  THR B N   1 
ATOM   17327 C  CA  . THR C 1 389  ? -38.821  88.385  43.184  1.00 81.31  ? 389  THR B CA  1 
ATOM   17328 C  C   . THR C 1 389  ? -38.666  89.132  44.536  1.00 84.85  ? 389  THR B C   1 
ATOM   17329 O  O   . THR C 1 389  ? -38.126  88.576  45.501  1.00 87.53  ? 389  THR B O   1 
ATOM   17330 C  CB  . THR C 1 389  ? -40.308  87.893  43.001  1.00 92.89  ? 389  THR B CB  1 
ATOM   17331 O  OG1 . THR C 1 389  ? -40.379  86.465  43.018  1.00 91.72  ? 389  THR B OG1 1 
ATOM   17332 C  CG2 . THR C 1 389  ? -40.886  88.385  41.685  1.00 93.14  ? 389  THR B CG2 1 
ATOM   17333 N  N   . LEU C 1 390  ? -39.124  90.382  44.607  1.00 80.09  ? 390  LEU B N   1 
ATOM   17334 C  CA  . LEU C 1 390  ? -38.948  91.154  45.823  1.00 77.72  ? 390  LEU B CA  1 
ATOM   17335 C  C   . LEU C 1 390  ? -40.222  91.895  46.172  1.00 82.10  ? 390  LEU B C   1 
ATOM   17336 O  O   . LEU C 1 390  ? -40.400  93.036  45.757  1.00 88.23  ? 390  LEU B O   1 
ATOM   17337 C  CB  . LEU C 1 390  ? -37.839  92.178  45.638  1.00 74.14  ? 390  LEU B CB  1 
ATOM   17338 C  CG  . LEU C 1 390  ? -37.900  93.241  46.731  1.00 77.52  ? 390  LEU B CG  1 
ATOM   17339 C  CD1 . LEU C 1 390  ? -37.184  92.700  47.888  1.00 80.71  ? 390  LEU B CD1 1 
ATOM   17340 C  CD2 . LEU C 1 390  ? -37.283  94.551  46.377  1.00 74.64  ? 390  LEU B CD2 1 
ATOM   17341 N  N   . ASN C 1 391  ? -41.119  91.260  46.915  1.00 80.96  ? 391  ASN B N   1 
ATOM   17342 C  CA  . ASN C 1 391  ? -42.332  91.936  47.359  1.00 85.21  ? 391  ASN B CA  1 
ATOM   17343 C  C   . ASN C 1 391  ? -42.033  92.728  48.599  1.00 88.73  ? 391  ASN B C   1 
ATOM   17344 O  O   . ASN C 1 391  ? -41.351  92.231  49.488  1.00 90.67  ? 391  ASN B O   1 
ATOM   17345 C  CB  . ASN C 1 391  ? -43.405  90.924  47.690  1.00 88.76  ? 391  ASN B CB  1 
ATOM   17346 C  CG  . ASN C 1 391  ? -44.103  90.390  46.464  1.00 91.23  ? 391  ASN B CG  1 
ATOM   17347 O  OD1 . ASN C 1 391  ? -43.534  89.618  45.672  1.00 89.32  ? 391  ASN B OD1 1 
ATOM   17348 N  ND2 . ASN C 1 391  ? -45.371  90.775  46.315  1.00 94.03  ? 391  ASN B ND2 1 
ATOM   17349 N  N   . ALA C 1 392  ? -42.549  93.951  48.688  1.00 91.57  ? 392  ALA B N   1 
ATOM   17350 C  CA  . ALA C 1 392  ? -42.232  94.807  49.846  1.00 91.15  ? 392  ALA B CA  1 
ATOM   17351 C  C   . ALA C 1 392  ? -43.424  95.595  50.287  1.00 90.35  ? 392  ALA B C   1 
ATOM   17352 O  O   . ALA C 1 392  ? -44.346  95.781  49.520  1.00 90.54  ? 392  ALA B O   1 
ATOM   17353 C  CB  . ALA C 1 392  ? -41.101  95.758  49.533  1.00 91.99  ? 392  ALA B CB  1 
ATOM   17354 N  N   . GLN C 1 393  ? -43.405  96.080  51.516  1.00 92.07  ? 393  GLN B N   1 
ATOM   17355 C  CA  . GLN C 1 393  ? -44.637  96.623  52.092  1.00 98.21  ? 393  GLN B CA  1 
ATOM   17356 C  C   . GLN C 1 393  ? -44.383  97.699  53.161  1.00 100.80 ? 393  GLN B C   1 
ATOM   17357 O  O   . GLN C 1 393  ? -43.429  97.628  53.944  1.00 98.99  ? 393  GLN B O   1 
ATOM   17358 C  CB  . GLN C 1 393  ? -45.548  95.483  52.589  1.00 99.59  ? 393  GLN B CB  1 
ATOM   17359 C  CG  . GLN C 1 393  ? -46.922  95.895  53.035  1.00 100.69 ? 393  GLN B CG  1 
ATOM   17360 C  CD  . GLN C 1 393  ? -46.902  96.556  54.384  1.00 101.59 ? 393  GLN B CD  1 
ATOM   17361 O  OE1 . GLN C 1 393  ? -47.717  97.433  54.662  1.00 103.00 ? 393  GLN B OE1 1 
ATOM   17362 N  NE2 . GLN C 1 393  ? -45.962  96.150  55.234  1.00 100.80 ? 393  GLN B NE2 1 
ATOM   17363 N  N   . THR C 1 394  ? -45.262  98.690  53.178  1.00 103.01 ? 394  THR B N   1 
ATOM   17364 C  CA  . THR C 1 394  ? -44.894  99.989  53.683  1.00 107.77 ? 394  THR B CA  1 
ATOM   17365 C  C   . THR C 1 394  ? -46.015  100.774 54.365  1.00 118.42 ? 394  THR B C   1 
ATOM   17366 O  O   . THR C 1 394  ? -47.164  100.743 53.921  1.00 122.12 ? 394  THR B O   1 
ATOM   17367 C  CB  . THR C 1 394  ? -44.315  100.789 52.520  1.00 102.51 ? 394  THR B CB  1 
ATOM   17368 O  OG1 . THR C 1 394  ? -42.904  100.575 52.497  1.00 100.08 ? 394  THR B OG1 1 
ATOM   17369 C  CG2 . THR C 1 394  ? -44.608  102.291 52.649  1.00 104.21 ? 394  THR B CG2 1 
ATOM   17370 N  N   . ILE C 1 395  ? -45.687  101.478 55.449  1.00 122.61 ? 395  ILE B N   1 
ATOM   17371 C  CA  . ILE C 1 395  ? -46.649  102.422 55.996  1.00 127.96 ? 395  ILE B CA  1 
ATOM   17372 C  C   . ILE C 1 395  ? -46.071  103.816 56.147  1.00 134.40 ? 395  ILE B C   1 
ATOM   17373 O  O   . ILE C 1 395  ? -44.862  103.991 56.337  1.00 135.93 ? 395  ILE B O   1 
ATOM   17374 C  CB  . ILE C 1 395  ? -47.215  102.013 57.342  1.00 127.89 ? 395  ILE B CB  1 
ATOM   17375 C  CG1 . ILE C 1 395  ? -46.168  102.222 58.427  1.00 127.42 ? 395  ILE B CG1 1 
ATOM   17376 C  CG2 . ILE C 1 395  ? -47.730  100.594 57.288  1.00 127.06 ? 395  ILE B CG2 1 
ATOM   17377 C  CD1 . ILE C 1 395  ? -46.732  102.913 59.633  1.00 129.77 ? 395  ILE B CD1 1 
ATOM   17378 N  N   . ASP C 1 396  ? -46.972  104.796 56.061  1.00 138.22 ? 396  ASP B N   1 
ATOM   17379 C  CA  . ASP C 1 396  ? -46.646  106.206 56.035  1.00 140.39 ? 396  ASP B CA  1 
ATOM   17380 C  C   . ASP C 1 396  ? -46.372  106.631 57.445  1.00 142.24 ? 396  ASP B C   1 
ATOM   17381 O  O   . ASP C 1 396  ? -46.719  105.926 58.382  1.00 142.67 ? 396  ASP B O   1 
ATOM   17382 C  CB  . ASP C 1 396  ? -47.844  106.988 55.503  1.00 145.36 ? 396  ASP B CB  1 
ATOM   17383 C  CG  . ASP C 1 396  ? -47.435  108.082 54.544  1.00 152.02 ? 396  ASP B CG  1 
ATOM   17384 O  OD1 . ASP C 1 396  ? -48.228  109.034 54.320  1.00 156.51 ? 396  ASP B OD1 1 
ATOM   17385 O  OD2 . ASP C 1 396  ? -46.305  107.982 54.007  1.00 152.58 ? 396  ASP B OD2 1 
ATOM   17386 N  N   . VAL C 1 397  ? -45.749  107.782 57.620  1.00 144.91 ? 397  VAL B N   1 
ATOM   17387 C  CA  . VAL C 1 397  ? -45.743  108.370 58.949  1.00 149.93 ? 397  VAL B CA  1 
ATOM   17388 C  C   . VAL C 1 397  ? -47.184  108.766 59.281  1.00 152.36 ? 397  VAL B C   1 
ATOM   17389 O  O   . VAL C 1 397  ? -47.580  108.841 60.442  1.00 153.42 ? 397  VAL B O   1 
ATOM   17390 C  CB  . VAL C 1 397  ? -44.799  109.584 59.061  1.00 150.75 ? 397  VAL B CB  1 
ATOM   17391 C  CG1 . VAL C 1 397  ? -45.441  110.813 58.460  1.00 152.44 ? 397  VAL B CG1 1 
ATOM   17392 C  CG2 . VAL C 1 397  ? -44.431  109.816 60.533  1.00 153.55 ? 397  VAL B CG2 1 
ATOM   17393 N  N   . ASN C 1 398  ? -47.961  108.984 58.228  1.00 153.00 ? 398  ASN B N   1 
ATOM   17394 C  CA  . ASN C 1 398  ? -49.371  109.308 58.320  1.00 156.02 ? 398  ASN B CA  1 
ATOM   17395 C  C   . ASN C 1 398  ? -50.196  108.087 58.706  1.00 152.93 ? 398  ASN B C   1 
ATOM   17396 O  O   . ASN C 1 398  ? -51.419  108.128 58.726  1.00 152.40 ? 398  ASN B O   1 
ATOM   17397 C  CB  . ASN C 1 398  ? -49.838  109.825 56.964  1.00 157.93 ? 398  ASN B CB  1 
ATOM   17398 C  CG  . ASN C 1 398  ? -50.894  110.900 57.080  1.00 162.95 ? 398  ASN B CG  1 
ATOM   17399 O  OD1 . ASN C 1 398  ? -51.145  111.428 58.162  1.00 167.15 ? 398  ASN B OD1 1 
ATOM   17400 N  ND2 . ASN C 1 398  ? -51.517  111.238 55.957  1.00 162.99 ? 398  ASN B ND2 1 
ATOM   17401 N  N   . GLN C 1 399  ? -49.514  106.988 58.987  1.00 153.68 ? 399  GLN B N   1 
ATOM   17402 C  CA  . GLN C 1 399  ? -50.178  105.749 59.386  1.00 154.86 ? 399  GLN B CA  1 
ATOM   17403 C  C   . GLN C 1 399  ? -51.025  105.081 58.291  1.00 154.75 ? 399  GLN B C   1 
ATOM   17404 O  O   . GLN C 1 399  ? -51.951  104.320 58.589  1.00 154.56 ? 399  GLN B O   1 
ATOM   17405 C  CB  . GLN C 1 399  ? -50.975  105.968 60.668  1.00 158.44 ? 399  GLN B CB  1 
ATOM   17406 C  CG  . GLN C 1 399  ? -50.074  106.065 61.878  1.00 160.81 ? 399  GLN B CG  1 
ATOM   17407 C  CD  . GLN C 1 399  ? -49.187  104.836 62.014  1.00 159.60 ? 399  GLN B CD  1 
ATOM   17408 O  OE1 . GLN C 1 399  ? -49.606  103.808 62.552  1.00 159.50 ? 399  GLN B OE1 1 
ATOM   17409 N  NE2 . GLN C 1 399  ? -47.951  104.939 61.531  1.00 158.30 ? 399  GLN B NE2 1 
ATOM   17410 N  N   . GLU C 1 400  ? -50.672  105.361 57.034  1.00 154.71 ? 400  GLU B N   1 
ATOM   17411 C  CA  . GLU C 1 400  ? -51.280  104.741 55.856  1.00 151.83 ? 400  GLU B CA  1 
ATOM   17412 C  C   . GLU C 1 400  ? -50.354  103.651 55.316  1.00 146.81 ? 400  GLU B C   1 
ATOM   17413 O  O   . GLU C 1 400  ? -49.144  103.792 55.430  1.00 144.80 ? 400  GLU B O   1 
ATOM   17414 C  CB  . GLU C 1 400  ? -51.465  105.803 54.785  1.00 155.71 ? 400  GLU B CB  1 
ATOM   17415 C  CG  . GLU C 1 400  ? -52.775  105.710 54.051  1.00 160.36 ? 400  GLU B CG  1 
ATOM   17416 C  CD  . GLU C 1 400  ? -53.149  107.022 53.398  1.00 166.84 ? 400  GLU B CD  1 
ATOM   17417 O  OE1 . GLU C 1 400  ? -54.256  107.533 53.685  1.00 169.84 ? 400  GLU B OE1 1 
ATOM   17418 O  OE2 . GLU C 1 400  ? -52.324  107.550 52.614  1.00 168.85 ? 400  GLU B OE2 1 
ATOM   17419 N  N   . THR C 1 401  ? -50.891  102.569 54.739  1.00 142.05 ? 401  THR B N   1 
ATOM   17420 C  CA  . THR C 1 401  ? -50.025  101.529 54.155  1.00 134.93 ? 401  THR B CA  1 
ATOM   17421 C  C   . THR C 1 401  ? -49.897  101.638 52.665  1.00 129.60 ? 401  THR B C   1 
ATOM   17422 O  O   . THR C 1 401  ? -50.511  102.479 52.022  1.00 132.14 ? 401  THR B O   1 
ATOM   17423 C  CB  . THR C 1 401  ? -50.536  100.096 54.317  1.00 133.96 ? 401  THR B CB  1 
ATOM   17424 O  OG1 . THR C 1 401  ? -51.667  99.909  53.455  1.00 133.56 ? 401  THR B OG1 1 
ATOM   17425 C  CG2 . THR C 1 401  ? -50.873  99.762  55.754  1.00 136.05 ? 401  THR B CG2 1 
ATOM   17426 N  N   . SER C 1 402  ? -49.127  100.706 52.126  1.00 122.76 ? 402  SER B N   1 
ATOM   17427 C  CA  . SER C 1 402  ? -48.898  100.596 50.695  1.00 117.03 ? 402  SER B CA  1 
ATOM   17428 C  C   . SER C 1 402  ? -48.423  99.183  50.345  1.00 108.81 ? 402  SER B C   1 
ATOM   17429 O  O   . SER C 1 402  ? -47.400  98.717  50.839  1.00 105.12 ? 402  SER B O   1 
ATOM   17430 C  CB  . SER C 1 402  ? -47.865  101.635 50.257  1.00 117.47 ? 402  SER B CB  1 
ATOM   17431 O  OG  . SER C 1 402  ? -46.718  101.569 51.087  1.00 118.09 ? 402  SER B OG  1 
ATOM   17432 N  N   . ASP C 1 403  ? -49.181  98.494  49.506  1.00 106.35 ? 403  ASP B N   1 
ATOM   17433 C  CA  . ASP C 1 403  ? -48.740  97.200  49.035  1.00 103.62 ? 403  ASP B CA  1 
ATOM   17434 C  C   . ASP C 1 403  ? -48.049  97.304  47.691  1.00 100.48 ? 403  ASP B C   1 
ATOM   17435 O  O   . ASP C 1 403  ? -48.650  97.111  46.624  1.00 100.92 ? 403  ASP B O   1 
ATOM   17436 C  CB  . ASP C 1 403  ? -49.883  96.226  48.950  1.00 108.32 ? 403  ASP B CB  1 
ATOM   17437 C  CG  . ASP C 1 403  ? -49.964  95.348  50.161  1.00 112.14 ? 403  ASP B CG  1 
ATOM   17438 O  OD1 . ASP C 1 403  ? -48.982  94.570  50.437  1.00 109.05 ? 403  ASP B OD1 1 
ATOM   17439 O  OD2 . ASP C 1 403  ? -51.034  95.448  50.822  1.00 116.26 ? 403  ASP B OD2 1 
ATOM   17440 N  N   . LEU C 1 404  ? -46.761  97.591  47.764  1.00 96.54  ? 404  LEU B N   1 
ATOM   17441 C  CA  . LEU C 1 404  ? -45.892  97.669  46.606  1.00 92.80  ? 404  LEU B CA  1 
ATOM   17442 C  C   . LEU C 1 404  ? -46.193  96.681  45.476  1.00 94.26  ? 404  LEU B C   1 
ATOM   17443 O  O   . LEU C 1 404  ? -46.830  95.621  45.665  1.00 95.81  ? 404  LEU B O   1 
ATOM   17444 C  CB  . LEU C 1 404  ? -44.453  97.476  47.071  1.00 87.02  ? 404  LEU B CB  1 
ATOM   17445 C  CG  . LEU C 1 404  ? -43.996  98.718  47.816  1.00 85.14  ? 404  LEU B CG  1 
ATOM   17446 C  CD1 . LEU C 1 404  ? -42.531  98.624  48.166  1.00 80.86  ? 404  LEU B CD1 1 
ATOM   17447 C  CD2 . LEU C 1 404  ? -44.254  99.914  46.934  1.00 82.51  ? 404  LEU B CD2 1 
ATOM   17448 N  N   . ASP C 1 405  ? -45.730  97.057  44.289  1.00 91.05  ? 405  ASP B N   1 
ATOM   17449 C  CA  . ASP C 1 405  ? -45.729  96.158  43.161  1.00 87.14  ? 405  ASP B CA  1 
ATOM   17450 C  C   . ASP C 1 405  ? -44.418  95.405  43.251  1.00 82.27  ? 405  ASP B C   1 
ATOM   17451 O  O   . ASP C 1 405  ? -43.397  95.947  43.680  1.00 81.38  ? 405  ASP B O   1 
ATOM   17452 C  CB  . ASP C 1 405  ? -45.892  96.930  41.852  1.00 95.02  ? 405  ASP B CB  1 
ATOM   17453 C  CG  . ASP C 1 405  ? -47.369  97.143  41.471  1.00 106.24 ? 405  ASP B CG  1 
ATOM   17454 O  OD1 . ASP C 1 405  ? -48.074  96.105  41.492  1.00 109.50 ? 405  ASP B OD1 1 
ATOM   17455 O  OD2 . ASP C 1 405  ? -47.815  98.298  41.145  1.00 107.69 ? 405  ASP B OD2 1 
ATOM   17456 N  N   . PRO C 1 406  ? -44.452  94.123  42.898  1.00 80.15  ? 406  PRO B N   1 
ATOM   17457 C  CA  . PRO C 1 406  ? -43.370  93.160  43.103  1.00 79.10  ? 406  PRO B CA  1 
ATOM   17458 C  C   . PRO C 1 406  ? -42.406  93.341  42.021  1.00 82.66  ? 406  PRO B C   1 
ATOM   17459 O  O   . PRO C 1 406  ? -42.807  93.504  40.864  1.00 88.08  ? 406  PRO B O   1 
ATOM   17460 C  CB  . PRO C 1 406  ? -44.038  91.805  42.887  1.00 76.87  ? 406  PRO B CB  1 
ATOM   17461 C  CG  . PRO C 1 406  ? -45.484  92.084  42.743  1.00 80.05  ? 406  PRO B CG  1 
ATOM   17462 C  CD  . PRO C 1 406  ? -45.620  93.499  42.281  1.00 81.30  ? 406  PRO B CD  1 
ATOM   17463 N  N   . SER C 1 407  ? -41.140  93.310  42.366  1.00 83.97  ? 407  SER B N   1 
ATOM   17464 C  CA  . SER C 1 407  ? -40.132  93.515  41.356  1.00 87.11  ? 407  SER B CA  1 
ATOM   17465 C  C   . SER C 1 407  ? -39.443  92.185  41.197  1.00 86.67  ? 407  SER B C   1 
ATOM   17466 O  O   . SER C 1 407  ? -39.560  91.322  42.069  1.00 86.71  ? 407  SER B O   1 
ATOM   17467 C  CB  . SER C 1 407  ? -39.186  94.564  41.865  1.00 90.17  ? 407  SER B CB  1 
ATOM   17468 O  OG  . SER C 1 407  ? -39.800  95.109  43.028  1.00 93.02  ? 407  SER B OG  1 
ATOM   17469 N  N   . LYS C 1 408  ? -38.765  91.997  40.072  1.00 84.65  ? 408  LYS B N   1 
ATOM   17470 C  CA  . LYS C 1 408  ? -38.001  90.780  39.855  1.00 80.64  ? 408  LYS B CA  1 
ATOM   17471 C  C   . LYS C 1 408  ? -36.735  91.160  39.150  1.00 76.70  ? 408  LYS B C   1 
ATOM   17472 O  O   . LYS C 1 408  ? -36.741  91.990  38.251  1.00 77.61  ? 408  LYS B O   1 
ATOM   17473 C  CB  . LYS C 1 408  ? -38.764  89.784  38.998  1.00 80.17  ? 408  LYS B CB  1 
ATOM   17474 C  CG  . LYS C 1 408  ? -37.976  88.535  38.685  1.00 82.54  ? 408  LYS B CG  1 
ATOM   17475 C  CD  . LYS C 1 408  ? -38.877  87.496  38.026  1.00 86.31  ? 408  LYS B CD  1 
ATOM   17476 C  CE  . LYS C 1 408  ? -40.334  87.645  38.479  1.00 88.41  ? 408  LYS B CE  1 
ATOM   17477 N  NZ  . LYS C 1 408  ? -41.165  86.425  38.226  1.00 88.84  ? 408  LYS B NZ  1 
ATOM   17478 N  N   . SER C 1 409  ? -35.631  90.595  39.585  1.00 73.21  ? 409  SER B N   1 
ATOM   17479 C  CA  . SER C 1 409  ? -34.404  90.792  38.855  1.00 75.50  ? 409  SER B CA  1 
ATOM   17480 C  C   . SER C 1 409  ? -33.821  89.414  38.764  1.00 73.18  ? 409  SER B C   1 
ATOM   17481 O  O   . SER C 1 409  ? -34.498  88.409  39.054  1.00 69.33  ? 409  SER B O   1 
ATOM   17482 C  CB  . SER C 1 409  ? -33.437  91.776  39.549  1.00 79.01  ? 409  SER B CB  1 
ATOM   17483 O  OG  . SER C 1 409  ? -32.172  91.881  38.888  1.00 72.43  ? 409  SER B OG  1 
ATOM   17484 N  N   . VAL C 1 410  ? -32.574  89.359  38.334  1.00 72.13  ? 410  VAL B N   1 
ATOM   17485 C  CA  . VAL C 1 410  ? -31.934  88.087  38.263  1.00 73.81  ? 410  VAL B CA  1 
ATOM   17486 C  C   . VAL C 1 410  ? -30.521  88.170  38.764  1.00 78.83  ? 410  VAL B C   1 
ATOM   17487 O  O   . VAL C 1 410  ? -29.883  89.218  38.735  1.00 80.39  ? 410  VAL B O   1 
ATOM   17488 C  CB  . VAL C 1 410  ? -31.958  87.556  36.886  1.00 74.37  ? 410  VAL B CB  1 
ATOM   17489 C  CG1 . VAL C 1 410  ? -31.285  86.194  36.894  1.00 76.59  ? 410  VAL B CG1 1 
ATOM   17490 C  CG2 . VAL C 1 410  ? -33.407  87.464  36.430  1.00 73.38  ? 410  VAL B CG2 1 
ATOM   17491 N  N   . THR C 1 411  ? -30.057  87.042  39.268  1.00 79.31  ? 411  THR B N   1 
ATOM   17492 C  CA  . THR C 1 411  ? -28.886  87.024  40.096  1.00 78.71  ? 411  THR B CA  1 
ATOM   17493 C  C   . THR C 1 411  ? -27.740  87.096  39.139  1.00 76.45  ? 411  THR B C   1 
ATOM   17494 O  O   . THR C 1 411  ? -27.711  86.328  38.206  1.00 73.17  ? 411  THR B O   1 
ATOM   17495 C  CB  . THR C 1 411  ? -28.909  85.742  40.969  1.00 79.75  ? 411  THR B CB  1 
ATOM   17496 O  OG1 . THR C 1 411  ? -27.875  85.780  41.947  1.00 82.95  ? 411  THR B OG1 1 
ATOM   17497 C  CG2 . THR C 1 411  ? -28.722  84.561  40.133  1.00 78.09  ? 411  THR B CG2 1 
ATOM   17498 N  N   . ARG C 1 412  ? -26.828  88.044  39.339  1.00 82.86  ? 412  ARG B N   1 
ATOM   17499 C  CA  . ARG C 1 412  ? -25.714  88.224  38.408  1.00 93.14  ? 412  ARG B CA  1 
ATOM   17500 C  C   . ARG C 1 412  ? -24.901  86.952  38.256  1.00 94.61  ? 412  ARG B C   1 
ATOM   17501 O  O   . ARG C 1 412  ? -25.039  86.052  39.056  1.00 95.91  ? 412  ARG B O   1 
ATOM   17502 C  CB  . ARG C 1 412  ? -24.807  89.368  38.833  1.00 104.26 ? 412  ARG B CB  1 
ATOM   17503 C  CG  . ARG C 1 412  ? -23.728  89.665  37.804  1.00 115.46 ? 412  ARG B CG  1 
ATOM   17504 C  CD  . ARG C 1 412  ? -22.870  90.850  38.205  1.00 125.57 ? 412  ARG B CD  1 
ATOM   17505 N  NE  . ARG C 1 412  ? -23.297  92.103  37.594  1.00 133.32 ? 412  ARG B NE  1 
ATOM   17506 C  CZ  . ARG C 1 412  ? -22.624  93.245  37.721  1.00 140.20 ? 412  ARG B CZ  1 
ATOM   17507 N  NH1 . ARG C 1 412  ? -21.500  93.277  38.438  1.00 142.55 ? 412  ARG B NH1 1 
ATOM   17508 N  NH2 . ARG C 1 412  ? -23.067  94.354  37.136  1.00 142.78 ? 412  ARG B NH2 1 
ATOM   17509 N  N   . VAL C 1 413  ? -24.064  86.862  37.231  1.00 96.90  ? 413  VAL B N   1 
ATOM   17510 C  CA  . VAL C 1 413  ? -23.339  85.620  36.958  1.00 99.30  ? 413  VAL B CA  1 
ATOM   17511 C  C   . VAL C 1 413  ? -22.018  85.507  37.704  1.00 101.27 ? 413  VAL B C   1 
ATOM   17512 O  O   . VAL C 1 413  ? -21.654  84.442  38.194  1.00 101.61 ? 413  VAL B O   1 
ATOM   17513 C  CB  . VAL C 1 413  ? -23.049  85.492  35.470  1.00 101.74 ? 413  VAL B CB  1 
ATOM   17514 C  CG1 . VAL C 1 413  ? -22.541  84.089  35.138  1.00 102.24 ? 413  VAL B CG1 1 
ATOM   17515 C  CG2 . VAL C 1 413  ? -24.295  85.849  34.671  1.00 102.10 ? 413  VAL B CG2 1 
ATOM   17516 N  N   . ASP C 1 414  ? -21.295  86.617  37.753  1.00 103.70 ? 414  ASP B N   1 
ATOM   17517 C  CA  . ASP C 1 414  ? -19.981  86.702  38.379  1.00 105.32 ? 414  ASP B CA  1 
ATOM   17518 C  C   . ASP C 1 414  ? -20.155  87.049  39.823  1.00 101.35 ? 414  ASP B C   1 
ATOM   17519 O  O   . ASP C 1 414  ? -19.216  86.989  40.601  1.00 101.53 ? 414  ASP B O   1 
ATOM   17520 C  CB  . ASP C 1 414  ? -19.222  87.881  37.787  1.00 111.35 ? 414  ASP B CB  1 
ATOM   17521 C  CG  . ASP C 1 414  ? -20.032  89.175  37.855  1.00 114.50 ? 414  ASP B CG  1 
ATOM   17522 O  OD1 . ASP C 1 414  ? -20.962  89.329  37.030  1.00 115.07 ? 414  ASP B OD1 1 
ATOM   17523 O  OD2 . ASP C 1 414  ? -19.761  90.026  38.735  1.00 116.19 ? 414  ASP B OD2 1 
ATOM   17524 N  N   . ASP C 1 415  ? -21.362  87.478  40.152  1.00 98.29  ? 415  ASP B N   1 
ATOM   17525 C  CA  . ASP C 1 415  ? -21.611  88.211  41.371  1.00 97.82  ? 415  ASP B CA  1 
ATOM   17526 C  C   . ASP C 1 415  ? -22.295  87.303  42.365  1.00 87.92  ? 415  ASP B C   1 
ATOM   17527 O  O   . ASP C 1 415  ? -21.996  87.327  43.551  1.00 85.68  ? 415  ASP B O   1 
ATOM   17528 C  CB  . ASP C 1 415  ? -22.506  89.403  41.031  1.00 105.02 ? 415  ASP B CB  1 
ATOM   17529 C  CG  . ASP C 1 415  ? -22.520  90.450  42.109  1.00 112.29 ? 415  ASP B CG  1 
ATOM   17530 O  OD1 . ASP C 1 415  ? -21.885  90.171  43.149  1.00 116.06 ? 415  ASP B OD1 1 
ATOM   17531 O  OD2 . ASP C 1 415  ? -23.163  91.529  41.929  1.00 113.01 ? 415  ASP B OD2 1 
ATOM   17532 N  N   . GLY C 1 416  ? -23.199  86.483  41.847  1.00 82.90  ? 416  GLY B N   1 
ATOM   17533 C  CA  . GLY C 1 416  ? -24.135  85.723  42.641  1.00 80.45  ? 416  GLY B CA  1 
ATOM   17534 C  C   . GLY C 1 416  ? -25.218  86.632  43.195  1.00 82.20  ? 416  GLY B C   1 
ATOM   17535 O  O   . GLY C 1 416  ? -26.114  86.178  43.893  1.00 85.36  ? 416  GLY B O   1 
ATOM   17536 N  N   . VAL C 1 417  ? -25.153  87.922  42.899  1.00 81.07  ? 417  VAL B N   1 
ATOM   17537 C  CA  . VAL C 1 417  ? -26.048  88.874  43.548  1.00 81.04  ? 417  VAL B CA  1 
ATOM   17538 C  C   . VAL C 1 417  ? -27.238  89.290  42.714  1.00 79.15  ? 417  VAL B C   1 
ATOM   17539 O  O   . VAL C 1 417  ? -27.111  89.563  41.525  1.00 78.93  ? 417  VAL B O   1 
ATOM   17540 C  CB  . VAL C 1 417  ? -25.306  90.159  43.872  1.00 87.10  ? 417  VAL B CB  1 
ATOM   17541 C  CG1 . VAL C 1 417  ? -26.299  91.284  44.088  1.00 87.44  ? 417  VAL B CG1 1 
ATOM   17542 C  CG2 . VAL C 1 417  ? -24.367  89.963  45.077  1.00 89.66  ? 417  VAL B CG2 1 
ATOM   17543 N  N   . ALA C 1 418  ? -28.397  89.369  43.336  1.00 79.65  ? 418  ALA B N   1 
ATOM   17544 C  CA  . ALA C 1 418  ? -29.547  89.904  42.650  1.00 81.01  ? 418  ALA B CA  1 
ATOM   17545 C  C   . ALA C 1 418  ? -29.891  91.231  43.267  1.00 82.33  ? 418  ALA B C   1 
ATOM   17546 O  O   . ALA C 1 418  ? -30.533  91.263  44.301  1.00 81.67  ? 418  ALA B O   1 
ATOM   17547 C  CB  . ALA C 1 418  ? -30.709  88.956  42.809  1.00 81.06  ? 418  ALA B CB  1 
ATOM   17548 N  N   . SER C 1 419  ? -29.490  92.326  42.632  1.00 84.74  ? 419  SER B N   1 
ATOM   17549 C  CA  . SER C 1 419  ? -29.623  93.667  43.234  1.00 86.96  ? 419  SER B CA  1 
ATOM   17550 C  C   . SER C 1 419  ? -30.964  94.364  42.983  1.00 83.33  ? 419  SER B C   1 
ATOM   17551 O  O   . SER C 1 419  ? -31.392  94.488  41.845  1.00 83.67  ? 419  SER B O   1 
ATOM   17552 C  CB  . SER C 1 419  ? -28.492  94.598  42.733  1.00 91.71  ? 419  SER B CB  1 
ATOM   17553 O  OG  . SER C 1 419  ? -27.343  93.879  42.261  1.00 93.31  ? 419  SER B OG  1 
ATOM   17554 N  N   . PHE C 1 420  ? -31.620  94.850  44.023  1.00 82.87  ? 420  PHE B N   1 
ATOM   17555 C  CA  . PHE C 1 420  ? -32.787  95.713  43.788  1.00 86.60  ? 420  PHE B CA  1 
ATOM   17556 C  C   . PHE C 1 420  ? -32.641  97.192  44.184  1.00 95.08  ? 420  PHE B C   1 
ATOM   17557 O  O   . PHE C 1 420  ? -31.590  97.623  44.671  1.00 99.71  ? 420  PHE B O   1 
ATOM   17558 C  CB  . PHE C 1 420  ? -34.001  95.187  44.508  1.00 82.55  ? 420  PHE B CB  1 
ATOM   17559 C  CG  . PHE C 1 420  ? -34.372  93.856  44.104  1.00 73.66  ? 420  PHE B CG  1 
ATOM   17560 C  CD1 . PHE C 1 420  ? -35.625  93.595  43.627  1.00 73.10  ? 420  PHE B CD1 1 
ATOM   17561 C  CD2 . PHE C 1 420  ? -33.467  92.850  44.195  1.00 72.98  ? 420  PHE B CD2 1 
ATOM   17562 C  CE1 . PHE C 1 420  ? -35.978  92.331  43.258  1.00 73.90  ? 420  PHE B CE1 1 
ATOM   17563 C  CE2 . PHE C 1 420  ? -33.813  91.589  43.845  1.00 75.40  ? 420  PHE B CE2 1 
ATOM   17564 C  CZ  . PHE C 1 420  ? -35.074  91.327  43.366  1.00 73.89  ? 420  PHE B CZ  1 
ATOM   17565 N  N   . VAL C 1 421  ? -33.717  97.951  43.954  1.00 90.50  ? 421  VAL B N   1 
ATOM   17566 C  CA  . VAL C 1 421  ? -33.879  99.278  44.525  1.00 87.12  ? 421  VAL B CA  1 
ATOM   17567 C  C   . VAL C 1 421  ? -35.307  99.699  44.379  1.00 87.19  ? 421  VAL B C   1 
ATOM   17568 O  O   . VAL C 1 421  ? -35.893  99.544  43.315  1.00 89.03  ? 421  VAL B O   1 
ATOM   17569 C  CB  . VAL C 1 421  ? -33.049  100.340 43.812  1.00 84.85  ? 421  VAL B CB  1 
ATOM   17570 C  CG1 . VAL C 1 421  ? -33.800  101.689 43.803  1.00 85.38  ? 421  VAL B CG1 1 
ATOM   17571 C  CG2 . VAL C 1 421  ? -31.693  100.471 44.462  1.00 84.06  ? 421  VAL B CG2 1 
ATOM   17572 N  N   . LEU C 1 422  ? -35.868  100.232 45.456  1.00 86.59  ? 422  LEU B N   1 
ATOM   17573 C  CA  . LEU C 1 422  ? -37.209  100.773 45.431  1.00 88.77  ? 422  LEU B CA  1 
ATOM   17574 C  C   . LEU C 1 422  ? -37.085  102.181 45.901  1.00 93.05  ? 422  LEU B C   1 
ATOM   17575 O  O   . LEU C 1 422  ? -36.263  102.471 46.765  1.00 94.58  ? 422  LEU B O   1 
ATOM   17576 C  CB  . LEU C 1 422  ? -38.192  99.975  46.312  1.00 86.53  ? 422  LEU B CB  1 
ATOM   17577 C  CG  . LEU C 1 422  ? -37.723  98.770  47.108  1.00 79.71  ? 422  LEU B CG  1 
ATOM   17578 C  CD1 . LEU C 1 422  ? -37.087  99.257  48.344  1.00 80.94  ? 422  LEU B CD1 1 
ATOM   17579 C  CD2 . LEU C 1 422  ? -38.887  97.887  47.403  1.00 78.80  ? 422  LEU B CD2 1 
ATOM   17580 N  N   . ASN C 1 423  ? -37.875  103.063 45.299  1.00 97.48  ? 423  ASN B N   1 
ATOM   17581 C  CA  . ASN C 1 423  ? -37.816  104.485 45.631  1.00 100.42 ? 423  ASN B CA  1 
ATOM   17582 C  C   . ASN C 1 423  ? -38.883  104.859 46.643  1.00 99.53  ? 423  ASN B C   1 
ATOM   17583 O  O   . ASN C 1 423  ? -40.075  104.752 46.376  1.00 97.97  ? 423  ASN B O   1 
ATOM   17584 C  CB  . ASN C 1 423  ? -37.830  105.333 44.360  1.00 99.56  ? 423  ASN B CB  1 
ATOM   17585 C  CG  . ASN C 1 423  ? -36.816  104.838 43.377  1.00 98.96  ? 423  ASN B CG  1 
ATOM   17586 O  OD1 . ASN C 1 423  ? -35.844  105.523 43.081  1.00 100.89 ? 423  ASN B OD1 1 
ATOM   17587 N  ND2 . ASN C 1 423  ? -36.985  103.590 42.930  1.00 95.83  ? 423  ASN B ND2 1 
ATOM   17588 N  N   . LEU C 1 424  ? -38.438  105.272 47.820  1.00 100.89 ? 424  LEU B N   1 
ATOM   17589 C  CA  . LEU C 1 424  ? -39.341  105.329 48.945  1.00 102.20 ? 424  LEU B CA  1 
ATOM   17590 C  C   . LEU C 1 424  ? -39.915  106.708 49.299  1.00 106.22 ? 424  LEU B C   1 
ATOM   17591 O  O   . LEU C 1 424  ? -39.182  107.687 49.517  1.00 107.72 ? 424  LEU B O   1 
ATOM   17592 C  CB  . LEU C 1 424  ? -38.711  104.624 50.135  1.00 101.16 ? 424  LEU B CB  1 
ATOM   17593 C  CG  . LEU C 1 424  ? -38.967  103.136 49.958  1.00 99.05  ? 424  LEU B CG  1 
ATOM   17594 C  CD1 . LEU C 1 424  ? -38.788  102.379 51.249  1.00 100.34 ? 424  LEU B CD1 1 
ATOM   17595 C  CD2 . LEU C 1 424  ? -40.370  102.933 49.458  1.00 98.02  ? 424  LEU B CD2 1 
ATOM   17596 N  N   . PRO C 1 425  ? -41.245  106.773 49.361  1.00 106.55 ? 425  PRO B N   1 
ATOM   17597 C  CA  . PRO C 1 425  ? -41.914  108.041 49.597  1.00 112.32 ? 425  PRO B CA  1 
ATOM   17598 C  C   . PRO C 1 425  ? -41.401  108.638 50.881  1.00 119.66 ? 425  PRO B C   1 
ATOM   17599 O  O   . PRO C 1 425  ? -41.719  108.104 51.922  1.00 123.75 ? 425  PRO B O   1 
ATOM   17600 C  CB  . PRO C 1 425  ? -43.366  107.624 49.754  1.00 111.13 ? 425  PRO B CB  1 
ATOM   17601 C  CG  . PRO C 1 425  ? -43.463  106.306 49.033  1.00 106.29 ? 425  PRO B CG  1 
ATOM   17602 C  CD  . PRO C 1 425  ? -42.185  105.643 49.299  1.00 103.72 ? 425  PRO B CD  1 
ATOM   17603 N  N   . SER C 1 426  ? -40.621  109.709 50.813  1.00 122.83 ? 426  SER B N   1 
ATOM   17604 C  CA  . SER C 1 426  ? -40.135  110.402 52.013  1.00 127.89 ? 426  SER B CA  1 
ATOM   17605 C  C   . SER C 1 426  ? -40.852  110.042 53.349  1.00 135.67 ? 426  SER B C   1 
ATOM   17606 O  O   . SER C 1 426  ? -40.214  109.611 54.319  1.00 133.47 ? 426  SER B O   1 
ATOM   17607 C  CB  . SER C 1 426  ? -40.144  111.924 51.767  1.00 132.78 ? 426  SER B CB  1 
ATOM   17608 O  OG  . SER C 1 426  ? -40.942  112.271 50.632  1.00 133.73 ? 426  SER B OG  1 
ATOM   17609 N  N   . GLY C 1 427  ? -42.170  110.194 53.390  1.00 137.55 ? 427  GLY B N   1 
ATOM   17610 C  CA  . GLY C 1 427  ? -42.933  109.818 54.570  1.00 139.32 ? 427  GLY B CA  1 
ATOM   17611 C  C   . GLY C 1 427  ? -43.006  108.327 54.914  1.00 135.28 ? 427  GLY B C   1 
ATOM   17612 O  O   . GLY C 1 427  ? -43.961  107.854 55.542  1.00 135.48 ? 427  GLY B O   1 
ATOM   17613 N  N   . VAL C 1 428  ? -42.002  107.568 54.506  1.00 130.41 ? 428  VAL B N   1 
ATOM   17614 C  CA  . VAL C 1 428  ? -42.000  106.151 54.810  1.00 124.94 ? 428  VAL B CA  1 
ATOM   17615 C  C   . VAL C 1 428  ? -41.210  105.949 56.080  1.00 123.06 ? 428  VAL B C   1 
ATOM   17616 O  O   . VAL C 1 428  ? -40.396  106.802 56.444  1.00 124.85 ? 428  VAL B O   1 
ATOM   17617 C  CB  . VAL C 1 428  ? -41.361  105.351 53.706  1.00 122.92 ? 428  VAL B CB  1 
ATOM   17618 C  CG1 . VAL C 1 428  ? -39.866  105.589 53.727  1.00 123.72 ? 428  VAL B CG1 1 
ATOM   17619 C  CG2 . VAL C 1 428  ? -41.686  103.876 53.868  1.00 120.38 ? 428  VAL B CG2 1 
ATOM   17620 N  N   . THR C 1 429  ? -41.396  104.781 56.694  1.00 119.48 ? 429  THR B N   1 
ATOM   17621 C  CA  . THR C 1 429  ? -41.165  104.575 58.123  1.00 117.30 ? 429  THR B CA  1 
ATOM   17622 C  C   . THR C 1 429  ? -40.513  103.222 58.452  1.00 110.88 ? 429  THR B C   1 
ATOM   17623 O  O   . THR C 1 429  ? -39.323  103.121 58.801  1.00 107.17 ? 429  THR B O   1 
ATOM   17624 C  CB  . THR C 1 429  ? -42.548  104.552 58.823  1.00 128.98 ? 429  THR B CB  1 
ATOM   17625 O  OG1 . THR C 1 429  ? -43.330  103.452 58.309  1.00 127.91 ? 429  THR B OG1 1 
ATOM   17626 C  CG2 . THR C 1 429  ? -43.307  105.839 58.536  1.00 130.89 ? 429  THR B CG2 1 
ATOM   17627 N  N   . VAL C 1 430  ? -41.368  102.203 58.416  1.00 107.17 ? 430  VAL B N   1 
ATOM   17628 C  CA  . VAL C 1 430  ? -40.993  100.817 58.373  1.00 101.92 ? 430  VAL B CA  1 
ATOM   17629 C  C   . VAL C 1 430  ? -41.388  100.373 56.974  1.00 103.00 ? 430  VAL B C   1 
ATOM   17630 O  O   . VAL C 1 430  ? -42.524  100.618 56.525  1.00 103.37 ? 430  VAL B O   1 
ATOM   17631 C  CB  . VAL C 1 430  ? -41.831  99.999  59.331  1.00 97.57  ? 430  VAL B CB  1 
ATOM   17632 C  CG1 . VAL C 1 430  ? -41.308  98.579  59.444  1.00 93.33  ? 430  VAL B CG1 1 
ATOM   17633 C  CG2 . VAL C 1 430  ? -41.841  100.636 60.642  1.00 98.78  ? 430  VAL B CG2 1 
ATOM   17634 N  N   . LEU C 1 431  ? -40.416  99.754  56.302  1.00 100.80 ? 431  LEU B N   1 
ATOM   17635 C  CA  . LEU C 1 431  ? -40.590  98.931  55.114  1.00 94.06  ? 431  LEU B CA  1 
ATOM   17636 C  C   . LEU C 1 431  ? -40.409  97.443  55.511  1.00 94.01  ? 431  LEU B C   1 
ATOM   17637 O  O   . LEU C 1 431  ? -39.434  97.083  56.179  1.00 84.03  ? 431  LEU B O   1 
ATOM   17638 C  CB  . LEU C 1 431  ? -39.524  99.358  54.115  1.00 89.06  ? 431  LEU B CB  1 
ATOM   17639 C  CG  . LEU C 1 431  ? -39.433  98.916  52.664  1.00 85.88  ? 431  LEU B CG  1 
ATOM   17640 C  CD1 . LEU C 1 431  ? -37.976  98.659  52.428  1.00 82.71  ? 431  LEU B CD1 1 
ATOM   17641 C  CD2 . LEU C 1 431  ? -40.241  97.681  52.372  1.00 84.06  ? 431  LEU B CD2 1 
ATOM   17642 N  N   . GLU C 1 432  ? -41.342  96.586  55.115  1.00 91.74  ? 432  GLU B N   1 
ATOM   17643 C  CA  . GLU C 1 432  ? -41.181  95.156  55.344  1.00 91.64  ? 432  GLU B CA  1 
ATOM   17644 C  C   . GLU C 1 432  ? -40.960  94.350  54.041  1.00 91.76  ? 432  GLU B C   1 
ATOM   17645 O  O   . GLU C 1 432  ? -41.864  94.288  53.209  1.00 95.07  ? 432  GLU B O   1 
ATOM   17646 C  CB  . GLU C 1 432  ? -42.432  94.634  56.035  1.00 92.86  ? 432  GLU B CB  1 
ATOM   17647 C  CG  . GLU C 1 432  ? -42.654  95.185  57.434  1.00 98.99  ? 432  GLU B CG  1 
ATOM   17648 C  CD  . GLU C 1 432  ? -41.928  94.395  58.528  1.00 101.89 ? 432  GLU B CD  1 
ATOM   17649 O  OE1 . GLU C 1 432  ? -41.262  93.365  58.231  1.00 97.45  ? 432  GLU B OE1 1 
ATOM   17650 O  OE2 . GLU C 1 432  ? -42.039  94.829  59.697  1.00 106.72 ? 432  GLU B OE2 1 
ATOM   17651 N  N   . PHE C 1 433  ? -39.807  93.708  53.832  1.00 86.67  ? 433  PHE B N   1 
ATOM   17652 C  CA  . PHE C 1 433  ? -39.688  92.907  52.601  1.00 83.86  ? 433  PHE B CA  1 
ATOM   17653 C  C   . PHE C 1 433  ? -39.500  91.386  52.700  1.00 87.33  ? 433  PHE B C   1 
ATOM   17654 O  O   . PHE C 1 433  ? -38.846  90.873  53.609  1.00 89.43  ? 433  PHE B O   1 
ATOM   17655 C  CB  . PHE C 1 433  ? -38.743  93.533  51.570  1.00 80.13  ? 433  PHE B CB  1 
ATOM   17656 C  CG  . PHE C 1 433  ? -37.338  93.741  52.044  1.00 80.03  ? 433  PHE B CG  1 
ATOM   17657 C  CD1 . PHE C 1 433  ? -37.005  94.859  52.801  1.00 81.59  ? 433  PHE B CD1 1 
ATOM   17658 C  CD2 . PHE C 1 433  ? -36.330  92.862  51.671  1.00 75.59  ? 433  PHE B CD2 1 
ATOM   17659 C  CE1 . PHE C 1 433  ? -35.691  95.076  53.221  1.00 78.95  ? 433  PHE B CE1 1 
ATOM   17660 C  CE2 . PHE C 1 433  ? -35.025  93.063  52.083  1.00 76.12  ? 433  PHE B CE2 1 
ATOM   17661 C  CZ  . PHE C 1 433  ? -34.703  94.170  52.867  1.00 77.81  ? 433  PHE B CZ  1 
ATOM   17662 N  N   . ASN C 1 434  ? -40.140  90.681  51.768  1.00 87.95  ? 434  ASN B N   1 
ATOM   17663 C  CA  . ASN C 1 434  ? -39.918  89.253  51.511  1.00 86.88  ? 434  ASN B CA  1 
ATOM   17664 C  C   . ASN C 1 434  ? -39.210  89.116  50.181  1.00 90.48  ? 434  ASN B C   1 
ATOM   17665 O  O   . ASN C 1 434  ? -39.450  89.898  49.260  1.00 91.77  ? 434  ASN B O   1 
ATOM   17666 C  CB  . ASN C 1 434  ? -41.236  88.536  51.357  1.00 82.22  ? 434  ASN B CB  1 
ATOM   17667 C  CG  . ASN C 1 434  ? -42.114  88.708  52.539  1.00 81.95  ? 434  ASN B CG  1 
ATOM   17668 O  OD1 . ASN C 1 434  ? -41.775  88.265  53.636  1.00 79.26  ? 434  ASN B OD1 1 
ATOM   17669 N  ND2 . ASN C 1 434  ? -43.280  89.319  52.328  1.00 82.67  ? 434  ASN B ND2 1 
ATOM   17670 N  N   . VAL C 1 435  ? -38.394  88.089  50.035  1.00 89.95  ? 435  VAL B N   1 
ATOM   17671 C  CA  . VAL C 1 435  ? -37.501  88.042  48.907  1.00 90.27  ? 435  VAL B CA  1 
ATOM   17672 C  C   . VAL C 1 435  ? -37.464  86.601  48.544  1.00 85.75  ? 435  VAL B C   1 
ATOM   17673 O  O   . VAL C 1 435  ? -37.235  85.771  49.408  1.00 90.78  ? 435  VAL B O   1 
ATOM   17674 C  CB  . VAL C 1 435  ? -36.105  88.491  49.345  1.00 70.83  ? 435  VAL B CB  1 
ATOM   17675 C  CG1 . VAL C 1 435  ? -35.063  87.664  48.716  1.00 70.11  ? 435  VAL B CG1 1 
ATOM   17676 C  CG2 . VAL C 1 435  ? -35.885  89.908  49.013  1.00 71.69  ? 435  VAL B CG2 1 
ATOM   17677 N  N   . LYS C 1 436  ? -37.713  86.263  47.290  1.00 80.84  ? 436  LYS B N   1 
ATOM   17678 C  CA  . LYS C 1 436  ? -37.588  84.861  46.950  1.00 77.87  ? 436  LYS B CA  1 
ATOM   17679 C  C   . LYS C 1 436  ? -36.997  84.574  45.594  1.00 78.23  ? 436  LYS B C   1 
ATOM   17680 O  O   . LYS C 1 436  ? -36.891  85.485  44.760  1.00 80.34  ? 436  LYS B O   1 
ATOM   17681 C  CB  . LYS C 1 436  ? -38.917  84.131  47.120  1.00 71.96  ? 436  LYS B CB  1 
ATOM   17682 C  CG  . LYS C 1 436  ? -39.947  84.362  46.050  1.00 68.02  ? 436  LYS B CG  1 
ATOM   17683 C  CD  . LYS C 1 436  ? -40.761  83.063  45.792  1.00 85.95  ? 436  LYS B CD  1 
ATOM   17684 C  CE  . LYS C 1 436  ? -42.241  83.303  45.308  1.00 91.76  ? 436  LYS B CE  1 
ATOM   17685 N  NZ  . LYS C 1 436  ? -43.363  83.266  46.357  1.00 90.69  ? 436  LYS B NZ  1 
ATOM   17686 N  N   . THR C 1 437  ? -36.591  83.306  45.409  1.00 76.98  ? 437  THR B N   1 
ATOM   17687 C  CA  . THR C 1 437  ? -36.205  82.767  44.106  1.00 80.49  ? 437  THR B CA  1 
ATOM   17688 C  C   . THR C 1 437  ? -37.417  82.374  43.310  1.00 78.84  ? 437  THR B C   1 
ATOM   17689 O  O   . THR C 1 437  ? -38.367  81.770  43.839  1.00 77.50  ? 437  THR B O   1 
ATOM   17690 C  CB  . THR C 1 437  ? -35.386  81.499  44.198  1.00 67.24  ? 437  THR B CB  1 
ATOM   17691 O  OG1 . THR C 1 437  ? -36.062  80.556  45.018  1.00 66.49  ? 437  THR B OG1 1 
ATOM   17692 C  CG2 . THR C 1 437  ? -34.030  81.781  44.721  1.00 66.83  ? 437  THR B CG2 1 
ATOM   17693 N  N   . ASP C 1 438  ? -37.376  82.706  42.025  1.00 86.24  ? 438  ASP B N   1 
ATOM   17694 C  CA  . ASP C 1 438  ? -38.406  82.203  41.144  1.00 95.73  ? 438  ASP B CA  1 
ATOM   17695 C  C   . ASP C 1 438  ? -37.957  81.155  40.112  1.00 94.75  ? 438  ASP B C   1 
ATOM   17696 O  O   . ASP C 1 438  ? -38.476  81.108  38.998  1.00 93.38  ? 438  ASP B O   1 
ATOM   17697 C  CB  . ASP C 1 438  ? -39.201  83.329  40.509  1.00 102.36 ? 438  ASP B CB  1 
ATOM   17698 C  CG  . ASP C 1 438  ? -40.677  83.168  40.751  1.00 109.64 ? 438  ASP B CG  1 
ATOM   17699 O  OD1 . ASP C 1 438  ? -41.035  82.269  41.575  1.00 111.10 ? 438  ASP B OD1 1 
ATOM   17700 O  OD2 . ASP C 1 438  ? -41.460  83.938  40.139  1.00 112.50 ? 438  ASP B OD2 1 
ATOM   17701 N  N   . ALA C 1 439  ? -37.018  80.301  40.506  1.00 96.35  ? 439  ALA B N   1 
ATOM   17702 C  CA  . ALA C 1 439  ? -36.774  79.057  39.805  1.00 99.53  ? 439  ALA B CA  1 
ATOM   17703 C  C   . ALA C 1 439  ? -38.035  78.642  39.087  1.00 100.21 ? 439  ALA B C   1 
ATOM   17704 O  O   . ALA C 1 439  ? -39.080  78.439  39.691  1.00 103.45 ? 439  ALA B O   1 
ATOM   17705 C  CB  . ALA C 1 439  ? -36.374  77.994  40.782  1.00 101.05 ? 439  ALA B CB  1 
ATOM   17706 N  N   . PRO C 1 440  ? -37.933  78.499  37.778  1.00 99.34  ? 440  PRO B N   1 
ATOM   17707 C  CA  . PRO C 1 440  ? -39.108  78.283  36.949  1.00 95.10  ? 440  PRO B CA  1 
ATOM   17708 C  C   . PRO C 1 440  ? -39.466  76.830  37.045  1.00 92.52  ? 440  PRO B C   1 
ATOM   17709 O  O   . PRO C 1 440  ? -40.623  76.473  36.821  1.00 92.47  ? 440  PRO B O   1 
ATOM   17710 C  CB  . PRO C 1 440  ? -38.590  78.583  35.545  1.00 96.46  ? 440  PRO B CB  1 
ATOM   17711 C  CG  . PRO C 1 440  ? -37.025  78.821  35.700  1.00 103.26 ? 440  PRO B CG  1 
ATOM   17712 C  CD  . PRO C 1 440  ? -36.682  78.295  37.033  1.00 101.44 ? 440  PRO B CD  1 
ATOM   17713 N  N   . ASP C 1 441  ? -38.458  76.026  37.380  1.00 90.44  ? 441  ASP B N   1 
ATOM   17714 C  CA  . ASP C 1 441  ? -38.537  74.579  37.482  1.00 92.88  ? 441  ASP B CA  1 
ATOM   17715 C  C   . ASP C 1 441  ? -38.545  74.167  38.941  1.00 88.99  ? 441  ASP B C   1 
ATOM   17716 O  O   . ASP C 1 441  ? -38.660  72.995  39.254  1.00 88.35  ? 441  ASP B O   1 
ATOM   17717 C  CB  . ASP C 1 441  ? -37.293  73.994  36.871  1.00 101.81 ? 441  ASP B CB  1 
ATOM   17718 C  CG  . ASP C 1 441  ? -36.048  74.592  37.480  1.00 109.92 ? 441  ASP B CG  1 
ATOM   17719 O  OD1 . ASP C 1 441  ? -35.030  73.877  37.605  1.00 115.73 ? 441  ASP B OD1 1 
ATOM   17720 O  OD2 . ASP C 1 441  ? -36.103  75.778  37.871  1.00 109.09 ? 441  ASP B OD2 1 
ATOM   17721 N  N   . LEU C 1 442  ? -38.375  75.115  39.851  1.00 86.73  ? 442  LEU B N   1 
ATOM   17722 C  CA  . LEU C 1 442  ? -38.651  74.802  41.253  1.00 83.07  ? 442  LEU B CA  1 
ATOM   17723 C  C   . LEU C 1 442  ? -40.128  74.974  41.558  1.00 83.37  ? 442  LEU B C   1 
ATOM   17724 O  O   . LEU C 1 442  ? -40.723  75.996  41.179  1.00 85.10  ? 442  LEU B O   1 
ATOM   17725 C  CB  . LEU C 1 442  ? -37.812  75.642  42.206  1.00 76.47  ? 442  LEU B CB  1 
ATOM   17726 C  CG  . LEU C 1 442  ? -36.620  74.813  42.638  1.00 72.20  ? 442  LEU B CG  1 
ATOM   17727 C  CD1 . LEU C 1 442  ? -35.936  75.410  43.850  1.00 70.79  ? 442  LEU B CD1 1 
ATOM   17728 C  CD2 . LEU C 1 442  ? -37.084  73.386  42.889  1.00 69.63  ? 442  LEU B CD2 1 
ATOM   17729 N  N   . PRO C 1 443  ? -40.724  73.988  42.254  1.00 81.80  ? 443  PRO B N   1 
ATOM   17730 C  CA  . PRO C 1 443  ? -42.133  74.052  42.619  1.00 83.71  ? 443  PRO B CA  1 
ATOM   17731 C  C   . PRO C 1 443  ? -42.271  75.094  43.710  1.00 92.11  ? 443  PRO B C   1 
ATOM   17732 O  O   . PRO C 1 443  ? -41.271  75.383  44.381  1.00 94.27  ? 443  PRO B O   1 
ATOM   17733 C  CB  . PRO C 1 443  ? -42.417  72.665  43.171  1.00 79.40  ? 443  PRO B CB  1 
ATOM   17734 C  CG  . PRO C 1 443  ? -41.206  71.907  42.963  1.00 79.25  ? 443  PRO B CG  1 
ATOM   17735 C  CD  . PRO C 1 443  ? -40.089  72.853  42.909  1.00 79.13  ? 443  PRO B CD  1 
ATOM   17736 N  N   . GLU C 1 444  ? -43.463  75.663  43.879  1.00 96.16  ? 444  GLU B N   1 
ATOM   17737 C  CA  . GLU C 1 444  ? -43.567  76.859  44.686  1.00 99.01  ? 444  GLU B CA  1 
ATOM   17738 C  C   . GLU C 1 444  ? -42.992  76.636  46.060  1.00 92.03  ? 444  GLU B C   1 
ATOM   17739 O  O   . GLU C 1 444  ? -42.111  77.374  46.479  1.00 86.42  ? 444  GLU B O   1 
ATOM   17740 C  CB  . GLU C 1 444  ? -44.998  77.341  44.780  1.00 113.27 ? 444  GLU B CB  1 
ATOM   17741 C  CG  . GLU C 1 444  ? -45.082  78.876  44.760  1.00 126.46 ? 444  GLU B CG  1 
ATOM   17742 C  CD  . GLU C 1 444  ? -44.510  79.545  46.023  1.00 135.98 ? 444  GLU B CD  1 
ATOM   17743 O  OE1 . GLU C 1 444  ? -44.118  78.810  46.962  1.00 139.02 ? 444  GLU B OE1 1 
ATOM   17744 O  OE2 . GLU C 1 444  ? -44.468  80.806  46.077  1.00 138.79 ? 444  GLU B OE2 1 
ATOM   17745 N  N   . GLU C 1 445  ? -43.490  75.600  46.737  1.00 92.75  ? 445  GLU B N   1 
ATOM   17746 C  CA  . GLU C 1 445  ? -43.007  75.163  48.062  1.00 92.02  ? 445  GLU B CA  1 
ATOM   17747 C  C   . GLU C 1 445  ? -41.518  75.313  48.230  1.00 85.73  ? 445  GLU B C   1 
ATOM   17748 O  O   . GLU C 1 445  ? -41.043  76.175  48.961  1.00 84.99  ? 445  GLU B O   1 
ATOM   17749 C  CB  . GLU C 1 445  ? -43.342  73.691  48.312  1.00 98.70  ? 445  GLU B CB  1 
ATOM   17750 C  CG  . GLU C 1 445  ? -44.810  73.411  48.586  1.00 107.15 ? 445  GLU B CG  1 
ATOM   17751 C  CD  . GLU C 1 445  ? -45.067  71.944  48.922  1.00 114.84 ? 445  GLU B CD  1 
ATOM   17752 O  OE1 . GLU C 1 445  ? -44.353  71.048  48.377  1.00 116.57 ? 445  GLU B OE1 1 
ATOM   17753 O  OE2 . GLU C 1 445  ? -45.985  71.693  49.740  1.00 117.76 ? 445  GLU B OE2 1 
ATOM   17754 N  N   . ASN C 1 446  ? -40.786  74.463  47.533  1.00 81.90  ? 446  ASN B N   1 
ATOM   17755 C  CA  . ASN C 1 446  ? -39.339  74.412  47.634  1.00 81.40  ? 446  ASN B CA  1 
ATOM   17756 C  C   . ASN C 1 446  ? -38.569  75.604  47.060  1.00 78.52  ? 446  ASN B C   1 
ATOM   17757 O  O   . ASN C 1 446  ? -37.359  75.591  47.002  1.00 76.84  ? 446  ASN B O   1 
ATOM   17758 C  CB  . ASN C 1 446  ? -38.900  73.123  47.014  1.00 86.17  ? 446  ASN B CB  1 
ATOM   17759 C  CG  . ASN C 1 446  ? -39.871  72.023  47.318  1.00 91.86  ? 446  ASN B CG  1 
ATOM   17760 O  OD1 . ASN C 1 446  ? -40.628  71.578  46.456  1.00 92.13  ? 446  ASN B OD1 1 
ATOM   17761 N  ND2 . ASN C 1 446  ? -39.884  71.593  48.576  1.00 96.24  ? 446  ASN B ND2 1 
ATOM   17762 N  N   . GLN C 1 447  ? -39.265  76.649  46.648  1.00 77.34  ? 447  GLN B N   1 
ATOM   17763 C  CA  . GLN C 1 447  ? -38.609  77.913  46.357  1.00 76.69  ? 447  GLN B CA  1 
ATOM   17764 C  C   . GLN C 1 447  ? -37.994  78.527  47.609  1.00 76.37  ? 447  GLN B C   1 
ATOM   17765 O  O   . GLN C 1 447  ? -38.585  78.510  48.687  1.00 74.35  ? 447  GLN B O   1 
ATOM   17766 C  CB  . GLN C 1 447  ? -39.655  78.878  45.827  1.00 83.76  ? 447  GLN B CB  1 
ATOM   17767 C  CG  . GLN C 1 447  ? -39.999  78.699  44.378  1.00 87.19  ? 447  GLN B CG  1 
ATOM   17768 C  CD  . GLN C 1 447  ? -38.769  78.744  43.523  1.00 88.56  ? 447  GLN B CD  1 
ATOM   17769 O  OE1 . GLN C 1 447  ? -37.676  79.099  43.985  1.00 88.13  ? 447  GLN B OE1 1 
ATOM   17770 N  NE2 . GLN C 1 447  ? -38.929  78.366  42.267  1.00 90.31  ? 447  GLN B NE2 1 
ATOM   17771 N  N   . ALA C 1 448  ? -36.835  79.131  47.466  1.00 66.88  ? 448  ALA B N   1 
ATOM   17772 C  CA  . ALA C 1 448  ? -36.176  79.682  48.636  1.00 67.22  ? 448  ALA B CA  1 
ATOM   17773 C  C   . ALA C 1 448  ? -36.544  81.126  49.044  1.00 77.39  ? 448  ALA B C   1 
ATOM   17774 O  O   . ALA C 1 448  ? -36.441  82.034  48.238  1.00 73.91  ? 448  ALA B O   1 
ATOM   17775 C  CB  . ALA C 1 448  ? -34.707  79.559  48.459  1.00 67.18  ? 448  ALA B CB  1 
ATOM   17776 N  N   . ARG C 1 449  ? -36.892  81.346  50.317  1.00 79.79  ? 449  ARG B N   1 
ATOM   17777 C  CA  . ARG C 1 449  ? -37.333  82.674  50.791  1.00 79.80  ? 449  ARG B CA  1 
ATOM   17778 C  C   . ARG C 1 449  ? -36.758  83.178  52.118  1.00 81.40  ? 449  ARG B C   1 
ATOM   17779 O  O   . ARG C 1 449  ? -36.313  82.413  52.962  1.00 82.44  ? 449  ARG B O   1 
ATOM   17780 C  CB  . ARG C 1 449  ? -38.831  82.673  50.924  1.00 81.20  ? 449  ARG B CB  1 
ATOM   17781 C  CG  . ARG C 1 449  ? -39.270  81.392  51.484  1.00 84.96  ? 449  ARG B CG  1 
ATOM   17782 C  CD  . ARG C 1 449  ? -40.729  81.265  51.327  1.00 89.63  ? 449  ARG B CD  1 
ATOM   17783 N  NE  . ARG C 1 449  ? -41.059  80.419  50.198  1.00 92.32  ? 449  ARG B NE  1 
ATOM   17784 C  CZ  . ARG C 1 449  ? -42.114  80.648  49.427  1.00 95.59  ? 449  ARG B CZ  1 
ATOM   17785 N  NH1 . ARG C 1 449  ? -42.899  81.718  49.659  1.00 97.35  ? 449  ARG B NH1 1 
ATOM   17786 N  NH2 . ARG C 1 449  ? -42.369  79.829  48.417  1.00 95.17  ? 449  ARG B NH2 1 
ATOM   17787 N  N   . GLU C 1 450  ? -36.801  84.491  52.282  1.00 83.95  ? 450  GLU B N   1 
ATOM   17788 C  CA  . GLU C 1 450  ? -36.246  85.186  53.426  1.00 86.65  ? 450  GLU B CA  1 
ATOM   17789 C  C   . GLU C 1 450  ? -37.007  86.470  53.534  1.00 85.37  ? 450  GLU B C   1 
ATOM   17790 O  O   . GLU C 1 450  ? -37.540  86.961  52.545  1.00 86.64  ? 450  GLU B O   1 
ATOM   17791 C  CB  . GLU C 1 450  ? -34.783  85.530  53.202  1.00 92.43  ? 450  GLU B CB  1 
ATOM   17792 C  CG  . GLU C 1 450  ? -33.839  84.403  53.517  1.00 99.44  ? 450  GLU B CG  1 
ATOM   17793 C  CD  . GLU C 1 450  ? -33.929  83.981  54.964  1.00 106.50 ? 450  GLU B CD  1 
ATOM   17794 O  OE1 . GLU C 1 450  ? -34.230  84.870  55.804  1.00 109.95 ? 450  GLU B OE1 1 
ATOM   17795 O  OE2 . GLU C 1 450  ? -33.711  82.774  55.252  1.00 106.98 ? 450  GLU B OE2 1 
ATOM   17796 N  N   . GLY C 1 451  ? -37.055  87.020  54.735  1.00 85.00  ? 451  GLY B N   1 
ATOM   17797 C  CA  . GLY C 1 451  ? -37.778  88.256  54.965  1.00 83.59  ? 451  GLY B CA  1 
ATOM   17798 C  C   . GLY C 1 451  ? -36.961  89.170  55.857  1.00 83.87  ? 451  GLY B C   1 
ATOM   17799 O  O   . GLY C 1 451  ? -36.127  88.696  56.654  1.00 86.46  ? 451  GLY B O   1 
ATOM   17800 N  N   . TYR C 1 452  ? -37.193  90.473  55.728  1.00 78.88  ? 452  TYR B N   1 
ATOM   17801 C  CA  . TYR C 1 452  ? -36.394  91.463  56.420  1.00 79.64  ? 452  TYR B CA  1 
ATOM   17802 C  C   . TYR C 1 452  ? -37.272  92.695  56.745  1.00 83.97  ? 452  TYR B C   1 
ATOM   17803 O  O   . TYR C 1 452  ? -38.388  92.808  56.223  1.00 84.17  ? 452  TYR B O   1 
ATOM   17804 C  CB  . TYR C 1 452  ? -35.201  91.827  55.540  1.00 77.88  ? 452  TYR B CB  1 
ATOM   17805 C  CG  . TYR C 1 452  ? -34.261  90.685  55.191  1.00 77.82  ? 452  TYR B CG  1 
ATOM   17806 C  CD1 . TYR C 1 452  ? -32.981  90.656  55.693  1.00 82.12  ? 452  TYR B CD1 1 
ATOM   17807 C  CD2 . TYR C 1 452  ? -34.637  89.650  54.346  1.00 77.99  ? 452  TYR B CD2 1 
ATOM   17808 C  CE1 . TYR C 1 452  ? -32.089  89.633  55.379  1.00 83.77  ? 452  TYR B CE1 1 
ATOM   17809 C  CE2 . TYR C 1 452  ? -33.747  88.605  54.027  1.00 79.36  ? 452  TYR B CE2 1 
ATOM   17810 C  CZ  . TYR C 1 452  ? -32.467  88.617  54.555  1.00 81.54  ? 452  TYR B CZ  1 
ATOM   17811 O  OH  . TYR C 1 452  ? -31.531  87.635  54.308  1.00 79.88  ? 452  TYR B OH  1 
ATOM   17812 N  N   . ARG C 1 453  ? -36.795  93.598  57.615  1.00 84.63  ? 453  ARG B N   1 
ATOM   17813 C  CA  . ARG C 1 453  ? -37.528  94.842  57.935  1.00 82.77  ? 453  ARG B CA  1 
ATOM   17814 C  C   . ARG C 1 453  ? -36.621  96.075  58.087  1.00 84.30  ? 453  ARG B C   1 
ATOM   17815 O  O   . ARG C 1 453  ? -35.571  95.995  58.713  1.00 84.84  ? 453  ARG B O   1 
ATOM   17816 C  CB  . ARG C 1 453  ? -38.338  94.663  59.210  1.00 83.99  ? 453  ARG B CB  1 
ATOM   17817 C  CG  . ARG C 1 453  ? -38.909  95.971  59.696  1.00 86.59  ? 453  ARG B CG  1 
ATOM   17818 C  CD  . ARG C 1 453  ? -39.125  96.017  61.196  1.00 90.63  ? 453  ARG B CD  1 
ATOM   17819 N  NE  . ARG C 1 453  ? -40.433  95.506  61.580  1.00 93.38  ? 453  ARG B NE  1 
ATOM   17820 C  CZ  . ARG C 1 453  ? -40.614  94.460  62.381  1.00 96.76  ? 453  ARG B CZ  1 
ATOM   17821 N  NH1 . ARG C 1 453  ? -39.559  93.823  62.892  1.00 97.44  ? 453  ARG B NH1 1 
ATOM   17822 N  NH2 . ARG C 1 453  ? -41.847  94.059  62.687  1.00 98.69  ? 453  ARG B NH2 1 
ATOM   17823 N  N   . ALA C 1 454  ? -37.024  97.218  57.537  1.00 85.20  ? 454  ALA B N   1 
ATOM   17824 C  CA  . ALA C 1 454  ? -36.136  98.376  57.531  1.00 90.37  ? 454  ALA B CA  1 
ATOM   17825 C  C   . ALA C 1 454  ? -36.835  99.564  58.098  1.00 95.64  ? 454  ALA B C   1 
ATOM   17826 O  O   . ALA C 1 454  ? -38.034  99.712  57.892  1.00 98.47  ? 454  ALA B O   1 
ATOM   17827 C  CB  . ALA C 1 454  ? -35.694  98.691  56.150  1.00 87.64  ? 454  ALA B CB  1 
ATOM   17828 N  N   . ILE C 1 455  ? -36.086  100.439 58.775  1.00 99.34  ? 455  ILE B N   1 
ATOM   17829 C  CA  . ILE C 1 455  ? -36.680  101.517 59.589  1.00 101.96 ? 455  ILE B CA  1 
ATOM   17830 C  C   . ILE C 1 455  ? -35.923  102.827 59.480  1.00 100.79 ? 455  ILE B C   1 
ATOM   17831 O  O   . ILE C 1 455  ? -34.699  102.833 59.397  1.00 99.75  ? 455  ILE B O   1 
ATOM   17832 C  CB  . ILE C 1 455  ? -36.624  101.144 61.014  1.00 94.60  ? 455  ILE B CB  1 
ATOM   17833 C  CG1 . ILE C 1 455  ? -37.687  100.101 61.296  1.00 93.43  ? 455  ILE B CG1 1 
ATOM   17834 C  CG2 . ILE C 1 455  ? -36.801  102.342 61.836  1.00 97.56  ? 455  ILE B CG2 1 
ATOM   17835 C  CD1 . ILE C 1 455  ? -37.101  98.901  62.075  1.00 95.10  ? 455  ILE B CD1 1 
ATOM   17836 N  N   . ALA C 1 456  ? -36.642  103.942 59.499  1.00 100.68 ? 456  ALA B N   1 
ATOM   17837 C  CA  . ALA C 1 456  ? -36.027  105.215 59.144  1.00 102.24 ? 456  ALA B CA  1 
ATOM   17838 C  C   . ALA C 1 456  ? -35.170  105.889 60.229  1.00 104.41 ? 456  ALA B C   1 
ATOM   17839 O  O   . ALA C 1 456  ? -35.573  105.975 61.396  1.00 105.00 ? 456  ALA B O   1 
ATOM   17840 C  CB  . ALA C 1 456  ? -37.081  106.163 58.633  1.00 102.24 ? 456  ALA B CB  1 
ATOM   17841 N  N   . TYR C 1 457  ? -33.979  106.340 59.822  1.00 106.40 ? 457  TYR B N   1 
ATOM   17842 C  CA  . TYR C 1 457  ? -33.125  107.195 60.637  1.00 110.98 ? 457  TYR B CA  1 
ATOM   17843 C  C   . TYR C 1 457  ? -33.961  108.389 60.965  1.00 114.56 ? 457  TYR B C   1 
ATOM   17844 O  O   . TYR C 1 457  ? -34.004  109.371 60.240  1.00 113.48 ? 457  TYR B O   1 
ATOM   17845 C  CB  . TYR C 1 457  ? -31.911  107.679 59.858  1.00 114.60 ? 457  TYR B CB  1 
ATOM   17846 C  CG  . TYR C 1 457  ? -30.860  108.461 60.645  1.00 122.06 ? 457  TYR B CG  1 
ATOM   17847 C  CD1 . TYR C 1 457  ? -29.531  108.483 60.222  1.00 125.22 ? 457  TYR B CD1 1 
ATOM   17848 C  CD2 . TYR C 1 457  ? -31.178  109.167 61.794  1.00 126.42 ? 457  TYR B CD2 1 
ATOM   17849 C  CE1 . TYR C 1 457  ? -28.548  109.182 60.918  1.00 127.71 ? 457  TYR B CE1 1 
ATOM   17850 C  CE2 . TYR C 1 457  ? -30.194  109.879 62.505  1.00 129.69 ? 457  TYR B CE2 1 
ATOM   17851 C  CZ  . TYR C 1 457  ? -28.879  109.876 62.054  1.00 129.23 ? 457  TYR B CZ  1 
ATOM   17852 O  OH  . TYR C 1 457  ? -27.896  110.562 62.731  1.00 130.63 ? 457  TYR B OH  1 
ATOM   17853 N  N   . SER C 1 458  ? -34.638  108.284 62.088  1.00 121.11 ? 458  SER B N   1 
ATOM   17854 C  CA  . SER C 1 458  ? -35.479  109.345 62.599  1.00 126.22 ? 458  SER B CA  1 
ATOM   17855 C  C   . SER C 1 458  ? -34.563  110.478 63.118  1.00 128.89 ? 458  SER B C   1 
ATOM   17856 O  O   . SER C 1 458  ? -33.667  110.250 63.939  1.00 125.25 ? 458  SER B O   1 
ATOM   17857 C  CB  . SER C 1 458  ? -36.363  108.737 63.709  1.00 129.88 ? 458  SER B CB  1 
ATOM   17858 O  OG  . SER C 1 458  ? -36.540  107.310 63.498  1.00 127.69 ? 458  SER B OG  1 
ATOM   17859 N  N   . SER C 1 459  ? -34.751  111.687 62.594  1.00 134.01 ? 459  SER B N   1 
ATOM   17860 C  CA  . SER C 1 459  ? -34.025  112.867 63.080  1.00 138.96 ? 459  SER B CA  1 
ATOM   17861 C  C   . SER C 1 459  ? -34.864  114.126 62.895  1.00 143.47 ? 459  SER B C   1 
ATOM   17862 O  O   . SER C 1 459  ? -35.242  114.462 61.782  1.00 141.28 ? 459  SER B O   1 
ATOM   17863 C  CB  . SER C 1 459  ? -32.681  113.013 62.372  1.00 136.92 ? 459  SER B CB  1 
ATOM   17864 O  OG  . SER C 1 459  ? -31.735  113.669 63.194  1.00 137.84 ? 459  SER B OG  1 
ATOM   17865 N  N   . LEU C 1 460  ? -35.152  114.807 63.999  1.00 152.40 ? 460  LEU B N   1 
ATOM   17866 C  CA  . LEU C 1 460  ? -36.108  115.910 63.999  1.00 164.22 ? 460  LEU B CA  1 
ATOM   17867 C  C   . LEU C 1 460  ? -35.586  117.115 63.231  1.00 169.92 ? 460  LEU B C   1 
ATOM   17868 O  O   . LEU C 1 460  ? -36.367  117.954 62.778  1.00 173.41 ? 460  LEU B O   1 
ATOM   17869 C  CB  . LEU C 1 460  ? -36.506  116.321 65.427  1.00 172.33 ? 460  LEU B CB  1 
ATOM   17870 C  CG  . LEU C 1 460  ? -37.901  116.965 65.604  1.00 179.11 ? 460  LEU B CG  1 
ATOM   17871 C  CD1 . LEU C 1 460  ? -38.972  115.896 65.844  1.00 178.13 ? 460  LEU B CD1 1 
ATOM   17872 C  CD2 . LEU C 1 460  ? -37.958  118.023 66.726  1.00 185.82 ? 460  LEU B CD2 1 
ATOM   17873 N  N   . SER C 1 461  ? -34.266  117.198 63.079  1.00 172.60 ? 461  SER B N   1 
ATOM   17874 C  CA  . SER C 1 461  ? -33.676  118.211 62.210  1.00 175.02 ? 461  SER B CA  1 
ATOM   17875 C  C   . SER C 1 461  ? -34.069  117.944 60.773  1.00 171.47 ? 461  SER B C   1 
ATOM   17876 O  O   . SER C 1 461  ? -33.681  118.681 59.875  1.00 171.09 ? 461  SER B O   1 
ATOM   17877 C  CB  . SER C 1 461  ? -32.153  118.224 62.330  1.00 177.11 ? 461  SER B CB  1 
ATOM   17878 O  OG  . SER C 1 461  ? -31.761  118.713 63.601  1.00 182.47 ? 461  SER B OG  1 
ATOM   17879 N  N   . GLN C 1 462  ? -34.835  116.876 60.572  1.00 168.64 ? 462  GLN B N   1 
ATOM   17880 C  CA  . GLN C 1 462  ? -35.215  116.437 59.241  1.00 162.25 ? 462  GLN B CA  1 
ATOM   17881 C  C   . GLN C 1 462  ? -33.957  116.062 58.491  1.00 155.53 ? 462  GLN B C   1 
ATOM   17882 O  O   . GLN C 1 462  ? -33.984  115.779 57.291  1.00 152.61 ? 462  GLN B O   1 
ATOM   17883 C  CB  . GLN C 1 462  ? -35.969  117.547 58.507  1.00 165.07 ? 462  GLN B CB  1 
ATOM   17884 C  CG  . GLN C 1 462  ? -37.466  117.499 58.686  1.00 164.95 ? 462  GLN B CG  1 
ATOM   17885 C  CD  . GLN C 1 462  ? -38.080  116.252 58.072  1.00 161.53 ? 462  GLN B CD  1 
ATOM   17886 O  OE1 . GLN C 1 462  ? -37.384  115.407 57.493  1.00 156.83 ? 462  GLN B OE1 1 
ATOM   17887 N  NE2 . GLN C 1 462  ? -39.394  116.129 58.200  1.00 163.34 ? 462  GLN B NE2 1 
ATOM   17888 N  N   . SER C 1 463  ? -32.850  116.073 59.221  1.00 150.81 ? 463  SER B N   1 
ATOM   17889 C  CA  . SER C 1 463  ? -31.533  115.883 58.642  1.00 146.04 ? 463  SER B CA  1 
ATOM   17890 C  C   . SER C 1 463  ? -31.161  114.406 58.630  1.00 138.82 ? 463  SER B C   1 
ATOM   17891 O  O   . SER C 1 463  ? -31.448  113.712 59.590  1.00 140.41 ? 463  SER B O   1 
ATOM   17892 C  CB  . SER C 1 463  ? -30.510  116.668 59.462  1.00 149.19 ? 463  SER B CB  1 
ATOM   17893 O  OG  . SER C 1 463  ? -29.189  116.245 59.166  1.00 148.22 ? 463  SER B OG  1 
ATOM   17894 N  N   . TYR C 1 464  ? -30.541  113.920 57.557  1.00 130.43 ? 464  TYR B N   1 
ATOM   17895 C  CA  . TYR C 1 464  ? -30.031  112.561 57.560  1.00 124.68 ? 464  TYR B CA  1 
ATOM   17896 C  C   . TYR C 1 464  ? -28.715  112.495 56.835  1.00 121.19 ? 464  TYR B C   1 
ATOM   17897 O  O   . TYR C 1 464  ? -28.203  113.514 56.380  1.00 121.47 ? 464  TYR B O   1 
ATOM   17898 C  CB  . TYR C 1 464  ? -31.005  111.596 56.916  1.00 122.02 ? 464  TYR B CB  1 
ATOM   17899 C  CG  . TYR C 1 464  ? -32.446  111.918 57.155  1.00 124.71 ? 464  TYR B CG  1 
ATOM   17900 C  CD1 . TYR C 1 464  ? -33.025  111.743 58.399  1.00 128.52 ? 464  TYR B CD1 1 
ATOM   17901 C  CD2 . TYR C 1 464  ? -33.238  112.374 56.130  1.00 126.26 ? 464  TYR B CD2 1 
ATOM   17902 C  CE1 . TYR C 1 464  ? -34.370  112.035 58.617  1.00 131.62 ? 464  TYR B CE1 1 
ATOM   17903 C  CE2 . TYR C 1 464  ? -34.571  112.662 56.326  1.00 129.78 ? 464  TYR B CE2 1 
ATOM   17904 C  CZ  . TYR C 1 464  ? -35.142  112.495 57.567  1.00 132.76 ? 464  TYR B CZ  1 
ATOM   17905 O  OH  . TYR C 1 464  ? -36.486  112.794 57.740  1.00 135.06 ? 464  TYR B OH  1 
ATOM   17906 N  N   . LEU C 1 465  ? -28.165  111.288 56.736  1.00 119.85 ? 465  LEU B N   1 
ATOM   17907 C  CA  . LEU C 1 465  ? -26.934  111.074 55.970  1.00 120.74 ? 465  LEU B CA  1 
ATOM   17908 C  C   . LEU C 1 465  ? -26.848  109.655 55.378  1.00 119.39 ? 465  LEU B C   1 
ATOM   17909 O  O   . LEU C 1 465  ? -27.322  108.696 56.003  1.00 119.99 ? 465  LEU B O   1 
ATOM   17910 C  CB  . LEU C 1 465  ? -25.694  111.390 56.813  1.00 122.68 ? 465  LEU B CB  1 
ATOM   17911 C  CG  . LEU C 1 465  ? -24.364  111.173 56.091  1.00 123.99 ? 465  LEU B CG  1 
ATOM   17912 C  CD1 . LEU C 1 465  ? -24.233  112.130 54.927  1.00 126.63 ? 465  LEU B CD1 1 
ATOM   17913 C  CD2 . LEU C 1 465  ? -23.176  111.308 57.024  1.00 125.55 ? 465  LEU B CD2 1 
ATOM   17914 N  N   . TYR C 1 466  ? -26.231  109.548 54.188  1.00 116.11 ? 466  TYR B N   1 
ATOM   17915 C  CA  . TYR C 1 466  ? -26.098  108.301 53.423  1.00 110.21 ? 466  TYR B CA  1 
ATOM   17916 C  C   . TYR C 1 466  ? -24.740  108.135 52.737  1.00 109.47 ? 466  TYR B C   1 
ATOM   17917 O  O   . TYR C 1 466  ? -24.438  108.845 51.784  1.00 112.07 ? 466  TYR B O   1 
ATOM   17918 C  CB  . TYR C 1 466  ? -27.125  108.256 52.303  1.00 106.61 ? 466  TYR B CB  1 
ATOM   17919 C  CG  . TYR C 1 466  ? -27.031  106.983 51.521  1.00 101.29 ? 466  TYR B CG  1 
ATOM   17920 C  CD1 . TYR C 1 466  ? -26.180  105.995 51.931  1.00 101.40 ? 466  TYR B CD1 1 
ATOM   17921 C  CD2 . TYR C 1 466  ? -27.809  106.738 50.414  1.00 98.85  ? 466  TYR B CD2 1 
ATOM   17922 C  CE1 . TYR C 1 466  ? -26.068  104.792 51.258  1.00 98.77  ? 466  TYR B CE1 1 
ATOM   17923 C  CE2 . TYR C 1 466  ? -27.722  105.514 49.731  1.00 96.76  ? 466  TYR B CE2 1 
ATOM   17924 C  CZ  . TYR C 1 466  ? -26.838  104.544 50.175  1.00 95.64  ? 466  TYR B CZ  1 
ATOM   17925 O  OH  . TYR C 1 466  ? -26.679  103.320 49.575  1.00 91.71  ? 466  TYR B OH  1 
ATOM   17926 N  N   . ILE C 1 467  ? -23.935  107.170 53.166  1.00 106.07 ? 467  ILE B N   1 
ATOM   17927 C  CA  . ILE C 1 467  ? -22.689  106.897 52.443  1.00 103.89 ? 467  ILE B CA  1 
ATOM   17928 C  C   . ILE C 1 467  ? -22.589  105.498 51.836  1.00 103.20 ? 467  ILE B C   1 
ATOM   17929 O  O   . ILE C 1 467  ? -23.054  104.508 52.396  1.00 102.21 ? 467  ILE B O   1 
ATOM   17930 C  CB  . ILE C 1 467  ? -21.475  107.140 53.317  1.00 102.73 ? 467  ILE B CB  1 
ATOM   17931 C  CG1 . ILE C 1 467  ? -21.354  106.017 54.348  1.00 99.90  ? 467  ILE B CG1 1 
ATOM   17932 C  CG2 . ILE C 1 467  ? -21.592  108.512 53.970  1.00 106.00 ? 467  ILE B CG2 1 
ATOM   17933 C  CD1 . ILE C 1 467  ? -20.033  106.005 55.081  1.00 100.10 ? 467  ILE B CD1 1 
ATOM   17934 N  N   . ASP C 1 468  ? -21.950  105.410 50.689  1.00 105.51 ? 468  ASP B N   1 
ATOM   17935 C  CA  . ASP C 1 468  ? -21.861  104.146 50.022  1.00 108.21 ? 468  ASP B CA  1 
ATOM   17936 C  C   . ASP C 1 468  ? -20.570  104.243 49.289  1.00 109.03 ? 468  ASP B C   1 
ATOM   17937 O  O   . ASP C 1 468  ? -19.832  105.191 49.481  1.00 108.36 ? 468  ASP B O   1 
ATOM   17938 C  CB  . ASP C 1 468  ? -23.031  103.990 49.054  1.00 115.56 ? 468  ASP B CB  1 
ATOM   17939 C  CG  . ASP C 1 468  ? -23.257  102.543 48.619  1.00 119.93 ? 468  ASP B CG  1 
ATOM   17940 O  OD1 . ASP C 1 468  ? -22.629  101.644 49.210  1.00 121.13 ? 468  ASP B OD1 1 
ATOM   17941 O  OD2 . ASP C 1 468  ? -24.064  102.299 47.685  1.00 121.29 ? 468  ASP B OD2 1 
ATOM   17942 N  N   . TRP C 1 469  ? -20.303  103.272 48.438  1.00 112.20 ? 469  TRP B N   1 
ATOM   17943 C  CA  . TRP C 1 469  ? -19.081  103.242 47.666  1.00 121.81 ? 469  TRP B CA  1 
ATOM   17944 C  C   . TRP C 1 469  ? -19.262  102.108 46.697  1.00 131.66 ? 469  TRP B C   1 
ATOM   17945 O  O   . TRP C 1 469  ? -20.030  101.201 47.001  1.00 131.34 ? 469  TRP B O   1 
ATOM   17946 C  CB  . TRP C 1 469  ? -17.927  102.917 48.602  1.00 119.21 ? 469  TRP B CB  1 
ATOM   17947 C  CG  . TRP C 1 469  ? -17.848  101.469 49.002  1.00 116.28 ? 469  TRP B CG  1 
ATOM   17948 C  CD1 . TRP C 1 469  ? -16.874  100.586 48.660  1.00 115.48 ? 469  TRP B CD1 1 
ATOM   17949 C  CD2 . TRP C 1 469  ? -18.778  100.737 49.813  1.00 115.43 ? 469  TRP B CD2 1 
ATOM   17950 N  NE1 . TRP C 1 469  ? -17.134  99.345  49.201  1.00 113.32 ? 469  TRP B NE1 1 
ATOM   17951 C  CE2 . TRP C 1 469  ? -18.297  99.417  49.914  1.00 113.60 ? 469  TRP B CE2 1 
ATOM   17952 C  CE3 . TRP C 1 469  ? -19.968  101.066 50.461  1.00 116.88 ? 469  TRP B CE3 1 
ATOM   17953 C  CZ2 . TRP C 1 469  ? -18.961  98.439  50.637  1.00 112.55 ? 469  TRP B CZ2 1 
ATOM   17954 C  CZ3 . TRP C 1 469  ? -20.629  100.076 51.187  1.00 114.95 ? 469  TRP B CZ3 1 
ATOM   17955 C  CH2 . TRP C 1 469  ? -20.122  98.789  51.268  1.00 112.50 ? 469  TRP B CH2 1 
ATOM   17956 N  N   . THR C 1 470  ? -18.586  102.104 45.549  1.00 143.59 ? 470  THR B N   1 
ATOM   17957 C  CA  . THR C 1 470  ? -18.569  100.833 44.804  1.00 154.22 ? 470  THR B CA  1 
ATOM   17958 C  C   . THR C 1 470  ? -17.208  100.296 44.385  1.00 168.99 ? 470  THR B C   1 
ATOM   17959 O  O   . THR C 1 470  ? -16.225  101.029 44.260  1.00 172.22 ? 470  THR B O   1 
ATOM   17960 C  CB  . THR C 1 470  ? -19.542  100.748 43.610  1.00 149.31 ? 470  THR B CB  1 
ATOM   17961 O  OG1 . THR C 1 470  ? -20.854  101.124 44.030  1.00 150.14 ? 470  THR B OG1 1 
ATOM   17962 C  CG2 . THR C 1 470  ? -19.601  99.319  43.099  1.00 144.69 ? 470  THR B CG2 1 
ATOM   17963 N  N   . ASP C 1 471  ? -17.203  98.983  44.188  1.00 181.87 ? 471  ASP B N   1 
ATOM   17964 C  CA  . ASP C 1 471  ? -16.044  98.196  43.819  1.00 199.01 ? 471  ASP B CA  1 
ATOM   17965 C  C   . ASP C 1 471  ? -16.644  96.858  43.351  1.00 209.13 ? 471  ASP B C   1 
ATOM   17966 O  O   . ASP C 1 471  ? -17.459  96.266  44.061  1.00 209.21 ? 471  ASP B O   1 
ATOM   17967 C  CB  . ASP C 1 471  ? -15.125  98.028  45.043  1.00 205.35 ? 471  ASP B CB  1 
ATOM   17968 C  CG  . ASP C 1 471  ? -13.768  97.389  44.702  1.00 213.85 ? 471  ASP B CG  1 
ATOM   17969 O  OD1 . ASP C 1 471  ? -12.746  98.103  44.696  1.00 218.20 ? 471  ASP B OD1 1 
ATOM   17970 O  OD2 . ASP C 1 471  ? -13.699  96.166  44.456  1.00 215.86 ? 471  ASP B OD2 1 
ATOM   17971 N  N   . ASN C 1 472  ? -16.275  96.399  42.155  1.00 220.47 ? 472  ASN B N   1 
ATOM   17972 C  CA  . ASN C 1 472  ? -16.917  95.222  41.549  1.00 227.89 ? 472  ASN B CA  1 
ATOM   17973 C  C   . ASN C 1 472  ? -16.594  93.837  42.143  1.00 234.90 ? 472  ASN B C   1 
ATOM   17974 O  O   . ASN C 1 472  ? -17.256  92.856  41.801  1.00 232.64 ? 472  ASN B O   1 
ATOM   17975 C  CB  . ASN C 1 472  ? -16.761  95.211  40.011  1.00 228.10 ? 472  ASN B CB  1 
ATOM   17976 C  CG  . ASN C 1 472  ? -15.445  95.824  39.527  1.00 226.80 ? 472  ASN B CG  1 
ATOM   17977 O  OD1 . ASN C 1 472  ? -14.643  96.316  40.314  1.00 226.26 ? 472  ASN B OD1 1 
ATOM   17978 N  ND2 . ASN C 1 472  ? -15.233  95.801  38.212  1.00 225.76 ? 472  ASN B ND2 1 
ATOM   17979 N  N   . HIS C 1 473  ? -15.595  93.751  43.021  1.00 242.92 ? 473  HIS B N   1 
ATOM   17980 C  CA  . HIS C 1 473  ? -15.223  92.461  43.618  1.00 250.50 ? 473  HIS B CA  1 
ATOM   17981 C  C   . HIS C 1 473  ? -15.498  92.313  45.113  1.00 236.26 ? 473  HIS B C   1 
ATOM   17982 O  O   . HIS C 1 473  ? -15.462  93.276  45.879  1.00 236.52 ? 473  HIS B O   1 
ATOM   17983 C  CB  . HIS C 1 473  ? -13.730  92.194  43.428  1.00 272.72 ? 473  HIS B CB  1 
ATOM   17984 C  CG  . HIS C 1 473  ? -13.017  93.237  42.531  1.00 293.89 ? 473  HIS B CG  1 
ATOM   17985 N  ND1 . HIS C 1 473  ? -11.689  93.570  42.688  1.00 306.37 ? 473  HIS B ND1 1 
ATOM   17986 C  CD2 . HIS C 1 473  ? -13.475  93.984  41.500  1.00 303.92 ? 473  HIS B CD2 1 
ATOM   17987 C  CE1 . HIS C 1 473  ? -11.359  94.479  41.790  1.00 315.94 ? 473  HIS B CE1 1 
ATOM   17988 N  NE2 . HIS C 1 473  ? -12.423  94.747  41.057  1.00 313.58 ? 473  HIS B NE2 1 
ATOM   17989 N  N   . LYS C 1 474  ? -15.735  91.069  45.507  1.00 223.02 ? 474  LYS B N   1 
ATOM   17990 C  CA  . LYS C 1 474  ? -16.261  90.747  46.824  1.00 212.49 ? 474  LYS B CA  1 
ATOM   17991 C  C   . LYS C 1 474  ? -15.337  91.095  47.986  1.00 199.52 ? 474  LYS B C   1 
ATOM   17992 O  O   . LYS C 1 474  ? -15.709  90.930  49.149  1.00 201.80 ? 474  LYS B O   1 
ATOM   17993 C  CB  . LYS C 1 474  ? -16.677  89.268  46.898  1.00 213.15 ? 474  LYS B CB  1 
ATOM   17994 C  CG  . LYS C 1 474  ? -15.642  88.278  46.380  1.00 215.10 ? 474  LYS B CG  1 
ATOM   17995 C  CD  . LYS C 1 474  ? -16.007  86.853  46.767  1.00 215.19 ? 474  LYS B CD  1 
ATOM   17996 C  CE  . LYS C 1 474  ? -16.009  86.684  48.277  1.00 216.23 ? 474  LYS B CE  1 
ATOM   17997 N  NZ  . LYS C 1 474  ? -16.213  85.269  48.682  1.00 215.31 ? 474  LYS B NZ  1 
ATOM   17998 N  N   . ALA C 1 475  ? -14.141  91.580  47.692  1.00 184.42 ? 475  ALA B N   1 
ATOM   17999 C  CA  . ALA C 1 475  ? -13.206  91.850  48.772  1.00 168.95 ? 475  ALA B CA  1 
ATOM   18000 C  C   . ALA C 1 475  ? -12.310  92.993  48.382  1.00 154.27 ? 475  ALA B C   1 
ATOM   18001 O  O   . ALA C 1 475  ? -11.797  93.032  47.266  1.00 152.12 ? 475  ALA B O   1 
ATOM   18002 C  CB  . ALA C 1 475  ? -12.383  90.618  49.089  1.00 167.67 ? 475  ALA B CB  1 
ATOM   18003 N  N   . LEU C 1 476  ? -12.128  93.933  49.298  1.00 143.05 ? 476  LEU B N   1 
ATOM   18004 C  CA  . LEU C 1 476  ? -11.273  95.066  49.016  1.00 131.70 ? 476  LEU B CA  1 
ATOM   18005 C  C   . LEU C 1 476  ? -9.855   94.639  49.280  1.00 127.02 ? 476  LEU B C   1 
ATOM   18006 O  O   . LEU C 1 476  ? -9.492   94.310  50.403  1.00 128.98 ? 476  LEU B O   1 
ATOM   18007 C  CB  . LEU C 1 476  ? -11.631  96.265  49.879  1.00 125.38 ? 476  LEU B CB  1 
ATOM   18008 C  CG  . LEU C 1 476  ? -13.112  96.466  50.152  1.00 117.45 ? 476  LEU B CG  1 
ATOM   18009 C  CD1 . LEU C 1 476  ? -13.358  97.808  50.787  1.00 116.80 ? 476  LEU B CD1 1 
ATOM   18010 C  CD2 . LEU C 1 476  ? -13.886  96.371  48.881  1.00 115.61 ? 476  LEU B CD2 1 
ATOM   18011 N  N   . LEU C 1 477  ? -9.046   94.628  48.237  1.00 121.70 ? 477  LEU B N   1 
ATOM   18012 C  CA  . LEU C 1 477  ? -7.651   94.276  48.403  1.00 116.92 ? 477  LEU B CA  1 
ATOM   18013 C  C   . LEU C 1 477  ? -6.970   95.402  49.135  1.00 111.38 ? 477  LEU B C   1 
ATOM   18014 O  O   . LEU C 1 477  ? -7.233   96.570  48.871  1.00 111.12 ? 477  LEU B O   1 
ATOM   18015 C  CB  . LEU C 1 477  ? -6.992   94.028  47.052  1.00 121.28 ? 477  LEU B CB  1 
ATOM   18016 C  CG  . LEU C 1 477  ? -7.848   93.142  46.139  1.00 125.97 ? 477  LEU B CG  1 
ATOM   18017 C  CD1 . LEU C 1 477  ? -7.395   93.267  44.687  1.00 129.87 ? 477  LEU B CD1 1 
ATOM   18018 C  CD2 . LEU C 1 477  ? -7.884   91.663  46.583  1.00 125.37 ? 477  LEU B CD2 1 
ATOM   18019 N  N   . VAL C 1 478  ? -6.123   95.041  50.085  1.00 108.24 ? 478  VAL B N   1 
ATOM   18020 C  CA  . VAL C 1 478  ? -5.336   96.019  50.799  1.00 110.57 ? 478  VAL B CA  1 
ATOM   18021 C  C   . VAL C 1 478  ? -4.413   96.620  49.783  1.00 113.25 ? 478  VAL B C   1 
ATOM   18022 O  O   . VAL C 1 478  ? -3.944   95.911  48.907  1.00 111.26 ? 478  VAL B O   1 
ATOM   18023 C  CB  . VAL C 1 478  ? -4.468   95.365  51.830  1.00 112.20 ? 478  VAL B CB  1 
ATOM   18024 C  CG1 . VAL C 1 478  ? -3.084   95.103  51.226  1.00 113.06 ? 478  VAL B CG1 1 
ATOM   18025 C  CG2 . VAL C 1 478  ? -4.386   96.252  53.059  1.00 113.78 ? 478  VAL B CG2 1 
ATOM   18026 N  N   . GLY C 1 479  ? -4.137   97.912  49.901  1.00 118.12 ? 479  GLY B N   1 
ATOM   18027 C  CA  . GLY C 1 479  ? -3.440   98.619  48.847  1.00 121.91 ? 479  GLY B CA  1 
ATOM   18028 C  C   . GLY C 1 479  ? -4.395   99.407  47.968  1.00 124.10 ? 479  GLY B C   1 
ATOM   18029 O  O   . GLY C 1 479  ? -4.017   100.421 47.394  1.00 127.56 ? 479  GLY B O   1 
ATOM   18030 N  N   . GLU C 1 480  ? -5.639   98.957  47.860  1.00 120.72 ? 480  GLU B N   1 
ATOM   18031 C  CA  . GLU C 1 480  ? -6.626   99.675  47.053  1.00 120.76 ? 480  GLU B CA  1 
ATOM   18032 C  C   . GLU C 1 480  ? -7.034   101.007 47.689  1.00 120.50 ? 480  GLU B C   1 
ATOM   18033 O  O   . GLU C 1 480  ? -6.541   101.376 48.747  1.00 120.10 ? 480  GLU B O   1 
ATOM   18034 C  CB  . GLU C 1 480  ? -7.850   98.801  46.750  1.00 121.39 ? 480  GLU B CB  1 
ATOM   18035 C  CG  . GLU C 1 480  ? -7.693   97.964  45.462  1.00 128.30 ? 480  GLU B CG  1 
ATOM   18036 C  CD  . GLU C 1 480  ? -8.998   97.284  45.003  1.00 135.16 ? 480  GLU B CD  1 
ATOM   18037 O  OE1 . GLU C 1 480  ? -9.078   96.821  43.838  1.00 136.63 ? 480  GLU B OE1 1 
ATOM   18038 O  OE2 . GLU C 1 480  ? -9.958   97.208  45.806  1.00 138.18 ? 480  GLU B OE2 1 
ATOM   18039 N  N   . HIS C 1 481  ? -7.929   101.732 47.033  1.00 122.06 ? 481  HIS B N   1 
ATOM   18040 C  CA  . HIS C 1 481  ? -8.334   103.045 47.509  1.00 125.88 ? 481  HIS B CA  1 
ATOM   18041 C  C   . HIS C 1 481  ? -9.832   103.186 47.373  1.00 121.20 ? 481  HIS B C   1 
ATOM   18042 O  O   . HIS C 1 481  ? -10.373  103.172 46.268  1.00 119.15 ? 481  HIS B O   1 
ATOM   18043 C  CB  . HIS C 1 481  ? -7.642   104.151 46.709  1.00 134.74 ? 481  HIS B CB  1 
ATOM   18044 C  CG  . HIS C 1 481  ? -6.271   104.502 47.206  1.00 142.37 ? 481  HIS B CG  1 
ATOM   18045 N  ND1 . HIS C 1 481  ? -6.026   105.603 48.002  1.00 146.95 ? 481  HIS B ND1 1 
ATOM   18046 C  CD2 . HIS C 1 481  ? -5.067   103.913 47.003  1.00 144.62 ? 481  HIS B CD2 1 
ATOM   18047 C  CE1 . HIS C 1 481  ? -4.735   105.670 48.277  1.00 149.45 ? 481  HIS B CE1 1 
ATOM   18048 N  NE2 . HIS C 1 481  ? -4.129   104.658 47.680  1.00 148.12 ? 481  HIS B NE2 1 
ATOM   18049 N  N   . LEU C 1 482  ? -10.492  103.340 48.511  1.00 119.58 ? 482  LEU B N   1 
ATOM   18050 C  CA  . LEU C 1 482  ? -11.942  103.310 48.568  1.00 118.59 ? 482  LEU B CA  1 
ATOM   18051 C  C   . LEU C 1 482  ? -12.595  104.666 48.307  1.00 121.23 ? 482  LEU B C   1 
ATOM   18052 O  O   . LEU C 1 482  ? -12.577  105.554 49.164  1.00 124.56 ? 482  LEU B O   1 
ATOM   18053 C  CB  . LEU C 1 482  ? -12.383  102.776 49.932  1.00 117.10 ? 482  LEU B CB  1 
ATOM   18054 C  CG  . LEU C 1 482  ? -13.763  102.111 49.990  1.00 113.61 ? 482  LEU B CG  1 
ATOM   18055 C  CD1 . LEU C 1 482  ? -13.887  101.175 51.189  1.00 110.87 ? 482  LEU B CD1 1 
ATOM   18056 C  CD2 . LEU C 1 482  ? -14.880  103.142 49.982  1.00 114.92 ? 482  LEU B CD2 1 
ATOM   18057 N  N   . ASN C 1 483  ? -13.183  104.831 47.128  1.00 118.95 ? 483  ASN B N   1 
ATOM   18058 C  CA  . ASN C 1 483  ? -13.937  106.045 46.866  1.00 119.48 ? 483  ASN B CA  1 
ATOM   18059 C  C   . ASN C 1 483  ? -15.361  105.866 47.358  1.00 115.56 ? 483  ASN B C   1 
ATOM   18060 O  O   . ASN C 1 483  ? -16.111  105.052 46.815  1.00 114.43 ? 483  ASN B O   1 
ATOM   18061 C  CB  . ASN C 1 483  ? -13.923  106.411 45.385  1.00 121.50 ? 483  ASN B CB  1 
ATOM   18062 C  CG  . ASN C 1 483  ? -14.251  107.876 45.150  1.00 126.47 ? 483  ASN B CG  1 
ATOM   18063 O  OD1 . ASN C 1 483  ? -13.565  108.772 45.655  1.00 128.49 ? 483  ASN B OD1 1 
ATOM   18064 N  ND2 . ASN C 1 483  ? -15.308  108.128 44.381  1.00 127.77 ? 483  ASN B ND2 1 
ATOM   18065 N  N   . ILE C 1 484  ? -15.730  106.659 48.363  1.00 113.95 ? 484  ILE B N   1 
ATOM   18066 C  CA  . ILE C 1 484  ? -16.969  106.467 49.111  1.00 108.85 ? 484  ILE B CA  1 
ATOM   18067 C  C   . ILE C 1 484  ? -17.841  107.728 49.183  1.00 106.37 ? 484  ILE B C   1 
ATOM   18068 O  O   . ILE C 1 484  ? -17.395  108.783 49.643  1.00 108.23 ? 484  ILE B O   1 
ATOM   18069 C  CB  . ILE C 1 484  ? -16.639  105.947 50.514  1.00 107.89 ? 484  ILE B CB  1 
ATOM   18070 C  CG1 . ILE C 1 484  ? -17.727  106.306 51.532  1.00 107.22 ? 484  ILE B CG1 1 
ATOM   18071 C  CG2 . ILE C 1 484  ? -15.314  106.493 50.961  1.00 109.78 ? 484  ILE B CG2 1 
ATOM   18072 C  CD1 . ILE C 1 484  ? -17.412  105.783 52.929  1.00 104.47 ? 484  ILE B CD1 1 
ATOM   18073 N  N   . ILE C 1 485  ? -19.094  107.590 48.746  1.00 102.35 ? 485  ILE B N   1 
ATOM   18074 C  CA  . ILE C 1 485  ? -19.937  108.735 48.393  1.00 103.32 ? 485  ILE B CA  1 
ATOM   18075 C  C   . ILE C 1 485  ? -20.829  109.306 49.480  1.00 106.09 ? 485  ILE B C   1 
ATOM   18076 O  O   . ILE C 1 485  ? -21.829  108.699 49.877  1.00 108.26 ? 485  ILE B O   1 
ATOM   18077 C  CB  . ILE C 1 485  ? -20.846  108.391 47.258  1.00 99.89  ? 485  ILE B CB  1 
ATOM   18078 C  CG1 . ILE C 1 485  ? -20.022  108.336 45.991  1.00 99.66  ? 485  ILE B CG1 1 
ATOM   18079 C  CG2 . ILE C 1 485  ? -21.904  109.470 47.137  1.00 102.44 ? 485  ILE B CG2 1 
ATOM   18080 C  CD1 . ILE C 1 485  ? -18.538  108.438 46.257  1.00 100.38 ? 485  ILE B CD1 1 
ATOM   18081 N  N   . VAL C 1 486  ? -20.492  110.511 49.914  1.00 106.35 ? 486  VAL B N   1 
ATOM   18082 C  CA  . VAL C 1 486  ? -21.145  111.116 51.053  1.00 106.08 ? 486  VAL B CA  1 
ATOM   18083 C  C   . VAL C 1 486  ? -22.301  111.962 50.589  1.00 108.14 ? 486  VAL B C   1 
ATOM   18084 O  O   . VAL C 1 486  ? -22.093  113.088 50.160  1.00 111.47 ? 486  VAL B O   1 
ATOM   18085 C  CB  . VAL C 1 486  ? -20.161  112.014 51.795  1.00 106.85 ? 486  VAL B CB  1 
ATOM   18086 C  CG1 . VAL C 1 486  ? -20.592  112.193 53.237  1.00 109.77 ? 486  VAL B CG1 1 
ATOM   18087 C  CG2 . VAL C 1 486  ? -18.768  111.418 51.723  1.00 104.75 ? 486  VAL B CG2 1 
ATOM   18088 N  N   . THR C 1 487  ? -23.515  111.426 50.659  1.00 106.35 ? 487  THR B N   1 
ATOM   18089 C  CA  . THR C 1 487  ? -24.713  112.188 50.284  1.00 108.48 ? 487  THR B CA  1 
ATOM   18090 C  C   . THR C 1 487  ? -25.531  112.573 51.531  1.00 109.89 ? 487  THR B C   1 
ATOM   18091 O  O   . THR C 1 487  ? -26.213  111.723 52.104  1.00 108.34 ? 487  THR B O   1 
ATOM   18092 C  CB  . THR C 1 487  ? -25.602  111.406 49.260  1.00 109.10 ? 487  THR B CB  1 
ATOM   18093 O  OG1 . THR C 1 487  ? -25.803  110.066 49.725  1.00 108.45 ? 487  THR B OG1 1 
ATOM   18094 C  CG2 . THR C 1 487  ? -24.939  111.341 47.887  1.00 106.44 ? 487  THR B CG2 1 
ATOM   18095 N  N   . PRO C 1 488  ? -25.459  113.852 51.950  1.00 114.03 ? 488  PRO B N   1 
ATOM   18096 C  CA  . PRO C 1 488  ? -26.133  114.396 53.131  1.00 118.69 ? 488  PRO B CA  1 
ATOM   18097 C  C   . PRO C 1 488  ? -27.613  114.657 52.921  1.00 125.98 ? 488  PRO B C   1 
ATOM   18098 O  O   . PRO C 1 488  ? -28.283  115.010 53.877  1.00 122.32 ? 488  PRO B O   1 
ATOM   18099 C  CB  . PRO C 1 488  ? -25.423  115.723 53.347  1.00 118.89 ? 488  PRO B CB  1 
ATOM   18100 C  CG  . PRO C 1 488  ? -24.241  115.698 52.476  1.00 117.45 ? 488  PRO B CG  1 
ATOM   18101 C  CD  . PRO C 1 488  ? -24.622  114.874 51.318  1.00 115.75 ? 488  PRO B CD  1 
ATOM   18102 N  N   . LYS C 1 489  ? -28.094  114.478 51.693  1.00 139.14 ? 489  LYS B N   1 
ATOM   18103 C  CA  . LYS C 1 489  ? -29.514  114.616 51.350  1.00 152.43 ? 489  LYS B CA  1 
ATOM   18104 C  C   . LYS C 1 489  ? -30.462  114.841 52.528  1.00 162.39 ? 489  LYS B C   1 
ATOM   18105 O  O   . LYS C 1 489  ? -30.367  114.183 53.559  1.00 163.30 ? 489  LYS B O   1 
ATOM   18106 C  CB  . LYS C 1 489  ? -29.997  113.401 50.539  1.00 152.44 ? 489  LYS B CB  1 
ATOM   18107 C  CG  . LYS C 1 489  ? -31.495  113.396 50.210  1.00 155.27 ? 489  LYS B CG  1 
ATOM   18108 C  CD  . LYS C 1 489  ? -31.731  112.868 48.794  1.00 156.27 ? 489  LYS B CD  1 
ATOM   18109 C  CE  . LYS C 1 489  ? -33.021  113.400 48.170  1.00 158.94 ? 489  LYS B CE  1 
ATOM   18110 N  NZ  . LYS C 1 489  ? -33.044  114.890 48.000  1.00 162.92 ? 489  LYS B NZ  1 
ATOM   18111 N  N   . SER C 1 490  ? -31.370  115.794 52.340  1.00 170.65 ? 490  SER B N   1 
ATOM   18112 C  CA  . SER C 1 490  ? -32.488  116.074 53.246  1.00 177.28 ? 490  SER B CA  1 
ATOM   18113 C  C   . SER C 1 490  ? -32.277  117.276 54.178  1.00 182.29 ? 490  SER B C   1 
ATOM   18114 O  O   . SER C 1 490  ? -32.950  118.300 54.012  1.00 186.40 ? 490  SER B O   1 
ATOM   18115 C  CB  . SER C 1 490  ? -32.925  114.812 53.993  1.00 178.72 ? 490  SER B CB  1 
ATOM   18116 O  OG  . SER C 1 490  ? -33.098  113.744 53.064  1.00 178.13 ? 490  SER B OG  1 
ATOM   18117 N  N   . PRO C 1 491  ? -31.323  117.177 55.125  1.00 181.71 ? 491  PRO B N   1 
ATOM   18118 C  CA  . PRO C 1 491  ? -31.101  118.260 56.081  1.00 179.78 ? 491  PRO B CA  1 
ATOM   18119 C  C   . PRO C 1 491  ? -31.643  119.562 55.570  1.00 171.22 ? 491  PRO B C   1 
ATOM   18120 O  O   . PRO C 1 491  ? -31.218  120.090 54.537  1.00 167.03 ? 491  PRO B O   1 
ATOM   18121 C  CB  . PRO C 1 491  ? -29.581  118.301 56.190  1.00 184.65 ? 491  PRO B CB  1 
ATOM   18122 C  CG  . PRO C 1 491  ? -29.207  116.836 56.093  1.00 184.07 ? 491  PRO B CG  1 
ATOM   18123 C  CD  . PRO C 1 491  ? -30.308  116.129 55.299  1.00 181.63 ? 491  PRO B CD  1 
ATOM   18124 N  N   . TYR C 1 492  ? -32.627  120.046 56.304  1.00 166.58 ? 492  TYR B N   1 
ATOM   18125 C  CA  . TYR C 1 492  ? -33.308  121.219 55.915  1.00 164.69 ? 492  TYR B CA  1 
ATOM   18126 C  C   . TYR C 1 492  ? -32.255  122.123 55.400  1.00 166.56 ? 492  TYR B C   1 
ATOM   18127 O  O   . TYR C 1 492  ? -32.541  122.920 54.540  1.00 169.10 ? 492  TYR B O   1 
ATOM   18128 C  CB  . TYR C 1 492  ? -34.019  121.844 57.099  1.00 166.80 ? 492  TYR B CB  1 
ATOM   18129 C  CG  . TYR C 1 492  ? -33.149  122.527 58.166  1.00 166.69 ? 492  TYR B CG  1 
ATOM   18130 C  CD1 . TYR C 1 492  ? -33.716  123.462 59.054  1.00 168.07 ? 492  TYR B CD1 1 
ATOM   18131 C  CD2 . TYR C 1 492  ? -31.788  122.245 58.302  1.00 163.11 ? 492  TYR B CD2 1 
ATOM   18132 C  CE1 . TYR C 1 492  ? -32.961  124.085 60.034  1.00 169.11 ? 492  TYR B CE1 1 
ATOM   18133 C  CE2 . TYR C 1 492  ? -31.021  122.873 59.288  1.00 164.28 ? 492  TYR B CE2 1 
ATOM   18134 C  CZ  . TYR C 1 492  ? -31.617  123.786 60.150  1.00 168.00 ? 492  TYR B CZ  1 
ATOM   18135 O  OH  . TYR C 1 492  ? -30.870  124.408 61.124  1.00 171.64 ? 492  TYR B OH  1 
ATOM   18136 N  N   . ILE C 1 493  ? -31.022  122.003 55.880  1.00 166.65 ? 493  ILE B N   1 
ATOM   18137 C  CA  . ILE C 1 493  ? -29.984  122.816 55.255  1.00 172.77 ? 493  ILE B CA  1 
ATOM   18138 C  C   . ILE C 1 493  ? -28.577  122.222 55.024  1.00 174.51 ? 493  ILE B C   1 
ATOM   18139 O  O   . ILE C 1 493  ? -28.254  121.124 55.465  1.00 174.84 ? 493  ILE B O   1 
ATOM   18140 C  CB  . ILE C 1 493  ? -29.987  124.311 55.761  1.00 244.24 ? 493  ILE B CB  1 
ATOM   18141 C  CG1 . ILE C 1 493  ? -30.850  125.199 54.834  1.00 245.26 ? 493  ILE B CG1 1 
ATOM   18142 C  CG2 . ILE C 1 493  ? -28.585  124.883 55.834  1.00 245.63 ? 493  ILE B CG2 1 
ATOM   18143 C  CD1 . ILE C 1 493  ? -30.928  126.692 55.229  1.00 249.22 ? 493  ILE B CD1 1 
ATOM   18144 N  N   . ASP C 1 494  ? -27.800  122.986 54.254  1.00 178.15 ? 494  ASP B N   1 
ATOM   18145 C  CA  . ASP C 1 494  ? -26.502  122.648 53.679  1.00 176.49 ? 494  ASP B CA  1 
ATOM   18146 C  C   . ASP C 1 494  ? -25.330  123.357 54.359  1.00 179.68 ? 494  ASP B C   1 
ATOM   18147 O  O   . ASP C 1 494  ? -24.241  123.410 53.790  1.00 179.48 ? 494  ASP B O   1 
ATOM   18148 C  CB  . ASP C 1 494  ? -26.488  123.091 52.206  1.00 177.16 ? 494  ASP B CB  1 
ATOM   18149 C  CG  . ASP C 1 494  ? -26.672  124.642 52.025  1.00 174.91 ? 494  ASP B CG  1 
ATOM   18150 O  OD1 . ASP C 1 494  ? -27.516  125.259 52.720  1.00 175.56 ? 494  ASP B OD1 1 
ATOM   18151 O  OD2 . ASP C 1 494  ? -25.984  125.243 51.166  1.00 175.56 ? 494  ASP B OD2 1 
ATOM   18152 N  N   . LYS C 1 495  ? -25.547  123.933 55.541  1.00 181.88 ? 495  LYS B N   1 
ATOM   18153 C  CA  . LYS C 1 495  ? -24.490  124.699 56.218  1.00 183.05 ? 495  LYS B CA  1 
ATOM   18154 C  C   . LYS C 1 495  ? -23.401  123.821 56.829  1.00 176.86 ? 495  LYS B C   1 
ATOM   18155 O  O   . LYS C 1 495  ? -22.875  124.099 57.914  1.00 176.41 ? 495  LYS B O   1 
ATOM   18156 C  CB  . LYS C 1 495  ? -25.068  125.661 57.261  1.00 188.71 ? 495  LYS B CB  1 
ATOM   18157 C  CG  . LYS C 1 495  ? -25.668  126.948 56.666  1.00 192.63 ? 495  LYS B CG  1 
ATOM   18158 C  CD  . LYS C 1 495  ? -24.927  127.392 55.393  1.00 192.03 ? 495  LYS B CD  1 
ATOM   18159 C  CE  . LYS C 1 495  ? -25.490  126.714 54.144  1.00 187.47 ? 495  LYS B CE  1 
ATOM   18160 N  NZ  . LYS C 1 495  ? -24.429  126.129 53.281  1.00 184.00 ? 495  LYS B NZ  1 
ATOM   18161 N  N   . ILE C 1 496  ? -23.067  122.761 56.103  1.00 171.78 ? 496  ILE B N   1 
ATOM   18162 C  CA  . ILE C 1 496  ? -22.093  121.792 56.557  1.00 167.75 ? 496  ILE B CA  1 
ATOM   18163 C  C   . ILE C 1 496  ? -20.671  122.343 56.448  1.00 171.74 ? 496  ILE B C   1 
ATOM   18164 O  O   . ILE C 1 496  ? -20.245  122.824 55.400  1.00 172.34 ? 496  ILE B O   1 
ATOM   18165 C  CB  . ILE C 1 496  ? -22.223  120.464 55.780  1.00 159.91 ? 496  ILE B CB  1 
ATOM   18166 C  CG1 . ILE C 1 496  ? -23.694  120.041 55.639  1.00 153.02 ? 496  ILE B CG1 1 
ATOM   18167 C  CG2 . ILE C 1 496  ? -21.431  119.385 56.468  1.00 161.88 ? 496  ILE B CG2 1 
ATOM   18168 C  CD1 . ILE C 1 496  ? -24.371  120.475 54.328  1.00 149.75 ? 496  ILE B CD1 1 
ATOM   18169 N  N   . THR C 1 497  ? -19.946  122.277 57.553  1.00 176.32 ? 497  THR B N   1 
ATOM   18170 C  CA  . THR C 1 497  ? -18.559  122.699 57.585  1.00 183.29 ? 497  THR B CA  1 
ATOM   18171 C  C   . THR C 1 497  ? -17.651  121.597 57.050  1.00 180.68 ? 497  THR B C   1 
ATOM   18172 O  O   . THR C 1 497  ? -17.093  121.712 55.961  1.00 181.89 ? 497  THR B O   1 
ATOM   18173 C  CB  . THR C 1 497  ? -18.140  123.058 59.020  1.00 189.82 ? 497  THR B CB  1 
ATOM   18174 O  OG1 . THR C 1 497  ? -16.715  123.177 59.093  1.00 192.74 ? 497  THR B OG1 1 
ATOM   18175 C  CG2 . THR C 1 497  ? -18.611  121.981 60.006  1.00 189.93 ? 497  THR B CG2 1 
ATOM   18176 N  N   . HIS C 1 498  ? -17.525  120.523 57.823  1.00 177.88 ? 498  HIS B N   1 
ATOM   18177 C  CA  . HIS C 1 498  ? -16.645  119.412 57.490  1.00 174.38 ? 498  HIS B CA  1 
ATOM   18178 C  C   . HIS C 1 498  ? -17.386  118.084 57.600  1.00 165.80 ? 498  HIS B C   1 
ATOM   18179 O  O   . HIS C 1 498  ? -18.245  117.911 58.473  1.00 167.44 ? 498  HIS B O   1 
ATOM   18180 C  CB  . HIS C 1 498  ? -15.470  119.354 58.466  1.00 178.74 ? 498  HIS B CB  1 
ATOM   18181 C  CG  . HIS C 1 498  ? -14.485  120.469 58.315  1.00 185.10 ? 498  HIS B CG  1 
ATOM   18182 N  ND1 . HIS C 1 498  ? -14.428  121.529 59.190  1.00 191.21 ? 498  HIS B ND1 1 
ATOM   18183 C  CD2 . HIS C 1 498  ? -13.499  120.669 57.410  1.00 187.19 ? 498  HIS B CD2 1 
ATOM   18184 C  CE1 . HIS C 1 498  ? -13.454  122.347 58.823  1.00 194.05 ? 498  HIS B CE1 1 
ATOM   18185 N  NE2 . HIS C 1 498  ? -12.875  121.847 57.748  1.00 191.79 ? 498  HIS B NE2 1 
ATOM   18186 N  N   . TYR C 1 499  ? -17.052  117.151 56.713  1.00 157.03 ? 499  TYR B N   1 
ATOM   18187 C  CA  . TYR C 1 499  ? -17.420  115.761 56.909  1.00 146.97 ? 499  TYR B CA  1 
ATOM   18188 C  C   . TYR C 1 499  ? -16.327  115.112 57.732  1.00 142.03 ? 499  TYR B C   1 
ATOM   18189 O  O   . TYR C 1 499  ? -15.150  115.350 57.474  1.00 140.81 ? 499  TYR B O   1 
ATOM   18190 C  CB  . TYR C 1 499  ? -17.530  115.035 55.577  1.00 143.46 ? 499  TYR B CB  1 
ATOM   18191 C  CG  . TYR C 1 499  ? -18.624  115.561 54.695  1.00 143.57 ? 499  TYR B CG  1 
ATOM   18192 C  CD1 . TYR C 1 499  ? -19.953  115.213 54.908  1.00 141.78 ? 499  TYR B CD1 1 
ATOM   18193 C  CD2 . TYR C 1 499  ? -18.331  116.410 53.649  1.00 145.23 ? 499  TYR B CD2 1 
ATOM   18194 C  CE1 . TYR C 1 499  ? -20.965  115.703 54.092  1.00 142.19 ? 499  TYR B CE1 1 
ATOM   18195 C  CE2 . TYR C 1 499  ? -19.323  116.898 52.824  1.00 145.99 ? 499  TYR B CE2 1 
ATOM   18196 C  CZ  . TYR C 1 499  ? -20.641  116.550 53.045  1.00 144.04 ? 499  TYR B CZ  1 
ATOM   18197 O  OH  . TYR C 1 499  ? -21.615  117.059 52.205  1.00 143.80 ? 499  TYR B OH  1 
ATOM   18198 N  N   . ASN C 1 500  ? -16.714  114.285 58.704  1.00 138.68 ? 500  ASN B N   1 
ATOM   18199 C  CA  . ASN C 1 500  ? -15.759  113.545 59.531  1.00 135.15 ? 500  ASN B CA  1 
ATOM   18200 C  C   . ASN C 1 500  ? -16.027  112.026 59.558  1.00 129.27 ? 500  ASN B C   1 
ATOM   18201 O  O   . ASN C 1 500  ? -17.141  111.575 59.831  1.00 127.90 ? 500  ASN B O   1 
ATOM   18202 C  CB  . ASN C 1 500  ? -15.767  114.084 60.963  1.00 139.23 ? 500  ASN B CB  1 
ATOM   18203 C  CG  . ASN C 1 500  ? -16.141  115.561 61.043  1.00 142.97 ? 500  ASN B CG  1 
ATOM   18204 O  OD1 . ASN C 1 500  ? -15.509  116.418 60.422  1.00 144.55 ? 500  ASN B OD1 1 
ATOM   18205 N  ND2 . ASN C 1 500  ? -17.163  115.863 61.837  1.00 143.97 ? 500  ASN B ND2 1 
ATOM   18206 N  N   . TYR C 1 501  ? -15.004  111.234 59.277  1.00 123.16 ? 501  TYR B N   1 
ATOM   18207 C  CA  . TYR C 1 501  ? -15.163  109.799 59.325  1.00 119.97 ? 501  TYR B CA  1 
ATOM   18208 C  C   . TYR C 1 501  ? -14.440  109.205 60.524  1.00 118.63 ? 501  TYR B C   1 
ATOM   18209 O  O   . TYR C 1 501  ? -13.830  109.916 61.324  1.00 119.93 ? 501  TYR B O   1 
ATOM   18210 C  CB  . TYR C 1 501  ? -14.630  109.164 58.056  1.00 120.03 ? 501  TYR B CB  1 
ATOM   18211 C  CG  . TYR C 1 501  ? -13.143  109.321 57.912  1.00 124.31 ? 501  TYR B CG  1 
ATOM   18212 C  CD1 . TYR C 1 501  ? -12.273  108.285 58.218  1.00 124.85 ? 501  TYR B CD1 1 
ATOM   18213 C  CD2 . TYR C 1 501  ? -12.608  110.512 57.481  1.00 128.75 ? 501  TYR B CD2 1 
ATOM   18214 C  CE1 . TYR C 1 501  ? -10.902  108.443 58.083  1.00 127.55 ? 501  TYR B CE1 1 
ATOM   18215 C  CE2 . TYR C 1 501  ? -11.251  110.684 57.342  1.00 131.44 ? 501  TYR B CE2 1 
ATOM   18216 C  CZ  . TYR C 1 501  ? -10.398  109.655 57.645  1.00 131.53 ? 501  TYR B CZ  1 
ATOM   18217 O  OH  . TYR C 1 501  ? -9.044   109.866 57.502  1.00 133.97 ? 501  TYR B OH  1 
ATOM   18218 N  N   . LEU C 1 502  ? -14.483  107.879 60.606  1.00 116.57 ? 502  LEU B N   1 
ATOM   18219 C  CA  . LEU C 1 502  ? -14.066  107.156 61.801  1.00 114.88 ? 502  LEU B CA  1 
ATOM   18220 C  C   . LEU C 1 502  ? -14.083  105.643 61.506  1.00 111.92 ? 502  LEU B C   1 
ATOM   18221 O  O   . LEU C 1 502  ? -15.145  105.055 61.325  1.00 110.12 ? 502  LEU B O   1 
ATOM   18222 C  CB  . LEU C 1 502  ? -15.035  107.521 62.934  1.00 111.21 ? 502  LEU B CB  1 
ATOM   18223 C  CG  . LEU C 1 502  ? -14.642  107.290 64.388  1.00 108.14 ? 502  LEU B CG  1 
ATOM   18224 C  CD1 . LEU C 1 502  ? -13.233  107.803 64.679  1.00 107.98 ? 502  LEU B CD1 1 
ATOM   18225 C  CD2 . LEU C 1 502  ? -15.699  107.942 65.263  1.00 109.31 ? 502  LEU B CD2 1 
ATOM   18226 N  N   . ILE C 1 503  ? -12.904  105.029 61.437  1.00 112.98 ? 503  ILE B N   1 
ATOM   18227 C  CA  . ILE C 1 503  ? -12.792  103.638 61.003  1.00 110.51 ? 503  ILE B CA  1 
ATOM   18228 C  C   . ILE C 1 503  ? -12.254  102.712 62.092  1.00 113.56 ? 503  ILE B C   1 
ATOM   18229 O  O   . ILE C 1 503  ? -11.115  102.877 62.546  1.00 114.02 ? 503  ILE B O   1 
ATOM   18230 C  CB  . ILE C 1 503  ? -11.883  103.504 59.756  1.00 111.35 ? 503  ILE B CB  1 
ATOM   18231 C  CG1 . ILE C 1 503  ? -12.306  104.492 58.663  1.00 112.21 ? 503  ILE B CG1 1 
ATOM   18232 C  CG2 . ILE C 1 503  ? -11.901  102.077 59.234  1.00 107.93 ? 503  ILE B CG2 1 
ATOM   18233 C  CD1 . ILE C 1 503  ? -11.407  104.495 57.420  1.00 110.87 ? 503  ILE B CD1 1 
ATOM   18234 N  N   . LEU C 1 504  ? -13.074  101.733 62.491  1.00 112.12 ? 504  LEU B N   1 
ATOM   18235 C  CA  . LEU C 1 504  ? -12.702  100.730 63.498  1.00 111.99 ? 504  LEU B CA  1 
ATOM   18236 C  C   . LEU C 1 504  ? -12.282  99.423  62.835  1.00 116.07 ? 504  LEU B C   1 
ATOM   18237 O  O   . LEU C 1 504  ? -12.534  99.217  61.654  1.00 116.42 ? 504  LEU B O   1 
ATOM   18238 C  CB  . LEU C 1 504  ? -13.874  100.425 64.424  1.00 107.42 ? 504  LEU B CB  1 
ATOM   18239 C  CG  . LEU C 1 504  ? -14.522  101.502 65.277  1.00 105.22 ? 504  LEU B CG  1 
ATOM   18240 C  CD1 . LEU C 1 504  ? -14.269  102.889 64.728  1.00 107.30 ? 504  LEU B CD1 1 
ATOM   18241 C  CD2 . LEU C 1 504  ? -16.012  101.232 65.359  1.00 99.48  ? 504  LEU B CD2 1 
ATOM   18242 N  N   . SER C 1 505  ? -11.676  98.526  63.606  1.00 118.67 ? 505  SER B N   1 
ATOM   18243 C  CA  . SER C 1 505  ? -11.312  97.200  63.111  1.00 118.81 ? 505  SER B CA  1 
ATOM   18244 C  C   . SER C 1 505  ? -10.714  96.309  64.194  1.00 121.21 ? 505  SER B C   1 
ATOM   18245 O  O   . SER C 1 505  ? -9.700   96.637  64.814  1.00 121.20 ? 505  SER B O   1 
ATOM   18246 C  CB  . SER C 1 505  ? -10.339  97.297  61.945  1.00 117.22 ? 505  SER B CB  1 
ATOM   18247 O  OG  . SER C 1 505  ? -10.003  95.995  61.509  1.00 115.44 ? 505  SER B OG  1 
ATOM   18248 N  N   . LYS C 1 506  ? -11.332  95.158  64.393  1.00 123.43 ? 506  LYS B N   1 
ATOM   18249 C  CA  . LYS C 1 506  ? -10.964  94.330  65.510  1.00 125.92 ? 506  LYS B CA  1 
ATOM   18250 C  C   . LYS C 1 506  ? -11.144  95.186  66.719  1.00 128.76 ? 506  LYS B C   1 
ATOM   18251 O  O   . LYS C 1 506  ? -10.179  95.502  67.403  1.00 132.47 ? 506  LYS B O   1 
ATOM   18252 C  CB  . LYS C 1 506  ? -9.519   93.869  65.407  1.00 124.67 ? 506  LYS B CB  1 
ATOM   18253 C  CG  . LYS C 1 506  ? -9.347   92.719  64.451  1.00 120.67 ? 506  LYS B CG  1 
ATOM   18254 C  CD  . LYS C 1 506  ? -7.940   92.667  63.949  1.00 118.91 ? 506  LYS B CD  1 
ATOM   18255 C  CE  . LYS C 1 506  ? -7.508   94.031  63.461  1.00 119.26 ? 506  LYS B CE  1 
ATOM   18256 N  NZ  . LYS C 1 506  ? -8.056   94.338  62.135  1.00 117.12 ? 506  LYS B NZ  1 
ATOM   18257 N  N   . GLY C 1 507  ? -12.388  95.609  66.928  1.00 129.21 ? 507  GLY B N   1 
ATOM   18258 C  CA  . GLY C 1 507  ? -12.803  96.281  68.152  1.00 133.53 ? 507  GLY B CA  1 
ATOM   18259 C  C   . GLY C 1 507  ? -12.178  97.635  68.472  1.00 138.05 ? 507  GLY B C   1 
ATOM   18260 O  O   . GLY C 1 507  ? -12.447  98.213  69.542  1.00 139.97 ? 507  GLY B O   1 
ATOM   18261 N  N   . LYS C 1 508  ? -11.364  98.143  67.541  1.00 139.32 ? 508  LYS B N   1 
ATOM   18262 C  CA  . LYS C 1 508  ? -10.573  99.361  67.756  1.00 140.36 ? 508  LYS B CA  1 
ATOM   18263 C  C   . LYS C 1 508  ? -10.642  100.355 66.602  1.00 136.22 ? 508  LYS B C   1 
ATOM   18264 O  O   . LYS C 1 508  ? -10.475  100.001 65.447  1.00 133.68 ? 508  LYS B O   1 
ATOM   18265 C  CB  . LYS C 1 508  ? -9.095   99.023  68.032  1.00 142.92 ? 508  LYS B CB  1 
ATOM   18266 C  CG  . LYS C 1 508  ? -8.756   98.953  69.508  1.00 146.18 ? 508  LYS B CG  1 
ATOM   18267 C  CD  . LYS C 1 508  ? -7.464   98.209  69.779  1.00 146.39 ? 508  LYS B CD  1 
ATOM   18268 C  CE  . LYS C 1 508  ? -7.544   97.534  71.152  1.00 148.31 ? 508  LYS B CE  1 
ATOM   18269 N  NZ  . LYS C 1 508  ? -6.474   96.527  71.399  1.00 147.66 ? 508  LYS B NZ  1 
ATOM   18270 N  N   . ILE C 1 509  ? -10.886  101.610 66.936  1.00 133.46 ? 509  ILE B N   1 
ATOM   18271 C  CA  . ILE C 1 509  ? -10.713  102.702 66.003  1.00 128.58 ? 509  ILE B CA  1 
ATOM   18272 C  C   . ILE C 1 509  ? -9.254   102.780 65.589  1.00 126.78 ? 509  ILE B C   1 
ATOM   18273 O  O   . ILE C 1 509  ? -8.368   102.746 66.436  1.00 128.12 ? 509  ILE B O   1 
ATOM   18274 C  CB  . ILE C 1 509  ? -11.070  104.003 66.694  1.00 129.32 ? 509  ILE B CB  1 
ATOM   18275 C  CG1 . ILE C 1 509  ? -12.433  103.856 67.360  1.00 126.77 ? 509  ILE B CG1 1 
ATOM   18276 C  CG2 . ILE C 1 509  ? -11.023  105.165 65.712  1.00 130.12 ? 509  ILE B CG2 1 
ATOM   18277 C  CD1 . ILE C 1 509  ? -12.842  105.035 68.187  1.00 129.02 ? 509  ILE B CD1 1 
ATOM   18278 N  N   . ILE C 1 510  ? -8.998   102.906 64.292  1.00 124.01 ? 510  ILE B N   1 
ATOM   18279 C  CA  . ILE C 1 510  ? -7.620   102.955 63.800  1.00 124.25 ? 510  ILE B CA  1 
ATOM   18280 C  C   . ILE C 1 510  ? -7.351   104.135 62.851  1.00 126.25 ? 510  ILE B C   1 
ATOM   18281 O  O   . ILE C 1 510  ? -6.203   104.532 62.624  1.00 125.51 ? 510  ILE B O   1 
ATOM   18282 C  CB  . ILE C 1 510  ? -7.204   101.619 63.125  1.00 130.89 ? 510  ILE B CB  1 
ATOM   18283 C  CG1 . ILE C 1 510  ? -8.416   100.927 62.502  1.00 127.91 ? 510  ILE B CG1 1 
ATOM   18284 C  CG2 . ILE C 1 510  ? -6.533   100.676 64.125  1.00 131.02 ? 510  ILE B CG2 1 
ATOM   18285 C  CD1 . ILE C 1 510  ? -8.059   99.627  61.801  1.00 125.03 ? 510  ILE B CD1 1 
ATOM   18286 N  N   . HIS C 1 511  ? -8.418   104.696 62.305  1.00 129.69 ? 511  HIS B N   1 
ATOM   18287 C  CA  . HIS C 1 511  ? -8.288   105.871 61.473  1.00 134.97 ? 511  HIS B CA  1 
ATOM   18288 C  C   . HIS C 1 511  ? -9.432   106.799 61.799  1.00 138.60 ? 511  HIS B C   1 
ATOM   18289 O  O   . HIS C 1 511  ? -10.459  106.374 62.330  1.00 137.65 ? 511  HIS B O   1 
ATOM   18290 C  CB  . HIS C 1 511  ? -8.337   105.499 59.993  1.00 136.37 ? 511  HIS B CB  1 
ATOM   18291 C  CG  . HIS C 1 511  ? -7.432   104.368 59.624  1.00 137.69 ? 511  HIS B CG  1 
ATOM   18292 N  ND1 . HIS C 1 511  ? -6.061   104.497 59.581  1.00 139.76 ? 511  HIS B ND1 1 
ATOM   18293 C  CD2 . HIS C 1 511  ? -7.700   103.086 59.279  1.00 135.38 ? 511  HIS B CD2 1 
ATOM   18294 C  CE1 . HIS C 1 511  ? -5.521   103.343 59.233  1.00 138.01 ? 511  HIS B CE1 1 
ATOM   18295 N  NE2 . HIS C 1 511  ? -6.495   102.470 59.043  1.00 135.41 ? 511  HIS B NE2 1 
ATOM   18296 N  N   . PHE C 1 512  ? -9.243   108.071 61.482  1.00 142.58 ? 512  PHE B N   1 
ATOM   18297 C  CA  . PHE C 1 512  ? -10.255  109.090 61.703  1.00 147.32 ? 512  PHE B CA  1 
ATOM   18298 C  C   . PHE C 1 512  ? -9.730   110.359 61.070  1.00 146.34 ? 512  PHE B C   1 
ATOM   18299 O  O   . PHE C 1 512  ? -8.522   110.556 60.989  1.00 145.55 ? 512  PHE B O   1 
ATOM   18300 C  CB  . PHE C 1 512  ? -10.481  109.309 63.193  1.00 154.36 ? 512  PHE B CB  1 
ATOM   18301 C  CG  . PHE C 1 512  ? -9.292   109.878 63.897  1.00 160.65 ? 512  PHE B CG  1 
ATOM   18302 C  CD1 . PHE C 1 512  ? -9.400   111.026 64.651  1.00 165.46 ? 512  PHE B CD1 1 
ATOM   18303 C  CD2 . PHE C 1 512  ? -8.052   109.269 63.780  1.00 161.77 ? 512  PHE B CD2 1 
ATOM   18304 C  CE1 . PHE C 1 512  ? -8.296   111.542 65.287  1.00 168.79 ? 512  PHE B CE1 1 
ATOM   18305 C  CE2 . PHE C 1 512  ? -6.946   109.781 64.410  1.00 164.40 ? 512  PHE B CE2 1 
ATOM   18306 C  CZ  . PHE C 1 512  ? -7.065   110.920 65.163  1.00 168.21 ? 512  PHE B CZ  1 
ATOM   18307 N  N   . GLY C 1 513  ? -10.627  111.218 60.608  1.00 148.42 ? 513  GLY B N   1 
ATOM   18308 C  CA  . GLY C 1 513  ? -10.191  112.395 59.878  1.00 151.09 ? 513  GLY B CA  1 
ATOM   18309 C  C   . GLY C 1 513  ? -11.285  113.338 59.416  1.00 152.22 ? 513  GLY B C   1 
ATOM   18310 O  O   . GLY C 1 513  ? -12.449  113.230 59.819  1.00 150.42 ? 513  GLY B O   1 
ATOM   18311 N  N   . THR C 1 514  ? -10.908  114.275 58.556  1.00 154.35 ? 514  THR B N   1 
ATOM   18312 C  CA  . THR C 1 514  ? -11.852  115.288 58.122  1.00 156.38 ? 514  THR B CA  1 
ATOM   18313 C  C   . THR C 1 514  ? -11.571  115.808 56.710  1.00 156.34 ? 514  THR B C   1 
ATOM   18314 O  O   . THR C 1 514  ? -10.441  116.151 56.374  1.00 156.74 ? 514  THR B O   1 
ATOM   18315 C  CB  . THR C 1 514  ? -11.926  116.443 59.156  1.00 163.29 ? 514  THR B CB  1 
ATOM   18316 O  OG1 . THR C 1 514  ? -12.829  116.082 60.209  1.00 163.09 ? 514  THR B OG1 1 
ATOM   18317 C  CG2 . THR C 1 514  ? -12.416  117.732 58.524  1.00 165.83 ? 514  THR B CG2 1 
ATOM   18318 N  N   . ARG C 1 515  ? -12.609  115.819 55.880  1.00 155.25 ? 515  ARG B N   1 
ATOM   18319 C  CA  . ARG C 1 515  ? -12.543  116.472 54.586  1.00 159.04 ? 515  ARG B CA  1 
ATOM   18320 C  C   . ARG C 1 515  ? -13.382  117.727 54.660  1.00 159.99 ? 515  ARG B C   1 
ATOM   18321 O  O   . ARG C 1 515  ? -14.474  117.706 55.232  1.00 159.49 ? 515  ARG B O   1 
ATOM   18322 C  CB  . ARG C 1 515  ? -13.085  115.562 53.485  1.00 161.41 ? 515  ARG B CB  1 
ATOM   18323 C  CG  . ARG C 1 515  ? -12.471  114.195 53.483  1.00 163.80 ? 515  ARG B CG  1 
ATOM   18324 C  CD  . ARG C 1 515  ? -10.976  114.289 53.683  1.00 169.97 ? 515  ARG B CD  1 
ATOM   18325 N  NE  . ARG C 1 515  ? -10.369  112.970 53.691  1.00 171.78 ? 515  ARG B NE  1 
ATOM   18326 C  CZ  . ARG C 1 515  ? -10.371  112.157 52.642  1.00 173.80 ? 515  ARG B CZ  1 
ATOM   18327 N  NH1 . ARG C 1 515  ? -10.953  112.532 51.503  1.00 174.92 ? 515  ARG B NH1 1 
ATOM   18328 N  NH2 . ARG C 1 515  ? -9.800   110.965 52.732  1.00 173.30 ? 515  ARG B NH2 1 
ATOM   18329 N  N   . GLU C 1 516  ? -12.882  118.819 54.089  1.00 160.02 ? 516  GLU B N   1 
ATOM   18330 C  CA  . GLU C 1 516  ? -13.678  120.031 54.026  1.00 160.34 ? 516  GLU B CA  1 
ATOM   18331 C  C   . GLU C 1 516  ? -14.822  119.803 53.050  1.00 154.81 ? 516  GLU B C   1 
ATOM   18332 O  O   . GLU C 1 516  ? -14.645  119.134 52.036  1.00 150.72 ? 516  GLU B O   1 
ATOM   18333 C  CB  . GLU C 1 516  ? -12.828  121.242 53.630  1.00 163.99 ? 516  GLU B CB  1 
ATOM   18334 C  CG  . GLU C 1 516  ? -13.647  122.530 53.516  1.00 168.00 ? 516  GLU B CG  1 
ATOM   18335 C  CD  . GLU C 1 516  ? -12.994  123.751 54.163  1.00 172.69 ? 516  GLU B CD  1 
ATOM   18336 O  OE1 . GLU C 1 516  ? -13.263  124.868 53.688  1.00 174.80 ? 516  GLU B OE1 1 
ATOM   18337 O  OE2 . GLU C 1 516  ? -12.241  123.608 55.151  1.00 174.25 ? 516  GLU B OE2 1 
ATOM   18338 N  N   . LYS C 1 517  ? -16.002  120.324 53.376  1.00 156.23 ? 517  LYS B N   1 
ATOM   18339 C  CA  . LYS C 1 517  ? -17.167  120.149 52.516  1.00 156.14 ? 517  LYS B CA  1 
ATOM   18340 C  C   . LYS C 1 517  ? -17.159  121.112 51.338  1.00 164.11 ? 517  LYS B C   1 
ATOM   18341 O  O   . LYS C 1 517  ? -16.951  122.316 51.510  1.00 169.90 ? 517  LYS B O   1 
ATOM   18342 C  CB  . LYS C 1 517  ? -18.465  120.320 53.302  1.00 152.48 ? 517  LYS B CB  1 
ATOM   18343 C  CG  . LYS C 1 517  ? -19.704  119.827 52.544  1.00 147.76 ? 517  LYS B CG  1 
ATOM   18344 C  CD  . LYS C 1 517  ? -20.591  120.930 51.972  1.00 147.87 ? 517  LYS B CD  1 
ATOM   18345 C  CE  . LYS C 1 517  ? -21.903  120.346 51.429  1.00 144.01 ? 517  LYS B CE  1 
ATOM   18346 N  NZ  . LYS C 1 517  ? -23.104  121.203 51.722  1.00 145.21 ? 517  LYS B NZ  1 
ATOM   18347 N  N   . PHE C 1 518  ? -17.412  120.588 50.143  1.00 165.75 ? 518  PHE B N   1 
ATOM   18348 C  CA  . PHE C 1 518  ? -17.426  121.416 48.945  1.00 171.17 ? 518  PHE B CA  1 
ATOM   18349 C  C   . PHE C 1 518  ? -18.583  122.403 48.929  1.00 175.55 ? 518  PHE B C   1 
ATOM   18350 O  O   . PHE C 1 518  ? -19.720  122.051 48.612  1.00 171.75 ? 518  PHE B O   1 
ATOM   18351 C  CB  . PHE C 1 518  ? -17.420  120.542 47.703  1.00 172.23 ? 518  PHE B CB  1 
ATOM   18352 C  CG  . PHE C 1 518  ? -16.079  119.956 47.408  1.00 176.13 ? 518  PHE B CG  1 
ATOM   18353 C  CD1 . PHE C 1 518  ? -14.938  120.553 47.918  1.00 180.04 ? 518  PHE B CD1 1 
ATOM   18354 C  CD2 . PHE C 1 518  ? -15.949  118.830 46.608  1.00 176.13 ? 518  PHE B CD2 1 
ATOM   18355 C  CE1 . PHE C 1 518  ? -13.694  120.035 47.651  1.00 181.03 ? 518  PHE B CE1 1 
ATOM   18356 C  CE2 . PHE C 1 518  ? -14.703  118.302 46.331  1.00 176.92 ? 518  PHE B CE2 1 
ATOM   18357 C  CZ  . PHE C 1 518  ? -13.572  118.907 46.856  1.00 179.28 ? 518  PHE B CZ  1 
ATOM   18358 N  N   . SER C 1 519  ? -18.247  123.648 49.254  1.00 184.29 ? 519  SER B N   1 
ATOM   18359 C  CA  . SER C 1 519  ? -19.208  124.703 49.538  1.00 190.77 ? 519  SER B CA  1 
ATOM   18360 C  C   . SER C 1 519  ? -20.404  124.651 48.618  1.00 193.20 ? 519  SER B C   1 
ATOM   18361 O  O   . SER C 1 519  ? -21.552  124.657 49.054  1.00 195.67 ? 519  SER B O   1 
ATOM   18362 C  CB  . SER C 1 519  ? -18.527  126.064 49.412  1.00 193.99 ? 519  SER B CB  1 
ATOM   18363 O  OG  . SER C 1 519  ? -17.204  126.013 49.912  1.00 193.89 ? 519  SER B OG  1 
ATOM   18364 N  N   . ASP C 1 520  ? -20.120  124.609 47.329  1.00 193.08 ? 520  ASP B N   1 
ATOM   18365 C  CA  . ASP C 1 520  ? -21.167  124.508 46.336  1.00 195.00 ? 520  ASP B CA  1 
ATOM   18366 C  C   . ASP C 1 520  ? -21.972  123.218 46.508  1.00 189.63 ? 520  ASP B C   1 
ATOM   18367 O  O   . ASP C 1 520  ? -22.842  123.146 47.376  1.00 189.59 ? 520  ASP B O   1 
ATOM   18368 C  CB  . ASP C 1 520  ? -20.582  124.601 44.922  1.00 203.57 ? 520  ASP B CB  1 
ATOM   18369 C  CG  . ASP C 1 520  ? -19.371  123.698 44.721  1.00 211.93 ? 520  ASP B CG  1 
ATOM   18370 O  OD1 . ASP C 1 520  ? -18.959  123.012 45.685  1.00 214.67 ? 520  ASP B OD1 1 
ATOM   18371 O  OD2 . ASP C 1 520  ? -18.835  123.678 43.590  1.00 215.88 ? 520  ASP B OD2 1 
ATOM   18372 N  N   . ALA C 1 521  ? -21.648  122.196 45.711  1.00 183.51 ? 521  ALA B N   1 
ATOM   18373 C  CA  . ALA C 1 521  ? -22.524  121.039 45.514  1.00 174.67 ? 521  ALA B CA  1 
ATOM   18374 C  C   . ALA C 1 521  ? -22.818  120.186 46.752  1.00 161.46 ? 521  ALA B C   1 
ATOM   18375 O  O   . ALA C 1 521  ? -22.184  120.322 47.801  1.00 160.70 ? 521  ALA B O   1 
ATOM   18376 C  CB  . ALA C 1 521  ? -22.020  120.173 44.351  1.00 175.19 ? 521  ALA B CB  1 
ATOM   18377 N  N   . SER C 1 522  ? -23.805  119.310 46.592  1.00 149.90 ? 522  SER B N   1 
ATOM   18378 C  CA  . SER C 1 522  ? -24.243  118.388 47.630  1.00 141.01 ? 522  SER B CA  1 
ATOM   18379 C  C   . SER C 1 522  ? -23.136  117.417 48.086  1.00 134.08 ? 522  SER B C   1 
ATOM   18380 O  O   . SER C 1 522  ? -22.379  117.694 49.036  1.00 135.22 ? 522  SER B O   1 
ATOM   18381 C  CB  . SER C 1 522  ? -25.457  117.591 47.121  1.00 137.55 ? 522  SER B CB  1 
ATOM   18382 O  OG  . SER C 1 522  ? -26.005  116.745 48.129  1.00 135.72 ? 522  SER B OG  1 
ATOM   18383 N  N   . TYR C 1 523  ? -23.051  116.283 47.394  1.00 125.34 ? 523  TYR B N   1 
ATOM   18384 C  CA  . TYR C 1 523  ? -22.177  115.194 47.790  1.00 117.23 ? 523  TYR B CA  1 
ATOM   18385 C  C   . TYR C 1 523  ? -20.783  115.321 47.253  1.00 113.83 ? 523  TYR B C   1 
ATOM   18386 O  O   . TYR C 1 523  ? -20.575  115.807 46.143  1.00 112.75 ? 523  TYR B O   1 
ATOM   18387 C  CB  . TYR C 1 523  ? -22.730  113.884 47.245  1.00 114.32 ? 523  TYR B CB  1 
ATOM   18388 C  CG  . TYR C 1 523  ? -22.941  113.852 45.730  1.00 112.87 ? 523  TYR B CG  1 
ATOM   18389 C  CD1 . TYR C 1 523  ? -21.915  113.496 44.857  1.00 111.97 ? 523  TYR B CD1 1 
ATOM   18390 C  CD2 . TYR C 1 523  ? -24.177  114.150 45.182  1.00 111.23 ? 523  TYR B CD2 1 
ATOM   18391 C  CE1 . TYR C 1 523  ? -22.120  113.456 43.494  1.00 110.21 ? 523  TYR B CE1 1 
ATOM   18392 C  CE2 . TYR C 1 523  ? -24.386  114.102 43.834  1.00 108.95 ? 523  TYR B CE2 1 
ATOM   18393 C  CZ  . TYR C 1 523  ? -23.359  113.763 42.996  1.00 109.45 ? 523  TYR B CZ  1 
ATOM   18394 O  OH  . TYR C 1 523  ? -23.584  113.727 41.644  1.00 110.26 ? 523  TYR B OH  1 
ATOM   18395 N  N   . GLN C 1 524  ? -19.824  114.820 48.009  1.00 114.06 ? 524  GLN B N   1 
ATOM   18396 C  CA  . GLN C 1 524  ? -18.535  114.542 47.408  1.00 117.63 ? 524  GLN B CA  1 
ATOM   18397 C  C   . GLN C 1 524  ? -18.017  113.137 47.716  1.00 118.70 ? 524  GLN B C   1 
ATOM   18398 O  O   . GLN C 1 524  ? -18.748  112.279 48.227  1.00 118.17 ? 524  GLN B O   1 
ATOM   18399 C  CB  . GLN C 1 524  ? -17.519  115.577 47.827  1.00 120.09 ? 524  GLN B CB  1 
ATOM   18400 C  CG  . GLN C 1 524  ? -17.233  115.569 49.278  1.00 120.60 ? 524  GLN B CG  1 
ATOM   18401 C  CD  . GLN C 1 524  ? -17.039  116.958 49.781  1.00 125.26 ? 524  GLN B CD  1 
ATOM   18402 O  OE1 . GLN C 1 524  ? -17.850  117.840 49.493  1.00 126.24 ? 524  GLN B OE1 1 
ATOM   18403 N  NE2 . GLN C 1 524  ? -15.951  117.182 50.523  1.00 127.64 ? 524  GLN B NE2 1 
ATOM   18404 N  N   . SER C 1 525  ? -16.764  112.893 47.352  1.00 120.04 ? 525  SER B N   1 
ATOM   18405 C  CA  . SER C 1 525  ? -16.156  111.598 47.582  1.00 119.65 ? 525  SER B CA  1 
ATOM   18406 C  C   . SER C 1 525  ? -15.153  111.775 48.705  1.00 120.30 ? 525  SER B C   1 
ATOM   18407 O  O   . SER C 1 525  ? -14.559  112.850 48.842  1.00 120.21 ? 525  SER B O   1 
ATOM   18408 C  CB  . SER C 1 525  ? -15.447  111.080 46.320  1.00 120.69 ? 525  SER B CB  1 
ATOM   18409 O  OG  . SER C 1 525  ? -16.192  111.315 45.128  1.00 122.68 ? 525  SER B OG  1 
ATOM   18410 N  N   . ILE C 1 526  ? -15.007  110.737 49.530  1.00 119.87 ? 526  ILE B N   1 
ATOM   18411 C  CA  . ILE C 1 526  ? -13.933  110.664 50.518  1.00 116.64 ? 526  ILE B CA  1 
ATOM   18412 C  C   . ILE C 1 526  ? -13.053  109.493 50.130  1.00 111.83 ? 526  ILE B C   1 
ATOM   18413 O  O   . ILE C 1 526  ? -13.521  108.366 50.026  1.00 106.80 ? 526  ILE B O   1 
ATOM   18414 C  CB  . ILE C 1 526  ? -14.451  110.431 51.951  1.00 110.57 ? 526  ILE B CB  1 
ATOM   18415 C  CG1 . ILE C 1 526  ? -15.571  111.404 52.315  1.00 110.19 ? 526  ILE B CG1 1 
ATOM   18416 C  CG2 . ILE C 1 526  ? -13.324  110.597 52.932  1.00 112.84 ? 526  ILE B CG2 1 
ATOM   18417 C  CD1 . ILE C 1 526  ? -15.898  111.460 53.793  1.00 103.00 ? 526  ILE B CD1 1 
ATOM   18418 N  N   . ASN C 1 527  ? -11.777  109.738 49.905  1.00 118.06 ? 527  ASN B N   1 
ATOM   18419 C  CA  . ASN C 1 527  ? -10.960  108.630 49.474  1.00 121.05 ? 527  ASN B CA  1 
ATOM   18420 C  C   . ASN C 1 527  ? -10.026  108.044 50.521  1.00 125.87 ? 527  ASN B C   1 
ATOM   18421 O  O   . ASN C 1 527  ? -8.930   108.551 50.756  1.00 128.70 ? 527  ASN B O   1 
ATOM   18422 C  CB  . ASN C 1 527  ? -10.189  108.988 48.230  1.00 124.11 ? 527  ASN B CB  1 
ATOM   18423 C  CG  . ASN C 1 527  ? -9.801   107.773 47.453  1.00 124.14 ? 527  ASN B CG  1 
ATOM   18424 O  OD1 . ASN C 1 527  ? -8.991   106.961 47.905  1.00 122.63 ? 527  ASN B OD1 1 
ATOM   18425 N  ND2 . ASN C 1 527  ? -10.393  107.620 46.277  1.00 125.82 ? 527  ASN B ND2 1 
ATOM   18426 N  N   . ILE C 1 528  ? -10.460  106.947 51.126  1.00 127.29 ? 528  ILE B N   1 
ATOM   18427 C  CA  . ILE C 1 528  ? -9.658   106.264 52.123  1.00 131.19 ? 528  ILE B CA  1 
ATOM   18428 C  C   . ILE C 1 528  ? -8.865   105.122 51.521  1.00 129.77 ? 528  ILE B C   1 
ATOM   18429 O  O   . ILE C 1 528  ? -9.436   104.197 50.936  1.00 129.05 ? 528  ILE B O   1 
ATOM   18430 C  CB  . ILE C 1 528  ? -10.538  105.663 53.218  1.00 132.01 ? 528  ILE B CB  1 
ATOM   18431 C  CG1 . ILE C 1 528  ? -11.569  106.686 53.673  1.00 135.17 ? 528  ILE B CG1 1 
ATOM   18432 C  CG2 . ILE C 1 528  ? -9.696   105.137 54.377  1.00 134.56 ? 528  ILE B CG2 1 
ATOM   18433 C  CD1 . ILE C 1 528  ? -12.792  106.666 52.826  1.00 134.24 ? 528  ILE B CD1 1 
ATOM   18434 N  N   . PRO C 1 529  ? -7.540   105.178 51.661  1.00 131.18 ? 529  PRO B N   1 
ATOM   18435 C  CA  . PRO C 1 529  ? -6.748   103.978 51.416  1.00 129.55 ? 529  PRO B CA  1 
ATOM   18436 C  C   . PRO C 1 529  ? -7.291   102.810 52.255  1.00 130.20 ? 529  PRO B C   1 
ATOM   18437 O  O   . PRO C 1 529  ? -7.742   103.035 53.380  1.00 131.27 ? 529  PRO B O   1 
ATOM   18438 C  CB  . PRO C 1 529  ? -5.363   104.395 51.912  1.00 131.72 ? 529  PRO B CB  1 
ATOM   18439 C  CG  . PRO C 1 529  ? -5.311   105.854 51.684  1.00 133.84 ? 529  PRO B CG  1 
ATOM   18440 C  CD  . PRO C 1 529  ? -6.704   106.364 51.901  1.00 133.37 ? 529  PRO B CD  1 
ATOM   18441 N  N   . VAL C 1 530  ? -7.282   101.591 51.725  1.00 126.47 ? 530  VAL B N   1 
ATOM   18442 C  CA  . VAL C 1 530  ? -7.491   100.430 52.582  1.00 124.46 ? 530  VAL B CA  1 
ATOM   18443 C  C   . VAL C 1 530  ? -6.117   100.048 53.153  1.00 123.34 ? 530  VAL B C   1 
ATOM   18444 O  O   . VAL C 1 530  ? -5.175   99.803  52.398  1.00 122.98 ? 530  VAL B O   1 
ATOM   18445 C  CB  . VAL C 1 530  ? -8.175   99.244  51.830  1.00 98.38  ? 530  VAL B CB  1 
ATOM   18446 C  CG1 . VAL C 1 530  ? -7.160   98.352  51.203  1.00 97.33  ? 530  VAL B CG1 1 
ATOM   18447 C  CG2 . VAL C 1 530  ? -9.027   98.422  52.771  1.00 97.01  ? 530  VAL B CG2 1 
ATOM   18448 N  N   . THR C 1 531  ? -5.984   100.060 54.480  1.00 123.49 ? 531  THR B N   1 
ATOM   18449 C  CA  . THR C 1 531  ? -4.708   99.711  55.106  1.00 124.35 ? 531  THR B CA  1 
ATOM   18450 C  C   . THR C 1 531  ? -4.667   98.327  55.717  1.00 123.76 ? 531  THR B C   1 
ATOM   18451 O  O   . THR C 1 531  ? -5.683   97.773  56.136  1.00 122.01 ? 531  THR B O   1 
ATOM   18452 C  CB  . THR C 1 531  ? -4.295   100.665 56.222  1.00 127.58 ? 531  THR B CB  1 
ATOM   18453 O  OG1 . THR C 1 531  ? -2.941   100.378 56.596  1.00 128.75 ? 531  THR B OG1 1 
ATOM   18454 C  CG2 . THR C 1 531  ? -5.172   100.467 57.438  1.00 127.16 ? 531  THR B CG2 1 
ATOM   18455 N  N   . GLN C 1 532  ? -3.454   97.802  55.804  1.00 125.73 ? 532  GLN B N   1 
ATOM   18456 C  CA  . GLN C 1 532  ? -3.219   96.496  56.369  1.00 126.56 ? 532  GLN B CA  1 
ATOM   18457 C  C   . GLN C 1 532  ? -3.798   96.376  57.779  1.00 128.58 ? 532  GLN B C   1 
ATOM   18458 O  O   . GLN C 1 532  ? -4.031   95.278  58.263  1.00 128.00 ? 532  GLN B O   1 
ATOM   18459 C  CB  . GLN C 1 532  ? -1.721   96.215  56.369  1.00 129.06 ? 532  GLN B CB  1 
ATOM   18460 C  CG  . GLN C 1 532  ? -1.329   94.915  57.054  1.00 129.53 ? 532  GLN B CG  1 
ATOM   18461 C  CD  . GLN C 1 532  ? -1.623   93.673  56.222  1.00 126.91 ? 532  GLN B CD  1 
ATOM   18462 O  OE1 . GLN C 1 532  ? -1.838   93.757  55.009  1.00 126.64 ? 532  GLN B OE1 1 
ATOM   18463 N  NE2 . GLN C 1 532  ? -1.625   92.507  56.879  1.00 124.34 ? 532  GLN B NE2 1 
ATOM   18464 N  N   . ASN C 1 533  ? -4.039   97.500  58.441  1.00 130.59 ? 533  ASN B N   1 
ATOM   18465 C  CA  . ASN C 1 533  ? -4.666   97.455  59.760  1.00 131.45 ? 533  ASN B CA  1 
ATOM   18466 C  C   . ASN C 1 533  ? -6.152   97.116  59.699  1.00 128.16 ? 533  ASN B C   1 
ATOM   18467 O  O   . ASN C 1 533  ? -6.752   96.763  60.714  1.00 128.50 ? 533  ASN B O   1 
ATOM   18468 C  CB  . ASN C 1 533  ? -4.477   98.776  60.507  1.00 136.19 ? 533  ASN B CB  1 
ATOM   18469 C  CG  . ASN C 1 533  ? -3.029   99.109  60.732  1.00 140.14 ? 533  ASN B CG  1 
ATOM   18470 O  OD1 . ASN C 1 533  ? -2.534   100.123 60.239  1.00 143.27 ? 533  ASN B OD1 1 
ATOM   18471 N  ND2 . ASN C 1 533  ? -2.331   98.253  61.468  1.00 140.17 ? 533  ASN B ND2 1 
ATOM   18472 N  N   . MET C 1 534  ? -6.744   97.242  58.515  1.00 124.34 ? 534  MET B N   1 
ATOM   18473 C  CA  . MET C 1 534  ? -8.165   96.999  58.338  1.00 120.18 ? 534  MET B CA  1 
ATOM   18474 C  C   . MET C 1 534  ? -8.411   95.534  58.026  1.00 115.16 ? 534  MET B C   1 
ATOM   18475 O  O   . MET C 1 534  ? -9.548   95.108  57.879  1.00 113.31 ? 534  MET B O   1 
ATOM   18476 C  CB  . MET C 1 534  ? -8.688   97.883  57.212  1.00 119.03 ? 534  MET B CB  1 
ATOM   18477 C  CG  . MET C 1 534  ? -8.087   99.268  57.238  1.00 121.41 ? 534  MET B CG  1 
ATOM   18478 S  SD  . MET C 1 534  ? -8.438   100.283 55.802  1.00 116.60 ? 534  MET B SD  1 
ATOM   18479 C  CE  . MET C 1 534  ? -10.169  100.608 56.053  1.00 92.03  ? 534  MET B CE  1 
ATOM   18480 N  N   . VAL C 1 535  ? -7.328   94.764  57.995  1.00 114.58 ? 535  VAL B N   1 
ATOM   18481 C  CA  . VAL C 1 535  ? -7.259   93.465  57.305  1.00 112.28 ? 535  VAL B CA  1 
ATOM   18482 C  C   . VAL C 1 535  ? -8.362   92.411  57.421  1.00 110.48 ? 535  VAL B C   1 
ATOM   18483 O  O   . VAL C 1 535  ? -8.652   91.729  56.452  1.00 110.58 ? 535  VAL B O   1 
ATOM   18484 C  CB  . VAL C 1 535  ? -5.932   92.749  57.579  1.00 113.71 ? 535  VAL B CB  1 
ATOM   18485 C  CG1 . VAL C 1 535  ? -4.919   93.070  56.469  1.00 114.22 ? 535  VAL B CG1 1 
ATOM   18486 C  CG2 . VAL C 1 535  ? -5.427   93.071  59.002  1.00 116.85 ? 535  VAL B CG2 1 
ATOM   18487 N  N   . PRO C 1 536  ? -8.925   92.195  58.601  1.00 109.61 ? 536  PRO B N   1 
ATOM   18488 C  CA  . PRO C 1 536  ? -9.935   91.141  58.437  1.00 105.18 ? 536  PRO B CA  1 
ATOM   18489 C  C   . PRO C 1 536  ? -11.241  91.719  57.933  1.00 100.91 ? 536  PRO B C   1 
ATOM   18490 O  O   . PRO C 1 536  ? -11.942  91.109  57.131  1.00 100.33 ? 536  PRO B O   1 
ATOM   18491 C  CB  . PRO C 1 536  ? -10.092  90.572  59.849  1.00 108.75 ? 536  PRO B CB  1 
ATOM   18492 C  CG  . PRO C 1 536  ? -8.793   90.951  60.556  1.00 113.03 ? 536  PRO B CG  1 
ATOM   18493 C  CD  . PRO C 1 536  ? -8.378   92.266  59.964  1.00 113.29 ? 536  PRO B CD  1 
ATOM   18494 N  N   . SER C 1 537  ? -11.546  92.908  58.425  1.00 98.55  ? 537  SER B N   1 
ATOM   18495 C  CA  . SER C 1 537  ? -12.721  93.679  58.050  1.00 96.20  ? 537  SER B CA  1 
ATOM   18496 C  C   . SER C 1 537  ? -12.534  94.970  58.839  1.00 100.04 ? 537  SER B C   1 
ATOM   18497 O  O   . SER C 1 537  ? -11.488  95.151  59.477  1.00 102.81 ? 537  SER B O   1 
ATOM   18498 C  CB  . SER C 1 537  ? -14.038  92.972  58.430  1.00 91.08  ? 537  SER B CB  1 
ATOM   18499 O  OG  . SER C 1 537  ? -14.403  93.194  59.791  1.00 90.63  ? 537  SER B OG  1 
ATOM   18500 N  N   . SER C 1 538  ? -13.526  95.859  58.793  1.00 96.77  ? 538  SER B N   1 
ATOM   18501 C  CA  . SER C 1 538  ? -13.495  97.128  59.513  1.00 92.67  ? 538  SER B CA  1 
ATOM   18502 C  C   . SER C 1 538  ? -14.900  97.685  59.445  1.00 91.29  ? 538  SER B C   1 
ATOM   18503 O  O   . SER C 1 538  ? -15.731  97.171  58.706  1.00 91.01  ? 538  SER B O   1 
ATOM   18504 C  CB  . SER C 1 538  ? -12.545  98.111  58.818  1.00 91.30  ? 538  SER B CB  1 
ATOM   18505 O  OG  . SER C 1 538  ? -11.205  97.635  58.782  1.00 88.73  ? 538  SER B OG  1 
ATOM   18506 N  N   . ARG C 1 539  ? -15.183  98.739  60.195  1.00 90.39  ? 539  ARG B N   1 
ATOM   18507 C  CA  . ARG C 1 539  ? -16.339  99.558  59.863  1.00 90.33  ? 539  ARG B CA  1 
ATOM   18508 C  C   . ARG C 1 539  ? -15.932  101.004 59.816  1.00 92.80  ? 539  ARG B C   1 
ATOM   18509 O  O   . ARG C 1 539  ? -14.998  101.426 60.503  1.00 89.59  ? 539  ARG B O   1 
ATOM   18510 C  CB  . ARG C 1 539  ? -17.467  99.421  60.868  1.00 86.15  ? 539  ARG B CB  1 
ATOM   18511 C  CG  . ARG C 1 539  ? -17.608  98.078  61.482  1.00 88.33  ? 539  ARG B CG  1 
ATOM   18512 C  CD  . ARG C 1 539  ? -18.786  98.154  62.388  1.00 94.37  ? 539  ARG B CD  1 
ATOM   18513 N  NE  . ARG C 1 539  ? -19.920  97.475  61.812  1.00 97.57  ? 539  ARG B NE  1 
ATOM   18514 C  CZ  . ARG C 1 539  ? -20.084  96.163  61.923  1.00 102.67 ? 539  ARG B CZ  1 
ATOM   18515 N  NH1 . ARG C 1 539  ? -19.182  95.441  62.582  1.00 101.61 ? 539  ARG B NH1 1 
ATOM   18516 N  NH2 . ARG C 1 539  ? -21.138  95.569  61.380  1.00 103.43 ? 539  ARG B NH2 1 
ATOM   18517 N  N   . LEU C 1 540  ? -16.635  101.768 58.995  1.00 94.68  ? 540  LEU B N   1 
ATOM   18518 C  CA  . LEU C 1 540  ? -16.514  103.206 59.090  1.00 98.48  ? 540  LEU B CA  1 
ATOM   18519 C  C   . LEU C 1 540  ? -17.873  103.882 59.250  1.00 99.04  ? 540  LEU B C   1 
ATOM   18520 O  O   . LEU C 1 540  ? -18.925  103.333 58.883  1.00 95.34  ? 540  LEU B O   1 
ATOM   18521 C  CB  . LEU C 1 540  ? -15.675  103.824 57.953  1.00 102.80 ? 540  LEU B CB  1 
ATOM   18522 C  CG  . LEU C 1 540  ? -16.118  103.997 56.490  1.00 106.22 ? 540  LEU B CG  1 
ATOM   18523 C  CD1 . LEU C 1 540  ? -17.562  104.447 56.345  1.00 108.47 ? 540  LEU B CD1 1 
ATOM   18524 C  CD2 . LEU C 1 540  ? -15.177  104.978 55.780  1.00 108.33 ? 540  LEU B CD2 1 
ATOM   18525 N  N   . LEU C 1 541  ? -17.816  105.071 59.839  1.00 102.26 ? 541  LEU B N   1 
ATOM   18526 C  CA  . LEU C 1 541  ? -18.986  105.847 60.164  1.00 103.77 ? 541  LEU B CA  1 
ATOM   18527 C  C   . LEU C 1 541  ? -18.580  107.287 59.883  1.00 109.53 ? 541  LEU B C   1 
ATOM   18528 O  O   . LEU C 1 541  ? -17.427  107.673 60.062  1.00 110.71 ? 541  LEU B O   1 
ATOM   18529 C  CB  . LEU C 1 541  ? -19.395  105.592 61.619  1.00 102.56 ? 541  LEU B CB  1 
ATOM   18530 C  CG  . LEU C 1 541  ? -20.152  106.630 62.436  1.00 107.23 ? 541  LEU B CG  1 
ATOM   18531 C  CD1 . LEU C 1 541  ? -21.118  105.962 63.400  1.00 101.64 ? 541  LEU B CD1 1 
ATOM   18532 C  CD2 . LEU C 1 541  ? -19.142  107.509 63.172  1.00 109.05 ? 541  LEU B CD2 1 
ATOM   18533 N  N   . VAL C 1 542  ? -19.523  108.065 59.389  1.00 113.47 ? 542  VAL B N   1 
ATOM   18534 C  CA  . VAL C 1 542  ? -19.210  109.368 58.873  1.00 119.27 ? 542  VAL B CA  1 
ATOM   18535 C  C   . VAL C 1 542  ? -20.275  110.303 59.375  1.00 126.43 ? 542  VAL B C   1 
ATOM   18536 O  O   . VAL C 1 542  ? -21.459  109.990 59.292  1.00 125.92 ? 542  VAL B O   1 
ATOM   18537 C  CB  . VAL C 1 542  ? -19.236  109.337 57.341  1.00 117.19 ? 542  VAL B CB  1 
ATOM   18538 C  CG1 . VAL C 1 542  ? -19.595  110.707 56.774  1.00 119.21 ? 542  VAL B CG1 1 
ATOM   18539 C  CG2 . VAL C 1 542  ? -17.912  108.841 56.801  1.00 115.94 ? 542  VAL B CG2 1 
ATOM   18540 N  N   . TYR C 1 543  ? -19.848  111.447 59.899  1.00 133.28 ? 543  TYR B N   1 
ATOM   18541 C  CA  . TYR C 1 543  ? -20.775  112.424 60.444  1.00 138.71 ? 543  TYR B CA  1 
ATOM   18542 C  C   . TYR C 1 543  ? -20.415  113.865 60.144  1.00 142.79 ? 543  TYR B C   1 
ATOM   18543 O  O   . TYR C 1 543  ? -19.250  114.254 60.214  1.00 143.91 ? 543  TYR B O   1 
ATOM   18544 C  CB  . TYR C 1 543  ? -20.883  112.274 61.947  1.00 141.67 ? 543  TYR B CB  1 
ATOM   18545 C  CG  . TYR C 1 543  ? -19.605  112.520 62.725  1.00 145.20 ? 543  TYR B CG  1 
ATOM   18546 C  CD1 . TYR C 1 543  ? -18.700  111.490 62.945  1.00 145.01 ? 543  TYR B CD1 1 
ATOM   18547 C  CD2 . TYR C 1 543  ? -19.330  113.759 63.294  1.00 148.37 ? 543  TYR B CD2 1 
ATOM   18548 C  CE1 . TYR C 1 543  ? -17.541  111.691 63.694  1.00 146.91 ? 543  TYR B CE1 1 
ATOM   18549 C  CE2 . TYR C 1 543  ? -18.166  113.971 64.049  1.00 150.14 ? 543  TYR B CE2 1 
ATOM   18550 C  CZ  . TYR C 1 543  ? -17.273  112.931 64.249  1.00 148.17 ? 543  TYR B CZ  1 
ATOM   18551 O  OH  . TYR C 1 543  ? -16.114  113.103 64.997  1.00 147.15 ? 543  TYR B OH  1 
ATOM   18552 N  N   . TYR C 1 544  ? -21.437  114.645 59.803  1.00 144.80 ? 544  TYR B N   1 
ATOM   18553 C  CA  . TYR C 1 544  ? -21.343  116.100 59.785  1.00 148.30 ? 544  TYR B CA  1 
ATOM   18554 C  C   . TYR C 1 544  ? -22.090  116.629 61.004  1.00 149.86 ? 544  TYR B C   1 
ATOM   18555 O  O   . TYR C 1 544  ? -23.059  116.008 61.467  1.00 149.29 ? 544  TYR B O   1 
ATOM   18556 C  CB  . TYR C 1 544  ? -21.921  116.689 58.490  1.00 148.77 ? 544  TYR B CB  1 
ATOM   18557 C  CG  . TYR C 1 544  ? -23.391  116.408 58.288  1.00 147.63 ? 544  TYR B CG  1 
ATOM   18558 C  CD1 . TYR C 1 544  ? -23.874  115.120 58.384  1.00 144.93 ? 544  TYR B CD1 1 
ATOM   18559 C  CD2 . TYR C 1 544  ? -24.291  117.429 57.988  1.00 149.40 ? 544  TYR B CD2 1 
ATOM   18560 C  CE1 . TYR C 1 544  ? -25.195  114.846 58.203  1.00 144.05 ? 544  TYR B CE1 1 
ATOM   18561 C  CE2 . TYR C 1 544  ? -25.629  117.159 57.801  1.00 148.08 ? 544  TYR B CE2 1 
ATOM   18562 C  CZ  . TYR C 1 544  ? -26.069  115.858 57.917  1.00 145.89 ? 544  TYR B CZ  1 
ATOM   18563 O  OH  . TYR C 1 544  ? -27.384  115.525 57.745  1.00 145.21 ? 544  TYR B OH  1 
ATOM   18564 N  N   . ILE C 1 545  ? -21.621  117.758 61.536  1.00 151.58 ? 545  ILE B N   1 
ATOM   18565 C  CA  . ILE C 1 545  ? -22.267  118.392 62.680  1.00 152.29 ? 545  ILE B CA  1 
ATOM   18566 C  C   . ILE C 1 545  ? -23.161  119.551 62.203  1.00 154.96 ? 545  ILE B C   1 
ATOM   18567 O  O   . ILE C 1 545  ? -22.663  120.556 61.701  1.00 153.09 ? 545  ILE B O   1 
ATOM   18568 C  CB  . ILE C 1 545  ? -21.236  118.885 63.731  1.00 148.47 ? 545  ILE B CB  1 
ATOM   18569 C  CG1 . ILE C 1 545  ? -20.016  117.958 63.809  1.00 142.28 ? 545  ILE B CG1 1 
ATOM   18570 C  CG2 . ILE C 1 545  ? -21.885  118.996 65.101  1.00 152.47 ? 545  ILE B CG2 1 
ATOM   18571 C  CD1 . ILE C 1 545  ? -18.940  118.411 64.827  1.00 139.70 ? 545  ILE B CD1 1 
ATOM   18572 N  N   . VAL C 1 546  ? -24.475  119.384 62.371  1.00 158.91 ? 546  VAL B N   1 
ATOM   18573 C  CA  . VAL C 1 546  ? -25.495  120.280 61.811  1.00 164.85 ? 546  VAL B CA  1 
ATOM   18574 C  C   . VAL C 1 546  ? -26.104  121.250 62.813  1.00 179.62 ? 546  VAL B C   1 
ATOM   18575 O  O   . VAL C 1 546  ? -26.749  120.836 63.773  1.00 179.88 ? 546  VAL B O   1 
ATOM   18576 C  CB  . VAL C 1 546  ? -26.656  119.473 61.195  1.00 157.85 ? 546  VAL B CB  1 
ATOM   18577 C  CG1 . VAL C 1 546  ? -28.000  120.111 61.521  1.00 157.65 ? 546  VAL B CG1 1 
ATOM   18578 C  CG2 . VAL C 1 546  ? -26.476  119.337 59.704  1.00 153.58 ? 546  VAL B CG2 1 
ATOM   18579 N  N   . THR C 1 547  ? -25.932  122.545 62.568  1.00 193.49 ? 547  THR B N   1 
ATOM   18580 C  CA  . THR C 1 547  ? -26.453  123.556 63.478  1.00 209.74 ? 547  THR B CA  1 
ATOM   18581 C  C   . THR C 1 547  ? -27.919  123.913 63.220  1.00 224.50 ? 547  THR B C   1 
ATOM   18582 O  O   . THR C 1 547  ? -28.220  124.984 62.693  1.00 227.60 ? 547  THR B O   1 
ATOM   18583 C  CB  . THR C 1 547  ? -25.599  124.839 63.440  1.00 211.51 ? 547  THR B CB  1 
ATOM   18584 O  OG1 . THR C 1 547  ? -24.220  124.492 63.596  1.00 210.14 ? 547  THR B OG1 1 
ATOM   18585 C  CG2 . THR C 1 547  ? -26.005  125.803 64.554  1.00 216.20 ? 547  THR B CG2 1 
ATOM   18586 N  N   . GLY C 1 548  ? -28.830  123.022 63.601  1.00 236.06 ? 548  GLY B N   1 
ATOM   18587 C  CA  . GLY C 1 548  ? -30.232  123.388 63.658  1.00 251.15 ? 548  GLY B CA  1 
ATOM   18588 C  C   . GLY C 1 548  ? -30.336  124.565 64.612  1.00 269.93 ? 548  GLY B C   1 
ATOM   18589 O  O   . GLY C 1 548  ? -29.591  124.627 65.592  1.00 273.74 ? 548  GLY B O   1 
ATOM   18590 N  N   . GLU C 1 549  ? -31.237  125.503 64.338  1.00 282.92 ? 549  GLU B N   1 
ATOM   18591 C  CA  . GLU C 1 549  ? -31.360  126.699 65.177  1.00 297.22 ? 549  GLU B CA  1 
ATOM   18592 C  C   . GLU C 1 549  ? -31.658  126.373 66.647  1.00 298.86 ? 549  GLU B C   1 
ATOM   18593 O  O   . GLU C 1 549  ? -31.166  127.044 67.555  1.00 302.53 ? 549  GLU B O   1 
ATOM   18594 C  CB  . GLU C 1 549  ? -32.412  127.667 64.615  1.00 307.47 ? 549  GLU B CB  1 
ATOM   18595 C  CG  . GLU C 1 549  ? -33.836  127.134 64.612  1.00 314.04 ? 549  GLU B CG  1 
ATOM   18596 C  CD  . GLU C 1 549  ? -34.077  126.115 63.515  1.00 315.63 ? 549  GLU B CD  1 
ATOM   18597 O  OE1 . GLU C 1 549  ? -33.196  125.950 62.644  1.00 315.70 ? 549  GLU B OE1 1 
ATOM   18598 O  OE2 . GLU C 1 549  ? -35.151  125.478 63.519  1.00 316.41 ? 549  GLU B OE2 1 
ATOM   18599 N  N   . GLN C 1 550  ? -32.453  125.331 66.868  1.00 295.60 ? 550  GLN B N   1 
ATOM   18600 C  CA  . GLN C 1 550  ? -32.866  124.932 68.211  1.00 293.98 ? 550  GLN B CA  1 
ATOM   18601 C  C   . GLN C 1 550  ? -31.762  124.245 69.019  1.00 284.78 ? 550  GLN B C   1 
ATOM   18602 O  O   . GLN C 1 550  ? -31.568  124.552 70.191  1.00 288.94 ? 550  GLN B O   1 
ATOM   18603 C  CB  . GLN C 1 550  ? -34.112  124.037 68.144  1.00 295.90 ? 550  GLN B CB  1 
ATOM   18604 C  CG  . GLN C 1 550  ? -33.891  122.649 67.525  1.00 293.82 ? 550  GLN B CG  1 
ATOM   18605 C  CD  . GLN C 1 550  ? -33.876  122.651 65.995  1.00 292.83 ? 550  GLN B CD  1 
ATOM   18606 O  OE1 . GLN C 1 550  ? -34.110  123.678 65.357  1.00 295.34 ? 550  GLN B OE1 1 
ATOM   18607 N  NE2 . GLN C 1 550  ? -33.601  121.490 65.404  1.00 288.68 ? 550  GLN B NE2 1 
ATOM   18608 N  N   . THR C 1 551  ? -31.038  123.327 68.385  1.00 271.61 ? 551  THR B N   1 
ATOM   18609 C  CA  . THR C 1 551  ? -30.061  122.489 69.082  1.00 261.26 ? 551  THR B CA  1 
ATOM   18610 C  C   . THR C 1 551  ? -29.080  121.813 68.118  1.00 246.83 ? 551  THR B C   1 
ATOM   18611 O  O   . THR C 1 551  ? -29.463  121.382 67.026  1.00 243.67 ? 551  THR B O   1 
ATOM   18612 C  CB  . THR C 1 551  ? -30.767  121.381 69.887  1.00 262.29 ? 551  THR B CB  1 
ATOM   18613 O  OG1 . THR C 1 551  ? -31.607  121.971 70.886  1.00 267.06 ? 551  THR B OG1 1 
ATOM   18614 C  CG2 . THR C 1 551  ? -29.750  120.462 70.551  1.00 261.30 ? 551  THR B CG2 1 
ATOM   18615 N  N   . ALA C 1 552  ? -27.820  121.706 68.529  1.00 235.90 ? 552  ALA B N   1 
ATOM   18616 C  CA  . ALA C 1 552  ? -26.791  121.099 67.686  1.00 220.60 ? 552  ALA B CA  1 
ATOM   18617 C  C   . ALA C 1 552  ? -27.067  119.623 67.396  1.00 205.41 ? 552  ALA B C   1 
ATOM   18618 O  O   . ALA C 1 552  ? -27.202  118.830 68.333  1.00 203.13 ? 552  ALA B O   1 
ATOM   18619 C  CB  . ALA C 1 552  ? -25.422  121.259 68.334  1.00 222.46 ? 552  ALA B CB  1 
ATOM   18620 N  N   . GLU C 1 553  ? -27.147  119.269 66.104  1.00 192.84 ? 553  GLU B N   1 
ATOM   18621 C  CA  . GLU C 1 553  ? -27.315  117.866 65.644  1.00 178.21 ? 553  GLU B CA  1 
ATOM   18622 C  C   . GLU C 1 553  ? -26.078  117.166 65.074  1.00 168.38 ? 553  GLU B C   1 
ATOM   18623 O  O   . GLU C 1 553  ? -25.531  117.574 64.052  1.00 165.68 ? 553  GLU B O   1 
ATOM   18624 C  CB  . GLU C 1 553  ? -28.449  117.723 64.618  1.00 172.04 ? 553  GLU B CB  1 
ATOM   18625 C  CG  . GLU C 1 553  ? -29.615  116.871 65.103  1.00 167.62 ? 553  GLU B CG  1 
ATOM   18626 C  CD  . GLU C 1 553  ? -30.432  116.300 63.967  1.00 162.11 ? 553  GLU B CD  1 
ATOM   18627 O  OE1 . GLU C 1 553  ? -29.860  116.082 62.891  1.00 160.35 ? 553  GLU B OE1 1 
ATOM   18628 O  OE2 . GLU C 1 553  ? -31.645  116.070 64.139  1.00 160.57 ? 553  GLU B OE2 1 
ATOM   18629 N  N   . LEU C 1 554  ? -25.657  116.100 65.743  1.00 162.87 ? 554  LEU B N   1 
ATOM   18630 C  CA  . LEU C 1 554  ? -24.723  115.173 65.152  1.00 157.45 ? 554  LEU B CA  1 
ATOM   18631 C  C   . LEU C 1 554  ? -25.567  114.283 64.287  1.00 153.08 ? 554  LEU B C   1 
ATOM   18632 O  O   . LEU C 1 554  ? -26.690  113.924 64.646  1.00 153.31 ? 554  LEU B O   1 
ATOM   18633 C  CB  . LEU C 1 554  ? -24.020  114.325 66.208  1.00 157.34 ? 554  LEU B CB  1 
ATOM   18634 C  CG  . LEU C 1 554  ? -22.809  114.899 66.942  1.00 160.50 ? 554  LEU B CG  1 
ATOM   18635 C  CD1 . LEU C 1 554  ? -21.847  113.791 67.370  1.00 158.59 ? 554  LEU B CD1 1 
ATOM   18636 C  CD2 . LEU C 1 554  ? -22.102  115.883 66.047  1.00 162.00 ? 554  LEU B CD2 1 
ATOM   18637 N  N   . VAL C 1 555  ? -25.027  113.920 63.140  1.00 149.83 ? 555  VAL B N   1 
ATOM   18638 C  CA  . VAL C 1 555  ? -25.745  113.045 62.243  1.00 145.99 ? 555  VAL B CA  1 
ATOM   18639 C  C   . VAL C 1 555  ? -24.718  112.212 61.483  1.00 138.54 ? 555  VAL B C   1 
ATOM   18640 O  O   . VAL C 1 555  ? -23.651  112.700 61.113  1.00 137.71 ? 555  VAL B O   1 
ATOM   18641 C  CB  . VAL C 1 555  ? -26.660  113.862 61.310  1.00 147.59 ? 555  VAL B CB  1 
ATOM   18642 C  CG1 . VAL C 1 555  ? -27.101  113.042 60.135  1.00 146.85 ? 555  VAL B CG1 1 
ATOM   18643 C  CG2 . VAL C 1 555  ? -27.866  114.334 62.079  1.00 149.86 ? 555  VAL B CG2 1 
ATOM   18644 N  N   . SER C 1 556  ? -25.016  110.937 61.292  1.00 132.31 ? 556  SER B N   1 
ATOM   18645 C  CA  . SER C 1 556  ? -24.072  110.093 60.609  1.00 129.15 ? 556  SER B CA  1 
ATOM   18646 C  C   . SER C 1 556  ? -24.721  108.791 60.205  1.00 127.79 ? 556  SER B C   1 
ATOM   18647 O  O   . SER C 1 556  ? -25.729  108.388 60.791  1.00 130.77 ? 556  SER B O   1 
ATOM   18648 C  CB  . SER C 1 556  ? -22.882  109.814 61.515  1.00 127.84 ? 556  SER B CB  1 
ATOM   18649 O  OG  . SER C 1 556  ? -23.178  108.753 62.400  1.00 126.50 ? 556  SER B OG  1 
ATOM   18650 N  N   . ASP C 1 557  ? -24.128  108.156 59.192  1.00 121.47 ? 557  ASP B N   1 
ATOM   18651 C  CA  . ASP C 1 557  ? -24.461  106.802 58.773  1.00 114.00 ? 557  ASP B CA  1 
ATOM   18652 C  C   . ASP C 1 557  ? -23.132  106.046 58.793  1.00 108.75 ? 557  ASP B C   1 
ATOM   18653 O  O   . ASP C 1 557  ? -22.094  106.640 59.084  1.00 106.84 ? 557  ASP B O   1 
ATOM   18654 C  CB  . ASP C 1 557  ? -25.104  106.818 57.381  1.00 114.25 ? 557  ASP B CB  1 
ATOM   18655 C  CG  . ASP C 1 557  ? -25.134  105.436 56.704  1.00 113.66 ? 557  ASP B CG  1 
ATOM   18656 O  OD1 . ASP C 1 557  ? -25.825  104.523 57.204  1.00 114.93 ? 557  ASP B OD1 1 
ATOM   18657 O  OD2 . ASP C 1 557  ? -24.484  105.272 55.646  1.00 111.22 ? 557  ASP B OD2 1 
ATOM   18658 N  N   . SER C 1 558  ? -23.168  104.742 58.514  1.00 107.94 ? 558  SER B N   1 
ATOM   18659 C  CA  . SER C 1 558  ? -21.998  103.866 58.642  1.00 106.86 ? 558  SER B CA  1 
ATOM   18660 C  C   . SER C 1 558  ? -22.173  102.572 57.829  1.00 103.89 ? 558  SER B C   1 
ATOM   18661 O  O   . SER C 1 558  ? -23.302  102.177 57.530  1.00 100.96 ? 558  SER B O   1 
ATOM   18662 C  CB  . SER C 1 558  ? -21.740  103.548 60.123  1.00 108.27 ? 558  SER B CB  1 
ATOM   18663 O  OG  . SER C 1 558  ? -22.843  102.866 60.717  1.00 108.32 ? 558  SER B OG  1 
ATOM   18664 N  N   . VAL C 1 559  ? -21.056  101.922 57.484  1.00 104.76 ? 559  VAL B N   1 
ATOM   18665 C  CA  . VAL C 1 559  ? -21.056  100.745 56.593  1.00 103.23 ? 559  VAL B CA  1 
ATOM   18666 C  C   . VAL C 1 559  ? -19.997  99.701  56.987  1.00 103.44 ? 559  VAL B C   1 
ATOM   18667 O  O   . VAL C 1 559  ? -18.870  100.057 57.355  1.00 106.96 ? 559  VAL B O   1 
ATOM   18668 C  CB  . VAL C 1 559  ? -20.806  101.138 55.112  1.00 90.57  ? 559  VAL B CB  1 
ATOM   18669 C  CG1 . VAL C 1 559  ? -21.792  102.195 54.668  1.00 88.74  ? 559  VAL B CG1 1 
ATOM   18670 C  CG2 . VAL C 1 559  ? -19.392  101.619 54.928  1.00 83.92  ? 559  VAL B CG2 1 
ATOM   18671 N  N   . TRP C 1 560  ? -20.346  98.417  56.911  1.00 99.11  ? 560  TRP B N   1 
ATOM   18672 C  CA  . TRP C 1 560  ? -19.398  97.372  57.279  1.00 97.36  ? 560  TRP B CA  1 
ATOM   18673 C  C   . TRP C 1 560  ? -18.525  97.040  56.096  1.00 92.57  ? 560  TRP B C   1 
ATOM   18674 O  O   . TRP C 1 560  ? -19.039  96.746  55.023  1.00 91.67  ? 560  TRP B O   1 
ATOM   18675 C  CB  . TRP C 1 560  ? -20.139  96.121  57.746  1.00 102.40 ? 560  TRP B CB  1 
ATOM   18676 C  CG  . TRP C 1 560  ? -19.222  94.999  58.051  1.00 107.96 ? 560  TRP B CG  1 
ATOM   18677 C  CD1 . TRP C 1 560  ? -18.420  94.879  59.130  1.00 112.38 ? 560  TRP B CD1 1 
ATOM   18678 C  CD2 . TRP C 1 560  ? -18.999  93.833  57.250  1.00 109.12 ? 560  TRP B CD2 1 
ATOM   18679 N  NE1 . TRP C 1 560  ? -17.697  93.709  59.056  1.00 112.85 ? 560  TRP B NE1 1 
ATOM   18680 C  CE2 . TRP C 1 560  ? -18.035  93.054  57.907  1.00 109.86 ? 560  TRP B CE2 1 
ATOM   18681 C  CE3 . TRP C 1 560  ? -19.511  93.385  56.030  1.00 110.48 ? 560  TRP B CE3 1 
ATOM   18682 C  CZ2 . TRP C 1 560  ? -17.578  91.855  57.399  1.00 108.47 ? 560  TRP B CZ2 1 
ATOM   18683 C  CZ3 . TRP C 1 560  ? -19.053  92.190  55.524  1.00 109.51 ? 560  TRP B CZ3 1 
ATOM   18684 C  CH2 . TRP C 1 560  ? -18.098  91.436  56.213  1.00 108.14 ? 560  TRP B CH2 1 
ATOM   18685 N  N   . LEU C 1 561  ? -17.213  97.072  56.268  1.00 92.38  ? 561  LEU B N   1 
ATOM   18686 C  CA  . LEU C 1 561  ? -16.318  96.858  55.124  1.00 95.20  ? 561  LEU B CA  1 
ATOM   18687 C  C   . LEU C 1 561  ? -15.558  95.538  55.102  1.00 98.31  ? 561  LEU B C   1 
ATOM   18688 O  O   . LEU C 1 561  ? -14.472  95.458  55.679  1.00 102.66 ? 561  LEU B O   1 
ATOM   18689 C  CB  . LEU C 1 561  ? -15.269  97.961  55.086  1.00 95.33  ? 561  LEU B CB  1 
ATOM   18690 C  CG  . LEU C 1 561  ? -15.799  99.383  54.948  1.00 94.26  ? 561  LEU B CG  1 
ATOM   18691 C  CD1 . LEU C 1 561  ? -14.630  100.311 54.840  1.00 94.46  ? 561  LEU B CD1 1 
ATOM   18692 C  CD2 . LEU C 1 561  ? -16.658  99.459  53.712  1.00 94.46  ? 561  LEU B CD2 1 
ATOM   18693 N  N   . ASN C 1 562  ? -16.076  94.517  54.415  1.00 97.57  ? 562  ASN B N   1 
ATOM   18694 C  CA  . ASN C 1 562  ? -15.360  93.230  54.366  1.00 95.78  ? 562  ASN B CA  1 
ATOM   18695 C  C   . ASN C 1 562  ? -14.155  93.324  53.464  1.00 98.65  ? 562  ASN B C   1 
ATOM   18696 O  O   . ASN C 1 562  ? -14.264  93.675  52.292  1.00 99.45  ? 562  ASN B O   1 
ATOM   18697 C  CB  . ASN C 1 562  ? -16.247  92.058  53.909  1.00 90.32  ? 562  ASN B CB  1 
ATOM   18698 C  CG  . ASN C 1 562  ? -15.475  90.709  53.812  1.00 118.54 ? 562  ASN B CG  1 
ATOM   18699 O  OD1 . ASN C 1 562  ? -14.357  90.543  54.331  1.00 117.63 ? 562  ASN B OD1 1 
ATOM   18700 N  ND2 . ASN C 1 562  ? -16.094  89.743  53.142  1.00 117.43 ? 562  ASN B ND2 1 
ATOM   18701 N  N   . ILE C 1 563  ? -12.996  92.980  53.991  1.00 98.81  ? 563  ILE B N   1 
ATOM   18702 C  CA  . ILE C 1 563  ? -11.838  93.100  53.164  1.00 99.53  ? 563  ILE B CA  1 
ATOM   18703 C  C   . ILE C 1 563  ? -11.034  91.814  53.142  1.00 102.28 ? 563  ILE B C   1 
ATOM   18704 O  O   . ILE C 1 563  ? -11.325  90.863  53.875  1.00 102.30 ? 563  ILE B O   1 
ATOM   18705 C  CB  . ILE C 1 563  ? -11.029  94.350  53.537  1.00 98.31  ? 563  ILE B CB  1 
ATOM   18706 C  CG1 . ILE C 1 563  ? -9.740   93.984  54.236  1.00 99.45  ? 563  ILE B CG1 1 
ATOM   18707 C  CG2 . ILE C 1 563  ? -11.862  95.285  54.381  1.00 97.48  ? 563  ILE B CG2 1 
ATOM   18708 C  CD1 . ILE C 1 563  ? -8.712   95.072  54.111  1.00 101.96 ? 563  ILE B CD1 1 
ATOM   18709 N  N   . GLU C 1 564  ? -10.054  91.790  52.249  1.00 104.67 ? 564  GLU B N   1 
ATOM   18710 C  CA  . GLU C 1 564  ? -9.301   90.594  51.924  1.00 106.54 ? 564  GLU B CA  1 
ATOM   18711 C  C   . GLU C 1 564  ? -8.553   90.019  53.107  1.00 109.78 ? 564  GLU B C   1 
ATOM   18712 O  O   . GLU C 1 564  ? -7.909   90.745  53.854  1.00 113.01 ? 564  GLU B O   1 
ATOM   18713 C  CB  . GLU C 1 564  ? -8.304   90.901  50.804  1.00 107.24 ? 564  GLU B CB  1 
ATOM   18714 C  CG  . GLU C 1 564  ? -7.208   91.929  51.139  1.00 111.03 ? 564  GLU B CG  1 
ATOM   18715 C  CD  . GLU C 1 564  ? -5.966   91.748  50.260  1.00 114.25 ? 564  GLU B CD  1 
ATOM   18716 O  OE1 . GLU C 1 564  ? -5.251   92.746  49.974  1.00 116.72 ? 564  GLU B OE1 1 
ATOM   18717 O  OE2 . GLU C 1 564  ? -5.708   90.589  49.852  1.00 113.35 ? 564  GLU B OE2 1 
ATOM   18718 N  N   . GLU C 1 565  ? -8.619   88.707  53.268  1.00 112.03 ? 565  GLU B N   1 
ATOM   18719 C  CA  . GLU C 1 565  ? -7.819   88.051  54.289  1.00 117.21 ? 565  GLU B CA  1 
ATOM   18720 C  C   . GLU C 1 565  ? -6.333   88.030  53.962  1.00 117.10 ? 565  GLU B C   1 
ATOM   18721 O  O   . GLU C 1 565  ? -5.704   86.985  54.005  1.00 115.63 ? 565  GLU B O   1 
ATOM   18722 C  CB  . GLU C 1 565  ? -8.310   86.631  54.521  1.00 122.38 ? 565  GLU B CB  1 
ATOM   18723 C  CG  . GLU C 1 565  ? -9.612   86.572  55.281  1.00 128.12 ? 565  GLU B CG  1 
ATOM   18724 C  CD  . GLU C 1 565  ? -10.193  85.178  55.297  1.00 131.06 ? 565  GLU B CD  1 
ATOM   18725 O  OE1 . GLU C 1 565  ? -9.634   84.296  54.589  1.00 131.32 ? 565  GLU B OE1 1 
ATOM   18726 O  OE2 . GLU C 1 565  ? -11.209  84.975  56.010  1.00 131.81 ? 565  GLU B OE2 1 
ATOM   18727 N  N   . LYS C 1 566  ? -5.773   89.180  53.622  1.00 120.06 ? 566  LYS B N   1 
ATOM   18728 C  CA  . LYS C 1 566  ? -4.328   89.304  53.539  1.00 121.42 ? 566  LYS B CA  1 
ATOM   18729 C  C   . LYS C 1 566  ? -3.765   89.106  54.933  1.00 121.53 ? 566  LYS B C   1 
ATOM   18730 O  O   . LYS C 1 566  ? -4.260   89.705  55.885  1.00 124.09 ? 566  LYS B O   1 
ATOM   18731 C  CB  . LYS C 1 566  ? -3.929   90.689  53.031  1.00 123.59 ? 566  LYS B CB  1 
ATOM   18732 C  CG  . LYS C 1 566  ? -2.441   90.902  52.977  1.00 124.55 ? 566  LYS B CG  1 
ATOM   18733 C  CD  . LYS C 1 566  ? -2.057   91.779  51.802  1.00 126.84 ? 566  LYS B CD  1 
ATOM   18734 C  CE  . LYS C 1 566  ? -0.556   92.064  51.800  1.00 129.92 ? 566  LYS B CE  1 
ATOM   18735 N  NZ  . LYS C 1 566  ? -0.094   92.766  53.056  1.00 131.59 ? 566  LYS B NZ  1 
ATOM   18736 N  N   . CYS C 1 567  ? -2.748   88.256  55.051  1.00 151.30 ? 567  CYS B N   1 
ATOM   18737 C  CA  . CYS C 1 567  ? -2.036   88.042  56.310  1.00 148.85 ? 567  CYS B CA  1 
ATOM   18738 C  C   . CYS C 1 567  ? -1.179   89.266  56.679  1.00 148.10 ? 567  CYS B C   1 
ATOM   18739 O  O   . CYS C 1 567  ? -1.109   90.229  55.928  1.00 149.89 ? 567  CYS B O   1 
ATOM   18740 C  CB  . CYS C 1 567  ? -1.141   86.796  56.206  1.00 147.24 ? 567  CYS B CB  1 
ATOM   18741 S  SG  . CYS C 1 567  ? -1.965   85.167  56.249  1.00 211.93 ? 567  CYS B SG  1 
ATOM   18742 N  N   . GLY C 1 568  ? -0.540   89.233  57.842  1.00 148.32 ? 568  GLY B N   1 
ATOM   18743 C  CA  . GLY C 1 568  ? 0.474    90.219  58.171  1.00 148.68 ? 568  GLY B CA  1 
ATOM   18744 C  C   . GLY C 1 568  ? 1.861    89.692  57.833  1.00 150.23 ? 568  GLY B C   1 
ATOM   18745 O  O   . GLY C 1 568  ? 2.688    90.413  57.275  1.00 149.55 ? 568  GLY B O   1 
ATOM   18746 N  N   . ASN C 1 569  ? 2.114    88.432  58.193  1.00 149.52 ? 569  ASN B N   1 
ATOM   18747 C  CA  . ASN C 1 569  ? 3.346    87.732  57.835  1.00 149.11 ? 569  ASN B CA  1 
ATOM   18748 C  C   . ASN C 1 569  ? 3.079    86.578  56.891  1.00 147.09 ? 569  ASN B C   1 
ATOM   18749 O  O   . ASN C 1 569  ? 2.680    85.502  57.318  1.00 147.85 ? 569  ASN B O   1 
ATOM   18750 C  CB  . ASN C 1 569  ? 4.033    87.203  59.087  1.00 149.75 ? 569  ASN B CB  1 
ATOM   18751 C  CG  . ASN C 1 569  ? 5.250    87.996  59.449  1.00 150.85 ? 569  ASN B CG  1 
ATOM   18752 O  OD1 . ASN C 1 569  ? 5.682    88.868  58.698  1.00 152.60 ? 569  ASN B OD1 1 
ATOM   18753 N  ND2 . ASN C 1 569  ? 5.825    87.695  60.602  1.00 150.92 ? 569  ASN B ND2 1 
ATOM   18754 N  N   . GLN C 1 570  ? 3.278    86.793  55.600  1.00 145.21 ? 570  GLN B N   1 
ATOM   18755 C  CA  . GLN C 1 570  ? 3.017    85.718  54.658  1.00 143.24 ? 570  GLN B CA  1 
ATOM   18756 C  C   . GLN C 1 570  ? 3.997    84.603  54.985  1.00 147.84 ? 570  GLN B C   1 
ATOM   18757 O  O   . GLN C 1 570  ? 5.181    84.682  54.665  1.00 146.14 ? 570  GLN B O   1 
ATOM   18758 C  CB  . GLN C 1 570  ? 3.149    86.166  53.185  1.00 140.91 ? 570  GLN B CB  1 
ATOM   18759 C  CG  . GLN C 1 570  ? 1.859    86.709  52.513  1.00 175.69 ? 570  GLN B CG  1 
ATOM   18760 C  CD  . GLN C 1 570  ? 1.742    88.243  52.534  1.00 174.87 ? 570  GLN B CD  1 
ATOM   18761 O  OE1 . GLN C 1 570  ? 2.033    88.886  53.542  1.00 173.99 ? 570  GLN B OE1 1 
ATOM   18762 N  NE2 . GLN C 1 570  ? 1.306    88.826  51.417  1.00 174.74 ? 570  GLN B NE2 1 
ATOM   18763 N  N   . LEU C 1 571  ? 3.509    83.582  55.670  1.00 150.99 ? 571  LEU B N   1 
ATOM   18764 C  CA  . LEU C 1 571  ? 4.287    82.376  55.855  1.00 151.83 ? 571  LEU B CA  1 
ATOM   18765 C  C   . LEU C 1 571  ? 3.904    81.385  54.783  1.00 153.44 ? 571  LEU B C   1 
ATOM   18766 O  O   . LEU C 1 571  ? 2.729    81.079  54.604  1.00 156.31 ? 571  LEU B O   1 
ATOM   18767 C  CB  . LEU C 1 571  ? 4.007    81.773  57.214  1.00 145.71 ? 571  LEU B CB  1 
ATOM   18768 C  CG  . LEU C 1 571  ? 4.018    80.250  57.223  1.00 131.90 ? 571  LEU B CG  1 
ATOM   18769 C  CD1 . LEU C 1 571  ? 5.278    79.679  56.600  1.00 131.19 ? 571  LEU B CD1 1 
ATOM   18770 C  CD2 . LEU C 1 571  ? 3.851    79.769  58.649  1.00 132.18 ? 571  LEU B CD2 1 
ATOM   18771 N  N   . GLN C 1 572  ? 4.895    80.863  54.078  1.00 155.07 ? 572  GLN B N   1 
ATOM   18772 C  CA  . GLN C 1 572  ? 4.613    79.880  53.047  1.00 156.88 ? 572  GLN B CA  1 
ATOM   18773 C  C   . GLN C 1 572  ? 5.613    78.747  53.095  1.00 151.25 ? 572  GLN B C   1 
ATOM   18774 O  O   . GLN C 1 572  ? 6.816    78.951  52.953  1.00 149.82 ? 572  GLN B O   1 
ATOM   18775 C  CB  . GLN C 1 572  ? 4.589    80.520  51.652  1.00 167.50 ? 572  GLN B CB  1 
ATOM   18776 C  CG  . GLN C 1 572  ? 4.071    79.603  50.534  1.00 178.44 ? 572  GLN B CG  1 
ATOM   18777 C  CD  . GLN C 1 572  ? 2.772    78.868  50.886  1.00 187.04 ? 572  GLN B CD  1 
ATOM   18778 O  OE1 . GLN C 1 572  ? 1.918    79.381  51.614  1.00 189.57 ? 572  GLN B OE1 1 
ATOM   18779 N  NE2 . GLN C 1 572  ? 2.625    77.656  50.359  1.00 190.71 ? 572  GLN B NE2 1 
ATOM   18780 N  N   . VAL C 1 573  ? 5.086    77.546  53.283  1.00 149.43 ? 573  VAL B N   1 
ATOM   18781 C  CA  . VAL C 1 573  ? 5.890    76.343  53.375  1.00 144.78 ? 573  VAL B CA  1 
ATOM   18782 C  C   . VAL C 1 573  ? 5.958    75.551  52.037  1.00 147.89 ? 573  VAL B C   1 
ATOM   18783 O  O   . VAL C 1 573  ? 4.961    75.456  51.316  1.00 149.38 ? 573  VAL B O   1 
ATOM   18784 C  CB  . VAL C 1 573  ? 5.354    75.514  54.538  1.00 135.95 ? 573  VAL B CB  1 
ATOM   18785 C  CG1 . VAL C 1 573  ? 5.957    76.015  55.812  1.00 132.44 ? 573  VAL B CG1 1 
ATOM   18786 C  CG2 . VAL C 1 573  ? 3.849    75.673  54.625  1.00 131.28 ? 573  VAL B CG2 1 
ATOM   18787 N  N   . HIS C 1 574  ? 7.130    75.003  51.701  1.00 146.85 ? 574  HIS B N   1 
ATOM   18788 C  CA  . HIS C 1 574  ? 7.287    74.230  50.466  1.00 148.55 ? 574  HIS B CA  1 
ATOM   18789 C  C   . HIS C 1 574  ? 8.193    73.012  50.611  1.00 151.79 ? 574  HIS B C   1 
ATOM   18790 O  O   . HIS C 1 574  ? 9.178    73.050  51.345  1.00 150.32 ? 574  HIS B O   1 
ATOM   18791 C  CB  . HIS C 1 574  ? 7.823    75.123  49.357  1.00 151.01 ? 574  HIS B CB  1 
ATOM   18792 C  CG  . HIS C 1 574  ? 6.876    76.205  48.961  1.00 154.29 ? 574  HIS B CG  1 
ATOM   18793 N  ND1 . HIS C 1 574  ? 5.570    75.950  48.601  1.00 155.89 ? 574  HIS B ND1 1 
ATOM   18794 C  CD2 . HIS C 1 574  ? 7.037    77.548  48.873  1.00 156.64 ? 574  HIS B CD2 1 
ATOM   18795 C  CE1 . HIS C 1 574  ? 4.966    77.088  48.309  1.00 156.50 ? 574  HIS B CE1 1 
ATOM   18796 N  NE2 . HIS C 1 574  ? 5.833    78.074  48.465  1.00 157.09 ? 574  HIS B NE2 1 
ATOM   18797 N  N   . LEU C 1 575  ? 7.854    71.932  49.907  1.00 158.92 ? 575  LEU B N   1 
ATOM   18798 C  CA  . LEU C 1 575  ? 8.691    70.727  49.880  1.00 166.05 ? 575  LEU B CA  1 
ATOM   18799 C  C   . LEU C 1 575  ? 9.731    70.782  48.760  1.00 177.71 ? 575  LEU B C   1 
ATOM   18800 O  O   . LEU C 1 575  ? 9.430    71.255  47.664  1.00 182.06 ? 575  LEU B O   1 
ATOM   18801 C  CB  . LEU C 1 575  ? 7.831    69.471  49.733  1.00 161.30 ? 575  LEU B CB  1 
ATOM   18802 C  CG  . LEU C 1 575  ? 7.084    69.029  50.991  1.00 155.62 ? 575  LEU B CG  1 
ATOM   18803 C  CD1 . LEU C 1 575  ? 6.389    67.689  50.786  1.00 153.01 ? 575  LEU B CD1 1 
ATOM   18804 C  CD2 . LEU C 1 575  ? 8.043    68.961  52.164  1.00 153.99 ? 575  LEU B CD2 1 
ATOM   18805 N  N   . SER C 1 576  ? 10.943   70.286  49.031  1.00 183.30 ? 576  SER B N   1 
ATOM   18806 C  CA  . SER C 1 576  ? 12.067   70.388  48.085  1.00 190.29 ? 576  SER B CA  1 
ATOM   18807 C  C   . SER C 1 576  ? 11.800   69.707  46.743  1.00 195.04 ? 576  SER B C   1 
ATOM   18808 O  O   . SER C 1 576  ? 11.797   70.365  45.698  1.00 193.91 ? 576  SER B O   1 
ATOM   18809 C  CB  . SER C 1 576  ? 13.377   69.870  48.700  1.00 195.88 ? 576  SER B CB  1 
ATOM   18810 O  OG  . SER C 1 576  ? 14.144   70.925  49.263  1.00 198.91 ? 576  SER B OG  1 
ATOM   18811 N  N   . PRO C 1 577  ? 11.606   68.383  46.755  1.00 198.39 ? 577  PRO B N   1 
ATOM   18812 C  CA  . PRO C 1 577  ? 11.056   67.813  45.527  1.00 202.64 ? 577  PRO B CA  1 
ATOM   18813 C  C   . PRO C 1 577  ? 9.566    68.156  45.464  1.00 199.67 ? 577  PRO B C   1 
ATOM   18814 O  O   . PRO C 1 577  ? 8.794    67.553  46.201  1.00 201.48 ? 577  PRO B O   1 
ATOM   18815 C  CB  . PRO C 1 577  ? 11.257   66.307  45.729  1.00 204.12 ? 577  PRO B CB  1 
ATOM   18816 C  CG  . PRO C 1 577  ? 12.266   66.181  46.836  1.00 204.73 ? 577  PRO B CG  1 
ATOM   18817 C  CD  . PRO C 1 577  ? 12.008   67.344  47.715  1.00 202.19 ? 577  PRO B CD  1 
ATOM   18818 N  N   . ASP C 1 578  ? 9.159    69.108  44.628  1.00 195.93 ? 578  ASP B N   1 
ATOM   18819 C  CA  . ASP C 1 578  ? 7.756    69.517  44.631  1.00 191.66 ? 578  ASP B CA  1 
ATOM   18820 C  C   . ASP C 1 578  ? 6.872    68.419  44.044  1.00 189.07 ? 578  ASP B C   1 
ATOM   18821 O  O   . ASP C 1 578  ? 5.677    68.623  43.873  1.00 186.10 ? 578  ASP B O   1 
ATOM   18822 C  CB  . ASP C 1 578  ? 7.548    70.855  43.894  1.00 194.15 ? 578  ASP B CB  1 
ATOM   18823 C  CG  . ASP C 1 578  ? 6.272    71.601  44.339  1.00 196.01 ? 578  ASP B CG  1 
ATOM   18824 O  OD1 . ASP C 1 578  ? 5.350    70.971  44.898  1.00 196.13 ? 578  ASP B OD1 1 
ATOM   18825 O  OD2 . ASP C 1 578  ? 6.190    72.831  44.119  1.00 197.46 ? 578  ASP B OD2 1 
ATOM   18826 N  N   . ALA C 1 579  ? 7.450    67.257  43.745  1.00 190.45 ? 579  ALA B N   1 
ATOM   18827 C  CA  . ALA C 1 579  ? 6.672    66.157  43.172  1.00 190.21 ? 579  ALA B CA  1 
ATOM   18828 C  C   . ALA C 1 579  ? 5.467    65.791  44.045  1.00 185.02 ? 579  ALA B C   1 
ATOM   18829 O  O   . ALA C 1 579  ? 5.498    65.948  45.263  1.00 185.14 ? 579  ALA B O   1 
ATOM   18830 C  CB  . ALA C 1 579  ? 7.548    64.944  42.907  1.00 193.41 ? 579  ALA B CB  1 
ATOM   18831 N  N   . ASP C 1 580  ? 4.402    65.319  43.403  1.00 181.09 ? 580  ASP B N   1 
ATOM   18832 C  CA  . ASP C 1 580  ? 3.112    65.113  44.060  1.00 179.13 ? 580  ASP B CA  1 
ATOM   18833 C  C   . ASP C 1 580  ? 2.970    63.702  44.597  1.00 176.79 ? 580  ASP B C   1 
ATOM   18834 O  O   . ASP C 1 580  ? 1.861    63.231  44.862  1.00 176.35 ? 580  ASP B O   1 
ATOM   18835 C  CB  . ASP C 1 580  ? 1.965    65.412  43.092  1.00 183.63 ? 580  ASP B CB  1 
ATOM   18836 C  CG  . ASP C 1 580  ? 1.938    64.459  41.907  1.00 191.88 ? 580  ASP B CG  1 
ATOM   18837 O  OD1 . ASP C 1 580  ? 2.448    63.322  42.047  1.00 195.38 ? 580  ASP B OD1 1 
ATOM   18838 O  OD2 . ASP C 1 580  ? 1.403    64.847  40.840  1.00 194.57 ? 580  ASP B OD2 1 
ATOM   18839 N  N   . ALA C 1 581  ? 4.099    63.021  44.723  1.00 175.56 ? 581  ALA B N   1 
ATOM   18840 C  CA  . ALA C 1 581  ? 4.128    61.702  45.324  1.00 174.51 ? 581  ALA B CA  1 
ATOM   18841 C  C   . ALA C 1 581  ? 5.566    61.420  45.731  1.00 171.18 ? 581  ALA B C   1 
ATOM   18842 O  O   . ALA C 1 581  ? 6.493    61.762  45.000  1.00 173.10 ? 581  ALA B O   1 
ATOM   18843 C  CB  . ALA C 1 581  ? 3.629    60.668  44.345  1.00 175.64 ? 581  ALA B CB  1 
ATOM   18844 N  N   . TYR C 1 582  ? 5.753    60.812  46.901  1.00 167.89 ? 582  TYR B N   1 
ATOM   18845 C  CA  . TYR C 1 582  ? 7.090    60.560  47.433  1.00 162.43 ? 582  TYR B CA  1 
ATOM   18846 C  C   . TYR C 1 582  ? 7.304    59.104  47.775  1.00 160.56 ? 582  TYR B C   1 
ATOM   18847 O  O   . TYR C 1 582  ? 6.366    58.344  48.006  1.00 160.25 ? 582  TYR B O   1 
ATOM   18848 C  CB  . TYR C 1 582  ? 7.358    61.382  48.698  1.00 160.11 ? 582  TYR B CB  1 
ATOM   18849 C  CG  . TYR C 1 582  ? 7.405    62.879  48.499  1.00 157.80 ? 582  TYR B CG  1 
ATOM   18850 C  CD1 . TYR C 1 582  ? 8.592    63.527  48.173  1.00 158.33 ? 582  TYR B CD1 1 
ATOM   18851 C  CD2 . TYR C 1 582  ? 6.262    63.651  48.658  1.00 155.90 ? 582  TYR B CD2 1 
ATOM   18852 C  CE1 . TYR C 1 582  ? 8.632    64.908  47.998  1.00 157.75 ? 582  TYR B CE1 1 
ATOM   18853 C  CE2 . TYR C 1 582  ? 6.287    65.027  48.487  1.00 155.27 ? 582  TYR B CE2 1 
ATOM   18854 C  CZ  . TYR C 1 582  ? 7.469    65.655  48.156  1.00 156.27 ? 582  TYR B CZ  1 
ATOM   18855 O  OH  . TYR C 1 582  ? 7.463    67.029  47.991  1.00 155.65 ? 582  TYR B OH  1 
ATOM   18856 N  N   . SER C 1 583  ? 8.571    58.737  47.823  1.00 158.65 ? 583  SER B N   1 
ATOM   18857 C  CA  . SER C 1 583  ? 8.978    57.396  48.201  1.00 160.28 ? 583  SER B CA  1 
ATOM   18858 C  C   . SER C 1 583  ? 8.941    57.211  49.720  1.00 153.57 ? 583  SER B C   1 
ATOM   18859 O  O   . SER C 1 583  ? 9.373    58.094  50.463  1.00 151.74 ? 583  SER B O   1 
ATOM   18860 C  CB  . SER C 1 583  ? 10.395   57.160  47.691  1.00 164.63 ? 583  SER B CB  1 
ATOM   18861 O  OG  . SER C 1 583  ? 11.201   58.297  47.980  1.00 167.35 ? 583  SER B OG  1 
ATOM   18862 N  N   . PRO C 1 584  ? 8.443    56.051  50.179  1.00 155.05 ? 584  PRO B N   1 
ATOM   18863 C  CA  . PRO C 1 584  ? 8.310    55.774  51.611  1.00 149.92 ? 584  PRO B CA  1 
ATOM   18864 C  C   . PRO C 1 584  ? 9.657    55.709  52.296  1.00 150.65 ? 584  PRO B C   1 
ATOM   18865 O  O   . PRO C 1 584  ? 10.031   54.642  52.741  1.00 149.88 ? 584  PRO B O   1 
ATOM   18866 C  CB  . PRO C 1 584  ? 7.664    54.387  51.647  1.00 153.62 ? 584  PRO B CB  1 
ATOM   18867 C  CG  . PRO C 1 584  ? 7.109    54.164  50.284  1.00 154.88 ? 584  PRO B CG  1 
ATOM   18868 C  CD  . PRO C 1 584  ? 7.997    54.915  49.353  1.00 155.59 ? 584  PRO B CD  1 
ATOM   18869 N  N   . GLY C 1 585  ? 10.379   56.815  52.370  1.00 149.23 ? 585  GLY B N   1 
ATOM   18870 C  CA  . GLY C 1 585  ? 11.622   56.834  53.111  1.00 151.53 ? 585  GLY B CA  1 
ATOM   18871 C  C   . GLY C 1 585  ? 12.503   57.959  52.637  1.00 152.81 ? 585  GLY B C   1 
ATOM   18872 O  O   . GLY C 1 585  ? 13.568   58.214  53.193  1.00 152.86 ? 585  GLY B O   1 
ATOM   18873 N  N   . GLN C 1 586  ? 12.046   58.640  51.596  1.00 154.51 ? 586  GLN B N   1 
ATOM   18874 C  CA  . GLN C 1 586  ? 12.837   59.694  50.990  1.00 157.51 ? 586  GLN B CA  1 
ATOM   18875 C  C   . GLN C 1 586  ? 13.265   60.733  51.996  1.00 159.42 ? 586  GLN B C   1 
ATOM   18876 O  O   . GLN C 1 586  ? 12.471   61.202  52.803  1.00 157.20 ? 586  GLN B O   1 
ATOM   18877 C  CB  . GLN C 1 586  ? 12.077   60.383  49.865  1.00 157.02 ? 586  GLN B CB  1 
ATOM   18878 C  CG  . GLN C 1 586  ? 12.940   61.341  49.088  1.00 159.69 ? 586  GLN B CG  1 
ATOM   18879 C  CD  . GLN C 1 586  ? 12.232   61.897  47.881  1.00 162.44 ? 586  GLN B CD  1 
ATOM   18880 O  OE1 . GLN C 1 586  ? 11.086   61.541  47.598  1.00 162.75 ? 586  GLN B OE1 1 
ATOM   18881 N  NE2 . GLN C 1 586  ? 12.910   62.782  47.154  1.00 164.62 ? 586  GLN B NE2 1 
ATOM   18882 N  N   . THR C 1 587  ? 14.543   61.066  51.947  1.00 164.15 ? 587  THR B N   1 
ATOM   18883 C  CA  . THR C 1 587  ? 15.050   62.238  52.615  1.00 168.80 ? 587  THR B CA  1 
ATOM   18884 C  C   . THR C 1 587  ? 14.543   63.404  51.780  1.00 170.16 ? 587  THR B C   1 
ATOM   18885 O  O   . THR C 1 587  ? 14.547   63.319  50.555  1.00 168.45 ? 587  THR B O   1 
ATOM   18886 C  CB  . THR C 1 587  ? 16.582   62.209  52.614  1.00 173.59 ? 587  THR B CB  1 
ATOM   18887 O  OG1 . THR C 1 587  ? 17.041   61.951  51.283  1.00 175.81 ? 587  THR B OG1 1 
ATOM   18888 C  CG2 . THR C 1 587  ? 17.096   61.096  53.522  1.00 175.30 ? 587  THR B CG2 1 
ATOM   18889 N  N   . VAL C 1 588  ? 14.092   64.477  52.429  1.00 173.20 ? 588  VAL B N   1 
ATOM   18890 C  CA  . VAL C 1 588  ? 13.516   65.619  51.711  1.00 174.87 ? 588  VAL B CA  1 
ATOM   18891 C  C   . VAL C 1 588  ? 13.461   66.901  52.529  1.00 173.82 ? 588  VAL B C   1 
ATOM   18892 O  O   . VAL C 1 588  ? 12.962   66.922  53.647  1.00 175.59 ? 588  VAL B O   1 
ATOM   18893 C  CB  . VAL C 1 588  ? 12.089   65.338  51.222  1.00 173.86 ? 588  VAL B CB  1 
ATOM   18894 C  CG1 . VAL C 1 588  ? 11.257   64.729  52.329  1.00 172.67 ? 588  VAL B CG1 1 
ATOM   18895 C  CG2 . VAL C 1 588  ? 11.454   66.621  50.750  1.00 172.85 ? 588  VAL B CG2 1 
ATOM   18896 N  N   . SER C 1 589  ? 13.944   67.982  51.936  1.00 172.72 ? 589  SER B N   1 
ATOM   18897 C  CA  . SER C 1 589  ? 14.059   69.255  52.628  1.00 171.89 ? 589  SER B CA  1 
ATOM   18898 C  C   . SER C 1 589  ? 12.765   70.075  52.558  1.00 168.24 ? 589  SER B C   1 
ATOM   18899 O  O   . SER C 1 589  ? 12.208   70.265  51.480  1.00 166.53 ? 589  SER B O   1 
ATOM   18900 C  CB  . SER C 1 589  ? 15.217   70.044  52.011  1.00 177.24 ? 589  SER B CB  1 
ATOM   18901 O  OG  . SER C 1 589  ? 16.199   69.168  51.457  1.00 181.82 ? 589  SER B OG  1 
ATOM   18902 N  N   . LEU C 1 590  ? 12.286   70.556  53.705  1.00 166.39 ? 590  LEU B N   1 
ATOM   18903 C  CA  . LEU C 1 590  ? 11.135   71.466  53.742  1.00 161.18 ? 590  LEU B CA  1 
ATOM   18904 C  C   . LEU C 1 590  ? 11.579   72.906  53.996  1.00 159.76 ? 590  LEU B C   1 
ATOM   18905 O  O   . LEU C 1 590  ? 12.500   73.144  54.779  1.00 161.96 ? 590  LEU B O   1 
ATOM   18906 C  CB  . LEU C 1 590  ? 10.134   71.035  54.810  1.00 155.55 ? 590  LEU B CB  1 
ATOM   18907 C  CG  . LEU C 1 590  ? 9.258    72.149  55.375  1.00 147.42 ? 590  LEU B CG  1 
ATOM   18908 C  CD1 . LEU C 1 590  ? 8.309    72.650  54.318  1.00 144.50 ? 590  LEU B CD1 1 
ATOM   18909 C  CD2 . LEU C 1 590  ? 8.486    71.678  56.594  1.00 143.56 ? 590  LEU B CD2 1 
ATOM   18910 N  N   . ASN C 1 591  ? 10.925   73.856  53.328  1.00 155.27 ? 591  ASN B N   1 
ATOM   18911 C  CA  . ASN C 1 591  ? 11.256   75.287  53.443  1.00 153.03 ? 591  ASN B CA  1 
ATOM   18912 C  C   . ASN C 1 591  ? 10.197   76.153  54.158  1.00 149.94 ? 591  ASN B C   1 
ATOM   18913 O  O   . ASN C 1 591  ? 9.002    76.010  53.911  1.00 148.63 ? 591  ASN B O   1 
ATOM   18914 C  CB  . ASN C 1 591  ? 11.536   75.882  52.048  1.00 154.03 ? 591  ASN B CB  1 
ATOM   18915 C  CG  . ASN C 1 591  ? 12.898   75.489  51.500  1.00 158.10 ? 591  ASN B CG  1 
ATOM   18916 O  OD1 . ASN C 1 591  ? 13.932   75.895  52.032  1.00 159.83 ? 591  ASN B OD1 1 
ATOM   18917 N  ND2 . ASN C 1 591  ? 12.903   74.708  50.421  1.00 159.42 ? 591  ASN B ND2 1 
ATOM   18918 N  N   . MET C 1 592  ? 10.637   77.050  55.037  1.00 148.13 ? 592  MET B N   1 
ATOM   18919 C  CA  . MET C 1 592  ? 9.755    78.073  55.585  1.00 145.69 ? 592  MET B CA  1 
ATOM   18920 C  C   . MET C 1 592  ? 9.951    79.388  54.833  1.00 146.13 ? 592  MET B C   1 
ATOM   18921 O  O   . MET C 1 592  ? 10.956   79.560  54.148  1.00 147.89 ? 592  MET B O   1 
ATOM   18922 C  CB  . MET C 1 592  ? 10.005   78.269  57.074  1.00 143.57 ? 592  MET B CB  1 
ATOM   18923 C  CG  . MET C 1 592  ? 9.052    77.499  57.990  1.00 141.99 ? 592  MET B CG  1 
ATOM   18924 S  SD  . MET C 1 592  ? 9.607    75.832  58.356  1.00 162.39 ? 592  MET B SD  1 
ATOM   18925 C  CE  . MET C 1 592  ? 11.370   76.145  58.319  1.00 151.37 ? 592  MET B CE  1 
ATOM   18926 N  N   . ALA C 1 593  ? 8.995    80.309  54.957  1.00 147.34 ? 593  ALA B N   1 
ATOM   18927 C  CA  . ALA C 1 593  ? 9.031    81.581  54.225  1.00 149.73 ? 593  ALA B CA  1 
ATOM   18928 C  C   . ALA C 1 593  ? 8.240    82.699  54.913  1.00 153.54 ? 593  ALA B C   1 
ATOM   18929 O  O   . ALA C 1 593  ? 7.125    82.475  55.391  1.00 151.18 ? 593  ALA B O   1 
ATOM   18930 C  CB  . ALA C 1 593  ? 8.531    81.386  52.795  1.00 148.36 ? 593  ALA B CB  1 
ATOM   18931 N  N   . THR C 1 594  ? 8.822    83.900  54.950  1.00 159.95 ? 594  THR B N   1 
ATOM   18932 C  CA  . THR C 1 594  ? 8.158    85.071  55.530  1.00 164.79 ? 594  THR B CA  1 
ATOM   18933 C  C   . THR C 1 594  ? 8.748    86.388  55.059  1.00 169.70 ? 594  THR B C   1 
ATOM   18934 O  O   . THR C 1 594  ? 9.951    86.497  54.818  1.00 171.96 ? 594  THR B O   1 
ATOM   18935 C  CB  . THR C 1 594  ? 8.273    85.120  57.060  1.00 165.42 ? 594  THR B CB  1 
ATOM   18936 O  OG1 . THR C 1 594  ? 8.559    83.818  57.578  1.00 165.55 ? 594  THR B OG1 1 
ATOM   18937 C  CG2 . THR C 1 594  ? 6.987    85.674  57.670  1.00 165.00 ? 594  THR B CG2 1 
ATOM   18938 N  N   . GLY C 1 595  ? 7.891    87.398  54.972  1.00 171.04 ? 595  GLY B N   1 
ATOM   18939 C  CA  . GLY C 1 595  ? 8.313    88.737  54.607  1.00 177.30 ? 595  GLY B CA  1 
ATOM   18940 C  C   . GLY C 1 595  ? 8.869    89.481  55.800  1.00 182.24 ? 595  GLY B C   1 
ATOM   18941 O  O   . GLY C 1 595  ? 9.315    90.619  55.693  1.00 183.95 ? 595  GLY B O   1 
ATOM   18942 N  N   . MET C 1 596  ? 8.836    88.828  56.949  1.00 188.16 ? 596  MET B N   1 
ATOM   18943 C  CA  . MET C 1 596  ? 9.339    89.422  58.169  1.00 191.80 ? 596  MET B CA  1 
ATOM   18944 C  C   . MET C 1 596  ? 9.650    88.294  59.123  1.00 192.09 ? 596  MET B C   1 
ATOM   18945 O  O   . MET C 1 596  ? 8.922    87.307  59.183  1.00 193.19 ? 596  MET B O   1 
ATOM   18946 C  CB  . MET C 1 596  ? 8.296    90.361  58.781  1.00 192.69 ? 596  MET B CB  1 
ATOM   18947 C  CG  . MET C 1 596  ? 8.209    91.722  58.117  1.00 193.41 ? 596  MET B CG  1 
ATOM   18948 S  SD  . MET C 1 596  ? 9.649    92.751  58.468  1.00 219.29 ? 596  MET B SD  1 
ATOM   18949 C  CE  . MET C 1 596  ? 9.298    93.236  60.155  1.00 169.67 ? 596  MET B CE  1 
ATOM   18950 N  N   . ASP C 1 597  ? 10.745   88.434  59.857  1.00 190.45 ? 597  ASP B N   1 
ATOM   18951 C  CA  . ASP C 1 597  ? 11.122   87.447  60.857  1.00 188.41 ? 597  ASP B CA  1 
ATOM   18952 C  C   . ASP C 1 597  ? 9.875    86.955  61.589  1.00 180.83 ? 597  ASP B C   1 
ATOM   18953 O  O   . ASP C 1 597  ? 9.014    87.758  61.952  1.00 177.78 ? 597  ASP B O   1 
ATOM   18954 C  CB  . ASP C 1 597  ? 12.104   88.076  61.848  1.00 196.16 ? 597  ASP B CB  1 
ATOM   18955 C  CG  . ASP C 1 597  ? 13.288   88.735  61.156  1.00 203.96 ? 597  ASP B CG  1 
ATOM   18956 O  OD1 . ASP C 1 597  ? 13.915   88.074  60.299  1.00 206.80 ? 597  ASP B OD1 1 
ATOM   18957 O  OD2 . ASP C 1 597  ? 13.591   89.908  61.472  1.00 206.94 ? 597  ASP B OD2 1 
ATOM   18958 N  N   . SER C 1 598  ? 9.776    85.645  61.813  1.00 175.42 ? 598  SER B N   1 
ATOM   18959 C  CA  . SER C 1 598  ? 8.557    85.079  62.389  1.00 167.47 ? 598  SER B CA  1 
ATOM   18960 C  C   . SER C 1 598  ? 8.710    83.736  63.095  1.00 159.24 ? 598  SER B C   1 
ATOM   18961 O  O   . SER C 1 598  ? 9.661    82.991  62.855  1.00 158.98 ? 598  SER B O   1 
ATOM   18962 C  CB  . SER C 1 598  ? 7.477    84.952  61.312  1.00 165.89 ? 598  SER B CB  1 
ATOM   18963 O  OG  . SER C 1 598  ? 6.247    84.526  61.869  1.00 163.41 ? 598  SER B OG  1 
ATOM   18964 N  N   . TRP C 1 599  ? 7.754    83.446  63.975  1.00 151.05 ? 599  TRP B N   1 
ATOM   18965 C  CA  . TRP C 1 599  ? 7.613    82.114  64.557  1.00 146.26 ? 599  TRP B CA  1 
ATOM   18966 C  C   . TRP C 1 599  ? 6.735    81.228  63.668  1.00 141.55 ? 599  TRP B C   1 
ATOM   18967 O  O   . TRP C 1 599  ? 5.738    81.684  63.112  1.00 142.29 ? 599  TRP B O   1 
ATOM   18968 C  CB  . TRP C 1 599  ? 7.079    82.196  65.992  1.00 147.52 ? 599  TRP B CB  1 
ATOM   18969 C  CG  . TRP C 1 599  ? 8.106    82.789  66.914  1.00 153.94 ? 599  TRP B CG  1 
ATOM   18970 C  CD1 . TRP C 1 599  ? 8.028    83.975  67.581  1.00 157.00 ? 599  TRP B CD1 1 
ATOM   18971 C  CD2 . TRP C 1 599  ? 9.396    82.243  67.227  1.00 156.65 ? 599  TRP B CD2 1 
ATOM   18972 N  NE1 . TRP C 1 599  ? 9.182    84.195  68.305  1.00 158.37 ? 599  TRP B NE1 1 
ATOM   18973 C  CE2 . TRP C 1 599  ? 10.033   83.145  68.101  1.00 157.49 ? 599  TRP B CE2 1 
ATOM   18974 C  CE3 . TRP C 1 599  ? 10.066   81.078  66.861  1.00 157.25 ? 599  TRP B CE3 1 
ATOM   18975 C  CZ2 . TRP C 1 599  ? 11.294   82.916  68.601  1.00 157.72 ? 599  TRP B CZ2 1 
ATOM   18976 C  CZ3 . TRP C 1 599  ? 11.311   80.856  67.367  1.00 157.72 ? 599  TRP B CZ3 1 
ATOM   18977 C  CH2 . TRP C 1 599  ? 11.915   81.767  68.224  1.00 157.99 ? 599  TRP B CH2 1 
ATOM   18978 N  N   . VAL C 1 600  ? 7.136    79.973  63.508  1.00 135.75 ? 600  VAL B N   1 
ATOM   18979 C  CA  . VAL C 1 600  ? 6.422    79.013  62.685  1.00 129.26 ? 600  VAL B CA  1 
ATOM   18980 C  C   . VAL C 1 600  ? 5.771    78.059  63.664  1.00 125.31 ? 600  VAL B C   1 
ATOM   18981 O  O   . VAL C 1 600  ? 5.818    78.308  64.852  1.00 126.49 ? 600  VAL B O   1 
ATOM   18982 C  CB  . VAL C 1 600  ? 7.420    78.254  61.798  1.00 128.52 ? 600  VAL B CB  1 
ATOM   18983 C  CG1 . VAL C 1 600  ? 6.710    77.396  60.778  1.00 127.74 ? 600  VAL B CG1 1 
ATOM   18984 C  CG2 . VAL C 1 600  ? 8.336    79.233  61.100  1.00 127.83 ? 600  VAL B CG2 1 
ATOM   18985 N  N   . ALA C 1 601  ? 5.159    76.982  63.179  1.00 123.00 ? 601  ALA B N   1 
ATOM   18986 C  CA  . ALA C 1 601  ? 4.749    75.858  64.033  1.00 120.74 ? 601  ALA B CA  1 
ATOM   18987 C  C   . ALA C 1 601  ? 4.207    74.694  63.208  1.00 121.55 ? 601  ALA B C   1 
ATOM   18988 O  O   . ALA C 1 601  ? 2.995    74.571  62.991  1.00 122.28 ? 601  ALA B O   1 
ATOM   18989 C  CB  . ALA C 1 601  ? 3.726    76.294  65.078  1.00 118.87 ? 601  ALA B CB  1 
ATOM   18990 N  N   . LEU C 1 602  ? 5.117    73.833  62.761  1.00 121.01 ? 602  LEU B N   1 
ATOM   18991 C  CA  . LEU C 1 602  ? 4.767    72.725  61.874  1.00 120.38 ? 602  LEU B CA  1 
ATOM   18992 C  C   . LEU C 1 602  ? 3.900    71.647  62.540  1.00 121.74 ? 602  LEU B C   1 
ATOM   18993 O  O   . LEU C 1 602  ? 3.633    71.674  63.744  1.00 122.13 ? 602  LEU B O   1 
ATOM   18994 C  CB  . LEU C 1 602  ? 6.023    72.100  61.240  1.00 117.89 ? 602  LEU B CB  1 
ATOM   18995 C  CG  . LEU C 1 602  ? 7.084    73.108  60.771  1.00 116.19 ? 602  LEU B CG  1 
ATOM   18996 C  CD1 . LEU C 1 602  ? 8.160    72.454  59.889  1.00 115.05 ? 602  LEU B CD1 1 
ATOM   18997 C  CD2 . LEU C 1 602  ? 6.444    74.307  60.071  1.00 114.23 ? 602  LEU B CD2 1 
ATOM   18998 N  N   . ALA C 1 603  ? 3.452    70.708  61.719  1.00 120.30 ? 603  ALA B N   1 
ATOM   18999 C  CA  . ALA C 1 603  ? 2.623    69.596  62.149  1.00 117.06 ? 603  ALA B CA  1 
ATOM   19000 C  C   . ALA C 1 603  ? 2.393    68.794  60.891  1.00 114.03 ? 603  ALA B C   1 
ATOM   19001 O  O   . ALA C 1 603  ? 2.344    69.349  59.801  1.00 114.33 ? 603  ALA B O   1 
ATOM   19002 C  CB  . ALA C 1 603  ? 1.314    70.080  62.731  1.00 114.47 ? 603  ALA B CB  1 
ATOM   19003 N  N   . ALA C 1 604  ? 2.293    67.486  61.032  1.00 114.61 ? 604  ALA B N   1 
ATOM   19004 C  CA  . ALA C 1 604  ? 2.128    66.620  59.880  1.00 113.40 ? 604  ALA B CA  1 
ATOM   19005 C  C   . ALA C 1 604  ? 1.137    65.555  60.286  1.00 115.09 ? 604  ALA B C   1 
ATOM   19006 O  O   . ALA C 1 604  ? 1.484    64.575  60.941  1.00 116.10 ? 604  ALA B O   1 
ATOM   19007 C  CB  . ALA C 1 604  ? 3.470    65.994  59.453  1.00 112.86 ? 604  ALA B CB  1 
ATOM   19008 N  N   . VAL C 1 605  ? -0.115   65.779  59.923  1.00 113.65 ? 605  VAL B N   1 
ATOM   19009 C  CA  . VAL C 1 605  ? -1.185   64.883  60.293  1.00 114.22 ? 605  VAL B CA  1 
ATOM   19010 C  C   . VAL C 1 605  ? -1.406   63.877  59.184  1.00 117.57 ? 605  VAL B C   1 
ATOM   19011 O  O   . VAL C 1 605  ? -1.232   64.201  58.013  1.00 117.77 ? 605  VAL B O   1 
ATOM   19012 C  CB  . VAL C 1 605  ? -2.468   65.680  60.471  1.00 113.13 ? 605  VAL B CB  1 
ATOM   19013 C  CG1 . VAL C 1 605  ? -3.647   64.749  60.647  1.00 112.77 ? 605  VAL B CG1 1 
ATOM   19014 C  CG2 . VAL C 1 605  ? -2.326   66.641  61.637  1.00 112.83 ? 605  VAL B CG2 1 
ATOM   19015 N  N   . ASP C 1 606  ? -1.777   62.651  59.524  1.00 119.15 ? 606  ASP B N   1 
ATOM   19016 C  CA  . ASP C 1 606  ? -2.295   61.787  58.484  1.00 121.48 ? 606  ASP B CA  1 
ATOM   19017 C  C   . ASP C 1 606  ? -3.547   62.483  58.023  1.00 121.89 ? 606  ASP B C   1 
ATOM   19018 O  O   . ASP C 1 606  ? -4.573   62.443  58.698  1.00 121.40 ? 606  ASP B O   1 
ATOM   19019 C  CB  . ASP C 1 606  ? -2.662   60.405  59.003  1.00 123.32 ? 606  ASP B CB  1 
ATOM   19020 C  CG  . ASP C 1 606  ? -3.532   59.642  58.028  1.00 123.58 ? 606  ASP B CG  1 
ATOM   19021 O  OD1 . ASP C 1 606  ? -3.796   60.215  56.952  1.00 123.68 ? 606  ASP B OD1 1 
ATOM   19022 O  OD2 . ASP C 1 606  ? -3.947   58.491  58.320  1.00 123.36 ? 606  ASP B OD2 1 
ATOM   19023 N  N   . SER C 1 607  ? -3.458   63.128  56.870  1.00 106.74 ? 607  SER B N   1 
ATOM   19024 C  CA  . SER C 1 607  ? -4.574   63.869  56.306  1.00 111.01 ? 607  SER B CA  1 
ATOM   19025 C  C   . SER C 1 607  ? -5.926   63.138  56.363  1.00 110.08 ? 607  SER B C   1 
ATOM   19026 O  O   . SER C 1 607  ? -6.969   63.751  56.118  1.00 109.23 ? 607  SER B O   1 
ATOM   19027 C  CB  . SER C 1 607  ? -4.287   64.153  54.834  1.00 118.50 ? 607  SER B CB  1 
ATOM   19028 O  OG  . SER C 1 607  ? -4.706   63.042  54.023  1.00 122.25 ? 607  SER B OG  1 
ATOM   19029 N  N   . ALA C 1 608  ? -5.922   61.837  56.642  1.00 109.87 ? 608  ALA B N   1 
ATOM   19030 C  CA  . ALA C 1 608  ? -7.141   61.044  56.502  1.00 107.68 ? 608  ALA B CA  1 
ATOM   19031 C  C   . ALA C 1 608  ? -8.220   61.275  57.573  1.00 104.29 ? 608  ALA B C   1 
ATOM   19032 O  O   . ALA C 1 608  ? -9.385   60.929  57.353  1.00 103.01 ? 608  ALA B O   1 
ATOM   19033 C  CB  . ALA C 1 608  ? -6.809   59.578  56.406  1.00 110.54 ? 608  ALA B CB  1 
ATOM   19034 N  N   . VAL C 1 609  ? -7.852   61.844  58.720  1.00 100.84 ? 609  VAL B N   1 
ATOM   19035 C  CA  . VAL C 1 609  ? -8.831   62.083  59.773  1.00 94.96  ? 609  VAL B CA  1 
ATOM   19036 C  C   . VAL C 1 609  ? -10.007  62.890  59.238  1.00 94.73  ? 609  VAL B C   1 
ATOM   19037 O  O   . VAL C 1 609  ? -11.100  62.344  59.060  1.00 95.52  ? 609  VAL B O   1 
ATOM   19038 C  CB  . VAL C 1 609  ? -8.189   62.763  60.932  1.00 92.13  ? 609  VAL B CB  1 
ATOM   19039 C  CG1 . VAL C 1 609  ? -7.313   61.774  61.599  1.00 93.43  ? 609  VAL B CG1 1 
ATOM   19040 C  CG2 . VAL C 1 609  ? -7.351   63.911  60.452  1.00 91.24  ? 609  VAL B CG2 1 
ATOM   19041 N  N   . TYR C 1 610  ? -9.764   64.164  58.949  1.00 93.19  ? 610  TYR B N   1 
ATOM   19042 C  CA  . TYR C 1 610  ? -10.720  65.010  58.264  1.00 90.49  ? 610  TYR B CA  1 
ATOM   19043 C  C   . TYR C 1 610  ? -11.324  64.293  57.022  1.00 150.98 ? 610  TYR B C   1 
ATOM   19044 O  O   . TYR C 1 610  ? -12.486  63.845  57.015  1.00 145.33 ? 610  TYR B O   1 
ATOM   19045 C  CB  . TYR C 1 610  ? -10.007  66.287  57.805  1.00 91.77  ? 610  TYR B CB  1 
ATOM   19046 C  CG  . TYR C 1 610  ? -8.796   66.726  58.605  1.00 90.41  ? 610  TYR B CG  1 
ATOM   19047 C  CD1 . TYR C 1 610  ? -8.918   67.686  59.572  1.00 95.20  ? 610  TYR B CD1 1 
ATOM   19048 C  CD2 . TYR C 1 610  ? -7.528   66.211  58.366  1.00 91.81  ? 610  TYR B CD2 1 
ATOM   19049 C  CE1 . TYR C 1 610  ? -7.819   68.115  60.325  1.00 97.51  ? 610  TYR B CE1 1 
ATOM   19050 C  CE2 . TYR C 1 610  ? -6.410   66.635  59.113  1.00 93.97  ? 610  TYR B CE2 1 
ATOM   19051 C  CZ  . TYR C 1 610  ? -6.572   67.595  60.100  1.00 95.05  ? 610  TYR B CZ  1 
ATOM   19052 O  OH  . TYR C 1 610  ? -5.529   68.079  60.881  1.00 94.94  ? 610  TYR B OH  1 
ATOM   19053 N  N   . GLY C 1 611  ? -10.518  64.209  55.967  1.00 157.54 ? 611  GLY B N   1 
ATOM   19054 C  CA  . GLY C 1 611  ? -10.841  63.429  54.788  1.00 164.96 ? 611  GLY B CA  1 
ATOM   19055 C  C   . GLY C 1 611  ? -12.245  63.530  54.220  1.00 171.91 ? 611  GLY B C   1 
ATOM   19056 O  O   . GLY C 1 611  ? -12.543  64.463  53.472  1.00 173.88 ? 611  GLY B O   1 
ATOM   19057 N  N   . VAL C 1 612  ? -13.101  62.565  54.570  1.00 178.78 ? 612  VAL B N   1 
ATOM   19058 C  CA  . VAL C 1 612  ? -14.408  62.387  53.914  1.00 186.13 ? 612  VAL B CA  1 
ATOM   19059 C  C   . VAL C 1 612  ? -15.161  63.705  53.810  1.00 197.37 ? 612  VAL B C   1 
ATOM   19060 O  O   . VAL C 1 612  ? -15.554  64.280  54.824  1.00 196.82 ? 612  VAL B O   1 
ATOM   19061 C  CB  . VAL C 1 612  ? -15.304  61.334  54.639  1.00 267.03 ? 612  VAL B CB  1 
ATOM   19062 C  CG1 . VAL C 1 612  ? -14.889  59.904  54.276  1.00 269.10 ? 612  VAL B CG1 1 
ATOM   19063 C  CG2 . VAL C 1 612  ? -15.291  61.549  56.149  1.00 266.62 ? 612  VAL B CG2 1 
ATOM   19064 N  N   . GLN C 1 613  ? -15.371  64.164  52.579  1.00 207.34 ? 613  GLN B N   1 
ATOM   19065 C  CA  . GLN C 1 613  ? -15.822  65.535  52.330  1.00 218.51 ? 613  GLN B CA  1 
ATOM   19066 C  C   . GLN C 1 613  ? -15.316  66.486  53.409  1.00 225.95 ? 613  GLN B C   1 
ATOM   19067 O  O   . GLN C 1 613  ? -16.013  66.758  54.390  1.00 224.61 ? 613  GLN B O   1 
ATOM   19068 C  CB  . GLN C 1 613  ? -17.356  65.650  52.175  1.00 218.35 ? 613  GLN B CB  1 
ATOM   19069 C  CG  . GLN C 1 613  ? -17.875  67.120  52.117  1.00 215.97 ? 613  GLN B CG  1 
ATOM   19070 C  CD  . GLN C 1 613  ? -19.184  67.309  51.338  1.00 214.30 ? 613  GLN B CD  1 
ATOM   19071 O  OE1 . GLN C 1 613  ? -19.365  66.762  50.252  1.00 214.65 ? 613  GLN B OE1 1 
ATOM   19072 N  NE2 . GLN C 1 613  ? -20.084  68.114  51.888  1.00 212.56 ? 613  GLN B NE2 1 
ATOM   19073 N  N   . ARG C 1 614  ? -14.095  66.979  53.236  1.00 234.99 ? 614  ARG B N   1 
ATOM   19074 C  CA  . ARG C 1 614  ? -13.587  68.009  54.123  1.00 240.95 ? 614  ARG B CA  1 
ATOM   19075 C  C   . ARG C 1 614  ? -14.359  69.275  53.817  1.00 244.07 ? 614  ARG B C   1 
ATOM   19076 O  O   . ARG C 1 614  ? -13.949  70.068  52.972  1.00 247.34 ? 614  ARG B O   1 
ATOM   19077 C  CB  . ARG C 1 614  ? -12.096  68.224  53.897  1.00 241.67 ? 614  ARG B CB  1 
ATOM   19078 C  CG  . ARG C 1 614  ? -11.396  68.947  55.026  1.00 240.25 ? 614  ARG B CG  1 
ATOM   19079 C  CD  . ARG C 1 614  ? -10.053  68.304  55.248  1.00 240.40 ? 614  ARG B CD  1 
ATOM   19080 N  NE  . ARG C 1 614  ? -9.024   69.267  55.597  1.00 240.95 ? 614  ARG B NE  1 
ATOM   19081 C  CZ  . ARG C 1 614  ? -7.752   69.130  55.254  1.00 243.35 ? 614  ARG B CZ  1 
ATOM   19082 N  NH1 . ARG C 1 614  ? -7.371   68.073  54.550  1.00 244.50 ? 614  ARG B NH1 1 
ATOM   19083 N  NH2 . ARG C 1 614  ? -6.872   70.052  55.600  1.00 245.11 ? 614  ARG B NH2 1 
ATOM   19084 N  N   . GLY C 1 615  ? -15.485  69.450  54.504  1.00 245.09 ? 615  GLY B N   1 
ATOM   19085 C  CA  . GLY C 1 615  ? -16.404  70.536  54.220  1.00 246.56 ? 615  GLY B CA  1 
ATOM   19086 C  C   . GLY C 1 615  ? -15.676  71.792  53.800  1.00 251.27 ? 615  GLY B C   1 
ATOM   19087 O  O   . GLY C 1 615  ? -14.703  72.200  54.443  1.00 253.07 ? 615  GLY B O   1 
ATOM   19088 N  N   . ALA C 1 616  ? -16.145  72.399  52.714  1.00 253.72 ? 616  ALA B N   1 
ATOM   19089 C  CA  . ALA C 1 616  ? -15.492  73.579  52.165  1.00 256.50 ? 616  ALA B CA  1 
ATOM   19090 C  C   . ALA C 1 616  ? -15.163  74.589  53.264  1.00 256.65 ? 616  ALA B C   1 
ATOM   19091 O  O   . ALA C 1 616  ? -13.992  74.909  53.478  1.00 258.88 ? 616  ALA B O   1 
ATOM   19092 C  CB  . ALA C 1 616  ? -16.353  74.212  51.075  1.00 256.74 ? 616  ALA B CB  1 
ATOM   19093 N  N   . LYS C 1 617  ? -16.189  75.060  53.973  1.00 253.67 ? 617  LYS B N   1 
ATOM   19094 C  CA  . LYS C 1 617  ? -16.019  76.088  55.003  1.00 251.34 ? 617  LYS B CA  1 
ATOM   19095 C  C   . LYS C 1 617  ? -14.838  76.969  54.637  1.00 248.81 ? 617  LYS B C   1 
ATOM   19096 O  O   . LYS C 1 617  ? -14.951  77.803  53.747  1.00 250.28 ? 617  LYS B O   1 
ATOM   19097 C  CB  . LYS C 1 617  ? -15.814  75.472  56.391  1.00 252.64 ? 617  LYS B CB  1 
ATOM   19098 C  CG  . LYS C 1 617  ? -15.937  76.471  57.547  1.00 253.72 ? 617  LYS B CG  1 
ATOM   19099 C  CD  . LYS C 1 617  ? -17.290  77.177  57.519  1.00 253.29 ? 617  LYS B CD  1 
ATOM   19100 C  CE  . LYS C 1 617  ? -17.528  78.020  58.763  1.00 253.82 ? 617  LYS B CE  1 
ATOM   19101 N  NZ  . LYS C 1 617  ? -18.850  78.710  58.704  1.00 252.96 ? 617  LYS B NZ  1 
ATOM   19102 N  N   . LYS C 1 618  ? -13.711  76.752  55.316  1.00 244.05 ? 618  LYS B N   1 
ATOM   19103 C  CA  . LYS C 1 618  ? -12.421  77.364  54.976  1.00 240.24 ? 618  LYS B CA  1 
ATOM   19104 C  C   . LYS C 1 618  ? -11.318  76.818  55.900  1.00 230.08 ? 618  LYS B C   1 
ATOM   19105 O  O   . LYS C 1 618  ? -11.613  76.273  56.969  1.00 225.54 ? 618  LYS B O   1 
ATOM   19106 C  CB  . LYS C 1 618  ? -12.473  78.890  55.096  1.00 247.18 ? 618  LYS B CB  1 
ATOM   19107 C  CG  . LYS C 1 618  ? -13.338  79.633  54.076  1.00 251.37 ? 618  LYS B CG  1 
ATOM   19108 C  CD  . LYS C 1 618  ? -12.758  79.653  52.668  1.00 255.89 ? 618  LYS B CD  1 
ATOM   19109 C  CE  . LYS C 1 618  ? -13.548  80.601  51.753  1.00 256.45 ? 618  LYS B CE  1 
ATOM   19110 N  NZ  . LYS C 1 618  ? -15.014  80.310  51.702  1.00 254.02 ? 618  LYS B NZ  1 
ATOM   19111 N  N   . PRO C 1 619  ? -10.044  76.946  55.481  1.00 224.14 ? 619  PRO B N   1 
ATOM   19112 C  CA  . PRO C 1 619  ? -8.892   76.583  56.323  1.00 220.59 ? 619  PRO B CA  1 
ATOM   19113 C  C   . PRO C 1 619  ? -8.412   77.720  57.248  1.00 215.30 ? 619  PRO B C   1 
ATOM   19114 O  O   . PRO C 1 619  ? -8.560   77.593  58.465  1.00 213.85 ? 619  PRO B O   1 
ATOM   19115 C  CB  . PRO C 1 619  ? -7.805   76.229  55.296  1.00 224.16 ? 619  PRO B CB  1 
ATOM   19116 C  CG  . PRO C 1 619  ? -8.496   76.244  53.931  1.00 224.74 ? 619  PRO B CG  1 
ATOM   19117 C  CD  . PRO C 1 619  ? -9.644   77.178  54.085  1.00 224.36 ? 619  PRO B CD  1 
ATOM   19118 N  N   . LEU C 1 620  ? -7.851   78.792  56.672  1.00 212.39 ? 620  LEU B N   1 
ATOM   19119 C  CA  . LEU C 1 620  ? -7.369   79.992  57.399  1.00 208.57 ? 620  LEU B CA  1 
ATOM   19120 C  C   . LEU C 1 620  ? -8.485   80.969  57.805  1.00 207.19 ? 620  LEU B C   1 
ATOM   19121 O  O   . LEU C 1 620  ? -8.279   81.855  58.641  1.00 208.73 ? 620  LEU B O   1 
ATOM   19122 C  CB  . LEU C 1 620  ? -6.316   80.745  56.565  1.00 206.37 ? 620  LEU B CB  1 
ATOM   19123 C  CG  . LEU C 1 620  ? -5.953   82.184  56.945  1.00 204.18 ? 620  LEU B CG  1 
ATOM   19124 C  CD1 . LEU C 1 620  ? -5.067   82.188  58.166  1.00 205.36 ? 620  LEU B CD1 1 
ATOM   19125 C  CD2 . LEU C 1 620  ? -5.264   82.912  55.802  1.00 205.43 ? 620  LEU B CD2 1 
ATOM   19126 N  N   . GLU C 1 621  ? -9.652   80.815  57.182  1.00 204.88 ? 621  GLU B N   1 
ATOM   19127 C  CA  . GLU C 1 621  ? -10.855  81.562  57.546  1.00 203.83 ? 621  GLU B CA  1 
ATOM   19128 C  C   . GLU C 1 621  ? -11.465  80.971  58.830  1.00 197.58 ? 621  GLU B C   1 
ATOM   19129 O  O   . GLU C 1 621  ? -12.168  81.667  59.568  1.00 196.82 ? 621  GLU B O   1 
ATOM   19130 C  CB  . GLU C 1 621  ? -11.846  81.573  56.362  1.00 208.18 ? 621  GLU B CB  1 
ATOM   19131 C  CG  . GLU C 1 621  ? -13.265  82.116  56.623  1.00 212.02 ? 621  GLU B CG  1 
ATOM   19132 C  CD  . GLU C 1 621  ? -14.179  82.031  55.389  1.00 214.20 ? 621  GLU B CD  1 
ATOM   19133 O  OE1 . GLU C 1 621  ? -13.760  82.488  54.303  1.00 216.72 ? 621  GLU B OE1 1 
ATOM   19134 O  OE2 . GLU C 1 621  ? -15.312  81.502  55.501  1.00 213.04 ? 621  GLU B OE2 1 
ATOM   19135 N  N   . ARG C 1 622  ? -11.173  79.697  59.106  1.00 191.77 ? 622  ARG B N   1 
ATOM   19136 C  CA  . ARG C 1 622  ? -11.567  79.075  60.371  1.00 184.74 ? 622  ARG B CA  1 
ATOM   19137 C  C   . ARG C 1 622  ? -11.166  80.021  61.500  1.00 179.24 ? 622  ARG B C   1 
ATOM   19138 O  O   . ARG C 1 622  ? -12.008  80.435  62.297  1.00 178.69 ? 622  ARG B O   1 
ATOM   19139 C  CB  . ARG C 1 622  ? -10.903  77.698  60.543  1.00 185.06 ? 622  ARG B CB  1 
ATOM   19140 C  CG  . ARG C 1 622  ? -11.543  76.781  61.600  1.00 183.78 ? 622  ARG B CG  1 
ATOM   19141 C  CD  . ARG C 1 622  ? -10.847  75.398  61.683  1.00 168.25 ? 622  ARG B CD  1 
ATOM   19142 N  NE  . ARG C 1 622  ? -9.457   75.468  62.163  1.00 171.11 ? 622  ARG B NE  1 
ATOM   19143 C  CZ  . ARG C 1 622  ? -8.649   74.417  62.321  1.00 171.44 ? 622  ARG B CZ  1 
ATOM   19144 N  NH1 . ARG C 1 622  ? -9.086   73.198  62.032  1.00 170.54 ? 622  ARG B NH1 1 
ATOM   19145 N  NH2 . ARG C 1 622  ? -7.402   74.584  62.761  1.00 172.46 ? 622  ARG B NH2 1 
ATOM   19146 N  N   . VAL C 1 623  ? -9.890   80.399  61.544  1.00 175.41 ? 623  VAL B N   1 
ATOM   19147 C  CA  . VAL C 1 623  ? -9.420   81.334  62.566  1.00 171.97 ? 623  VAL B CA  1 
ATOM   19148 C  C   . VAL C 1 623  ? -9.968   82.752  62.364  1.00 167.62 ? 623  VAL B C   1 
ATOM   19149 O  O   . VAL C 1 623  ? -10.545  83.331  63.282  1.00 167.00 ? 623  VAL B O   1 
ATOM   19150 C  CB  . VAL C 1 623  ? -7.868   81.336  62.714  1.00 130.55 ? 623  VAL B CB  1 
ATOM   19151 C  CG1 . VAL C 1 623  ? -7.331   82.754  62.725  1.00 132.52 ? 623  VAL B CG1 1 
ATOM   19152 C  CG2 . VAL C 1 623  ? -7.429   80.540  63.980  1.00 128.38 ? 623  VAL B CG2 1 
ATOM   19153 N  N   . PHE C 1 624  ? -9.819   83.309  61.171  1.00 163.66 ? 624  PHE B N   1 
ATOM   19154 C  CA  . PHE C 1 624  ? -10.305  84.665  60.956  1.00 159.67 ? 624  PHE B CA  1 
ATOM   19155 C  C   . PHE C 1 624  ? -11.746  84.852  61.395  1.00 161.41 ? 624  PHE B C   1 
ATOM   19156 O  O   . PHE C 1 624  ? -12.099  85.898  61.930  1.00 162.62 ? 624  PHE B O   1 
ATOM   19157 C  CB  . PHE C 1 624  ? -10.157  85.086  59.497  1.00 150.07 ? 624  PHE B CB  1 
ATOM   19158 C  CG  . PHE C 1 624  ? -9.025   86.025  59.263  1.00 141.96 ? 624  PHE B CG  1 
ATOM   19159 C  CD1 . PHE C 1 624  ? -8.119   85.800  58.247  1.00 139.21 ? 624  PHE B CD1 1 
ATOM   19160 C  CD2 . PHE C 1 624  ? -8.859   87.125  60.075  1.00 138.21 ? 624  PHE B CD2 1 
ATOM   19161 C  CE1 . PHE C 1 624  ? -7.067   86.663  58.036  1.00 139.66 ? 624  PHE B CE1 1 
ATOM   19162 C  CE2 . PHE C 1 624  ? -7.815   87.981  59.871  1.00 138.63 ? 624  PHE B CE2 1 
ATOM   19163 C  CZ  . PHE C 1 624  ? -6.914   87.751  58.848  1.00 139.85 ? 624  PHE B CZ  1 
ATOM   19164 N  N   . GLN C 1 625  ? -12.580  83.847  61.156  1.00 163.42 ? 625  GLN B N   1 
ATOM   19165 C  CA  . GLN C 1 625  ? -13.990  83.961  61.499  1.00 167.70 ? 625  GLN B CA  1 
ATOM   19166 C  C   . GLN C 1 625  ? -14.100  84.249  62.984  1.00 166.34 ? 625  GLN B C   1 
ATOM   19167 O  O   . GLN C 1 625  ? -14.591  85.303  63.398  1.00 167.27 ? 625  GLN B O   1 
ATOM   19168 C  CB  . GLN C 1 625  ? -14.751  82.676  61.160  1.00 174.19 ? 625  GLN B CB  1 
ATOM   19169 C  CG  . GLN C 1 625  ? -15.094  82.512  59.682  1.00 182.56 ? 625  GLN B CG  1 
ATOM   19170 C  CD  . GLN C 1 625  ? -16.152  81.441  59.437  1.00 188.43 ? 625  GLN B CD  1 
ATOM   19171 O  OE1 . GLN C 1 625  ? -17.327  81.634  59.754  1.00 190.14 ? 625  GLN B OE1 1 
ATOM   19172 N  NE2 . GLN C 1 625  ? -15.738  80.312  58.861  1.00 190.48 ? 625  GLN B NE2 1 
ATOM   19173 N  N   . PHE C 1 626  ? -13.615  83.298  63.772  1.00 164.21 ? 626  PHE B N   1 
ATOM   19174 C  CA  . PHE C 1 626  ? -13.564  83.420  65.217  1.00 161.62 ? 626  PHE B CA  1 
ATOM   19175 C  C   . PHE C 1 626  ? -12.895  84.737  65.648  1.00 155.28 ? 626  PHE B C   1 
ATOM   19176 O  O   . PHE C 1 626  ? -13.538  85.616  66.227  1.00 151.75 ? 626  PHE B O   1 
ATOM   19177 C  CB  . PHE C 1 626  ? -12.832  82.193  65.783  1.00 168.03 ? 626  PHE B CB  1 
ATOM   19178 C  CG  . PHE C 1 626  ? -12.412  82.335  67.218  1.00 175.49 ? 626  PHE B CG  1 
ATOM   19179 C  CD1 . PHE C 1 626  ? -13.145  81.743  68.231  1.00 177.14 ? 626  PHE B CD1 1 
ATOM   19180 C  CD2 . PHE C 1 626  ? -11.273  83.053  67.555  1.00 179.99 ? 626  PHE B CD2 1 
ATOM   19181 C  CE1 . PHE C 1 626  ? -12.752  81.873  69.558  1.00 180.18 ? 626  PHE B CE1 1 
ATOM   19182 C  CE2 . PHE C 1 626  ? -10.878  83.189  68.876  1.00 183.12 ? 626  PHE B CE2 1 
ATOM   19183 C  CZ  . PHE C 1 626  ? -11.616  82.597  69.878  1.00 182.85 ? 626  PHE B CZ  1 
ATOM   19184 N  N   . LEU C 1 627  ? -11.615  84.877  65.320  1.00 150.63 ? 627  LEU B N   1 
ATOM   19185 C  CA  . LEU C 1 627  ? -10.771  85.943  65.841  1.00 146.67 ? 627  LEU B CA  1 
ATOM   19186 C  C   . LEU C 1 627  ? -11.269  87.364  65.559  1.00 147.08 ? 627  LEU B C   1 
ATOM   19187 O  O   . LEU C 1 627  ? -10.596  88.340  65.870  1.00 151.20 ? 627  LEU B O   1 
ATOM   19188 C  CB  . LEU C 1 627  ? -9.344   85.732  65.335  1.00 143.36 ? 627  LEU B CB  1 
ATOM   19189 C  CG  . LEU C 1 627  ? -8.377   86.887  65.102  1.00 141.69 ? 627  LEU B CG  1 
ATOM   19190 C  CD1 . LEU C 1 627  ? -6.957   86.387  65.182  1.00 141.82 ? 627  LEU B CD1 1 
ATOM   19191 C  CD2 . LEU C 1 627  ? -8.624   87.511  63.751  1.00 140.20 ? 627  LEU B CD2 1 
ATOM   19192 N  N   . GLU C 1 628  ? -12.454  87.484  64.982  1.00 142.11 ? 628  GLU B N   1 
ATOM   19193 C  CA  . GLU C 1 628  ? -13.022  88.797  64.726  1.00 144.19 ? 628  GLU B CA  1 
ATOM   19194 C  C   . GLU C 1 628  ? -14.467  88.798  65.160  1.00 139.10 ? 628  GLU B C   1 
ATOM   19195 O  O   . GLU C 1 628  ? -15.343  89.324  64.476  1.00 139.40 ? 628  GLU B O   1 
ATOM   19196 C  CB  . GLU C 1 628  ? -12.865  89.236  63.258  1.00 152.29 ? 628  GLU B CB  1 
ATOM   19197 C  CG  . GLU C 1 628  ? -13.855  88.630  62.234  1.00 166.61 ? 628  GLU B CG  1 
ATOM   19198 C  CD  . GLU C 1 628  ? -14.088  89.544  61.018  1.00 174.46 ? 628  GLU B CD  1 
ATOM   19199 O  OE1 . GLU C 1 628  ? -14.457  90.729  61.213  1.00 178.16 ? 628  GLU B OE1 1 
ATOM   19200 O  OE2 . GLU C 1 628  ? -13.911  89.075  59.869  1.00 175.06 ? 628  GLU B OE2 1 
ATOM   19201 N  N   . LYS C 1 629  ? -14.719  88.165  66.295  1.00 136.42 ? 629  LYS B N   1 
ATOM   19202 C  CA  . LYS C 1 629  ? -15.965  88.401  67.007  1.00 133.69 ? 629  LYS B CA  1 
ATOM   19203 C  C   . LYS C 1 629  ? -15.676  89.423  68.124  1.00 132.20 ? 629  LYS B C   1 
ATOM   19204 O  O   . LYS C 1 629  ? -16.516  89.750  68.971  1.00 128.61 ? 629  LYS B O   1 
ATOM   19205 C  CB  . LYS C 1 629  ? -16.563  87.087  67.495  1.00 132.44 ? 629  LYS B CB  1 
ATOM   19206 C  CG  . LYS C 1 629  ? -16.681  86.049  66.364  1.00 131.67 ? 629  LYS B CG  1 
ATOM   19207 C  CD  . LYS C 1 629  ? -17.045  86.681  64.988  1.00 155.34 ? 629  LYS B CD  1 
ATOM   19208 C  CE  . LYS C 1 629  ? -17.330  85.621  63.893  1.00 138.72 ? 629  LYS B CE  1 
ATOM   19209 N  NZ  . LYS C 1 629  ? -17.498  86.205  62.531  1.00 137.76 ? 629  LYS B NZ  1 
ATOM   19210 N  N   . SER C 1 630  ? -14.455  89.935  68.090  1.00 133.93 ? 630  SER B N   1 
ATOM   19211 C  CA  . SER C 1 630  ? -14.081  91.071  68.884  1.00 134.70 ? 630  SER B CA  1 
ATOM   19212 C  C   . SER C 1 630  ? -14.546  92.308  68.148  1.00 137.89 ? 630  SER B C   1 
ATOM   19213 O  O   . SER C 1 630  ? -14.269  93.426  68.571  1.00 144.33 ? 630  SER B O   1 
ATOM   19214 C  CB  . SER C 1 630  ? -12.580  91.102  69.043  1.00 133.34 ? 630  SER B CB  1 
ATOM   19215 O  OG  . SER C 1 630  ? -11.967  91.053  67.786  1.00 130.47 ? 630  SER B OG  1 
ATOM   19216 N  N   . ASP C 1 631  ? -15.220  92.108  67.019  1.00 134.20 ? 631  ASP B N   1 
ATOM   19217 C  CA  . ASP C 1 631  ? -15.919  93.207  66.354  1.00 135.87 ? 631  ASP B CA  1 
ATOM   19218 C  C   . ASP C 1 631  ? -17.138  93.499  67.213  1.00 135.43 ? 631  ASP B C   1 
ATOM   19219 O  O   . ASP C 1 631  ? -18.120  92.744  67.214  1.00 132.71 ? 631  ASP B O   1 
ATOM   19220 C  CB  . ASP C 1 631  ? -16.310  92.861  64.894  1.00 135.02 ? 631  ASP B CB  1 
ATOM   19221 C  CG  . ASP C 1 631  ? -16.816  94.088  64.087  1.00 158.75 ? 631  ASP B CG  1 
ATOM   19222 O  OD1 . ASP C 1 631  ? -18.001  94.451  64.255  1.00 158.32 ? 631  ASP B OD1 1 
ATOM   19223 O  OD2 . ASP C 1 631  ? -16.045  94.665  63.270  1.00 160.72 ? 631  ASP B OD2 1 
ATOM   19224 N  N   . LEU C 1 632  ? -17.040  94.594  67.963  1.00 139.20 ? 632  LEU B N   1 
ATOM   19225 C  CA  . LEU C 1 632  ? -18.060  94.982  68.923  1.00 139.43 ? 632  LEU B CA  1 
ATOM   19226 C  C   . LEU C 1 632  ? -19.364  95.306  68.197  1.00 135.22 ? 632  LEU B C   1 
ATOM   19227 O  O   . LEU C 1 632  ? -20.443  94.879  68.625  1.00 136.03 ? 632  LEU B O   1 
ATOM   19228 C  CB  . LEU C 1 632  ? -17.572  96.178  69.742  1.00 142.29 ? 632  LEU B CB  1 
ATOM   19229 C  CG  . LEU C 1 632  ? -16.076  96.177  70.083  1.00 142.91 ? 632  LEU B CG  1 
ATOM   19230 C  CD1 . LEU C 1 632  ? -15.561  97.576  70.474  1.00 144.66 ? 632  LEU B CD1 1 
ATOM   19231 C  CD2 . LEU C 1 632  ? -15.768  95.142  71.160  1.00 143.09 ? 632  LEU B CD2 1 
ATOM   19232 N  N   . GLY C 1 633  ? -19.243  96.035  67.083  1.00 132.26 ? 633  GLY B N   1 
ATOM   19233 C  CA  . GLY C 1 633  ? -20.377  96.485  66.281  1.00 125.65 ? 633  GLY B CA  1 
ATOM   19234 C  C   . GLY C 1 633  ? -21.392  95.438  65.835  1.00 121.37 ? 633  GLY B C   1 
ATOM   19235 O  O   . GLY C 1 633  ? -21.547  94.397  66.471  1.00 118.20 ? 633  GLY B O   1 
ATOM   19236 N  N   . CYS C 1 634  ? -22.095  95.721  64.746  1.00 117.52 ? 634  CYS B N   1 
ATOM   19237 C  CA  . CYS C 1 634  ? -23.118  94.818  64.252  1.00 117.02 ? 634  CYS B CA  1 
ATOM   19238 C  C   . CYS C 1 634  ? -23.802  95.392  63.014  1.00 119.66 ? 634  CYS B C   1 
ATOM   19239 O  O   . CYS C 1 634  ? -23.811  96.612  62.810  1.00 124.31 ? 634  CYS B O   1 
ATOM   19240 C  CB  . CYS C 1 634  ? -24.159  94.573  65.338  1.00 117.54 ? 634  CYS B CB  1 
ATOM   19241 S  SG  . CYS C 1 634  ? -25.310  93.252  64.946  1.00 151.74 ? 634  CYS B SG  1 
ATOM   19242 N  N   . GLY C 1 635  ? -24.382  94.518  62.189  1.00 115.34 ? 635  GLY B N   1 
ATOM   19243 C  CA  . GLY C 1 635  ? -25.126  94.953  61.009  1.00 113.49 ? 635  GLY B CA  1 
ATOM   19244 C  C   . GLY C 1 635  ? -24.327  95.282  59.743  1.00 115.27 ? 635  GLY B C   1 
ATOM   19245 O  O   . GLY C 1 635  ? -23.096  95.160  59.720  1.00 114.11 ? 635  GLY B O   1 
ATOM   19246 N  N   . ALA C 1 636  ? -25.036  95.680  58.683  1.00 116.10 ? 636  ALA B N   1 
ATOM   19247 C  CA  . ALA C 1 636  ? -24.422  96.007  57.402  1.00 118.30 ? 636  ALA B CA  1 
ATOM   19248 C  C   . ALA C 1 636  ? -23.928  97.412  57.490  1.00 116.46 ? 636  ALA B C   1 
ATOM   19249 O  O   . ALA C 1 636  ? -23.082  97.842  56.711  1.00 118.09 ? 636  ALA B O   1 
ATOM   19250 C  CB  . ALA C 1 636  ? -25.424  95.884  56.300  1.00 120.20 ? 636  ALA B CB  1 
ATOM   19251 N  N   . GLY C 1 637  ? -24.498  98.116  58.459  1.00 116.45 ? 637  GLY B N   1 
ATOM   19252 C  CA  . GLY C 1 637  ? -24.091  99.462  58.807  1.00 120.80 ? 637  GLY B CA  1 
ATOM   19253 C  C   . GLY C 1 637  ? -25.284  100.268 59.282  1.00 124.88 ? 637  GLY B C   1 
ATOM   19254 O  O   . GLY C 1 637  ? -26.401  99.735  59.393  1.00 122.71 ? 637  GLY B O   1 
ATOM   19255 N  N   . GLY C 1 638  ? -25.033  101.543 59.576  1.00 132.39 ? 638  GLY B N   1 
ATOM   19256 C  CA  . GLY C 1 638  ? -26.079  102.528 59.776  1.00 134.58 ? 638  GLY B CA  1 
ATOM   19257 C  C   . GLY C 1 638  ? -27.036  102.259 60.912  1.00 132.96 ? 638  GLY B C   1 
ATOM   19258 O  O   . GLY C 1 638  ? -27.623  101.189 61.026  1.00 134.61 ? 638  GLY B O   1 
ATOM   19259 N  N   . GLY C 1 639  ? -27.200  103.262 61.759  1.00 130.88 ? 639  GLY B N   1 
ATOM   19260 C  CA  . GLY C 1 639  ? -28.112  103.155 62.882  1.00 127.40 ? 639  GLY B CA  1 
ATOM   19261 C  C   . GLY C 1 639  ? -29.554  103.582 62.630  1.00 129.16 ? 639  GLY B C   1 
ATOM   19262 O  O   . GLY C 1 639  ? -30.194  103.126 61.672  1.00 126.73 ? 639  GLY B O   1 
ATOM   19263 N  N   . LEU C 1 640  ? -30.041  104.492 63.483  1.00 130.95 ? 640  LEU B N   1 
ATOM   19264 C  CA  . LEU C 1 640  ? -31.467  104.775 63.643  1.00 129.90 ? 640  LEU B CA  1 
ATOM   19265 C  C   . LEU C 1 640  ? -31.630  106.130 64.362  1.00 131.38 ? 640  LEU B C   1 
ATOM   19266 O  O   . LEU C 1 640  ? -32.619  106.845 64.195  1.00 130.49 ? 640  LEU B O   1 
ATOM   19267 C  CB  . LEU C 1 640  ? -32.057  103.617 64.446  1.00 120.22 ? 640  LEU B CB  1 
ATOM   19268 C  CG  . LEU C 1 640  ? -33.514  103.462 64.830  1.00 100.44 ? 640  LEU B CG  1 
ATOM   19269 C  CD1 . LEU C 1 640  ? -34.413  104.444 64.054  1.00 94.52  ? 640  LEU B CD1 1 
ATOM   19270 C  CD2 . LEU C 1 640  ? -33.895  102.001 64.651  1.00 85.73  ? 640  LEU B CD2 1 
ATOM   19271 N  N   . ASN C 1 641  ? -30.614  106.437 65.162  1.00 131.31 ? 641  ASN B N   1 
ATOM   19272 C  CA  . ASN C 1 641  ? -30.358  107.726 65.768  1.00 133.34 ? 641  ASN B CA  1 
ATOM   19273 C  C   . ASN C 1 641  ? -28.879  107.858 65.540  1.00 134.90 ? 641  ASN B C   1 
ATOM   19274 O  O   . ASN C 1 641  ? -28.217  106.858 65.313  1.00 135.04 ? 641  ASN B O   1 
ATOM   19275 C  CB  . ASN C 1 641  ? -30.536  107.680 67.285  1.00 135.47 ? 641  ASN B CB  1 
ATOM   19276 C  CG  . ASN C 1 641  ? -31.731  106.850 67.723  1.00 137.81 ? 641  ASN B CG  1 
ATOM   19277 O  OD1 . ASN C 1 641  ? -32.848  107.078 67.263  1.00 138.81 ? 641  ASN B OD1 1 
ATOM   19278 N  ND2 . ASN C 1 641  ? -31.506  105.893 68.643  1.00 138.82 ? 641  ASN B ND2 1 
ATOM   19279 N  N   . ASN C 1 642  ? -28.337  109.063 65.628  1.00 138.75 ? 642  ASN B N   1 
ATOM   19280 C  CA  . ASN C 1 642  ? -26.892  109.222 65.567  1.00 140.44 ? 642  ASN B CA  1 
ATOM   19281 C  C   . ASN C 1 642  ? -26.302  108.387 66.691  1.00 137.66 ? 642  ASN B C   1 
ATOM   19282 O  O   . ASN C 1 642  ? -25.141  107.971 66.658  1.00 134.50 ? 642  ASN B O   1 
ATOM   19283 C  CB  . ASN C 1 642  ? -26.504  110.691 65.733  1.00 147.91 ? 642  ASN B CB  1 
ATOM   19284 C  CG  . ASN C 1 642  ? -25.006  110.894 65.795  1.00 153.86 ? 642  ASN B CG  1 
ATOM   19285 O  OD1 . ASN C 1 642  ? -24.506  111.700 66.575  1.00 158.26 ? 642  ASN B OD1 1 
ATOM   19286 N  ND2 . ASN C 1 642  ? -24.280  110.149 64.980  1.00 153.87 ? 642  ASN B ND2 1 
ATOM   19287 N  N   . ALA C 1 643  ? -27.122  108.147 67.700  1.00 139.02 ? 643  ALA B N   1 
ATOM   19288 C  CA  . ALA C 1 643  ? -26.739  107.212 68.723  1.00 140.95 ? 643  ALA B CA  1 
ATOM   19289 C  C   . ALA C 1 643  ? -26.617  105.842 68.072  1.00 132.16 ? 643  ALA B C   1 
ATOM   19290 O  O   . ALA C 1 643  ? -25.519  105.414 67.714  1.00 128.89 ? 643  ALA B O   1 
ATOM   19291 C  CB  . ALA C 1 643  ? -27.769  107.201 69.829  1.00 145.83 ? 643  ALA B CB  1 
ATOM   19292 N  N   . ASN C 1 644  ? -27.760  105.182 67.900  1.00 129.86 ? 644  ASN B N   1 
ATOM   19293 C  CA  . ASN C 1 644  ? -27.820  103.868 67.277  1.00 126.89 ? 644  ASN B CA  1 
ATOM   19294 C  C   . ASN C 1 644  ? -26.670  103.718 66.282  1.00 129.36 ? 644  ASN B C   1 
ATOM   19295 O  O   . ASN C 1 644  ? -25.796  102.880 66.483  1.00 132.39 ? 644  ASN B O   1 
ATOM   19296 C  CB  . ASN C 1 644  ? -29.178  103.658 66.582  1.00 123.72 ? 644  ASN B CB  1 
ATOM   19297 C  CG  . ASN C 1 644  ? -29.605  102.181 66.517  1.00 121.67 ? 644  ASN B CG  1 
ATOM   19298 O  OD1 . ASN C 1 644  ? -30.686  101.848 65.999  1.00 119.49 ? 644  ASN B OD1 1 
ATOM   19299 N  ND2 . ASN C 1 644  ? -28.760  101.292 67.046  1.00 122.12 ? 644  ASN B ND2 1 
ATOM   19300 N  N   . VAL C 1 645  ? -26.652  104.553 65.238  1.00 128.88 ? 645  VAL B N   1 
ATOM   19301 C  CA  . VAL C 1 645  ? -25.571  104.564 64.237  1.00 129.50 ? 645  VAL B CA  1 
ATOM   19302 C  C   . VAL C 1 645  ? -24.197  104.360 64.869  1.00 130.46 ? 645  VAL B C   1 
ATOM   19303 O  O   . VAL C 1 645  ? -23.451  103.464 64.461  1.00 129.74 ? 645  VAL B O   1 
ATOM   19304 C  CB  . VAL C 1 645  ? -25.497  105.904 63.474  1.00 132.34 ? 645  VAL B CB  1 
ATOM   19305 C  CG1 . VAL C 1 645  ? -24.298  105.910 62.543  1.00 133.92 ? 645  VAL B CG1 1 
ATOM   19306 C  CG2 . VAL C 1 645  ? -26.780  106.177 62.715  1.00 131.49 ? 645  VAL B CG2 1 
ATOM   19307 N  N   . PHE C 1 646  ? -23.864  105.200 65.849  1.00 130.50 ? 646  PHE B N   1 
ATOM   19308 C  CA  . PHE C 1 646  ? -22.617  105.075 66.577  1.00 129.92 ? 646  PHE B CA  1 
ATOM   19309 C  C   . PHE C 1 646  ? -22.574  103.777 67.362  1.00 129.58 ? 646  PHE B C   1 
ATOM   19310 O  O   . PHE C 1 646  ? -21.519  103.157 67.481  1.00 130.25 ? 646  PHE B O   1 
ATOM   19311 C  CB  . PHE C 1 646  ? -22.453  106.253 67.524  1.00 129.23 ? 646  PHE B CB  1 
ATOM   19312 C  CG  . PHE C 1 646  ? -21.527  107.311 67.015  1.00 125.90 ? 646  PHE B CG  1 
ATOM   19313 C  CD1 . PHE C 1 646  ? -22.008  108.542 66.624  1.00 124.55 ? 646  PHE B CD1 1 
ATOM   19314 C  CD2 . PHE C 1 646  ? -20.169  107.067 66.915  1.00 125.08 ? 646  PHE B CD2 1 
ATOM   19315 C  CE1 . PHE C 1 646  ? -21.146  109.509 66.146  1.00 124.13 ? 646  PHE B CE1 1 
ATOM   19316 C  CE2 . PHE C 1 646  ? -19.302  108.041 66.436  1.00 124.63 ? 646  PHE B CE2 1 
ATOM   19317 C  CZ  . PHE C 1 646  ? -19.789  109.253 66.052  1.00 124.80 ? 646  PHE B CZ  1 
ATOM   19318 N  N   . HIS C 1 647  ? -23.724  103.371 67.895  1.00 131.19 ? 647  HIS B N   1 
ATOM   19319 C  CA  . HIS C 1 647  ? -23.826  102.146 68.695  1.00 132.14 ? 647  HIS B CA  1 
ATOM   19320 C  C   . HIS C 1 647  ? -23.388  100.915 67.897  1.00 122.36 ? 647  HIS B C   1 
ATOM   19321 O  O   . HIS C 1 647  ? -22.290  100.403 68.081  1.00 119.73 ? 647  HIS B O   1 
ATOM   19322 C  CB  . HIS C 1 647  ? -25.265  101.950 69.209  1.00 142.31 ? 647  HIS B CB  1 
ATOM   19323 C  CG  . HIS C 1 647  ? -25.369  101.077 70.429  1.00 153.42 ? 647  HIS B CG  1 
ATOM   19324 N  ND1 . HIS C 1 647  ? -24.656  99.904  70.576  1.00 156.15 ? 647  HIS B ND1 1 
ATOM   19325 C  CD2 . HIS C 1 647  ? -26.123  101.198 71.550  1.00 158.95 ? 647  HIS B CD2 1 
ATOM   19326 C  CE1 . HIS C 1 647  ? -24.948  99.351  71.743  1.00 158.79 ? 647  HIS B CE1 1 
ATOM   19327 N  NE2 . HIS C 1 647  ? -25.839  100.114 72.351  1.00 160.82 ? 647  HIS B NE2 1 
ATOM   19328 N  N   . LEU C 1 648  ? -24.263  100.450 67.017  1.00 116.39 ? 648  LEU B N   1 
ATOM   19329 C  CA  . LEU C 1 648  ? -23.957  99.360  66.106  1.00 111.64 ? 648  LEU B CA  1 
ATOM   19330 C  C   . LEU C 1 648  ? -22.552  99.434  65.483  1.00 112.18 ? 648  LEU B C   1 
ATOM   19331 O  O   . LEU C 1 648  ? -21.999  98.412  65.055  1.00 109.91 ? 648  LEU B O   1 
ATOM   19332 C  CB  . LEU C 1 648  ? -25.012  99.332  65.008  1.00 108.98 ? 648  LEU B CB  1 
ATOM   19333 C  CG  . LEU C 1 648  ? -26.364  98.820  65.486  1.00 105.50 ? 648  LEU B CG  1 
ATOM   19334 C  CD1 . LEU C 1 648  ? -27.498  99.454  64.705  1.00 103.29 ? 648  LEU B CD1 1 
ATOM   19335 C  CD2 . LEU C 1 648  ? -26.388  97.305  65.343  1.00 102.86 ? 648  LEU B CD2 1 
ATOM   19336 N  N   . ALA C 1 649  ? -21.982  100.631 65.423  1.00 110.71 ? 649  ALA B N   1 
ATOM   19337 C  CA  . ALA C 1 649  ? -20.613  100.783 64.975  1.00 109.90 ? 649  ALA B CA  1 
ATOM   19338 C  C   . ALA C 1 649  ? -19.666  100.059 65.901  1.00 106.69 ? 649  ALA B C   1 
ATOM   19339 O  O   . ALA C 1 649  ? -18.547  99.766  65.527  1.00 104.39 ? 649  ALA B O   1 
ATOM   19340 C  CB  . ALA C 1 649  ? -20.260  102.221 64.963  1.00 114.58 ? 649  ALA B CB  1 
ATOM   19341 N  N   . GLY C 1 650  ? -20.125  99.787  67.117  1.00 108.33 ? 650  GLY B N   1 
ATOM   19342 C  CA  . GLY C 1 650  ? -19.278  99.248  68.171  1.00 111.08 ? 650  GLY B CA  1 
ATOM   19343 C  C   . GLY C 1 650  ? -18.822  100.304 69.177  1.00 113.43 ? 650  GLY B C   1 
ATOM   19344 O  O   . GLY C 1 650  ? -18.036  100.036 70.108  1.00 113.54 ? 650  GLY B O   1 
ATOM   19345 N  N   . LEU C 1 651  ? -19.328  101.516 68.980  1.00 117.02 ? 651  LEU B N   1 
ATOM   19346 C  CA  . LEU C 1 651  ? -18.884  102.668 69.747  1.00 121.92 ? 651  LEU B CA  1 
ATOM   19347 C  C   . LEU C 1 651  ? -19.930  103.195 70.724  1.00 125.08 ? 651  LEU B C   1 
ATOM   19348 O  O   . LEU C 1 651  ? -21.140  103.035 70.523  1.00 124.14 ? 651  LEU B O   1 
ATOM   19349 C  CB  . LEU C 1 651  ? -18.499  103.803 68.787  1.00 122.33 ? 651  LEU B CB  1 
ATOM   19350 C  CG  . LEU C 1 651  ? -17.257  103.578 67.923  1.00 121.08 ? 651  LEU B CG  1 
ATOM   19351 C  CD1 . LEU C 1 651  ? -17.140  104.651 66.886  1.00 121.68 ? 651  LEU B CD1 1 
ATOM   19352 C  CD2 . LEU C 1 651  ? -16.015  103.554 68.775  1.00 123.88 ? 651  LEU B CD2 1 
ATOM   19353 N  N   . THR C 1 652  ? -19.456  103.824 71.791  1.00 127.71 ? 652  THR B N   1 
ATOM   19354 C  CA  . THR C 1 652  ? -20.229  104.912 72.366  1.00 127.54 ? 652  THR B CA  1 
ATOM   19355 C  C   . THR C 1 652  ? -19.312  106.133 72.519  1.00 128.60 ? 652  THR B C   1 
ATOM   19356 O  O   . THR C 1 652  ? -18.097  106.018 72.726  1.00 126.97 ? 652  THR B O   1 
ATOM   19357 C  CB  . THR C 1 652  ? -21.077  104.524 73.605  1.00 125.91 ? 652  THR B CB  1 
ATOM   19358 O  OG1 . THR C 1 652  ? -22.262  105.330 73.626  1.00 126.24 ? 652  THR B OG1 1 
ATOM   19359 C  CG2 . THR C 1 652  ? -20.308  104.714 74.887  1.00 128.95 ? 652  THR B CG2 1 
ATOM   19360 N  N   . PHE C 1 653  ? -19.889  107.302 72.314  1.00 128.52 ? 653  PHE B N   1 
ATOM   19361 C  CA  . PHE C 1 653  ? -19.071  108.450 72.057  1.00 133.83 ? 653  PHE B CA  1 
ATOM   19362 C  C   . PHE C 1 653  ? -19.311  109.474 73.110  1.00 140.10 ? 653  PHE B C   1 
ATOM   19363 O  O   . PHE C 1 653  ? -20.204  109.326 73.928  1.00 137.08 ? 653  PHE B O   1 
ATOM   19364 C  CB  . PHE C 1 653  ? -19.394  109.021 70.692  1.00 135.92 ? 653  PHE B CB  1 
ATOM   19365 C  CG  . PHE C 1 653  ? -20.844  109.403 70.511  1.00 139.65 ? 653  PHE B CG  1 
ATOM   19366 C  CD1 . PHE C 1 653  ? -21.202  110.727 70.247  1.00 143.29 ? 653  PHE B CD1 1 
ATOM   19367 C  CD2 . PHE C 1 653  ? -21.851  108.443 70.574  1.00 138.17 ? 653  PHE B CD2 1 
ATOM   19368 C  CE1 . PHE C 1 653  ? -22.537  111.084 70.054  1.00 142.74 ? 653  PHE B CE1 1 
ATOM   19369 C  CE2 . PHE C 1 653  ? -23.191  108.793 70.383  1.00 137.80 ? 653  PHE B CE2 1 
ATOM   19370 C  CZ  . PHE C 1 653  ? -23.534  110.110 70.121  1.00 139.92 ? 653  PHE B CZ  1 
ATOM   19371 N  N   . LEU C 1 654  ? -18.534  110.545 73.038  1.00 149.42 ? 654  LEU B N   1 
ATOM   19372 C  CA  . LEU C 1 654  ? -18.404  111.496 74.114  1.00 157.86 ? 654  LEU B CA  1 
ATOM   19373 C  C   . LEU C 1 654  ? -18.494  112.891 73.566  1.00 168.61 ? 654  LEU B C   1 
ATOM   19374 O  O   . LEU C 1 654  ? -17.464  113.515 73.349  1.00 176.28 ? 654  LEU B O   1 
ATOM   19375 C  CB  . LEU C 1 654  ? -17.021  111.336 74.679  1.00 154.64 ? 654  LEU B CB  1 
ATOM   19376 C  CG  . LEU C 1 654  ? -17.015  111.636 76.141  1.00 155.09 ? 654  LEU B CG  1 
ATOM   19377 C  CD1 . LEU C 1 654  ? -18.429  111.439 76.654  1.00 152.44 ? 654  LEU B CD1 1 
ATOM   19378 C  CD2 . LEU C 1 654  ? -16.055  110.662 76.744  1.00 155.27 ? 654  LEU B CD2 1 
ATOM   19379 N  N   . THR C 1 655  ? -19.715  113.389 73.369  1.00 172.63 ? 655  THR B N   1 
ATOM   19380 C  CA  . THR C 1 655  ? -19.951  114.628 72.605  1.00 178.96 ? 655  THR B CA  1 
ATOM   19381 C  C   . THR C 1 655  ? -21.135  115.451 73.117  1.00 187.66 ? 655  THR B C   1 
ATOM   19382 O  O   . THR C 1 655  ? -22.295  115.111 72.874  1.00 184.04 ? 655  THR B O   1 
ATOM   19383 C  CB  . THR C 1 655  ? -20.249  114.312 71.113  1.00 201.74 ? 655  THR B CB  1 
ATOM   19384 O  OG1 . THR C 1 655  ? -19.079  113.786 70.471  1.00 199.50 ? 655  THR B OG1 1 
ATOM   19385 C  CG2 . THR C 1 655  ? -20.727  115.566 70.379  1.00 203.06 ? 655  THR B CG2 1 
ATOM   19386 N  N   . ASN C 1 656  ? -20.861  116.551 73.799  1.00 201.61 ? 656  ASN B N   1 
ATOM   19387 C  CA  . ASN C 1 656  ? -21.979  117.304 74.326  1.00 212.15 ? 656  ASN B CA  1 
ATOM   19388 C  C   . ASN C 1 656  ? -22.681  118.116 73.258  1.00 213.42 ? 656  ASN B C   1 
ATOM   19389 O  O   . ASN C 1 656  ? -22.175  119.126 72.763  1.00 216.42 ? 656  ASN B O   1 
ATOM   19390 C  CB  . ASN C 1 656  ? -21.619  118.109 75.576  1.00 221.34 ? 656  ASN B CB  1 
ATOM   19391 C  CG  . ASN C 1 656  ? -21.714  117.271 76.858  1.00 220.76 ? 656  ASN B CG  1 
ATOM   19392 O  OD1 . ASN C 1 656  ? -21.247  117.689 77.921  1.00 224.02 ? 656  ASN B OD1 1 
ATOM   19393 N  ND2 . ASN C 1 656  ? -22.323  116.086 76.756  1.00 215.35 ? 656  ASN B ND2 1 
ATOM   19394 N  N   . ALA C 1 657  ? -23.859  117.608 72.917  1.00 209.67 ? 657  ALA B N   1 
ATOM   19395 C  CA  . ALA C 1 657  ? -24.719  118.117 71.866  1.00 207.08 ? 657  ALA B CA  1 
ATOM   19396 C  C   . ALA C 1 657  ? -25.808  117.068 71.711  1.00 203.78 ? 657  ALA B C   1 
ATOM   19397 O  O   . ALA C 1 657  ? -26.951  117.260 72.141  1.00 203.62 ? 657  ALA B O   1 
ATOM   19398 C  CB  . ALA C 1 657  ? -23.945  118.264 70.562  1.00 204.75 ? 657  ALA B CB  1 
ATOM   19399 N  N   . ASN C 1 658  ? -25.433  115.942 71.113  1.00 199.82 ? 658  ASN B N   1 
ATOM   19400 C  CA  . ASN C 1 658  ? -26.332  114.806 70.995  1.00 195.39 ? 658  ASN B CA  1 
ATOM   19401 C  C   . ASN C 1 658  ? -26.196  113.824 72.143  1.00 193.89 ? 658  ASN B C   1 
ATOM   19402 O  O   . ASN C 1 658  ? -25.105  113.611 72.671  1.00 193.82 ? 658  ASN B O   1 
ATOM   19403 C  CB  . ASN C 1 658  ? -26.108  114.081 69.674  1.00 191.14 ? 658  ASN B CB  1 
ATOM   19404 C  CG  . ASN C 1 658  ? -26.977  114.616 68.579  1.00 186.76 ? 658  ASN B CG  1 
ATOM   19405 O  OD1 . ASN C 1 658  ? -27.143  113.983 67.537  1.00 182.81 ? 658  ASN B OD1 1 
ATOM   19406 N  ND2 . ASN C 1 658  ? -27.556  115.788 68.809  1.00 187.38 ? 658  ASN B ND2 1 
ATOM   19407 N  N   . ALA C 1 659  ? -27.316  113.222 72.518  1.00 190.78 ? 659  ALA B N   1 
ATOM   19408 C  CA  . ALA C 1 659  ? -27.299  112.194 73.533  1.00 190.20 ? 659  ALA B CA  1 
ATOM   19409 C  C   . ALA C 1 659  ? -26.399  111.069 73.057  1.00 187.26 ? 659  ALA B C   1 
ATOM   19410 O  O   . ALA C 1 659  ? -26.777  110.313 72.160  1.00 185.53 ? 659  ALA B O   1 
ATOM   19411 C  CB  . ALA C 1 659  ? -28.699  111.681 73.770  1.00 189.44 ? 659  ALA B CB  1 
ATOM   19412 N  N   . ASP C 1 660  ? -25.208  110.958 73.647  1.00 187.05 ? 660  ASP B N   1 
ATOM   19413 C  CA  . ASP C 1 660  ? -24.275  109.878 73.283  1.00 184.51 ? 660  ASP B CA  1 
ATOM   19414 C  C   . ASP C 1 660  ? -24.745  108.491 73.741  1.00 180.18 ? 660  ASP B C   1 
ATOM   19415 O  O   . ASP C 1 660  ? -24.021  107.495 73.615  1.00 175.92 ? 660  ASP B O   1 
ATOM   19416 C  CB  . ASP C 1 660  ? -22.827  110.178 73.730  1.00 188.80 ? 660  ASP B CB  1 
ATOM   19417 C  CG  . ASP C 1 660  ? -22.719  110.586 75.192  1.00 195.39 ? 660  ASP B CG  1 
ATOM   19418 O  OD1 . ASP C 1 660  ? -23.296  109.888 76.054  1.00 196.61 ? 660  ASP B OD1 1 
ATOM   19419 O  OD2 . ASP C 1 660  ? -22.025  111.589 75.480  1.00 199.81 ? 660  ASP B OD2 1 
ATOM   19420 N  N   . ASP C 1 661  ? -25.987  108.460 74.223  1.00 181.38 ? 661  ASP B N   1 
ATOM   19421 C  CA  . ASP C 1 661  ? -26.593  107.316 74.890  1.00 178.82 ? 661  ASP B CA  1 
ATOM   19422 C  C   . ASP C 1 661  ? -26.520  105.997 74.108  1.00 177.91 ? 661  ASP B C   1 
ATOM   19423 O  O   . ASP C 1 661  ? -26.046  105.952 72.972  1.00 177.38 ? 661  ASP B O   1 
ATOM   19424 C  CB  . ASP C 1 661  ? -28.042  107.643 75.239  1.00 172.70 ? 661  ASP B CB  1 
ATOM   19425 C  CG  . ASP C 1 661  ? -29.004  107.203 74.164  1.00 161.64 ? 661  ASP B CG  1 
ATOM   19426 O  OD1 . ASP C 1 661  ? -29.393  108.026 73.306  1.00 156.25 ? 661  ASP B OD1 1 
ATOM   19427 O  OD2 . ASP C 1 661  ? -29.360  106.011 74.176  1.00 158.10 ? 661  ASP B OD2 1 
ATOM   19428 N  N   . SER C 1 662  ? -26.998  104.928 74.742  1.00 178.53 ? 662  SER B N   1 
ATOM   19429 C  CA  . SER C 1 662  ? -26.823  103.567 74.242  1.00 178.75 ? 662  SER B CA  1 
ATOM   19430 C  C   . SER C 1 662  ? -27.882  102.659 74.857  1.00 181.69 ? 662  SER B C   1 
ATOM   19431 O  O   . SER C 1 662  ? -27.573  101.693 75.570  1.00 178.32 ? 662  SER B O   1 
ATOM   19432 C  CB  . SER C 1 662  ? -25.411  103.044 74.562  1.00 180.64 ? 662  SER B CB  1 
ATOM   19433 O  OG  . SER C 1 662  ? -25.315  102.486 75.872  1.00 182.75 ? 662  SER B OG  1 
ATOM   19434 N  N   . GLN C 1 663  ? -29.134  102.980 74.552  1.00 188.83 ? 663  GLN B N   1 
ATOM   19435 C  CA  . GLN C 1 663  ? -30.294  102.353 75.177  1.00 195.54 ? 663  GLN B CA  1 
ATOM   19436 C  C   . GLN C 1 663  ? -30.029  101.057 75.945  1.00 204.38 ? 663  GLN B C   1 
ATOM   19437 O  O   . GLN C 1 663  ? -29.889  99.990  75.364  1.00 202.18 ? 663  GLN B O   1 
ATOM   19438 C  CB  . GLN C 1 663  ? -31.407  102.158 74.151  1.00 187.82 ? 663  GLN B CB  1 
ATOM   19439 C  CG  . GLN C 1 663  ? -31.788  103.452 73.471  1.00 182.70 ? 663  GLN B CG  1 
ATOM   19440 C  CD  . GLN C 1 663  ? -31.977  104.590 74.462  1.00 180.88 ? 663  GLN B CD  1 
ATOM   19441 O  OE1 . GLN C 1 663  ? -32.198  104.358 75.647  1.00 180.81 ? 663  GLN B OE1 1 
ATOM   19442 N  NE2 . GLN C 1 663  ? -31.903  105.828 73.976  1.00 180.03 ? 663  GLN B NE2 1 
ATOM   19443 N  N   . GLU C 1 664  ? -29.960  101.203 77.267  1.00 217.73 ? 664  GLU B N   1 
ATOM   19444 C  CA  . GLU C 1 664  ? -29.887  100.115 78.260  1.00 228.50 ? 664  GLU B CA  1 
ATOM   19445 C  C   . GLU C 1 664  ? -29.153  98.831  77.874  1.00 235.81 ? 664  GLU B C   1 
ATOM   19446 O  O   . GLU C 1 664  ? -29.348  98.299  76.789  1.00 232.41 ? 664  GLU B O   1 
ATOM   19447 C  CB  . GLU C 1 664  ? -31.284  99.782  78.821  1.00 231.73 ? 664  GLU B CB  1 
ATOM   19448 C  CG  . GLU C 1 664  ? -32.344  99.419  77.787  1.00 231.98 ? 664  GLU B CG  1 
ATOM   19449 C  CD  . GLU C 1 664  ? -33.687  99.095  78.423  1.00 236.82 ? 664  GLU B CD  1 
ATOM   19450 O  OE1 . GLU C 1 664  ? -33.754  98.129  79.213  1.00 238.55 ? 664  GLU B OE1 1 
ATOM   19451 O  OE2 . GLU C 1 664  ? -34.674  99.805  78.126  1.00 238.87 ? 664  GLU B OE2 1 
ATOM   19452 N  N   . ASN C 1 665  ? -28.323  98.326  78.785  1.00 246.83 ? 665  ASN B N   1 
ATOM   19453 C  CA  . ASN C 1 665  ? -27.704  97.034  78.561  1.00 253.05 ? 665  ASN B CA  1 
ATOM   19454 C  C   . ASN C 1 665  ? -26.969  97.121  77.226  1.00 257.21 ? 665  ASN B C   1 
ATOM   19455 O  O   . ASN C 1 665  ? -26.559  98.217  76.832  1.00 259.95 ? 665  ASN B O   1 
ATOM   19456 C  CB  . ASN C 1 665  ? -28.809  95.978  78.544  1.00 252.36 ? 665  ASN B CB  1 
ATOM   19457 C  CG  . ASN C 1 665  ? -28.281  94.572  78.455  1.00 249.76 ? 665  ASN B CG  1 
ATOM   19458 O  OD1 . ASN C 1 665  ? -28.105  94.036  77.363  1.00 246.56 ? 665  ASN B OD1 1 
ATOM   19459 N  ND2 . ASN C 1 665  ? -28.059  93.948  79.605  1.00 250.92 ? 665  ASN B ND2 1 
ATOM   19460 N  N   . ASP C 1 666  ? -26.799  96.001  76.522  1.00 257.81 ? 666  ASP B N   1 
ATOM   19461 C  CA  . ASP C 1 666  ? -26.276  96.071  75.149  1.00 259.66 ? 666  ASP B CA  1 
ATOM   19462 C  C   . ASP C 1 666  ? -26.495  94.874  74.205  1.00 251.40 ? 666  ASP B C   1 
ATOM   19463 O  O   . ASP C 1 666  ? -25.832  93.847  74.311  1.00 249.72 ? 666  ASP B O   1 
ATOM   19464 C  CB  . ASP C 1 666  ? -24.799  96.511  75.129  1.00 269.15 ? 666  ASP B CB  1 
ATOM   19465 C  CG  . ASP C 1 666  ? -23.857  95.470  75.719  1.00 276.96 ? 666  ASP B CG  1 
ATOM   19466 O  OD1 . ASP C 1 666  ? -24.309  94.628  76.523  1.00 279.90 ? 666  ASP B OD1 1 
ATOM   19467 O  OD2 . ASP C 1 666  ? -22.654  95.504  75.381  1.00 280.01 ? 666  ASP B OD2 1 
ATOM   19468 N  N   . GLU C 1 667  ? -27.464  95.033  73.310  1.00 246.82 ? 667  GLU B N   1 
ATOM   19469 C  CA  . GLU C 1 667  ? -27.489  94.399  71.989  1.00 238.93 ? 667  GLU B CA  1 
ATOM   19470 C  C   . GLU C 1 667  ? -26.737  93.088  71.784  1.00 237.98 ? 667  GLU B C   1 
ATOM   19471 O  O   . GLU C 1 667  ? -25.704  93.089  71.116  1.00 238.02 ? 667  GLU B O   1 
ATOM   19472 C  CB  . GLU C 1 667  ? -26.878  95.390  70.999  1.00 231.94 ? 667  GLU B CB  1 
ATOM   19473 C  CG  . GLU C 1 667  ? -26.662  96.768  71.594  1.00 227.52 ? 667  GLU B CG  1 
ATOM   19474 C  CD  . GLU C 1 667  ? -27.968  97.470  71.881  1.00 222.45 ? 667  GLU B CD  1 
ATOM   19475 O  OE1 . GLU C 1 667  ? -28.990  96.776  72.048  1.00 219.68 ? 667  GLU B OE1 1 
ATOM   19476 O  OE2 . GLU C 1 667  ? -27.981  98.715  71.933  1.00 222.22 ? 667  GLU B OE2 1 
ATOM   19477 N  N   . PRO C 1 668  ? -27.265  91.964  72.295  1.00 236.02 ? 668  PRO B N   1 
ATOM   19478 C  CA  . PRO C 1 668  ? -26.586  90.678  72.051  1.00 233.53 ? 668  PRO B CA  1 
ATOM   19479 C  C   . PRO C 1 668  ? -26.496  90.259  70.564  1.00 231.45 ? 668  PRO B C   1 
ATOM   19480 O  O   . PRO C 1 668  ? -26.546  89.062  70.270  1.00 229.01 ? 668  PRO B O   1 
ATOM   19481 C  CB  . PRO C 1 668  ? -27.431  89.680  72.852  1.00 233.21 ? 668  PRO B CB  1 
ATOM   19482 C  CG  . PRO C 1 668  ? -28.090  90.509  73.920  1.00 235.34 ? 668  PRO B CG  1 
ATOM   19483 C  CD  . PRO C 1 668  ? -28.356  91.842  73.281  1.00 236.26 ? 668  PRO B CD  1 
ATOM   19484 N  N   . CYS C 1 669  ? -26.339  91.234  69.666  1.00 231.67 ? 669  CYS B N   1 
ATOM   19485 C  CA  . CYS C 1 669  ? -26.280  91.021  68.214  1.00 230.61 ? 669  CYS B CA  1 
ATOM   19486 C  C   . CYS C 1 669  ? -25.860  89.616  67.795  1.00 229.24 ? 669  CYS B C   1 
ATOM   19487 O  O   . CYS C 1 669  ? -25.012  88.992  68.431  1.00 229.45 ? 669  CYS B O   1 
ATOM   19488 C  CB  . CYS C 1 669  ? -25.354  92.056  67.560  1.00 231.71 ? 669  CYS B CB  1 
ATOM   19489 S  SG  . CYS C 1 669  ? -24.697  91.584  65.926  1.00 279.83 ? 669  CYS B SG  1 
ATOM   19490 N  N   . LYS C 1 670  ? -26.448  89.142  66.700  1.00 227.68 ? 670  LYS B N   1 
ATOM   19491 C  CA  . LYS C 1 670  ? -26.243  87.775  66.239  1.00 225.08 ? 670  LYS B CA  1 
ATOM   19492 C  C   . LYS C 1 670  ? -26.555  87.643  64.746  1.00 220.87 ? 670  LYS B C   1 
ATOM   19493 O  O   . LYS C 1 670  ? -27.716  87.551  64.356  1.00 219.34 ? 670  LYS B O   1 
ATOM   19494 C  CB  . LYS C 1 670  ? -27.131  86.823  67.050  1.00 226.44 ? 670  LYS B CB  1 
ATOM   19495 C  CG  . LYS C 1 670  ? -27.028  85.367  66.649  1.00 226.17 ? 670  LYS B CG  1 
ATOM   19496 C  CD  . LYS C 1 670  ? -25.622  84.842  66.864  1.00 227.23 ? 670  LYS B CD  1 
ATOM   19497 C  CE  . LYS C 1 670  ? -25.468  83.414  66.350  1.00 226.47 ? 670  LYS B CE  1 
ATOM   19498 N  NZ  . LYS C 1 670  ? -26.247  82.425  67.142  1.00 226.47 ? 670  LYS B NZ  1 
ATOM   19499 N  N   . GLU C 1 671  ? -25.513  87.657  63.919  1.00 216.73 ? 671  GLU B N   1 
ATOM   19500 C  CA  . GLU C 1 671  ? -25.629  87.341  62.486  1.00 210.80 ? 671  GLU B CA  1 
ATOM   19501 C  C   . GLU C 1 671  ? -26.602  88.190  61.632  1.00 195.76 ? 671  GLU B C   1 
ATOM   19502 O  O   . GLU C 1 671  ? -27.369  87.638  60.841  1.00 195.72 ? 671  GLU B O   1 
ATOM   19503 C  CB  . GLU C 1 671  ? -25.932  85.846  62.293  1.00 210.74 ? 671  GLU B CB  1 
ATOM   19504 C  CG  . GLU C 1 671  ? -24.891  84.898  62.906  1.00 210.63 ? 671  GLU B CG  1 
ATOM   19505 C  CD  . GLU C 1 671  ? -25.164  83.426  62.596  1.00 207.42 ? 671  GLU B CD  1 
ATOM   19506 O  OE1 . GLU C 1 671  ? -26.153  83.136  61.887  1.00 205.60 ? 671  GLU B OE1 1 
ATOM   19507 O  OE2 . GLU C 1 671  ? -24.385  82.563  63.060  1.00 206.70 ? 671  GLU B OE2 1 
ATOM   19508 N  N   . ILE C 1 672  ? -26.566  89.518  61.795  1.00 187.85 ? 672  ILE B N   1 
ATOM   19509 C  CA  . ILE C 1 672  ? -27.304  90.465  60.923  1.00 178.02 ? 672  ILE B CA  1 
ATOM   19510 C  C   . ILE C 1 672  ? -26.361  91.236  59.973  1.00 170.82 ? 672  ILE B C   1 
ATOM   19511 O  O   . ILE C 1 672  ? -26.799  91.825  58.988  1.00 168.66 ? 672  ILE B O   1 
ATOM   19512 C  CB  . ILE C 1 672  ? -28.170  91.496  61.744  1.00 198.13 ? 672  ILE B CB  1 
ATOM   19513 C  CG1 . ILE C 1 672  ? -29.450  91.903  60.996  1.00 196.43 ? 672  ILE B CG1 1 
ATOM   19514 C  CG2 . ILE C 1 672  ? -27.352  92.735  62.120  1.00 200.03 ? 672  ILE B CG2 1 
ATOM   19515 C  CD1 . ILE C 1 672  ? -30.226  93.039  61.671  1.00 197.57 ? 672  ILE B CD1 1 
ATOM   19516 N  N   . LEU C 1 673  ? -25.067  91.234  60.277  1.00 163.99 ? 673  LEU B N   1 
ATOM   19517 C  CA  . LEU C 1 673  ? -24.115  91.997  59.488  1.00 155.75 ? 673  LEU B CA  1 
ATOM   19518 C  C   . LEU C 1 673  ? -24.161  91.563  58.048  1.00 152.78 ? 673  LEU B C   1 
ATOM   19519 O  O   . LEU C 1 673  ? -23.279  91.908  57.281  1.00 152.51 ? 673  LEU B O   1 
ATOM   19520 C  CB  . LEU C 1 673  ? -22.698  91.830  60.021  1.00 149.18 ? 673  LEU B CB  1 
ATOM   19521 C  CG  . LEU C 1 673  ? -21.752  90.863  59.313  1.00 139.78 ? 673  LEU B CG  1 
ATOM   19522 C  CD1 . LEU C 1 673  ? -20.364  91.449  59.390  1.00 138.44 ? 673  LEU B CD1 1 
ATOM   19523 C  CD2 . LEU C 1 673  ? -21.792  89.434  59.877  1.00 136.03 ? 673  LEU B CD2 1 
ATOM   19524 N  N   . LEU C 1 679  ? -40.631  42.493  61.146  1.00 238.82 ? 679  LEU B N   1 
ATOM   19525 C  CA  . LEU C 1 679  ? -40.843  41.481  62.176  1.00 237.39 ? 679  LEU B CA  1 
ATOM   19526 C  C   . LEU C 1 679  ? -40.119  41.833  63.477  1.00 236.63 ? 679  LEU B C   1 
ATOM   19527 O  O   . LEU C 1 679  ? -40.514  41.385  64.553  1.00 236.26 ? 679  LEU B O   1 
ATOM   19528 C  CB  . LEU C 1 679  ? -40.423  40.101  61.665  1.00 236.07 ? 679  LEU B CB  1 
ATOM   19529 C  CG  . LEU C 1 679  ? -41.304  39.522  60.552  1.00 236.15 ? 679  LEU B CG  1 
ATOM   19530 C  CD1 . LEU C 1 679  ? -40.533  38.533  59.686  1.00 235.42 ? 679  LEU B CD1 1 
ATOM   19531 C  CD2 . LEU C 1 679  ? -42.572  38.886  61.127  1.00 235.98 ? 679  LEU B CD2 1 
ATOM   19532 N  N   . GLN C 1 680  ? -39.059  42.633  63.372  1.00 236.66 ? 680  GLN B N   1 
ATOM   19533 C  CA  . GLN C 1 680  ? -38.392  43.185  64.551  1.00 236.13 ? 680  GLN B CA  1 
ATOM   19534 C  C   . GLN C 1 680  ? -39.093  44.477  64.986  1.00 234.40 ? 680  GLN B C   1 
ATOM   19535 O  O   . GLN C 1 680  ? -38.866  44.979  66.085  1.00 233.95 ? 680  GLN B O   1 
ATOM   19536 C  CB  . GLN C 1 680  ? -36.895  43.428  64.286  1.00 238.22 ? 680  GLN B CB  1 
ATOM   19537 C  CG  . GLN C 1 680  ? -36.476  44.893  64.104  1.00 240.85 ? 680  GLN B CG  1 
ATOM   19538 C  CD  . GLN C 1 680  ? -36.961  45.506  62.802  1.00 243.23 ? 680  GLN B CD  1 
ATOM   19539 O  OE1 . GLN C 1 680  ? -37.500  44.818  61.942  1.00 244.25 ? 680  GLN B OE1 1 
ATOM   19540 N  NE2 . GLN C 1 680  ? -36.771  46.812  62.656  1.00 244.13 ? 680  GLN B NE2 1 
ATOM   19541 N  N   . LYS C 1 681  ? -39.949  45.004  64.112  1.00 232.92 ? 681  LYS B N   1 
ATOM   19542 C  CA  . LYS C 1 681  ? -40.742  46.195  64.410  1.00 230.11 ? 681  LYS B CA  1 
ATOM   19543 C  C   . LYS C 1 681  ? -41.843  45.853  65.411  1.00 229.87 ? 681  LYS B C   1 
ATOM   19544 O  O   . LYS C 1 681  ? -42.289  46.713  66.172  1.00 230.25 ? 681  LYS B O   1 
ATOM   19545 C  CB  . LYS C 1 681  ? -41.373  46.749  63.130  1.00 227.61 ? 681  LYS B CB  1 
ATOM   19546 C  CG  . LYS C 1 681  ? -40.556  46.509  61.868  1.00 224.25 ? 681  LYS B CG  1 
ATOM   19547 C  CD  . LYS C 1 681  ? -41.440  46.539  60.633  1.00 222.75 ? 681  LYS B CD  1 
ATOM   19548 C  CE  . LYS C 1 681  ? -40.733  45.921  59.450  1.00 221.56 ? 681  LYS B CE  1 
ATOM   19549 N  NZ  . LYS C 1 681  ? -41.636  45.821  58.283  1.00 222.78 ? 681  LYS B NZ  1 
ATOM   19550 N  N   . LYS C 1 682  ? -42.275  44.590  65.386  1.00 229.55 ? 682  LYS B N   1 
ATOM   19551 C  CA  . LYS C 1 682  ? -43.311  44.064  66.281  1.00 229.90 ? 682  LYS B CA  1 
ATOM   19552 C  C   . LYS C 1 682  ? -42.858  44.061  67.739  1.00 232.10 ? 682  LYS B C   1 
ATOM   19553 O  O   . LYS C 1 682  ? -43.676  44.120  68.660  1.00 230.89 ? 682  LYS B O   1 
ATOM   19554 C  CB  . LYS C 1 682  ? -43.713  42.645  65.851  1.00 227.41 ? 682  LYS B CB  1 
ATOM   19555 C  CG  . LYS C 1 682  ? -44.294  41.769  66.967  1.00 224.93 ? 682  LYS B CG  1 
ATOM   19556 C  CD  . LYS C 1 682  ? -45.698  42.204  67.379  1.00 224.07 ? 682  LYS B CD  1 
ATOM   19557 C  CE  . LYS C 1 682  ? -46.232  41.361  68.537  1.00 221.83 ? 682  LYS B CE  1 
ATOM   19558 N  NZ  . LYS C 1 682  ? -47.612  41.750  68.950  1.00 221.51 ? 682  LYS B NZ  1 
ATOM   19559 N  N   . ILE C 1 683  ? -41.551  43.970  67.946  1.00 236.08 ? 683  ILE B N   1 
ATOM   19560 C  CA  . ILE C 1 683  ? -41.002  44.111  69.283  1.00 239.63 ? 683  ILE B CA  1 
ATOM   19561 C  C   . ILE C 1 683  ? -40.786  45.600  69.580  1.00 243.87 ? 683  ILE B C   1 
ATOM   19562 O  O   . ILE C 1 683  ? -41.045  46.054  70.694  1.00 245.88 ? 683  ILE B O   1 
ATOM   19563 C  CB  . ILE C 1 683  ? -39.680  43.311  69.463  1.00 201.25 ? 683  ILE B CB  1 
ATOM   19564 C  CG1 . ILE C 1 683  ? -39.711  42.016  68.654  1.00 198.82 ? 683  ILE B CG1 1 
ATOM   19565 C  CG2 . ILE C 1 683  ? -39.435  42.994  70.928  1.00 201.46 ? 683  ILE B CG2 1 
ATOM   19566 C  CD1 . ILE C 1 683  ? -38.362  41.348  68.512  1.00 196.12 ? 683  ILE B CD1 1 
ATOM   19567 N  N   . GLU C 1 684  ? -40.347  46.359  68.570  1.00 245.87 ? 684  GLU B N   1 
ATOM   19568 C  CA  . GLU C 1 684  ? -39.947  47.767  68.749  1.00 247.81 ? 684  GLU B CA  1 
ATOM   19569 C  C   . GLU C 1 684  ? -41.095  48.694  69.153  1.00 245.65 ? 684  GLU B C   1 
ATOM   19570 O  O   . GLU C 1 684  ? -40.878  49.850  69.522  1.00 245.07 ? 684  GLU B O   1 
ATOM   19571 C  CB  . GLU C 1 684  ? -39.203  48.315  67.511  1.00 253.24 ? 684  GLU B CB  1 
ATOM   19572 C  CG  . GLU C 1 684  ? -37.722  47.889  67.432  1.00 257.07 ? 684  GLU B CG  1 
ATOM   19573 C  CD  . GLU C 1 684  ? -36.857  48.780  66.538  1.00 261.08 ? 684  GLU B CD  1 
ATOM   19574 O  OE1 . GLU C 1 684  ? -37.370  49.778  65.984  1.00 263.15 ? 684  GLU B OE1 1 
ATOM   19575 O  OE2 . GLU C 1 684  ? -35.650  48.476  66.397  1.00 261.81 ? 684  GLU B OE2 1 
ATOM   19576 N  N   . GLU C 1 685  ? -42.312  48.174  69.085  1.00 244.17 ? 685  GLU B N   1 
ATOM   19577 C  CA  . GLU C 1 685  ? -43.483  48.898  69.545  1.00 243.42 ? 685  GLU B CA  1 
ATOM   19578 C  C   . GLU C 1 685  ? -43.577  48.812  71.064  1.00 238.60 ? 685  GLU B C   1 
ATOM   19579 O  O   . GLU C 1 685  ? -44.130  49.693  71.718  1.00 239.01 ? 685  GLU B O   1 
ATOM   19580 C  CB  . GLU C 1 685  ? -44.727  48.285  68.916  1.00 245.53 ? 685  GLU B CB  1 
ATOM   19581 C  CG  . GLU C 1 685  ? -44.854  46.804  69.208  1.00 245.67 ? 685  GLU B CG  1 
ATOM   19582 C  CD  . GLU C 1 685  ? -45.762  46.094  68.233  1.00 247.32 ? 685  GLU B CD  1 
ATOM   19583 O  OE1 . GLU C 1 685  ? -46.115  46.702  67.196  1.00 248.62 ? 685  GLU B OE1 1 
ATOM   19584 O  OE2 . GLU C 1 685  ? -46.115  44.927  68.508  1.00 247.15 ? 685  GLU B OE2 1 
ATOM   19585 N  N   . ILE C 1 686  ? -43.026  47.736  71.613  1.00 233.71 ? 686  ILE B N   1 
ATOM   19586 C  CA  . ILE C 1 686  ? -43.052  47.487  73.054  1.00 229.15 ? 686  ILE B CA  1 
ATOM   19587 C  C   . ILE C 1 686  ? -42.026  48.338  73.839  1.00 225.23 ? 686  ILE B C   1 
ATOM   19588 O  O   . ILE C 1 686  ? -41.593  47.962  74.934  1.00 225.49 ? 686  ILE B O   1 
ATOM   19589 C  CB  . ILE C 1 686  ? -42.890  45.975  73.356  1.00 229.25 ? 686  ILE B CB  1 
ATOM   19590 C  CG1 . ILE C 1 686  ? -43.723  45.147  72.370  1.00 228.95 ? 686  ILE B CG1 1 
ATOM   19591 C  CG2 . ILE C 1 686  ? -43.289  45.656  74.791  1.00 228.88 ? 686  ILE B CG2 1 
ATOM   19592 C  CD1 . ILE C 1 686  ? -45.215  45.413  72.442  1.00 229.29 ? 686  ILE B CD1 1 
ATOM   19593 N  N   . ALA C 1 687  ? -41.633  49.473  73.254  1.00 220.43 ? 687  ALA B N   1 
ATOM   19594 C  CA  . ALA C 1 687  ? -40.974  50.555  73.989  1.00 214.24 ? 687  ALA B CA  1 
ATOM   19595 C  C   . ALA C 1 687  ? -42.085  51.268  74.743  1.00 209.99 ? 687  ALA B C   1 
ATOM   19596 O  O   . ALA C 1 687  ? -41.870  52.269  75.435  1.00 207.94 ? 687  ALA B O   1 
ATOM   19597 C  CB  . ALA C 1 687  ? -40.277  51.514  73.032  1.00 213.95 ? 687  ALA B CB  1 
ATOM   19598 N  N   . ALA C 1 688  ? -43.286  50.722  74.568  1.00 206.80 ? 688  ALA B N   1 
ATOM   19599 C  CA  . ALA C 1 688  ? -44.495  51.168  75.236  1.00 204.60 ? 688  ALA B CA  1 
ATOM   19600 C  C   . ALA C 1 688  ? -44.391  51.000  76.741  1.00 199.86 ? 688  ALA B C   1 
ATOM   19601 O  O   . ALA C 1 688  ? -45.243  51.480  77.483  1.00 199.27 ? 688  ALA B O   1 
ATOM   19602 C  CB  . ALA C 1 688  ? -45.691  50.400  74.704  1.00 203.83 ? 688  ALA B CB  1 
ATOM   19603 N  N   . LYS C 1 689  ? -43.364  50.289  77.189  1.00 199.49 ? 689  LYS B N   1 
ATOM   19604 C  CA  . LYS C 1 689  ? -43.088  50.222  78.618  1.00 198.98 ? 689  LYS B CA  1 
ATOM   19605 C  C   . LYS C 1 689  ? -41.886  51.069  79.007  1.00 206.49 ? 689  LYS B C   1 
ATOM   19606 O  O   . LYS C 1 689  ? -41.119  50.702  79.897  1.00 207.04 ? 689  LYS B O   1 
ATOM   19607 C  CB  . LYS C 1 689  ? -42.966  48.782  79.140  1.00 192.35 ? 689  LYS B CB  1 
ATOM   19608 C  CG  . LYS C 1 689  ? -41.881  47.924  78.526  1.00 186.37 ? 689  LYS B CG  1 
ATOM   19609 C  CD  . LYS C 1 689  ? -41.982  46.523  79.105  1.00 181.40 ? 689  LYS B CD  1 
ATOM   19610 C  CE  . LYS C 1 689  ? -43.389  45.963  78.924  1.00 178.68 ? 689  LYS B CE  1 
ATOM   19611 N  NZ  . LYS C 1 689  ? -43.749  44.922  79.928  1.00 176.08 ? 689  LYS B NZ  1 
ATOM   19612 N  N   . TYR C 1 690  ? -41.724  52.200  78.326  1.00 212.49 ? 690  TYR B N   1 
ATOM   19613 C  CA  . TYR C 1 690  ? -40.782  53.208  78.783  1.00 220.25 ? 690  TYR B CA  1 
ATOM   19614 C  C   . TYR C 1 690  ? -41.236  53.755  80.146  1.00 223.05 ? 690  TYR B C   1 
ATOM   19615 O  O   . TYR C 1 690  ? -42.425  53.968  80.392  1.00 222.48 ? 690  TYR B O   1 
ATOM   19616 C  CB  . TYR C 1 690  ? -40.621  54.328  77.750  1.00 227.40 ? 690  TYR B CB  1 
ATOM   19617 C  CG  . TYR C 1 690  ? -40.111  55.618  78.346  1.00 234.74 ? 690  TYR B CG  1 
ATOM   19618 C  CD1 . TYR C 1 690  ? -38.810  55.715  78.837  1.00 237.28 ? 690  TYR B CD1 1 
ATOM   19619 C  CD2 . TYR C 1 690  ? -40.934  56.739  78.428  1.00 239.02 ? 690  TYR B CD2 1 
ATOM   19620 C  CE1 . TYR C 1 690  ? -38.344  56.894  79.395  1.00 240.43 ? 690  TYR B CE1 1 
ATOM   19621 C  CE2 . TYR C 1 690  ? -40.480  57.923  78.981  1.00 242.05 ? 690  TYR B CE2 1 
ATOM   19622 C  CZ  . TYR C 1 690  ? -39.185  57.997  79.463  1.00 242.96 ? 690  TYR B CZ  1 
ATOM   19623 O  OH  . TYR C 1 690  ? -38.740  59.181  80.012  1.00 245.01 ? 690  TYR B OH  1 
ATOM   19624 N  N   . LYS C 1 691  ? -40.269  53.957  81.031  1.00 225.67 ? 691  LYS B N   1 
ATOM   19625 C  CA  . LYS C 1 691  ? -40.502  54.400  82.399  1.00 228.57 ? 691  LYS B CA  1 
ATOM   19626 C  C   . LYS C 1 691  ? -39.106  54.545  82.982  1.00 229.12 ? 691  LYS B C   1 
ATOM   19627 O  O   . LYS C 1 691  ? -38.912  54.699  84.192  1.00 230.77 ? 691  LYS B O   1 
ATOM   19628 C  CB  . LYS C 1 691  ? -41.326  53.371  83.180  1.00 226.86 ? 691  LYS B CB  1 
ATOM   19629 C  CG  . LYS C 1 691  ? -40.821  51.933  83.064  1.00 224.66 ? 691  LYS B CG  1 
ATOM   19630 C  CD  . LYS C 1 691  ? -41.786  50.942  83.700  1.00 222.36 ? 691  LYS B CD  1 
ATOM   19631 C  CE  . LYS C 1 691  ? -41.459  49.511  83.310  1.00 220.01 ? 691  LYS B CE  1 
ATOM   19632 N  NZ  . LYS C 1 691  ? -42.504  48.580  83.799  1.00 219.11 ? 691  LYS B NZ  1 
ATOM   19633 N  N   . HIS C 1 692  ? -38.141  54.478  82.067  1.00 229.01 ? 692  HIS B N   1 
ATOM   19634 C  CA  . HIS C 1 692  ? -36.717  54.591  82.350  1.00 228.36 ? 692  HIS B CA  1 
ATOM   19635 C  C   . HIS C 1 692  ? -35.964  54.049  81.134  1.00 222.19 ? 692  HIS B C   1 
ATOM   19636 O  O   . HIS C 1 692  ? -36.451  53.160  80.435  1.00 219.52 ? 692  HIS B O   1 
ATOM   19637 C  CB  . HIS C 1 692  ? -36.339  53.812  83.614  1.00 232.73 ? 692  HIS B CB  1 
ATOM   19638 C  CG  . HIS C 1 692  ? -35.012  54.201  84.189  1.00 239.32 ? 692  HIS B CG  1 
ATOM   19639 N  ND1 . HIS C 1 692  ? -34.716  55.493  84.571  1.00 243.08 ? 692  HIS B ND1 1 
ATOM   19640 C  CD2 . HIS C 1 692  ? -33.905  53.467  84.456  1.00 240.95 ? 692  HIS B CD2 1 
ATOM   19641 C  CE1 . HIS C 1 692  ? -33.481  55.538  85.040  1.00 245.20 ? 692  HIS B CE1 1 
ATOM   19642 N  NE2 . HIS C 1 692  ? -32.967  54.322  84.983  1.00 243.86 ? 692  HIS B NE2 1 
ATOM   19643 N  N   . SER C 1 693  ? -34.784  54.594  80.868  1.00 219.13 ? 693  SER B N   1 
ATOM   19644 C  CA  . SER C 1 693  ? -33.972  54.108  79.762  1.00 213.48 ? 693  SER B CA  1 
ATOM   19645 C  C   . SER C 1 693  ? -33.715  52.620  79.929  1.00 205.67 ? 693  SER B C   1 
ATOM   19646 O  O   . SER C 1 693  ? -34.026  51.821  79.046  1.00 204.25 ? 693  SER B O   1 
ATOM   19647 C  CB  . SER C 1 693  ? -32.636  54.858  79.712  1.00 214.54 ? 693  SER B CB  1 
ATOM   19648 O  OG  . SER C 1 693  ? -31.690  54.188  78.890  1.00 213.04 ? 693  SER B OG  1 
ATOM   19649 N  N   . VAL C 1 694  ? -33.173  52.272  81.095  1.00 200.12 ? 694  VAL B N   1 
ATOM   19650 C  CA  . VAL C 1 694  ? -32.637  50.936  81.385  1.00 194.44 ? 694  VAL B CA  1 
ATOM   19651 C  C   . VAL C 1 694  ? -33.636  49.806  81.094  1.00 189.57 ? 694  VAL B C   1 
ATOM   19652 O  O   . VAL C 1 694  ? -33.240  48.659  80.879  1.00 188.56 ? 694  VAL B O   1 
ATOM   19653 C  CB  . VAL C 1 694  ? -32.062  50.833  82.858  1.00 188.84 ? 694  VAL B CB  1 
ATOM   19654 C  CG1 . VAL C 1 694  ? -31.293  49.536  83.066  1.00 187.31 ? 694  VAL B CG1 1 
ATOM   19655 C  CG2 . VAL C 1 694  ? -31.151  52.019  83.187  1.00 190.29 ? 694  VAL B CG2 1 
ATOM   19656 N  N   . VAL C 1 695  ? -34.925  50.123  81.076  1.00 186.81 ? 695  VAL B N   1 
ATOM   19657 C  CA  . VAL C 1 695  ? -35.904  49.119  80.689  1.00 183.61 ? 695  VAL B CA  1 
ATOM   19658 C  C   . VAL C 1 695  ? -35.924  48.995  79.169  1.00 180.50 ? 695  VAL B C   1 
ATOM   19659 O  O   . VAL C 1 695  ? -36.097  47.894  78.643  1.00 178.53 ? 695  VAL B O   1 
ATOM   19660 C  CB  . VAL C 1 695  ? -37.307  49.408  81.260  1.00 184.20 ? 695  VAL B CB  1 
ATOM   19661 C  CG1 . VAL C 1 695  ? -38.275  48.297  80.895  1.00 183.53 ? 695  VAL B CG1 1 
ATOM   19662 C  CG2 . VAL C 1 695  ? -37.231  49.537  82.768  1.00 185.26 ? 695  VAL B CG2 1 
ATOM   19663 N  N   . LYS C 1 696  ? -35.724  50.107  78.462  1.00 179.08 ? 696  LYS B N   1 
ATOM   19664 C  CA  . LYS C 1 696  ? -35.608  50.034  77.009  1.00 177.94 ? 696  LYS B CA  1 
ATOM   19665 C  C   . LYS C 1 696  ? -34.554  48.997  76.666  1.00 175.91 ? 696  LYS B C   1 
ATOM   19666 O  O   . LYS C 1 696  ? -34.849  47.948  76.082  1.00 175.40 ? 696  LYS B O   1 
ATOM   19667 C  CB  . LYS C 1 696  ? -35.223  51.380  76.398  1.00 178.13 ? 696  LYS B CB  1 
ATOM   19668 C  CG  . LYS C 1 696  ? -34.703  51.268  74.948  1.00 178.44 ? 696  LYS B CG  1 
ATOM   19669 C  CD  . LYS C 1 696  ? -35.721  50.594  73.993  1.00 174.03 ? 696  LYS B CD  1 
ATOM   19670 C  CE  . LYS C 1 696  ? -35.234  50.561  72.525  1.00 173.04 ? 696  LYS B CE  1 
ATOM   19671 N  NZ  . LYS C 1 696  ? -36.179  49.887  71.561  1.00 171.00 ? 696  LYS B NZ  1 
ATOM   19672 N  N   . LYS C 1 697  ? -33.320  49.300  77.052  1.00 175.46 ? 697  LYS B N   1 
ATOM   19673 C  CA  . LYS C 1 697  ? -32.211  48.370  76.907  1.00 173.29 ? 697  LYS B CA  1 
ATOM   19674 C  C   . LYS C 1 697  ? -32.637  46.988  77.406  1.00 171.42 ? 697  LYS B C   1 
ATOM   19675 O  O   . LYS C 1 697  ? -32.288  45.972  76.806  1.00 171.65 ? 697  LYS B O   1 
ATOM   19676 C  CB  . LYS C 1 697  ? -30.987  48.900  77.667  1.00 174.02 ? 697  LYS B CB  1 
ATOM   19677 C  CG  . LYS C 1 697  ? -29.816  47.948  77.774  1.00 174.68 ? 697  LYS B CG  1 
ATOM   19678 C  CD  . LYS C 1 697  ? -29.028  47.831  76.486  1.00 175.86 ? 697  LYS B CD  1 
ATOM   19679 C  CE  . LYS C 1 697  ? -27.806  46.941  76.708  1.00 176.27 ? 697  LYS B CE  1 
ATOM   19680 N  NZ  . LYS C 1 697  ? -27.089  46.554  75.457  1.00 176.37 ? 697  LYS B NZ  1 
ATOM   19681 N  N   . CYS C 1 698  ? -33.422  46.952  78.482  1.00 169.90 ? 698  CYS B N   1 
ATOM   19682 C  CA  . CYS C 1 698  ? -33.916  45.687  79.018  1.00 166.81 ? 698  CYS B CA  1 
ATOM   19683 C  C   . CYS C 1 698  ? -34.647  44.860  77.955  1.00 165.85 ? 698  CYS B C   1 
ATOM   19684 O  O   . CYS C 1 698  ? -34.293  43.712  77.714  1.00 161.66 ? 698  CYS B O   1 
ATOM   19685 C  CB  . CYS C 1 698  ? -34.806  45.908  80.249  1.00 167.56 ? 698  CYS B CB  1 
ATOM   19686 S  SG  . CYS C 1 698  ? -33.932  46.019  81.850  1.00 200.74 ? 698  CYS B SG  1 
ATOM   19687 N  N   . CYS C 1 699  ? -35.655  45.424  77.307  1.00 167.83 ? 699  CYS B N   1 
ATOM   19688 C  CA  . CYS C 1 699  ? -36.340  44.653  76.285  1.00 172.26 ? 699  CYS B CA  1 
ATOM   19689 C  C   . CYS C 1 699  ? -35.470  44.495  75.058  1.00 174.49 ? 699  CYS B C   1 
ATOM   19690 O  O   . CYS C 1 699  ? -35.347  43.404  74.507  1.00 174.16 ? 699  CYS B O   1 
ATOM   19691 C  CB  . CYS C 1 699  ? -37.653  45.305  75.882  1.00 173.76 ? 699  CYS B CB  1 
ATOM   19692 S  SG  . CYS C 1 699  ? -38.303  44.668  74.316  1.00 171.92 ? 699  CYS B SG  1 
ATOM   19693 N  N   . TYR C 1 700  ? -34.869  45.601  74.639  1.00 179.98 ? 700  TYR B N   1 
ATOM   19694 C  CA  . TYR C 1 700  ? -34.097  45.650  73.404  1.00 187.64 ? 700  TYR B CA  1 
ATOM   19695 C  C   . TYR C 1 700  ? -33.095  44.492  73.341  1.00 189.64 ? 700  TYR B C   1 
ATOM   19696 O  O   . TYR C 1 700  ? -33.278  43.540  72.577  1.00 190.36 ? 700  TYR B O   1 
ATOM   19697 C  CB  . TYR C 1 700  ? -33.391  47.007  73.296  1.00 194.30 ? 700  TYR B CB  1 
ATOM   19698 C  CG  . TYR C 1 700  ? -33.123  47.493  71.886  1.00 202.27 ? 700  TYR B CG  1 
ATOM   19699 C  CD1 . TYR C 1 700  ? -31.860  47.364  71.317  1.00 205.93 ? 700  TYR B CD1 1 
ATOM   19700 C  CD2 . TYR C 1 700  ? -34.125  48.094  71.131  1.00 205.96 ? 700  TYR B CD2 1 
ATOM   19701 C  CE1 . TYR C 1 700  ? -31.605  47.808  70.040  1.00 208.83 ? 700  TYR B CE1 1 
ATOM   19702 C  CE2 . TYR C 1 700  ? -33.880  48.546  69.852  1.00 209.10 ? 700  TYR B CE2 1 
ATOM   19703 C  CZ  . TYR C 1 700  ? -32.615  48.399  69.310  1.00 210.54 ? 700  TYR B CZ  1 
ATOM   19704 O  OH  . TYR C 1 700  ? -32.353  48.839  68.031  1.00 212.12 ? 700  TYR B OH  1 
ATOM   19705 N  N   . ASP C 1 701  ? -32.044  44.572  74.156  1.00 192.62 ? 701  ASP B N   1 
ATOM   19706 C  CA  . ASP C 1 701  ? -31.077  43.474  74.274  1.00 193.15 ? 701  ASP B CA  1 
ATOM   19707 C  C   . ASP C 1 701  ? -31.733  42.291  74.982  1.00 191.58 ? 701  ASP B C   1 
ATOM   19708 O  O   . ASP C 1 701  ? -31.133  41.223  75.152  1.00 191.85 ? 701  ASP B O   1 
ATOM   19709 C  CB  . ASP C 1 701  ? -29.763  43.922  74.962  1.00 194.99 ? 701  ASP B CB  1 
ATOM   19710 C  CG  . ASP C 1 701  ? -29.871  44.022  76.485  1.00 195.54 ? 701  ASP B CG  1 
ATOM   19711 O  OD1 . ASP C 1 701  ? -30.918  43.661  77.056  1.00 195.63 ? 701  ASP B OD1 1 
ATOM   19712 O  OD2 . ASP C 1 701  ? -28.886  44.460  77.118  1.00 195.56 ? 701  ASP B OD2 1 
ATOM   19713 N  N   . GLY C 1 702  ? -32.982  42.507  75.385  1.00 188.13 ? 702  GLY B N   1 
ATOM   19714 C  CA  . GLY C 1 702  ? -33.776  41.487  76.029  1.00 184.07 ? 702  GLY B CA  1 
ATOM   19715 C  C   . GLY C 1 702  ? -34.137  40.368  75.084  1.00 179.80 ? 702  GLY B C   1 
ATOM   19716 O  O   . GLY C 1 702  ? -34.026  39.191  75.419  1.00 178.47 ? 702  GLY B O   1 
ATOM   19717 N  N   . ALA C 1 703  ? -34.579  40.726  73.891  1.00 177.36 ? 703  ALA B N   1 
ATOM   19718 C  CA  . ALA C 1 703  ? -34.930  39.707  72.928  1.00 174.96 ? 703  ALA B CA  1 
ATOM   19719 C  C   . ALA C 1 703  ? -33.668  39.202  72.277  1.00 170.98 ? 703  ALA B C   1 
ATOM   19720 O  O   . ALA C 1 703  ? -33.594  38.047  71.865  1.00 171.88 ? 703  ALA B O   1 
ATOM   19721 C  CB  . ALA C 1 703  ? -35.856  40.273  71.892  1.00 176.50 ? 703  ALA B CB  1 
ATOM   19722 N  N   . CYS C 1 704  ? -32.661  40.069  72.247  1.00 167.91 ? 704  CYS B N   1 
ATOM   19723 C  CA  . CYS C 1 704  ? -31.551  39.932  71.315  1.00 164.86 ? 704  CYS B CA  1 
ATOM   19724 C  C   . CYS C 1 704  ? -31.578  38.586  70.598  1.00 165.39 ? 704  CYS B C   1 
ATOM   19725 O  O   . CYS C 1 704  ? -32.214  38.473  69.551  1.00 165.27 ? 704  CYS B O   1 
ATOM   19726 C  CB  . CYS C 1 704  ? -30.203  40.184  71.987  1.00 163.55 ? 704  CYS B CB  1 
ATOM   19727 S  SG  . CYS C 1 704  ? -28.963  40.812  70.835  1.00 140.22 ? 704  CYS B SG  1 
ATOM   19728 N  N   . VAL C 1 705  ? -30.939  37.561  71.160  1.00 164.98 ? 705  VAL B N   1 
ATOM   19729 C  CA  . VAL C 1 705  ? -30.841  36.277  70.467  1.00 164.71 ? 705  VAL B CA  1 
ATOM   19730 C  C   . VAL C 1 705  ? -30.215  35.199  71.298  1.00 167.83 ? 705  VAL B C   1 
ATOM   19731 O  O   . VAL C 1 705  ? -29.032  34.917  71.121  1.00 169.59 ? 705  VAL B O   1 
ATOM   19732 C  CB  . VAL C 1 705  ? -29.887  36.376  69.266  1.00 163.46 ? 705  VAL B CB  1 
ATOM   19733 C  CG1 . VAL C 1 705  ? -30.641  36.671  67.991  1.00 163.96 ? 705  VAL B CG1 1 
ATOM   19734 C  CG2 . VAL C 1 705  ? -28.772  37.400  69.536  1.00 161.78 ? 705  VAL B CG2 1 
ATOM   19735 N  N   . ASN C 1 706  ? -30.970  34.549  72.170  1.00 168.34 ? 706  ASN B N   1 
ATOM   19736 C  CA  . ASN C 1 706  ? -30.304  33.558  73.011  1.00 169.73 ? 706  ASN B CA  1 
ATOM   19737 C  C   . ASN C 1 706  ? -31.009  32.234  73.119  1.00 168.11 ? 706  ASN B C   1 
ATOM   19738 O  O   . ASN C 1 706  ? -31.945  32.062  73.896  1.00 168.17 ? 706  ASN B O   1 
ATOM   19739 C  CB  . ASN C 1 706  ? -29.985  34.111  74.398  1.00 172.83 ? 706  ASN B CB  1 
ATOM   19740 C  CG  . ASN C 1 706  ? -28.663  33.620  74.915  1.00 175.51 ? 706  ASN B CG  1 
ATOM   19741 O  OD1 . ASN C 1 706  ? -28.149  32.600  74.453  1.00 176.30 ? 706  ASN B OD1 1 
ATOM   19742 N  ND2 . ASN C 1 706  ? -28.089  34.353  75.863  1.00 176.66 ? 706  ASN B ND2 1 
ATOM   19743 N  N   . ASN C 1 707  ? -30.521  31.290  72.330  1.00 166.39 ? 707  ASN B N   1 
ATOM   19744 C  CA  . ASN C 1 707  ? -31.192  30.011  72.180  1.00 165.25 ? 707  ASN B CA  1 
ATOM   19745 C  C   . ASN C 1 707  ? -30.615  28.881  73.023  1.00 160.32 ? 707  ASN B C   1 
ATOM   19746 O  O   . ASN C 1 707  ? -31.097  27.751  72.965  1.00 156.95 ? 707  ASN B O   1 
ATOM   19747 C  CB  . ASN C 1 707  ? -31.321  29.605  70.695  1.00 167.46 ? 707  ASN B CB  1 
ATOM   19748 C  CG  . ASN C 1 707  ? -30.140  30.052  69.836  1.00 168.08 ? 707  ASN B CG  1 
ATOM   19749 O  OD1 . ASN C 1 707  ? -29.292  30.842  70.258  1.00 168.11 ? 707  ASN B OD1 1 
ATOM   19750 N  ND2 . ASN C 1 707  ? -30.096  29.545  68.610  1.00 168.23 ? 707  ASN B ND2 1 
ATOM   19751 N  N   . ASP C 1 708  ? -29.591  29.181  73.810  1.00 159.17 ? 708  ASP B N   1 
ATOM   19752 C  CA  . ASP C 1 708  ? -28.991  28.145  74.639  1.00 155.85 ? 708  ASP B CA  1 
ATOM   19753 C  C   . ASP C 1 708  ? -29.579  28.096  76.039  1.00 154.09 ? 708  ASP B C   1 
ATOM   19754 O  O   . ASP C 1 708  ? -29.309  27.177  76.809  1.00 152.50 ? 708  ASP B O   1 
ATOM   19755 C  CB  . ASP C 1 708  ? -27.473  28.272  74.667  1.00 150.16 ? 708  ASP B CB  1 
ATOM   19756 C  CG  . ASP C 1 708  ? -26.818  27.495  73.555  1.00 142.26 ? 708  ASP B CG  1 
ATOM   19757 O  OD1 . ASP C 1 708  ? -27.539  26.712  72.896  1.00 138.10 ? 708  ASP B OD1 1 
ATOM   19758 O  OD2 . ASP C 1 708  ? -25.595  27.662  73.353  1.00 138.88 ? 708  ASP B OD2 1 
ATOM   19759 N  N   . GLU C 1 709  ? -30.404  29.084  76.355  1.00 154.86 ? 709  GLU B N   1 
ATOM   19760 C  CA  . GLU C 1 709  ? -31.138  29.067  77.606  1.00 156.45 ? 709  GLU B CA  1 
ATOM   19761 C  C   . GLU C 1 709  ? -32.502  29.724  77.459  1.00 158.16 ? 709  GLU B C   1 
ATOM   19762 O  O   . GLU C 1 709  ? -32.687  30.576  76.591  1.00 162.36 ? 709  GLU B O   1 
ATOM   19763 C  CB  . GLU C 1 709  ? -30.323  29.709  78.743  1.00 158.12 ? 709  GLU B CB  1 
ATOM   19764 C  CG  . GLU C 1 709  ? -29.470  30.938  78.373  1.00 159.29 ? 709  GLU B CG  1 
ATOM   19765 C  CD  . GLU C 1 709  ? -28.426  31.271  79.448  1.00 158.88 ? 709  GLU B CD  1 
ATOM   19766 O  OE1 . GLU C 1 709  ? -28.613  30.821  80.608  1.00 158.06 ? 709  GLU B OE1 1 
ATOM   19767 O  OE2 . GLU C 1 709  ? -27.431  31.975  79.125  1.00 158.77 ? 709  GLU B OE2 1 
ATOM   19768 N  N   . THR C 1 710  ? -33.445  29.313  78.307  1.00 156.97 ? 710  THR B N   1 
ATOM   19769 C  CA  . THR C 1 710  ? -34.816  29.836  78.303  1.00 159.05 ? 710  THR B CA  1 
ATOM   19770 C  C   . THR C 1 710  ? -34.871  31.354  78.471  1.00 162.93 ? 710  THR B C   1 
ATOM   19771 O  O   . THR C 1 710  ? -33.856  31.996  78.746  1.00 162.04 ? 710  THR B O   1 
ATOM   19772 C  CB  . THR C 1 710  ? -35.673  29.207  79.441  1.00 179.90 ? 710  THR B CB  1 
ATOM   19773 O  OG1 . THR C 1 710  ? -35.543  29.978  80.643  1.00 179.65 ? 710  THR B OG1 1 
ATOM   19774 C  CG2 . THR C 1 710  ? -35.260  27.764  79.708  1.00 179.30 ? 710  THR B CG2 1 
ATOM   19775 N  N   . CYS C 1 711  ? -36.050  31.939  78.304  1.00 166.98 ? 711  CYS B N   1 
ATOM   19776 C  CA  . CYS C 1 711  ? -36.159  33.352  78.595  1.00 170.60 ? 711  CYS B CA  1 
ATOM   19777 C  C   . CYS C 1 711  ? -35.939  33.564  80.071  1.00 170.63 ? 711  CYS B C   1 
ATOM   19778 O  O   . CYS C 1 711  ? -35.086  34.346  80.457  1.00 172.42 ? 711  CYS B O   1 
ATOM   19779 C  CB  . CYS C 1 711  ? -37.487  33.941  78.133  1.00 173.34 ? 711  CYS B CB  1 
ATOM   19780 S  SG  . CYS C 1 711  ? -37.319  34.919  76.620  1.00 172.21 ? 711  CYS B SG  1 
ATOM   19781 N  N   . GLU C 1 712  ? -36.675  32.839  80.900  1.00 169.23 ? 712  GLU B N   1 
ATOM   19782 C  CA  . GLU C 1 712  ? -36.552  33.035  82.341  1.00 169.85 ? 712  GLU B CA  1 
ATOM   19783 C  C   . GLU C 1 712  ? -35.256  32.474  82.966  1.00 164.46 ? 712  GLU B C   1 
ATOM   19784 O  O   . GLU C 1 712  ? -34.983  32.713  84.142  1.00 162.69 ? 712  GLU B O   1 
ATOM   19785 C  CB  . GLU C 1 712  ? -37.810  32.557  83.083  1.00 176.46 ? 712  GLU B CB  1 
ATOM   19786 C  CG  . GLU C 1 712  ? -38.100  31.069  82.971  1.00 183.04 ? 712  GLU B CG  1 
ATOM   19787 C  CD  . GLU C 1 712  ? -39.365  30.671  83.712  1.00 188.10 ? 712  GLU B CD  1 
ATOM   19788 O  OE1 . GLU C 1 712  ? -40.359  31.435  83.646  1.00 190.32 ? 712  GLU B OE1 1 
ATOM   19789 O  OE2 . GLU C 1 712  ? -39.360  29.594  84.354  1.00 188.98 ? 712  GLU B OE2 1 
ATOM   19790 N  N   . GLN C 1 713  ? -34.456  31.743  82.192  1.00 162.05 ? 713  GLN B N   1 
ATOM   19791 C  CA  . GLN C 1 713  ? -33.114  31.370  82.646  1.00 159.05 ? 713  GLN B CA  1 
ATOM   19792 C  C   . GLN C 1 713  ? -32.253  32.608  82.571  1.00 154.82 ? 713  GLN B C   1 
ATOM   19793 O  O   . GLN C 1 713  ? -31.480  32.906  83.474  1.00 155.22 ? 713  GLN B O   1 
ATOM   19794 C  CB  . GLN C 1 713  ? -32.506  30.254  81.787  1.00 159.28 ? 713  GLN B CB  1 
ATOM   19795 C  CG  . GLN C 1 713  ? -32.947  28.861  82.197  1.00 159.18 ? 713  GLN B CG  1 
ATOM   19796 C  CD  . GLN C 1 713  ? -32.680  27.797  81.145  1.00 158.92 ? 713  GLN B CD  1 
ATOM   19797 O  OE1 . GLN C 1 713  ? -32.311  28.091  80.015  1.00 158.98 ? 713  GLN B OE1 1 
ATOM   19798 N  NE2 . GLN C 1 713  ? -32.889  26.546  81.518  1.00 158.46 ? 713  GLN B NE2 1 
ATOM   19799 N  N   . ARG C 1 714  ? -32.414  33.337  81.477  1.00 150.82 ? 714  ARG B N   1 
ATOM   19800 C  CA  . ARG C 1 714  ? -31.722  34.600  81.295  1.00 147.84 ? 714  ARG B CA  1 
ATOM   19801 C  C   . ARG C 1 714  ? -32.219  35.629  82.307  1.00 144.08 ? 714  ARG B C   1 
ATOM   19802 O  O   . ARG C 1 714  ? -31.421  36.318  82.923  1.00 142.92 ? 714  ARG B O   1 
ATOM   19803 C  CB  . ARG C 1 714  ? -31.895  35.110  79.856  1.00 150.00 ? 714  ARG B CB  1 
ATOM   19804 C  CG  . ARG C 1 714  ? -31.181  34.270  78.799  1.00 152.24 ? 714  ARG B CG  1 
ATOM   19805 C  CD  . ARG C 1 714  ? -31.809  34.438  77.427  1.00 155.43 ? 714  ARG B CD  1 
ATOM   19806 N  NE  . ARG C 1 714  ? -31.609  35.780  76.894  1.00 159.35 ? 714  ARG B NE  1 
ATOM   19807 C  CZ  . ARG C 1 714  ? -32.159  36.233  75.765  1.00 162.58 ? 714  ARG B CZ  1 
ATOM   19808 N  NH1 . ARG C 1 714  ? -32.958  35.463  75.024  1.00 162.67 ? 714  ARG B NH1 1 
ATOM   19809 N  NH2 . ARG C 1 714  ? -31.908  37.471  75.366  1.00 164.28 ? 714  ARG B NH2 1 
ATOM   19810 N  N   . ALA C 1 715  ? -33.534  35.720  82.486  1.00 141.98 ? 715  ALA B N   1 
ATOM   19811 C  CA  . ALA C 1 715  ? -34.119  36.705  83.394  1.00 136.52 ? 715  ALA B CA  1 
ATOM   19812 C  C   . ALA C 1 715  ? -33.575  36.504  84.788  1.00 139.11 ? 715  ALA B C   1 
ATOM   19813 O  O   . ALA C 1 715  ? -33.405  37.458  85.544  1.00 139.64 ? 715  ALA B O   1 
ATOM   19814 C  CB  . ALA C 1 715  ? -35.626  36.595  83.415  1.00 136.65 ? 715  ALA B CB  1 
ATOM   19815 N  N   . ALA C 1 716  ? -33.308  35.252  85.131  1.00 137.94 ? 716  ALA B N   1 
ATOM   19816 C  CA  . ALA C 1 716  ? -32.731  34.956  86.427  1.00 139.60 ? 716  ALA B CA  1 
ATOM   19817 C  C   . ALA C 1 716  ? -31.494  35.827  86.649  1.00 141.45 ? 716  ALA B C   1 
ATOM   19818 O  O   . ALA C 1 716  ? -31.390  36.542  87.648  1.00 141.08 ? 716  ALA B O   1 
ATOM   19819 C  CB  . ALA C 1 716  ? -32.373  33.490  86.513  1.00 139.91 ? 716  ALA B CB  1 
ATOM   19820 N  N   . ARG C 1 717  ? -30.577  35.780  85.690  1.00 142.47 ? 717  ARG B N   1 
ATOM   19821 C  CA  . ARG C 1 717  ? -29.290  36.460  85.801  1.00 145.33 ? 717  ARG B CA  1 
ATOM   19822 C  C   . ARG C 1 717  ? -29.437  37.970  85.832  1.00 145.22 ? 717  ARG B C   1 
ATOM   19823 O  O   . ARG C 1 717  ? -28.442  38.678  85.918  1.00 144.84 ? 717  ARG B O   1 
ATOM   19824 C  CB  . ARG C 1 717  ? -28.390  36.066  84.624  1.00 148.89 ? 717  ARG B CB  1 
ATOM   19825 C  CG  . ARG C 1 717  ? -26.892  36.054  84.917  1.00 152.19 ? 717  ARG B CG  1 
ATOM   19826 C  CD  . ARG C 1 717  ? -26.120  35.499  83.709  1.00 153.14 ? 717  ARG B CD  1 
ATOM   19827 N  NE  . ARG C 1 717  ? -26.744  34.304  83.134  1.00 151.55 ? 717  ARG B NE  1 
ATOM   19828 C  CZ  . ARG C 1 717  ? -27.478  34.291  82.026  1.00 149.39 ? 717  ARG B CZ  1 
ATOM   19829 N  NH1 . ARG C 1 717  ? -27.685  35.400  81.349  1.00 148.82 ? 717  ARG B NH1 1 
ATOM   19830 N  NH2 . ARG C 1 717  ? -28.004  33.162  81.595  1.00 148.91 ? 717  ARG B NH2 1 
ATOM   19831 N  N   . ILE C 1 718  ? -30.671  38.458  85.742  1.00 145.79 ? 718  ILE B N   1 
ATOM   19832 C  CA  . ILE C 1 718  ? -30.918  39.892  85.711  1.00 148.67 ? 718  ILE B CA  1 
ATOM   19833 C  C   . ILE C 1 718  ? -30.834  40.465  87.098  1.00 154.64 ? 718  ILE B C   1 
ATOM   19834 O  O   . ILE C 1 718  ? -31.404  39.921  88.038  1.00 152.74 ? 718  ILE B O   1 
ATOM   19835 C  CB  . ILE C 1 718  ? -32.299  40.232  85.156  1.00 147.04 ? 718  ILE B CB  1 
ATOM   19836 C  CG1 . ILE C 1 718  ? -32.300  40.106  83.642  1.00 147.58 ? 718  ILE B CG1 1 
ATOM   19837 C  CG2 . ILE C 1 718  ? -32.692  41.653  85.526  1.00 146.02 ? 718  ILE B CG2 1 
ATOM   19838 C  CD1 . ILE C 1 718  ? -33.595  40.516  83.032  1.00 148.65 ? 718  ILE B CD1 1 
ATOM   19839 N  N   . SER C 1 719  ? -30.112  41.568  87.225  1.00 161.59 ? 719  SER B N   1 
ATOM   19840 C  CA  . SER C 1 719  ? -30.031  42.250  88.496  1.00 166.08 ? 719  SER B CA  1 
ATOM   19841 C  C   . SER C 1 719  ? -30.749  43.585  88.431  1.00 174.79 ? 719  SER B C   1 
ATOM   19842 O  O   . SER C 1 719  ? -31.558  43.906  89.296  1.00 177.08 ? 719  SER B O   1 
ATOM   19843 C  CB  . SER C 1 719  ? -28.586  42.467  88.878  1.00 161.59 ? 719  SER B CB  1 
ATOM   19844 O  OG  . SER C 1 719  ? -28.542  42.875  90.217  1.00 160.22 ? 719  SER B OG  1 
ATOM   19845 N  N   . LEU C 1 720  ? -30.473  44.332  87.367  1.00 181.90 ? 720  LEU B N   1 
ATOM   19846 C  CA  . LEU C 1 720  ? -30.859  45.744  87.238  1.00 190.88 ? 720  LEU B CA  1 
ATOM   19847 C  C   . LEU C 1 720  ? -32.159  46.172  87.933  1.00 197.02 ? 720  LEU B C   1 
ATOM   19848 O  O   . LEU C 1 720  ? -32.283  47.320  88.365  1.00 197.14 ? 720  LEU B O   1 
ATOM   19849 C  CB  . LEU C 1 720  ? -30.870  46.169  85.756  1.00 194.76 ? 720  LEU B CB  1 
ATOM   19850 C  CG  . LEU C 1 720  ? -29.533  46.114  84.996  1.00 201.22 ? 720  LEU B CG  1 
ATOM   19851 C  CD1 . LEU C 1 720  ? -29.660  46.649  83.576  1.00 203.37 ? 720  LEU B CD1 1 
ATOM   19852 C  CD2 . LEU C 1 720  ? -28.448  46.877  85.745  1.00 205.68 ? 720  LEU B CD2 1 
ATOM   19853 N  N   . GLY C 1 721  ? -33.125  45.267  88.036  1.00 204.31 ? 721  GLY B N   1 
ATOM   19854 C  CA  . GLY C 1 721  ? -34.355  45.579  88.740  1.00 211.13 ? 721  GLY B CA  1 
ATOM   19855 C  C   . GLY C 1 721  ? -35.573  44.871  88.185  1.00 214.52 ? 721  GLY B C   1 
ATOM   19856 O  O   . GLY C 1 721  ? -35.886  45.013  86.998  1.00 215.84 ? 721  GLY B O   1 
ATOM   19857 N  N   . PRO C 1 722  ? -36.270  44.100  89.044  1.00 214.30 ? 722  PRO B N   1 
ATOM   19858 C  CA  . PRO C 1 722  ? -37.525  43.426  88.679  1.00 212.19 ? 722  PRO B CA  1 
ATOM   19859 C  C   . PRO C 1 722  ? -38.484  44.352  87.924  1.00 208.55 ? 722  PRO B C   1 
ATOM   19860 O  O   . PRO C 1 722  ? -39.534  43.927  87.447  1.00 207.32 ? 722  PRO B O   1 
ATOM   19861 C  CB  . PRO C 1 722  ? -38.098  43.020  90.039  1.00 212.18 ? 722  PRO B CB  1 
ATOM   19862 C  CG  . PRO C 1 722  ? -36.861  42.748  90.887  1.00 212.22 ? 722  PRO B CG  1 
ATOM   19863 C  CD  . PRO C 1 722  ? -35.806  43.723  90.398  1.00 213.76 ? 722  PRO B CD  1 
ATOM   19864 N  N   . ARG C 1 723  ? -38.100  45.616  87.823  1.00 207.00 ? 723  ARG B N   1 
ATOM   19865 C  CA  . ARG C 1 723  ? -38.835  46.610  87.066  1.00 203.72 ? 723  ARG B CA  1 
ATOM   19866 C  C   . ARG C 1 723  ? -38.789  46.298  85.568  1.00 201.89 ? 723  ARG B C   1 
ATOM   19867 O  O   . ARG C 1 723  ? -39.737  46.574  84.831  1.00 202.66 ? 723  ARG B O   1 
ATOM   19868 C  CB  . ARG C 1 723  ? -38.214  47.981  87.331  1.00 201.95 ? 723  ARG B CB  1 
ATOM   19869 C  CG  . ARG C 1 723  ? -37.551  48.119  88.716  1.00 197.65 ? 723  ARG B CG  1 
ATOM   19870 C  CD  . ARG C 1 723  ? -36.963  49.519  88.894  1.00 194.98 ? 723  ARG B CD  1 
ATOM   19871 N  NE  . ARG C 1 723  ? -36.508  49.804  90.251  1.00 192.43 ? 723  ARG B NE  1 
ATOM   19872 C  CZ  . ARG C 1 723  ? -35.235  49.760  90.633  1.00 191.54 ? 723  ARG B CZ  1 
ATOM   19873 N  NH1 . ARG C 1 723  ? -34.291  49.433  89.761  1.00 190.85 ? 723  ARG B NH1 1 
ATOM   19874 N  NH2 . ARG C 1 723  ? -34.900  50.039  91.887  1.00 191.82 ? 723  ARG B NH2 1 
ATOM   19875 N  N   . CYS C 1 724  ? -37.672  45.728  85.124  1.00 198.60 ? 724  CYS B N   1 
ATOM   19876 C  CA  . CYS C 1 724  ? -37.455  45.448  83.707  1.00 195.67 ? 724  CYS B CA  1 
ATOM   19877 C  C   . CYS C 1 724  ? -37.441  43.951  83.377  1.00 194.77 ? 724  CYS B C   1 
ATOM   19878 O  O   . CYS C 1 724  ? -37.404  43.568  82.211  1.00 193.02 ? 724  CYS B O   1 
ATOM   19879 C  CB  . CYS C 1 724  ? -36.159  46.113  83.218  1.00 194.49 ? 724  CYS B CB  1 
ATOM   19880 S  SG  . CYS C 1 724  ? -34.610  45.224  83.605  1.00 162.38 ? 724  CYS B SG  1 
ATOM   19881 N  N   . ILE C 1 725  ? -37.463  43.105  84.398  1.00 195.51 ? 725  ILE B N   1 
ATOM   19882 C  CA  . ILE C 1 725  ? -37.496  41.671  84.156  1.00 194.72 ? 725  ILE B CA  1 
ATOM   19883 C  C   . ILE C 1 725  ? -38.646  41.289  83.240  1.00 195.74 ? 725  ILE B C   1 
ATOM   19884 O  O   . ILE C 1 725  ? -38.499  40.411  82.394  1.00 196.16 ? 725  ILE B O   1 
ATOM   19885 C  CB  . ILE C 1 725  ? -37.639  40.889  85.448  1.00 192.61 ? 725  ILE B CB  1 
ATOM   19886 C  CG1 . ILE C 1 725  ? -36.363  41.030  86.269  1.00 191.61 ? 725  ILE B CG1 1 
ATOM   19887 C  CG2 . ILE C 1 725  ? -37.940  39.428  85.140  1.00 191.52 ? 725  ILE B CG2 1 
ATOM   19888 C  CD1 . ILE C 1 725  ? -36.379  40.256  87.565  1.00 190.89 ? 725  ILE B CD1 1 
ATOM   19889 N  N   . LYS C 1 726  ? -39.791  41.946  83.425  1.00 196.95 ? 726  LYS B N   1 
ATOM   19890 C  CA  . LYS C 1 726  ? -40.951  41.744  82.559  1.00 198.03 ? 726  LYS B CA  1 
ATOM   19891 C  C   . LYS C 1 726  ? -40.607  42.217  81.162  1.00 191.86 ? 726  LYS B C   1 
ATOM   19892 O  O   . LYS C 1 726  ? -40.807  41.502  80.181  1.00 189.20 ? 726  LYS B O   1 
ATOM   19893 C  CB  . LYS C 1 726  ? -42.175  42.524  83.061  1.00 206.91 ? 726  LYS B CB  1 
ATOM   19894 C  CG  . LYS C 1 726  ? -43.134  41.740  83.970  1.00 214.59 ? 726  LYS B CG  1 
ATOM   19895 C  CD  . LYS C 1 726  ? -44.538  42.369  83.985  1.00 221.28 ? 726  LYS B CD  1 
ATOM   19896 C  CE  . LYS C 1 726  ? -45.463  41.692  84.998  1.00 224.46 ? 726  LYS B CE  1 
ATOM   19897 N  NZ  . LYS C 1 726  ? -46.822  42.317  85.036  1.00 226.44 ? 726  LYS B NZ  1 
ATOM   19898 N  N   . ALA C 1 727  ? -40.083  43.433  81.082  1.00 189.71 ? 727  ALA B N   1 
ATOM   19899 C  CA  . ALA C 1 727  ? -39.674  43.995  79.806  1.00 186.53 ? 727  ALA B CA  1 
ATOM   19900 C  C   . ALA C 1 727  ? -38.730  43.038  79.079  1.00 180.97 ? 727  ALA B C   1 
ATOM   19901 O  O   . ALA C 1 727  ? -38.623  43.066  77.853  1.00 179.58 ? 727  ALA B O   1 
ATOM   19902 C  CB  . ALA C 1 727  ? -39.010  45.335  80.020  1.00 188.88 ? 727  ALA B CB  1 
ATOM   19903 N  N   . PHE C 1 728  ? -38.051  42.192  79.849  1.00 175.72 ? 728  PHE B N   1 
ATOM   19904 C  CA  . PHE C 1 728  ? -37.106  41.226  79.298  1.00 169.81 ? 728  PHE B CA  1 
ATOM   19905 C  C   . PHE C 1 728  ? -37.812  39.951  78.808  1.00 173.31 ? 728  PHE B C   1 
ATOM   19906 O  O   . PHE C 1 728  ? -37.716  39.594  77.627  1.00 174.33 ? 728  PHE B O   1 
ATOM   19907 C  CB  . PHE C 1 728  ? -36.025  40.903  80.339  1.00 160.57 ? 728  PHE B CB  1 
ATOM   19908 C  CG  . PHE C 1 728  ? -34.918  40.024  79.822  1.00 152.80 ? 728  PHE B CG  1 
ATOM   19909 C  CD1 . PHE C 1 728  ? -34.098  40.446  78.801  1.00 150.40 ? 728  PHE B CD1 1 
ATOM   19910 C  CD2 . PHE C 1 728  ? -34.683  38.785  80.384  1.00 149.57 ? 728  PHE B CD2 1 
ATOM   19911 C  CE1 . PHE C 1 728  ? -33.079  39.642  78.339  1.00 149.21 ? 728  PHE B CE1 1 
ATOM   19912 C  CE2 . PHE C 1 728  ? -33.667  37.981  79.925  1.00 148.04 ? 728  PHE B CE2 1 
ATOM   19913 C  CZ  . PHE C 1 728  ? -32.866  38.410  78.900  1.00 148.31 ? 728  PHE B CZ  1 
ATOM   19914 N  N   . THR C 1 729  ? -38.524  39.277  79.713  1.00 173.65 ? 729  THR B N   1 
ATOM   19915 C  CA  . THR C 1 729  ? -39.227  38.033  79.383  1.00 173.76 ? 729  THR B CA  1 
ATOM   19916 C  C   . THR C 1 729  ? -40.315  38.282  78.345  1.00 175.06 ? 729  THR B C   1 
ATOM   19917 O  O   . THR C 1 729  ? -40.533  37.468  77.453  1.00 175.27 ? 729  THR B O   1 
ATOM   19918 C  CB  . THR C 1 729  ? -39.814  37.324  80.647  1.00 200.82 ? 729  THR B CB  1 
ATOM   19919 O  OG1 . THR C 1 729  ? -39.760  38.211  81.771  1.00 200.68 ? 729  THR B OG1 1 
ATOM   19920 C  CG2 . THR C 1 729  ? -39.020  36.065  80.995  1.00 200.23 ? 729  THR B CG2 1 
ATOM   19921 N  N   . GLU C 1 730  ? -40.983  39.421  78.453  1.00 177.47 ? 730  GLU B N   1 
ATOM   19922 C  CA  . GLU C 1 730  ? -41.995  39.781  77.479  1.00 180.80 ? 730  GLU B CA  1 
ATOM   19923 C  C   . GLU C 1 730  ? -41.385  39.787  76.093  1.00 181.75 ? 730  GLU B C   1 
ATOM   19924 O  O   . GLU C 1 730  ? -41.614  38.882  75.290  1.00 182.18 ? 730  GLU B O   1 
ATOM   19925 C  CB  . GLU C 1 730  ? -42.556  41.166  77.790  1.00 182.23 ? 730  GLU B CB  1 
ATOM   19926 C  CG  . GLU C 1 730  ? -43.571  41.194  78.923  1.00 181.80 ? 730  GLU B CG  1 
ATOM   19927 C  CD  . GLU C 1 730  ? -44.995  41.094  78.419  1.00 181.24 ? 730  GLU B CD  1 
ATOM   19928 O  OE1 . GLU C 1 730  ? -45.312  41.748  77.394  1.00 180.53 ? 730  GLU B OE1 1 
ATOM   19929 O  OE2 . GLU C 1 730  ? -45.789  40.364  79.055  1.00 180.77 ? 730  GLU B OE2 1 
ATOM   19930 N  N   . CYS C 1 731  ? -40.584  40.813  75.836  1.00 183.50 ? 731  CYS B N   1 
ATOM   19931 C  CA  . CYS C 1 731  ? -40.030  41.045  74.513  1.00 184.85 ? 731  CYS B CA  1 
ATOM   19932 C  C   . CYS C 1 731  ? -39.236  39.835  74.035  1.00 187.69 ? 731  CYS B C   1 
ATOM   19933 O  O   . CYS C 1 731  ? -39.137  39.588  72.830  1.00 188.03 ? 731  CYS B O   1 
ATOM   19934 C  CB  . CYS C 1 731  ? -39.156  42.308  74.506  1.00 184.83 ? 731  CYS B CB  1 
ATOM   19935 S  SG  . CYS C 1 731  ? -40.011  43.835  75.001  1.00 232.02 ? 731  CYS B SG  1 
ATOM   19936 N  N   . CYS C 1 732  ? -38.681  39.074  74.976  1.00 188.98 ? 732  CYS B N   1 
ATOM   19937 C  CA  . CYS C 1 732  ? -37.881  37.915  74.613  1.00 189.38 ? 732  CYS B CA  1 
ATOM   19938 C  C   . CYS C 1 732  ? -38.743  36.827  73.990  1.00 191.21 ? 732  CYS B C   1 
ATOM   19939 O  O   . CYS C 1 732  ? -38.426  36.322  72.911  1.00 191.57 ? 732  CYS B O   1 
ATOM   19940 C  CB  . CYS C 1 732  ? -37.131  37.359  75.812  1.00 188.79 ? 732  CYS B CB  1 
ATOM   19941 S  SG  . CYS C 1 732  ? -36.106  35.964  75.360  1.00 181.70 ? 732  CYS B SG  1 
ATOM   19942 N  N   . VAL C 1 733  ? -39.832  36.468  74.669  1.00 190.58 ? 733  VAL B N   1 
ATOM   19943 C  CA  . VAL C 1 733  ? -40.746  35.461  74.138  1.00 189.34 ? 733  VAL B CA  1 
ATOM   19944 C  C   . VAL C 1 733  ? -41.242  35.931  72.779  1.00 188.44 ? 733  VAL B C   1 
ATOM   19945 O  O   . VAL C 1 733  ? -41.156  35.204  71.794  1.00 187.23 ? 733  VAL B O   1 
ATOM   19946 C  CB  . VAL C 1 733  ? -41.931  35.168  75.092  1.00 189.01 ? 733  VAL B CB  1 
ATOM   19947 C  CG1 . VAL C 1 733  ? -43.008  34.383  74.370  1.00 190.24 ? 733  VAL B CG1 1 
ATOM   19948 C  CG2 . VAL C 1 733  ? -41.456  34.397  76.317  1.00 187.36 ? 733  VAL B CG2 1 
ATOM   19949 N  N   . VAL C 1 734  ? -41.720  37.167  72.726  1.00 188.67 ? 734  VAL B N   1 
ATOM   19950 C  CA  . VAL C 1 734  ? -42.177  37.755  71.475  1.00 190.03 ? 734  VAL B CA  1 
ATOM   19951 C  C   . VAL C 1 734  ? -41.218  37.458  70.324  1.00 191.00 ? 734  VAL B C   1 
ATOM   19952 O  O   . VAL C 1 734  ? -41.637  37.034  69.245  1.00 193.79 ? 734  VAL B O   1 
ATOM   19953 C  CB  . VAL C 1 734  ? -42.359  39.280  71.619  1.00 189.25 ? 734  VAL B CB  1 
ATOM   19954 C  CG1 . VAL C 1 734  ? -42.581  39.938  70.261  1.00 189.20 ? 734  VAL B CG1 1 
ATOM   19955 C  CG2 . VAL C 1 734  ? -43.508  39.581  72.567  1.00 189.16 ? 734  VAL B CG2 1 
ATOM   19956 N  N   . ALA C 1 735  ? -39.928  37.667  70.560  1.00 189.50 ? 735  ALA B N   1 
ATOM   19957 C  CA  . ALA C 1 735  ? -38.928  37.479  69.514  1.00 188.92 ? 735  ALA B CA  1 
ATOM   19958 C  C   . ALA C 1 735  ? -38.500  36.020  69.366  1.00 189.75 ? 735  ALA B C   1 
ATOM   19959 O  O   . ALA C 1 735  ? -37.806  35.671  68.412  1.00 189.96 ? 735  ALA B O   1 
ATOM   19960 C  CB  . ALA C 1 735  ? -37.714  38.364  69.765  1.00 187.78 ? 735  ALA B CB  1 
ATOM   19961 N  N   . SER C 1 736  ? -38.900  35.172  70.308  1.00 190.37 ? 736  SER B N   1 
ATOM   19962 C  CA  . SER C 1 736  ? -38.521  33.762  70.257  1.00 190.48 ? 736  SER B CA  1 
ATOM   19963 C  C   . SER C 1 736  ? -39.490  32.919  69.427  1.00 192.48 ? 736  SER B C   1 
ATOM   19964 O  O   . SER C 1 736  ? -39.070  32.044  68.661  1.00 192.62 ? 736  SER B O   1 
ATOM   19965 C  CB  . SER C 1 736  ? -38.387  33.197  71.665  1.00 189.55 ? 736  SER B CB  1 
ATOM   19966 O  OG  . SER C 1 736  ? -37.326  33.836  72.343  1.00 188.84 ? 736  SER B OG  1 
ATOM   19967 N  N   . GLN C 1 737  ? -40.784  33.185  69.591  1.00 192.33 ? 737  GLN B N   1 
ATOM   19968 C  CA  . GLN C 1 737  ? -41.817  32.515  68.811  1.00 192.03 ? 737  GLN B CA  1 
ATOM   19969 C  C   . GLN C 1 737  ? -41.707  33.017  67.379  1.00 192.65 ? 737  GLN B C   1 
ATOM   19970 O  O   . GLN C 1 737  ? -41.960  32.288  66.423  1.00 191.40 ? 737  GLN B O   1 
ATOM   19971 C  CB  . GLN C 1 737  ? -43.211  32.811  69.388  1.00 191.58 ? 737  GLN B CB  1 
ATOM   19972 C  CG  . GLN C 1 737  ? -43.222  33.214  70.881  1.00 190.97 ? 737  GLN B CG  1 
ATOM   19973 C  CD  . GLN C 1 737  ? -43.291  32.037  71.855  1.00 190.55 ? 737  GLN B CD  1 
ATOM   19974 O  OE1 . GLN C 1 737  ? -44.333  31.402  71.990  1.00 191.70 ? 737  GLN B OE1 1 
ATOM   19975 N  NE2 . GLN C 1 737  ? -42.190  31.768  72.559  1.00 188.77 ? 737  GLN B NE2 1 
ATOM   19976 N  N   . LEU C 1 738  ? -41.300  34.272  67.244  1.00 195.20 ? 738  LEU B N   1 
ATOM   19977 C  CA  . LEU C 1 738  ? -41.174  34.888  65.941  1.00 199.85 ? 738  LEU B CA  1 
ATOM   19978 C  C   . LEU C 1 738  ? -40.133  34.190  65.079  1.00 205.28 ? 738  LEU B C   1 
ATOM   19979 O  O   . LEU C 1 738  ? -40.265  34.149  63.862  1.00 207.92 ? 738  LEU B O   1 
ATOM   19980 C  CB  . LEU C 1 738  ? -40.829  36.371  66.071  1.00 196.89 ? 738  LEU B CB  1 
ATOM   19981 C  CG  . LEU C 1 738  ? -40.906  37.183  64.772  1.00 194.78 ? 738  LEU B CG  1 
ATOM   19982 C  CD1 . LEU C 1 738  ? -42.332  37.691  64.520  1.00 194.81 ? 738  LEU B CD1 1 
ATOM   19983 C  CD2 . LEU C 1 738  ? -39.916  38.338  64.797  1.00 192.84 ? 738  LEU B CD2 1 
ATOM   19984 N  N   . ARG C 1 739  ? -39.090  33.645  65.689  1.00 209.89 ? 739  ARG B N   1 
ATOM   19985 C  CA  . ARG C 1 739  ? -38.040  33.031  64.880  1.00 217.00 ? 739  ARG B CA  1 
ATOM   19986 C  C   . ARG C 1 739  ? -38.483  31.677  64.334  1.00 218.71 ? 739  ARG B C   1 
ATOM   19987 O  O   . ARG C 1 739  ? -37.838  31.108  63.452  1.00 219.33 ? 739  ARG B O   1 
ATOM   19988 C  CB  . ARG C 1 739  ? -36.708  32.935  65.636  1.00 222.23 ? 739  ARG B CB  1 
ATOM   19989 C  CG  . ARG C 1 739  ? -36.695  31.993  66.810  1.00 228.30 ? 739  ARG B CG  1 
ATOM   19990 C  CD  . ARG C 1 739  ? -35.328  32.012  67.467  1.00 234.44 ? 739  ARG B CD  1 
ATOM   19991 N  NE  . ARG C 1 739  ? -35.276  31.144  68.639  1.00 239.55 ? 739  ARG B NE  1 
ATOM   19992 C  CZ  . ARG C 1 739  ? -34.193  30.955  69.389  1.00 242.44 ? 739  ARG B CZ  1 
ATOM   19993 N  NH1 . ARG C 1 739  ? -33.056  31.576  69.096  1.00 243.21 ? 739  ARG B NH1 1 
ATOM   19994 N  NH2 . ARG C 1 739  ? -34.250  30.142  70.436  1.00 243.01 ? 739  ARG B NH2 1 
ATOM   19995 N  N   . ALA C 1 740  ? -39.597  31.177  64.856  1.00 220.35 ? 740  ALA B N   1 
ATOM   19996 C  CA  . ALA C 1 740  ? -40.177  29.937  64.362  1.00 221.45 ? 740  ALA B CA  1 
ATOM   19997 C  C   . ALA C 1 740  ? -40.943  30.189  63.069  1.00 222.24 ? 740  ALA B C   1 
ATOM   19998 O  O   . ALA C 1 740  ? -41.242  29.257  62.324  1.00 225.64 ? 740  ALA B O   1 
ATOM   19999 C  CB  . ALA C 1 740  ? -41.093  29.329  65.406  1.00 222.01 ? 740  ALA B CB  1 
ATOM   20000 N  N   . ASN C 1 741  ? -41.244  31.461  62.810  1.00 217.77 ? 741  ASN B N   1 
ATOM   20001 C  CA  . ASN C 1 741  ? -42.135  31.856  61.715  1.00 213.75 ? 741  ASN B CA  1 
ATOM   20002 C  C   . ASN C 1 741  ? -41.499  32.574  60.519  1.00 224.20 ? 741  ASN B C   1 
ATOM   20003 O  O   . ASN C 1 741  ? -41.995  32.463  59.403  1.00 225.91 ? 741  ASN B O   1 
ATOM   20004 C  CB  . ASN C 1 741  ? -43.319  32.664  62.263  1.00 202.01 ? 741  ASN B CB  1 
ATOM   20005 C  CG  . ASN C 1 741  ? -44.347  31.783  62.955  1.00 193.19 ? 741  ASN B CG  1 
ATOM   20006 O  OD1 . ASN C 1 741  ? -44.693  31.988  64.129  1.00 189.79 ? 741  ASN B OD1 1 
ATOM   20007 N  ND2 . ASN C 1 741  ? -44.817  30.765  62.233  1.00 188.12 ? 741  ASN B ND2 1 
ATOM   20008 N  N   . ILE C 1 742  ? -40.422  33.320  60.746  1.00 233.08 ? 742  ILE B N   1 
ATOM   20009 C  CA  . ILE C 1 742  ? -39.717  33.972  59.643  1.00 242.22 ? 742  ILE B CA  1 
ATOM   20010 C  C   . ILE C 1 742  ? -39.046  32.902  58.795  1.00 247.16 ? 742  ILE B C   1 
ATOM   20011 O  O   . ILE C 1 742  ? -38.666  33.141  57.646  1.00 248.07 ? 742  ILE B O   1 
ATOM   20012 C  CB  . ILE C 1 742  ? -38.630  34.953  60.142  1.00 243.24 ? 742  ILE B CB  1 
ATOM   20013 C  CG1 . ILE C 1 742  ? -39.160  35.816  61.289  1.00 243.39 ? 742  ILE B CG1 1 
ATOM   20014 C  CG2 . ILE C 1 742  ? -38.125  35.822  58.997  1.00 244.40 ? 742  ILE B CG2 1 
ATOM   20015 C  CD1 . ILE C 1 742  ? -38.115  36.721  61.909  1.00 242.24 ? 742  ILE B CD1 1 
ATOM   20016 N  N   . SER C 1 743  ? -38.916  31.714  59.382  1.00 249.59 ? 743  SER B N   1 
ATOM   20017 C  CA  . SER C 1 743  ? -38.209  30.601  58.765  1.00 251.88 ? 743  SER B CA  1 
ATOM   20018 C  C   . SER C 1 743  ? -38.715  29.269  59.311  1.00 251.75 ? 743  SER B C   1 
ATOM   20019 O  O   . SER C 1 743  ? -38.906  29.111  60.517  1.00 250.62 ? 743  SER B O   1 
ATOM   20020 C  CB  . SER C 1 743  ? -36.708  30.730  59.023  1.00 251.69 ? 743  SER B CB  1 
ATOM   20021 O  OG  . SER C 1 743  ? -36.446  30.869  60.409  1.00 250.99 ? 743  SER B OG  1 
ATOM   20022 N  N   . LEU C 1 749  ? -31.751  24.557  54.167  1.00 243.11 ? 749  LEU B N   1 
ATOM   20023 C  CA  . LEU C 1 749  ? -30.586  24.910  54.978  1.00 241.44 ? 749  LEU B CA  1 
ATOM   20024 C  C   . LEU C 1 749  ? -31.006  25.189  56.416  1.00 241.95 ? 749  LEU B C   1 
ATOM   20025 O  O   . LEU C 1 749  ? -32.185  25.082  56.755  1.00 242.58 ? 749  LEU B O   1 
ATOM   20026 C  CB  . LEU C 1 749  ? -29.863  26.129  54.396  1.00 239.65 ? 749  LEU B CB  1 
ATOM   20027 C  CG  . LEU C 1 749  ? -28.405  26.337  54.808  1.00 236.55 ? 749  LEU B CG  1 
ATOM   20028 C  CD1 . LEU C 1 749  ? -27.562  25.152  54.364  1.00 236.28 ? 749  LEU B CD1 1 
ATOM   20029 C  CD2 . LEU C 1 749  ? -27.865  27.631  54.225  1.00 235.57 ? 749  LEU B CD2 1 
ATOM   20030 N  N   . GLY C 1 750  ? -30.040  25.559  57.251  1.00 241.79 ? 750  GLY B N   1 
ATOM   20031 C  CA  . GLY C 1 750  ? -30.293  25.775  58.663  1.00 242.41 ? 750  GLY B CA  1 
ATOM   20032 C  C   . GLY C 1 750  ? -29.801  27.129  59.134  1.00 244.30 ? 750  GLY B C   1 
ATOM   20033 O  O   . GLY C 1 750  ? -29.399  27.283  60.291  1.00 242.23 ? 750  GLY B O   1 
ATOM   20034 N  N   . ARG C 1 751  ? -29.826  28.108  58.228  1.00 247.27 ? 751  ARG B N   1 
ATOM   20035 C  CA  . ARG C 1 751  ? -29.409  29.477  58.547  1.00 248.76 ? 751  ARG B CA  1 
ATOM   20036 C  C   . ARG C 1 751  ? -30.573  30.376  59.015  1.00 254.93 ? 751  ARG B C   1 
ATOM   20037 O  O   . ARG C 1 751  ? -31.384  30.833  58.203  1.00 256.45 ? 751  ARG B O   1 
ATOM   20038 C  CB  . ARG C 1 751  ? -28.659  30.120  57.359  1.00 242.17 ? 751  ARG B CB  1 
ATOM   20039 C  CG  . ARG C 1 751  ? -27.357  29.407  56.935  1.00 235.00 ? 751  ARG B CG  1 
ATOM   20040 C  CD  . ARG C 1 751  ? -26.303  29.323  58.063  1.00 227.16 ? 751  ARG B CD  1 
ATOM   20041 N  NE  . ARG C 1 751  ? -25.213  28.387  57.755  1.00 220.59 ? 751  ARG B NE  1 
ATOM   20042 C  CZ  . ARG C 1 751  ? -25.083  27.173  58.289  1.00 215.13 ? 751  ARG B CZ  1 
ATOM   20043 N  NH1 . ARG C 1 751  ? -25.968  26.734  59.175  1.00 213.13 ? 751  ARG B NH1 1 
ATOM   20044 N  NH2 . ARG C 1 751  ? -24.064  26.394  57.944  1.00 213.15 ? 751  ARG B NH2 1 
ATOM   20045 N  N   . LEU C 1 752  ? -30.639  30.619  60.329  1.00 259.25 ? 752  LEU B N   1 
ATOM   20046 C  CA  . LEU C 1 752  ? -31.556  31.604  60.920  1.00 263.32 ? 752  LEU B CA  1 
ATOM   20047 C  C   . LEU C 1 752  ? -30.903  32.356  62.089  1.00 261.29 ? 752  LEU B C   1 
ATOM   20048 O  O   . LEU C 1 752  ? -30.324  31.746  62.993  1.00 261.73 ? 752  LEU B O   1 
ATOM   20049 C  CB  . LEU C 1 752  ? -32.865  30.962  61.392  1.00 267.67 ? 752  LEU B CB  1 
ATOM   20050 C  CG  . LEU C 1 752  ? -33.804  31.932  62.121  1.00 271.55 ? 752  LEU B CG  1 
ATOM   20051 C  CD1 . LEU C 1 752  ? -34.476  32.905  61.147  1.00 273.68 ? 752  LEU B CD1 1 
ATOM   20052 C  CD2 . LEU C 1 752  ? -34.838  31.178  62.938  1.00 272.82 ? 752  LEU B CD2 1 
ATOM   20053 N  N   . HIS C 1 753  ? -31.014  33.684  62.061  1.00 258.61 ? 753  HIS B N   1 
ATOM   20054 C  CA  . HIS C 1 753  ? -30.365  34.557  63.035  1.00 253.21 ? 753  HIS B CA  1 
ATOM   20055 C  C   . HIS C 1 753  ? -31.155  35.853  63.169  1.00 243.06 ? 753  HIS B C   1 
ATOM   20056 O  O   . HIS C 1 753  ? -31.008  36.767  62.361  1.00 241.19 ? 753  HIS B O   1 
ATOM   20057 C  CB  . HIS C 1 753  ? -28.947  34.906  62.576  1.00 259.91 ? 753  HIS B CB  1 
ATOM   20058 C  CG  . HIS C 1 753  ? -28.417  34.014  61.490  1.00 266.53 ? 753  HIS B CG  1 
ATOM   20059 N  ND1 . HIS C 1 753  ? -28.614  34.274  60.149  1.00 270.16 ? 753  HIS B ND1 1 
ATOM   20060 C  CD2 . HIS C 1 753  ? -27.693  32.872  61.558  1.00 268.32 ? 753  HIS B CD2 1 
ATOM   20061 C  CE1 . HIS C 1 753  ? -28.026  33.323  59.436  1.00 271.63 ? 753  HIS B CE1 1 
ATOM   20062 N  NE2 . HIS C 1 753  ? -27.465  32.464  60.264  1.00 270.53 ? 753  HIS B NE2 1 
ATOM   20063 N  N   . MET C 1 754  ? -31.995  35.941  64.189  1.00 234.26 ? 754  MET B N   1 
ATOM   20064 C  CA  . MET C 1 754  ? -32.770  37.148  64.402  1.00 226.15 ? 754  MET B CA  1 
ATOM   20065 C  C   . MET C 1 754  ? -31.817  38.301  64.624  1.00 220.30 ? 754  MET B C   1 
ATOM   20066 O  O   . MET C 1 754  ? -30.606  38.096  64.662  1.00 219.70 ? 754  MET B O   1 
ATOM   20067 C  CB  . MET C 1 754  ? -33.638  36.976  65.631  1.00 222.90 ? 754  MET B CB  1 
ATOM   20068 C  CG  . MET C 1 754  ? -34.235  35.597  65.741  1.00 220.66 ? 754  MET B CG  1 
ATOM   20069 S  SD  . MET C 1 754  ? -34.739  35.294  67.428  1.00 196.03 ? 754  MET B SD  1 
ATOM   20070 C  CE  . MET C 1 754  ? -34.883  36.981  68.031  1.00 133.33 ? 754  MET B CE  1 
ATOM   20071 N  N   . LYS C 1 755  ? -32.361  39.507  64.763  1.00 215.75 ? 755  LYS B N   1 
ATOM   20072 C  CA  . LYS C 1 755  ? -31.582  40.664  65.215  1.00 212.96 ? 755  LYS B CA  1 
ATOM   20073 C  C   . LYS C 1 755  ? -32.444  41.911  65.412  1.00 215.08 ? 755  LYS B C   1 
ATOM   20074 O  O   . LYS C 1 755  ? -33.623  41.940  65.046  1.00 213.96 ? 755  LYS B O   1 
ATOM   20075 C  CB  . LYS C 1 755  ? -30.424  41.000  64.257  1.00 209.57 ? 755  LYS B CB  1 
ATOM   20076 C  CG  . LYS C 1 755  ? -29.094  40.261  64.491  1.00 206.53 ? 755  LYS B CG  1 
ATOM   20077 C  CD  . LYS C 1 755  ? -28.758  40.071  65.969  1.00 204.31 ? 755  LYS B CD  1 
ATOM   20078 C  CE  . LYS C 1 755  ? -28.251  41.342  66.631  1.00 203.32 ? 755  LYS B CE  1 
ATOM   20079 N  NZ  . LYS C 1 755  ? -27.851  41.069  68.044  1.00 201.76 ? 755  LYS B NZ  1 
ATOM   20080 N  N   . THR C 1 756  ? -31.827  42.926  66.014  1.00 219.53 ? 756  THR B N   1 
ATOM   20081 C  CA  . THR C 1 756  ? -32.357  44.285  66.074  1.00 224.25 ? 756  THR B CA  1 
ATOM   20082 C  C   . THR C 1 756  ? -31.200  45.215  66.432  1.00 230.35 ? 756  THR B C   1 
ATOM   20083 O  O   . THR C 1 756  ? -30.976  45.529  67.602  1.00 231.45 ? 756  THR B O   1 
ATOM   20084 C  CB  . THR C 1 756  ? -33.499  44.435  67.096  1.00 221.84 ? 756  THR B CB  1 
ATOM   20085 O  OG1 . THR C 1 756  ? -34.600  43.600  66.712  1.00 221.14 ? 756  THR B OG1 1 
ATOM   20086 C  CG2 . THR C 1 756  ? -33.974  45.881  67.151  1.00 221.55 ? 756  THR B CG2 1 
ATOM   20087 N  N   . LEU C 1 757  ? -30.468  45.644  65.406  1.00 235.96 ? 757  LEU B N   1 
ATOM   20088 C  CA  . LEU C 1 757  ? -29.213  46.372  65.583  1.00 242.29 ? 757  LEU B CA  1 
ATOM   20089 C  C   . LEU C 1 757  ? -29.351  47.614  66.464  1.00 246.61 ? 757  LEU B C   1 
ATOM   20090 O  O   . LEU C 1 757  ? -30.392  48.271  66.486  1.00 244.81 ? 757  LEU B O   1 
ATOM   20091 C  CB  . LEU C 1 757  ? -28.608  46.750  64.214  1.00 246.93 ? 757  LEU B CB  1 
ATOM   20092 C  CG  . LEU C 1 757  ? -27.275  47.524  64.145  1.00 251.64 ? 757  LEU B CG  1 
ATOM   20093 C  CD1 . LEU C 1 757  ? -26.100  46.649  64.566  1.00 252.18 ? 757  LEU B CD1 1 
ATOM   20094 C  CD2 . LEU C 1 757  ? -27.026  48.124  62.753  1.00 253.57 ? 757  LEU B CD2 1 
ATOM   20095 N  N   . LEU C 1 758  ? -28.285  47.906  67.199  1.00 251.98 ? 758  LEU B N   1 
ATOM   20096 C  CA  . LEU C 1 758  ? -28.128  49.158  67.915  1.00 257.14 ? 758  LEU B CA  1 
ATOM   20097 C  C   . LEU C 1 758  ? -26.755  49.102  68.540  1.00 269.72 ? 758  LEU B C   1 
ATOM   20098 O  O   . LEU C 1 758  ? -26.584  48.492  69.595  1.00 270.02 ? 758  LEU B O   1 
ATOM   20099 C  CB  . LEU C 1 758  ? -29.173  49.312  69.011  1.00 246.37 ? 758  LEU B CB  1 
ATOM   20100 C  CG  . LEU C 1 758  ? -29.569  50.742  69.389  1.00 236.80 ? 758  LEU B CG  1 
ATOM   20101 C  CD1 . LEU C 1 758  ? -30.208  50.754  70.765  1.00 232.72 ? 758  LEU B CD1 1 
ATOM   20102 C  CD2 . LEU C 1 758  ? -28.385  51.695  69.344  1.00 233.56 ? 758  LEU B CD2 1 
ATOM   20103 N  N   . PRO C 1 759  ? -25.762  49.721  67.880  1.00 281.62 ? 759  PRO B N   1 
ATOM   20104 C  CA  . PRO C 1 759  ? -24.379  49.750  68.373  1.00 289.09 ? 759  PRO B CA  1 
ATOM   20105 C  C   . PRO C 1 759  ? -24.281  50.253  69.813  1.00 298.22 ? 759  PRO B C   1 
ATOM   20106 O  O   . PRO C 1 759  ? -23.176  50.401  70.333  1.00 300.56 ? 759  PRO B O   1 
ATOM   20107 C  CB  . PRO C 1 759  ? -23.690  50.730  67.415  1.00 288.73 ? 759  PRO B CB  1 
ATOM   20108 C  CG  . PRO C 1 759  ? -24.459  50.604  66.144  1.00 286.46 ? 759  PRO B CG  1 
ATOM   20109 C  CD  . PRO C 1 759  ? -25.889  50.360  66.557  1.00 284.07 ? 759  PRO B CD  1 
ATOM   20110 N  N   . VAL C 1 760  ? -25.430  50.499  70.440  1.00 294.06 ? 760  VAL B N   1 
ATOM   20111 C  CA  . VAL C 1 760  ? -25.502  50.983  71.819  1.00 299.47 ? 760  VAL B CA  1 
ATOM   20112 C  C   . VAL C 1 760  ? -24.941  52.404  71.937  1.00 293.18 ? 760  VAL B C   1 
ATOM   20113 O  O   . VAL C 1 760  ? -24.699  52.905  73.038  1.00 294.97 ? 760  VAL B O   1 
ATOM   20114 C  CB  . VAL C 1 760  ? -24.795  50.024  72.812  1.00 326.93 ? 760  VAL B CB  1 
ATOM   20115 C  CG1 . VAL C 1 760  ? -25.230  50.316  74.241  1.00 330.71 ? 760  VAL B CG1 1 
ATOM   20116 C  CG2 . VAL C 1 760  ? -25.100  48.576  72.460  1.00 329.14 ? 760  VAL B CG2 1 
ATOM   20117 N  N   . SER C 1 761  ? -24.746  53.046  70.787  1.00 278.61 ? 761  SER B N   1 
ATOM   20118 C  CA  . SER C 1 761  ? -24.241  54.414  70.729  1.00 265.00 ? 761  SER B CA  1 
ATOM   20119 C  C   . SER C 1 761  ? -22.738  54.505  71.029  1.00 247.18 ? 761  SER B C   1 
ATOM   20120 O  O   . SER C 1 761  ? -22.264  55.541  71.487  1.00 245.87 ? 761  SER B O   1 
ATOM   20121 C  CB  . SER C 1 761  ? -25.041  55.322  71.673  1.00 267.68 ? 761  SER B CB  1 
ATOM   20122 O  OG  . SER C 1 761  ? -24.728  56.687  71.472  1.00 266.75 ? 761  SER B OG  1 
ATOM   20123 N  N   . LYS C 1 762  ? -21.997  53.426  70.769  1.00 230.88 ? 762  LYS B N   1 
ATOM   20124 C  CA  . LYS C 1 762  ? -20.547  53.405  70.995  1.00 211.66 ? 762  LYS B CA  1 
ATOM   20125 C  C   . LYS C 1 762  ? -19.764  53.860  69.777  1.00 199.49 ? 762  LYS B C   1 
ATOM   20126 O  O   . LYS C 1 762  ? -19.977  53.359  68.670  1.00 200.75 ? 762  LYS B O   1 
ATOM   20127 C  CB  . LYS C 1 762  ? -20.058  52.008  71.377  1.00 201.99 ? 762  LYS B CB  1 
ATOM   20128 C  CG  . LYS C 1 762  ? -20.496  51.509  72.742  1.00 193.94 ? 762  LYS B CG  1 
ATOM   20129 C  CD  . LYS C 1 762  ? -20.099  50.048  72.915  1.00 185.60 ? 762  LYS B CD  1 
ATOM   20130 C  CE  . LYS C 1 762  ? -20.806  49.407  74.090  1.00 181.52 ? 762  LYS B CE  1 
ATOM   20131 N  NZ  . LYS C 1 762  ? -20.216  48.076  74.361  1.00 179.60 ? 762  LYS B NZ  1 
ATOM   20132 N  N   . PRO C 1 763  ? -18.841  54.811  69.982  1.00 188.43 ? 763  PRO B N   1 
ATOM   20133 C  CA  . PRO C 1 763  ? -17.968  55.266  68.900  1.00 178.11 ? 763  PRO B CA  1 
ATOM   20134 C  C   . PRO C 1 763  ? -16.886  54.242  68.574  1.00 171.35 ? 763  PRO B C   1 
ATOM   20135 O  O   . PRO C 1 763  ? -15.808  54.301  69.171  1.00 170.62 ? 763  PRO B O   1 
ATOM   20136 C  CB  . PRO C 1 763  ? -17.321  56.546  69.475  1.00 177.37 ? 763  PRO B CB  1 
ATOM   20137 C  CG  . PRO C 1 763  ? -18.189  56.957  70.607  1.00 179.59 ? 763  PRO B CG  1 
ATOM   20138 C  CD  . PRO C 1 763  ? -18.709  55.662  71.175  1.00 184.17 ? 763  PRO B CD  1 
ATOM   20139 N  N   . GLU C 1 764  ? -17.169  53.317  67.657  1.00 162.64 ? 764  GLU B N   1 
ATOM   20140 C  CA  . GLU C 1 764  ? -16.127  52.446  67.122  1.00 153.67 ? 764  GLU B CA  1 
ATOM   20141 C  C   . GLU C 1 764  ? -15.617  53.079  65.854  1.00 143.44 ? 764  GLU B C   1 
ATOM   20142 O  O   . GLU C 1 764  ? -16.252  53.992  65.333  1.00 142.56 ? 764  GLU B O   1 
ATOM   20143 C  CB  . GLU C 1 764  ? -16.661  51.054  66.835  1.00 154.39 ? 764  GLU B CB  1 
ATOM   20144 C  CG  . GLU C 1 764  ? -18.049  51.052  66.274  1.00 155.83 ? 764  GLU B CG  1 
ATOM   20145 C  CD  . GLU C 1 764  ? -18.742  49.716  66.477  1.00 158.71 ? 764  GLU B CD  1 
ATOM   20146 O  OE1 . GLU C 1 764  ? -18.045  48.677  66.535  1.00 158.90 ? 764  GLU B OE1 1 
ATOM   20147 O  OE2 . GLU C 1 764  ? -19.988  49.706  66.589  1.00 160.81 ? 764  GLU B OE2 1 
ATOM   20148 N  N   . ILE C 1 765  ? -14.479  52.611  65.356  1.00 135.96 ? 765  ILE B N   1 
ATOM   20149 C  CA  . ILE C 1 765  ? -13.868  53.248  64.193  1.00 128.65 ? 765  ILE B CA  1 
ATOM   20150 C  C   . ILE C 1 765  ? -12.852  52.349  63.492  1.00 129.05 ? 765  ILE B C   1 
ATOM   20151 O  O   . ILE C 1 765  ? -11.706  52.273  63.918  1.00 130.62 ? 765  ILE B O   1 
ATOM   20152 C  CB  . ILE C 1 765  ? -13.193  54.568  64.606  1.00 123.02 ? 765  ILE B CB  1 
ATOM   20153 C  CG1 . ILE C 1 765  ? -12.735  55.356  63.384  1.00 120.29 ? 765  ILE B CG1 1 
ATOM   20154 C  CG2 . ILE C 1 765  ? -12.031  54.288  65.503  1.00 121.20 ? 765  ILE B CG2 1 
ATOM   20155 C  CD1 . ILE C 1 765  ? -12.760  56.853  63.599  1.00 119.20 ? 765  ILE B CD1 1 
ATOM   20156 N  N   . ARG C 1 766  ? -13.262  51.696  62.401  1.00 126.68 ? 766  ARG B N   1 
ATOM   20157 C  CA  . ARG C 1 766  ? -12.459  50.614  61.816  1.00 125.33 ? 766  ARG B CA  1 
ATOM   20158 C  C   . ARG C 1 766  ? -11.216  51.037  61.022  1.00 126.23 ? 766  ARG B C   1 
ATOM   20159 O  O   . ARG C 1 766  ? -10.718  50.267  60.202  1.00 126.41 ? 766  ARG B O   1 
ATOM   20160 C  CB  . ARG C 1 766  ? -13.323  49.700  60.951  1.00 122.51 ? 766  ARG B CB  1 
ATOM   20161 C  CG  . ARG C 1 766  ? -14.710  49.525  61.461  1.00 121.74 ? 766  ARG B CG  1 
ATOM   20162 C  CD  . ARG C 1 766  ? -14.800  48.348  62.358  1.00 123.37 ? 766  ARG B CD  1 
ATOM   20163 N  NE  . ARG C 1 766  ? -16.168  48.194  62.831  1.00 127.42 ? 766  ARG B NE  1 
ATOM   20164 C  CZ  . ARG C 1 766  ? -16.709  47.035  63.214  1.00 132.09 ? 766  ARG B CZ  1 
ATOM   20165 N  NH1 . ARG C 1 766  ? -16.008  45.904  63.167  1.00 134.94 ? 766  ARG B NH1 1 
ATOM   20166 N  NH2 . ARG C 1 766  ? -17.965  46.996  63.640  1.00 133.07 ? 766  ARG B NH2 1 
ATOM   20167 N  N   . SER C 1 767  ? -10.702  52.237  61.259  1.00 128.16 ? 767  SER B N   1 
ATOM   20168 C  CA  . SER C 1 767  ? -9.480   52.649  60.579  1.00 131.52 ? 767  SER B CA  1 
ATOM   20169 C  C   . SER C 1 767  ? -8.567   53.423  61.515  1.00 132.53 ? 767  SER B C   1 
ATOM   20170 O  O   . SER C 1 767  ? -9.007   54.305  62.248  1.00 132.23 ? 767  SER B O   1 
ATOM   20171 C  CB  . SER C 1 767  ? -9.794   53.467  59.316  1.00 133.91 ? 767  SER B CB  1 
ATOM   20172 O  OG  . SER C 1 767  ? -10.303  54.764  59.603  1.00 134.38 ? 767  SER B OG  1 
ATOM   20173 N  N   . TYR C 1 768  ? -7.288   53.081  61.493  1.00 134.86 ? 768  TYR B N   1 
ATOM   20174 C  CA  . TYR C 1 768  ? -6.325   53.688  62.403  1.00 137.45 ? 768  TYR B CA  1 
ATOM   20175 C  C   . TYR C 1 768  ? -5.772   54.953  61.785  1.00 131.19 ? 768  TYR B C   1 
ATOM   20176 O  O   . TYR C 1 768  ? -5.766   55.094  60.558  1.00 132.29 ? 768  TYR B O   1 
ATOM   20177 C  CB  . TYR C 1 768  ? -5.185   52.700  62.693  1.00 146.72 ? 768  TYR B CB  1 
ATOM   20178 C  CG  . TYR C 1 768  ? -4.093   53.218  63.609  1.00 154.12 ? 768  TYR B CG  1 
ATOM   20179 C  CD1 . TYR C 1 768  ? -4.172   53.041  64.986  1.00 158.31 ? 768  TYR B CD1 1 
ATOM   20180 C  CD2 . TYR C 1 768  ? -2.972   53.857  63.093  1.00 156.25 ? 768  TYR B CD2 1 
ATOM   20181 C  CE1 . TYR C 1 768  ? -3.176   53.506  65.829  1.00 161.39 ? 768  TYR B CE1 1 
ATOM   20182 C  CE2 . TYR C 1 768  ? -1.972   54.322  63.923  1.00 159.64 ? 768  TYR B CE2 1 
ATOM   20183 C  CZ  . TYR C 1 768  ? -2.076   54.147  65.292  1.00 161.86 ? 768  TYR B CZ  1 
ATOM   20184 O  OH  . TYR C 1 768  ? -1.078   54.620  66.122  1.00 163.13 ? 768  TYR B OH  1 
ATOM   20185 N  N   . PHE C 1 769  ? -5.293   55.864  62.624  1.00 124.02 ? 769  PHE B N   1 
ATOM   20186 C  CA  . PHE C 1 769  ? -4.622   57.056  62.124  1.00 119.03 ? 769  PHE B CA  1 
ATOM   20187 C  C   . PHE C 1 769  ? -3.345   57.263  62.889  1.00 117.95 ? 769  PHE B C   1 
ATOM   20188 O  O   . PHE C 1 769  ? -3.396   57.558  64.075  1.00 119.31 ? 769  PHE B O   1 
ATOM   20189 C  CB  . PHE C 1 769  ? -5.482   58.310  62.312  1.00 117.31 ? 769  PHE B CB  1 
ATOM   20190 C  CG  . PHE C 1 769  ? -6.824   58.239  61.658  1.00 114.49 ? 769  PHE B CG  1 
ATOM   20191 C  CD1 . PHE C 1 769  ? -6.942   58.336  60.296  1.00 113.33 ? 769  PHE B CD1 1 
ATOM   20192 C  CD2 . PHE C 1 769  ? -7.967   58.079  62.426  1.00 113.86 ? 769  PHE B CD2 1 
ATOM   20193 C  CE1 . PHE C 1 769  ? -8.168   58.256  59.725  1.00 114.65 ? 769  PHE B CE1 1 
ATOM   20194 C  CE2 . PHE C 1 769  ? -9.194   58.009  61.868  1.00 109.72 ? 769  PHE B CE2 1 
ATOM   20195 C  CZ  . PHE C 1 769  ? -9.304   58.090  60.526  1.00 115.80 ? 769  PHE B CZ  1 
ATOM   20196 N  N   . PRO C 1 770  ? -2.206   57.168  62.198  1.00 118.45 ? 770  PRO B N   1 
ATOM   20197 C  CA  . PRO C 1 770  ? -0.819   57.205  62.682  1.00 122.65 ? 770  PRO B CA  1 
ATOM   20198 C  C   . PRO C 1 770  ? -0.480   58.422  63.514  1.00 127.07 ? 770  PRO B C   1 
ATOM   20199 O  O   . PRO C 1 770  ? -0.955   59.519  63.216  1.00 128.37 ? 770  PRO B O   1 
ATOM   20200 C  CB  . PRO C 1 770  ? -0.009   57.272  61.397  1.00 121.77 ? 770  PRO B CB  1 
ATOM   20201 C  CG  . PRO C 1 770  ? -0.883   56.671  60.371  1.00 121.27 ? 770  PRO B CG  1 
ATOM   20202 C  CD  . PRO C 1 770  ? -2.271   57.057  60.736  1.00 119.18 ? 770  PRO B CD  1 
ATOM   20203 N  N   . GLU C 1 771  ? 0.352    58.237  64.533  1.00 130.14 ? 771  GLU B N   1 
ATOM   20204 C  CA  . GLU C 1 771  ? 0.796    59.375  65.309  1.00 133.41 ? 771  GLU B CA  1 
ATOM   20205 C  C   . GLU C 1 771  ? 1.349    60.417  64.336  1.00 131.25 ? 771  GLU B C   1 
ATOM   20206 O  O   . GLU C 1 771  ? 1.957    60.045  63.324  1.00 129.63 ? 771  GLU B O   1 
ATOM   20207 C  CB  . GLU C 1 771  ? 1.871    58.951  66.304  1.00 141.66 ? 771  GLU B CB  1 
ATOM   20208 C  CG  . GLU C 1 771  ? 2.388    60.099  67.195  1.00 148.18 ? 771  GLU B CG  1 
ATOM   20209 C  CD  . GLU C 1 771  ? 3.421    59.642  68.230  1.00 154.24 ? 771  GLU B CD  1 
ATOM   20210 O  OE1 . GLU C 1 771  ? 3.295    60.012  69.424  1.00 155.49 ? 771  GLU B OE1 1 
ATOM   20211 O  OE2 . GLU C 1 771  ? 4.358    58.906  67.847  1.00 157.59 ? 771  GLU B OE2 1 
ATOM   20212 N  N   . SER C 1 772  ? 1.118    61.703  64.639  1.00 129.20 ? 772  SER B N   1 
ATOM   20213 C  CA  . SER C 1 772  ? 1.590    62.836  63.820  1.00 126.18 ? 772  SER B CA  1 
ATOM   20214 C  C   . SER C 1 772  ? 3.058    63.192  64.086  1.00 123.39 ? 772  SER B C   1 
ATOM   20215 O  O   . SER C 1 772  ? 3.677    62.645  65.004  1.00 123.64 ? 772  SER B O   1 
ATOM   20216 C  CB  . SER C 1 772  ? 0.707    64.083  64.018  1.00 125.24 ? 772  SER B CB  1 
ATOM   20217 O  OG  . SER C 1 772  ? -0.598   63.920  63.491  1.00 124.64 ? 772  SER B OG  1 
ATOM   20218 N  N   . TRP C 1 773  ? 3.601    64.128  63.306  1.00 121.65 ? 773  TRP B N   1 
ATOM   20219 C  CA  . TRP C 1 773  ? 5.027    64.473  63.394  1.00 123.76 ? 773  TRP B CA  1 
ATOM   20220 C  C   . TRP C 1 773  ? 5.397    65.829  62.782  1.00 127.66 ? 773  TRP B C   1 
ATOM   20221 O  O   . TRP C 1 773  ? 4.559    66.490  62.178  1.00 129.91 ? 773  TRP B O   1 
ATOM   20222 C  CB  . TRP C 1 773  ? 5.843    63.403  62.706  1.00 123.36 ? 773  TRP B CB  1 
ATOM   20223 C  CG  . TRP C 1 773  ? 5.439    63.189  61.290  1.00 123.66 ? 773  TRP B CG  1 
ATOM   20224 C  CD1 . TRP C 1 773  ? 4.310    62.565  60.842  1.00 122.84 ? 773  TRP B CD1 1 
ATOM   20225 C  CD2 . TRP C 1 773  ? 6.169    63.584  60.128  1.00 123.98 ? 773  TRP B CD2 1 
ATOM   20226 N  NE1 . TRP C 1 773  ? 4.293    62.551  59.472  1.00 123.50 ? 773  TRP B NE1 1 
ATOM   20227 C  CE2 . TRP C 1 773  ? 5.424    63.172  59.009  1.00 124.30 ? 773  TRP B CE2 1 
ATOM   20228 C  CE3 . TRP C 1 773  ? 7.384    64.245  59.925  1.00 125.09 ? 773  TRP B CE3 1 
ATOM   20229 C  CZ2 . TRP C 1 773  ? 5.853    63.396  57.706  1.00 124.33 ? 773  TRP B CZ2 1 
ATOM   20230 C  CZ3 . TRP C 1 773  ? 7.807    64.469  58.632  1.00 125.14 ? 773  TRP B CZ3 1 
ATOM   20231 C  CH2 . TRP C 1 773  ? 7.047    64.043  57.538  1.00 124.82 ? 773  TRP B CH2 1 
ATOM   20232 N  N   . LEU C 1 774  ? 6.662    66.224  62.908  1.00 128.51 ? 774  LEU B N   1 
ATOM   20233 C  CA  . LEU C 1 774  ? 7.084    67.581  62.548  1.00 129.38 ? 774  LEU B CA  1 
ATOM   20234 C  C   . LEU C 1 774  ? 6.402    68.628  63.420  1.00 126.73 ? 774  LEU B C   1 
ATOM   20235 O  O   . LEU C 1 774  ? 6.190    69.763  62.987  1.00 124.19 ? 774  LEU B O   1 
ATOM   20236 C  CB  . LEU C 1 774  ? 6.864    67.886  61.064  1.00 132.52 ? 774  LEU B CB  1 
ATOM   20237 C  CG  . LEU C 1 774  ? 8.160    68.032  60.269  1.00 136.56 ? 774  LEU B CG  1 
ATOM   20238 C  CD1 . LEU C 1 774  ? 7.944    68.648  58.896  1.00 136.93 ? 774  LEU B CD1 1 
ATOM   20239 C  CD2 . LEU C 1 774  ? 9.093    68.901  61.069  1.00 139.25 ? 774  LEU B CD2 1 
ATOM   20240 N  N   . TRP C 1 775  ? 6.080    68.213  64.649  1.00 126.85 ? 775  TRP B N   1 
ATOM   20241 C  CA  . TRP C 1 775  ? 5.362    69.012  65.648  1.00 125.04 ? 775  TRP B CA  1 
ATOM   20242 C  C   . TRP C 1 775  ? 6.266    70.016  66.360  1.00 126.85 ? 775  TRP B C   1 
ATOM   20243 O  O   . TRP C 1 775  ? 5.954    70.464  67.458  1.00 125.80 ? 775  TRP B O   1 
ATOM   20244 C  CB  . TRP C 1 775  ? 4.690    68.077  66.660  1.00 122.42 ? 775  TRP B CB  1 
ATOM   20245 C  CG  . TRP C 1 775  ? 3.774    68.732  67.647  1.00 122.41 ? 775  TRP B CG  1 
ATOM   20246 C  CD1 . TRP C 1 775  ? 4.064    69.020  68.936  1.00 124.96 ? 775  TRP B CD1 1 
ATOM   20247 C  CD2 . TRP C 1 775  ? 2.410    69.141  67.446  1.00 120.92 ? 775  TRP B CD2 1 
ATOM   20248 N  NE1 . TRP C 1 775  ? 2.981    69.602  69.557  1.00 124.73 ? 775  TRP B NE1 1 
ATOM   20249 C  CE2 . TRP C 1 775  ? 1.951    69.682  68.662  1.00 121.84 ? 775  TRP B CE2 1 
ATOM   20250 C  CE3 . TRP C 1 775  ? 1.542    69.117  66.357  1.00 120.39 ? 775  TRP B CE3 1 
ATOM   20251 C  CZ2 . TRP C 1 775  ? 0.669    70.192  68.819  1.00 120.40 ? 775  TRP B CZ2 1 
ATOM   20252 C  CZ3 . TRP C 1 775  ? 0.268    69.618  66.520  1.00 119.88 ? 775  TRP B CZ3 1 
ATOM   20253 C  CH2 . TRP C 1 775  ? -0.157   70.145  67.741  1.00 119.84 ? 775  TRP B CH2 1 
ATOM   20254 N  N   . GLU C 1 776  ? 7.374    70.374  65.710  1.00 130.12 ? 776  GLU B N   1 
ATOM   20255 C  CA  . GLU C 1 776  ? 8.344    71.338  66.235  1.00 135.11 ? 776  GLU B CA  1 
ATOM   20256 C  C   . GLU C 1 776  ? 7.982    72.801  65.980  1.00 133.93 ? 776  GLU B C   1 
ATOM   20257 O  O   . GLU C 1 776  ? 7.335    73.103  64.993  1.00 131.89 ? 776  GLU B O   1 
ATOM   20258 C  CB  . GLU C 1 776  ? 9.724    71.057  65.637  1.00 140.47 ? 776  GLU B CB  1 
ATOM   20259 C  CG  . GLU C 1 776  ? 9.712    70.367  64.276  1.00 144.73 ? 776  GLU B CG  1 
ATOM   20260 C  CD  . GLU C 1 776  ? 11.040   69.670  63.978  1.00 151.64 ? 776  GLU B CD  1 
ATOM   20261 O  OE1 . GLU C 1 776  ? 11.046   68.619  63.292  1.00 152.75 ? 776  GLU B OE1 1 
ATOM   20262 O  OE2 . GLU C 1 776  ? 12.088   70.168  64.452  1.00 155.73 ? 776  GLU B OE2 1 
ATOM   20263 N  N   . VAL C 1 777  ? 8.387    73.702  66.877  1.00 135.52 ? 777  VAL B N   1 
ATOM   20264 C  CA  . VAL C 1 777  ? 8.367    75.143  66.601  1.00 134.92 ? 777  VAL B CA  1 
ATOM   20265 C  C   . VAL C 1 777  ? 9.690    75.495  65.928  1.00 143.30 ? 777  VAL B C   1 
ATOM   20266 O  O   . VAL C 1 777  ? 10.610   74.692  65.945  1.00 146.30 ? 777  VAL B O   1 
ATOM   20267 C  CB  . VAL C 1 777  ? 8.195    75.975  67.883  1.00 124.61 ? 777  VAL B CB  1 
ATOM   20268 C  CG1 . VAL C 1 777  ? 8.675    77.407  67.670  1.00 121.25 ? 777  VAL B CG1 1 
ATOM   20269 C  CG2 . VAL C 1 777  ? 6.749    75.953  68.345  1.00 122.00 ? 777  VAL B CG2 1 
ATOM   20270 N  N   . HIS C 1 778  ? 9.796    76.674  65.328  1.00 148.13 ? 778  HIS B N   1 
ATOM   20271 C  CA  . HIS C 1 778  ? 11.048   77.080  64.704  1.00 156.69 ? 778  HIS B CA  1 
ATOM   20272 C  C   . HIS C 1 778  ? 11.123   78.589  64.639  1.00 167.81 ? 778  HIS B C   1 
ATOM   20273 O  O   . HIS C 1 778  ? 10.094   79.260  64.649  1.00 167.26 ? 778  HIS B O   1 
ATOM   20274 C  CB  . HIS C 1 778  ? 11.139   76.548  63.281  1.00 152.70 ? 778  HIS B CB  1 
ATOM   20275 C  CG  . HIS C 1 778  ? 11.691   75.161  63.167  1.00 151.61 ? 778  HIS B CG  1 
ATOM   20276 N  ND1 . HIS C 1 778  ? 12.955   74.903  62.680  1.00 152.48 ? 778  HIS B ND1 1 
ATOM   20277 C  CD2 . HIS C 1 778  ? 11.135   73.953  63.424  1.00 150.14 ? 778  HIS B CD2 1 
ATOM   20278 C  CE1 . HIS C 1 778  ? 13.161   73.599  62.665  1.00 152.26 ? 778  HIS B CE1 1 
ATOM   20279 N  NE2 . HIS C 1 778  ? 12.070   72.999  63.107  1.00 150.71 ? 778  HIS B NE2 1 
ATOM   20280 N  N   . LEU C 1 779  ? 12.341   79.124  64.558  1.00 181.11 ? 779  LEU B N   1 
ATOM   20281 C  CA  . LEU C 1 779  ? 12.529   80.561  64.362  1.00 191.72 ? 779  LEU B CA  1 
ATOM   20282 C  C   . LEU C 1 779  ? 12.982   80.898  62.955  1.00 199.67 ? 779  LEU B C   1 
ATOM   20283 O  O   . LEU C 1 779  ? 14.179   80.901  62.671  1.00 203.31 ? 779  LEU B O   1 
ATOM   20284 C  CB  . LEU C 1 779  ? 13.573   81.108  65.313  1.00 194.70 ? 779  LEU B CB  1 
ATOM   20285 C  CG  . LEU C 1 779  ? 13.740   82.583  64.992  1.00 195.95 ? 779  LEU B CG  1 
ATOM   20286 C  CD1 . LEU C 1 779  ? 12.516   83.323  65.486  1.00 195.20 ? 779  LEU B CD1 1 
ATOM   20287 C  CD2 . LEU C 1 779  ? 15.004   83.140  65.606  1.00 198.47 ? 779  LEU B CD2 1 
ATOM   20288 N  N   . VAL C 1 780  ? 12.039   81.215  62.080  1.00 203.88 ? 780  VAL B N   1 
ATOM   20289 C  CA  . VAL C 1 780  ? 12.394   81.449  60.689  1.00 209.25 ? 780  VAL B CA  1 
ATOM   20290 C  C   . VAL C 1 780  ? 12.474   82.922  60.323  1.00 208.87 ? 780  VAL B C   1 
ATOM   20291 O  O   . VAL C 1 780  ? 11.454   83.595  60.170  1.00 205.30 ? 780  VAL B O   1 
ATOM   20292 C  CB  . VAL C 1 780  ? 11.439   80.728  59.733  1.00 215.78 ? 780  VAL B CB  1 
ATOM   20293 C  CG1 . VAL C 1 780  ? 11.791   81.060  58.290  1.00 220.67 ? 780  VAL B CG1 1 
ATOM   20294 C  CG2 . VAL C 1 780  ? 11.507   79.232  59.975  1.00 218.42 ? 780  VAL B CG2 1 
ATOM   20295 N  N   . PRO C 1 781  ? 13.699   83.426  60.189  1.00 210.67 ? 781  PRO B N   1 
ATOM   20296 C  CA  . PRO C 1 781  ? 13.914   84.788  59.722  1.00 212.27 ? 781  PRO B CA  1 
ATOM   20297 C  C   . PRO C 1 781  ? 13.831   84.778  58.216  1.00 211.35 ? 781  PRO B C   1 
ATOM   20298 O  O   . PRO C 1 781  ? 14.850   84.582  57.566  1.00 213.88 ? 781  PRO B O   1 
ATOM   20299 C  CB  . PRO C 1 781  ? 15.350   85.078  60.154  1.00 215.45 ? 781  PRO B CB  1 
ATOM   20300 C  CG  . PRO C 1 781  ? 15.727   83.955  61.084  1.00 216.71 ? 781  PRO B CG  1 
ATOM   20301 C  CD  . PRO C 1 781  ? 14.953   82.791  60.602  1.00 214.82 ? 781  PRO B CD  1 
ATOM   20302 N  N   . ARG C 1 782  ? 12.631   84.960  57.675  1.00 208.93 ? 782  ARG B N   1 
ATOM   20303 C  CA  . ARG C 1 782  ? 12.433   85.064  56.229  1.00 209.16 ? 782  ARG B CA  1 
ATOM   20304 C  C   . ARG C 1 782  ? 12.839   83.809  55.449  1.00 205.48 ? 782  ARG B C   1 
ATOM   20305 O  O   . ARG C 1 782  ? 12.548   83.706  54.261  1.00 205.73 ? 782  ARG B O   1 
ATOM   20306 C  CB  . ARG C 1 782  ? 13.166   86.292  55.665  1.00 215.67 ? 782  ARG B CB  1 
ATOM   20307 C  CG  . ARG C 1 782  ? 12.762   87.623  56.296  1.00 222.10 ? 782  ARG B CG  1 
ATOM   20308 C  CD  . ARG C 1 782  ? 13.416   88.814  55.586  1.00 229.77 ? 782  ARG B CD  1 
ATOM   20309 N  NE  . ARG C 1 782  ? 14.871   88.834  55.737  1.00 236.32 ? 782  ARG B NE  1 
ATOM   20310 C  CZ  . ARG C 1 782  ? 15.676   89.733  55.173  1.00 241.49 ? 782  ARG B CZ  1 
ATOM   20311 N  NH1 . ARG C 1 782  ? 15.175   90.696  54.411  1.00 242.72 ? 782  ARG B NH1 1 
ATOM   20312 N  NH2 . ARG C 1 782  ? 16.989   89.670  55.368  1.00 244.10 ? 782  ARG B NH2 1 
ATOM   20313 N  N   . ARG C 1 783  ? 13.505   82.867  56.117  1.00 202.26 ? 783  ARG B N   1 
ATOM   20314 C  CA  . ARG C 1 783  ? 13.976   81.633  55.483  1.00 199.07 ? 783  ARG B CA  1 
ATOM   20315 C  C   . ARG C 1 783  ? 14.436   80.627  56.526  1.00 194.27 ? 783  ARG B C   1 
ATOM   20316 O  O   . ARG C 1 783  ? 14.918   81.003  57.590  1.00 194.64 ? 783  ARG B O   1 
ATOM   20317 C  CB  . ARG C 1 783  ? 15.162   81.906  54.553  1.00 202.16 ? 783  ARG B CB  1 
ATOM   20318 C  CG  . ARG C 1 783  ? 14.822   82.406  53.168  1.00 203.32 ? 783  ARG B CG  1 
ATOM   20319 C  CD  . ARG C 1 783  ? 16.038   83.075  52.549  1.00 206.65 ? 783  ARG B CD  1 
ATOM   20320 N  NE  . ARG C 1 783  ? 15.658   84.283  51.822  1.00 208.27 ? 783  ARG B NE  1 
ATOM   20321 C  CZ  . ARG C 1 783  ? 16.477   85.302  51.570  1.00 209.96 ? 783  ARG B CZ  1 
ATOM   20322 N  NH1 . ARG C 1 783  ? 17.736   85.263  51.991  1.00 211.40 ? 783  ARG B NH1 1 
ATOM   20323 N  NH2 . ARG C 1 783  ? 16.033   86.364  50.902  1.00 209.85 ? 783  ARG B NH2 1 
ATOM   20324 N  N   . LYS C 1 784  ? 14.284   79.349  56.204  1.00 189.34 ? 784  LYS B N   1 
ATOM   20325 C  CA  . LYS C 1 784  ? 14.881   78.254  56.963  1.00 185.55 ? 784  LYS B CA  1 
ATOM   20326 C  C   . LYS C 1 784  ? 14.461   76.964  56.294  1.00 182.75 ? 784  LYS B C   1 
ATOM   20327 O  O   . LYS C 1 784  ? 13.311   76.813  55.898  1.00 181.99 ? 784  LYS B O   1 
ATOM   20328 C  CB  . LYS C 1 784  ? 14.447   78.245  58.433  1.00 183.15 ? 784  LYS B CB  1 
ATOM   20329 C  CG  . LYS C 1 784  ? 15.220   77.227  59.300  1.00 182.21 ? 784  LYS B CG  1 
ATOM   20330 C  CD  . LYS C 1 784  ? 14.876   77.316  60.804  1.00 179.67 ? 784  LYS B CD  1 
ATOM   20331 C  CE  . LYS C 1 784  ? 15.745   76.374  61.664  1.00 178.38 ? 784  LYS B CE  1 
ATOM   20332 N  NZ  . LYS C 1 784  ? 15.446   76.445  63.133  1.00 176.38 ? 784  LYS B NZ  1 
ATOM   20333 N  N   . GLN C 1 785  ? 15.396   76.032  56.177  1.00 181.70 ? 785  GLN B N   1 
ATOM   20334 C  CA  . GLN C 1 785  ? 15.165   74.792  55.451  1.00 179.07 ? 785  GLN B CA  1 
ATOM   20335 C  C   . GLN C 1 785  ? 15.691   73.640  56.280  1.00 175.99 ? 785  GLN B C   1 
ATOM   20336 O  O   . GLN C 1 785  ? 16.801   73.709  56.797  1.00 175.89 ? 785  GLN B O   1 
ATOM   20337 C  CB  . GLN C 1 785  ? 15.900   74.839  54.120  1.00 181.76 ? 785  GLN B CB  1 
ATOM   20338 C  CG  . GLN C 1 785  ? 15.975   73.515  53.414  1.00 184.54 ? 785  GLN B CG  1 
ATOM   20339 C  CD  . GLN C 1 785  ? 16.896   73.575  52.224  1.00 188.78 ? 785  GLN B CD  1 
ATOM   20340 O  OE1 . GLN C 1 785  ? 17.947   74.213  52.277  1.00 191.44 ? 785  GLN B OE1 1 
ATOM   20341 N  NE2 . GLN C 1 785  ? 16.510   72.915  51.138  1.00 189.81 ? 785  GLN B NE2 1 
ATOM   20342 N  N   . LEU C 1 786  ? 14.913   72.575  56.410  1.00 174.09 ? 786  LEU B N   1 
ATOM   20343 C  CA  . LEU C 1 786  ? 15.266   71.562  57.394  1.00 174.59 ? 786  LEU B CA  1 
ATOM   20344 C  C   . LEU C 1 786  ? 14.945   70.148  56.954  1.00 176.61 ? 786  LEU B C   1 
ATOM   20345 O  O   . LEU C 1 786  ? 13.951   69.566  57.374  1.00 177.31 ? 786  LEU B O   1 
ATOM   20346 C  CB  . LEU C 1 786  ? 14.601   71.860  58.741  1.00 170.69 ? 786  LEU B CB  1 
ATOM   20347 C  CG  . LEU C 1 786  ? 13.116   72.214  58.719  1.00 165.03 ? 786  LEU B CG  1 
ATOM   20348 C  CD1 . LEU C 1 786  ? 12.558   72.362  60.120  1.00 162.70 ? 786  LEU B CD1 1 
ATOM   20349 C  CD2 . LEU C 1 786  ? 12.908   73.485  57.941  1.00 164.06 ? 786  LEU B CD2 1 
ATOM   20350 N  N   . GLN C 1 787  ? 15.828   69.586  56.141  1.00 178.23 ? 787  GLN B N   1 
ATOM   20351 C  CA  . GLN C 1 787  ? 15.636   68.250  55.601  1.00 178.23 ? 787  GLN B CA  1 
ATOM   20352 C  C   . GLN C 1 787  ? 15.287   67.194  56.663  1.00 174.09 ? 787  GLN B C   1 
ATOM   20353 O  O   . GLN C 1 787  ? 15.428   67.419  57.871  1.00 172.59 ? 787  GLN B O   1 
ATOM   20354 C  CB  . GLN C 1 787  ? 16.862   67.825  54.778  1.00 184.74 ? 787  GLN B CB  1 
ATOM   20355 C  CG  . GLN C 1 787  ? 18.188   67.916  55.521  1.00 191.32 ? 787  GLN B CG  1 
ATOM   20356 C  CD  . GLN C 1 787  ? 19.378   67.793  54.592  1.00 197.99 ? 787  GLN B CD  1 
ATOM   20357 O  OE1 . GLN C 1 787  ? 20.429   67.269  54.972  1.00 201.70 ? 787  GLN B OE1 1 
ATOM   20358 N  NE2 . GLN C 1 787  ? 19.217   68.269  53.361  1.00 199.41 ? 787  GLN B NE2 1 
ATOM   20359 N  N   . PHE C 1 788  ? 14.811   66.053  56.166  1.00 171.03 ? 788  PHE B N   1 
ATOM   20360 C  CA  . PHE C 1 788  ? 14.447   64.874  56.949  1.00 166.14 ? 788  PHE B CA  1 
ATOM   20361 C  C   . PHE C 1 788  ? 13.814   63.882  55.968  1.00 163.26 ? 788  PHE B C   1 
ATOM   20362 O  O   . PHE C 1 788  ? 13.253   64.298  54.958  1.00 164.71 ? 788  PHE B O   1 
ATOM   20363 C  CB  . PHE C 1 788  ? 13.472   65.244  58.071  1.00 161.91 ? 788  PHE B CB  1 
ATOM   20364 C  CG  . PHE C 1 788  ? 12.197   65.907  57.594  1.00 157.14 ? 788  PHE B CG  1 
ATOM   20365 C  CD1 . PHE C 1 788  ? 11.121   65.147  57.152  1.00 155.03 ? 788  PHE B CD1 1 
ATOM   20366 C  CD2 . PHE C 1 788  ? 12.059   67.282  57.616  1.00 154.58 ? 788  PHE B CD2 1 
ATOM   20367 C  CE1 . PHE C 1 788  ? 9.945    65.749  56.727  1.00 151.36 ? 788  PHE B CE1 1 
ATOM   20368 C  CE2 . PHE C 1 788  ? 10.878   67.883  57.193  1.00 151.39 ? 788  PHE B CE2 1 
ATOM   20369 C  CZ  . PHE C 1 788  ? 9.828    67.115  56.752  1.00 149.83 ? 788  PHE B CZ  1 
ATOM   20370 N  N   . ALA C 1 789  ? 13.919   62.582  56.215  1.00 158.20 ? 789  ALA B N   1 
ATOM   20371 C  CA  . ALA C 1 789  ? 13.196   61.637  55.363  1.00 153.39 ? 789  ALA B CA  1 
ATOM   20372 C  C   . ALA C 1 789  ? 11.856   61.287  55.996  1.00 148.34 ? 789  ALA B C   1 
ATOM   20373 O  O   . ALA C 1 789  ? 11.773   61.064  57.203  1.00 147.33 ? 789  ALA B O   1 
ATOM   20374 C  CB  . ALA C 1 789  ? 14.018   60.387  55.105  1.00 155.26 ? 789  ALA B CB  1 
ATOM   20375 N  N   . LEU C 1 790  ? 10.796   61.260  55.201  1.00 146.24 ? 790  LEU B N   1 
ATOM   20376 C  CA  . LEU C 1 790  ? 9.478    61.028  55.780  1.00 144.55 ? 790  LEU B CA  1 
ATOM   20377 C  C   . LEU C 1 790  ? 9.237    59.551  56.090  1.00 148.05 ? 790  LEU B C   1 
ATOM   20378 O  O   . LEU C 1 790  ? 9.891    58.682  55.520  1.00 146.62 ? 790  LEU B O   1 
ATOM   20379 C  CB  . LEU C 1 790  ? 8.363    61.675  54.947  1.00 140.89 ? 790  LEU B CB  1 
ATOM   20380 C  CG  . LEU C 1 790  ? 8.771    62.379  53.656  1.00 138.38 ? 790  LEU B CG  1 
ATOM   20381 C  CD1 . LEU C 1 790  ? 8.852    61.389  52.508  1.00 139.65 ? 790  LEU B CD1 1 
ATOM   20382 C  CD2 . LEU C 1 790  ? 7.806    63.478  53.306  1.00 134.82 ? 790  LEU B CD2 1 
ATOM   20383 N  N   . PRO C 1 791  ? 8.299    59.273  57.007  1.00 153.44 ? 791  PRO B N   1 
ATOM   20384 C  CA  . PRO C 1 791  ? 8.178    57.970  57.669  1.00 160.50 ? 791  PRO B CA  1 
ATOM   20385 C  C   . PRO C 1 791  ? 7.800    56.873  56.713  1.00 168.99 ? 791  PRO B C   1 
ATOM   20386 O  O   . PRO C 1 791  ? 6.956    57.084  55.849  1.00 171.85 ? 791  PRO B O   1 
ATOM   20387 C  CB  . PRO C 1 791  ? 7.011    58.167  58.639  1.00 157.65 ? 791  PRO B CB  1 
ATOM   20388 C  CG  . PRO C 1 791  ? 6.719    59.635  58.642  1.00 154.51 ? 791  PRO B CG  1 
ATOM   20389 C  CD  . PRO C 1 791  ? 7.174    60.160  57.338  1.00 152.80 ? 791  PRO B CD  1 
ATOM   20390 N  N   . ASP C 1 792  ? 8.403    55.707  56.884  1.00 174.72 ? 792  ASP B N   1 
ATOM   20391 C  CA  . ASP C 1 792  ? 7.997    54.538  56.129  1.00 181.59 ? 792  ASP B CA  1 
ATOM   20392 C  C   . ASP C 1 792  ? 6.529    54.268  56.441  1.00 176.05 ? 792  ASP B C   1 
ATOM   20393 O  O   . ASP C 1 792  ? 6.231    53.608  57.430  1.00 174.43 ? 792  ASP B O   1 
ATOM   20394 C  CB  . ASP C 1 792  ? 8.861    53.329  56.537  1.00 196.02 ? 792  ASP B CB  1 
ATOM   20395 C  CG  . ASP C 1 792  ? 8.623    52.088  55.661  1.00 209.89 ? 792  ASP B CG  1 
ATOM   20396 O  OD1 . ASP C 1 792  ? 7.578    52.013  54.973  1.00 217.15 ? 792  ASP B OD1 1 
ATOM   20397 O  OD2 . ASP C 1 792  ? 9.492    51.181  55.672  1.00 216.44 ? 792  ASP B OD2 1 
ATOM   20398 N  N   . SER C 1 793  ? 5.612    54.778  55.618  1.00 171.34 ? 793  SER B N   1 
ATOM   20399 C  CA  . SER C 1 793  ? 4.196    54.453  55.792  1.00 165.06 ? 793  SER B CA  1 
ATOM   20400 C  C   . SER C 1 793  ? 3.265    55.039  54.751  1.00 157.46 ? 793  SER B C   1 
ATOM   20401 O  O   . SER C 1 793  ? 3.338    56.225  54.432  1.00 156.74 ? 793  SER B O   1 
ATOM   20402 C  CB  . SER C 1 793  ? 3.694    54.886  57.158  1.00 162.86 ? 793  SER B CB  1 
ATOM   20403 O  OG  . SER C 1 793  ? 2.299    54.691  57.235  1.00 160.07 ? 793  SER B OG  1 
ATOM   20404 N  N   . LEU C 1 794  ? 2.372    54.187  54.251  1.00 151.25 ? 794  LEU B N   1 
ATOM   20405 C  CA  . LEU C 1 794  ? 1.315    54.574  53.321  1.00 144.49 ? 794  LEU B CA  1 
ATOM   20406 C  C   . LEU C 1 794  ? 0.391    55.575  53.986  1.00 142.58 ? 794  LEU B C   1 
ATOM   20407 O  O   . LEU C 1 794  ? -0.604   55.175  54.583  1.00 144.92 ? 794  LEU B O   1 
ATOM   20408 C  CB  . LEU C 1 794  ? 0.454    53.357  52.964  1.00 142.95 ? 794  LEU B CB  1 
ATOM   20409 C  CG  . LEU C 1 794  ? 0.811    52.338  51.878  1.00 145.32 ? 794  LEU B CG  1 
ATOM   20410 C  CD1 . LEU C 1 794  ? 2.312    52.087  51.795  1.00 146.60 ? 794  LEU B CD1 1 
ATOM   20411 C  CD2 . LEU C 1 794  ? 0.016    51.024  52.076  1.00 146.70 ? 794  LEU B CD2 1 
ATOM   20412 N  N   . THR C 1 795  ? 0.688    56.866  53.861  1.00 138.85 ? 795  THR B N   1 
ATOM   20413 C  CA  . THR C 1 795  ? -0.163   57.918  54.428  1.00 134.09 ? 795  THR B CA  1 
ATOM   20414 C  C   . THR C 1 795  ? -0.065   59.214  53.604  1.00 130.12 ? 795  THR B C   1 
ATOM   20415 O  O   . THR C 1 795  ? 1.010    59.553  53.115  1.00 127.82 ? 795  THR B O   1 
ATOM   20416 C  CB  . THR C 1 795  ? 0.196    58.196  55.915  1.00 189.76 ? 795  THR B CB  1 
ATOM   20417 O  OG1 . THR C 1 795  ? 1.576    57.891  56.145  1.00 190.71 ? 795  THR B OG1 1 
ATOM   20418 C  CG2 . THR C 1 795  ? -0.653   57.343  56.846  1.00 189.71 ? 795  THR B CG2 1 
ATOM   20419 N  N   . THR C 1 796  ? -1.178   59.922  53.417  1.00 129.56 ? 796  THR B N   1 
ATOM   20420 C  CA  . THR C 1 796  ? -1.099   61.250  52.814  1.00 128.56 ? 796  THR B CA  1 
ATOM   20421 C  C   . THR C 1 796  ? -0.877   62.299  53.878  1.00 130.41 ? 796  THR B C   1 
ATOM   20422 O  O   . THR C 1 796  ? -1.817   62.773  54.507  1.00 132.03 ? 796  THR B O   1 
ATOM   20423 C  CB  . THR C 1 796  ? -2.340   61.639  52.064  1.00 125.61 ? 796  THR B CB  1 
ATOM   20424 O  OG1 . THR C 1 796  ? -2.547   60.726  50.984  1.00 126.91 ? 796  THR B OG1 1 
ATOM   20425 C  CG2 . THR C 1 796  ? -2.155   63.044  51.507  1.00 123.80 ? 796  THR B CG2 1 
ATOM   20426 N  N   . TRP C 1 797  ? 0.381    62.658  54.078  1.00 130.88 ? 797  TRP B N   1 
ATOM   20427 C  CA  . TRP C 1 797  ? 0.743    63.568  55.148  1.00 128.54 ? 797  TRP B CA  1 
ATOM   20428 C  C   . TRP C 1 797  ? 0.312    64.972  54.784  1.00 122.71 ? 797  TRP B C   1 
ATOM   20429 O  O   . TRP C 1 797  ? 0.955    65.624  53.962  1.00 122.45 ? 797  TRP B O   1 
ATOM   20430 C  CB  . TRP C 1 797  ? 2.259    63.564  55.364  1.00 132.51 ? 797  TRP B CB  1 
ATOM   20431 C  CG  . TRP C 1 797  ? 2.820    62.311  55.951  1.00 138.04 ? 797  TRP B CG  1 
ATOM   20432 C  CD1 . TRP C 1 797  ? 3.865    61.581  55.471  1.00 142.15 ? 797  TRP B CD1 1 
ATOM   20433 C  CD2 . TRP C 1 797  ? 2.378    61.649  57.134  1.00 141.51 ? 797  TRP B CD2 1 
ATOM   20434 N  NE1 . TRP C 1 797  ? 4.101    60.504  56.282  1.00 145.27 ? 797  TRP B NE1 1 
ATOM   20435 C  CE2 . TRP C 1 797  ? 3.200    60.523  57.313  1.00 144.78 ? 797  TRP B CE2 1 
ATOM   20436 C  CE3 . TRP C 1 797  ? 1.366    61.898  58.059  1.00 141.90 ? 797  TRP B CE3 1 
ATOM   20437 C  CZ2 . TRP C 1 797  ? 3.044    59.649  58.379  1.00 146.26 ? 797  TRP B CZ2 1 
ATOM   20438 C  CZ3 . TRP C 1 797  ? 1.212    61.034  59.111  1.00 144.00 ? 797  TRP B CZ3 1 
ATOM   20439 C  CH2 . TRP C 1 797  ? 2.047    59.921  59.267  1.00 145.73 ? 797  TRP B CH2 1 
ATOM   20440 N  N   . GLU C 1 798  ? -0.771   65.455  55.374  1.00 118.62 ? 798  GLU B N   1 
ATOM   20441 C  CA  . GLU C 1 798  ? -1.039   66.869  55.222  1.00 116.26 ? 798  GLU B CA  1 
ATOM   20442 C  C   . GLU C 1 798  ? -0.181   67.630  56.217  1.00 115.20 ? 798  GLU B C   1 
ATOM   20443 O  O   . GLU C 1 798  ? -0.434   67.593  57.412  1.00 114.43 ? 798  GLU B O   1 
ATOM   20444 C  CB  . GLU C 1 798  ? -2.496   67.204  55.455  1.00 115.82 ? 798  GLU B CB  1 
ATOM   20445 C  CG  . GLU C 1 798  ? -2.670   68.683  55.629  1.00 116.63 ? 798  GLU B CG  1 
ATOM   20446 C  CD  . GLU C 1 798  ? -4.107   69.068  55.714  1.00 119.00 ? 798  GLU B CD  1 
ATOM   20447 O  OE1 . GLU C 1 798  ? -4.962   68.216  55.391  1.00 120.52 ? 798  GLU B OE1 1 
ATOM   20448 O  OE2 . GLU C 1 798  ? -4.383   70.221  56.105  1.00 119.46 ? 798  GLU B OE2 1 
ATOM   20449 N  N   . ILE C 1 799  ? 0.842    68.315  55.736  1.00 116.62 ? 799  ILE B N   1 
ATOM   20450 C  CA  . ILE C 1 799  ? 1.734    69.015  56.643  1.00 117.86 ? 799  ILE B CA  1 
ATOM   20451 C  C   . ILE C 1 799  ? 1.423    70.521  56.691  1.00 119.97 ? 799  ILE B C   1 
ATOM   20452 O  O   . ILE C 1 799  ? 1.903    71.315  55.882  1.00 119.56 ? 799  ILE B O   1 
ATOM   20453 C  CB  . ILE C 1 799  ? 3.218    68.628  56.353  1.00 106.45 ? 799  ILE B CB  1 
ATOM   20454 C  CG1 . ILE C 1 799  ? 4.216    69.655  56.851  1.00 106.82 ? 799  ILE B CG1 1 
ATOM   20455 C  CG2 . ILE C 1 799  ? 3.446    68.440  54.886  1.00 106.73 ? 799  ILE B CG2 1 
ATOM   20456 C  CD1 . ILE C 1 799  ? 5.597    69.421  56.257  1.00 107.83 ? 799  ILE B CD1 1 
ATOM   20457 N  N   . GLN C 1 800  ? 0.561    70.880  57.637  1.00 121.29 ? 800  GLN B N   1 
ATOM   20458 C  CA  . GLN C 1 800  ? 0.187    72.267  57.906  1.00 123.26 ? 800  GLN B CA  1 
ATOM   20459 C  C   . GLN C 1 800  ? 1.269    72.985  58.727  1.00 123.40 ? 800  GLN B C   1 
ATOM   20460 O  O   . GLN C 1 800  ? 2.183    72.349  59.254  1.00 123.48 ? 800  GLN B O   1 
ATOM   20461 C  CB  . GLN C 1 800  ? -1.175   72.319  58.620  1.00 123.69 ? 800  GLN B CB  1 
ATOM   20462 C  CG  . GLN C 1 800  ? -1.228   71.561  59.958  1.00 125.61 ? 800  GLN B CG  1 
ATOM   20463 C  CD  . GLN C 1 800  ? -2.423   70.599  60.077  1.00 126.58 ? 800  GLN B CD  1 
ATOM   20464 O  OE1 . GLN C 1 800  ? -2.817   69.971  59.098  1.00 127.93 ? 800  GLN B OE1 1 
ATOM   20465 N  NE2 . GLN C 1 800  ? -2.983   70.470  61.284  1.00 125.57 ? 800  GLN B NE2 1 
ATOM   20466 N  N   . GLY C 1 801  ? 1.172    74.309  58.824  1.00 123.17 ? 801  GLY B N   1 
ATOM   20467 C  CA  . GLY C 1 801  ? 2.171    75.093  59.535  1.00 123.64 ? 801  GLY B CA  1 
ATOM   20468 C  C   . GLY C 1 801  ? 1.770    76.544  59.763  1.00 123.41 ? 801  GLY B C   1 
ATOM   20469 O  O   . GLY C 1 801  ? 2.030    77.408  58.941  1.00 122.47 ? 801  GLY B O   1 
ATOM   20470 N  N   . ILE C 1 802  ? 1.133    76.806  60.894  1.00 126.20 ? 802  ILE B N   1 
ATOM   20471 C  CA  . ILE C 1 802  ? 0.760    78.151  61.304  1.00 126.95 ? 802  ILE B CA  1 
ATOM   20472 C  C   . ILE C 1 802  ? 2.007    78.937  61.712  1.00 127.24 ? 802  ILE B C   1 
ATOM   20473 O  O   . ILE C 1 802  ? 3.033    78.350  62.057  1.00 131.75 ? 802  ILE B O   1 
ATOM   20474 C  CB  . ILE C 1 802  ? -0.225   78.054  62.486  1.00 127.54 ? 802  ILE B CB  1 
ATOM   20475 C  CG1 . ILE C 1 802  ? 0.153    78.987  63.627  1.00 128.58 ? 802  ILE B CG1 1 
ATOM   20476 C  CG2 . ILE C 1 802  ? -0.212   76.653  63.060  1.00 128.69 ? 802  ILE B CG2 1 
ATOM   20477 C  CD1 . ILE C 1 802  ? -0.721   80.193  63.738  1.00 129.08 ? 802  ILE B CD1 1 
ATOM   20478 N  N   . GLY C 1 803  ? 1.921    80.264  61.678  1.00 123.35 ? 803  GLY B N   1 
ATOM   20479 C  CA  . GLY C 1 803  ? 2.982    81.107  62.216  1.00 122.26 ? 803  GLY B CA  1 
ATOM   20480 C  C   . GLY C 1 803  ? 2.455    82.283  63.036  1.00 123.96 ? 803  GLY B C   1 
ATOM   20481 O  O   . GLY C 1 803  ? 1.364    82.790  62.785  1.00 121.76 ? 803  GLY B O   1 
ATOM   20482 N  N   . ILE C 1 804  ? 3.211    82.722  64.035  1.00 128.32 ? 804  ILE B N   1 
ATOM   20483 C  CA  . ILE C 1 804  ? 2.823    83.923  64.749  1.00 127.44 ? 804  ILE B CA  1 
ATOM   20484 C  C   . ILE C 1 804  ? 4.003    84.798  65.066  1.00 129.98 ? 804  ILE B C   1 
ATOM   20485 O  O   . ILE C 1 804  ? 5.059    84.321  65.491  1.00 126.46 ? 804  ILE B O   1 
ATOM   20486 C  CB  . ILE C 1 804  ? 2.005    83.648  66.010  1.00 121.59 ? 804  ILE B CB  1 
ATOM   20487 C  CG1 . ILE C 1 804  ? 2.760    82.764  66.975  1.00 118.95 ? 804  ILE B CG1 1 
ATOM   20488 C  CG2 . ILE C 1 804  ? 0.711    82.952  65.664  1.00 117.87 ? 804  ILE B CG2 1 
ATOM   20489 C  CD1 . ILE C 1 804  ? 1.819    82.145  68.000  1.00 117.15 ? 804  ILE B CD1 1 
ATOM   20490 N  N   . SER C 1 805  ? 3.785    86.087  64.814  1.00 137.87 ? 805  SER B N   1 
ATOM   20491 C  CA  . SER C 1 805  ? 4.754    87.144  65.041  1.00 141.71 ? 805  SER B CA  1 
ATOM   20492 C  C   . SER C 1 805  ? 4.045    88.462  65.292  1.00 148.87 ? 805  SER B C   1 
ATOM   20493 O  O   . SER C 1 805  ? 2.850    88.492  65.538  1.00 146.99 ? 805  SER B O   1 
ATOM   20494 C  CB  . SER C 1 805  ? 5.732    87.267  63.871  1.00 144.65 ? 805  SER B CB  1 
ATOM   20495 O  OG  . SER C 1 805  ? 6.878    86.448  64.089  1.00 144.81 ? 805  SER B OG  1 
ATOM   20496 N  N   . ASN C 1 806  ? 4.790    89.554  65.238  1.00 154.76 ? 806  ASN B N   1 
ATOM   20497 C  CA  . ASN C 1 806  ? 4.271    90.837  65.698  1.00 164.16 ? 806  ASN B CA  1 
ATOM   20498 C  C   . ASN C 1 806  ? 3.175    91.431  64.814  1.00 166.86 ? 806  ASN B C   1 
ATOM   20499 O  O   . ASN C 1 806  ? 2.636    92.500  65.087  1.00 166.81 ? 806  ASN B O   1 
ATOM   20500 C  CB  . ASN C 1 806  ? 5.420    91.821  65.914  1.00 170.74 ? 806  ASN B CB  1 
ATOM   20501 C  CG  . ASN C 1 806  ? 6.291    91.434  67.100  1.00 177.26 ? 806  ASN B CG  1 
ATOM   20502 O  OD1 . ASN C 1 806  ? 7.460    91.085  66.940  1.00 179.14 ? 806  ASN B OD1 1 
ATOM   20503 N  ND2 . ASN C 1 806  ? 5.711    91.466  68.297  1.00 179.71 ? 806  ASN B ND2 1 
ATOM   20504 N  N   . THR C 1 807  ? 2.841    90.723  63.752  1.00 167.59 ? 807  THR B N   1 
ATOM   20505 C  CA  . THR C 1 807  ? 1.750    91.140  62.904  1.00 166.50 ? 807  THR B CA  1 
ATOM   20506 C  C   . THR C 1 807  ? 0.442    90.491  63.377  1.00 161.46 ? 807  THR B C   1 
ATOM   20507 O  O   . THR C 1 807  ? -0.636   91.076  63.246  1.00 164.03 ? 807  THR B O   1 
ATOM   20508 C  CB  . THR C 1 807  ? 2.067    90.776  61.453  1.00 169.10 ? 807  THR B CB  1 
ATOM   20509 O  OG1 . THR C 1 807  ? 2.461    89.398  61.387  1.00 169.74 ? 807  THR B OG1 1 
ATOM   20510 C  CG2 . THR C 1 807  ? 3.225    91.630  60.950  1.00 169.79 ? 807  THR B CG2 1 
ATOM   20511 N  N   . GLY C 1 808  ? 0.563    89.285  63.943  1.00 153.14 ? 808  GLY B N   1 
ATOM   20512 C  CA  . GLY C 1 808  ? -0.571   88.441  64.318  1.00 146.29 ? 808  GLY B CA  1 
ATOM   20513 C  C   . GLY C 1 808  ? -0.416   86.952  63.961  1.00 142.82 ? 808  GLY B C   1 
ATOM   20514 O  O   . GLY C 1 808  ? 0.698    86.445  63.790  1.00 140.55 ? 808  GLY B O   1 
ATOM   20515 N  N   . ILE C 1 809  ? -1.543   86.250  63.844  1.00 141.25 ? 809  ILE B N   1 
ATOM   20516 C  CA  . ILE C 1 809  ? -1.567   84.836  63.469  1.00 138.16 ? 809  ILE B CA  1 
ATOM   20517 C  C   . ILE C 1 809  ? -1.836   84.628  61.978  1.00 138.29 ? 809  ILE B C   1 
ATOM   20518 O  O   . ILE C 1 809  ? -2.808   85.171  61.457  1.00 141.07 ? 809  ILE B O   1 
ATOM   20519 C  CB  . ILE C 1 809  ? -2.693   84.130  64.205  1.00 134.37 ? 809  ILE B CB  1 
ATOM   20520 C  CG1 . ILE C 1 809  ? -2.972   82.776  63.569  1.00 131.43 ? 809  ILE B CG1 1 
ATOM   20521 C  CG2 . ILE C 1 809  ? -3.963   84.958  64.141  1.00 133.13 ? 809  ILE B CG2 1 
ATOM   20522 C  CD1 . ILE C 1 809  ? -4.244   82.137  64.071  1.00 130.12 ? 809  ILE B CD1 1 
ATOM   20523 N  N   . CYS C 1 810  ? -1.008   83.819  61.306  1.00 135.67 ? 810  CYS B N   1 
ATOM   20524 C  CA  . CYS C 1 810  ? -1.181   83.511  59.867  1.00 132.81 ? 810  CYS B CA  1 
ATOM   20525 C  C   . CYS C 1 810  ? -0.903   82.048  59.499  1.00 133.40 ? 810  CYS B C   1 
ATOM   20526 O  O   . CYS C 1 810  ? 0.237    81.670  59.204  1.00 132.09 ? 810  CYS B O   1 
ATOM   20527 C  CB  . CYS C 1 810  ? -0.311   84.423  58.977  1.00 131.59 ? 810  CYS B CB  1 
ATOM   20528 S  SG  . CYS C 1 810  ? -0.456   84.145  57.159  1.00 163.28 ? 810  CYS B SG  1 
ATOM   20529 N  N   . VAL C 1 811  ? -1.964   81.245  59.506  1.00 134.60 ? 811  VAL B N   1 
ATOM   20530 C  CA  . VAL C 1 811  ? -1.934   79.889  58.982  1.00 134.83 ? 811  VAL B CA  1 
ATOM   20531 C  C   . VAL C 1 811  ? -1.582   79.907  57.509  1.00 134.61 ? 811  VAL B C   1 
ATOM   20532 O  O   . VAL C 1 811  ? -2.096   80.728  56.746  1.00 135.44 ? 811  VAL B O   1 
ATOM   20533 C  CB  . VAL C 1 811  ? -3.308   79.273  59.041  1.00 133.82 ? 811  VAL B CB  1 
ATOM   20534 C  CG1 . VAL C 1 811  ? -3.230   77.835  58.588  1.00 135.47 ? 811  VAL B CG1 1 
ATOM   20535 C  CG2 . VAL C 1 811  ? -3.885   79.401  60.433  1.00 133.42 ? 811  VAL B CG2 1 
ATOM   20536 N  N   . ALA C 1 812  ? -0.721   78.994  57.093  1.00 132.88 ? 812  ALA B N   1 
ATOM   20537 C  CA  . ALA C 1 812  ? -0.334   78.975  55.697  1.00 132.67 ? 812  ALA B CA  1 
ATOM   20538 C  C   . ALA C 1 812  ? -1.102   77.932  54.936  1.00 129.74 ? 812  ALA B C   1 
ATOM   20539 O  O   . ALA C 1 812  ? -1.727   77.039  55.510  1.00 130.24 ? 812  ALA B O   1 
ATOM   20540 C  CB  . ALA C 1 812  ? 1.148    78.751  55.537  1.00 133.73 ? 812  ALA B CB  1 
ATOM   20541 N  N   . ASP C 1 813  ? -1.041   78.064  53.621  1.00 129.04 ? 813  ASP B N   1 
ATOM   20542 C  CA  . ASP C 1 813  ? -1.681   77.118  52.750  1.00 127.01 ? 813  ASP B CA  1 
ATOM   20543 C  C   . ASP C 1 813  ? -0.959   75.806  53.002  1.00 121.99 ? 813  ASP B C   1 
ATOM   20544 O  O   . ASP C 1 813  ? 0.271    75.743  52.972  1.00 121.08 ? 813  ASP B O   1 
ATOM   20545 C  CB  . ASP C 1 813  ? -1.593   77.609  51.300  1.00 131.36 ? 813  ASP B CB  1 
ATOM   20546 C  CG  . ASP C 1 813  ? -2.294   78.976  51.093  1.00 134.63 ? 813  ASP B CG  1 
ATOM   20547 O  OD1 . ASP C 1 813  ? -3.552   79.030  51.168  1.00 134.61 ? 813  ASP B OD1 1 
ATOM   20548 O  OD2 . ASP C 1 813  ? -1.585   79.992  50.857  1.00 135.34 ? 813  ASP B OD2 1 
ATOM   20549 N  N   . THR C 1 814  ? -1.743   74.781  53.311  1.00 119.95 ? 814  THR B N   1 
ATOM   20550 C  CA  . THR C 1 814  ? -1.249   73.461  53.679  1.00 118.31 ? 814  THR B CA  1 
ATOM   20551 C  C   . THR C 1 814  ? -0.272   72.945  52.653  1.00 119.56 ? 814  THR B C   1 
ATOM   20552 O  O   . THR C 1 814  ? -0.040   73.600  51.661  1.00 119.26 ? 814  THR B O   1 
ATOM   20553 C  CB  . THR C 1 814  ? -2.416   72.495  53.703  1.00 117.93 ? 814  THR B CB  1 
ATOM   20554 O  OG1 . THR C 1 814  ? -1.936   71.175  53.461  1.00 117.57 ? 814  THR B OG1 1 
ATOM   20555 C  CG2 . THR C 1 814  ? -3.411   72.852  52.606  1.00 117.32 ? 814  THR B CG2 1 
ATOM   20556 N  N   . VAL C 1 815  ? 0.299    71.769  52.869  1.00 121.03 ? 815  VAL B N   1 
ATOM   20557 C  CA  . VAL C 1 815  ? 1.053    71.107  51.801  1.00 123.93 ? 815  VAL B CA  1 
ATOM   20558 C  C   . VAL C 1 815  ? 1.017    69.584  51.913  1.00 124.96 ? 815  VAL B C   1 
ATOM   20559 O  O   . VAL C 1 815  ? 1.875    68.983  52.549  1.00 127.34 ? 815  VAL B O   1 
ATOM   20560 C  CB  . VAL C 1 815  ? 2.518    71.592  51.713  1.00 125.92 ? 815  VAL B CB  1 
ATOM   20561 C  CG1 . VAL C 1 815  ? 3.371    70.606  50.927  1.00 126.60 ? 815  VAL B CG1 1 
ATOM   20562 C  CG2 . VAL C 1 815  ? 2.599    72.980  51.076  1.00 126.66 ? 815  VAL B CG2 1 
ATOM   20563 N  N   . LYS C 1 816  ? 0.019    68.968  51.277  1.00 124.00 ? 816  LYS B N   1 
ATOM   20564 C  CA  . LYS C 1 816  ? -0.134   67.510  51.299  1.00 125.69 ? 816  LYS B CA  1 
ATOM   20565 C  C   . LYS C 1 816  ? 1.158    66.890  50.773  1.00 130.89 ? 816  LYS B C   1 
ATOM   20566 O  O   . LYS C 1 816  ? 1.823    67.459  49.907  1.00 130.88 ? 816  LYS B O   1 
ATOM   20567 C  CB  . LYS C 1 816  ? -1.352   67.037  50.463  1.00 152.24 ? 816  LYS B CB  1 
ATOM   20568 C  CG  . LYS C 1 816  ? -2.776   67.270  51.079  1.00 169.92 ? 816  LYS B CG  1 
ATOM   20569 C  CD  . LYS C 1 816  ? -3.265   68.724  50.887  1.00 168.25 ? 816  LYS B CD  1 
ATOM   20570 C  CE  . LYS C 1 816  ? -4.689   68.985  51.381  1.00 164.95 ? 816  LYS B CE  1 
ATOM   20571 N  NZ  . LYS C 1 816  ? -5.089   70.400  51.103  1.00 162.61 ? 816  LYS B NZ  1 
ATOM   20572 N  N   . ALA C 1 817  ? 1.518    65.728  51.301  1.00 138.39 ? 817  ALA B N   1 
ATOM   20573 C  CA  . ALA C 1 817  ? 2.738    65.064  50.882  1.00 145.29 ? 817  ALA B CA  1 
ATOM   20574 C  C   . ALA C 1 817  ? 2.595    63.559  51.011  1.00 145.77 ? 817  ALA B C   1 
ATOM   20575 O  O   . ALA C 1 817  ? 3.332    62.926  51.760  1.00 147.98 ? 817  ALA B O   1 
ATOM   20576 C  CB  . ALA C 1 817  ? 3.914    65.562  51.693  1.00 149.06 ? 817  ALA B CB  1 
ATOM   20577 N  N   . LYS C 1 818  ? 1.638    62.990  50.281  1.00 144.95 ? 818  LYS B N   1 
ATOM   20578 C  CA  . LYS C 1 818  ? 1.427    61.547  50.306  1.00 145.81 ? 818  LYS B CA  1 
ATOM   20579 C  C   . LYS C 1 818  ? 2.703    60.835  49.908  1.00 145.18 ? 818  LYS B C   1 
ATOM   20580 O  O   . LYS C 1 818  ? 3.322    61.172  48.900  1.00 143.12 ? 818  LYS B O   1 
ATOM   20581 C  CB  . LYS C 1 818  ? 0.282    61.116  49.371  1.00 150.32 ? 818  LYS B CB  1 
ATOM   20582 C  CG  . LYS C 1 818  ? 0.698    60.760  47.932  1.00 156.35 ? 818  LYS B CG  1 
ATOM   20583 C  CD  . LYS C 1 818  ? -0.428   60.065  47.152  1.00 161.89 ? 818  LYS B CD  1 
ATOM   20584 C  CE  . LYS C 1 818  ? -0.147   60.057  45.645  1.00 166.95 ? 818  LYS B CE  1 
ATOM   20585 N  NZ  . LYS C 1 818  ? -1.317   59.639  44.811  1.00 168.38 ? 818  LYS B NZ  1 
ATOM   20586 N  N   . VAL C 1 819  ? 3.108    59.872  50.722  1.00 145.72 ? 819  VAL B N   1 
ATOM   20587 C  CA  . VAL C 1 819  ? 4.179    58.979  50.349  1.00 146.42 ? 819  VAL B CA  1 
ATOM   20588 C  C   . VAL C 1 819  ? 3.525    57.662  50.036  1.00 148.03 ? 819  VAL B C   1 
ATOM   20589 O  O   . VAL C 1 819  ? 2.390    57.421  50.437  1.00 147.07 ? 819  VAL B O   1 
ATOM   20590 C  CB  . VAL C 1 819  ? 5.206    58.811  51.472  1.00 145.54 ? 819  VAL B CB  1 
ATOM   20591 C  CG1 . VAL C 1 819  ? 6.028    60.072  51.614  1.00 144.34 ? 819  VAL B CG1 1 
ATOM   20592 C  CG2 . VAL C 1 819  ? 4.511    58.458  52.788  1.00 143.61 ? 819  VAL B CG2 1 
ATOM   20593 N  N   . PHE C 1 820  ? 4.236    56.813  49.312  1.00 151.76 ? 820  PHE B N   1 
ATOM   20594 C  CA  . PHE C 1 820  ? 3.677    55.525  48.962  1.00 158.12 ? 820  PHE B CA  1 
ATOM   20595 C  C   . PHE C 1 820  ? 4.540    54.718  47.986  1.00 159.03 ? 820  PHE B C   1 
ATOM   20596 O  O   . PHE C 1 820  ? 5.084    55.267  47.027  1.00 157.12 ? 820  PHE B O   1 
ATOM   20597 C  CB  . PHE C 1 820  ? 2.279    55.725  48.396  1.00 165.85 ? 820  PHE B CB  1 
ATOM   20598 C  CG  . PHE C 1 820  ? 1.834    54.611  47.536  1.00 178.90 ? 820  PHE B CG  1 
ATOM   20599 C  CD1 . PHE C 1 820  ? 1.867    54.735  46.160  1.00 185.37 ? 820  PHE B CD1 1 
ATOM   20600 C  CD2 . PHE C 1 820  ? 1.417    53.420  48.102  1.00 184.65 ? 820  PHE B CD2 1 
ATOM   20601 C  CE1 . PHE C 1 820  ? 1.470    53.695  45.363  1.00 190.45 ? 820  PHE B CE1 1 
ATOM   20602 C  CE2 . PHE C 1 820  ? 1.019    52.377  47.320  1.00 189.14 ? 820  PHE B CE2 1 
ATOM   20603 C  CZ  . PHE C 1 820  ? 1.047    52.508  45.945  1.00 191.69 ? 820  PHE B CZ  1 
ATOM   20604 N  N   . LYS C 1 821  ? 4.653    53.415  48.250  1.00 163.60 ? 821  LYS B N   1 
ATOM   20605 C  CA  . LYS C 1 821  ? 5.397    52.493  47.399  1.00 168.30 ? 821  LYS B CA  1 
ATOM   20606 C  C   . LYS C 1 821  ? 4.449    51.754  46.457  1.00 173.57 ? 821  LYS B C   1 
ATOM   20607 O  O   . LYS C 1 821  ? 3.392    51.288  46.873  1.00 172.21 ? 821  LYS B O   1 
ATOM   20608 C  CB  . LYS C 1 821  ? 6.173    51.497  48.255  1.00 166.39 ? 821  LYS B CB  1 
ATOM   20609 C  CG  . LYS C 1 821  ? 6.971    50.456  47.481  1.00 164.74 ? 821  LYS B CG  1 
ATOM   20610 C  CD  . LYS C 1 821  ? 8.486    50.694  47.576  1.00 162.73 ? 821  LYS B CD  1 
ATOM   20611 C  CE  . LYS C 1 821  ? 9.288    49.404  47.283  1.00 162.79 ? 821  LYS B CE  1 
ATOM   20612 N  NZ  . LYS C 1 821  ? 10.783   49.580  47.274  1.00 163.26 ? 821  LYS B NZ  1 
ATOM   20613 N  N   . ASP C 1 822  ? 4.867    51.636  45.196  1.00 153.52 ? 822  ASP B N   1 
ATOM   20614 C  CA  . ASP C 1 822  ? 4.024    51.196  44.071  1.00 158.14 ? 822  ASP B CA  1 
ATOM   20615 C  C   . ASP C 1 822  ? 3.446    49.797  44.229  1.00 157.63 ? 822  ASP B C   1 
ATOM   20616 O  O   . ASP C 1 822  ? 2.224    49.606  44.205  1.00 153.72 ? 822  ASP B O   1 
ATOM   20617 C  CB  . ASP C 1 822  ? 4.834    51.226  42.770  1.00 166.16 ? 822  ASP B CB  1 
ATOM   20618 C  CG  . ASP C 1 822  ? 4.908    52.615  42.146  1.00 175.74 ? 822  ASP B CG  1 
ATOM   20619 O  OD1 . ASP C 1 822  ? 4.789    53.636  42.882  1.00 179.46 ? 822  ASP B OD1 1 
ATOM   20620 O  OD2 . ASP C 1 822  ? 5.100    52.676  40.906  1.00 178.85 ? 822  ASP B OD2 1 
ATOM   20621 N  N   . VAL C 1 823  ? 4.348    48.821  44.332  1.00 160.66 ? 823  VAL B N   1 
ATOM   20622 C  CA  . VAL C 1 823  ? 3.988    47.445  44.646  1.00 159.81 ? 823  VAL B CA  1 
ATOM   20623 C  C   . VAL C 1 823  ? 4.788    46.964  45.842  1.00 164.33 ? 823  VAL B C   1 
ATOM   20624 O  O   . VAL C 1 823  ? 5.998    47.206  45.939  1.00 167.69 ? 823  VAL B O   1 
ATOM   20625 C  CB  . VAL C 1 823  ? 4.252    46.491  43.489  1.00 155.65 ? 823  VAL B CB  1 
ATOM   20626 C  CG1 . VAL C 1 823  ? 4.140    45.061  43.969  1.00 152.67 ? 823  VAL B CG1 1 
ATOM   20627 C  CG2 . VAL C 1 823  ? 3.273    46.748  42.377  1.00 154.05 ? 823  VAL B CG2 1 
ATOM   20628 N  N   . PHE C 1 824  ? 4.101    46.274  46.748  1.00 161.87 ? 824  PHE B N   1 
ATOM   20629 C  CA  . PHE C 1 824  ? 4.717    45.786  47.975  1.00 160.84 ? 824  PHE B CA  1 
ATOM   20630 C  C   . PHE C 1 824  ? 3.970    44.558  48.514  1.00 155.22 ? 824  PHE B C   1 
ATOM   20631 O  O   . PHE C 1 824  ? 2.751    44.442  48.369  1.00 151.79 ? 824  PHE B O   1 
ATOM   20632 C  CB  . PHE C 1 824  ? 4.765    46.902  49.028  1.00 164.08 ? 824  PHE B CB  1 
ATOM   20633 C  CG  . PHE C 1 824  ? 3.420    47.292  49.560  1.00 167.29 ? 824  PHE B CG  1 
ATOM   20634 C  CD1 . PHE C 1 824  ? 2.998    46.851  50.797  1.00 170.04 ? 824  PHE B CD1 1 
ATOM   20635 C  CD2 . PHE C 1 824  ? 2.583    48.099  48.826  1.00 168.60 ? 824  PHE B CD2 1 
ATOM   20636 C  CE1 . PHE C 1 824  ? 1.765    47.209  51.292  1.00 171.39 ? 824  PHE B CE1 1 
ATOM   20637 C  CE2 . PHE C 1 824  ? 1.349    48.458  49.316  1.00 170.19 ? 824  PHE B CE2 1 
ATOM   20638 C  CZ  . PHE C 1 824  ? 0.941    48.013  50.550  1.00 171.08 ? 824  PHE B CZ  1 
ATOM   20639 N  N   . LEU C 1 825  ? 4.710    43.634  49.116  1.00 151.81 ? 825  LEU B N   1 
ATOM   20640 C  CA  . LEU C 1 825  ? 4.084    42.475  49.720  1.00 145.58 ? 825  LEU B CA  1 
ATOM   20641 C  C   . LEU C 1 825  ? 4.046    42.543  51.243  1.00 145.86 ? 825  LEU B C   1 
ATOM   20642 O  O   . LEU C 1 825  ? 4.968    43.058  51.888  1.00 148.27 ? 825  LEU B O   1 
ATOM   20643 C  CB  . LEU C 1 825  ? 4.790    41.201  49.293  1.00 138.42 ? 825  LEU B CB  1 
ATOM   20644 C  CG  . LEU C 1 825  ? 4.497    40.086  50.289  1.00 130.06 ? 825  LEU B CG  1 
ATOM   20645 C  CD1 . LEU C 1 825  ? 3.122    39.484  50.047  1.00 125.00 ? 825  LEU B CD1 1 
ATOM   20646 C  CD2 . LEU C 1 825  ? 5.573    39.036  50.230  1.00 128.83 ? 825  LEU B CD2 1 
ATOM   20647 N  N   . GLU C 1 826  ? 2.966    42.004  51.801  1.00 143.63 ? 826  GLU B N   1 
ATOM   20648 C  CA  . GLU C 1 826  ? 2.847    41.773  53.230  1.00 143.74 ? 826  GLU B CA  1 
ATOM   20649 C  C   . GLU C 1 826  ? 2.574    40.282  53.441  1.00 142.41 ? 826  GLU B C   1 
ATOM   20650 O  O   . GLU C 1 826  ? 1.856    39.649  52.651  1.00 139.16 ? 826  GLU B O   1 
ATOM   20651 C  CB  . GLU C 1 826  ? 1.684    42.583  53.793  1.00 145.41 ? 826  GLU B CB  1 
ATOM   20652 C  CG  . GLU C 1 826  ? 0.335    42.170  53.208  1.00 147.06 ? 826  GLU B CG  1 
ATOM   20653 C  CD  . GLU C 1 826  ? -0.844   42.791  53.925  1.00 150.18 ? 826  GLU B CD  1 
ATOM   20654 O  OE1 . GLU C 1 826  ? -1.918   42.140  53.957  1.00 150.03 ? 826  GLU B OE1 1 
ATOM   20655 O  OE2 . GLU C 1 826  ? -0.693   43.920  54.451  1.00 152.76 ? 826  GLU B OE2 1 
ATOM   20656 N  N   . MET C 1 827  ? 3.160    39.720  54.493  1.00 142.97 ? 827  MET B N   1 
ATOM   20657 C  CA  . MET C 1 827  ? 2.904    38.340  54.867  1.00 140.74 ? 827  MET B CA  1 
ATOM   20658 C  C   . MET C 1 827  ? 2.222    38.325  56.210  1.00 138.64 ? 827  MET B C   1 
ATOM   20659 O  O   . MET C 1 827  ? 2.660    39.011  57.117  1.00 141.68 ? 827  MET B O   1 
ATOM   20660 C  CB  . MET C 1 827  ? 4.222    37.619  55.022  1.00 142.15 ? 827  MET B CB  1 
ATOM   20661 C  CG  . MET C 1 827  ? 5.054    37.600  53.788  1.00 141.49 ? 827  MET B CG  1 
ATOM   20662 S  SD  . MET C 1 827  ? 4.349    36.413  52.657  1.00 127.84 ? 827  MET B SD  1 
ATOM   20663 C  CE  . MET C 1 827  ? 4.030    35.020  53.716  1.00 90.33  ? 827  MET B CE  1 
ATOM   20664 N  N   . ASN C 1 828  ? 1.169    37.537  56.361  1.00 134.40 ? 828  ASN B N   1 
ATOM   20665 C  CA  . ASN C 1 828  ? 0.547    37.416  57.670  1.00 135.91 ? 828  ASN B CA  1 
ATOM   20666 C  C   . ASN C 1 828  ? 1.100    36.255  58.537  1.00 125.46 ? 828  ASN B C   1 
ATOM   20667 O  O   . ASN C 1 828  ? 0.661    35.102  58.405  1.00 125.48 ? 828  ASN B O   1 
ATOM   20668 C  CB  . ASN C 1 828  ? -0.975   37.333  57.542  1.00 140.09 ? 828  ASN B CB  1 
ATOM   20669 C  CG  . ASN C 1 828  ? -1.681   37.832  58.791  1.00 149.03 ? 828  ASN B CG  1 
ATOM   20670 O  OD1 . ASN C 1 828  ? -1.512   38.987  59.180  1.00 152.72 ? 828  ASN B OD1 1 
ATOM   20671 N  ND2 . ASN C 1 828  ? -2.472   36.966  59.427  1.00 151.48 ? 828  ASN B ND2 1 
ATOM   20672 N  N   . ILE C 1 829  ? 2.057    36.565  59.417  1.00 122.12 ? 829  ILE B N   1 
ATOM   20673 C  CA  . ILE C 1 829  ? 2.595    35.590  60.362  1.00 114.06 ? 829  ILE B CA  1 
ATOM   20674 C  C   . ILE C 1 829  ? 1.676    35.574  61.563  1.00 108.49 ? 829  ILE B C   1 
ATOM   20675 O  O   . ILE C 1 829  ? 1.051    36.583  61.874  1.00 109.75 ? 829  ILE B O   1 
ATOM   20676 C  CB  . ILE C 1 829  ? 4.013    35.969  60.795  1.00 111.91 ? 829  ILE B CB  1 
ATOM   20677 C  CG1 . ILE C 1 829  ? 4.810    36.438  59.584  1.00 110.52 ? 829  ILE B CG1 1 
ATOM   20678 C  CG2 . ILE C 1 829  ? 4.724    34.788  61.413  1.00 111.19 ? 829  ILE B CG2 1 
ATOM   20679 C  CD1 . ILE C 1 829  ? 5.078    35.336  58.574  1.00 108.28 ? 829  ILE B CD1 1 
ATOM   20680 N  N   . PRO C 1 830  ? 1.562    34.421  62.229  1.00 102.30 ? 830  PRO B N   1 
ATOM   20681 C  CA  . PRO C 1 830  ? 0.699    34.253  63.393  1.00 107.30 ? 830  PRO B CA  1 
ATOM   20682 C  C   . PRO C 1 830  ? 1.438    34.739  64.595  1.00 123.87 ? 830  PRO B C   1 
ATOM   20683 O  O   . PRO C 1 830  ? 2.633    35.031  64.514  1.00 135.90 ? 830  PRO B O   1 
ATOM   20684 C  CB  . PRO C 1 830  ? 0.587    32.731  63.547  1.00 98.07  ? 830  PRO B CB  1 
ATOM   20685 C  CG  . PRO C 1 830  ? 1.401    32.159  62.463  1.00 94.42  ? 830  PRO B CG  1 
ATOM   20686 C  CD  . PRO C 1 830  ? 2.319    33.200  61.969  1.00 96.84  ? 830  PRO B CD  1 
ATOM   20687 N  N   . TYR C 1 831  ? 0.755    34.818  65.720  1.00 125.01 ? 831  TYR B N   1 
ATOM   20688 C  CA  . TYR C 1 831  ? 1.486    35.030  66.931  1.00 127.29 ? 831  TYR B CA  1 
ATOM   20689 C  C   . TYR C 1 831  ? 2.383    33.824  67.013  1.00 123.97 ? 831  TYR B C   1 
ATOM   20690 O  O   . TYR C 1 831  ? 3.571    33.894  66.742  1.00 125.43 ? 831  TYR B O   1 
ATOM   20691 C  CB  . TYR C 1 831  ? 0.538    35.070  68.114  1.00 132.28 ? 831  TYR B CB  1 
ATOM   20692 C  CG  . TYR C 1 831  ? 1.186    35.434  69.433  1.00 136.72 ? 831  TYR B CG  1 
ATOM   20693 C  CD1 . TYR C 1 831  ? 0.842    34.758  70.595  1.00 138.54 ? 831  TYR B CD1 1 
ATOM   20694 C  CD2 . TYR C 1 831  ? 2.124    36.451  69.519  1.00 139.44 ? 831  TYR B CD2 1 
ATOM   20695 C  CE1 . TYR C 1 831  ? 1.402    35.079  71.793  1.00 141.12 ? 831  TYR B CE1 1 
ATOM   20696 C  CE2 . TYR C 1 831  ? 2.697    36.776  70.720  1.00 142.04 ? 831  TYR B CE2 1 
ATOM   20697 C  CZ  . TYR C 1 831  ? 2.328    36.084  71.857  1.00 143.66 ? 831  TYR B CZ  1 
ATOM   20698 O  OH  . TYR C 1 831  ? 2.884    36.383  73.079  1.00 146.62 ? 831  TYR B OH  1 
ATOM   20699 N  N   . SER C 1 832  ? 1.810    32.684  67.327  1.00 121.50 ? 832  SER B N   1 
ATOM   20700 C  CA  . SER C 1 832  ? 2.679    31.596  67.681  1.00 124.09 ? 832  SER B CA  1 
ATOM   20701 C  C   . SER C 1 832  ? 2.223    30.299  67.071  1.00 122.36 ? 832  SER B C   1 
ATOM   20702 O  O   . SER C 1 832  ? 1.041    30.139  66.770  1.00 120.62 ? 832  SER B O   1 
ATOM   20703 C  CB  . SER C 1 832  ? 2.731    31.467  69.197  1.00 129.39 ? 832  SER B CB  1 
ATOM   20704 O  OG  . SER C 1 832  ? 1.435    31.213  69.706  1.00 130.66 ? 832  SER B OG  1 
ATOM   20705 N  N   . VAL C 1 833  ? 3.183    29.384  66.910  1.00 120.23 ? 833  VAL B N   1 
ATOM   20706 C  CA  . VAL C 1 833  ? 2.954    28.046  66.387  1.00 115.32 ? 833  VAL B CA  1 
ATOM   20707 C  C   . VAL C 1 833  ? 3.637    27.018  67.263  1.00 114.72 ? 833  VAL B C   1 
ATOM   20708 O  O   . VAL C 1 833  ? 4.758    27.228  67.705  1.00 115.29 ? 833  VAL B O   1 
ATOM   20709 C  CB  . VAL C 1 833  ? 3.604    27.878  65.028  1.00 115.09 ? 833  VAL B CB  1 
ATOM   20710 C  CG1 . VAL C 1 833  ? 2.748    26.986  64.167  1.00 112.71 ? 833  VAL B CG1 1 
ATOM   20711 C  CG2 . VAL C 1 833  ? 3.805    29.214  64.374  1.00 114.77 ? 833  VAL B CG2 1 
ATOM   20712 N  N   . VAL C 1 834  ? 2.976    25.892  67.492  1.00 112.58 ? 834  VAL B N   1 
ATOM   20713 C  CA  . VAL C 1 834  ? 3.600    24.773  68.196  1.00 113.62 ? 834  VAL B CA  1 
ATOM   20714 C  C   . VAL C 1 834  ? 4.611    24.016  67.329  1.00 116.31 ? 834  VAL B C   1 
ATOM   20715 O  O   . VAL C 1 834  ? 4.485    23.966  66.106  1.00 115.88 ? 834  VAL B O   1 
ATOM   20716 C  CB  . VAL C 1 834  ? 2.544    23.780  68.692  1.00 110.80 ? 834  VAL B CB  1 
ATOM   20717 C  CG1 . VAL C 1 834  ? 3.183    22.454  69.082  1.00 111.39 ? 834  VAL B CG1 1 
ATOM   20718 C  CG2 . VAL C 1 834  ? 1.755    24.386  69.841  1.00 110.31 ? 834  VAL B CG2 1 
ATOM   20719 N  N   . ARG C 1 835  ? 5.617    23.430  67.968  1.00 121.16 ? 835  ARG B N   1 
ATOM   20720 C  CA  . ARG C 1 835  ? 6.608    22.622  67.268  1.00 125.21 ? 835  ARG B CA  1 
ATOM   20721 C  C   . ARG C 1 835  ? 5.951    21.417  66.601  1.00 125.49 ? 835  ARG B C   1 
ATOM   20722 O  O   . ARG C 1 835  ? 5.184    20.683  67.234  1.00 124.26 ? 835  ARG B O   1 
ATOM   20723 C  CB  . ARG C 1 835  ? 7.723    22.177  68.232  1.00 130.22 ? 835  ARG B CB  1 
ATOM   20724 C  CG  . ARG C 1 835  ? 8.288    20.774  67.962  1.00 133.43 ? 835  ARG B CG  1 
ATOM   20725 C  CD  . ARG C 1 835  ? 9.698    20.567  68.543  1.00 136.82 ? 835  ARG B CD  1 
ATOM   20726 N  NE  . ARG C 1 835  ? 9.793    20.112  69.935  1.00 137.80 ? 835  ARG B NE  1 
ATOM   20727 C  CZ  . ARG C 1 835  ? 8.780    19.788  70.737  1.00 136.37 ? 835  ARG B CZ  1 
ATOM   20728 N  NH1 . ARG C 1 835  ? 7.517    19.857  70.336  1.00 133.96 ? 835  ARG B NH1 1 
ATOM   20729 N  NH2 . ARG C 1 835  ? 9.046    19.389  71.970  1.00 137.17 ? 835  ARG B NH2 1 
ATOM   20730 N  N   . GLY C 1 836  ? 6.252    21.230  65.318  1.00 125.61 ? 836  GLY B N   1 
ATOM   20731 C  CA  . GLY C 1 836  ? 5.737    20.101  64.565  1.00 126.33 ? 836  GLY B CA  1 
ATOM   20732 C  C   . GLY C 1 836  ? 4.262    20.175  64.204  1.00 124.40 ? 836  GLY B C   1 
ATOM   20733 O  O   . GLY C 1 836  ? 3.638    19.134  63.968  1.00 122.63 ? 836  GLY B O   1 
ATOM   20734 N  N   . GLU C 1 837  ? 3.718    21.398  64.213  1.00 125.94 ? 837  GLU B N   1 
ATOM   20735 C  CA  . GLU C 1 837  ? 2.390    21.732  63.708  1.00 124.80 ? 837  GLU B CA  1 
ATOM   20736 C  C   . GLU C 1 837  ? 2.727    22.245  62.313  1.00 128.44 ? 837  GLU B C   1 
ATOM   20737 O  O   . GLU C 1 837  ? 3.689    23.003  62.187  1.00 130.76 ? 837  GLU B O   1 
ATOM   20738 C  CB  . GLU C 1 837  ? 1.811    22.881  64.544  1.00 121.84 ? 837  GLU B CB  1 
ATOM   20739 C  CG  . GLU C 1 837  ? 0.462    22.627  65.249  1.00 116.49 ? 837  GLU B CG  1 
ATOM   20740 C  CD  . GLU C 1 837  ? 0.110    23.705  66.314  1.00 106.64 ? 837  GLU B CD  1 
ATOM   20741 O  OE1 . GLU C 1 837  ? 0.666    24.828  66.246  1.00 107.25 ? 837  GLU B OE1 1 
ATOM   20742 O  OE2 . GLU C 1 837  ? -0.726   23.436  67.219  1.00 104.29 ? 837  GLU B OE2 1 
ATOM   20743 N  N   . GLN C 1 838  ? 1.997    21.827  61.269  1.00 129.06 ? 838  GLN B N   1 
ATOM   20744 C  CA  . GLN C 1 838  ? 2.275    22.279  59.888  1.00 129.45 ? 838  GLN B CA  1 
ATOM   20745 C  C   . GLN C 1 838  ? 1.456    23.518  59.512  1.00 128.15 ? 838  GLN B C   1 
ATOM   20746 O  O   . GLN C 1 838  ? 0.247    23.454  59.360  1.00 125.04 ? 838  GLN B O   1 
ATOM   20747 C  CB  . GLN C 1 838  ? 2.032    21.148  58.889  1.00 129.72 ? 838  GLN B CB  1 
ATOM   20748 C  CG  . GLN C 1 838  ? 2.107    21.536  57.405  1.00 132.19 ? 838  GLN B CG  1 
ATOM   20749 C  CD  . GLN C 1 838  ? 1.364    20.528  56.479  1.00 145.33 ? 838  GLN B CD  1 
ATOM   20750 O  OE1 . GLN C 1 838  ? 1.954    19.542  56.003  1.00 146.36 ? 838  GLN B OE1 1 
ATOM   20751 N  NE2 . GLN C 1 838  ? 0.066    20.775  56.239  1.00 143.32 ? 838  GLN B NE2 1 
ATOM   20752 N  N   . ILE C 1 839  ? 2.126    24.650  59.356  1.00 131.84 ? 839  ILE B N   1 
ATOM   20753 C  CA  . ILE C 1 839  ? 1.438    25.941  59.322  1.00 133.47 ? 839  ILE B CA  1 
ATOM   20754 C  C   . ILE C 1 839  ? 1.303    26.540  57.911  1.00 134.36 ? 839  ILE B C   1 
ATOM   20755 O  O   . ILE C 1 839  ? 2.214    26.420  57.096  1.00 137.31 ? 839  ILE B O   1 
ATOM   20756 C  CB  . ILE C 1 839  ? 2.168    26.947  60.242  1.00 133.62 ? 839  ILE B CB  1 
ATOM   20757 C  CG1 . ILE C 1 839  ? 1.278    28.148  60.572  1.00 133.68 ? 839  ILE B CG1 1 
ATOM   20758 C  CG2 . ILE C 1 839  ? 3.462    27.390  59.603  1.00 135.02 ? 839  ILE B CG2 1 
ATOM   20759 C  CD1 . ILE C 1 839  ? 0.234    27.870  61.625  1.00 132.96 ? 839  ILE B CD1 1 
ATOM   20760 N  N   . GLN C 1 840  ? 0.171    27.186  57.624  1.00 133.39 ? 840  GLN B N   1 
ATOM   20761 C  CA  . GLN C 1 840  ? -0.005   27.871  56.341  1.00 132.26 ? 840  GLN B CA  1 
ATOM   20762 C  C   . GLN C 1 840  ? 0.175    29.389  56.423  1.00 127.37 ? 840  GLN B C   1 
ATOM   20763 O  O   . GLN C 1 840  ? -0.666   30.105  56.958  1.00 124.63 ? 840  GLN B O   1 
ATOM   20764 C  CB  . GLN C 1 840  ? -1.353   27.539  55.716  1.00 137.86 ? 840  GLN B CB  1 
ATOM   20765 C  CG  . GLN C 1 840  ? -1.235   27.264  54.235  1.00 145.15 ? 840  GLN B CG  1 
ATOM   20766 C  CD  . GLN C 1 840  ? -2.203   28.085  53.424  1.00 151.63 ? 840  GLN B CD  1 
ATOM   20767 O  OE1 . GLN C 1 840  ? -2.605   27.686  52.329  1.00 153.67 ? 840  GLN B OE1 1 
ATOM   20768 N  NE2 . GLN C 1 840  ? -2.592   29.244  53.960  1.00 153.18 ? 840  GLN B NE2 1 
ATOM   20769 N  N   . LEU C 1 841  ? 1.275    29.863  55.856  1.00 124.60 ? 841  LEU B N   1 
ATOM   20770 C  CA  . LEU C 1 841  ? 1.682    31.249  55.976  1.00 122.04 ? 841  LEU B CA  1 
ATOM   20771 C  C   . LEU C 1 841  ? 1.229    32.128  54.824  1.00 118.84 ? 841  LEU B C   1 
ATOM   20772 O  O   . LEU C 1 841  ? 1.918    32.238  53.820  1.00 116.78 ? 841  LEU B O   1 
ATOM   20773 C  CB  . LEU C 1 841  ? 3.200    31.303  56.054  1.00 121.16 ? 841  LEU B CB  1 
ATOM   20774 C  CG  . LEU C 1 841  ? 3.763    31.272  57.465  1.00 118.10 ? 841  LEU B CG  1 
ATOM   20775 C  CD1 . LEU C 1 841  ? 5.263    31.547  57.438  1.00 117.84 ? 841  LEU B CD1 1 
ATOM   20776 C  CD2 . LEU C 1 841  ? 3.018    32.321  58.280  1.00 115.75 ? 841  LEU B CD2 1 
ATOM   20777 N  N   . LYS C 1 842  ? 0.098    32.797  54.987  1.00 119.04 ? 842  LYS B N   1 
ATOM   20778 C  CA  . LYS C 1 842  ? -0.430   33.627  53.916  1.00 119.21 ? 842  LYS B CA  1 
ATOM   20779 C  C   . LYS C 1 842  ? 0.134    35.042  53.859  1.00 121.60 ? 842  LYS B C   1 
ATOM   20780 O  O   . LYS C 1 842  ? 1.057    35.404  54.568  1.00 123.72 ? 842  LYS B O   1 
ATOM   20781 C  CB  . LYS C 1 842  ? -1.949   33.687  53.977  1.00 117.05 ? 842  LYS B CB  1 
ATOM   20782 C  CG  . LYS C 1 842  ? -2.607   32.336  53.939  1.00 116.37 ? 842  LYS B CG  1 
ATOM   20783 C  CD  . LYS C 1 842  ? -4.102   32.510  54.043  1.00 116.65 ? 842  LYS B CD  1 
ATOM   20784 C  CE  . LYS C 1 842  ? -4.798   31.235  54.465  1.00 117.71 ? 842  LYS B CE  1 
ATOM   20785 N  NZ  . LYS C 1 842  ? -6.247   31.514  54.673  1.00 118.90 ? 842  LYS B NZ  1 
ATOM   20786 N  N   . GLY C 1 843  ? -0.455   35.832  52.975  1.00 124.36 ? 843  GLY B N   1 
ATOM   20787 C  CA  . GLY C 1 843  ? -0.003   37.177  52.672  1.00 126.82 ? 843  GLY B CA  1 
ATOM   20788 C  C   . GLY C 1 843  ? -0.646   37.608  51.368  1.00 131.64 ? 843  GLY B C   1 
ATOM   20789 O  O   . GLY C 1 843  ? -1.152   36.776  50.608  1.00 129.47 ? 843  GLY B O   1 
ATOM   20790 N  N   . THR C 1 844  ? -0.648   38.906  51.103  1.00 135.27 ? 844  THR B N   1 
ATOM   20791 C  CA  . THR C 1 844  ? -1.195   39.395  49.839  1.00 139.14 ? 844  THR B CA  1 
ATOM   20792 C  C   . THR C 1 844  ? -0.184   40.403  49.212  1.00 138.48 ? 844  THR B C   1 
ATOM   20793 O  O   . THR C 1 844  ? 0.547    41.085  49.945  1.00 138.50 ? 844  THR B O   1 
ATOM   20794 C  CB  . THR C 1 844  ? -2.727   39.861  49.980  1.00 119.00 ? 844  THR B CB  1 
ATOM   20795 O  OG1 . THR C 1 844  ? -2.849   41.243  50.351  1.00 118.52 ? 844  THR B OG1 1 
ATOM   20796 C  CG2 . THR C 1 844  ? -3.492   38.985  51.008  1.00 111.54 ? 844  THR B CG2 1 
ATOM   20797 N  N   . VAL C 1 845  ? -0.056   40.426  47.881  1.00 138.92 ? 845  VAL B N   1 
ATOM   20798 C  CA  . VAL C 1 845  ? 0.959    41.285  47.241  1.00 140.96 ? 845  VAL B CA  1 
ATOM   20799 C  C   . VAL C 1 845  ? 0.348    42.463  46.498  1.00 140.19 ? 845  VAL B C   1 
ATOM   20800 O  O   . VAL C 1 845  ? -0.508   42.295  45.629  1.00 137.73 ? 845  VAL B O   1 
ATOM   20801 C  CB  . VAL C 1 845  ? 1.953    40.501  46.328  1.00 105.83 ? 845  VAL B CB  1 
ATOM   20802 C  CG1 . VAL C 1 845  ? 1.221    39.736  45.246  1.00 104.40 ? 845  VAL B CG1 1 
ATOM   20803 C  CG2 . VAL C 1 845  ? 3.008    41.449  45.743  1.00 106.23 ? 845  VAL B CG2 1 
ATOM   20804 N  N   . TYR C 1 846  ? 0.794    43.661  46.853  1.00 143.37 ? 846  TYR B N   1 
ATOM   20805 C  CA  . TYR C 1 846  ? 0.057    44.858  46.473  1.00 143.72 ? 846  TYR B CA  1 
ATOM   20806 C  C   . TYR C 1 846  ? 0.527    45.525  45.190  1.00 151.13 ? 846  TYR B C   1 
ATOM   20807 O  O   . TYR C 1 846  ? 1.670    45.967  45.076  1.00 150.98 ? 846  TYR B O   1 
ATOM   20808 C  CB  . TYR C 1 846  ? -0.106   45.833  47.662  1.00 137.96 ? 846  TYR B CB  1 
ATOM   20809 C  CG  . TYR C 1 846  ? -1.053   45.264  48.708  1.00 131.59 ? 846  TYR B CG  1 
ATOM   20810 C  CD1 . TYR C 1 846  ? -0.805   45.372  50.064  1.00 129.34 ? 846  TYR B CD1 1 
ATOM   20811 C  CD2 . TYR C 1 846  ? -2.180   44.558  48.317  1.00 128.05 ? 846  TYR B CD2 1 
ATOM   20812 C  CE1 . TYR C 1 846  ? -1.684   44.813  50.993  1.00 126.97 ? 846  TYR B CE1 1 
ATOM   20813 C  CE2 . TYR C 1 846  ? -3.048   44.001  49.232  1.00 125.04 ? 846  TYR B CE2 1 
ATOM   20814 C  CZ  . TYR C 1 846  ? -2.801   44.129  50.556  1.00 124.29 ? 846  TYR B CZ  1 
ATOM   20815 O  OH  . TYR C 1 846  ? -3.692   43.548  51.422  1.00 123.30 ? 846  TYR B OH  1 
ATOM   20816 N  N   . ASN C 1 847  ? -0.382   45.528  44.213  1.00 158.28 ? 847  ASN B N   1 
ATOM   20817 C  CA  . ASN C 1 847  ? -0.231   46.279  42.974  1.00 166.03 ? 847  ASN B CA  1 
ATOM   20818 C  C   . ASN C 1 847  ? -1.088   47.517  43.053  1.00 169.33 ? 847  ASN B C   1 
ATOM   20819 O  O   . ASN C 1 847  ? -2.298   47.454  43.287  1.00 166.22 ? 847  ASN B O   1 
ATOM   20820 C  CB  . ASN C 1 847  ? -0.617   45.448  41.741  1.00 169.28 ? 847  ASN B CB  1 
ATOM   20821 C  CG  . ASN C 1 847  ? 0.057    45.946  40.463  1.00 174.14 ? 847  ASN B CG  1 
ATOM   20822 O  OD1 . ASN C 1 847  ? 0.158    47.152  40.227  1.00 176.38 ? 847  ASN B OD1 1 
ATOM   20823 N  ND2 . ASN C 1 847  ? 0.526    45.011  39.638  1.00 175.46 ? 847  ASN B ND2 1 
ATOM   20824 N  N   . TYR C 1 848  ? -0.434   48.644  42.842  1.00 176.09 ? 848  TYR B N   1 
ATOM   20825 C  CA  . TYR C 1 848  ? -1.068   49.925  42.978  1.00 180.90 ? 848  TYR B CA  1 
ATOM   20826 C  C   . TYR C 1 848  ? -0.699   50.768  41.767  1.00 184.27 ? 848  TYR B C   1 
ATOM   20827 O  O   . TYR C 1 848  ? -1.189   51.883  41.582  1.00 184.41 ? 848  TYR B O   1 
ATOM   20828 C  CB  . TYR C 1 848  ? -0.627   50.567  44.284  1.00 182.32 ? 848  TYR B CB  1 
ATOM   20829 C  CG  . TYR C 1 848  ? -1.510   50.186  45.460  1.00 180.96 ? 848  TYR B CG  1 
ATOM   20830 C  CD1 . TYR C 1 848  ? -2.622   49.367  45.278  1.00 178.64 ? 848  TYR B CD1 1 
ATOM   20831 C  CD2 . TYR C 1 848  ? -1.267   50.691  46.740  1.00 180.92 ? 848  TYR B CD2 1 
ATOM   20832 C  CE1 . TYR C 1 848  ? -3.444   49.039  46.335  1.00 177.61 ? 848  TYR B CE1 1 
ATOM   20833 C  CE2 . TYR C 1 848  ? -2.081   50.374  47.801  1.00 179.65 ? 848  TYR B CE2 1 
ATOM   20834 C  CZ  . TYR C 1 848  ? -3.167   49.548  47.590  1.00 179.03 ? 848  TYR B CZ  1 
ATOM   20835 O  OH  . TYR C 1 848  ? -3.981   49.226  48.641  1.00 180.28 ? 848  TYR B OH  1 
ATOM   20836 N  N   . ARG C 1 849  ? 0.174    50.210  40.937  1.00 187.67 ? 849  ARG B N   1 
ATOM   20837 C  CA  . ARG C 1 849  ? 0.438    50.753  39.616  1.00 191.17 ? 849  ARG B CA  1 
ATOM   20838 C  C   . ARG C 1 849  ? -0.877   50.652  38.831  1.00 189.55 ? 849  ARG B C   1 
ATOM   20839 O  O   . ARG C 1 849  ? -1.681   49.748  39.077  1.00 187.25 ? 849  ARG B O   1 
ATOM   20840 C  CB  . ARG C 1 849  ? 1.585    49.965  38.958  1.00 196.04 ? 849  ARG B CB  1 
ATOM   20841 C  CG  . ARG C 1 849  ? 1.957    50.377  37.534  1.00 202.25 ? 849  ARG B CG  1 
ATOM   20842 C  CD  . ARG C 1 849  ? 2.359    51.847  37.416  1.00 208.84 ? 849  ARG B CD  1 
ATOM   20843 N  NE  . ARG C 1 849  ? 2.852    52.172  36.075  1.00 213.30 ? 849  ARG B NE  1 
ATOM   20844 C  CZ  . ARG C 1 849  ? 2.967    53.408  35.589  1.00 216.14 ? 849  ARG B CZ  1 
ATOM   20845 N  NH1 . ARG C 1 849  ? 2.613    54.453  36.328  1.00 217.42 ? 849  ARG B NH1 1 
ATOM   20846 N  NH2 . ARG C 1 849  ? 3.430    53.601  34.358  1.00 216.57 ? 849  ARG B NH2 1 
ATOM   20847 N  N   . THR C 1 850  ? -1.108   51.595  37.919  1.00 190.86 ? 850  THR B N   1 
ATOM   20848 C  CA  . THR C 1 850  ? -2.367   51.668  37.166  1.00 189.13 ? 850  THR B CA  1 
ATOM   20849 C  C   . THR C 1 850  ? -2.592   50.447  36.280  1.00 188.63 ? 850  THR B C   1 
ATOM   20850 O  O   . THR C 1 850  ? -3.724   50.006  36.071  1.00 188.77 ? 850  THR B O   1 
ATOM   20851 C  CB  . THR C 1 850  ? -2.425   52.939  36.293  1.00 187.78 ? 850  THR B CB  1 
ATOM   20852 O  OG1 . THR C 1 850  ? -1.180   53.101  35.602  1.00 187.83 ? 850  THR B OG1 1 
ATOM   20853 C  CG2 . THR C 1 850  ? -2.683   54.164  37.151  1.00 187.71 ? 850  THR B CG2 1 
ATOM   20854 N  N   . SER C 1 851  ? -1.495   49.924  35.746  1.00 188.26 ? 851  SER B N   1 
ATOM   20855 C  CA  . SER C 1 851  ? -1.506   48.679  34.987  1.00 189.20 ? 851  SER B CA  1 
ATOM   20856 C  C   . SER C 1 851  ? -1.142   47.484  35.875  1.00 190.08 ? 851  SER B C   1 
ATOM   20857 O  O   . SER C 1 851  ? -0.724   47.654  37.022  1.00 188.28 ? 851  SER B O   1 
ATOM   20858 C  CB  . SER C 1 851  ? -0.541   48.769  33.793  1.00 192.07 ? 851  SER B CB  1 
ATOM   20859 O  OG  . SER C 1 851  ? 0.790    49.064  34.208  1.00 195.47 ? 851  SER B OG  1 
ATOM   20860 N  N   . GLY C 1 852  ? -1.308   46.277  35.344  1.00 191.64 ? 852  GLY B N   1 
ATOM   20861 C  CA  . GLY C 1 852  ? -0.934   45.079  36.069  1.00 190.95 ? 852  GLY B CA  1 
ATOM   20862 C  C   . GLY C 1 852  ? 0.549    44.823  35.927  1.00 186.51 ? 852  GLY B C   1 
ATOM   20863 O  O   . GLY C 1 852  ? 1.256    45.599  35.281  1.00 187.31 ? 852  GLY B O   1 
ATOM   20864 N  N   . MET C 1 853  ? 1.026    43.738  36.532  1.00 180.65 ? 853  MET B N   1 
ATOM   20865 C  CA  . MET C 1 853  ? 2.410    43.304  36.326  1.00 176.70 ? 853  MET B CA  1 
ATOM   20866 C  C   . MET C 1 853  ? 2.706    41.863  36.769  1.00 172.06 ? 853  MET B C   1 
ATOM   20867 O  O   . MET C 1 853  ? 1.843    41.160  37.296  1.00 170.03 ? 853  MET B O   1 
ATOM   20868 C  CB  . MET C 1 853  ? 3.388    44.282  36.985  1.00 178.25 ? 853  MET B CB  1 
ATOM   20869 C  CG  . MET C 1 853  ? 3.383    44.268  38.496  1.00 179.44 ? 853  MET B CG  1 
ATOM   20870 S  SD  . MET C 1 853  ? 4.290    45.682  39.128  1.00 206.44 ? 853  MET B SD  1 
ATOM   20871 C  CE  . MET C 1 853  ? 3.172    47.009  38.683  1.00 217.23 ? 853  MET B CE  1 
ATOM   20872 N  N   . GLN C 1 854  ? 3.933    41.425  36.522  1.00 170.60 ? 854  GLN B N   1 
ATOM   20873 C  CA  . GLN C 1 854  ? 4.348    40.095  36.917  1.00 169.03 ? 854  GLN B CA  1 
ATOM   20874 C  C   . GLN C 1 854  ? 5.198    40.182  38.169  1.00 167.54 ? 854  GLN B C   1 
ATOM   20875 O  O   . GLN C 1 854  ? 6.082    41.037  38.252  1.00 168.36 ? 854  GLN B O   1 
ATOM   20876 C  CB  . GLN C 1 854  ? 5.140    39.450  35.787  1.00 170.04 ? 854  GLN B CB  1 
ATOM   20877 C  CG  . GLN C 1 854  ? 4.460    39.592  34.435  1.00 169.57 ? 854  GLN B CG  1 
ATOM   20878 C  CD  . GLN C 1 854  ? 5.175    38.842  33.323  1.00 170.16 ? 854  GLN B CD  1 
ATOM   20879 O  OE1 . GLN C 1 854  ? 6.290    38.339  33.505  1.00 171.31 ? 854  GLN B OE1 1 
ATOM   20880 N  NE2 . GLN C 1 854  ? 4.533    38.765  32.156  1.00 168.90 ? 854  GLN B NE2 1 
ATOM   20881 N  N   . PHE C 1 855  ? 4.909    39.322  39.150  1.00 164.54 ? 855  PHE B N   1 
ATOM   20882 C  CA  . PHE C 1 855  ? 5.784    39.145  40.319  1.00 162.09 ? 855  PHE B CA  1 
ATOM   20883 C  C   . PHE C 1 855  ? 6.396    37.748  40.416  1.00 163.09 ? 855  PHE B C   1 
ATOM   20884 O  O   . PHE C 1 855  ? 6.427    37.014  39.430  1.00 164.62 ? 855  PHE B O   1 
ATOM   20885 C  CB  . PHE C 1 855  ? 5.092    39.533  41.630  1.00 156.64 ? 855  PHE B CB  1 
ATOM   20886 C  CG  . PHE C 1 855  ? 3.862    38.728  41.956  1.00 150.57 ? 855  PHE B CG  1 
ATOM   20887 C  CD1 . PHE C 1 855  ? 3.936    37.618  42.766  1.00 149.14 ? 855  PHE B CD1 1 
ATOM   20888 C  CD2 . PHE C 1 855  ? 2.619    39.118  41.498  1.00 147.42 ? 855  PHE B CD2 1 
ATOM   20889 C  CE1 . PHE C 1 855  ? 2.791    36.893  43.085  1.00 146.82 ? 855  PHE B CE1 1 
ATOM   20890 C  CE2 . PHE C 1 855  ? 1.474    38.392  41.825  1.00 145.11 ? 855  PHE B CE2 1 
ATOM   20891 C  CZ  . PHE C 1 855  ? 1.561    37.284  42.617  1.00 144.53 ? 855  PHE B CZ  1 
ATOM   20892 N  N   . CYS C 1 856  ? 6.892    37.397  41.600  1.00 163.55 ? 856  CYS B N   1 
ATOM   20893 C  CA  . CYS C 1 856  ? 7.515    36.092  41.839  1.00 164.55 ? 856  CYS B CA  1 
ATOM   20894 C  C   . CYS C 1 856  ? 8.020    36.025  43.276  1.00 167.31 ? 856  CYS B C   1 
ATOM   20895 O  O   . CYS C 1 856  ? 9.205    36.249  43.521  1.00 169.00 ? 856  CYS B O   1 
ATOM   20896 C  CB  . CYS C 1 856  ? 8.688    35.880  40.868  1.00 165.05 ? 856  CYS B CB  1 
ATOM   20897 S  SG  . CYS C 1 856  ? 9.732    34.398  41.116  1.00 203.55 ? 856  CYS B SG  1 
ATOM   20898 N  N   . VAL C 1 857  ? 7.136    35.727  44.229  1.00 167.60 ? 857  VAL B N   1 
ATOM   20899 C  CA  . VAL C 1 857  ? 7.520    35.750  45.646  1.00 167.55 ? 857  VAL B CA  1 
ATOM   20900 C  C   . VAL C 1 857  ? 8.152    34.445  46.103  1.00 168.18 ? 857  VAL B C   1 
ATOM   20901 O  O   . VAL C 1 857  ? 7.608    33.371  45.862  1.00 168.36 ? 857  VAL B O   1 
ATOM   20902 C  CB  . VAL C 1 857  ? 6.321    36.031  46.554  1.00 164.34 ? 857  VAL B CB  1 
ATOM   20903 C  CG1 . VAL C 1 857  ? 5.824    37.444  46.346  1.00 163.60 ? 857  VAL B CG1 1 
ATOM   20904 C  CG2 . VAL C 1 857  ? 5.233    35.029  46.271  1.00 162.28 ? 857  VAL B CG2 1 
ATOM   20905 N  N   . LYS C 1 858  ? 9.290    34.541  46.778  1.00 168.50 ? 858  LYS B N   1 
ATOM   20906 C  CA  . LYS C 1 858  ? 9.973    33.349  47.256  1.00 170.47 ? 858  LYS B CA  1 
ATOM   20907 C  C   . LYS C 1 858  ? 10.383   33.493  48.721  1.00 168.79 ? 858  LYS B C   1 
ATOM   20908 O  O   . LYS C 1 858  ? 10.845   34.555  49.153  1.00 169.64 ? 858  LYS B O   1 
ATOM   20909 C  CB  . LYS C 1 858  ? 11.177   32.995  46.360  1.00 176.26 ? 858  LYS B CB  1 
ATOM   20910 C  CG  . LYS C 1 858  ? 12.211   34.108  46.198  1.00 182.24 ? 858  LYS B CG  1 
ATOM   20911 C  CD  . LYS C 1 858  ? 13.404   33.679  45.335  1.00 187.05 ? 858  LYS B CD  1 
ATOM   20912 C  CE  . LYS C 1 858  ? 14.517   34.736  45.371  1.00 191.26 ? 858  LYS B CE  1 
ATOM   20913 N  NZ  . LYS C 1 858  ? 15.623   34.464  44.405  1.00 193.52 ? 858  LYS B NZ  1 
ATOM   20914 N  N   . MET C 1 859  ? 10.190   32.416  49.481  1.00 165.38 ? 859  MET B N   1 
ATOM   20915 C  CA  . MET C 1 859  ? 10.481   32.389  50.912  1.00 161.96 ? 859  MET B CA  1 
ATOM   20916 C  C   . MET C 1 859  ? 11.802   31.698  51.228  1.00 161.99 ? 859  MET B C   1 
ATOM   20917 O  O   . MET C 1 859  ? 12.173   30.724  50.584  1.00 161.90 ? 859  MET B O   1 
ATOM   20918 C  CB  . MET C 1 859  ? 9.334    31.712  51.651  1.00 158.53 ? 859  MET B CB  1 
ATOM   20919 C  CG  . MET C 1 859  ? 9.759    30.665  52.636  1.00 158.46 ? 859  MET B CG  1 
ATOM   20920 S  SD  . MET C 1 859  ? 8.319    29.739  53.176  1.00 116.84 ? 859  MET B SD  1 
ATOM   20921 C  CE  . MET C 1 859  ? 7.639    30.855  54.394  1.00 190.41 ? 859  MET B CE  1 
ATOM   20922 N  N   . SER C 1 860  ? 12.502   32.209  52.230  1.00 163.16 ? 860  SER B N   1 
ATOM   20923 C  CA  . SER C 1 860  ? 13.836   31.733  52.555  1.00 166.02 ? 860  SER B CA  1 
ATOM   20924 C  C   . SER C 1 860  ? 13.896   30.573  53.557  1.00 166.87 ? 860  SER B C   1 
ATOM   20925 O  O   . SER C 1 860  ? 13.520   30.720  54.726  1.00 167.43 ? 860  SER B O   1 
ATOM   20926 C  CB  . SER C 1 860  ? 14.676   32.895  53.072  1.00 168.83 ? 860  SER B CB  1 
ATOM   20927 O  OG  . SER C 1 860  ? 15.565   32.451  54.089  1.00 172.20 ? 860  SER B OG  1 
ATOM   20928 N  N   . ALA C 1 861  ? 14.410   29.432  53.095  1.00 166.01 ? 861  ALA B N   1 
ATOM   20929 C  CA  . ALA C 1 861  ? 14.578   28.245  53.934  1.00 164.22 ? 861  ALA B CA  1 
ATOM   20930 C  C   . ALA C 1 861  ? 15.524   28.501  55.103  1.00 163.21 ? 861  ALA B C   1 
ATOM   20931 O  O   . ALA C 1 861  ? 16.739   28.479  54.934  1.00 162.85 ? 861  ALA B O   1 
ATOM   20932 C  CB  . ALA C 1 861  ? 15.072   27.059  53.090  1.00 163.41 ? 861  ALA B CB  1 
ATOM   20933 N  N   . VAL C 1 862  ? 14.968   28.740  56.285  1.00 162.87 ? 862  VAL B N   1 
ATOM   20934 C  CA  . VAL C 1 862  ? 15.803   28.932  57.457  1.00 165.84 ? 862  VAL B CA  1 
ATOM   20935 C  C   . VAL C 1 862  ? 15.957   27.658  58.270  1.00 164.25 ? 862  VAL B C   1 
ATOM   20936 O  O   . VAL C 1 862  ? 14.981   26.944  58.499  1.00 164.80 ? 862  VAL B O   1 
ATOM   20937 C  CB  . VAL C 1 862  ? 15.275   30.031  58.356  1.00 166.66 ? 862  VAL B CB  1 
ATOM   20938 C  CG1 . VAL C 1 862  ? 16.176   30.152  59.586  1.00 169.71 ? 862  VAL B CG1 1 
ATOM   20939 C  CG2 . VAL C 1 862  ? 15.210   31.340  57.586  1.00 166.55 ? 862  VAL B CG2 1 
ATOM   20940 N  N   . GLU C 1 863  ? 17.181   27.421  58.739  1.00 161.60 ? 863  GLU B N   1 
ATOM   20941 C  CA  . GLU C 1 863  ? 17.619   26.109  59.231  1.00 159.40 ? 863  GLU B CA  1 
ATOM   20942 C  C   . GLU C 1 863  ? 16.537   25.160  59.771  1.00 153.09 ? 863  GLU B C   1 
ATOM   20943 O  O   . GLU C 1 863  ? 16.446   24.008  59.345  1.00 151.04 ? 863  GLU B O   1 
ATOM   20944 C  CB  . GLU C 1 863  ? 18.750   26.266  60.266  1.00 164.10 ? 863  GLU B CB  1 
ATOM   20945 C  CG  . GLU C 1 863  ? 20.195   26.081  59.737  1.00 183.68 ? 863  GLU B CG  1 
ATOM   20946 C  CD  . GLU C 1 863  ? 20.693   24.626  59.770  1.00 185.95 ? 863  GLU B CD  1 
ATOM   20947 O  OE1 . GLU C 1 863  ? 19.976   23.726  59.268  1.00 184.55 ? 863  GLU B OE1 1 
ATOM   20948 O  OE2 . GLU C 1 863  ? 21.812   24.387  60.287  1.00 188.33 ? 863  GLU B OE2 1 
ATOM   20949 N  N   . GLY C 1 864  ? 15.730   25.631  60.710  1.00 151.76 ? 864  GLY B N   1 
ATOM   20950 C  CA  . GLY C 1 864  ? 14.891   24.736  61.484  1.00 149.89 ? 864  GLY B CA  1 
ATOM   20951 C  C   . GLY C 1 864  ? 13.507   24.507  60.928  1.00 146.86 ? 864  GLY B C   1 
ATOM   20952 O  O   . GLY C 1 864  ? 12.648   23.906  61.582  1.00 146.14 ? 864  GLY B O   1 
ATOM   20953 N  N   . ILE C 1 865  ? 13.291   24.968  59.704  1.00 142.66 ? 865  ILE B N   1 
ATOM   20954 C  CA  . ILE C 1 865  ? 11.953   24.976  59.141  1.00 137.11 ? 865  ILE B CA  1 
ATOM   20955 C  C   . ILE C 1 865  ? 11.828   24.215  57.832  1.00 137.16 ? 865  ILE B C   1 
ATOM   20956 O  O   . ILE C 1 865  ? 12.511   24.519  56.853  1.00 135.29 ? 865  ILE B O   1 
ATOM   20957 C  CB  . ILE C 1 865  ? 11.483   26.402  58.899  1.00 133.59 ? 865  ILE B CB  1 
ATOM   20958 C  CG1 . ILE C 1 865  ? 11.848   27.289  60.085  1.00 133.01 ? 865  ILE B CG1 1 
ATOM   20959 C  CG2 . ILE C 1 865  ? 9.990    26.408  58.654  1.00 131.14 ? 865  ILE B CG2 1 
ATOM   20960 C  CD1 . ILE C 1 865  ? 11.281   28.672  59.978  1.00 132.45 ? 865  ILE B CD1 1 
ATOM   20961 N  N   . CYS C 1 866  ? 10.937   23.229  57.831  1.00 139.72 ? 866  CYS B N   1 
ATOM   20962 C  CA  . CYS C 1 866  ? 10.660   22.433  56.646  1.00 144.54 ? 866  CYS B CA  1 
ATOM   20963 C  C   . CYS C 1 866  ? 9.924    23.224  55.585  1.00 151.58 ? 866  CYS B C   1 
ATOM   20964 O  O   . CYS C 1 866  ? 9.271    24.228  55.877  1.00 147.64 ? 866  CYS B O   1 
ATOM   20965 C  CB  . CYS C 1 866  ? 9.834    21.210  57.007  1.00 141.43 ? 866  CYS B CB  1 
ATOM   20966 S  SG  . CYS C 1 866  ? 10.833   19.788  57.294  1.00 145.31 ? 866  CYS B SG  1 
ATOM   20967 N  N   . THR C 1 867  ? 10.024   22.746  54.352  1.00 162.25 ? 867  THR B N   1 
ATOM   20968 C  CA  . THR C 1 867  ? 9.427    23.420  53.217  1.00 171.50 ? 867  THR B CA  1 
ATOM   20969 C  C   . THR C 1 867  ? 9.501    22.567  51.961  1.00 182.95 ? 867  THR B C   1 
ATOM   20970 O  O   . THR C 1 867  ? 10.169   21.534  51.924  1.00 186.18 ? 867  THR B O   1 
ATOM   20971 C  CB  . THR C 1 867  ? 10.080   24.797  52.951  1.00 164.06 ? 867  THR B CB  1 
ATOM   20972 O  OG1 . THR C 1 867  ? 11.246   24.946  53.769  1.00 164.30 ? 867  THR B OG1 1 
ATOM   20973 C  CG2 . THR C 1 867  ? 9.112    25.920  53.268  1.00 161.49 ? 867  THR B CG2 1 
ATOM   20974 N  N   . SER C 1 868  ? 8.808    23.030  50.928  1.00 195.49 ? 868  SER B N   1 
ATOM   20975 C  CA  . SER C 1 868  ? 8.641    22.277  49.690  1.00 207.45 ? 868  SER B CA  1 
ATOM   20976 C  C   . SER C 1 868  ? 9.843    22.357  48.733  1.00 222.21 ? 868  SER B C   1 
ATOM   20977 O  O   . SER C 1 868  ? 9.956    21.546  47.816  1.00 222.21 ? 868  SER B O   1 
ATOM   20978 C  CB  . SER C 1 868  ? 7.354    22.725  48.980  1.00 206.65 ? 868  SER B CB  1 
ATOM   20979 O  OG  . SER C 1 868  ? 6.261    22.807  49.889  1.00 206.49 ? 868  SER B OG  1 
ATOM   20980 N  N   . GLU C 1 869  ? 10.726   23.335  48.930  1.00 236.78 ? 869  GLU B N   1 
ATOM   20981 C  CA  . GLU C 1 869  ? 11.946   23.432  48.122  1.00 249.49 ? 869  GLU B CA  1 
ATOM   20982 C  C   . GLU C 1 869  ? 13.025   22.509  48.697  1.00 258.63 ? 869  GLU B C   1 
ATOM   20983 O  O   . GLU C 1 869  ? 13.036   22.231  49.897  1.00 259.14 ? 869  GLU B O   1 
ATOM   20984 C  CB  . GLU C 1 869  ? 12.433   24.888  48.033  1.00 252.94 ? 869  GLU B CB  1 
ATOM   20985 C  CG  . GLU C 1 869  ? 13.622   25.126  47.088  1.00 254.69 ? 869  GLU B CG  1 
ATOM   20986 C  CD  . GLU C 1 869  ? 14.983   24.935  47.763  1.00 256.56 ? 869  GLU B CD  1 
ATOM   20987 O  OE1 . GLU C 1 869  ? 15.045   24.957  49.010  1.00 257.10 ? 869  GLU B OE1 1 
ATOM   20988 O  OE2 . GLU C 1 869  ? 15.996   24.772  47.050  1.00 257.16 ? 869  GLU B OE2 1 
ATOM   20989 N  N   . SER C 1 870  ? 13.923   22.030  47.840  1.00 264.76 ? 870  SER B N   1 
ATOM   20990 C  CA  . SER C 1 870  ? 14.939   21.061  48.252  1.00 270.89 ? 870  SER B CA  1 
ATOM   20991 C  C   . SER C 1 870  ? 15.817   21.582  49.387  1.00 273.95 ? 870  SER B C   1 
ATOM   20992 O  O   . SER C 1 870  ? 16.343   22.693  49.321  1.00 275.52 ? 870  SER B O   1 
ATOM   20993 C  CB  . SER C 1 870  ? 15.808   20.649  47.061  1.00 273.71 ? 870  SER B CB  1 
ATOM   20994 O  OG  . SER C 1 870  ? 16.509   21.761  46.537  1.00 275.90 ? 870  SER B OG  1 
ATOM   20995 N  N   . LYS C 1 882  ? 11.933   29.050  45.298  1.00 223.66 ? 882  LYS B N   1 
ATOM   20996 C  CA  . LYS C 1 882  ? 11.684   28.805  43.873  1.00 223.65 ? 882  LYS B CA  1 
ATOM   20997 C  C   . LYS C 1 882  ? 10.911   29.957  43.221  1.00 221.26 ? 882  LYS B C   1 
ATOM   20998 O  O   . LYS C 1 882  ? 10.020   30.530  43.841  1.00 219.53 ? 882  LYS B O   1 
ATOM   20999 C  CB  . LYS C 1 882  ? 10.951   27.466  43.663  1.00 225.15 ? 882  LYS B CB  1 
ATOM   21000 C  CG  . LYS C 1 882  ? 9.505    27.416  44.169  1.00 224.77 ? 882  LYS B CG  1 
ATOM   21001 C  CD  . LYS C 1 882  ? 8.858    26.036  43.961  1.00 224.94 ? 882  LYS B CD  1 
ATOM   21002 C  CE  . LYS C 1 882  ? 9.482    24.964  44.863  1.00 226.91 ? 882  LYS B CE  1 
ATOM   21003 N  NZ  . LYS C 1 882  ? 8.827    23.619  44.757  1.00 225.99 ? 882  LYS B NZ  1 
ATOM   21004 N  N   . CYS C 1 883  ? 11.248   30.293  41.975  1.00 219.62 ? 883  CYS B N   1 
ATOM   21005 C  CA  . CYS C 1 883  ? 10.622   31.436  41.300  1.00 216.75 ? 883  CYS B CA  1 
ATOM   21006 C  C   . CYS C 1 883  ? 9.291    31.138  40.600  1.00 212.49 ? 883  CYS B C   1 
ATOM   21007 O  O   . CYS C 1 883  ? 9.220    31.089  39.369  1.00 211.78 ? 883  CYS B O   1 
ATOM   21008 C  CB  . CYS C 1 883  ? 11.582   32.089  40.305  1.00 218.14 ? 883  CYS B CB  1 
ATOM   21009 S  SG  . CYS C 1 883  ? 10.925   33.636  39.648  1.00 272.04 ? 883  CYS B SG  1 
ATOM   21010 N  N   . VAL C 1 884  ? 8.238    30.974  41.397  1.00 208.66 ? 884  VAL B N   1 
ATOM   21011 C  CA  . VAL C 1 884  ? 6.885    30.782  40.886  1.00 206.31 ? 884  VAL B CA  1 
ATOM   21012 C  C   . VAL C 1 884  ? 6.282    32.125  40.451  1.00 206.39 ? 884  VAL B C   1 
ATOM   21013 O  O   . VAL C 1 884  ? 5.596    32.792  41.237  1.00 206.28 ? 884  VAL B O   1 
ATOM   21014 C  CB  . VAL C 1 884  ? 5.976    30.108  41.956  1.00 168.30 ? 884  VAL B CB  1 
ATOM   21015 C  CG1 . VAL C 1 884  ? 6.480    28.710  42.293  1.00 168.49 ? 884  VAL B CG1 1 
ATOM   21016 C  CG2 . VAL C 1 884  ? 5.899    30.953  43.225  1.00 169.31 ? 884  VAL B CG2 1 
ATOM   21017 N  N   . ARG C 1 885  ? 6.531    32.524  39.202  1.00 207.61 ? 885  ARG B N   1 
ATOM   21018 C  CA  . ARG C 1 885  ? 6.143    33.868  38.758  1.00 206.85 ? 885  ARG B CA  1 
ATOM   21019 C  C   . ARG C 1 885  ? 4.695    33.996  38.307  1.00 203.52 ? 885  ARG B C   1 
ATOM   21020 O  O   . ARG C 1 885  ? 4.244    33.340  37.375  1.00 202.29 ? 885  ARG B O   1 
ATOM   21021 C  CB  . ARG C 1 885  ? 7.094    34.423  37.698  1.00 207.63 ? 885  ARG B CB  1 
ATOM   21022 C  CG  . ARG C 1 885  ? 7.205    33.590  36.459  1.00 207.50 ? 885  ARG B CG  1 
ATOM   21023 C  CD  . ARG C 1 885  ? 7.898    34.376  35.363  1.00 208.71 ? 885  ARG B CD  1 
ATOM   21024 N  NE  . ARG C 1 885  ? 9.185    34.919  35.797  1.00 211.36 ? 885  ARG B NE  1 
ATOM   21025 C  CZ  . ARG C 1 885  ? 9.901    35.784  35.084  1.00 213.28 ? 885  ARG B CZ  1 
ATOM   21026 N  NH1 . ARG C 1 885  ? 9.447    36.204  33.906  1.00 213.20 ? 885  ARG B NH1 1 
ATOM   21027 N  NH2 . ARG C 1 885  ? 11.064   36.232  35.546  1.00 214.79 ? 885  ARG B NH2 1 
ATOM   21028 N  N   . GLN C 1 886  ? 3.984    34.877  38.990  1.00 203.42 ? 886  GLN B N   1 
ATOM   21029 C  CA  . GLN C 1 886  ? 2.563    35.037  38.808  1.00 202.55 ? 886  GLN B CA  1 
ATOM   21030 C  C   . GLN C 1 886  ? 2.268    36.357  38.116  1.00 199.61 ? 886  GLN B C   1 
ATOM   21031 O  O   . GLN C 1 886  ? 3.185    37.060  37.697  1.00 200.06 ? 886  GLN B O   1 
ATOM   21032 C  CB  . GLN C 1 886  ? 1.905    35.024  40.176  1.00 209.09 ? 886  GLN B CB  1 
ATOM   21033 C  CG  . GLN C 1 886  ? 0.446    34.706  40.139  1.00 213.70 ? 886  GLN B CG  1 
ATOM   21034 C  CD  . GLN C 1 886  ? 0.188    33.218  40.081  1.00 217.87 ? 886  GLN B CD  1 
ATOM   21035 O  OE1 . GLN C 1 886  ? -0.963   32.777  40.160  1.00 219.83 ? 886  GLN B OE1 1 
ATOM   21036 N  NE2 . GLN C 1 886  ? 1.255    32.430  39.955  1.00 218.76 ? 886  GLN B NE2 1 
ATOM   21037 N  N   . LYS C 1 887  ? 0.986    36.704  38.021  1.00 195.58 ? 887  LYS B N   1 
ATOM   21038 C  CA  . LYS C 1 887  ? 0.569    37.957  37.396  1.00 193.49 ? 887  LYS B CA  1 
ATOM   21039 C  C   . LYS C 1 887  ? -0.446   38.678  38.283  1.00 190.46 ? 887  LYS B C   1 
ATOM   21040 O  O   . LYS C 1 887  ? -1.496   38.121  38.600  1.00 185.52 ? 887  LYS B O   1 
ATOM   21041 C  CB  . LYS C 1 887  ? -0.066   37.697  36.020  1.00 194.02 ? 887  LYS B CB  1 
ATOM   21042 C  CG  . LYS C 1 887  ? 0.620    36.637  35.145  1.00 195.02 ? 887  LYS B CG  1 
ATOM   21043 C  CD  . LYS C 1 887  ? 0.145    35.223  35.487  1.00 195.06 ? 887  LYS B CD  1 
ATOM   21044 C  CE  . LYS C 1 887  ? 0.804    34.160  34.610  1.00 195.45 ? 887  LYS B CE  1 
ATOM   21045 N  NZ  . LYS C 1 887  ? 0.246    34.130  33.234  1.00 194.38 ? 887  LYS B NZ  1 
ATOM   21046 N  N   . VAL C 1 888  ? -0.132   39.910  38.685  1.00 191.74 ? 888  VAL B N   1 
ATOM   21047 C  CA  . VAL C 1 888  ? -1.055   40.722  39.482  1.00 190.97 ? 888  VAL B CA  1 
ATOM   21048 C  C   . VAL C 1 888  ? -1.822   41.700  38.643  1.00 193.95 ? 888  VAL B C   1 
ATOM   21049 O  O   . VAL C 1 888  ? -1.244   42.627  38.082  1.00 197.57 ? 888  VAL B O   1 
ATOM   21050 C  CB  . VAL C 1 888  ? -0.331   41.593  40.503  1.00 188.20 ? 888  VAL B CB  1 
ATOM   21051 C  CG1 . VAL C 1 888  ? -0.400   40.974  41.882  1.00 186.65 ? 888  VAL B CG1 1 
ATOM   21052 C  CG2 . VAL C 1 888  ? 1.091    41.854  40.050  1.00 187.58 ? 888  VAL B CG2 1 
ATOM   21053 N  N   . GLU C 1 889  ? -3.133   41.523  38.594  1.00 195.11 ? 889  GLU B N   1 
ATOM   21054 C  CA  . GLU C 1 889  ? -3.986   42.462  37.882  1.00 200.38 ? 889  GLU B CA  1 
ATOM   21055 C  C   . GLU C 1 889  ? -3.847   43.884  38.468  1.00 198.17 ? 889  GLU B C   1 
ATOM   21056 O  O   . GLU C 1 889  ? -3.709   44.057  39.682  1.00 195.66 ? 889  GLU B O   1 
ATOM   21057 C  CB  . GLU C 1 889  ? -5.443   41.969  37.880  1.00 209.77 ? 889  GLU B CB  1 
ATOM   21058 C  CG  . GLU C 1 889  ? -6.078   41.787  39.268  1.00 221.02 ? 889  GLU B CG  1 
ATOM   21059 C  CD  . GLU C 1 889  ? -5.635   40.517  40.002  1.00 229.76 ? 889  GLU B CD  1 
ATOM   21060 O  OE1 . GLU C 1 889  ? -4.883   39.703  39.420  1.00 233.11 ? 889  GLU B OE1 1 
ATOM   21061 O  OE2 . GLU C 1 889  ? -6.054   40.336  41.171  1.00 232.61 ? 889  GLU B OE2 1 
ATOM   21062 N  N   . GLY C 1 890  ? -3.869   44.893  37.597  1.00 198.99 ? 890  GLY B N   1 
ATOM   21063 C  CA  . GLY C 1 890  ? -3.574   46.263  37.984  1.00 196.32 ? 890  GLY B CA  1 
ATOM   21064 C  C   . GLY C 1 890  ? -4.453   46.803  39.088  1.00 189.06 ? 890  GLY B C   1 
ATOM   21065 O  O   . GLY C 1 890  ? -5.638   46.493  39.148  1.00 186.99 ? 890  GLY B O   1 
ATOM   21066 N  N   . SER C 1 891  ? -3.863   47.612  39.962  1.00 183.44 ? 891  SER B N   1 
ATOM   21067 C  CA  . SER C 1 891  ? -4.585   48.239  41.070  1.00 177.89 ? 891  SER B CA  1 
ATOM   21068 C  C   . SER C 1 891  ? -5.305   47.232  41.951  1.00 175.53 ? 891  SER B C   1 
ATOM   21069 O  O   . SER C 1 891  ? -6.398   47.510  42.455  1.00 175.73 ? 891  SER B O   1 
ATOM   21070 C  CB  . SER C 1 891  ? -5.588   49.260  40.549  1.00 175.70 ? 891  SER B CB  1 
ATOM   21071 O  OG  . SER C 1 891  ? -4.934   50.212  39.740  1.00 176.25 ? 891  SER B OG  1 
ATOM   21072 N  N   . SER C 1 892  ? -4.677   46.073  42.139  1.00 172.34 ? 892  SER B N   1 
ATOM   21073 C  CA  . SER C 1 892  ? -5.270   44.977  42.897  1.00 170.06 ? 892  SER B CA  1 
ATOM   21074 C  C   . SER C 1 892  ? -4.214   44.259  43.719  1.00 169.52 ? 892  SER B C   1 
ATOM   21075 O  O   . SER C 1 892  ? -3.218   44.863  44.115  1.00 168.16 ? 892  SER B O   1 
ATOM   21076 C  CB  . SER C 1 892  ? -5.941   43.976  41.959  1.00 168.65 ? 892  SER B CB  1 
ATOM   21077 O  OG  . SER C 1 892  ? -7.002   44.572  41.239  1.00 168.07 ? 892  SER B OG  1 
ATOM   21078 N  N   . SER C 1 893  ? -4.439   42.967  43.964  1.00 169.86 ? 893  SER B N   1 
ATOM   21079 C  CA  . SER C 1 893  ? -3.520   42.157  44.753  1.00 170.74 ? 893  SER B CA  1 
ATOM   21080 C  C   . SER C 1 893  ? -3.720   40.661  44.571  1.00 170.85 ? 893  SER B C   1 
ATOM   21081 O  O   . SER C 1 893  ? -4.846   40.177  44.552  1.00 171.12 ? 893  SER B O   1 
ATOM   21082 C  CB  . SER C 1 893  ? -3.695   42.470  46.225  1.00 169.54 ? 893  SER B CB  1 
ATOM   21083 O  OG  . SER C 1 893  ? -2.775   41.717  46.984  1.00 169.51 ? 893  SER B OG  1 
ATOM   21084 N  N   . HIS C 1 894  ? -2.615   39.927  44.467  1.00 174.22 ? 894  HIS B N   1 
ATOM   21085 C  CA  . HIS C 1 894  ? -2.668   38.472  44.336  1.00 183.28 ? 894  HIS B CA  1 
ATOM   21086 C  C   . HIS C 1 894  ? -2.253   37.743  45.593  1.00 166.22 ? 894  HIS B C   1 
ATOM   21087 O  O   . HIS C 1 894  ? -1.113   37.853  46.028  1.00 164.90 ? 894  HIS B O   1 
ATOM   21088 C  CB  . HIS C 1 894  ? -1.774   38.005  43.187  1.00 220.84 ? 894  HIS B CB  1 
ATOM   21089 C  CG  . HIS C 1 894  ? -1.539   36.474  43.160  1.00 268.08 ? 894  HIS B CG  1 
ATOM   21090 N  ND1 . HIS C 1 894  ? -2.308   35.590  43.885  1.00 292.84 ? 894  HIS B ND1 1 
ATOM   21091 C  CD2 . HIS C 1 894  ? -0.627   35.726  42.497  1.00 288.68 ? 894  HIS B CD2 1 
ATOM   21092 C  CE1 . HIS C 1 894  ? -1.880   34.360  43.669  1.00 312.55 ? 894  HIS B CE1 1 
ATOM   21093 N  NE2 . HIS C 1 894  ? -0.862   34.415  42.831  1.00 302.32 ? 894  HIS B NE2 1 
ATOM   21094 N  N   . LEU C 1 895  ? -3.176   36.972  46.152  1.00 157.35 ? 895  LEU B N   1 
ATOM   21095 C  CA  . LEU C 1 895  ? -2.884   36.159  47.317  1.00 150.78 ? 895  LEU B CA  1 
ATOM   21096 C  C   . LEU C 1 895  ? -1.606   35.387  47.144  1.00 142.83 ? 895  LEU B C   1 
ATOM   21097 O  O   . LEU C 1 895  ? -1.273   34.941  46.049  1.00 142.55 ? 895  LEU B O   1 
ATOM   21098 C  CB  . LEU C 1 895  ? -4.004   35.166  47.552  1.00 152.92 ? 895  LEU B CB  1 
ATOM   21099 C  CG  . LEU C 1 895  ? -4.847   35.496  48.768  1.00 155.10 ? 895  LEU B CG  1 
ATOM   21100 C  CD1 . LEU C 1 895  ? -6.307   35.217  48.440  1.00 154.87 ? 895  LEU B CD1 1 
ATOM   21101 C  CD2 . LEU C 1 895  ? -4.351   34.716  49.991  1.00 155.71 ? 895  LEU B CD2 1 
ATOM   21102 N  N   . VAL C 1 896  ? -0.892   35.225  48.242  1.00 134.10 ? 896  VAL B N   1 
ATOM   21103 C  CA  . VAL C 1 896  ? 0.288    34.406  48.238  1.00 126.24 ? 896  VAL B CA  1 
ATOM   21104 C  C   . VAL C 1 896  ? 0.103    33.493  49.416  1.00 123.91 ? 896  VAL B C   1 
ATOM   21105 O  O   . VAL C 1 896  ? -0.690   33.789  50.313  1.00 124.41 ? 896  VAL B O   1 
ATOM   21106 C  CB  . VAL C 1 896  ? 1.550    35.229  48.477  1.00 122.20 ? 896  VAL B CB  1 
ATOM   21107 C  CG1 . VAL C 1 896  ? 2.758    34.420  48.118  1.00 122.61 ? 896  VAL B CG1 1 
ATOM   21108 C  CG2 . VAL C 1 896  ? 1.528    36.487  47.666  1.00 120.37 ? 896  VAL B CG2 1 
ATOM   21109 N  N   . THR C 1 897  ? 0.807    32.369  49.406  1.00 119.87 ? 897  THR B N   1 
ATOM   21110 C  CA  . THR C 1 897  ? 0.834    31.494  50.555  1.00 116.02 ? 897  THR B CA  1 
ATOM   21111 C  C   . THR C 1 897  ? 2.063    30.616  50.497  1.00 118.47 ? 897  THR B C   1 
ATOM   21112 O  O   . THR C 1 897  ? 2.693    30.455  49.449  1.00 120.10 ? 897  THR B O   1 
ATOM   21113 C  CB  . THR C 1 897  ? -0.350   30.555  50.587  1.00 111.63 ? 897  THR B CB  1 
ATOM   21114 O  OG1 . THR C 1 897  ? 0.123    29.211  50.489  1.00 112.03 ? 897  THR B OG1 1 
ATOM   21115 C  CG2 . THR C 1 897  ? -1.262   30.826  49.441  1.00 109.86 ? 897  THR B CG2 1 
ATOM   21116 N  N   . PHE C 1 898  ? 2.392    30.053  51.652  1.00 119.12 ? 898  PHE B N   1 
ATOM   21117 C  CA  . PHE C 1 898  ? 3.441    29.063  51.791  1.00 118.63 ? 898  PHE B CA  1 
ATOM   21118 C  C   . PHE C 1 898  ? 3.030    28.158  52.937  1.00 116.30 ? 898  PHE B C   1 
ATOM   21119 O  O   . PHE C 1 898  ? 2.412    28.596  53.905  1.00 115.38 ? 898  PHE B O   1 
ATOM   21120 C  CB  . PHE C 1 898  ? 4.772    29.717  52.152  1.00 119.01 ? 898  PHE B CB  1 
ATOM   21121 C  CG  . PHE C 1 898  ? 5.238    30.742  51.167  1.00 118.44 ? 898  PHE B CG  1 
ATOM   21122 C  CD1 . PHE C 1 898  ? 6.328    30.493  50.361  1.00 119.03 ? 898  PHE B CD1 1 
ATOM   21123 C  CD2 . PHE C 1 898  ? 4.605    31.962  51.070  1.00 117.97 ? 898  PHE B CD2 1 
ATOM   21124 C  CE1 . PHE C 1 898  ? 6.771    31.431  49.469  1.00 119.86 ? 898  PHE B CE1 1 
ATOM   21125 C  CE2 . PHE C 1 898  ? 5.040    32.907  50.177  1.00 118.75 ? 898  PHE B CE2 1 
ATOM   21126 C  CZ  . PHE C 1 898  ? 6.127    32.642  49.375  1.00 119.95 ? 898  PHE B CZ  1 
ATOM   21127 N  N   . THR C 1 899  ? 3.369    26.890  52.830  1.00 116.17 ? 899  THR B N   1 
ATOM   21128 C  CA  . THR C 1 899  ? 3.229    26.012  53.965  1.00 113.34 ? 899  THR B CA  1 
ATOM   21129 C  C   . THR C 1 899  ? 4.631    25.754  54.526  1.00 111.28 ? 899  THR B C   1 
ATOM   21130 O  O   . THR C 1 899  ? 5.582    25.645  53.761  1.00 110.26 ? 899  THR B O   1 
ATOM   21131 C  CB  . THR C 1 899  ? 2.417    24.740  53.575  1.00 116.49 ? 899  THR B CB  1 
ATOM   21132 O  OG1 . THR C 1 899  ? 3.124    23.969  52.583  1.00 116.92 ? 899  THR B OG1 1 
ATOM   21133 C  CG2 . THR C 1 899  ? 1.024    25.163  53.031  1.00 108.87 ? 899  THR B CG2 1 
ATOM   21134 N  N   . VAL C 1 900  ? 4.747    25.755  55.859  1.00 111.93 ? 900  VAL B N   1 
ATOM   21135 C  CA  . VAL C 1 900  ? 5.995    25.478  56.607  1.00 111.63 ? 900  VAL B CA  1 
ATOM   21136 C  C   . VAL C 1 900  ? 5.692    24.584  57.793  1.00 109.70 ? 900  VAL B C   1 
ATOM   21137 O  O   . VAL C 1 900  ? 4.546    24.171  58.009  1.00 107.39 ? 900  VAL B O   1 
ATOM   21138 C  CB  . VAL C 1 900  ? 6.710    26.754  57.196  1.00 95.52  ? 900  VAL B CB  1 
ATOM   21139 C  CG1 . VAL C 1 900  ? 7.788    27.277  56.253  1.00 97.22  ? 900  VAL B CG1 1 
ATOM   21140 C  CG2 . VAL C 1 900  ? 5.712    27.854  57.573  1.00 93.58  ? 900  VAL B CG2 1 
ATOM   21141 N  N   . LEU C 1 901  ? 6.719    24.287  58.572  1.00 111.04 ? 901  LEU B N   1 
ATOM   21142 C  CA  . LEU C 1 901  ? 6.515    23.428  59.728  1.00 115.09 ? 901  LEU B CA  1 
ATOM   21143 C  C   . LEU C 1 901  ? 7.785    23.300  60.573  1.00 123.42 ? 901  LEU B C   1 
ATOM   21144 O  O   . LEU C 1 901  ? 8.716    22.559  60.211  1.00 125.00 ? 901  LEU B O   1 
ATOM   21145 C  CB  . LEU C 1 901  ? 5.967    22.066  59.288  1.00 112.75 ? 901  LEU B CB  1 
ATOM   21146 C  CG  . LEU C 1 901  ? 6.243    20.854  60.164  1.00 112.53 ? 901  LEU B CG  1 
ATOM   21147 C  CD1 . LEU C 1 901  ? 5.007    20.002  60.263  1.00 111.11 ? 901  LEU B CD1 1 
ATOM   21148 C  CD2 . LEU C 1 901  ? 7.400    20.083  59.572  1.00 113.97 ? 901  LEU B CD2 1 
ATOM   21149 N  N   . PRO C 1 902  ? 7.826    24.029  61.710  1.00 123.53 ? 902  PRO B N   1 
ATOM   21150 C  CA  . PRO C 1 902  ? 9.080    24.147  62.443  1.00 127.81 ? 902  PRO B CA  1 
ATOM   21151 C  C   . PRO C 1 902  ? 9.228    22.994  63.418  1.00 129.65 ? 902  PRO B C   1 
ATOM   21152 O  O   . PRO C 1 902  ? 8.232    22.546  63.993  1.00 129.08 ? 902  PRO B O   1 
ATOM   21153 C  CB  . PRO C 1 902  ? 8.905    25.476  63.194  1.00 126.96 ? 902  PRO B CB  1 
ATOM   21154 C  CG  . PRO C 1 902  ? 7.515    26.018  62.790  1.00 121.62 ? 902  PRO B CG  1 
ATOM   21155 C  CD  . PRO C 1 902  ? 6.766    24.818  62.359  1.00 121.12 ? 902  PRO B CD  1 
ATOM   21156 N  N   . LEU C 1 903  ? 10.452   22.500  63.573  1.00 133.81 ? 903  LEU B N   1 
ATOM   21157 C  CA  . LEU C 1 903  ? 10.753   21.493  64.597  1.00 136.83 ? 903  LEU B CA  1 
ATOM   21158 C  C   . LEU C 1 903  ? 11.590   22.134  65.715  1.00 139.35 ? 903  LEU B C   1 
ATOM   21159 O  O   . LEU C 1 903  ? 11.550   21.738  66.881  1.00 140.83 ? 903  LEU B O   1 
ATOM   21160 C  CB  . LEU C 1 903  ? 11.484   20.274  63.986  1.00 137.01 ? 903  LEU B CB  1 
ATOM   21161 C  CG  . LEU C 1 903  ? 11.073   19.663  62.629  1.00 133.78 ? 903  LEU B CG  1 
ATOM   21162 C  CD1 . LEU C 1 903  ? 9.634    19.192  62.647  1.00 132.28 ? 903  LEU B CD1 1 
ATOM   21163 C  CD2 . LEU C 1 903  ? 11.326   20.617  61.457  1.00 132.73 ? 903  LEU B CD2 1 
ATOM   21164 N  N   . GLU C 1 904  ? 12.354   23.139  65.336  1.00 141.32 ? 904  GLU B N   1 
ATOM   21165 C  CA  . GLU C 1 904  ? 13.145   23.847  66.305  1.00 146.93 ? 904  GLU B CA  1 
ATOM   21166 C  C   . GLU C 1 904  ? 12.319   24.946  66.992  1.00 146.29 ? 904  GLU B C   1 
ATOM   21167 O  O   . GLU C 1 904  ? 11.787   25.862  66.329  1.00 141.59 ? 904  GLU B O   1 
ATOM   21168 C  CB  . GLU C 1 904  ? 14.413   24.385  65.644  1.00 155.84 ? 904  GLU B CB  1 
ATOM   21169 C  CG  . GLU C 1 904  ? 15.254   23.284  64.994  1.00 161.85 ? 904  GLU B CG  1 
ATOM   21170 C  CD  . GLU C 1 904  ? 16.736   23.624  64.953  1.00 169.75 ? 904  GLU B CD  1 
ATOM   21171 O  OE1 . GLU C 1 904  ? 17.085   24.812  65.166  1.00 173.26 ? 904  GLU B OE1 1 
ATOM   21172 O  OE2 . GLU C 1 904  ? 17.546   22.700  64.707  1.00 172.68 ? 904  GLU B OE2 1 
ATOM   21173 N  N   . ILE C 1 905  ? 12.218   24.828  68.322  1.00 144.69 ? 905  ILE B N   1 
ATOM   21174 C  CA  . ILE C 1 905  ? 11.391   25.714  69.138  1.00 136.52 ? 905  ILE B CA  1 
ATOM   21175 C  C   . ILE C 1 905  ? 12.009   27.083  69.155  1.00 134.21 ? 905  ILE B C   1 
ATOM   21176 O  O   . ILE C 1 905  ? 13.209   27.209  68.936  1.00 123.05 ? 905  ILE B O   1 
ATOM   21177 C  CB  . ILE C 1 905  ? 11.218   25.176  70.589  1.00 115.63 ? 905  ILE B CB  1 
ATOM   21178 C  CG1 . ILE C 1 905  ? 11.034   23.653  70.568  1.00 116.19 ? 905  ILE B CG1 1 
ATOM   21179 C  CG2 . ILE C 1 905  ? 10.051   25.855  71.291  1.00 111.01 ? 905  ILE B CG2 1 
ATOM   21180 C  CD1 . ILE C 1 905  ? 9.801    23.163  71.316  1.00 114.72 ? 905  ILE B CD1 1 
ATOM   21181 N  N   . GLY C 1 906  ? 11.169   28.096  69.369  1.00 138.81 ? 906  GLY B N   1 
ATOM   21182 C  CA  . GLY C 1 906  ? 11.588   29.486  69.486  1.00 147.36 ? 906  GLY B CA  1 
ATOM   21183 C  C   . GLY C 1 906  ? 12.140   30.108  68.220  1.00 150.01 ? 906  GLY B C   1 
ATOM   21184 O  O   . GLY C 1 906  ? 11.916   31.282  67.949  1.00 149.10 ? 906  GLY B O   1 
ATOM   21185 N  N   . LEU C 1 907  ? 12.853   29.285  67.451  1.00 155.31 ? 907  LEU B N   1 
ATOM   21186 C  CA  . LEU C 1 907  ? 13.490   29.664  66.187  1.00 158.92 ? 907  LEU B CA  1 
ATOM   21187 C  C   . LEU C 1 907  ? 12.638   30.591  65.358  1.00 159.83 ? 907  LEU B C   1 
ATOM   21188 O  O   . LEU C 1 907  ? 11.423   30.457  65.308  1.00 157.48 ? 907  LEU B O   1 
ATOM   21189 C  CB  . LEU C 1 907  ? 13.781   28.421  65.352  1.00 160.55 ? 907  LEU B CB  1 
ATOM   21190 C  CG  . LEU C 1 907  ? 14.226   28.749  63.937  1.00 166.29 ? 907  LEU B CG  1 
ATOM   21191 C  CD1 . LEU C 1 907  ? 15.441   29.670  63.931  1.00 169.72 ? 907  LEU B CD1 1 
ATOM   21192 C  CD2 . LEU C 1 907  ? 14.528   27.459  63.252  1.00 170.10 ? 907  LEU B CD2 1 
ATOM   21193 N  N   . HIS C 1 908  ? 13.274   31.516  64.671  1.00 164.91 ? 908  HIS B N   1 
ATOM   21194 C  CA  . HIS C 1 908  ? 12.507   32.551  64.030  1.00 168.15 ? 908  HIS B CA  1 
ATOM   21195 C  C   . HIS C 1 908  ? 13.104   32.837  62.676  1.00 167.64 ? 908  HIS B C   1 
ATOM   21196 O  O   . HIS C 1 908  ? 13.903   32.054  62.169  1.00 169.93 ? 908  HIS B O   1 
ATOM   21197 C  CB  . HIS C 1 908  ? 12.533   33.826  64.881  1.00 170.36 ? 908  HIS B CB  1 
ATOM   21198 C  CG  . HIS C 1 908  ? 12.700   33.587  66.356  1.00 167.80 ? 908  HIS B CG  1 
ATOM   21199 N  ND1 . HIS C 1 908  ? 13.690   32.780  66.875  1.00 166.08 ? 908  HIS B ND1 1 
ATOM   21200 C  CD2 . HIS C 1 908  ? 12.026   34.090  67.419  1.00 165.11 ? 908  HIS B CD2 1 
ATOM   21201 C  CE1 . HIS C 1 908  ? 13.605   32.782  68.192  1.00 166.03 ? 908  HIS B CE1 1 
ATOM   21202 N  NE2 . HIS C 1 908  ? 12.600   33.563  68.547  1.00 165.21 ? 908  HIS B NE2 1 
ATOM   21203 N  N   . ASN C 1 909  ? 12.705   33.967  62.106  1.00 164.49 ? 909  ASN B N   1 
ATOM   21204 C  CA  . ASN C 1 909  ? 13.290   34.476  60.874  1.00 164.35 ? 909  ASN B CA  1 
ATOM   21205 C  C   . ASN C 1 909  ? 12.933   33.699  59.607  1.00 158.15 ? 909  ASN B C   1 
ATOM   21206 O  O   . ASN C 1 909  ? 13.204   32.508  59.478  1.00 156.69 ? 909  ASN B O   1 
ATOM   21207 C  CB  . ASN C 1 909  ? 14.810   34.608  60.998  1.00 171.22 ? 909  ASN B CB  1 
ATOM   21208 C  CG  . ASN C 1 909  ? 15.463   34.983  59.682  1.00 176.69 ? 909  ASN B CG  1 
ATOM   21209 O  OD1 . ASN C 1 909  ? 16.470   34.400  59.277  1.00 179.58 ? 909  ASN B OD1 1 
ATOM   21210 N  ND2 . ASN C 1 909  ? 14.876   35.952  58.997  1.00 177.96 ? 909  ASN B ND2 1 
ATOM   21211 N  N   . ILE C 1 910  ? 12.327   34.417  58.673  1.00 154.09 ? 910  ILE B N   1 
ATOM   21212 C  CA  . ILE C 1 910  ? 12.046   33.924  57.346  1.00 147.42 ? 910  ILE B CA  1 
ATOM   21213 C  C   . ILE C 1 910  ? 12.111   35.155  56.441  1.00 148.76 ? 910  ILE B C   1 
ATOM   21214 O  O   . ILE C 1 910  ? 11.374   36.123  56.647  1.00 153.17 ? 910  ILE B O   1 
ATOM   21215 C  CB  . ILE C 1 910  ? 10.659   33.272  57.279  1.00 137.00 ? 910  ILE B CB  1 
ATOM   21216 C  CG1 . ILE C 1 910  ? 10.636   31.975  58.085  1.00 132.33 ? 910  ILE B CG1 1 
ATOM   21217 C  CG2 . ILE C 1 910  ? 10.277   33.005  55.850  1.00 134.36 ? 910  ILE B CG2 1 
ATOM   21218 C  CD1 . ILE C 1 910  ? 9.353    31.178  57.942  1.00 127.98 ? 910  ILE B CD1 1 
ATOM   21219 N  N   . ASN C 1 911  ? 13.043   35.149  55.488  1.00 145.38 ? 911  ASN B N   1 
ATOM   21220 C  CA  . ASN C 1 911  ? 13.146   36.224  54.507  1.00 140.35 ? 911  ASN B CA  1 
ATOM   21221 C  C   . ASN C 1 911  ? 12.067   35.969  53.445  1.00 141.03 ? 911  ASN B C   1 
ATOM   21222 O  O   . ASN C 1 911  ? 11.811   34.817  53.088  1.00 140.29 ? 911  ASN B O   1 
ATOM   21223 C  CB  . ASN C 1 911  ? 14.548   36.275  53.853  1.00 140.76 ? 911  ASN B CB  1 
ATOM   21224 C  CG  . ASN C 1 911  ? 15.710   36.587  54.862  1.00 144.06 ? 911  ASN B CG  1 
ATOM   21225 O  OD1 . ASN C 1 911  ? 16.253   35.679  55.518  1.00 147.48 ? 911  ASN B OD1 1 
ATOM   21226 N  ND2 . ASN C 1 911  ? 16.135   37.859  54.918  1.00 141.89 ? 911  ASN B ND2 1 
ATOM   21227 N  N   . PHE C 1 912  ? 11.424   37.022  52.951  1.00 142.48 ? 912  PHE B N   1 
ATOM   21228 C  CA  . PHE C 1 912  ? 10.475   36.886  51.849  1.00 141.16 ? 912  PHE B CA  1 
ATOM   21229 C  C   . PHE C 1 912  ? 10.916   37.838  50.763  1.00 145.37 ? 912  PHE B C   1 
ATOM   21230 O  O   . PHE C 1 912  ? 11.358   38.940  51.055  1.00 148.29 ? 912  PHE B O   1 
ATOM   21231 C  CB  . PHE C 1 912  ? 9.050    37.219  52.291  1.00 134.36 ? 912  PHE B CB  1 
ATOM   21232 C  CG  . PHE C 1 912  ? 8.365    36.097  53.007  1.00 127.64 ? 912  PHE B CG  1 
ATOM   21233 C  CD1 . PHE C 1 912  ? 8.131    34.902  52.379  1.00 123.93 ? 912  PHE B CD1 1 
ATOM   21234 C  CD2 . PHE C 1 912  ? 7.959    36.230  54.311  1.00 125.85 ? 912  PHE B CD2 1 
ATOM   21235 C  CE1 . PHE C 1 912  ? 7.504    33.862  53.042  1.00 121.06 ? 912  PHE B CE1 1 
ATOM   21236 C  CE2 . PHE C 1 912  ? 7.328    35.179  54.973  1.00 122.71 ? 912  PHE B CE2 1 
ATOM   21237 C  CZ  . PHE C 1 912  ? 7.105    34.004  54.334  1.00 120.04 ? 912  PHE B CZ  1 
ATOM   21238 N  N   . SER C 1 913  ? 10.803   37.419  49.512  1.00 146.91 ? 913  SER B N   1 
ATOM   21239 C  CA  . SER C 1 913  ? 11.291   38.218  48.395  1.00 151.01 ? 913  SER B CA  1 
ATOM   21240 C  C   . SER C 1 913  ? 10.245   38.244  47.275  1.00 155.01 ? 913  SER B C   1 
ATOM   21241 O  O   . SER C 1 913  ? 9.464    37.301  47.132  1.00 153.61 ? 913  SER B O   1 
ATOM   21242 C  CB  . SER C 1 913  ? 12.608   37.610  47.885  1.00 150.33 ? 913  SER B CB  1 
ATOM   21243 O  OG  . SER C 1 913  ? 13.126   38.294  46.753  1.00 149.88 ? 913  SER B OG  1 
ATOM   21244 N  N   . LEU C 1 914  ? 10.210   39.315  46.488  1.00 161.21 ? 914  LEU B N   1 
ATOM   21245 C  CA  . LEU C 1 914  ? 9.446    39.275  45.240  1.00 164.14 ? 914  LEU B CA  1 
ATOM   21246 C  C   . LEU C 1 914  ? 10.177   39.945  44.077  1.00 174.68 ? 914  LEU B C   1 
ATOM   21247 O  O   . LEU C 1 914  ? 11.061   40.781  44.283  1.00 177.77 ? 914  LEU B O   1 
ATOM   21248 C  CB  . LEU C 1 914  ? 8.032    39.833  45.403  1.00 156.59 ? 914  LEU B CB  1 
ATOM   21249 C  CG  . LEU C 1 914  ? 7.796    41.214  45.999  1.00 150.40 ? 914  LEU B CG  1 
ATOM   21250 C  CD1 . LEU C 1 914  ? 8.869    42.217  45.597  1.00 149.07 ? 914  LEU B CD1 1 
ATOM   21251 C  CD2 . LEU C 1 914  ? 6.408    41.689  45.583  1.00 146.35 ? 914  LEU B CD2 1 
ATOM   21252 N  N   . GLU C 1 915  ? 9.801    39.571  42.856  1.00 180.87 ? 915  GLU B N   1 
ATOM   21253 C  CA  . GLU C 1 915  ? 10.506   40.037  41.665  1.00 188.55 ? 915  GLU B CA  1 
ATOM   21254 C  C   . GLU C 1 915  ? 9.580    40.667  40.623  1.00 193.88 ? 915  GLU B C   1 
ATOM   21255 O  O   . GLU C 1 915  ? 8.624    40.049  40.158  1.00 189.85 ? 915  GLU B O   1 
ATOM   21256 C  CB  . GLU C 1 915  ? 11.322   38.897  41.036  1.00 191.91 ? 915  GLU B CB  1 
ATOM   21257 C  CG  . GLU C 1 915  ? 12.628   38.562  41.764  1.00 196.42 ? 915  GLU B CG  1 
ATOM   21258 C  CD  . GLU C 1 915  ? 12.512   37.360  42.689  1.00 199.35 ? 915  GLU B CD  1 
ATOM   21259 O  OE1 . GLU C 1 915  ? 11.774   36.410  42.349  1.00 198.85 ? 915  GLU B OE1 1 
ATOM   21260 O  OE2 . GLU C 1 915  ? 13.174   37.358  43.751  1.00 202.38 ? 915  GLU B OE2 1 
ATOM   21261 N  N   . THR C 1 916  ? 9.897    41.907  40.264  1.00 202.13 ? 916  THR B N   1 
ATOM   21262 C  CA  . THR C 1 916  ? 9.177    42.645  39.243  1.00 209.27 ? 916  THR B CA  1 
ATOM   21263 C  C   . THR C 1 916  ? 10.195   43.285  38.312  1.00 219.87 ? 916  THR B C   1 
ATOM   21264 O  O   . THR C 1 916  ? 11.292   43.646  38.732  1.00 221.35 ? 916  THR B O   1 
ATOM   21265 C  CB  . THR C 1 916  ? 8.284    43.736  39.856  1.00 206.32 ? 916  THR B CB  1 
ATOM   21266 O  OG1 . THR C 1 916  ? 7.300    43.122  40.691  1.00 204.27 ? 916  THR B OG1 1 
ATOM   21267 C  CG2 . THR C 1 916  ? 7.575    44.539  38.772  1.00 204.61 ? 916  THR B CG2 1 
ATOM   21268 N  N   . TRP C 1 917  ? 9.817    43.407  37.046  1.00 228.20 ? 917  TRP B N   1 
ATOM   21269 C  CA  . TRP C 1 917  ? 10.675   43.944  35.997  1.00 238.26 ? 917  TRP B CA  1 
ATOM   21270 C  C   . TRP C 1 917  ? 11.609   45.031  36.515  1.00 243.13 ? 917  TRP B C   1 
ATOM   21271 O  O   . TRP C 1 917  ? 12.814   44.996  36.268  1.00 243.54 ? 917  TRP B O   1 
ATOM   21272 C  CB  . TRP C 1 917  ? 9.797    44.509  34.878  1.00 241.93 ? 917  TRP B CB  1 
ATOM   21273 C  CG  . TRP C 1 917  ? 10.369   44.386  33.500  1.00 247.08 ? 917  TRP B CG  1 
ATOM   21274 C  CD1 . TRP C 1 917  ? 10.905   45.389  32.742  1.00 249.68 ? 917  TRP B CD1 1 
ATOM   21275 C  CD2 . TRP C 1 917  ? 10.445   43.195  32.704  1.00 249.49 ? 917  TRP B CD2 1 
ATOM   21276 N  NE1 . TRP C 1 917  ? 11.314   44.895  31.526  1.00 250.75 ? 917  TRP B NE1 1 
ATOM   21277 C  CE2 . TRP C 1 917  ? 11.044   43.551  31.478  1.00 250.31 ? 917  TRP B CE2 1 
ATOM   21278 C  CE3 . TRP C 1 917  ? 10.070   41.862  32.910  1.00 249.38 ? 917  TRP B CE3 1 
ATOM   21279 C  CZ2 . TRP C 1 917  ? 11.276   42.624  30.465  1.00 250.48 ? 917  TRP B CZ2 1 
ATOM   21280 C  CZ3 . TRP C 1 917  ? 10.302   40.945  31.903  1.00 249.54 ? 917  TRP B CZ3 1 
ATOM   21281 C  CH2 . TRP C 1 917  ? 10.899   41.330  30.696  1.00 250.00 ? 917  TRP B CH2 1 
ATOM   21282 N  N   . PHE C 1 918  ? 11.048   46.000  37.229  1.00 248.71 ? 918  PHE B N   1 
ATOM   21283 C  CA  . PHE C 1 918  ? 11.841   47.112  37.736  1.00 253.86 ? 918  PHE B CA  1 
ATOM   21284 C  C   . PHE C 1 918  ? 11.990   47.119  39.255  1.00 248.04 ? 918  PHE B C   1 
ATOM   21285 O  O   . PHE C 1 918  ? 12.446   48.106  39.828  1.00 249.60 ? 918  PHE B O   1 
ATOM   21286 C  CB  . PHE C 1 918  ? 11.288   48.452  37.240  1.00 261.39 ? 918  PHE B CB  1 
ATOM   21287 C  CG  . PHE C 1 918  ? 9.904    48.758  37.726  1.00 265.62 ? 918  PHE B CG  1 
ATOM   21288 C  CD1 . PHE C 1 918  ? 9.713    49.476  38.891  1.00 268.28 ? 918  PHE B CD1 1 
ATOM   21289 C  CD2 . PHE C 1 918  ? 8.795    48.343  37.011  1.00 265.36 ? 918  PHE B CD2 1 
ATOM   21290 C  CE1 . PHE C 1 918  ? 8.441    49.767  39.340  1.00 268.28 ? 918  PHE B CE1 1 
ATOM   21291 C  CE2 . PHE C 1 918  ? 7.521    48.632  37.454  1.00 265.36 ? 918  PHE B CE2 1 
ATOM   21292 C  CZ  . PHE C 1 918  ? 7.343    49.345  38.620  1.00 266.49 ? 918  PHE B CZ  1 
ATOM   21293 N  N   . GLY C 1 919  ? 11.622   46.020  39.905  1.00 239.50 ? 919  GLY B N   1 
ATOM   21294 C  CA  . GLY C 1 919  ? 11.760   45.936  41.347  1.00 232.38 ? 919  GLY B CA  1 
ATOM   21295 C  C   . GLY C 1 919  ? 11.968   44.540  41.906  1.00 225.00 ? 919  GLY B C   1 
ATOM   21296 O  O   . GLY C 1 919  ? 11.273   43.601  41.525  1.00 223.08 ? 919  GLY B O   1 
ATOM   21297 N  N   . LYS C 1 920  ? 12.933   44.417  42.816  1.00 220.78 ? 920  LYS B N   1 
ATOM   21298 C  CA  . LYS C 1 920  ? 13.162   43.190  43.582  1.00 213.38 ? 920  LYS B CA  1 
ATOM   21299 C  C   . LYS C 1 920  ? 13.386   43.546  45.056  1.00 208.50 ? 920  LYS B C   1 
ATOM   21300 O  O   . LYS C 1 920  ? 14.384   44.175  45.418  1.00 211.42 ? 920  LYS B O   1 
ATOM   21301 C  CB  . LYS C 1 920  ? 14.356   42.405  43.035  1.00 212.37 ? 920  LYS B CB  1 
ATOM   21302 C  CG  . LYS C 1 920  ? 14.679   41.155  43.835  1.00 210.04 ? 920  LYS B CG  1 
ATOM   21303 C  CD  . LYS C 1 920  ? 15.609   40.233  43.068  1.00 208.12 ? 920  LYS B CD  1 
ATOM   21304 C  CE  . LYS C 1 920  ? 15.766   38.892  43.770  1.00 206.06 ? 920  LYS B CE  1 
ATOM   21305 N  NZ  . LYS C 1 920  ? 16.410   37.876  42.889  1.00 205.01 ? 920  LYS B NZ  1 
ATOM   21306 N  N   . GLU C 1 921  ? 12.459   43.117  45.904  1.00 199.11 ? 921  GLU B N   1 
ATOM   21307 C  CA  . GLU C 1 921  ? 12.351   43.647  47.257  1.00 192.42 ? 921  GLU B CA  1 
ATOM   21308 C  C   . GLU C 1 921  ? 12.364   42.520  48.294  1.00 182.46 ? 921  GLU B C   1 
ATOM   21309 O  O   . GLU C 1 921  ? 11.770   41.459  48.072  1.00 180.03 ? 921  GLU B O   1 
ATOM   21310 C  CB  . GLU C 1 921  ? 11.044   44.441  47.363  1.00 194.33 ? 921  GLU B CB  1 
ATOM   21311 C  CG  . GLU C 1 921  ? 10.865   45.233  48.643  1.00 199.54 ? 921  GLU B CG  1 
ATOM   21312 C  CD  . GLU C 1 921  ? 11.391   46.646  48.534  1.00 204.72 ? 921  GLU B CD  1 
ATOM   21313 O  OE1 . GLU C 1 921  ? 12.326   46.878  47.737  1.00 207.31 ? 921  GLU B OE1 1 
ATOM   21314 O  OE2 . GLU C 1 921  ? 10.866   47.524  49.250  1.00 206.16 ? 921  GLU B OE2 1 
ATOM   21315 N  N   . ILE C 1 922  ? 13.029   42.750  49.430  1.00 175.17 ? 922  ILE B N   1 
ATOM   21316 C  CA  . ILE C 1 922  ? 13.087   41.731  50.485  1.00 165.24 ? 922  ILE B CA  1 
ATOM   21317 C  C   . ILE C 1 922  ? 12.525   42.147  51.842  1.00 158.81 ? 922  ILE B C   1 
ATOM   21318 O  O   . ILE C 1 922  ? 12.983   43.105  52.470  1.00 158.63 ? 922  ILE B O   1 
ATOM   21319 C  CB  . ILE C 1 922  ? 14.497   41.189  50.726  1.00 164.37 ? 922  ILE B CB  1 
ATOM   21320 C  CG1 . ILE C 1 922  ? 14.874   40.166  49.652  1.00 161.96 ? 922  ILE B CG1 1 
ATOM   21321 C  CG2 . ILE C 1 922  ? 14.530   40.503  52.058  1.00 164.31 ? 922  ILE B CG2 1 
ATOM   21322 C  CD1 . ILE C 1 922  ? 15.953   39.168  50.081  1.00 161.97 ? 922  ILE B CD1 1 
ATOM   21323 N  N   . LEU C 1 923  ? 11.538   41.377  52.284  1.00 153.84 ? 923  LEU B N   1 
ATOM   21324 C  CA  . LEU C 1 923  ? 10.839   41.595  53.541  1.00 150.64 ? 923  LEU B CA  1 
ATOM   21325 C  C   . LEU C 1 923  ? 11.207   40.484  54.518  1.00 150.98 ? 923  LEU B C   1 
ATOM   21326 O  O   . LEU C 1 923  ? 11.065   39.298  54.184  1.00 151.09 ? 923  LEU B O   1 
ATOM   21327 C  CB  . LEU C 1 923  ? 9.322    41.616  53.277  1.00 147.54 ? 923  LEU B CB  1 
ATOM   21328 C  CG  . LEU C 1 923  ? 8.281    41.223  54.337  1.00 145.99 ? 923  LEU B CG  1 
ATOM   21329 C  CD1 . LEU C 1 923  ? 8.488    41.979  55.648  1.00 147.29 ? 923  LEU B CD1 1 
ATOM   21330 C  CD2 . LEU C 1 923  ? 6.861    41.438  53.817  1.00 143.07 ? 923  LEU B CD2 1 
ATOM   21331 N  N   . VAL C 1 924  ? 11.696   40.860  55.709  1.00 149.32 ? 924  VAL B N   1 
ATOM   21332 C  CA  . VAL C 1 924  ? 11.957   39.865  56.766  1.00 145.15 ? 924  VAL B CA  1 
ATOM   21333 C  C   . VAL C 1 924  ? 10.932   39.863  57.904  1.00 139.67 ? 924  VAL B C   1 
ATOM   21334 O  O   . VAL C 1 924  ? 10.371   40.903  58.275  1.00 135.82 ? 924  VAL B O   1 
ATOM   21335 C  CB  . VAL C 1 924  ? 13.381   39.933  57.373  1.00 147.75 ? 924  VAL B CB  1 
ATOM   21336 C  CG1 . VAL C 1 924  ? 13.753   38.564  57.899  1.00 147.49 ? 924  VAL B CG1 1 
ATOM   21337 C  CG2 . VAL C 1 924  ? 14.396   40.369  56.339  1.00 148.86 ? 924  VAL B CG2 1 
ATOM   21338 N  N   . LYS C 1 925  ? 10.747   38.670  58.463  1.00 135.87 ? 925  LYS B N   1 
ATOM   21339 C  CA  . LYS C 1 925  ? 9.638    38.332  59.333  1.00 130.95 ? 925  LYS B CA  1 
ATOM   21340 C  C   . LYS C 1 925  ? 10.234   37.366  60.363  1.00 129.21 ? 925  LYS B C   1 
ATOM   21341 O  O   . LYS C 1 925  ? 11.296   36.806  60.102  1.00 134.61 ? 925  LYS B O   1 
ATOM   21342 C  CB  . LYS C 1 925  ? 8.601    37.611  58.479  1.00 126.57 ? 925  LYS B CB  1 
ATOM   21343 C  CG  . LYS C 1 925  ? 7.194    37.992  58.769  1.00 123.60 ? 925  LYS B CG  1 
ATOM   21344 C  CD  . LYS C 1 925  ? 6.932    39.403  58.365  1.00 123.11 ? 925  LYS B CD  1 
ATOM   21345 C  CE  . LYS C 1 925  ? 5.661    39.910  59.003  1.00 122.85 ? 925  LYS B CE  1 
ATOM   21346 N  NZ  . LYS C 1 925  ? 5.280    41.235  58.439  1.00 123.58 ? 925  LYS B NZ  1 
ATOM   21347 N  N   . THR C 1 926  ? 9.597    37.160  61.522  1.00 120.44 ? 926  THR B N   1 
ATOM   21348 C  CA  . THR C 1 926  ? 10.127   36.195  62.520  1.00 115.16 ? 926  THR B CA  1 
ATOM   21349 C  C   . THR C 1 926  ? 9.058    35.343  63.245  1.00 109.82 ? 926  THR B C   1 
ATOM   21350 O  O   . THR C 1 926  ? 8.053    35.857  63.730  1.00 109.14 ? 926  THR B O   1 
ATOM   21351 C  CB  . THR C 1 926  ? 11.058   36.887  63.568  1.00 143.83 ? 926  THR B CB  1 
ATOM   21352 O  OG1 . THR C 1 926  ? 10.669   38.261  63.739  1.00 144.32 ? 926  THR B OG1 1 
ATOM   21353 C  CG2 . THR C 1 926  ? 12.535   36.826  63.135  1.00 143.73 ? 926  THR B CG2 1 
ATOM   21354 N  N   . LEU C 1 927  ? 9.302    34.041  63.336  1.00 108.04 ? 927  LEU B N   1 
ATOM   21355 C  CA  . LEU C 1 927  ? 8.248    33.084  63.682  1.00 108.32 ? 927  LEU B CA  1 
ATOM   21356 C  C   . LEU C 1 927  ? 8.325    32.487  65.090  1.00 109.84 ? 927  LEU B C   1 
ATOM   21357 O  O   . LEU C 1 927  ? 9.144    31.610  65.349  1.00 111.74 ? 927  LEU B O   1 
ATOM   21358 C  CB  . LEU C 1 927  ? 8.259    31.935  62.661  1.00 109.53 ? 927  LEU B CB  1 
ATOM   21359 C  CG  . LEU C 1 927  ? 7.030    31.072  62.332  1.00 107.05 ? 927  LEU B CG  1 
ATOM   21360 C  CD1 . LEU C 1 927  ? 7.423    29.855  61.496  1.00 104.95 ? 927  LEU B CD1 1 
ATOM   21361 C  CD2 . LEU C 1 927  ? 6.330    30.625  63.584  1.00 107.27 ? 927  LEU B CD2 1 
ATOM   21362 N  N   . ARG C 1 928  ? 7.437    32.919  65.982  1.00 109.39 ? 928  ARG B N   1 
ATOM   21363 C  CA  . ARG C 1 928  ? 7.373    32.365  67.342  1.00 109.38 ? 928  ARG B CA  1 
ATOM   21364 C  C   . ARG C 1 928  ? 6.925    30.897  67.313  1.00 108.45 ? 928  ARG B C   1 
ATOM   21365 O  O   . ARG C 1 928  ? 5.801    30.590  66.925  1.00 107.31 ? 928  ARG B O   1 
ATOM   21366 C  CB  . ARG C 1 928  ? 6.463    33.224  68.258  1.00 110.16 ? 928  ARG B CB  1 
ATOM   21367 C  CG  . ARG C 1 928  ? 7.183    34.371  68.985  1.00 115.18 ? 928  ARG B CG  1 
ATOM   21368 C  CD  . ARG C 1 928  ? 6.324    35.635  69.157  1.00 122.41 ? 928  ARG B CD  1 
ATOM   21369 N  NE  . ARG C 1 928  ? 5.767    36.110  67.876  1.00 130.08 ? 928  ARG B NE  1 
ATOM   21370 C  CZ  . ARG C 1 928  ? 6.017    37.289  67.279  1.00 133.84 ? 928  ARG B CZ  1 
ATOM   21371 N  NH1 . ARG C 1 928  ? 6.833    38.199  67.845  1.00 136.62 ? 928  ARG B NH1 1 
ATOM   21372 N  NH2 . ARG C 1 928  ? 5.425    37.562  66.103  1.00 130.80 ? 928  ARG B NH2 1 
ATOM   21373 N  N   . VAL C 1 929  ? 7.823    29.994  67.695  1.00 109.35 ? 929  VAL B N   1 
ATOM   21374 C  CA  . VAL C 1 929  ? 7.490    28.578  67.830  1.00 109.81 ? 929  VAL B CA  1 
ATOM   21375 C  C   . VAL C 1 929  ? 7.515    28.169  69.302  1.00 108.92 ? 929  VAL B C   1 
ATOM   21376 O  O   . VAL C 1 929  ? 8.340    28.663  70.060  1.00 109.64 ? 929  VAL B O   1 
ATOM   21377 C  CB  . VAL C 1 929  ? 8.456    27.706  67.005  1.00 112.12 ? 929  VAL B CB  1 
ATOM   21378 C  CG1 . VAL C 1 929  ? 8.137    26.232  67.170  1.00 112.01 ? 929  VAL B CG1 1 
ATOM   21379 C  CG2 . VAL C 1 929  ? 8.394    28.114  65.545  1.00 111.72 ? 929  VAL B CG2 1 
ATOM   21380 N  N   . VAL C 1 930  ? 6.628    27.256  69.692  1.00 109.37 ? 930  VAL B N   1 
ATOM   21381 C  CA  . VAL C 1 930  ? 6.337    26.979  71.103  1.00 114.08 ? 930  VAL B CA  1 
ATOM   21382 C  C   . VAL C 1 930  ? 6.272    25.484  71.376  1.00 117.10 ? 930  VAL B C   1 
ATOM   21383 O  O   . VAL C 1 930  ? 6.422    24.687  70.466  1.00 121.14 ? 930  VAL B O   1 
ATOM   21384 C  CB  . VAL C 1 930  ? 4.952    27.529  71.459  1.00 113.72 ? 930  VAL B CB  1 
ATOM   21385 C  CG1 . VAL C 1 930  ? 4.640    27.320  72.937  1.00 116.01 ? 930  VAL B CG1 1 
ATOM   21386 C  CG2 . VAL C 1 930  ? 4.841    29.002  71.072  1.00 114.50 ? 930  VAL B CG2 1 
ATOM   21387 N  N   . PRO C 1 931  ? 6.095    25.089  72.635  1.00 118.66 ? 931  PRO B N   1 
ATOM   21388 C  CA  . PRO C 1 931  ? 5.727    23.706  72.972  1.00 119.21 ? 931  PRO B CA  1 
ATOM   21389 C  C   . PRO C 1 931  ? 4.275    23.523  73.465  1.00 117.43 ? 931  PRO B C   1 
ATOM   21390 O  O   . PRO C 1 931  ? 3.413    24.137  72.879  1.00 119.16 ? 931  PRO B O   1 
ATOM   21391 C  CB  . PRO C 1 931  ? 6.737    23.347  74.043  1.00 119.00 ? 931  PRO B CB  1 
ATOM   21392 C  CG  . PRO C 1 931  ? 7.760    24.505  74.032  1.00 116.74 ? 931  PRO B CG  1 
ATOM   21393 C  CD  . PRO C 1 931  ? 6.968    25.675  73.653  1.00 115.44 ? 931  PRO B CD  1 
ATOM   21394 N  N   . GLU C 1 932  ? 4.007    22.729  74.507  1.00 115.71 ? 932  GLU B N   1 
ATOM   21395 C  CA  . GLU C 1 932  ? 2.625    22.299  74.813  1.00 116.88 ? 932  GLU B CA  1 
ATOM   21396 C  C   . GLU C 1 932  ? 2.206    22.082  76.307  1.00 112.39 ? 932  GLU B C   1 
ATOM   21397 O  O   . GLU C 1 932  ? 2.465    21.001  76.842  1.00 108.77 ? 932  GLU B O   1 
ATOM   21398 C  CB  . GLU C 1 932  ? 2.372    20.988  74.062  1.00 119.77 ? 932  GLU B CB  1 
ATOM   21399 C  CG  . GLU C 1 932  ? 2.960    20.921  72.663  1.00 122.28 ? 932  GLU B CG  1 
ATOM   21400 C  CD  . GLU C 1 932  ? 4.436    20.589  72.645  1.00 122.61 ? 932  GLU B CD  1 
ATOM   21401 O  OE1 . GLU C 1 932  ? 5.160    21.080  73.525  1.00 120.70 ? 932  GLU B OE1 1 
ATOM   21402 O  OE2 . GLU C 1 932  ? 4.876    19.834  71.748  1.00 124.97 ? 932  GLU B OE2 1 
ATOM   21403 N  N   . GLY C 1 933  ? 1.525    23.068  76.934  1.00 115.16 ? 933  GLY B N   1 
ATOM   21404 C  CA  . GLY C 1 933  ? 1.095    23.042  78.350  1.00 115.83 ? 933  GLY B CA  1 
ATOM   21405 C  C   . GLY C 1 933  ? 2.070    23.572  79.408  1.00 113.84 ? 933  GLY B C   1 
ATOM   21406 O  O   . GLY C 1 933  ? 2.919    22.833  79.899  1.00 111.53 ? 933  GLY B O   1 
ATOM   21407 N  N   . VAL C 1 934  ? 1.956    24.844  79.783  1.00 117.13 ? 934  VAL B N   1 
ATOM   21408 C  CA  . VAL C 1 934  ? 3.107    25.556  80.420  1.00 121.69 ? 934  VAL B CA  1 
ATOM   21409 C  C   . VAL C 1 934  ? 3.072    25.977  81.888  1.00 120.35 ? 934  VAL B C   1 
ATOM   21410 O  O   . VAL C 1 934  ? 2.525    27.023  82.257  1.00 118.24 ? 934  VAL B O   1 
ATOM   21411 C  CB  . VAL C 1 934  ? 3.493    26.859  79.693  1.00 128.95 ? 934  VAL B CB  1 
ATOM   21412 C  CG1 . VAL C 1 934  ? 4.536    27.676  80.527  1.00 98.99  ? 934  VAL B CG1 1 
ATOM   21413 C  CG2 . VAL C 1 934  ? 3.995    26.540  78.294  1.00 133.70 ? 934  VAL B CG2 1 
ATOM   21414 N  N   . LYS C 1 935  ? 3.759    25.200  82.703  1.00 120.80 ? 935  LYS B N   1 
ATOM   21415 C  CA  . LYS C 1 935  ? 3.833    25.450  84.116  1.00 121.87 ? 935  LYS B CA  1 
ATOM   21416 C  C   . LYS C 1 935  ? 5.203    26.101  84.422  1.00 122.92 ? 935  LYS B C   1 
ATOM   21417 O  O   . LYS C 1 935  ? 6.208    25.787  83.773  1.00 121.26 ? 935  LYS B O   1 
ATOM   21418 C  CB  . LYS C 1 935  ? 3.592    24.111  84.845  1.00 123.07 ? 935  LYS B CB  1 
ATOM   21419 C  CG  . LYS C 1 935  ? 2.098    23.727  85.050  1.00 99.51  ? 935  LYS B CG  1 
ATOM   21420 C  CD  . LYS C 1 935  ? 1.158    24.709  84.345  1.00 100.83 ? 935  LYS B CD  1 
ATOM   21421 C  CE  . LYS C 1 935  ? -0.069   25.092  85.182  1.00 105.80 ? 935  LYS B CE  1 
ATOM   21422 N  NZ  . LYS C 1 935  ? -1.246   24.217  84.948  1.00 109.19 ? 935  LYS B NZ  1 
ATOM   21423 N  N   . ARG C 1 936  ? 5.244    27.040  85.369  1.00 124.46 ? 936  ARG B N   1 
ATOM   21424 C  CA  . ARG C 1 936  ? 6.532    27.547  85.829  1.00 124.79 ? 936  ARG B CA  1 
ATOM   21425 C  C   . ARG C 1 936  ? 6.585    27.503  87.346  1.00 127.38 ? 936  ARG B C   1 
ATOM   21426 O  O   . ARG C 1 936  ? 5.695    28.026  88.012  1.00 130.39 ? 936  ARG B O   1 
ATOM   21427 C  CB  . ARG C 1 936  ? 6.830    28.936  85.280  1.00 124.07 ? 936  ARG B CB  1 
ATOM   21428 C  CG  . ARG C 1 936  ? 6.200    30.083  86.018  1.00 125.25 ? 936  ARG B CG  1 
ATOM   21429 C  CD  . ARG C 1 936  ? 5.882    31.208  85.037  1.00 130.20 ? 936  ARG B CD  1 
ATOM   21430 N  NE  . ARG C 1 936  ? 6.431    32.495  85.457  1.00 133.77 ? 936  ARG B NE  1 
ATOM   21431 C  CZ  . ARG C 1 936  ? 6.462    33.588  84.694  1.00 136.84 ? 936  ARG B CZ  1 
ATOM   21432 N  NH1 . ARG C 1 936  ? 5.956    33.559  83.464  1.00 137.50 ? 936  ARG B NH1 1 
ATOM   21433 N  NH2 . ARG C 1 936  ? 6.997    34.713  85.170  1.00 137.44 ? 936  ARG B NH2 1 
ATOM   21434 N  N   . GLU C 1 937  ? 7.616    26.821  87.860  1.00 125.89 ? 937  GLU B N   1 
ATOM   21435 C  CA  . GLU C 1 937  ? 7.837    26.582  89.288  1.00 130.93 ? 937  GLU B CA  1 
ATOM   21436 C  C   . GLU C 1 937  ? 9.068    27.339  89.790  1.00 135.81 ? 937  GLU B C   1 
ATOM   21437 O  O   . GLU C 1 937  ? 10.203   27.041  89.421  1.00 132.58 ? 937  GLU B O   1 
ATOM   21438 C  CB  . GLU C 1 937  ? 7.936    25.071  89.580  1.00 136.80 ? 937  GLU B CB  1 
ATOM   21439 C  CG  . GLU C 1 937  ? 8.813    24.235  88.603  1.00 198.24 ? 937  GLU B CG  1 
ATOM   21440 C  CD  . GLU C 1 937  ? 8.471    22.713  88.573  1.00 210.10 ? 937  GLU B CD  1 
ATOM   21441 O  OE1 . GLU C 1 937  ? 7.487    22.328  87.884  1.00 211.01 ? 937  GLU B OE1 1 
ATOM   21442 O  OE2 . GLU C 1 937  ? 9.206    21.904  89.207  1.00 209.62 ? 937  GLU B OE2 1 
ATOM   21443 N  N   . SER C 1 938  ? 8.818    28.310  90.656  1.00 148.35 ? 938  SER B N   1 
ATOM   21444 C  CA  . SER C 1 938  ? 9.775    29.347  90.991  1.00 147.28 ? 938  SER B CA  1 
ATOM   21445 C  C   . SER C 1 938  ? 10.262   29.259  92.419  1.00 164.92 ? 938  SER B C   1 
ATOM   21446 O  O   . SER C 1 938  ? 11.234   29.909  92.796  1.00 167.49 ? 938  SER B O   1 
ATOM   21447 C  CB  . SER C 1 938  ? 9.027    30.638  90.911  1.00 132.13 ? 938  SER B CB  1 
ATOM   21448 O  OG  . SER C 1 938  ? 7.958    30.520  91.808  1.00 114.86 ? 938  SER B OG  1 
ATOM   21449 N  N   . TYR C 1 939  ? 9.554    28.473  93.218  1.00 169.91 ? 939  TYR B N   1 
ATOM   21450 C  CA  . TYR C 1 939  ? 9.697    28.486  94.677  1.00 176.79 ? 939  TYR B CA  1 
ATOM   21451 C  C   . TYR C 1 939  ? 11.141   28.586  95.209  1.00 170.89 ? 939  TYR B C   1 
ATOM   21452 O  O   . TYR C 1 939  ? 11.365   28.803  96.415  1.00 170.32 ? 939  TYR B O   1 
ATOM   21453 C  CB  . TYR C 1 939  ? 8.903    27.326  95.339  1.00 225.82 ? 939  TYR B CB  1 
ATOM   21454 C  CG  . TYR C 1 939  ? 9.403    25.907  95.108  1.00 235.01 ? 939  TYR B CG  1 
ATOM   21455 C  CD1 . TYR C 1 939  ? 10.535   25.430  95.767  1.00 237.92 ? 939  TYR B CD1 1 
ATOM   21456 C  CD2 . TYR C 1 939  ? 8.709    25.030  94.281  1.00 239.71 ? 939  TYR B CD2 1 
ATOM   21457 C  CE1 . TYR C 1 939  ? 10.983   24.134  95.579  1.00 240.24 ? 939  TYR B CE1 1 
ATOM   21458 C  CE2 . TYR C 1 939  ? 9.148    23.731  94.085  1.00 242.17 ? 939  TYR B CE2 1 
ATOM   21459 C  CZ  . TYR C 1 939  ? 10.286   23.289  94.738  1.00 242.05 ? 939  TYR B CZ  1 
ATOM   21460 O  OH  . TYR C 1 939  ? 10.735   21.998  94.558  1.00 243.10 ? 939  TYR B OH  1 
ATOM   21461 N  N   . SER C 1 940  ? 12.111   28.442  94.311  1.00 163.45 ? 940  SER B N   1 
ATOM   21462 C  CA  . SER C 1 940  ? 13.502   28.574  94.684  1.00 155.39 ? 940  SER B CA  1 
ATOM   21463 C  C   . SER C 1 940  ? 13.847   30.046  94.834  1.00 144.82 ? 940  SER B C   1 
ATOM   21464 O  O   . SER C 1 940  ? 13.346   30.904  94.097  1.00 144.31 ? 940  SER B O   1 
ATOM   21465 C  CB  . SER C 1 940  ? 14.383   27.948  93.623  1.00 157.51 ? 940  SER B CB  1 
ATOM   21466 O  OG  . SER C 1 940  ? 14.139   28.601  92.400  1.00 157.49 ? 940  SER B OG  1 
ATOM   21467 N  N   . GLY C 1 941  ? 14.713   30.312  95.804  1.00 134.03 ? 941  GLY B N   1 
ATOM   21468 C  CA  . GLY C 1 941  ? 15.173   31.645  96.133  1.00 124.64 ? 941  GLY B CA  1 
ATOM   21469 C  C   . GLY C 1 941  ? 16.009   31.532  97.392  1.00 118.64 ? 941  GLY B C   1 
ATOM   21470 O  O   . GLY C 1 941  ? 16.053   30.449  97.996  1.00 117.84 ? 941  GLY B O   1 
ATOM   21471 N  N   . VAL C 1 942  ? 16.690   32.622  97.769  1.00 112.84 ? 942  VAL B N   1 
ATOM   21472 C  CA  . VAL C 1 942  ? 17.413   32.719  99.050  1.00 105.04 ? 942  VAL B CA  1 
ATOM   21473 C  C   . VAL C 1 942  ? 17.372   34.127  99.541  1.00 99.97  ? 942  VAL B C   1 
ATOM   21474 O  O   . VAL C 1 942  ? 17.161   35.046  98.753  1.00 101.70 ? 942  VAL B O   1 
ATOM   21475 C  CB  . VAL C 1 942  ? 18.902   32.498  98.915  1.00 102.96 ? 942  VAL B CB  1 
ATOM   21476 C  CG1 . VAL C 1 942  ? 19.470   32.107  100.251 1.00 103.05 ? 942  VAL B CG1 1 
ATOM   21477 C  CG2 . VAL C 1 942  ? 19.182   31.453  97.923  1.00 103.75 ? 942  VAL B CG2 1 
ATOM   21478 N  N   . THR C 1 943  ? 17.593   34.329  100.832 1.00 92.89  ? 943  THR B N   1 
ATOM   21479 C  CA  . THR C 1 943  ? 18.048   35.656  101.207 1.00 88.99  ? 943  THR B CA  1 
ATOM   21480 C  C   . THR C 1 943  ? 19.525   35.653  101.568 1.00 87.32  ? 943  THR B C   1 
ATOM   21481 O  O   . THR C 1 943  ? 19.928   35.060  102.566 1.00 88.52  ? 943  THR B O   1 
ATOM   21482 C  CB  . THR C 1 943  ? 17.191   36.372  102.262 1.00 84.36  ? 943  THR B CB  1 
ATOM   21483 O  OG1 . THR C 1 943  ? 15.914   36.708  101.701 1.00 84.45  ? 943  THR B OG1 1 
ATOM   21484 C  CG2 . THR C 1 943  ? 17.861   37.662  102.593 1.00 81.98  ? 943  THR B CG2 1 
ATOM   21485 N  N   . LEU C 1 944  ? 20.329   36.278  100.714 1.00 84.84  ? 944  LEU B N   1 
ATOM   21486 C  CA  . LEU C 1 944  ? 21.744   36.355  100.956 1.00 83.14  ? 944  LEU B CA  1 
ATOM   21487 C  C   . LEU C 1 944  ? 21.922   37.276  102.147 1.00 86.33  ? 944  LEU B C   1 
ATOM   21488 O  O   . LEU C 1 944  ? 21.517   38.459  102.088 1.00 86.33  ? 944  LEU B O   1 
ATOM   21489 C  CB  . LEU C 1 944  ? 22.481   36.865  99.719  1.00 80.41  ? 944  LEU B CB  1 
ATOM   21490 C  CG  . LEU C 1 944  ? 22.690   35.722  98.725  1.00 79.56  ? 944  LEU B CG  1 
ATOM   21491 C  CD1 . LEU C 1 944  ? 23.765   35.983  97.679  1.00 79.02  ? 944  LEU B CD1 1 
ATOM   21492 C  CD2 . LEU C 1 944  ? 23.068   34.528  99.523  1.00 78.13  ? 944  LEU B CD2 1 
ATOM   21493 N  N   . ASP C 1 945  ? 22.480   36.705  103.230 1.00 87.60  ? 945  ASP B N   1 
ATOM   21494 C  CA  . ASP C 1 945  ? 22.710   37.406  104.497 1.00 86.09  ? 945  ASP B CA  1 
ATOM   21495 C  C   . ASP C 1 945  ? 24.060   37.038  105.007 1.00 83.70  ? 945  ASP B C   1 
ATOM   21496 O  O   . ASP C 1 945  ? 24.201   36.037  105.690 1.00 83.55  ? 945  ASP B O   1 
ATOM   21497 C  CB  . ASP C 1 945  ? 21.719   36.970  105.578 1.00 86.74  ? 945  ASP B CB  1 
ATOM   21498 C  CG  . ASP C 1 945  ? 21.526   38.043  106.645 1.00 87.49  ? 945  ASP B CG  1 
ATOM   21499 O  OD1 . ASP C 1 945  ? 22.455   38.897  106.815 1.00 86.82  ? 945  ASP B OD1 1 
ATOM   21500 O  OD2 . ASP C 1 945  ? 20.437   38.023  107.281 1.00 86.70  ? 945  ASP B OD2 1 
ATOM   21501 N  N   . PRO C 1 946  ? 25.055   37.866  104.733 1.00 82.32  ? 946  PRO B N   1 
ATOM   21502 C  CA  . PRO C 1 946  ? 26.404   37.346  104.982 1.00 82.30  ? 946  PRO B CA  1 
ATOM   21503 C  C   . PRO C 1 946  ? 26.740   37.532  106.462 1.00 83.53  ? 946  PRO B C   1 
ATOM   21504 O  O   . PRO C 1 946  ? 27.632   36.900  107.043 1.00 82.93  ? 946  PRO B O   1 
ATOM   21505 C  CB  . PRO C 1 946  ? 27.268   38.262  104.128 1.00 81.24  ? 946  PRO B CB  1 
ATOM   21506 C  CG  . PRO C 1 946  ? 26.346   39.506  103.793 1.00 79.94  ? 946  PRO B CG  1 
ATOM   21507 C  CD  . PRO C 1 946  ? 25.036   39.314  104.475 1.00 79.05  ? 946  PRO B CD  1 
ATOM   21508 N  N   . ARG C 1 947  ? 25.964   38.434  107.050 1.00 82.85  ? 947  ARG B N   1 
ATOM   21509 C  CA  . ARG C 1 947  ? 26.244   39.024  108.325 1.00 82.85  ? 947  ARG B CA  1 
ATOM   21510 C  C   . ARG C 1 947  ? 25.215   38.480  109.273 1.00 82.92  ? 947  ARG B C   1 
ATOM   21511 O  O   . ARG C 1 947  ? 24.947   39.091  110.291 1.00 85.31  ? 947  ARG B O   1 
ATOM   21512 C  CB  . ARG C 1 947  ? 26.075   40.548  108.222 1.00 84.70  ? 947  ARG B CB  1 
ATOM   21513 C  CG  . ARG C 1 947  ? 27.206   41.309  107.530 1.00 85.63  ? 947  ARG B CG  1 
ATOM   21514 C  CD  . ARG C 1 947  ? 28.350   41.692  108.496 1.00 86.04  ? 947  ARG B CD  1 
ATOM   21515 N  NE  . ARG C 1 947  ? 28.414   43.132  108.762 1.00 86.92  ? 947  ARG B NE  1 
ATOM   21516 C  CZ  . ARG C 1 947  ? 29.398   43.934  108.334 1.00 90.21  ? 947  ARG B CZ  1 
ATOM   21517 N  NH1 . ARG C 1 947  ? 30.417   43.449  107.618 1.00 90.69  ? 947  ARG B NH1 1 
ATOM   21518 N  NH2 . ARG C 1 947  ? 29.377   45.236  108.622 1.00 91.80  ? 947  ARG B NH2 1 
ATOM   21519 N  N   . GLY C 1 948  ? 24.595   37.361  108.922 1.00 80.41  ? 948  GLY B N   1 
ATOM   21520 C  CA  . GLY C 1 948  ? 23.618   36.725  109.801 1.00 79.40  ? 948  GLY B CA  1 
ATOM   21521 C  C   . GLY C 1 948  ? 22.479   37.562  110.419 1.00 78.43  ? 948  GLY B C   1 
ATOM   21522 O  O   . GLY C 1 948  ? 21.661   37.026  111.180 1.00 75.17  ? 948  GLY B O   1 
ATOM   21523 N  N   . ILE C 1 949  ? 22.419   38.859  110.104 1.00 76.29  ? 949  ILE B N   1 
ATOM   21524 C  CA  . ILE C 1 949  ? 21.355   39.754  110.571 1.00 75.14  ? 949  ILE B CA  1 
ATOM   21525 C  C   . ILE C 1 949  ? 20.022   39.098  110.868 1.00 78.29  ? 949  ILE B C   1 
ATOM   21526 O  O   . ILE C 1 949  ? 19.332   39.475  111.812 1.00 74.29  ? 949  ILE B O   1 
ATOM   21527 C  CB  . ILE C 1 949  ? 21.037   40.749  109.490 1.00 76.25  ? 949  ILE B CB  1 
ATOM   21528 C  CG1 . ILE C 1 949  ? 22.321   41.354  108.983 1.00 83.07  ? 949  ILE B CG1 1 
ATOM   21529 C  CG2 . ILE C 1 949  ? 20.088   41.813  110.004 1.00 74.97  ? 949  ILE B CG2 1 
ATOM   21530 C  CD1 . ILE C 1 949  ? 22.849   42.430  109.897 1.00 83.69  ? 949  ILE B CD1 1 
ATOM   21531 N  N   . TYR C 1 950  ? 19.653   38.139  110.019 1.00 80.93  ? 950  TYR B N   1 
ATOM   21532 C  CA  . TYR C 1 950  ? 18.273   37.664  109.923 1.00 82.12  ? 950  TYR B CA  1 
ATOM   21533 C  C   . TYR C 1 950  ? 18.008   36.363  110.637 1.00 83.65  ? 950  TYR B C   1 
ATOM   21534 O  O   . TYR C 1 950  ? 16.877   35.872  110.646 1.00 86.00  ? 950  TYR B O   1 
ATOM   21535 C  CB  . TYR C 1 950  ? 17.716   37.744  108.471 1.00 74.96  ? 950  TYR B CB  1 
ATOM   21536 C  CG  . TYR C 1 950  ? 17.198   39.150  108.279 1.00 75.74  ? 950  TYR B CG  1 
ATOM   21537 C  CD1 . TYR C 1 950  ? 15.852   39.475  108.510 1.00 74.17  ? 950  TYR B CD1 1 
ATOM   21538 C  CD2 . TYR C 1 950  ? 18.088   40.184  108.010 1.00 75.40  ? 950  TYR B CD2 1 
ATOM   21539 C  CE1 . TYR C 1 950  ? 15.401   40.782  108.416 1.00 74.29  ? 950  TYR B CE1 1 
ATOM   21540 C  CE2 . TYR C 1 950  ? 17.658   41.492  107.918 1.00 76.90  ? 950  TYR B CE2 1 
ATOM   21541 C  CZ  . TYR C 1 950  ? 16.317   41.798  108.114 1.00 78.09  ? 950  TYR B CZ  1 
ATOM   21542 O  OH  . TYR C 1 950  ? 15.956   43.136  107.997 1.00 77.00  ? 950  TYR B OH  1 
ATOM   21543 N  N   . GLY C 1 951  ? 19.046   35.833  111.272 1.00 84.34  ? 951  GLY B N   1 
ATOM   21544 C  CA  . GLY C 1 951  ? 18.880   34.697  112.160 1.00 87.12  ? 951  GLY B CA  1 
ATOM   21545 C  C   . GLY C 1 951  ? 19.882   33.598  111.896 1.00 89.58  ? 951  GLY B C   1 
ATOM   21546 O  O   . GLY C 1 951  ? 20.023   32.661  112.685 1.00 89.91  ? 951  GLY B O   1 
ATOM   21547 N  N   . THR C 1 952  ? 20.562   33.710  110.759 1.00 90.47  ? 952  THR B N   1 
ATOM   21548 C  CA  . THR C 1 952  ? 21.683   32.841  110.440 1.00 88.14  ? 952  THR B CA  1 
ATOM   21549 C  C   . THR C 1 952  ? 22.431   33.353  109.233 1.00 85.15  ? 952  THR B C   1 
ATOM   21550 O  O   . THR C 1 952  ? 22.014   34.311  108.580 1.00 84.60  ? 952  THR B O   1 
ATOM   21551 C  CB  . THR C 1 952  ? 21.217   31.457  110.107 1.00 87.36  ? 952  THR B CB  1 
ATOM   21552 O  OG1 . THR C 1 952  ? 22.197   30.830  109.266 1.00 88.67  ? 952  THR B OG1 1 
ATOM   21553 C  CG2 . THR C 1 952  ? 19.919   31.550  109.366 1.00 84.97  ? 952  THR B CG2 1 
ATOM   21554 N  N   . ILE C 1 953  ? 23.524   32.682  108.920 1.00 84.74  ? 953  ILE B N   1 
ATOM   21555 C  CA  . ILE C 1 953  ? 24.374   33.163  107.873 1.00 88.41  ? 953  ILE B CA  1 
ATOM   21556 C  C   . ILE C 1 953  ? 24.110   32.457  106.520 1.00 96.14  ? 953  ILE B C   1 
ATOM   21557 O  O   . ILE C 1 953  ? 24.279   31.238  106.378 1.00 99.55  ? 953  ILE B O   1 
ATOM   21558 C  CB  . ILE C 1 953  ? 25.844   33.187  108.389 1.00 91.75  ? 953  ILE B CB  1 
ATOM   21559 C  CG1 . ILE C 1 953  ? 26.770   32.161  107.729 1.00 90.66  ? 953  ILE B CG1 1 
ATOM   21560 C  CG2 . ILE C 1 953  ? 25.850   32.991  109.891 1.00 94.38  ? 953  ILE B CG2 1 
ATOM   21561 C  CD1 . ILE C 1 953  ? 28.251   32.489  107.997 1.00 89.63  ? 953  ILE B CD1 1 
ATOM   21562 N  N   . SER C 1 954  ? 23.621   33.248  105.558 1.00 93.44  ? 954  SER B N   1 
ATOM   21563 C  CA  . SER C 1 954  ? 23.283   32.774  104.216 1.00 88.28  ? 954  SER B CA  1 
ATOM   21564 C  C   . SER C 1 954  ? 24.411   33.172  103.301 1.00 87.46  ? 954  SER B C   1 
ATOM   21565 O  O   . SER C 1 954  ? 24.461   34.315  102.872 1.00 88.05  ? 954  SER B O   1 
ATOM   21566 C  CB  . SER C 1 954  ? 21.995   33.450  103.717 1.00 83.79  ? 954  SER B CB  1 
ATOM   21567 O  OG  . SER C 1 954  ? 21.067   32.497  103.222 1.00 81.25  ? 954  SER B OG  1 
ATOM   21568 N  N   . ARG C 1 955  ? 25.333   32.265  103.012 1.00 85.11  ? 955  ARG B N   1 
ATOM   21569 C  CA  . ARG C 1 955  ? 26.307   32.576  101.977 1.00 86.44  ? 955  ARG B CA  1 
ATOM   21570 C  C   . ARG C 1 955  ? 26.312   31.521  100.903 1.00 88.14  ? 955  ARG B C   1 
ATOM   21571 O  O   . ARG C 1 955  ? 27.290   31.375  100.160 1.00 91.26  ? 955  ARG B O   1 
ATOM   21572 C  CB  . ARG C 1 955  ? 27.699   32.718  102.537 1.00 85.06  ? 955  ARG B CB  1 
ATOM   21573 C  CG  . ARG C 1 955  ? 27.863   33.890  103.452 1.00 85.32  ? 955  ARG B CG  1 
ATOM   21574 C  CD  . ARG C 1 955  ? 28.997   33.541  104.362 1.00 84.98  ? 955  ARG B CD  1 
ATOM   21575 N  NE  . ARG C 1 955  ? 29.373   34.530  105.349 1.00 81.70  ? 955  ARG B NE  1 
ATOM   21576 C  CZ  . ARG C 1 955  ? 30.272   34.238  106.260 1.00 81.80  ? 955  ARG B CZ  1 
ATOM   21577 N  NH1 . ARG C 1 955  ? 30.793   33.028  106.248 1.00 82.46  ? 955  ARG B NH1 1 
ATOM   21578 N  NH2 . ARG C 1 955  ? 30.646   35.121  107.156 1.00 84.62  ? 955  ARG B NH2 1 
ATOM   21579 N  N   . ARG C 1 956  ? 25.220   30.777  100.828 1.00 86.41  ? 956  ARG B N   1 
ATOM   21580 C  CA  . ARG C 1 956  ? 25.063   29.789  99.791  1.00 86.39  ? 956  ARG B CA  1 
ATOM   21581 C  C   . ARG C 1 956  ? 23.669   29.276  99.791  1.00 92.15  ? 956  ARG B C   1 
ATOM   21582 O  O   . ARG C 1 956  ? 23.046   29.132  100.840 1.00 91.65  ? 956  ARG B O   1 
ATOM   21583 C  CB  . ARG C 1 956  ? 26.028   28.621  99.940  1.00 84.60  ? 956  ARG B CB  1 
ATOM   21584 C  CG  . ARG C 1 956  ? 27.123   28.709  98.925  1.00 85.93  ? 956  ARG B CG  1 
ATOM   21585 C  CD  . ARG C 1 956  ? 28.185   27.666  99.092  1.00 89.29  ? 956  ARG B CD  1 
ATOM   21586 N  NE  . ARG C 1 956  ? 27.719   26.346  98.690  1.00 92.27  ? 956  ARG B NE  1 
ATOM   21587 C  CZ  . ARG C 1 956  ? 28.495   25.435  98.104  1.00 95.05  ? 956  ARG B CZ  1 
ATOM   21588 N  NH1 . ARG C 1 956  ? 29.774   25.734  97.826  1.00 96.24  ? 956  ARG B NH1 1 
ATOM   21589 N  NH2 . ARG C 1 956  ? 27.989   24.236  97.785  1.00 95.26  ? 956  ARG B NH2 1 
ATOM   21590 N  N   . LYS C 1 957  ? 23.177   29.064  98.572  1.00 99.29  ? 957  LYS B N   1 
ATOM   21591 C  CA  . LYS C 1 957  ? 22.033   28.211  98.280  1.00 100.55 ? 957  LYS B CA  1 
ATOM   21592 C  C   . LYS C 1 957  ? 22.370   27.556  96.985  1.00 98.80  ? 957  LYS B C   1 
ATOM   21593 O  O   . LYS C 1 957  ? 22.913   28.203  96.099  1.00 95.03  ? 957  LYS B O   1 
ATOM   21594 C  CB  . LYS C 1 957  ? 20.726   28.981  98.108  1.00 103.34 ? 957  LYS B CB  1 
ATOM   21595 C  CG  . LYS C 1 957  ? 19.552   28.060  97.762  1.00 108.02 ? 957  LYS B CG  1 
ATOM   21596 C  CD  . LYS C 1 957  ? 18.392   28.188  98.755  1.00 112.48 ? 957  LYS B CD  1 
ATOM   21597 C  CE  . LYS C 1 957  ? 17.627   26.860  98.918  1.00 116.83 ? 957  LYS B CE  1 
ATOM   21598 N  NZ  . LYS C 1 957  ? 16.916   26.406  97.673  1.00 119.64 ? 957  LYS B NZ  1 
ATOM   21599 N  N   . GLU C 1 958  ? 22.083   26.265  96.906  1.00 101.24 ? 958  GLU B N   1 
ATOM   21600 C  CA  . GLU C 1 958  ? 22.174   25.526  95.668  1.00 108.21 ? 958  GLU B CA  1 
ATOM   21601 C  C   . GLU C 1 958  ? 20.761   25.329  95.116  1.00 108.96 ? 958  GLU B C   1 
ATOM   21602 O  O   . GLU C 1 958  ? 19.893   24.817  95.819  1.00 109.98 ? 958  GLU B O   1 
ATOM   21603 C  CB  . GLU C 1 958  ? 22.814   24.175  95.939  1.00 113.88 ? 958  GLU B CB  1 
ATOM   21604 C  CG  . GLU C 1 958  ? 23.550   23.567  94.762  1.00 121.06 ? 958  GLU B CG  1 
ATOM   21605 C  CD  . GLU C 1 958  ? 24.169   22.214  95.107  1.00 127.97 ? 958  GLU B CD  1 
ATOM   21606 O  OE1 . GLU C 1 958  ? 25.246   22.197  95.756  1.00 130.04 ? 958  GLU B OE1 1 
ATOM   21607 O  OE2 . GLU C 1 958  ? 23.582   21.170  94.727  1.00 130.37 ? 958  GLU B OE2 1 
ATOM   21608 N  N   . PHE C 1 959  ? 20.514   25.777  93.884  1.00 109.30 ? 959  PHE B N   1 
ATOM   21609 C  CA  . PHE C 1 959  ? 19.323   25.372  93.138  1.00 109.12 ? 959  PHE B CA  1 
ATOM   21610 C  C   . PHE C 1 959  ? 19.800   24.359  92.107  1.00 116.17 ? 959  PHE B C   1 
ATOM   21611 O  O   . PHE C 1 959  ? 20.751   24.643  91.364  1.00 116.84 ? 959  PHE B O   1 
ATOM   21612 C  CB  . PHE C 1 959  ? 18.679   26.546  92.422  1.00 103.64 ? 959  PHE B CB  1 
ATOM   21613 C  CG  . PHE C 1 959  ? 18.833   27.824  93.137  1.00 98.72  ? 959  PHE B CG  1 
ATOM   21614 C  CD1 . PHE C 1 959  ? 17.735   28.527  93.561  1.00 98.75  ? 959  PHE B CD1 1 
ATOM   21615 C  CD2 . PHE C 1 959  ? 20.077   28.333  93.389  1.00 96.39  ? 959  PHE B CD2 1 
ATOM   21616 C  CE1 . PHE C 1 959  ? 17.882   29.725  94.221  1.00 96.81  ? 959  PHE B CE1 1 
ATOM   21617 C  CE2 . PHE C 1 959  ? 20.227   29.513  94.055  1.00 95.10  ? 959  PHE B CE2 1 
ATOM   21618 C  CZ  . PHE C 1 959  ? 19.127   30.211  94.463  1.00 95.40  ? 959  PHE B CZ  1 
ATOM   21619 N  N   . PRO C 1 960  ? 19.166   23.170  92.068  1.00 118.20 ? 960  PRO B N   1 
ATOM   21620 C  CA  . PRO C 1 960  ? 19.681   22.140  91.183  1.00 125.12 ? 960  PRO B CA  1 
ATOM   21621 C  C   . PRO C 1 960  ? 18.737   21.919  90.005  1.00 132.66 ? 960  PRO B C   1 
ATOM   21622 O  O   . PRO C 1 960  ? 17.791   22.677  89.794  1.00 133.49 ? 960  PRO B O   1 
ATOM   21623 C  CB  . PRO C 1 960  ? 19.680   20.913  92.095  1.00 124.04 ? 960  PRO B CB  1 
ATOM   21624 C  CG  . PRO C 1 960  ? 18.951   21.353  93.397  1.00 111.27 ? 960  PRO B CG  1 
ATOM   21625 C  CD  . PRO C 1 960  ? 18.224   22.583  93.030  1.00 114.20 ? 960  PRO B CD  1 
ATOM   21626 N  N   . TYR C 1 961  ? 19.018   20.883  89.233  1.00 140.12 ? 961  TYR B N   1 
ATOM   21627 C  CA  . TYR C 1 961  ? 18.071   20.346  88.288  1.00 146.85 ? 961  TYR B CA  1 
ATOM   21628 C  C   . TYR C 1 961  ? 17.013   19.512  88.977  1.00 151.32 ? 961  TYR B C   1 
ATOM   21629 O  O   . TYR C 1 961  ? 17.324   18.598  89.752  1.00 152.62 ? 961  TYR B O   1 
ATOM   21630 C  CB  . TYR C 1 961  ? 18.803   19.401  87.370  1.00 152.75 ? 961  TYR B CB  1 
ATOM   21631 C  CG  . TYR C 1 961  ? 19.003   19.924  85.998  1.00 156.45 ? 961  TYR B CG  1 
ATOM   21632 C  CD1 . TYR C 1 961  ? 18.468   19.255  84.898  1.00 159.12 ? 961  TYR B CD1 1 
ATOM   21633 C  CD2 . TYR C 1 961  ? 19.719   21.079  85.793  1.00 157.99 ? 961  TYR B CD2 1 
ATOM   21634 C  CE1 . TYR C 1 961  ? 18.648   19.718  83.633  1.00 160.40 ? 961  TYR B CE1 1 
ATOM   21635 C  CE2 . TYR C 1 961  ? 19.908   21.560  84.533  1.00 160.31 ? 961  TYR B CE2 1 
ATOM   21636 C  CZ  . TYR C 1 961  ? 19.369   20.874  83.453  1.00 162.04 ? 961  TYR B CZ  1 
ATOM   21637 O  OH  . TYR C 1 961  ? 19.536   21.364  82.186  1.00 164.38 ? 961  TYR B OH  1 
ATOM   21638 N  N   . ARG C 1 962  ? 15.758   19.795  88.665  1.00 153.80 ? 962  ARG B N   1 
ATOM   21639 C  CA  . ARG C 1 962  ? 14.705   18.828  88.928  1.00 159.28 ? 962  ARG B CA  1 
ATOM   21640 C  C   . ARG C 1 962  ? 13.804   18.778  87.698  1.00 156.56 ? 962  ARG B C   1 
ATOM   21641 O  O   . ARG C 1 962  ? 13.055   19.727  87.413  1.00 154.08 ? 962  ARG B O   1 
ATOM   21642 C  CB  . ARG C 1 962  ? 13.925   19.125  90.224  1.00 167.55 ? 962  ARG B CB  1 
ATOM   21643 C  CG  . ARG C 1 962  ? 12.656   18.275  90.396  1.00 178.48 ? 962  ARG B CG  1 
ATOM   21644 C  CD  . ARG C 1 962  ? 12.473   17.703  91.812  1.00 186.68 ? 962  ARG B CD  1 
ATOM   21645 N  NE  . ARG C 1 962  ? 11.764   18.599  92.725  1.00 192.18 ? 962  ARG B NE  1 
ATOM   21646 C  CZ  . ARG C 1 962  ? 10.997   18.185  93.733  1.00 196.23 ? 962  ARG B CZ  1 
ATOM   21647 N  NH1 . ARG C 1 962  ? 10.822   16.885  93.949  1.00 198.44 ? 962  ARG B NH1 1 
ATOM   21648 N  NH2 . ARG C 1 962  ? 10.394   19.071  94.519  1.00 196.46 ? 962  ARG B NH2 1 
ATOM   21649 N  N   . ILE C 1 963  ? 13.938   17.677  86.951  1.00 153.72 ? 963  ILE B N   1 
ATOM   21650 C  CA  . ILE C 1 963  ? 13.147   17.430  85.768  1.00 146.13 ? 963  ILE B CA  1 
ATOM   21651 C  C   . ILE C 1 963  ? 11.933   16.657  86.177  1.00 148.58 ? 963  ILE B C   1 
ATOM   21652 O  O   . ILE C 1 963  ? 12.036   15.569  86.712  1.00 148.27 ? 963  ILE B O   1 
ATOM   21653 C  CB  . ILE C 1 963  ? 13.894   16.613  84.781  1.00 138.52 ? 963  ILE B CB  1 
ATOM   21654 C  CG1 . ILE C 1 963  ? 15.346   17.035  84.761  1.00 131.88 ? 963  ILE B CG1 1 
ATOM   21655 C  CG2 . ILE C 1 963  ? 13.306   16.822  83.441  1.00 137.95 ? 963  ILE B CG2 1 
ATOM   21656 C  CD1 . ILE C 1 963  ? 16.146   16.243  83.831  1.00 131.35 ? 963  ILE B CD1 1 
ATOM   21657 N  N   . PRO C 1 964  ? 10.768   17.254  85.966  1.00 150.12 ? 964  PRO B N   1 
ATOM   21658 C  CA  . PRO C 1 964  ? 9.469    16.677  86.324  1.00 155.22 ? 964  PRO B CA  1 
ATOM   21659 C  C   . PRO C 1 964  ? 9.099    15.625  85.298  1.00 159.40 ? 964  PRO B C   1 
ATOM   21660 O  O   . PRO C 1 964  ? 9.194    15.897  84.105  1.00 161.18 ? 964  PRO B O   1 
ATOM   21661 C  CB  . PRO C 1 964  ? 8.515    17.882  86.234  1.00 154.97 ? 964  PRO B CB  1 
ATOM   21662 C  CG  . PRO C 1 964  ? 9.437    19.133  86.176  1.00 147.07 ? 964  PRO B CG  1 
ATOM   21663 C  CD  . PRO C 1 964  ? 10.660   18.641  85.483  1.00 148.03 ? 964  PRO B CD  1 
ATOM   21664 N  N   . LEU C 1 965  ? 8.700    14.436  85.723  1.00 164.87 ? 965  LEU B N   1 
ATOM   21665 C  CA  . LEU C 1 965  ? 8.549    13.360  84.745  1.00 172.59 ? 965  LEU B CA  1 
ATOM   21666 C  C   . LEU C 1 965  ? 7.394    13.604  83.749  1.00 176.17 ? 965  LEU B C   1 
ATOM   21667 O  O   . LEU C 1 965  ? 6.987    12.697  83.013  1.00 179.07 ? 965  LEU B O   1 
ATOM   21668 C  CB  . LEU C 1 965  ? 8.486    11.973  85.418  1.00 178.92 ? 965  LEU B CB  1 
ATOM   21669 C  CG  . LEU C 1 965  ? 9.763    11.485  86.139  1.00 186.92 ? 965  LEU B CG  1 
ATOM   21670 C  CD1 . LEU C 1 965  ? 9.556    10.133  86.828  1.00 190.78 ? 965  LEU B CD1 1 
ATOM   21671 C  CD2 . LEU C 1 965  ? 10.986   11.425  85.219  1.00 188.98 ? 965  LEU B CD2 1 
ATOM   21672 N  N   . ASP C 1 966  ? 6.889    14.837  83.720  1.00 174.42 ? 966  ASP B N   1 
ATOM   21673 C  CA  . ASP C 1 966  ? 5.862    15.231  82.761  1.00 172.85 ? 966  ASP B CA  1 
ATOM   21674 C  C   . ASP C 1 966  ? 6.416    16.156  81.693  1.00 164.54 ? 966  ASP B C   1 
ATOM   21675 O  O   . ASP C 1 966  ? 5.665    16.718  80.904  1.00 165.38 ? 966  ASP B O   1 
ATOM   21676 C  CB  . ASP C 1 966  ? 4.698    15.914  83.473  1.00 176.21 ? 966  ASP B CB  1 
ATOM   21677 C  CG  . ASP C 1 966  ? 3.806    14.930  84.199  1.00 179.27 ? 966  ASP B CG  1 
ATOM   21678 O  OD1 . ASP C 1 966  ? 3.487    13.868  83.618  1.00 181.13 ? 966  ASP B OD1 1 
ATOM   21679 O  OD2 . ASP C 1 966  ? 3.426    15.218  85.354  1.00 179.54 ? 966  ASP B OD2 1 
ATOM   21680 N  N   . LEU C 1 967  ? 7.731    16.316  81.672  1.00 156.28 ? 967  LEU B N   1 
ATOM   21681 C  CA  . LEU C 1 967  ? 8.354    17.262  80.757  1.00 149.70 ? 967  LEU B CA  1 
ATOM   21682 C  C   . LEU C 1 967  ? 8.140    16.872  79.301  1.00 147.25 ? 967  LEU B C   1 
ATOM   21683 O  O   . LEU C 1 967  ? 8.334    15.711  78.927  1.00 148.25 ? 967  LEU B O   1 
ATOM   21684 C  CB  . LEU C 1 967  ? 9.853    17.396  81.046  1.00 148.74 ? 967  LEU B CB  1 
ATOM   21685 C  CG  . LEU C 1 967  ? 10.635   18.320  80.103  1.00 149.98 ? 967  LEU B CG  1 
ATOM   21686 C  CD1 . LEU C 1 967  ? 9.961    19.687  79.966  1.00 150.27 ? 967  LEU B CD1 1 
ATOM   21687 C  CD2 . LEU C 1 967  ? 12.074   18.465  80.563  1.00 148.72 ? 967  LEU B CD2 1 
ATOM   21688 N  N   . VAL C 1 968  ? 7.747    17.850  78.487  1.00 141.48 ? 968  VAL B N   1 
ATOM   21689 C  CA  . VAL C 1 968  ? 7.614    17.652  77.047  1.00 138.07 ? 968  VAL B CA  1 
ATOM   21690 C  C   . VAL C 1 968  ? 8.971    17.371  76.378  1.00 136.54 ? 968  VAL B C   1 
ATOM   21691 O  O   . VAL C 1 968  ? 9.882    18.185  76.425  1.00 134.50 ? 968  VAL B O   1 
ATOM   21692 C  CB  . VAL C 1 968  ? 6.935    18.864  76.380  1.00 133.63 ? 968  VAL B CB  1 
ATOM   21693 C  CG1 . VAL C 1 968  ? 5.485    18.951  76.785  1.00 132.14 ? 968  VAL B CG1 1 
ATOM   21694 C  CG2 . VAL C 1 968  ? 7.636    20.128  76.778  1.00 132.38 ? 968  VAL B CG2 1 
ATOM   21695 N  N   . PRO C 1 969  ? 9.105    16.195  75.764  1.00 138.72 ? 969  PRO B N   1 
ATOM   21696 C  CA  . PRO C 1 969  ? 10.311   15.743  75.073  1.00 141.57 ? 969  PRO B CA  1 
ATOM   21697 C  C   . PRO C 1 969  ? 11.000   16.797  74.212  1.00 146.49 ? 969  PRO B C   1 
ATOM   21698 O  O   . PRO C 1 969  ? 10.349   17.657  73.632  1.00 147.28 ? 969  PRO B O   1 
ATOM   21699 C  CB  . PRO C 1 969  ? 9.774    14.635  74.181  1.00 142.61 ? 969  PRO B CB  1 
ATOM   21700 C  CG  . PRO C 1 969  ? 8.670    14.044  74.980  1.00 142.09 ? 969  PRO B CG  1 
ATOM   21701 C  CD  . PRO C 1 969  ? 8.075    15.145  75.797  1.00 140.07 ? 969  PRO B CD  1 
ATOM   21702 N  N   . LYS C 1 970  ? 12.322   16.689  74.125  1.00 153.03 ? 970  LYS B N   1 
ATOM   21703 C  CA  . LYS C 1 970  ? 13.170   17.605  73.360  1.00 160.53 ? 970  LYS B CA  1 
ATOM   21704 C  C   . LYS C 1 970  ? 12.832   19.058  73.585  1.00 162.77 ? 970  LYS B C   1 
ATOM   21705 O  O   . LYS C 1 970  ? 12.773   19.832  72.632  1.00 163.01 ? 970  LYS B O   1 
ATOM   21706 C  CB  . LYS C 1 970  ? 13.164   17.285  71.863  1.00 168.70 ? 970  LYS B CB  1 
ATOM   21707 C  CG  . LYS C 1 970  ? 14.180   16.219  71.457  1.00 177.20 ? 970  LYS B CG  1 
ATOM   21708 C  CD  . LYS C 1 970  ? 14.507   16.294  69.963  1.00 185.33 ? 970  LYS B CD  1 
ATOM   21709 C  CE  . LYS C 1 970  ? 15.333   15.095  69.477  1.00 189.90 ? 970  LYS B CE  1 
ATOM   21710 N  NZ  . LYS C 1 970  ? 15.515   15.115  67.991  1.00 192.62 ? 970  LYS B NZ  1 
ATOM   21711 N  N   . THR C 1 971  ? 12.608   19.412  74.850  1.00 165.59 ? 971  THR B N   1 
ATOM   21712 C  CA  . THR C 1 971  ? 12.431   20.805  75.257  1.00 167.50 ? 971  THR B CA  1 
ATOM   21713 C  C   . THR C 1 971  ? 13.243   21.058  76.501  1.00 165.71 ? 971  THR B C   1 
ATOM   21714 O  O   . THR C 1 971  ? 13.074   20.379  77.509  1.00 166.46 ? 971  THR B O   1 
ATOM   21715 C  CB  . THR C 1 971  ? 10.971   21.157  75.586  1.00 170.26 ? 971  THR B CB  1 
ATOM   21716 O  OG1 . THR C 1 971  ? 10.720   20.971  76.990  1.00 168.07 ? 971  THR B OG1 1 
ATOM   21717 C  CG2 . THR C 1 971  ? 10.023   20.318  74.739  1.00 174.42 ? 971  THR B CG2 1 
ATOM   21718 N  N   . GLU C 1 972  ? 14.127   22.043  76.410  1.00 162.18 ? 972  GLU B N   1 
ATOM   21719 C  CA  . GLU C 1 972  ? 15.062   22.376  77.477  1.00 158.71 ? 972  GLU B CA  1 
ATOM   21720 C  C   . GLU C 1 972  ? 14.346   23.058  78.630  1.00 147.65 ? 972  GLU B C   1 
ATOM   21721 O  O   . GLU C 1 972  ? 13.267   23.618  78.449  1.00 144.36 ? 972  GLU B O   1 
ATOM   21722 C  CB  . GLU C 1 972  ? 16.162   23.280  76.923  1.00 166.41 ? 972  GLU B CB  1 
ATOM   21723 C  CG  . GLU C 1 972  ? 15.680   24.107  75.730  1.00 175.85 ? 972  GLU B CG  1 
ATOM   21724 C  CD  . GLU C 1 972  ? 16.722   25.078  75.193  1.00 182.22 ? 972  GLU B CD  1 
ATOM   21725 O  OE1 . GLU C 1 972  ? 17.583   25.542  75.983  1.00 182.94 ? 972  GLU B OE1 1 
ATOM   21726 O  OE2 . GLU C 1 972  ? 16.660   25.383  73.974  1.00 185.77 ? 972  GLU B OE2 1 
ATOM   21727 N  N   . ILE C 1 973  ? 14.941   22.995  79.818  1.00 140.88 ? 973  ILE B N   1 
ATOM   21728 C  CA  . ILE C 1 973  ? 14.355   23.648  80.973  1.00 132.61 ? 973  ILE B CA  1 
ATOM   21729 C  C   . ILE C 1 973  ? 14.937   25.020  81.153  1.00 135.87 ? 973  ILE B C   1 
ATOM   21730 O  O   . ILE C 1 973  ? 16.128   25.170  81.458  1.00 138.03 ? 973  ILE B O   1 
ATOM   21731 C  CB  . ILE C 1 973  ? 14.620   22.921  82.246  1.00 120.54 ? 973  ILE B CB  1 
ATOM   21732 C  CG1 . ILE C 1 973  ? 14.160   21.487  82.127  1.00 118.26 ? 973  ILE B CG1 1 
ATOM   21733 C  CG2 . ILE C 1 973  ? 13.853   23.585  83.340  1.00 115.11 ? 973  ILE B CG2 1 
ATOM   21734 C  CD1 . ILE C 1 973  ? 14.640   20.633  83.248  1.00 117.39 ? 973  ILE B CD1 1 
ATOM   21735 N  N   . LYS C 1 974  ? 14.077   26.017  80.961  1.00 136.31 ? 974  LYS B N   1 
ATOM   21736 C  CA  . LYS C 1 974  ? 14.425   27.418  81.145  1.00 133.57 ? 974  LYS B CA  1 
ATOM   21737 C  C   . LYS C 1 974  ? 14.266   27.778  82.633  1.00 127.22 ? 974  LYS B C   1 
ATOM   21738 O  O   . LYS C 1 974  ? 13.377   27.262  83.311  1.00 126.40 ? 974  LYS B O   1 
ATOM   21739 C  CB  . LYS C 1 974  ? 13.543   28.299  80.229  1.00 138.85 ? 974  LYS B CB  1 
ATOM   21740 C  CG  . LYS C 1 974  ? 13.903   29.792  80.146  1.00 144.05 ? 974  LYS B CG  1 
ATOM   21741 C  CD  . LYS C 1 974  ? 12.978   30.521  79.155  1.00 151.95 ? 974  LYS B CD  1 
ATOM   21742 C  CE  . LYS C 1 974  ? 12.847   32.030  79.469  1.00 155.51 ? 974  LYS B CE  1 
ATOM   21743 N  NZ  . LYS C 1 974  ? 11.965   32.807  78.514  1.00 157.11 ? 974  LYS B NZ  1 
ATOM   21744 N  N   . ARG C 1 975  ? 15.157   28.628  83.140  1.00 121.85 ? 975  ARG B N   1 
ATOM   21745 C  CA  . ARG C 1 975  ? 15.012   29.207  84.471  1.00 114.61 ? 975  ARG B CA  1 
ATOM   21746 C  C   . ARG C 1 975  ? 15.895   30.426  84.626  1.00 109.77 ? 975  ARG B C   1 
ATOM   21747 O  O   . ARG C 1 975  ? 17.041   30.446  84.174  1.00 110.02 ? 975  ARG B O   1 
ATOM   21748 C  CB  . ARG C 1 975  ? 15.347   28.188  85.535  1.00 112.72 ? 975  ARG B CB  1 
ATOM   21749 C  CG  . ARG C 1 975  ? 16.689   27.602  85.352  1.00 111.03 ? 975  ARG B CG  1 
ATOM   21750 C  CD  . ARG C 1 975  ? 16.717   26.221  85.934  1.00 110.51 ? 975  ARG B CD  1 
ATOM   21751 N  NE  . ARG C 1 975  ? 18.055   25.680  85.790  1.00 109.87 ? 975  ARG B NE  1 
ATOM   21752 C  CZ  . ARG C 1 975  ? 18.831   25.330  86.802  1.00 108.09 ? 975  ARG B CZ  1 
ATOM   21753 N  NH1 . ARG C 1 975  ? 18.387   25.429  88.052  1.00 105.84 ? 975  ARG B NH1 1 
ATOM   21754 N  NH2 . ARG C 1 975  ? 20.044   24.860  86.550  1.00 108.90 ? 975  ARG B NH2 1 
ATOM   21755 N  N   . ILE C 1 976  ? 15.342   31.440  85.271  1.00 103.44 ? 976  ILE B N   1 
ATOM   21756 C  CA  . ILE C 1 976  ? 15.993   32.725  85.390  1.00 99.87  ? 976  ILE B CA  1 
ATOM   21757 C  C   . ILE C 1 976  ? 16.409   32.993  86.811  1.00 97.13  ? 976  ILE B C   1 
ATOM   21758 O  O   . ILE C 1 976  ? 15.706   32.605  87.740  1.00 99.50  ? 976  ILE B O   1 
ATOM   21759 C  CB  . ILE C 1 976  ? 15.017   33.775  85.056  1.00 99.40  ? 976  ILE B CB  1 
ATOM   21760 C  CG1 . ILE C 1 976  ? 14.161   33.243  83.923  1.00 104.77 ? 976  ILE B CG1 1 
ATOM   21761 C  CG2 . ILE C 1 976  ? 15.731   35.087  84.743  1.00 97.70  ? 976  ILE B CG2 1 
ATOM   21762 C  CD1 . ILE C 1 976  ? 12.695   33.552  84.084  1.00 107.84 ? 976  ILE B CD1 1 
ATOM   21763 N  N   . LEU C 1 977  ? 17.536   33.688  86.968  1.00 91.15  ? 977  LEU B N   1 
ATOM   21764 C  CA  . LEU C 1 977  ? 18.105   34.042  88.260  1.00 85.06  ? 977  LEU B CA  1 
ATOM   21765 C  C   . LEU C 1 977  ? 18.121   35.559  88.455  1.00 82.85  ? 977  LEU B C   1 
ATOM   21766 O  O   . LEU C 1 977  ? 18.733   36.260  87.662  1.00 83.39  ? 977  LEU B O   1 
ATOM   21767 C  CB  . LEU C 1 977  ? 19.528   33.543  88.274  1.00 83.03  ? 977  LEU B CB  1 
ATOM   21768 C  CG  . LEU C 1 977  ? 20.241   33.691  89.598  1.00 82.21  ? 977  LEU B CG  1 
ATOM   21769 C  CD1 . LEU C 1 977  ? 20.556   32.331  90.154  1.00 82.05  ? 977  LEU B CD1 1 
ATOM   21770 C  CD2 . LEU C 1 977  ? 21.515   34.415  89.316  1.00 85.78  ? 977  LEU B CD2 1 
ATOM   21771 N  N   . SER C 1 978  ? 17.480   36.070  89.505  1.00 83.45  ? 978  SER B N   1 
ATOM   21772 C  CA  . SER C 1 978  ? 17.403   37.526  89.701  1.00 87.57  ? 978  SER B CA  1 
ATOM   21773 C  C   . SER C 1 978  ? 17.940   38.017  91.057  1.00 96.41  ? 978  SER B C   1 
ATOM   21774 O  O   . SER C 1 978  ? 17.191   38.172  92.035  1.00 101.34 ? 978  SER B O   1 
ATOM   21775 C  CB  . SER C 1 978  ? 15.980   38.051  89.503  1.00 85.41  ? 978  SER B CB  1 
ATOM   21776 O  OG  . SER C 1 978  ? 15.950   39.452  89.752  1.00 82.51  ? 978  SER B OG  1 
ATOM   21777 N  N   . VAL C 1 979  ? 19.239   38.304  91.081  1.00 97.23  ? 979  VAL B N   1 
ATOM   21778 C  CA  . VAL C 1 979  ? 19.983   38.687  92.286  1.00 93.82  ? 979  VAL B CA  1 
ATOM   21779 C  C   . VAL C 1 979  ? 19.997   40.201  92.536  1.00 93.51  ? 979  VAL B C   1 
ATOM   21780 O  O   . VAL C 1 979  ? 20.512   40.944  91.711  1.00 95.36  ? 979  VAL B O   1 
ATOM   21781 C  CB  . VAL C 1 979  ? 21.442   38.276  92.078  1.00 91.31  ? 979  VAL B CB  1 
ATOM   21782 C  CG1 . VAL C 1 979  ? 22.225   38.384  93.345  1.00 88.29  ? 979  VAL B CG1 1 
ATOM   21783 C  CG2 . VAL C 1 979  ? 21.500   36.885  91.536  1.00 91.09  ? 979  VAL B CG2 1 
ATOM   21784 N  N   . LYS C 1 980  ? 19.466   40.681  93.657  1.00 92.23  ? 980  LYS B N   1 
ATOM   21785 C  CA  . LYS C 1 980  ? 19.575   42.127  93.933  1.00 92.98  ? 980  LYS B CA  1 
ATOM   21786 C  C   . LYS C 1 980  ? 19.729   42.556  95.389  1.00 92.96  ? 980  LYS B C   1 
ATOM   21787 O  O   . LYS C 1 980  ? 19.230   41.916  96.308  1.00 93.67  ? 980  LYS B O   1 
ATOM   21788 C  CB  . LYS C 1 980  ? 18.416   42.925  93.326  1.00 95.25  ? 980  LYS B CB  1 
ATOM   21789 C  CG  . LYS C 1 980  ? 17.199   42.113  92.960  1.00 96.88  ? 980  LYS B CG  1 
ATOM   21790 C  CD  . LYS C 1 980  ? 17.217   41.758  91.487  1.00 95.60  ? 980  LYS B CD  1 
ATOM   21791 C  CE  . LYS C 1 980  ? 17.146   42.989  90.626  1.00 93.91  ? 980  LYS B CE  1 
ATOM   21792 N  NZ  . LYS C 1 980  ? 17.343   42.518  89.253  1.00 94.24  ? 980  LYS B NZ  1 
ATOM   21793 N  N   . GLY C 1 981  ? 20.414   43.673  95.587  1.00 91.56  ? 981  GLY B N   1 
ATOM   21794 C  CA  . GLY C 1 981  ? 20.577   44.204  96.922  1.00 88.88  ? 981  GLY B CA  1 
ATOM   21795 C  C   . GLY C 1 981  ? 19.248   44.770  97.347  1.00 86.31  ? 981  GLY B C   1 
ATOM   21796 O  O   . GLY C 1 981  ? 18.452   45.150  96.498  1.00 87.82  ? 981  GLY B O   1 
ATOM   21797 N  N   . LEU C 1 982  ? 19.018   44.799  98.655  1.00 83.02  ? 982  LEU B N   1 
ATOM   21798 C  CA  . LEU C 1 982  ? 17.826   45.383  99.287  1.00 82.22  ? 982  LEU B CA  1 
ATOM   21799 C  C   . LEU C 1 982  ? 16.567   44.516  99.257  1.00 87.20  ? 982  LEU B C   1 
ATOM   21800 O  O   . LEU C 1 982  ? 16.269   43.844  98.263  1.00 87.86  ? 982  LEU B O   1 
ATOM   21801 C  CB  . LEU C 1 982  ? 17.522   46.784  98.760  1.00 80.48  ? 982  LEU B CB  1 
ATOM   21802 C  CG  . LEU C 1 982  ? 18.711   47.735  98.747  1.00 79.90  ? 982  LEU B CG  1 
ATOM   21803 C  CD1 . LEU C 1 982  ? 18.329   49.074  99.347  1.00 80.24  ? 982  LEU B CD1 1 
ATOM   21804 C  CD2 . LEU C 1 982  ? 19.829   47.133  99.531  1.00 79.48  ? 982  LEU B CD2 1 
ATOM   21805 N  N   . LEU C 1 983  ? 15.838   44.536  100.371 1.00 89.29  ? 983  LEU B N   1 
ATOM   21806 C  CA  . LEU C 1 983  ? 14.626   43.752  100.512 1.00 91.36  ? 983  LEU B CA  1 
ATOM   21807 C  C   . LEU C 1 983  ? 13.613   44.346  99.577  1.00 98.27  ? 983  LEU B C   1 
ATOM   21808 O  O   . LEU C 1 983  ? 12.647   43.704  99.183  1.00 97.88  ? 983  LEU B O   1 
ATOM   21809 C  CB  . LEU C 1 983  ? 14.126   43.843  101.941 1.00 88.44  ? 983  LEU B CB  1 
ATOM   21810 C  CG  . LEU C 1 983  ? 14.732   42.861  102.948 1.00 87.31  ? 983  LEU B CG  1 
ATOM   21811 C  CD1 . LEU C 1 983  ? 15.951   42.172  102.413 1.00 86.07  ? 983  LEU B CD1 1 
ATOM   21812 C  CD2 . LEU C 1 983  ? 15.067   43.568  104.241 1.00 88.47  ? 983  LEU B CD2 1 
ATOM   21813 N  N   . VAL C 1 984  ? 13.867   45.595  99.216  1.00 75.80  ? 984  VAL B N   1 
ATOM   21814 C  CA  . VAL C 1 984  ? 12.978   46.371  98.375  1.00 81.70  ? 984  VAL B CA  1 
ATOM   21815 C  C   . VAL C 1 984  ? 13.624   46.555  96.984  1.00 88.50  ? 984  VAL B C   1 
ATOM   21816 O  O   . VAL C 1 984  ? 13.370   47.513  96.269  1.00 92.68  ? 984  VAL B O   1 
ATOM   21817 C  CB  . VAL C 1 984  ? 12.680   47.712  99.079  1.00 78.09  ? 984  VAL B CB  1 
ATOM   21818 C  CG1 . VAL C 1 984  ? 13.699   48.750  98.674  1.00 79.86  ? 984  VAL B CG1 1 
ATOM   21819 C  CG2 . VAL C 1 984  ? 11.246   48.192  98.836  1.00 77.88  ? 984  VAL B CG2 1 
ATOM   21820 N  N   . GLY C 1 985  ? 14.474   45.609  96.608  1.00 91.90  ? 985  GLY B N   1 
ATOM   21821 C  CA  . GLY C 1 985  ? 15.180   45.661  95.335  1.00 91.70  ? 985  GLY B CA  1 
ATOM   21822 C  C   . GLY C 1 985  ? 14.512   45.051  94.098  1.00 92.47  ? 985  GLY B C   1 
ATOM   21823 O  O   . GLY C 1 985  ? 14.789   45.494  92.977  1.00 91.47  ? 985  GLY B O   1 
ATOM   21824 N  N   . GLU C 1 986  ? 13.679   44.022  94.254  1.00 91.19  ? 986  GLU B N   1 
ATOM   21825 C  CA  . GLU C 1 986  ? 12.896   43.607  93.113  1.00 89.48  ? 986  GLU B CA  1 
ATOM   21826 C  C   . GLU C 1 986  ? 12.006   44.781  92.836  1.00 88.63  ? 986  GLU B C   1 
ATOM   21827 O  O   . GLU C 1 986  ? 12.012   45.310  91.731  1.00 91.26  ? 986  GLU B O   1 
ATOM   21828 C  CB  . GLU C 1 986  ? 12.044   42.394  93.407  1.00 89.86  ? 986  GLU B CB  1 
ATOM   21829 C  CG  . GLU C 1 986  ? 11.948   41.444  92.234  1.00 92.30  ? 986  GLU B CG  1 
ATOM   21830 C  CD  . GLU C 1 986  ? 13.300   40.843  91.906  1.00 96.21  ? 986  GLU B CD  1 
ATOM   21831 O  OE1 . GLU C 1 986  ? 13.506   39.611  92.047  1.00 96.74  ? 986  GLU B OE1 1 
ATOM   21832 O  OE2 . GLU C 1 986  ? 14.181   41.626  91.516  1.00 98.67  ? 986  GLU B OE2 1 
ATOM   21833 N  N   . ILE C 1 987  ? 11.274   45.237  93.848  1.00 84.25  ? 987  ILE B N   1 
ATOM   21834 C  CA  . ILE C 1 987  ? 10.271   46.256  93.597  1.00 83.23  ? 987  ILE B CA  1 
ATOM   21835 C  C   . ILE C 1 987  ? 10.884   47.494  93.040  1.00 87.55  ? 987  ILE B C   1 
ATOM   21836 O  O   . ILE C 1 987  ? 10.177   48.354  92.556  1.00 89.43  ? 987  ILE B O   1 
ATOM   21837 C  CB  . ILE C 1 987  ? 9.571    46.722  94.825  1.00 79.06  ? 987  ILE B CB  1 
ATOM   21838 C  CG1 . ILE C 1 987  ? 9.550    45.628  95.873  1.00 86.25  ? 987  ILE B CG1 1 
ATOM   21839 C  CG2 . ILE C 1 987  ? 8.181    47.191  94.477  1.00 74.00  ? 987  ILE B CG2 1 
ATOM   21840 C  CD1 . ILE C 1 987  ? 8.473    45.864  96.948  1.00 89.71  ? 987  ILE B CD1 1 
ATOM   21841 N  N   . LEU C 1 988  ? 12.195   47.620  93.155  1.00 89.62  ? 988  LEU B N   1 
ATOM   21842 C  CA  . LEU C 1 988  ? 12.869   48.757  92.570  1.00 91.89  ? 988  LEU B CA  1 
ATOM   21843 C  C   . LEU C 1 988  ? 13.233   48.469  91.135  1.00 94.02  ? 988  LEU B C   1 
ATOM   21844 O  O   . LEU C 1 988  ? 12.993   49.294  90.278  1.00 96.77  ? 988  LEU B O   1 
ATOM   21845 C  CB  . LEU C 1 988  ? 14.117   49.107  93.358  1.00 93.35  ? 988  LEU B CB  1 
ATOM   21846 C  CG  . LEU C 1 988  ? 13.905   50.000  94.569  1.00 92.16  ? 988  LEU B CG  1 
ATOM   21847 C  CD1 . LEU C 1 988  ? 15.234   50.188  95.251  1.00 94.44  ? 988  LEU B CD1 1 
ATOM   21848 C  CD2 . LEU C 1 988  ? 13.291   51.336  94.179  1.00 90.59  ? 988  LEU B CD2 1 
ATOM   21849 N  N   . SER C 1 989  ? 13.822   47.303  90.875  1.00 95.15  ? 989  SER B N   1 
ATOM   21850 C  CA  . SER C 1 989  ? 14.236   46.932  89.520  1.00 95.88  ? 989  SER B CA  1 
ATOM   21851 C  C   . SER C 1 989  ? 13.029   46.905  88.590  1.00 91.77  ? 989  SER B C   1 
ATOM   21852 O  O   . SER C 1 989  ? 13.110   47.275  87.415  1.00 91.28  ? 989  SER B O   1 
ATOM   21853 C  CB  . SER C 1 989  ? 14.971   45.582  89.503  1.00 98.68  ? 989  SER B CB  1 
ATOM   21854 O  OG  . SER C 1 989  ? 15.386   45.243  88.187  1.00 101.79 ? 989  SER B OG  1 
ATOM   21855 N  N   . ALA C 1 990  ? 11.891   46.505  89.123  1.00 89.44  ? 990  ALA B N   1 
ATOM   21856 C  CA  . ALA C 1 990  ? 10.711   46.457  88.290  1.00 91.23  ? 990  ALA B CA  1 
ATOM   21857 C  C   . ALA C 1 990  ? 10.260   47.839  87.803  1.00 90.77  ? 990  ALA B C   1 
ATOM   21858 O  O   . ALA C 1 990  ? 9.688    47.975  86.722  1.00 94.18  ? 990  ALA B O   1 
ATOM   21859 C  CB  . ALA C 1 990  ? 9.573    45.723  88.996  1.00 90.82  ? 990  ALA B CB  1 
ATOM   21860 N  N   . VAL C 1 991  ? 10.504   48.874  88.583  1.00 88.18  ? 991  VAL B N   1 
ATOM   21861 C  CA  . VAL C 1 991  ? 10.011   50.187  88.171  1.00 89.18  ? 991  VAL B CA  1 
ATOM   21862 C  C   . VAL C 1 991  ? 11.098   51.002  87.466  1.00 92.08  ? 991  VAL B C   1 
ATOM   21863 O  O   . VAL C 1 991  ? 10.827   51.998  86.801  1.00 93.37  ? 991  VAL B O   1 
ATOM   21864 C  CB  . VAL C 1 991  ? 9.281    50.935  89.350  1.00 63.87  ? 991  VAL B CB  1 
ATOM   21865 C  CG1 . VAL C 1 991  ? 9.057    52.415  89.055  1.00 62.71  ? 991  VAL B CG1 1 
ATOM   21866 C  CG2 . VAL C 1 991  ? 7.953    50.233  89.666  1.00 63.55  ? 991  VAL B CG2 1 
ATOM   21867 N  N   . LEU C 1 992  ? 12.330   50.541  87.549  1.00 94.01  ? 992  LEU B N   1 
ATOM   21868 C  CA  . LEU C 1 992  ? 13.388   51.283  86.916  1.00 100.49 ? 992  LEU B CA  1 
ATOM   21869 C  C   . LEU C 1 992  ? 14.210   50.377  86.032  1.00 117.03 ? 992  LEU B C   1 
ATOM   21870 O  O   . LEU C 1 992  ? 15.432   50.376  86.124  1.00 123.50 ? 992  LEU B O   1 
ATOM   21871 C  CB  . LEU C 1 992  ? 14.290   51.933  87.960  1.00 93.37  ? 992  LEU B CB  1 
ATOM   21872 C  CG  . LEU C 1 992  ? 13.641   52.520  89.209  1.00 86.81  ? 992  LEU B CG  1 
ATOM   21873 C  CD1 . LEU C 1 992  ? 14.682   52.617  90.272  1.00 84.18  ? 992  LEU B CD1 1 
ATOM   21874 C  CD2 . LEU C 1 992  ? 13.069   53.880  88.918  1.00 87.74  ? 992  LEU B CD2 1 
ATOM   21875 N  N   . SER C 1 993  ? 13.551   49.606  85.175  1.00 126.34 ? 993  SER B N   1 
ATOM   21876 C  CA  . SER C 1 993  ? 14.255   48.784  84.199  1.00 136.18 ? 993  SER B CA  1 
ATOM   21877 C  C   . SER C 1 993  ? 13.380   48.648  82.975  1.00 147.03 ? 993  SER B C   1 
ATOM   21878 O  O   . SER C 1 993  ? 13.857   48.404  81.864  1.00 149.90 ? 993  SER B O   1 
ATOM   21879 C  CB  . SER C 1 993  ? 14.556   47.407  84.779  1.00 135.44 ? 993  SER B CB  1 
ATOM   21880 O  OG  . SER C 1 993  ? 15.555   47.485  85.788  1.00 134.38 ? 993  SER B OG  1 
ATOM   21881 N  N   . GLN C 1 994  ? 12.083   48.792  83.208  1.00 153.77 ? 994  GLN B N   1 
ATOM   21882 C  CA  . GLN C 1 994  ? 11.094   48.829  82.153  1.00 161.81 ? 994  GLN B CA  1 
ATOM   21883 C  C   . GLN C 1 994  ? 10.452   50.204  82.198  1.00 163.45 ? 994  GLN B C   1 
ATOM   21884 O  O   . GLN C 1 994  ? 10.218   50.732  83.282  1.00 159.38 ? 994  GLN B O   1 
ATOM   21885 C  CB  . GLN C 1 994  ? 10.031   47.771  82.415  1.00 166.27 ? 994  GLN B CB  1 
ATOM   21886 C  CG  . GLN C 1 994  ? 9.367    47.938  83.764  1.00 168.40 ? 994  GLN B CG  1 
ATOM   21887 C  CD  . GLN C 1 994  ? 7.865    48.089  83.650  1.00 171.16 ? 994  GLN B CD  1 
ATOM   21888 O  OE1 . GLN C 1 994  ? 7.247    47.543  82.731  1.00 173.90 ? 994  GLN B OE1 1 
ATOM   21889 N  NE2 . GLN C 1 994  ? 7.265    48.837  84.580  1.00 169.92 ? 994  GLN B NE2 1 
ATOM   21890 N  N   . GLU C 1 995  ? 10.182   50.793  81.034  1.00 169.72 ? 995  GLU B N   1 
ATOM   21891 C  CA  . GLU C 1 995  ? 9.422    52.046  80.981  1.00 174.50 ? 995  GLU B CA  1 
ATOM   21892 C  C   . GLU C 1 995  ? 7.939    51.742  81.028  1.00 174.05 ? 995  GLU B C   1 
ATOM   21893 O  O   . GLU C 1 995  ? 7.539    50.580  80.950  1.00 173.10 ? 995  GLU B O   1 
ATOM   21894 C  CB  . GLU C 1 995  ? 9.731    52.863  79.721  1.00 180.06 ? 995  GLU B CB  1 
ATOM   21895 C  CG  . GLU C 1 995  ? 10.809   53.927  79.886  1.00 184.00 ? 995  GLU B CG  1 
ATOM   21896 C  CD  . GLU C 1 995  ? 12.178   53.448  79.442  1.00 188.13 ? 995  GLU B CD  1 
ATOM   21897 O  OE1 . GLU C 1 995  ? 12.240   52.427  78.717  1.00 189.51 ? 995  GLU B OE1 1 
ATOM   21898 O  OE2 . GLU C 1 995  ? 13.186   54.094  79.816  1.00 189.28 ? 995  GLU B OE2 1 
ATOM   21899 N  N   . GLY C 1 996  ? 7.128    52.788  81.148  1.00 175.51 ? 996  GLY B N   1 
ATOM   21900 C  CA  . GLY C 1 996  ? 5.685    52.634  81.164  1.00 177.70 ? 996  GLY B CA  1 
ATOM   21901 C  C   . GLY C 1 996  ? 5.187    51.680  82.235  1.00 178.98 ? 996  GLY B C   1 
ATOM   21902 O  O   . GLY C 1 996  ? 5.610    50.526  82.305  1.00 178.83 ? 996  GLY B O   1 
ATOM   21903 N  N   . ILE C 1 997  ? 4.268    52.167  83.062  1.00 179.28 ? 997  ILE B N   1 
ATOM   21904 C  CA  . ILE C 1 997  ? 3.727    51.403  84.182  1.00 178.46 ? 997  ILE B CA  1 
ATOM   21905 C  C   . ILE C 1 997  ? 3.190    50.027  83.746  1.00 182.74 ? 997  ILE B C   1 
ATOM   21906 O  O   . ILE C 1 997  ? 2.720    49.861  82.621  1.00 185.27 ? 997  ILE B O   1 
ATOM   21907 C  CB  . ILE C 1 997  ? 2.641    52.220  84.878  1.00 174.82 ? 997  ILE B CB  1 
ATOM   21908 C  CG1 . ILE C 1 997  ? 1.312    52.061  84.150  1.00 173.98 ? 997  ILE B CG1 1 
ATOM   21909 C  CG2 . ILE C 1 997  ? 3.040    53.688  84.891  1.00 173.43 ? 997  ILE B CG2 1 
ATOM   21910 C  CD1 . ILE C 1 997  ? 0.323    53.155  84.445  1.00 173.57 ? 997  ILE B CD1 1 
ATOM   21911 N  N   . ASN C 1 998  ? 3.265    49.047  84.644  1.00 184.43 ? 998  ASN B N   1 
ATOM   21912 C  CA  . ASN C 1 998  ? 2.973    47.655  84.300  1.00 186.49 ? 998  ASN B CA  1 
ATOM   21913 C  C   . ASN C 1 998  ? 2.512    46.829  85.502  1.00 179.43 ? 998  ASN B C   1 
ATOM   21914 O  O   . ASN C 1 998  ? 3.003    47.039  86.607  1.00 181.67 ? 998  ASN B O   1 
ATOM   21915 C  CB  . ASN C 1 998  ? 4.217    47.011  83.679  1.00 194.07 ? 998  ASN B CB  1 
ATOM   21916 C  CG  . ASN C 1 998  ? 4.227    45.492  83.812  1.00 201.14 ? 998  ASN B CG  1 
ATOM   21917 O  OD1 . ASN C 1 998  ? 3.239    44.822  83.507  1.00 203.88 ? 998  ASN B OD1 1 
ATOM   21918 N  ND2 . ASN C 1 998  ? 5.354    44.942  84.260  1.00 203.15 ? 998  ASN B ND2 1 
ATOM   21919 N  N   . ILE C 1 999  ? 1.573    45.900  85.275  1.00 171.34 ? 999  ILE B N   1 
ATOM   21920 C  CA  . ILE C 1 999  ? 1.080    44.961  86.306  1.00 160.86 ? 999  ILE B CA  1 
ATOM   21921 C  C   . ILE C 1 999  ? 2.134    43.908  86.692  1.00 152.41 ? 999  ILE B C   1 
ATOM   21922 O  O   . ILE C 1 999  ? 3.033    43.578  85.914  1.00 152.50 ? 999  ILE B O   1 
ATOM   21923 C  CB  . ILE C 1 999  ? -0.241   44.226  85.878  1.00 272.31 ? 999  ILE B CB  1 
ATOM   21924 C  CG1 . ILE C 1 999  ? -1.211   45.174  85.164  1.00 272.77 ? 999  ILE B CG1 1 
ATOM   21925 C  CG2 . ILE C 1 999  ? -0.923   43.557  87.085  1.00 271.11 ? 999  ILE B CG2 1 
ATOM   21926 C  CD1 . ILE C 1 999  ? -1.828   46.217  86.067  1.00 271.29 ? 999  ILE B CD1 1 
ATOM   21927 N  N   . LEU C 1 1000 ? 2.013    43.374  87.899  1.00 144.85 ? 1000 LEU B N   1 
ATOM   21928 C  CA  . LEU C 1 1000 ? 3.084    42.561  88.434  1.00 137.22 ? 1000 LEU B CA  1 
ATOM   21929 C  C   . LEU C 1 1000 ? 2.790    41.062  88.407  1.00 134.31 ? 1000 LEU B C   1 
ATOM   21930 O  O   . LEU C 1 1000 ? 3.437    40.246  89.073  1.00 133.90 ? 1000 LEU B O   1 
ATOM   21931 C  CB  . LEU C 1 1000 ? 3.484    43.077  89.810  1.00 128.60 ? 1000 LEU B CB  1 
ATOM   21932 C  CG  . LEU C 1 1000 ? 4.538    44.170  89.690  1.00 119.52 ? 1000 LEU B CG  1 
ATOM   21933 C  CD1 . LEU C 1 1000 ? 5.090    44.455  91.053  1.00 115.52 ? 1000 LEU B CD1 1 
ATOM   21934 C  CD2 . LEU C 1 1000 ? 5.667    43.757  88.719  1.00 117.19 ? 1000 LEU B CD2 1 
ATOM   21935 N  N   . THR C 1 1001 ? 1.824    40.685  87.597  1.00 131.39 ? 1001 THR B N   1 
ATOM   21936 C  CA  . THR C 1 1001 ? 1.557    39.280  87.466  1.00 129.63 ? 1001 THR B CA  1 
ATOM   21937 C  C   . THR C 1 1001 ? 1.159    38.956  86.039  1.00 135.67 ? 1001 THR B C   1 
ATOM   21938 O  O   . THR C 1 1001 ? 1.312    39.778  85.143  1.00 139.55 ? 1001 THR B O   1 
ATOM   21939 C  CB  . THR C 1 1001 ? 0.471    38.891  88.423  1.00 123.20 ? 1001 THR B CB  1 
ATOM   21940 O  OG1 . THR C 1 1001 ? 0.395    39.886  89.448  1.00 115.44 ? 1001 THR B OG1 1 
ATOM   21941 C  CG2 . THR C 1 1001 ? 0.795    37.529  89.020  1.00 122.93 ? 1001 THR B CG2 1 
ATOM   21942 N  N   . HIS C 1 1002 ? 0.681    37.746  85.810  1.00 138.30 ? 1002 HIS B N   1 
ATOM   21943 C  CA  . HIS C 1 1002 ? 0.056    37.468  84.533  1.00 138.69 ? 1002 HIS B CA  1 
ATOM   21944 C  C   . HIS C 1 1002 ? -1.433   37.889  84.574  1.00 124.75 ? 1002 HIS B C   1 
ATOM   21945 O  O   . HIS C 1 1002 ? -2.153   37.736  83.587  1.00 123.68 ? 1002 HIS B O   1 
ATOM   21946 C  CB  . HIS C 1 1002 ? 0.255    35.994  84.122  1.00 152.32 ? 1002 HIS B CB  1 
ATOM   21947 C  CG  . HIS C 1 1002 ? 1.694    35.605  83.913  1.00 161.21 ? 1002 HIS B CG  1 
ATOM   21948 N  ND1 . HIS C 1 1002 ? 2.437    34.947  84.870  1.00 163.44 ? 1002 HIS B ND1 1 
ATOM   21949 C  CD2 . HIS C 1 1002 ? 2.519    35.774  82.850  1.00 165.20 ? 1002 HIS B CD2 1 
ATOM   21950 C  CE1 . HIS C 1 1002 ? 3.657    34.731  84.409  1.00 165.16 ? 1002 HIS B CE1 1 
ATOM   21951 N  NE2 . HIS C 1 1002 ? 3.733    35.224  83.187  1.00 166.15 ? 1002 HIS B NE2 1 
ATOM   21952 N  N   . LEU C 1 1003 ? -1.882   38.454  85.697  1.00 114.30 ? 1003 LEU B N   1 
ATOM   21953 C  CA  . LEU C 1 1003 ? -3.308   38.750  85.896  1.00 108.74 ? 1003 LEU B CA  1 
ATOM   21954 C  C   . LEU C 1 1003 ? -3.939   39.780  84.937  1.00 111.86 ? 1003 LEU B C   1 
ATOM   21955 O  O   . LEU C 1 1003 ? -3.565   40.963  84.933  1.00 112.61 ? 1003 LEU B O   1 
ATOM   21956 C  CB  . LEU C 1 1003 ? -3.600   39.107  87.358  1.00 98.77  ? 1003 LEU B CB  1 
ATOM   21957 C  CG  . LEU C 1 1003 ? -3.398   37.929  88.301  1.00 90.35  ? 1003 LEU B CG  1 
ATOM   21958 C  CD1 . LEU C 1 1003 ? -4.546   37.819  89.304  1.00 85.57  ? 1003 LEU B CD1 1 
ATOM   21959 C  CD2 . LEU C 1 1003 ? -3.266   36.651  87.472  1.00 91.51  ? 1003 LEU B CD2 1 
ATOM   21960 N  N   . PRO C 1 1004 ? -4.925   39.309  84.143  1.00 110.30 ? 1004 PRO B N   1 
ATOM   21961 C  CA  . PRO C 1 1004 ? -5.767   39.878  83.076  1.00 111.00 ? 1004 PRO B CA  1 
ATOM   21962 C  C   . PRO C 1 1004 ? -6.415   41.217  83.410  1.00 105.64 ? 1004 PRO B C   1 
ATOM   21963 O  O   . PRO C 1 1004 ? -6.973   41.402  84.486  1.00 105.41 ? 1004 PRO B O   1 
ATOM   21964 C  CB  . PRO C 1 1004 ? -6.871   38.829  82.945  1.00 112.55 ? 1004 PRO B CB  1 
ATOM   21965 C  CG  . PRO C 1 1004 ? -6.770   38.016  84.241  1.00 111.03 ? 1004 PRO B CG  1 
ATOM   21966 C  CD  . PRO C 1 1004 ? -5.326   37.921  84.406  1.00 110.44 ? 1004 PRO B CD  1 
ATOM   21967 N  N   . LYS C 1 1005 ? -6.388   42.132  82.459  1.00 105.94 ? 1005 LYS B N   1 
ATOM   21968 C  CA  . LYS C 1 1005 ? -6.655   43.531  82.769  1.00 108.48 ? 1005 LYS B CA  1 
ATOM   21969 C  C   . LYS C 1 1005 ? -8.116   43.975  82.970  1.00 109.60 ? 1005 LYS B C   1 
ATOM   21970 O  O   . LYS C 1 1005 ? -8.354   45.180  83.106  1.00 107.34 ? 1005 LYS B O   1 
ATOM   21971 C  CB  . LYS C 1 1005 ? -5.994   44.460  81.727  1.00 115.41 ? 1005 LYS B CB  1 
ATOM   21972 C  CG  . LYS C 1 1005 ? -4.470   44.390  81.660  1.00 122.65 ? 1005 LYS B CG  1 
ATOM   21973 C  CD  . LYS C 1 1005 ? -3.783   45.341  82.634  1.00 127.67 ? 1005 LYS B CD  1 
ATOM   21974 C  CE  . LYS C 1 1005 ? -3.953   46.813  82.240  1.00 132.48 ? 1005 LYS B CE  1 
ATOM   21975 N  NZ  . LYS C 1 1005 ? -3.257   47.692  83.235  1.00 132.72 ? 1005 LYS B NZ  1 
ATOM   21976 N  N   . GLY C 1 1006 ? -9.086   43.064  83.009  1.00 113.03 ? 1006 GLY B N   1 
ATOM   21977 C  CA  . GLY C 1 1006 ? -10.488  43.497  82.969  1.00 115.44 ? 1006 GLY B CA  1 
ATOM   21978 C  C   . GLY C 1 1006 ? -11.033  44.463  84.030  1.00 110.58 ? 1006 GLY B C   1 
ATOM   21979 O  O   . GLY C 1 1006 ? -11.719  45.477  83.768  1.00 107.42 ? 1006 GLY B O   1 
ATOM   21980 N  N   . SER C 1 1007 ? -10.728  44.114  85.265  1.00 108.06 ? 1007 SER B N   1 
ATOM   21981 C  CA  . SER C 1 1007 ? -11.232  44.837  86.413  1.00 104.99 ? 1007 SER B CA  1 
ATOM   21982 C  C   . SER C 1 1007 ? -10.737  46.269  86.389  1.00 99.87  ? 1007 SER B C   1 
ATOM   21983 O  O   . SER C 1 1007 ? -9.791   46.605  85.664  1.00 96.65  ? 1007 SER B O   1 
ATOM   21984 C  CB  . SER C 1 1007 ? -10.762  44.145  87.702  1.00 105.93 ? 1007 SER B CB  1 
ATOM   21985 O  OG  . SER C 1 1007 ? -11.194  44.830  88.860  1.00 106.53 ? 1007 SER B OG  1 
ATOM   21986 N  N   . ALA C 1 1008 ? -11.401  47.104  87.180  1.00 99.26  ? 1008 ALA B N   1 
ATOM   21987 C  CA  . ALA C 1 1008 ? -10.874  48.402  87.536  1.00 99.20  ? 1008 ALA B CA  1 
ATOM   21988 C  C   . ALA C 1 1008 ? -9.696   48.148  88.453  1.00 95.63  ? 1008 ALA B C   1 
ATOM   21989 O  O   . ALA C 1 1008 ? -8.748   48.929  88.517  1.00 96.37  ? 1008 ALA B O   1 
ATOM   21990 C  CB  . ALA C 1 1008 ? -11.916  49.202  88.245  1.00 100.66 ? 1008 ALA B CB  1 
ATOM   21991 N  N   . GLU C 1 1009 ? -9.760   47.035  89.163  1.00 92.83  ? 1009 GLU B N   1 
ATOM   21992 C  CA  . GLU C 1 1009 ? -8.706   46.697  90.096  1.00 91.10  ? 1009 GLU B CA  1 
ATOM   21993 C  C   . GLU C 1 1009 ? -7.366   46.567  89.361  1.00 89.89  ? 1009 GLU B C   1 
ATOM   21994 O  O   . GLU C 1 1009 ? -6.309   46.831  89.939  1.00 90.31  ? 1009 GLU B O   1 
ATOM   21995 C  CB  . GLU C 1 1009 ? -9.060   45.419  90.878  1.00 90.15  ? 1009 GLU B CB  1 
ATOM   21996 C  CG  . GLU C 1 1009 ? -8.311   45.194  92.202  1.00 85.18  ? 1009 GLU B CG  1 
ATOM   21997 C  CD  . GLU C 1 1009 ? -8.209   43.706  92.549  1.00 84.55  ? 1009 GLU B CD  1 
ATOM   21998 O  OE1 . GLU C 1 1009 ? -9.227   42.949  92.494  1.00 83.92  ? 1009 GLU B OE1 1 
ATOM   21999 O  OE2 . GLU C 1 1009 ? -7.081   43.292  92.861  1.00 84.03  ? 1009 GLU B OE2 1 
ATOM   22000 N  N   . ALA C 1 1010 ? -7.386   46.178  88.096  1.00 88.38  ? 1010 ALA B N   1 
ATOM   22001 C  CA  . ALA C 1 1010 ? -6.120   45.938  87.442  1.00 90.53  ? 1010 ALA B CA  1 
ATOM   22002 C  C   . ALA C 1 1010 ? -5.538   47.252  86.970  1.00 88.97  ? 1010 ALA B C   1 
ATOM   22003 O  O   . ALA C 1 1010 ? -4.338   47.417  86.725  1.00 86.20  ? 1010 ALA B O   1 
ATOM   22004 C  CB  . ALA C 1 1010 ? -6.303   44.970  86.309  1.00 96.02  ? 1010 ALA B CB  1 
ATOM   22005 N  N   . GLU C 1 1011 ? -6.423   48.212  86.849  1.00 91.39  ? 1011 GLU B N   1 
ATOM   22006 C  CA  . GLU C 1 1011 ? -6.005   49.506  86.379  1.00 94.35  ? 1011 GLU B CA  1 
ATOM   22007 C  C   . GLU C 1 1011 ? -5.336   50.193  87.548  1.00 92.23  ? 1011 GLU B C   1 
ATOM   22008 O  O   . GLU C 1 1011 ? -4.343   50.898  87.366  1.00 93.09  ? 1011 GLU B O   1 
ATOM   22009 C  CB  . GLU C 1 1011 ? -7.202   50.316  85.881  1.00 97.15  ? 1011 GLU B CB  1 
ATOM   22010 C  CG  . GLU C 1 1011 ? -6.979   50.805  84.486  1.00 99.64  ? 1011 GLU B CG  1 
ATOM   22011 C  CD  . GLU C 1 1011 ? -6.311   49.754  83.648  1.00 102.20 ? 1011 GLU B CD  1 
ATOM   22012 O  OE1 . GLU C 1 1011 ? -6.982   48.731  83.375  1.00 104.12 ? 1011 GLU B OE1 1 
ATOM   22013 O  OE2 . GLU C 1 1011 ? -5.122   49.939  83.289  1.00 102.17 ? 1011 GLU B OE2 1 
ATOM   22014 N  N   . LEU C 1 1012 ? -5.890   49.964  88.744  1.00 88.35  ? 1012 LEU B N   1 
ATOM   22015 C  CA  . LEU C 1 1012 ? -5.384   50.540  89.985  1.00 82.68  ? 1012 LEU B CA  1 
ATOM   22016 C  C   . LEU C 1 1012 ? -4.030   49.961  90.347  1.00 85.44  ? 1012 LEU B C   1 
ATOM   22017 O  O   . LEU C 1 1012 ? -3.080   50.712  90.597  1.00 87.13  ? 1012 LEU B O   1 
ATOM   22018 C  CB  . LEU C 1 1012 ? -6.380   50.331  91.119  1.00 75.32  ? 1012 LEU B CB  1 
ATOM   22019 C  CG  . LEU C 1 1012 ? -7.294   51.537  91.248  1.00 73.42  ? 1012 LEU B CG  1 
ATOM   22020 C  CD1 . LEU C 1 1012 ? -8.359   51.340  92.299  1.00 71.63  ? 1012 LEU B CD1 1 
ATOM   22021 C  CD2 . LEU C 1 1012 ? -6.449   52.757  91.563  1.00 72.62  ? 1012 LEU B CD2 1 
ATOM   22022 N  N   . MET C 1 1013 ? -3.945   48.628  90.340  1.00 85.70  ? 1013 MET B N   1 
ATOM   22023 C  CA  . MET C 1 1013 ? -2.726   47.895  90.674  1.00 84.77  ? 1013 MET B CA  1 
ATOM   22024 C  C   . MET C 1 1013 ? -1.517   48.264  89.808  1.00 88.81  ? 1013 MET B C   1 
ATOM   22025 O  O   . MET C 1 1013 ? -0.412   47.800  90.040  1.00 90.36  ? 1013 MET B O   1 
ATOM   22026 C  CB  . MET C 1 1013 ? -2.982   46.404  90.534  1.00 84.44  ? 1013 MET B CB  1 
ATOM   22027 C  CG  . MET C 1 1013 ? -1.964   45.541  91.251  1.00 85.18  ? 1013 MET B CG  1 
ATOM   22028 S  SD  . MET C 1 1013 ? -2.371   45.522  92.993  1.00 105.87 ? 1013 MET B SD  1 
ATOM   22029 C  CE  . MET C 1 1013 ? -4.163   45.637  92.851  1.00 84.86  ? 1013 MET B CE  1 
ATOM   22030 N  N   . SER C 1 1014 ? -1.741   49.082  88.794  1.00 91.08  ? 1014 SER B N   1 
ATOM   22031 C  CA  . SER C 1 1014 ? -0.695   49.519  87.882  1.00 91.78  ? 1014 SER B CA  1 
ATOM   22032 C  C   . SER C 1 1014 ? 0.089    50.682  88.480  1.00 85.16  ? 1014 SER B C   1 
ATOM   22033 O  O   . SER C 1 1014 ? 1.318    50.771  88.363  1.00 82.32  ? 1014 SER B O   1 
ATOM   22034 C  CB  . SER C 1 1014 ? -1.352   50.013  86.593  1.00 98.57  ? 1014 SER B CB  1 
ATOM   22035 O  OG  . SER C 1 1014 ? -1.831   51.362  86.726  1.00 101.01 ? 1014 SER B OG  1 
ATOM   22036 N  N   . VAL C 1 1015 ? -0.648   51.600  89.082  1.00 82.61  ? 1015 VAL B N   1 
ATOM   22037 C  CA  . VAL C 1 1015 ? -0.037   52.723  89.729  1.00 83.36  ? 1015 VAL B CA  1 
ATOM   22038 C  C   . VAL C 1 1015 ? 0.835    52.213  90.909  1.00 83.66  ? 1015 VAL B C   1 
ATOM   22039 O  O   . VAL C 1 1015 ? 1.861    52.807  91.240  1.00 86.44  ? 1015 VAL B O   1 
ATOM   22040 C  CB  . VAL C 1 1015 ? -1.137   53.744  90.169  1.00 90.40  ? 1015 VAL B CB  1 
ATOM   22041 C  CG1 . VAL C 1 1015 ? -2.127   53.119  91.137  1.00 88.69  ? 1015 VAL B CG1 1 
ATOM   22042 C  CG2 . VAL C 1 1015 ? -0.525   55.036  90.750  1.00 90.95  ? 1015 VAL B CG2 1 
ATOM   22043 N  N   . VAL C 1 1016 ? 0.457    51.079  91.500  1.00 77.56  ? 1016 VAL B N   1 
ATOM   22044 C  CA  . VAL C 1 1016 ? 1.078    50.581  92.741  1.00 69.67  ? 1016 VAL B CA  1 
ATOM   22045 C  C   . VAL C 1 1016 ? 2.613    50.597  92.811  1.00 65.35  ? 1016 VAL B C   1 
ATOM   22046 O  O   . VAL C 1 1016 ? 3.168    51.390  93.550  1.00 60.63  ? 1016 VAL B O   1 
ATOM   22047 C  CB  . VAL C 1 1016 ? 0.531    49.184  93.134  1.00 66.78  ? 1016 VAL B CB  1 
ATOM   22048 C  CG1 . VAL C 1 1016 ? 1.529    48.409  93.987  1.00 64.39  ? 1016 VAL B CG1 1 
ATOM   22049 C  CG2 . VAL C 1 1016 ? -0.801   49.308  93.829  1.00 67.40  ? 1016 VAL B CG2 1 
ATOM   22050 N  N   . PRO C 1 1017 ? 3.300    49.717  92.057  1.00 66.94  ? 1017 PRO B N   1 
ATOM   22051 C  CA  . PRO C 1 1017 ? 4.759    49.594  92.145  1.00 69.00  ? 1017 PRO B CA  1 
ATOM   22052 C  C   . PRO C 1 1017 ? 5.549    50.861  91.871  1.00 70.70  ? 1017 PRO B C   1 
ATOM   22053 O  O   . PRO C 1 1017 ? 6.691    50.977  92.286  1.00 69.19  ? 1017 PRO B O   1 
ATOM   22054 C  CB  . PRO C 1 1017 ? 5.078    48.520  91.094  1.00 68.02  ? 1017 PRO B CB  1 
ATOM   22055 C  CG  . PRO C 1 1017 ? 3.893    47.684  91.096  1.00 66.75  ? 1017 PRO B CG  1 
ATOM   22056 C  CD  . PRO C 1 1017 ? 2.759    48.671  91.177  1.00 67.69  ? 1017 PRO B CD  1 
ATOM   22057 N  N   . VAL C 1 1018 ? 4.964    51.799  91.155  1.00 75.22  ? 1018 VAL B N   1 
ATOM   22058 C  CA  . VAL C 1 1018 ? 5.610    53.098  91.072  1.00 83.07  ? 1018 VAL B CA  1 
ATOM   22059 C  C   . VAL C 1 1018 ? 5.394    53.783  92.415  1.00 84.14  ? 1018 VAL B C   1 
ATOM   22060 O  O   . VAL C 1 1018 ? 6.348    54.209  93.062  1.00 83.64  ? 1018 VAL B O   1 
ATOM   22061 C  CB  . VAL C 1 1018 ? 5.090    53.964  89.904  1.00 88.25  ? 1018 VAL B CB  1 
ATOM   22062 C  CG1 . VAL C 1 1018 ? 5.888    55.261  89.784  1.00 89.90  ? 1018 VAL B CG1 1 
ATOM   22063 C  CG2 . VAL C 1 1018 ? 5.166    53.164  88.606  1.00 91.07  ? 1018 VAL B CG2 1 
ATOM   22064 N  N   . PHE C 1 1019 ? 4.142    53.846  92.861  1.00 85.88  ? 1019 PHE B N   1 
ATOM   22065 C  CA  . PHE C 1 1019 ? 3.856    54.550  94.107  1.00 85.41  ? 1019 PHE B CA  1 
ATOM   22066 C  C   . PHE C 1 1019 ? 4.775    54.104  95.233  1.00 82.12  ? 1019 PHE B C   1 
ATOM   22067 O  O   . PHE C 1 1019 ? 5.417    54.940  95.873  1.00 83.11  ? 1019 PHE B O   1 
ATOM   22068 C  CB  . PHE C 1 1019 ? 2.427    54.375  94.602  1.00 84.45  ? 1019 PHE B CB  1 
ATOM   22069 C  CG  . PHE C 1 1019 ? 2.272    54.790  96.032  1.00 82.32  ? 1019 PHE B CG  1 
ATOM   22070 C  CD1 . PHE C 1 1019 ? 2.674    56.066  96.435  1.00 81.11  ? 1019 PHE B CD1 1 
ATOM   22071 C  CD2 . PHE C 1 1019 ? 1.789    53.911  96.978  1.00 80.46  ? 1019 PHE B CD2 1 
ATOM   22072 C  CE1 . PHE C 1 1019 ? 2.557    56.471  97.744  1.00 80.17  ? 1019 PHE B CE1 1 
ATOM   22073 C  CE2 . PHE C 1 1019 ? 1.672    54.304  98.298  1.00 79.79  ? 1019 PHE B CE2 1 
ATOM   22074 C  CZ  . PHE C 1 1019 ? 2.055    55.588  98.685  1.00 79.90  ? 1019 PHE B CZ  1 
ATOM   22075 N  N   . TYR C 1 1020 ? 4.812    52.801  95.499  1.00 77.23  ? 1020 TYR B N   1 
ATOM   22076 C  CA  . TYR C 1 1020 ? 5.672    52.316  96.551  1.00 73.57  ? 1020 TYR B CA  1 
ATOM   22077 C  C   . TYR C 1 1020 ? 7.135    52.666  96.277  1.00 71.42  ? 1020 TYR B C   1 
ATOM   22078 O  O   . TYR C 1 1020 ? 7.829    53.161  97.162  1.00 71.63  ? 1020 TYR B O   1 
ATOM   22079 C  CB  . TYR C 1 1020 ? 5.412    50.835  96.828  1.00 74.88  ? 1020 TYR B CB  1 
ATOM   22080 C  CG  . TYR C 1 1020 ? 4.097    50.657  97.517  1.00 77.47  ? 1020 TYR B CG  1 
ATOM   22081 C  CD1 . TYR C 1 1020 ? 3.794    51.394  98.646  1.00 79.72  ? 1020 TYR B CD1 1 
ATOM   22082 C  CD2 . TYR C 1 1020 ? 3.139    49.802  97.017  1.00 80.73  ? 1020 TYR B CD2 1 
ATOM   22083 C  CE1 . TYR C 1 1020 ? 2.578    51.271  99.275  1.00 82.73  ? 1020 TYR B CE1 1 
ATOM   22084 C  CE2 . TYR C 1 1020 ? 1.910    49.665  97.629  1.00 83.20  ? 1020 TYR B CE2 1 
ATOM   22085 C  CZ  . TYR C 1 1020 ? 1.632    50.406  98.759  1.00 85.57  ? 1020 TYR B CZ  1 
ATOM   22086 O  OH  . TYR C 1 1020 ? 0.409    50.274  99.382  1.00 88.34  ? 1020 TYR B OH  1 
ATOM   22087 N  N   . VAL C 1 1021 ? 7.597    52.463  95.051  1.00 69.85  ? 1021 VAL B N   1 
ATOM   22088 C  CA  . VAL C 1 1021 ? 8.972    52.835  94.742  1.00 70.12  ? 1021 VAL B CA  1 
ATOM   22089 C  C   . VAL C 1 1021 ? 9.191    54.316  94.982  1.00 69.96  ? 1021 VAL B C   1 
ATOM   22090 O  O   . VAL C 1 1021 ? 10.139   54.719  95.622  1.00 69.15  ? 1021 VAL B O   1 
ATOM   22091 C  CB  . VAL C 1 1021 ? 9.418    52.411  93.308  1.00 61.92  ? 1021 VAL B CB  1 
ATOM   22092 C  CG1 . VAL C 1 1021 ? 10.529   53.319  92.769  1.00 61.44  ? 1021 VAL B CG1 1 
ATOM   22093 C  CG2 . VAL C 1 1021 ? 9.882    50.974  93.312  1.00 61.55  ? 1021 VAL B CG2 1 
ATOM   22094 N  N   . PHE C 1 1022 ? 8.293    55.144  94.498  1.00 73.22  ? 1022 PHE B N   1 
ATOM   22095 C  CA  . PHE C 1 1022 ? 8.484    56.567  94.697  1.00 78.49  ? 1022 PHE B CA  1 
ATOM   22096 C  C   . PHE C 1 1022 ? 8.402    56.938  96.170  1.00 80.98  ? 1022 PHE B C   1 
ATOM   22097 O  O   . PHE C 1 1022 ? 9.024    57.913  96.604  1.00 84.39  ? 1022 PHE B O   1 
ATOM   22098 C  CB  . PHE C 1 1022 ? 7.473    57.390  93.898  1.00 80.25  ? 1022 PHE B CB  1 
ATOM   22099 C  CG  . PHE C 1 1022 ? 7.780    58.851  93.890  1.00 79.74  ? 1022 PHE B CG  1 
ATOM   22100 C  CD1 . PHE C 1 1022 ? 8.546    59.400  92.889  1.00 79.76  ? 1022 PHE B CD1 1 
ATOM   22101 C  CD2 . PHE C 1 1022 ? 7.328    59.664  94.909  1.00 79.19  ? 1022 PHE B CD2 1 
ATOM   22102 C  CE1 . PHE C 1 1022 ? 8.836    60.731  92.901  1.00 81.63  ? 1022 PHE B CE1 1 
ATOM   22103 C  CE2 . PHE C 1 1022 ? 7.624    60.988  94.922  1.00 80.65  ? 1022 PHE B CE2 1 
ATOM   22104 C  CZ  . PHE C 1 1022 ? 8.383    61.523  93.916  1.00 81.82  ? 1022 PHE B CZ  1 
ATOM   22105 N  N   . HIS C 1 1023 ? 7.631    56.171  96.937  1.00 79.94  ? 1023 HIS B N   1 
ATOM   22106 C  CA  . HIS C 1 1023 ? 7.495    56.423  98.376  1.00 77.67  ? 1023 HIS B CA  1 
ATOM   22107 C  C   . HIS C 1 1023 ? 8.743    56.032  99.145  1.00 74.23  ? 1023 HIS B C   1 
ATOM   22108 O  O   . HIS C 1 1023 ? 9.252    56.809  99.945  1.00 75.44  ? 1023 HIS B O   1 
ATOM   22109 C  CB  . HIS C 1 1023 ? 6.318    55.655  98.938  1.00 78.44  ? 1023 HIS B CB  1 
ATOM   22110 C  CG  . HIS C 1 1023 ? 6.102    55.885  100.391 1.00 79.68  ? 1023 HIS B CG  1 
ATOM   22111 N  ND1 . HIS C 1 1023 ? 6.034    54.858  101.307 1.00 81.39  ? 1023 HIS B ND1 1 
ATOM   22112 C  CD2 . HIS C 1 1023 ? 5.957    57.031  101.093 1.00 80.97  ? 1023 HIS B CD2 1 
ATOM   22113 C  CE1 . HIS C 1 1023 ? 5.845    55.362  102.513 1.00 81.89  ? 1023 HIS B CE1 1 
ATOM   22114 N  NE2 . HIS C 1 1023 ? 5.794    56.679  102.409 1.00 82.43  ? 1023 HIS B NE2 1 
ATOM   22115 N  N   . TYR C 1 1024 ? 9.234    54.827  98.899  1.00 70.19  ? 1024 TYR B N   1 
ATOM   22116 C  CA  . TYR C 1 1024 ? 10.524   54.439  99.420  1.00 69.85  ? 1024 TYR B CA  1 
ATOM   22117 C  C   . TYR C 1 1024 ? 11.671   55.302  98.910  1.00 71.69  ? 1024 TYR B C   1 
ATOM   22118 O  O   . TYR C 1 1024 ? 12.653   55.494  99.595  1.00 72.39  ? 1024 TYR B O   1 
ATOM   22119 C  CB  . TYR C 1 1024 ? 10.804   52.998  99.075  1.00 71.79  ? 1024 TYR B CB  1 
ATOM   22120 C  CG  . TYR C 1 1024 ? 12.263   52.658  99.171  1.00 76.24  ? 1024 TYR B CG  1 
ATOM   22121 C  CD1 . TYR C 1 1024 ? 12.735   51.877  100.211 1.00 79.43  ? 1024 TYR B CD1 1 
ATOM   22122 C  CD2 . TYR C 1 1024 ? 13.171   53.109  98.223  1.00 78.20  ? 1024 TYR B CD2 1 
ATOM   22123 C  CE1 . TYR C 1 1024 ? 14.063   51.555  100.312 1.00 83.12  ? 1024 TYR B CE1 1 
ATOM   22124 C  CE2 . TYR C 1 1024 ? 14.491   52.796  98.310  1.00 82.12  ? 1024 TYR B CE2 1 
ATOM   22125 C  CZ  . TYR C 1 1024 ? 14.937   52.014  99.357  1.00 86.42  ? 1024 TYR B CZ  1 
ATOM   22126 O  OH  . TYR C 1 1024 ? 16.271   51.683  99.460  1.00 92.70  ? 1024 TYR B OH  1 
ATOM   22127 N  N   . LEU C 1 1025 ? 11.575   55.790  97.685  1.00 75.02  ? 1025 LEU B N   1 
ATOM   22128 C  CA  . LEU C 1 1025 ? 12.682   56.559  97.117  1.00 78.06  ? 1025 LEU B CA  1 
ATOM   22129 C  C   . LEU C 1 1025 ? 12.785   57.913  97.773  1.00 78.04  ? 1025 LEU B C   1 
ATOM   22130 O  O   . LEU C 1 1025 ? 13.865   58.404  98.052  1.00 76.14  ? 1025 LEU B O   1 
ATOM   22131 C  CB  . LEU C 1 1025 ? 12.499   56.759  95.613  1.00 79.55  ? 1025 LEU B CB  1 
ATOM   22132 C  CG  . LEU C 1 1025 ? 13.216   55.807  94.671  1.00 79.09  ? 1025 LEU B CG  1 
ATOM   22133 C  CD1 . LEU C 1 1025 ? 13.078   56.363  93.275  1.00 79.83  ? 1025 LEU B CD1 1 
ATOM   22134 C  CD2 . LEU C 1 1025 ? 14.685   55.628  95.049  1.00 79.76  ? 1025 LEU B CD2 1 
ATOM   22135 N  N   . GLU C 1 1026 ? 11.625   58.506  97.991  1.00 81.78  ? 1026 GLU B N   1 
ATOM   22136 C  CA  . GLU C 1 1026 ? 11.513   59.876  98.434  1.00 88.68  ? 1026 GLU B CA  1 
ATOM   22137 C  C   . GLU C 1 1026 ? 11.479   59.928  99.949  1.00 93.26  ? 1026 GLU B C   1 
ATOM   22138 O  O   . GLU C 1 1026 ? 12.203   60.712  100.594 1.00 98.37  ? 1026 GLU B O   1 
ATOM   22139 C  CB  . GLU C 1 1026 ? 10.227   60.490  97.892  1.00 91.12  ? 1026 GLU B CB  1 
ATOM   22140 C  CG  . GLU C 1 1026 ? 9.872    61.818  98.534  1.00 95.96  ? 1026 GLU B CG  1 
ATOM   22141 C  CD  . GLU C 1 1026 ? 10.658   62.988  97.949  1.00 100.79 ? 1026 GLU B CD  1 
ATOM   22142 O  OE1 . GLU C 1 1026 ? 11.443   62.735  97.002  1.00 102.37 ? 1026 GLU B OE1 1 
ATOM   22143 O  OE2 . GLU C 1 1026 ? 10.477   64.147  98.422  1.00 102.09 ? 1026 GLU B OE2 1 
ATOM   22144 N  N   . THR C 1 1027 ? 10.642   59.100  100.544 1.00 90.47  ? 1027 THR B N   1 
ATOM   22145 C  CA  . THR C 1 1027 ? 10.482   59.241  101.962 1.00 88.49  ? 1027 THR B CA  1 
ATOM   22146 C  C   . THR C 1 1027 ? 11.613   58.643  102.752 1.00 89.97  ? 1027 THR B C   1 
ATOM   22147 O  O   . THR C 1 1027 ? 11.628   58.730  103.957 1.00 92.37  ? 1027 THR B O   1 
ATOM   22148 C  CB  . THR C 1 1027 ? 9.153    58.737  102.417 1.00 87.12  ? 1027 THR B CB  1 
ATOM   22149 O  OG1 . THR C 1 1027 ? 8.251    59.842  102.478 1.00 87.39  ? 1027 THR B OG1 1 
ATOM   22150 C  CG2 . THR C 1 1027 ? 9.273    58.168  103.797 1.00 85.81  ? 1027 THR B CG2 1 
ATOM   22151 N  N   . GLY C 1 1028 ? 12.588   58.062  102.084 1.00 91.70  ? 1028 GLY B N   1 
ATOM   22152 C  CA  . GLY C 1 1028 ? 13.768   57.614  102.795 1.00 95.09  ? 1028 GLY B CA  1 
ATOM   22153 C  C   . GLY C 1 1028 ? 14.994   58.204  102.131 1.00 99.56  ? 1028 GLY B C   1 
ATOM   22154 O  O   . GLY C 1 1028 ? 16.045   57.578  102.074 1.00 98.21  ? 1028 GLY B O   1 
ATOM   22155 N  N   . ASN C 1 1029 ? 14.859   59.425  101.633 1.00 105.00 ? 1029 ASN B N   1 
ATOM   22156 C  CA  . ASN C 1 1029 ? 15.750   59.897  100.581 1.00 112.28 ? 1029 ASN B CA  1 
ATOM   22157 C  C   . ASN C 1 1029 ? 16.810   58.858  100.186 1.00 109.75 ? 1029 ASN B C   1 
ATOM   22158 O  O   . ASN C 1 1029 ? 17.735   58.535  100.928 1.00 107.55 ? 1029 ASN B O   1 
ATOM   22159 C  CB  . ASN C 1 1029 ? 16.340   61.285  100.872 1.00 122.21 ? 1029 ASN B CB  1 
ATOM   22160 C  CG  . ASN C 1 1029 ? 17.626   61.220  101.667 1.00 131.73 ? 1029 ASN B CG  1 
ATOM   22161 O  OD1 . ASN C 1 1029 ? 18.617   61.881  101.324 1.00 136.53 ? 1029 ASN B OD1 1 
ATOM   22162 N  ND2 . ASN C 1 1029 ? 17.624   60.425  102.743 1.00 133.45 ? 1029 ASN B ND2 1 
ATOM   22163 N  N   . HIS C 1 1030 ? 16.616   58.325  98.988  1.00 110.79 ? 1030 HIS B N   1 
ATOM   22164 C  CA  . HIS C 1 1030 ? 17.512   57.348  98.390  1.00 110.22 ? 1030 HIS B CA  1 
ATOM   22165 C  C   . HIS C 1 1030 ? 17.765   57.723  96.913  1.00 108.95 ? 1030 HIS B C   1 
ATOM   22166 O  O   . HIS C 1 1030 ? 18.415   56.993  96.152  1.00 107.63 ? 1030 HIS B O   1 
ATOM   22167 C  CB  . HIS C 1 1030 ? 16.931   55.930  98.528  1.00 107.44 ? 1030 HIS B CB  1 
ATOM   22168 C  CG  . HIS C 1 1030 ? 16.896   55.430  99.938  1.00 104.46 ? 1030 HIS B CG  1 
ATOM   22169 N  ND1 . HIS C 1 1030 ? 18.036   55.261  100.691 1.00 103.69 ? 1030 HIS B ND1 1 
ATOM   22170 C  CD2 . HIS C 1 1030 ? 15.861   55.059  100.730 1.00 102.03 ? 1030 HIS B CD2 1 
ATOM   22171 C  CE1 . HIS C 1 1030 ? 17.703   54.811  101.888 1.00 102.59 ? 1030 HIS B CE1 1 
ATOM   22172 N  NE2 . HIS C 1 1030 ? 16.390   54.675  101.936 1.00 100.91 ? 1030 HIS B NE2 1 
ATOM   22173 N  N   . TRP C 1 1031 ? 17.253   58.887  96.533  1.00 106.82 ? 1031 TRP B N   1 
ATOM   22174 C  CA  . TRP C 1 1031 ? 17.403   59.392  95.187  1.00 104.50 ? 1031 TRP B CA  1 
ATOM   22175 C  C   . TRP C 1 1031 ? 18.847   59.367  94.720  1.00 106.65 ? 1031 TRP B C   1 
ATOM   22176 O  O   . TRP C 1 1031 ? 19.135   59.503  93.524  1.00 110.16 ? 1031 TRP B O   1 
ATOM   22177 C  CB  . TRP C 1 1031 ? 16.876   60.813  95.114  1.00 102.60 ? 1031 TRP B CB  1 
ATOM   22178 C  CG  . TRP C 1 1031 ? 15.418   60.900  95.218  1.00 98.80  ? 1031 TRP B CG  1 
ATOM   22179 C  CD1 . TRP C 1 1031 ? 14.695   61.491  96.207  1.00 98.06  ? 1031 TRP B CD1 1 
ATOM   22180 C  CD2 . TRP C 1 1031 ? 14.487   60.370  94.299  1.00 97.57  ? 1031 TRP B CD2 1 
ATOM   22181 N  NE1 . TRP C 1 1031 ? 13.357   61.367  95.953  1.00 96.90  ? 1031 TRP B NE1 1 
ATOM   22182 C  CE2 . TRP C 1 1031 ? 13.204   60.681  94.781  1.00 97.83  ? 1031 TRP B CE2 1 
ATOM   22183 C  CE3 . TRP C 1 1031 ? 14.610   59.664  93.103  1.00 98.49  ? 1031 TRP B CE3 1 
ATOM   22184 C  CZ2 . TRP C 1 1031 ? 12.057   60.306  94.115  1.00 99.70  ? 1031 TRP B CZ2 1 
ATOM   22185 C  CZ3 . TRP C 1 1031 ? 13.476   59.296  92.442  1.00 99.63  ? 1031 TRP B CZ3 1 
ATOM   22186 C  CH2 . TRP C 1 1031 ? 12.211   59.611  92.946  1.00 100.55 ? 1031 TRP B CH2 1 
ATOM   22187 N  N   . ASN C 1 1032 ? 19.766   59.207  95.653  1.00 104.82 ? 1032 ASN B N   1 
ATOM   22188 C  CA  . ASN C 1 1032 ? 21.159   59.179  95.269  1.00 107.39 ? 1032 ASN B CA  1 
ATOM   22189 C  C   . ASN C 1 1032 ? 21.553   57.800  94.789  1.00 103.90 ? 1032 ASN B C   1 
ATOM   22190 O  O   . ASN C 1 1032 ? 22.740   57.523  94.627  1.00 104.48 ? 1032 ASN B O   1 
ATOM   22191 C  CB  . ASN C 1 1032 ? 22.014   59.526  96.456  1.00 109.89 ? 1032 ASN B CB  1 
ATOM   22192 C  CG  . ASN C 1 1032 ? 21.824   58.555  97.555  1.00 108.46 ? 1032 ASN B CG  1 
ATOM   22193 O  OD1 . ASN C 1 1032 ? 20.737   58.469  98.130  1.00 106.09 ? 1032 ASN B OD1 1 
ATOM   22194 N  ND2 . ASN C 1 1032 ? 22.860   57.778  97.843  1.00 109.87 ? 1032 ASN B ND2 1 
ATOM   22195 N  N   . ILE C 1 1033 ? 20.571   56.923  94.593  1.00 100.81 ? 1033 ILE B N   1 
ATOM   22196 C  CA  . ILE C 1 1033 ? 20.874   55.626  94.010  1.00 100.40 ? 1033 ILE B CA  1 
ATOM   22197 C  C   . ILE C 1 1033 ? 21.473   55.886  92.657  1.00 103.72 ? 1033 ILE B C   1 
ATOM   22198 O  O   . ILE C 1 1033 ? 22.344   55.131  92.202  1.00 104.75 ? 1033 ILE B O   1 
ATOM   22199 C  CB  . ILE C 1 1033 ? 19.654   54.781  93.681  1.00 97.13  ? 1033 ILE B CB  1 
ATOM   22200 C  CG1 . ILE C 1 1033 ? 18.887   54.358  94.918  1.00 95.08  ? 1033 ILE B CG1 1 
ATOM   22201 C  CG2 . ILE C 1 1033 ? 20.107   53.526  92.952  1.00 96.92  ? 1033 ILE B CG2 1 
ATOM   22202 C  CD1 . ILE C 1 1033 ? 17.855   53.300  94.593  1.00 93.85  ? 1033 ILE B CD1 1 
ATOM   22203 N  N   . PHE C 1 1034 ? 20.972   56.956  92.026  1.00 105.36 ? 1034 PHE B N   1 
ATOM   22204 C  CA  . PHE C 1 1034 ? 21.140   57.195  90.598  1.00 107.63 ? 1034 PHE B CA  1 
ATOM   22205 C  C   . PHE C 1 1034 ? 22.464   57.791  90.235  1.00 115.75 ? 1034 PHE B C   1 
ATOM   22206 O  O   . PHE C 1 1034 ? 22.857   58.834  90.736  1.00 117.25 ? 1034 PHE B O   1 
ATOM   22207 C  CB  . PHE C 1 1034 ? 20.016   58.070  90.057  1.00 102.05 ? 1034 PHE B CB  1 
ATOM   22208 C  CG  . PHE C 1 1034 ? 18.663   57.493  90.275  1.00 95.68  ? 1034 PHE B CG  1 
ATOM   22209 C  CD1 . PHE C 1 1034 ? 18.261   56.362  89.595  1.00 93.01  ? 1034 PHE B CD1 1 
ATOM   22210 C  CD2 . PHE C 1 1034 ? 17.794   58.066  91.175  1.00 91.76  ? 1034 PHE B CD2 1 
ATOM   22211 C  CE1 . PHE C 1 1034 ? 17.014   55.817  89.818  1.00 89.73  ? 1034 PHE B CE1 1 
ATOM   22212 C  CE2 . PHE C 1 1034 ? 16.542   57.525  91.392  1.00 88.10  ? 1034 PHE B CE2 1 
ATOM   22213 C  CZ  . PHE C 1 1034 ? 16.158   56.401  90.725  1.00 87.23  ? 1034 PHE B CZ  1 
ATOM   22214 N  N   . HIS C 1 1035 ? 23.151   57.111  89.346  1.00 123.18 ? 1035 HIS B N   1 
ATOM   22215 C  CA  . HIS C 1 1035 ? 24.412   57.605  88.900  1.00 136.40 ? 1035 HIS B CA  1 
ATOM   22216 C  C   . HIS C 1 1035 ? 24.066   58.803  88.059  1.00 140.51 ? 1035 HIS B C   1 
ATOM   22217 O  O   . HIS C 1 1035 ? 24.805   59.794  88.051  1.00 145.29 ? 1035 HIS B O   1 
ATOM   22218 C  CB  . HIS C 1 1035 ? 25.103   56.513  88.113  1.00 145.54 ? 1035 HIS B CB  1 
ATOM   22219 C  CG  . HIS C 1 1035 ? 25.136   55.211  88.849  1.00 151.73 ? 1035 HIS B CG  1 
ATOM   22220 N  ND1 . HIS C 1 1035 ? 26.300   54.649  89.330  1.00 156.18 ? 1035 HIS B ND1 1 
ATOM   22221 C  CD2 . HIS C 1 1035 ? 24.134   54.386  89.240  1.00 152.86 ? 1035 HIS B CD2 1 
ATOM   22222 C  CE1 . HIS C 1 1035 ? 26.018   53.523  89.962  1.00 155.68 ? 1035 HIS B CE1 1 
ATOM   22223 N  NE2 . HIS C 1 1035 ? 24.710   53.341  89.924  1.00 153.92 ? 1035 HIS B NE2 1 
ATOM   22224 N  N   . SER C 1 1036 ? 22.907   58.718  87.398  1.00 139.87 ? 1036 SER B N   1 
ATOM   22225 C  CA  . SER C 1 1036 ? 22.402   59.780  86.516  1.00 140.78 ? 1036 SER B CA  1 
ATOM   22226 C  C   . SER C 1 1036 ? 21.898   61.005  87.280  1.00 138.79 ? 1036 SER B C   1 
ATOM   22227 O  O   . SER C 1 1036 ? 22.192   61.191  88.464  1.00 137.98 ? 1036 SER B O   1 
ATOM   22228 C  CB  . SER C 1 1036 ? 21.266   59.255  85.641  1.00 141.46 ? 1036 SER B CB  1 
ATOM   22229 O  OG  . SER C 1 1036 ? 20.084   59.096  86.412  1.00 140.69 ? 1036 SER B OG  1 
ATOM   22230 N  N   . ASP C 1 1037 ? 21.148   61.857  86.592  1.00 137.73 ? 1037 ASP B N   1 
ATOM   22231 C  CA  . ASP C 1 1037 ? 20.552   62.991  87.268  1.00 134.25 ? 1037 ASP B CA  1 
ATOM   22232 C  C   . ASP C 1 1037 ? 19.299   62.528  87.957  1.00 125.05 ? 1037 ASP B C   1 
ATOM   22233 O  O   . ASP C 1 1037 ? 18.383   62.042  87.318  1.00 124.10 ? 1037 ASP B O   1 
ATOM   22234 C  CB  . ASP C 1 1037 ? 20.218   64.106  86.291  1.00 138.57 ? 1037 ASP B CB  1 
ATOM   22235 C  CG  . ASP C 1 1037 ? 19.512   65.259  86.961  1.00 136.63 ? 1037 ASP B CG  1 
ATOM   22236 O  OD1 . ASP C 1 1037 ? 18.996   65.059  88.086  1.00 131.48 ? 1037 ASP B OD1 1 
ATOM   22237 O  OD2 . ASP C 1 1037 ? 19.481   66.356  86.354  1.00 139.31 ? 1037 ASP B OD2 1 
ATOM   22238 N  N   . PRO C 1 1038 ? 19.252   62.691  89.271  1.00 118.83 ? 1038 PRO B N   1 
ATOM   22239 C  CA  . PRO C 1 1038 ? 18.185   62.172  90.127  1.00 114.11 ? 1038 PRO B CA  1 
ATOM   22240 C  C   . PRO C 1 1038 ? 16.933   63.007  90.026  1.00 112.16 ? 1038 PRO B C   1 
ATOM   22241 O  O   . PRO C 1 1038 ? 15.818   62.494  90.121  1.00 110.97 ? 1038 PRO B O   1 
ATOM   22242 C  CB  . PRO C 1 1038 ? 18.762   62.323  91.540  1.00 114.73 ? 1038 PRO B CB  1 
ATOM   22243 C  CG  . PRO C 1 1038 ? 20.227   62.581  91.354  1.00 118.06 ? 1038 PRO B CG  1 
ATOM   22244 C  CD  . PRO C 1 1038 ? 20.324   63.312  90.053  1.00 120.28 ? 1038 PRO B CD  1 
ATOM   22245 N  N   . LEU C 1 1039 ? 17.123   64.304  89.844  1.00 111.64 ? 1039 LEU B N   1 
ATOM   22246 C  CA  . LEU C 1 1039 ? 16.006   65.241  89.845  1.00 109.65 ? 1039 LEU B CA  1 
ATOM   22247 C  C   . LEU C 1 1039 ? 15.038   64.957  88.694  1.00 105.31 ? 1039 LEU B C   1 
ATOM   22248 O  O   . LEU C 1 1039 ? 13.820   65.200  88.799  1.00 101.51 ? 1039 LEU B O   1 
ATOM   22249 C  CB  . LEU C 1 1039 ? 16.540   66.674  89.777  1.00 113.15 ? 1039 LEU B CB  1 
ATOM   22250 C  CG  . LEU C 1 1039 ? 15.545   67.769  90.126  1.00 114.37 ? 1039 LEU B CG  1 
ATOM   22251 C  CD1 . LEU C 1 1039 ? 14.554   67.282  91.190  1.00 111.44 ? 1039 LEU B CD1 1 
ATOM   22252 C  CD2 . LEU C 1 1039 ? 16.304   69.022  90.568  1.00 117.10 ? 1039 LEU B CD2 1 
ATOM   22253 N  N   . ILE C 1 1040 ? 15.611   64.438  87.608  1.00 103.94 ? 1040 ILE B N   1 
ATOM   22254 C  CA  . ILE C 1 1040 ? 14.885   64.135  86.385  1.00 102.80 ? 1040 ILE B CA  1 
ATOM   22255 C  C   . ILE C 1 1040 ? 14.389   62.695  86.364  1.00 101.81 ? 1040 ILE B C   1 
ATOM   22256 O  O   . ILE C 1 1040 ? 13.407   62.380  85.703  1.00 101.42 ? 1040 ILE B O   1 
ATOM   22257 C  CB  . ILE C 1 1040 ? 15.767   64.402  85.143  1.00 102.00 ? 1040 ILE B CB  1 
ATOM   22258 C  CG1 . ILE C 1 1040 ? 15.062   65.368  84.168  1.00 105.23 ? 1040 ILE B CG1 1 
ATOM   22259 C  CG2 . ILE C 1 1040 ? 16.222   63.092  84.493  1.00 98.96  ? 1040 ILE B CG2 1 
ATOM   22260 C  CD1 . ILE C 1 1040 ? 13.495   65.522  84.337  1.00 123.60 ? 1040 ILE B CD1 1 
ATOM   22261 N  N   . GLU C 1 1041 ? 15.085   61.826  87.085  1.00 102.81 ? 1041 GLU B N   1 
ATOM   22262 C  CA  . GLU C 1 1041 ? 14.626   60.469  87.289  1.00 104.42 ? 1041 GLU B CA  1 
ATOM   22263 C  C   . GLU C 1 1041 ? 13.398   60.522  88.163  1.00 104.03 ? 1041 GLU B C   1 
ATOM   22264 O  O   . GLU C 1 1041 ? 12.605   59.576  88.183  1.00 100.94 ? 1041 GLU B O   1 
ATOM   22265 C  CB  . GLU C 1 1041 ? 15.670   59.660  88.028  1.00 107.53 ? 1041 GLU B CB  1 
ATOM   22266 C  CG  . GLU C 1 1041 ? 15.596   58.219  87.707  1.00 111.80 ? 1041 GLU B CG  1 
ATOM   22267 C  CD  . GLU C 1 1041 ? 16.285   57.965  86.411  1.00 119.96 ? 1041 GLU B CD  1 
ATOM   22268 O  OE1 . GLU C 1 1041 ? 17.320   58.621  86.175  1.00 121.78 ? 1041 GLU B OE1 1 
ATOM   22269 O  OE2 . GLU C 1 1041 ? 15.791   57.142  85.612  1.00 124.51 ? 1041 GLU B OE2 1 
ATOM   22270 N  N   . LYS C 1 1042 ? 13.277   61.616  88.917  1.00 108.56 ? 1042 LYS B N   1 
ATOM   22271 C  CA  . LYS C 1 1042 ? 12.139   61.848  89.783  1.00 111.43 ? 1042 LYS B CA  1 
ATOM   22272 C  C   . LYS C 1 1042 ? 10.956   62.409  89.007  1.00 117.25 ? 1042 LYS B C   1 
ATOM   22273 O  O   . LYS C 1 1042 ? 9.807    62.081  89.308  1.00 117.01 ? 1042 LYS B O   1 
ATOM   22274 C  CB  . LYS C 1 1042 ? 12.495   62.811  90.900  1.00 114.16 ? 1042 LYS B CB  1 
ATOM   22275 C  CG  . LYS C 1 1042 ? 11.245   63.325  91.607  1.00 117.41 ? 1042 LYS B CG  1 
ATOM   22276 C  CD  . LYS C 1 1042 ? 11.505   64.480  92.573  1.00 121.35 ? 1042 LYS B CD  1 
ATOM   22277 C  CE  . LYS C 1 1042 ? 11.606   64.024  94.030  1.00 119.98 ? 1042 LYS B CE  1 
ATOM   22278 N  NZ  . LYS C 1 1042 ? 11.614   65.203  94.946  1.00 121.34 ? 1042 LYS B NZ  1 
ATOM   22279 N  N   . GLN C 1 1043 ? 11.229   63.269  88.024  1.00 122.47 ? 1043 GLN B N   1 
ATOM   22280 C  CA  . GLN C 1 1043 ? 10.166   63.764  87.141  1.00 124.40 ? 1043 GLN B CA  1 
ATOM   22281 C  C   . GLN C 1 1043 ? 9.447    62.581  86.543  1.00 119.29 ? 1043 GLN B C   1 
ATOM   22282 O  O   . GLN C 1 1043 ? 8.217    62.500  86.570  1.00 117.25 ? 1043 GLN B O   1 
ATOM   22283 C  CB  . GLN C 1 1043 ? 10.713   64.659  86.008  1.00 132.70 ? 1043 GLN B CB  1 
ATOM   22284 C  CG  . GLN C 1 1043 ? 10.789   66.122  86.391  1.00 139.43 ? 1043 GLN B CG  1 
ATOM   22285 C  CD  . GLN C 1 1043 ? 9.991    66.385  87.670  1.00 142.64 ? 1043 GLN B CD  1 
ATOM   22286 O  OE1 . GLN C 1 1043 ? 8.753    66.373  87.651  1.00 142.86 ? 1043 GLN B OE1 1 
ATOM   22287 N  NE2 . GLN C 1 1043 ? 10.700   66.586  88.797  1.00 143.26 ? 1043 GLN B NE2 1 
ATOM   22288 N  N   . LYS C 1 1044 ? 10.251   61.665  86.010  1.00 115.67 ? 1044 LYS B N   1 
ATOM   22289 C  CA  . LYS C 1 1044 ? 9.766    60.483  85.312  1.00 112.43 ? 1044 LYS B CA  1 
ATOM   22290 C  C   . LYS C 1 1044 ? 8.747    59.752  86.166  1.00 109.23 ? 1044 LYS B C   1 
ATOM   22291 O  O   . LYS C 1 1044 ? 7.688    59.378  85.683  1.00 110.01 ? 1044 LYS B O   1 
ATOM   22292 C  CB  . LYS C 1 1044 ? 10.929   59.532  84.945  1.00 111.87 ? 1044 LYS B CB  1 
ATOM   22293 C  CG  . LYS C 1 1044 ? 11.687   59.855  83.625  1.00 147.40 ? 1044 LYS B CG  1 
ATOM   22294 C  CD  . LYS C 1 1044 ? 13.038   59.090  83.480  1.00 144.04 ? 1044 LYS B CD  1 
ATOM   22295 C  CE  . LYS C 1 1044 ? 12.865   57.633  83.016  1.00 142.79 ? 1044 LYS B CE  1 
ATOM   22296 N  NZ  . LYS C 1 1044 ? 14.154   56.867  82.908  1.00 142.34 ? 1044 LYS B NZ  1 
ATOM   22297 N  N   . LEU C 1 1045 ? 9.061    59.557  87.440  1.00 105.51 ? 1045 LEU B N   1 
ATOM   22298 C  CA  . LEU C 1 1045 ? 8.200    58.759  88.301  1.00 100.69 ? 1045 LEU B CA  1 
ATOM   22299 C  C   . LEU C 1 1045 ? 6.942    59.495  88.694  1.00 98.56  ? 1045 LEU B C   1 
ATOM   22300 O  O   . LEU C 1 1045 ? 5.881    58.896  88.798  1.00 96.40  ? 1045 LEU B O   1 
ATOM   22301 C  CB  . LEU C 1 1045 ? 8.952    58.250  89.517  1.00 96.46  ? 1045 LEU B CB  1 
ATOM   22302 C  CG  . LEU C 1 1045 ? 10.134   57.389  89.112  1.00 93.29  ? 1045 LEU B CG  1 
ATOM   22303 C  CD1 . LEU C 1 1045 ? 10.705   56.810  90.360  1.00 93.27  ? 1045 LEU B CD1 1 
ATOM   22304 C  CD2 . LEU C 1 1045 ? 9.721    56.291  88.157  1.00 90.42  ? 1045 LEU B CD2 1 
ATOM   22305 N  N   . LYS C 1 1046 ? 7.051    60.795  88.916  1.00 101.56 ? 1046 LYS B N   1 
ATOM   22306 C  CA  . LYS C 1 1046 ? 5.849    61.563  89.157  1.00 105.27 ? 1046 LYS B CA  1 
ATOM   22307 C  C   . LYS C 1 1046 ? 4.928    61.265  87.983  1.00 109.48 ? 1046 LYS B C   1 
ATOM   22308 O  O   . LYS C 1 1046 ? 3.770    60.895  88.170  1.00 111.14 ? 1046 LYS B O   1 
ATOM   22309 C  CB  . LYS C 1 1046 ? 6.136    63.056  89.217  1.00 107.29 ? 1046 LYS B CB  1 
ATOM   22310 C  CG  . LYS C 1 1046 ? 7.019    63.521  90.345  1.00 109.23 ? 1046 LYS B CG  1 
ATOM   22311 C  CD  . LYS C 1 1046 ? 6.761    65.007  90.564  1.00 115.14 ? 1046 LYS B CD  1 
ATOM   22312 C  CE  . LYS C 1 1046 ? 7.906    65.732  91.277  1.00 118.87 ? 1046 LYS B CE  1 
ATOM   22313 N  NZ  . LYS C 1 1046 ? 7.751    67.233  91.177  1.00 122.12 ? 1046 LYS B NZ  1 
ATOM   22314 N  N   . LYS C 1 1047 ? 5.466    61.407  86.771  1.00 111.29 ? 1047 LYS B N   1 
ATOM   22315 C  CA  . LYS C 1 1047 ? 4.724    61.154  85.538  1.00 111.69 ? 1047 LYS B CA  1 
ATOM   22316 C  C   . LYS C 1 1047 ? 4.080    59.792  85.554  1.00 103.66 ? 1047 LYS B C   1 
ATOM   22317 O  O   . LYS C 1 1047 ? 2.860    59.691  85.603  1.00 101.56 ? 1047 LYS B O   1 
ATOM   22318 C  CB  . LYS C 1 1047 ? 5.662    61.239  84.339  1.00 120.68 ? 1047 LYS B CB  1 
ATOM   22319 C  CG  . LYS C 1 1047 ? 5.003    61.104  82.971  1.00 129.83 ? 1047 LYS B CG  1 
ATOM   22320 C  CD  . LYS C 1 1047 ? 5.920    61.746  81.919  1.00 139.72 ? 1047 LYS B CD  1 
ATOM   22321 C  CE  . LYS C 1 1047 ? 5.278    61.843  80.538  1.00 146.76 ? 1047 LYS B CE  1 
ATOM   22322 N  NZ  . LYS C 1 1047 ? 4.832    60.505  80.045  1.00 148.83 ? 1047 LYS B NZ  1 
ATOM   22323 N  N   . LYS C 1 1048 ? 4.919    58.756  85.511  1.00 99.70  ? 1048 LYS B N   1 
ATOM   22324 C  CA  . LYS C 1 1048 ? 4.472    57.363  85.487  1.00 93.90  ? 1048 LYS B CA  1 
ATOM   22325 C  C   . LYS C 1 1048 ? 3.335    57.235  86.450  1.00 89.32  ? 1048 LYS B C   1 
ATOM   22326 O  O   . LYS C 1 1048 ? 2.356    56.544  86.199  1.00 87.73  ? 1048 LYS B O   1 
ATOM   22327 C  CB  . LYS C 1 1048 ? 5.585    56.419  85.936  1.00 90.70  ? 1048 LYS B CB  1 
ATOM   22328 C  CG  . LYS C 1 1048 ? 6.399    55.784  84.856  1.00 90.10  ? 1048 LYS B CG  1 
ATOM   22329 C  CD  . LYS C 1 1048 ? 6.724    54.382  85.313  1.00 90.03  ? 1048 LYS B CD  1 
ATOM   22330 C  CE  . LYS C 1 1048 ? 8.162    53.965  85.026  1.00 90.93  ? 1048 LYS B CE  1 
ATOM   22331 N  NZ  . LYS C 1 1048 ? 8.324    52.480  85.244  1.00 88.96  ? 1048 LYS B NZ  1 
ATOM   22332 N  N   . LEU C 1 1049 ? 3.486    57.941  87.558  1.00 87.58  ? 1049 LEU B N   1 
ATOM   22333 C  CA  . LEU C 1 1049 ? 2.521    57.917  88.628  1.00 86.03  ? 1049 LEU B CA  1 
ATOM   22334 C  C   . LEU C 1 1049 ? 1.224    58.602  88.220  1.00 90.17  ? 1049 LEU B C   1 
ATOM   22335 O  O   . LEU C 1 1049 ? 0.150    58.173  88.620  1.00 92.14  ? 1049 LEU B O   1 
ATOM   22336 C  CB  . LEU C 1 1049 ? 3.095    58.633  89.831  1.00 81.37  ? 1049 LEU B CB  1 
ATOM   22337 C  CG  . LEU C 1 1049 ? 2.632    58.047  91.137  1.00 75.43  ? 1049 LEU B CG  1 
ATOM   22338 C  CD1 . LEU C 1 1049 ? 3.354    56.741  91.366  1.00 70.65  ? 1049 LEU B CD1 1 
ATOM   22339 C  CD2 . LEU C 1 1049 ? 2.972    59.058  92.174  1.00 74.77  ? 1049 LEU B CD2 1 
ATOM   22340 N  N   . LYS C 1 1050 ? 1.314    59.668  87.438  1.00 90.94  ? 1050 LYS B N   1 
ATOM   22341 C  CA  . LYS C 1 1050 ? 0.117    60.365  87.036  1.00 92.58  ? 1050 LYS B CA  1 
ATOM   22342 C  C   . LYS C 1 1050 ? -0.556   59.635  85.895  1.00 96.72  ? 1050 LYS B C   1 
ATOM   22343 O  O   . LYS C 1 1050 ? -1.745   59.344  85.942  1.00 95.43  ? 1050 LYS B O   1 
ATOM   22344 C  CB  . LYS C 1 1050 ? 0.433    61.795  86.625  1.00 92.81  ? 1050 LYS B CB  1 
ATOM   22345 C  CG  . LYS C 1 1050 ? -0.827   62.594  86.474  1.00 92.97  ? 1050 LYS B CG  1 
ATOM   22346 C  CD  . LYS C 1 1050 ? -0.620   63.993  85.967  1.00 94.20  ? 1050 LYS B CD  1 
ATOM   22347 C  CE  . LYS C 1 1050 ? -2.000   64.521  85.610  1.00 96.75  ? 1050 LYS B CE  1 
ATOM   22348 N  NZ  . LYS C 1 1050 ? -2.264   65.912  86.046  1.00 99.95  ? 1050 LYS B NZ  1 
ATOM   22349 N  N   . GLU C 1 1051 ? 0.189    59.340  84.844  1.00 103.88 ? 1051 GLU B N   1 
ATOM   22350 C  CA  . GLU C 1 1051 ? -0.495   58.807  83.687  1.00 112.03 ? 1051 GLU B CA  1 
ATOM   22351 C  C   . GLU C 1 1051 ? -1.219   57.589  84.196  1.00 110.01 ? 1051 GLU B C   1 
ATOM   22352 O  O   . GLU C 1 1051 ? -2.358   57.355  83.838  1.00 111.52 ? 1051 GLU B O   1 
ATOM   22353 C  CB  . GLU C 1 1051 ? 0.428    58.569  82.469  1.00 121.24 ? 1051 GLU B CB  1 
ATOM   22354 C  CG  . GLU C 1 1051 ? 1.187    57.257  82.415  1.00 129.04 ? 1051 GLU B CG  1 
ATOM   22355 C  CD  . GLU C 1 1051 ? 2.485    57.382  81.615  1.00 136.79 ? 1051 GLU B CD  1 
ATOM   22356 O  OE1 . GLU C 1 1051 ? 2.699    58.445  80.977  1.00 138.82 ? 1051 GLU B OE1 1 
ATOM   22357 O  OE2 . GLU C 1 1051 ? 3.292    56.420  81.645  1.00 139.42 ? 1051 GLU B OE2 1 
ATOM   22358 N  N   . GLY C 1 1052 ? -0.590   56.879  85.121  1.00 108.98 ? 1052 GLY B N   1 
ATOM   22359 C  CA  . GLY C 1 1052 ? -1.180   55.676  85.672  1.00 109.10 ? 1052 GLY B CA  1 
ATOM   22360 C  C   . GLY C 1 1052 ? -2.392   55.937  86.536  1.00 108.95 ? 1052 GLY B C   1 
ATOM   22361 O  O   . GLY C 1 1052 ? -3.253   55.077  86.702  1.00 108.56 ? 1052 GLY B O   1 
ATOM   22362 N  N   . MET C 1 1053 ? -2.466   57.134  87.088  1.00 108.29 ? 1053 MET B N   1 
ATOM   22363 C  CA  . MET C 1 1053 ? -3.558   57.459  87.991  1.00 110.44 ? 1053 MET B CA  1 
ATOM   22364 C  C   . MET C 1 1053 ? -4.830   57.664  87.207  1.00 109.54 ? 1053 MET B C   1 
ATOM   22365 O  O   . MET C 1 1053 ? -5.892   57.208  87.608  1.00 109.29 ? 1053 MET B O   1 
ATOM   22366 C  CB  . MET C 1 1053 ? -3.248   58.719  88.820  1.00 113.44 ? 1053 MET B CB  1 
ATOM   22367 C  CG  . MET C 1 1053 ? -3.926   58.718  90.174  1.00 112.82 ? 1053 MET B CG  1 
ATOM   22368 S  SD  . MET C 1 1053 ? -3.701   57.088  90.926  1.00 221.69 ? 1053 MET B SD  1 
ATOM   22369 C  CE  . MET C 1 1053 ? -5.022   57.074  92.128  1.00 54.91  ? 1053 MET B CE  1 
ATOM   22370 N  N   . LEU C 1 1054 ? -4.707   58.369  86.088  1.00 110.60 ? 1054 LEU B N   1 
ATOM   22371 C  CA  . LEU C 1 1054 ? -5.841   58.646  85.212  1.00 112.66 ? 1054 LEU B CA  1 
ATOM   22372 C  C   . LEU C 1 1054 ? -6.398   57.331  84.657  1.00 109.16 ? 1054 LEU B C   1 
ATOM   22373 O  O   . LEU C 1 1054 ? -7.610   57.128  84.580  1.00 108.64 ? 1054 LEU B O   1 
ATOM   22374 C  CB  . LEU C 1 1054 ? -5.417   59.592  84.073  1.00 117.94 ? 1054 LEU B CB  1 
ATOM   22375 C  CG  . LEU C 1 1054 ? -4.784   60.946  84.440  1.00 122.04 ? 1054 LEU B CG  1 
ATOM   22376 C  CD1 . LEU C 1 1054 ? -4.304   61.715  83.195  1.00 124.77 ? 1054 LEU B CD1 1 
ATOM   22377 C  CD2 . LEU C 1 1054 ? -5.751   61.790  85.265  1.00 123.78 ? 1054 LEU B CD2 1 
ATOM   22378 N  N   . SER C 1 1055 ? -5.484   56.440  84.292  1.00 106.58 ? 1055 SER B N   1 
ATOM   22379 C  CA  . SER C 1 1055 ? -5.814   55.124  83.774  1.00 104.76 ? 1055 SER B CA  1 
ATOM   22380 C  C   . SER C 1 1055 ? -7.114   54.646  84.375  1.00 98.57  ? 1055 SER B C   1 
ATOM   22381 O  O   . SER C 1 1055 ? -7.916   54.021  83.704  1.00 100.46 ? 1055 SER B O   1 
ATOM   22382 C  CB  . SER C 1 1055 ? -4.673   54.147  84.101  1.00 109.29 ? 1055 SER B CB  1 
ATOM   22383 O  OG  . SER C 1 1055 ? -5.010   52.790  83.908  1.00 111.90 ? 1055 SER B OG  1 
ATOM   22384 N  N   . ILE C 1 1056 ? -7.342   54.942  85.640  1.00 93.48  ? 1056 ILE B N   1 
ATOM   22385 C  CA  . ILE C 1 1056 ? -8.499   54.351  86.306  1.00 92.84  ? 1056 ILE B CA  1 
ATOM   22386 C  C   . ILE C 1 1056 ? -9.816   55.080  85.991  1.00 91.03  ? 1056 ILE B C   1 
ATOM   22387 O  O   . ILE C 1 1056 ? -10.883  54.481  85.930  1.00 90.66  ? 1056 ILE B O   1 
ATOM   22388 C  CB  . ILE C 1 1056 ? -8.198   53.988  87.847  1.00 80.09  ? 1056 ILE B CB  1 
ATOM   22389 C  CG1 . ILE C 1 1056 ? -9.357   54.357  88.795  1.00 78.06  ? 1056 ILE B CG1 1 
ATOM   22390 C  CG2 . ILE C 1 1056 ? -6.848   54.576  88.295  1.00 77.13  ? 1056 ILE B CG2 1 
ATOM   22391 C  CD1 . ILE C 1 1056 ? -9.409   55.827  89.194  1.00 76.62  ? 1056 ILE B CD1 1 
ATOM   22392 N  N   . MET C 1 1057 ? -9.711   56.361  85.699  1.00 92.87  ? 1057 MET B N   1 
ATOM   22393 C  CA  . MET C 1 1057 ? -10.888  57.232  85.581  1.00 100.99 ? 1057 MET B CA  1 
ATOM   22394 C  C   . MET C 1 1057 ? -12.142  56.664  84.872  1.00 104.25 ? 1057 MET B C   1 
ATOM   22395 O  O   . MET C 1 1057 ? -13.283  57.012  85.230  1.00 105.20 ? 1057 MET B O   1 
ATOM   22396 C  CB  . MET C 1 1057 ? -10.500  58.552  84.897  1.00 107.26 ? 1057 MET B CB  1 
ATOM   22397 C  CG  . MET C 1 1057 ? -11.406  59.736  85.264  1.00 110.83 ? 1057 MET B CG  1 
ATOM   22398 S  SD  . MET C 1 1057 ? -10.836  60.660  86.701  1.00 143.21 ? 1057 MET B SD  1 
ATOM   22399 C  CE  . MET C 1 1057 ? -9.329   61.386  86.051  1.00 173.34 ? 1057 MET B CE  1 
ATOM   22400 N  N   . SER C 1 1058 ? -11.922  55.833  83.851  1.00 104.89 ? 1058 SER B N   1 
ATOM   22401 C  CA  . SER C 1 1058 ? -13.000  55.245  83.053  1.00 102.75 ? 1058 SER B CA  1 
ATOM   22402 C  C   . SER C 1 1058 ? -13.970  54.497  83.969  1.00 99.79  ? 1058 SER B C   1 
ATOM   22403 O  O   . SER C 1 1058 ? -15.186  54.442  83.722  1.00 99.54  ? 1058 SER B O   1 
ATOM   22404 C  CB  . SER C 1 1058 ? -12.404  54.277  82.028  1.00 101.33 ? 1058 SER B CB  1 
ATOM   22405 O  OG  . SER C 1 1058 ? -11.040  54.570  81.761  1.00 98.91  ? 1058 SER B OG  1 
ATOM   22406 N  N   . TYR C 1 1059 ? -13.406  53.918  85.024  1.00 95.64  ? 1059 TYR B N   1 
ATOM   22407 C  CA  . TYR C 1 1059 ? -14.184  53.196  85.989  1.00 95.52  ? 1059 TYR B CA  1 
ATOM   22408 C  C   . TYR C 1 1059 ? -14.658  54.136  87.091  1.00 101.64 ? 1059 TYR B C   1 
ATOM   22409 O  O   . TYR C 1 1059 ? -15.174  53.676  88.105  1.00 104.07 ? 1059 TYR B O   1 
ATOM   22410 C  CB  . TYR C 1 1059 ? -13.370  52.049  86.584  1.00 89.82  ? 1059 TYR B CB  1 
ATOM   22411 C  CG  . TYR C 1 1059 ? -12.719  51.137  85.585  1.00 88.66  ? 1059 TYR B CG  1 
ATOM   22412 C  CD1 . TYR C 1 1059 ? -11.649  51.571  84.798  1.00 90.03  ? 1059 TYR B CD1 1 
ATOM   22413 C  CD2 . TYR C 1 1059 ? -13.151  49.831  85.442  1.00 90.94  ? 1059 TYR B CD2 1 
ATOM   22414 C  CE1 . TYR C 1 1059 ? -11.030  50.715  83.860  1.00 93.82  ? 1059 TYR B CE1 1 
ATOM   22415 C  CE2 . TYR C 1 1059 ? -12.554  48.956  84.509  1.00 95.95  ? 1059 TYR B CE2 1 
ATOM   22416 C  CZ  . TYR C 1 1059 ? -11.491  49.396  83.715  1.00 97.21  ? 1059 TYR B CZ  1 
ATOM   22417 O  OH  . TYR C 1 1059 ? -10.913  48.516  82.797  1.00 98.41  ? 1059 TYR B OH  1 
ATOM   22418 N  N   . ARG C 1 1060 ? -14.474  55.444  86.935  1.00 104.80 ? 1060 ARG B N   1 
ATOM   22419 C  CA  . ARG C 1 1060 ? -15.078  56.354  87.908  1.00 109.23 ? 1060 ARG B CA  1 
ATOM   22420 C  C   . ARG C 1 1060 ? -16.462  56.672  87.439  1.00 113.30 ? 1060 ARG B C   1 
ATOM   22421 O  O   . ARG C 1 1060 ? -16.639  57.165  86.334  1.00 114.90 ? 1060 ARG B O   1 
ATOM   22422 C  CB  . ARG C 1 1060 ? -14.293  57.658  88.100  1.00 111.46 ? 1060 ARG B CB  1 
ATOM   22423 C  CG  . ARG C 1 1060 ? -14.655  58.413  89.406  1.00 106.58 ? 1060 ARG B CG  1 
ATOM   22424 C  CD  . ARG C 1 1060 ? -13.968  59.778  89.530  1.00 108.02 ? 1060 ARG B CD  1 
ATOM   22425 N  NE  . ARG C 1 1060 ? -14.855  60.876  89.134  1.00 113.48 ? 1060 ARG B NE  1 
ATOM   22426 C  CZ  . ARG C 1 1060 ? -14.447  62.130  88.924  1.00 117.18 ? 1060 ARG B CZ  1 
ATOM   22427 N  NH1 . ARG C 1 1060 ? -13.164  62.438  89.074  1.00 119.62 ? 1060 ARG B NH1 1 
ATOM   22428 N  NH2 . ARG C 1 1060 ? -15.307  63.082  88.564  1.00 117.14 ? 1060 ARG B NH2 1 
ATOM   22429 N  N   . ASN C 1 1061 ? -17.449  56.393  88.277  1.00 117.04 ? 1061 ASN B N   1 
ATOM   22430 C  CA  . ASN C 1 1061 ? -18.818  56.707  87.910  1.00 124.28 ? 1061 ASN B CA  1 
ATOM   22431 C  C   . ASN C 1 1061 ? -19.164  58.205  88.051  1.00 126.42 ? 1061 ASN B C   1 
ATOM   22432 O  O   . ASN C 1 1061 ? -18.300  59.030  88.341  1.00 125.02 ? 1061 ASN B O   1 
ATOM   22433 C  CB  . ASN C 1 1061 ? -19.812  55.779  88.625  1.00 128.22 ? 1061 ASN B CB  1 
ATOM   22434 C  CG  . ASN C 1 1061 ? -20.229  54.588  87.750  1.00 134.60 ? 1061 ASN B CG  1 
ATOM   22435 O  OD1 . ASN C 1 1061 ? -19.422  54.050  86.987  1.00 135.26 ? 1061 ASN B OD1 1 
ATOM   22436 N  ND2 . ASN C 1 1061 ? -21.504  54.192  87.839  1.00 138.46 ? 1061 ASN B ND2 1 
ATOM   22437 N  N   . ALA C 1 1062 ? -20.420  58.550  87.803  1.00 130.00 ? 1062 ALA B N   1 
ATOM   22438 C  CA  . ALA C 1 1062 ? -20.849  59.937  87.789  1.00 132.22 ? 1062 ALA B CA  1 
ATOM   22439 C  C   . ALA C 1 1062 ? -20.941  60.513  89.197  1.00 131.06 ? 1062 ALA B C   1 
ATOM   22440 O  O   . ALA C 1 1062 ? -20.669  61.686  89.424  1.00 132.95 ? 1062 ALA B O   1 
ATOM   22441 C  CB  . ALA C 1 1062 ? -22.190  60.041  87.085  1.00 135.70 ? 1062 ALA B CB  1 
ATOM   22442 N  N   . ASP C 1 1063 ? -21.343  59.671  90.137  1.00 128.68 ? 1063 ASP B N   1 
ATOM   22443 C  CA  . ASP C 1 1063 ? -21.555  60.079  91.523  1.00 127.05 ? 1063 ASP B CA  1 
ATOM   22444 C  C   . ASP C 1 1063 ? -20.246  60.115  92.316  1.00 121.30 ? 1063 ASP B C   1 
ATOM   22445 O  O   . ASP C 1 1063 ? -20.232  60.389  93.512  1.00 118.96 ? 1063 ASP B O   1 
ATOM   22446 C  CB  . ASP C 1 1063 ? -22.533  59.113  92.180  1.00 130.26 ? 1063 ASP B CB  1 
ATOM   22447 C  CG  . ASP C 1 1063 ? -22.186  57.668  91.889  1.00 133.29 ? 1063 ASP B CG  1 
ATOM   22448 O  OD1 . ASP C 1 1063 ? -21.069  57.426  91.363  1.00 132.46 ? 1063 ASP B OD1 1 
ATOM   22449 O  OD2 . ASP C 1 1063 ? -23.021  56.780  92.182  1.00 135.60 ? 1063 ASP B OD2 1 
ATOM   22450 N  N   . TYR C 1 1064 ? -19.149  59.835  91.629  1.00 118.08 ? 1064 TYR B N   1 
ATOM   22451 C  CA  . TYR C 1 1064 ? -17.833  59.787  92.244  1.00 113.96 ? 1064 TYR B CA  1 
ATOM   22452 C  C   . TYR C 1 1064 ? -17.548  58.406  92.787  1.00 112.85 ? 1064 TYR B C   1 
ATOM   22453 O  O   . TYR C 1 1064 ? -16.440  58.114  93.227  1.00 114.52 ? 1064 TYR B O   1 
ATOM   22454 C  CB  . TYR C 1 1064 ? -17.662  60.905  93.274  1.00 110.76 ? 1064 TYR B CB  1 
ATOM   22455 C  CG  . TYR C 1 1064 ? -17.503  62.201  92.562  1.00 109.56 ? 1064 TYR B CG  1 
ATOM   22456 C  CD1 . TYR C 1 1064 ? -16.322  62.494  91.910  1.00 109.71 ? 1064 TYR B CD1 1 
ATOM   22457 C  CD2 . TYR C 1 1064 ? -18.548  63.087  92.456  1.00 112.44 ? 1064 TYR B CD2 1 
ATOM   22458 C  CE1 . TYR C 1 1064 ? -16.162  63.667  91.201  1.00 112.49 ? 1064 TYR B CE1 1 
ATOM   22459 C  CE2 . TYR C 1 1064 ? -18.407  64.271  91.747  1.00 115.60 ? 1064 TYR B CE2 1 
ATOM   22460 C  CZ  . TYR C 1 1064 ? -17.205  64.562  91.113  1.00 115.23 ? 1064 TYR B CZ  1 
ATOM   22461 O  OH  . TYR C 1 1064 ? -17.041  65.738  90.390  1.00 116.05 ? 1064 TYR B OH  1 
ATOM   22462 N  N   . SER C 1 1065 ? -18.550  57.543  92.711  1.00 110.69 ? 1065 SER B N   1 
ATOM   22463 C  CA  . SER C 1 1065 ? -18.337  56.153  93.067  1.00 107.77 ? 1065 SER B CA  1 
ATOM   22464 C  C   . SER C 1 1065 ? -17.622  55.428  91.930  1.00 105.80 ? 1065 SER B C   1 
ATOM   22465 O  O   . SER C 1 1065 ? -18.079  55.454  90.780  1.00 106.04 ? 1065 SER B O   1 
ATOM   22466 C  CB  . SER C 1 1065 ? -19.658  55.461  93.381  1.00 109.13 ? 1065 SER B CB  1 
ATOM   22467 O  OG  . SER C 1 1065 ? -20.301  55.060  92.190  1.00 112.16 ? 1065 SER B OG  1 
ATOM   22468 N  N   . TYR C 1 1066 ? -16.493  54.797  92.245  1.00 102.64 ? 1066 TYR B N   1 
ATOM   22469 C  CA  . TYR C 1 1066 ? -15.817  53.965  91.264  1.00 101.26 ? 1066 TYR B CA  1 
ATOM   22470 C  C   . TYR C 1 1066 ? -16.522  52.638  91.184  1.00 102.19 ? 1066 TYR B C   1 
ATOM   22471 O  O   . TYR C 1 1066 ? -17.334  52.290  92.045  1.00 102.93 ? 1066 TYR B O   1 
ATOM   22472 C  CB  . TYR C 1 1066 ? -14.341  53.783  91.604  1.00 97.63  ? 1066 TYR B CB  1 
ATOM   22473 C  CG  . TYR C 1 1066 ? -13.650  55.092  91.759  1.00 96.80  ? 1066 TYR B CG  1 
ATOM   22474 C  CD1 . TYR C 1 1066 ? -14.076  55.995  92.719  1.00 98.27  ? 1066 TYR B CD1 1 
ATOM   22475 C  CD2 . TYR C 1 1066 ? -12.596  55.447  90.937  1.00 97.57  ? 1066 TYR B CD2 1 
ATOM   22476 C  CE1 . TYR C 1 1066 ? -13.468  57.221  92.868  1.00 100.58 ? 1066 TYR B CE1 1 
ATOM   22477 C  CE2 . TYR C 1 1066 ? -11.972  56.680  91.073  1.00 99.51  ? 1066 TYR B CE2 1 
ATOM   22478 C  CZ  . TYR C 1 1066 ? -12.415  57.567  92.045  1.00 101.89 ? 1066 TYR B CZ  1 
ATOM   22479 O  OH  . TYR C 1 1066 ? -11.821  58.806  92.210  1.00 104.05 ? 1066 TYR B OH  1 
ATOM   22480 N  N   . SER C 1 1067 ? -16.208  51.891  90.142  1.00 101.51 ? 1067 SER B N   1 
ATOM   22481 C  CA  . SER C 1 1067 ? -16.927  50.663  89.904  1.00 102.29 ? 1067 SER B CA  1 
ATOM   22482 C  C   . SER C 1 1067 ? -16.055  49.587  89.250  1.00 102.64 ? 1067 SER B C   1 
ATOM   22483 O  O   . SER C 1 1067 ? -15.326  49.845  88.290  1.00 102.51 ? 1067 SER B O   1 
ATOM   22484 C  CB  . SER C 1 1067 ? -18.165  50.959  89.068  1.00 103.39 ? 1067 SER B CB  1 
ATOM   22485 O  OG  . SER C 1 1067 ? -19.282  50.295  89.614  1.00 104.50 ? 1067 SER B OG  1 
ATOM   22486 N  N   . VAL C 1 1068 ? -16.141  48.380  89.787  1.00 102.75 ? 1068 VAL B N   1 
ATOM   22487 C  CA  . VAL C 1 1068 ? -15.258  47.297  89.416  1.00 104.08 ? 1068 VAL B CA  1 
ATOM   22488 C  C   . VAL C 1 1068 ? -14.908  47.205  87.923  1.00 109.24 ? 1068 VAL B C   1 
ATOM   22489 O  O   . VAL C 1 1068 ? -13.734  47.348  87.587  1.00 109.22 ? 1068 VAL B O   1 
ATOM   22490 C  CB  . VAL C 1 1068 ? -15.887  46.008  89.788  1.00 104.22 ? 1068 VAL B CB  1 
ATOM   22491 C  CG1 . VAL C 1 1068 ? -17.292  45.965  89.143  1.00 108.28 ? 1068 VAL B CG1 1 
ATOM   22492 C  CG2 . VAL C 1 1068 ? -14.981  44.875  89.321  1.00 102.69 ? 1068 VAL B CG2 1 
ATOM   22493 N  N   . TRP C 1 1069 ? -15.884  46.912  87.038  1.00 112.57 ? 1069 TRP B N   1 
ATOM   22494 C  CA  . TRP C 1 1069 ? -15.659  47.050  85.571  1.00 114.17 ? 1069 TRP B CA  1 
ATOM   22495 C  C   . TRP C 1 1069 ? -16.498  48.176  84.949  1.00 116.14 ? 1069 TRP B C   1 
ATOM   22496 O  O   . TRP C 1 1069 ? -17.395  48.715  85.611  1.00 116.91 ? 1069 TRP B O   1 
ATOM   22497 C  CB  . TRP C 1 1069 ? -15.881  45.763  84.746  1.00 114.10 ? 1069 TRP B CB  1 
ATOM   22498 C  CG  . TRP C 1 1069 ? -15.543  44.460  85.388  1.00 110.48 ? 1069 TRP B CG  1 
ATOM   22499 C  CD1 . TRP C 1 1069 ? -14.373  43.737  85.274  1.00 108.79 ? 1069 TRP B CD1 1 
ATOM   22500 C  CD2 . TRP C 1 1069 ? -16.405  43.697  86.206  1.00 108.14 ? 1069 TRP B CD2 1 
ATOM   22501 N  NE1 . TRP C 1 1069 ? -14.462  42.571  86.002  1.00 107.30 ? 1069 TRP B NE1 1 
ATOM   22502 C  CE2 . TRP C 1 1069 ? -15.698  42.526  86.588  1.00 108.26 ? 1069 TRP B CE2 1 
ATOM   22503 C  CE3 . TRP C 1 1069 ? -17.704  43.894  86.674  1.00 106.47 ? 1069 TRP B CE3 1 
ATOM   22504 C  CZ2 . TRP C 1 1069 ? -16.250  41.571  87.415  1.00 109.96 ? 1069 TRP B CZ2 1 
ATOM   22505 C  CZ3 . TRP C 1 1069 ? -18.252  42.946  87.482  1.00 108.84 ? 1069 TRP B CZ3 1 
ATOM   22506 C  CH2 . TRP C 1 1069 ? -17.528  41.793  87.852  1.00 111.09 ? 1069 TRP B CH2 1 
ATOM   22507 N  N   . LYS C 1 1070 ? -16.224  48.508  83.680  1.00 116.00 ? 1070 LYS B N   1 
ATOM   22508 C  CA  . LYS C 1 1070 ? -16.841  49.683  83.055  1.00 115.51 ? 1070 LYS B CA  1 
ATOM   22509 C  C   . LYS C 1 1070 ? -18.354  49.635  82.926  1.00 119.00 ? 1070 LYS B C   1 
ATOM   22510 O  O   . LYS C 1 1070 ? -18.916  48.757  82.265  1.00 120.69 ? 1070 LYS B O   1 
ATOM   22511 C  CB  . LYS C 1 1070 ? -16.196  50.020  81.711  1.00 113.69 ? 1070 LYS B CB  1 
ATOM   22512 C  CG  . LYS C 1 1070 ? -15.155  51.109  81.837  1.00 110.65 ? 1070 LYS B CG  1 
ATOM   22513 C  CD  . LYS C 1 1070 ? -15.135  52.067  80.657  1.00 112.03 ? 1070 LYS B CD  1 
ATOM   22514 C  CE  . LYS C 1 1070 ? -14.280  51.546  79.505  1.00 112.29 ? 1070 LYS B CE  1 
ATOM   22515 N  NZ  . LYS C 1 1070 ? -14.240  52.420  78.276  1.00 113.32 ? 1070 LYS B NZ  1 
ATOM   22516 N  N   . GLY C 1 1071 ? -19.003  50.603  83.559  1.00 120.42 ? 1071 GLY B N   1 
ATOM   22517 C  CA  . GLY C 1 1071 ? -20.438  50.741  83.446  1.00 126.34 ? 1071 GLY B CA  1 
ATOM   22518 C  C   . GLY C 1 1071 ? -21.134  49.796  84.383  1.00 128.28 ? 1071 GLY B C   1 
ATOM   22519 O  O   . GLY C 1 1071 ? -22.361  49.710  84.411  1.00 134.83 ? 1071 GLY B O   1 
ATOM   22520 N  N   . GLY C 1 1072 ? -20.328  49.080  85.153  1.00 126.21 ? 1072 GLY B N   1 
ATOM   22521 C  CA  . GLY C 1 1072 ? -20.827  48.168  86.166  1.00 126.51 ? 1072 GLY B CA  1 
ATOM   22522 C  C   . GLY C 1 1072 ? -21.283  48.890  87.419  1.00 127.92 ? 1072 GLY B C   1 
ATOM   22523 O  O   . GLY C 1 1072 ? -20.675  49.867  87.850  1.00 126.97 ? 1072 GLY B O   1 
ATOM   22524 N  N   . SER C 1 1073 ? -22.367  48.403  88.003  1.00 128.88 ? 1073 SER B N   1 
ATOM   22525 C  CA  . SER C 1 1073 ? -22.966  49.064  89.142  1.00 127.91 ? 1073 SER B CA  1 
ATOM   22526 C  C   . SER C 1 1073 ? -21.883  49.362  90.156  1.00 123.98 ? 1073 SER B C   1 
ATOM   22527 O  O   . SER C 1 1073 ? -20.925  48.595  90.286  1.00 120.84 ? 1073 SER B O   1 
ATOM   22528 C  CB  . SER C 1 1073 ? -24.038  48.164  89.725  1.00 131.16 ? 1073 SER B CB  1 
ATOM   22529 O  OG  . SER C 1 1073 ? -23.813  46.827  89.312  1.00 132.27 ? 1073 SER B OG  1 
ATOM   22530 N  N   . ALA C 1 1074 ? -22.028  50.489  90.847  1.00 122.30 ? 1074 ALA B N   1 
ATOM   22531 C  CA  . ALA C 1 1074 ? -21.010  50.965  91.770  1.00 119.74 ? 1074 ALA B CA  1 
ATOM   22532 C  C   . ALA C 1 1074 ? -20.698  49.851  92.709  1.00 113.98 ? 1074 ALA B C   1 
ATOM   22533 O  O   . ALA C 1 1074 ? -21.607  49.176  93.191  1.00 116.62 ? 1074 ALA B O   1 
ATOM   22534 C  CB  . ALA C 1 1074 ? -21.504  52.152  92.537  1.00 120.93 ? 1074 ALA B CB  1 
ATOM   22535 N  N   . SER C 1 1075 ? -19.412  49.626  92.938  1.00 109.77 ? 1075 SER B N   1 
ATOM   22536 C  CA  . SER C 1 1075 ? -19.018  48.664  93.950  1.00 108.83 ? 1075 SER B CA  1 
ATOM   22537 C  C   . SER C 1 1075 ? -18.476  49.442  95.106  1.00 106.70 ? 1075 SER B C   1 
ATOM   22538 O  O   . SER C 1 1075 ? -17.568  50.266  94.940  1.00 104.60 ? 1075 SER B O   1 
ATOM   22539 C  CB  . SER C 1 1075 ? -17.930  47.701  93.477  1.00 109.38 ? 1075 SER B CB  1 
ATOM   22540 O  OG  . SER C 1 1075 ? -16.730  47.943  94.209  1.00 108.20 ? 1075 SER B OG  1 
ATOM   22541 N  N   . THR C 1 1076 ? -19.041  49.154  96.271  1.00 106.72 ? 1076 THR B N   1 
ATOM   22542 C  CA  . THR C 1 1076 ? -18.652  49.768  97.508  1.00 102.12 ? 1076 THR B CA  1 
ATOM   22543 C  C   . THR C 1 1076 ? -17.209  49.411  97.728  1.00 100.37 ? 1076 THR B C   1 
ATOM   22544 O  O   . THR C 1 1076 ? -16.434  50.204  98.261  1.00 100.07 ? 1076 THR B O   1 
ATOM   22545 C  CB  . THR C 1 1076 ? -19.443  49.168  98.631  1.00 100.53 ? 1076 THR B CB  1 
ATOM   22546 O  OG1 . THR C 1 1076 ? -20.074  50.207  99.371  1.00 102.00 ? 1076 THR B OG1 1 
ATOM   22547 C  CG2 . THR C 1 1076 ? -18.526  48.390  99.535  1.00 97.13  ? 1076 THR B CG2 1 
ATOM   22548 N  N   . TRP C 1 1077 ? -16.853  48.214  97.267  1.00 99.51  ? 1077 TRP B N   1 
ATOM   22549 C  CA  . TRP C 1 1077 ? -15.521  47.652  97.471  1.00 98.25  ? 1077 TRP B CA  1 
ATOM   22550 C  C   . TRP C 1 1077 ? -14.440  48.428  96.732  1.00 93.91  ? 1077 TRP B C   1 
ATOM   22551 O  O   . TRP C 1 1077 ? -13.467  48.910  97.334  1.00 90.38  ? 1077 TRP B O   1 
ATOM   22552 C  CB  . TRP C 1 1077 ? -15.494  46.186  97.024  1.00 101.49 ? 1077 TRP B CB  1 
ATOM   22553 C  CG  . TRP C 1 1077 ? -14.247  45.458  97.384  1.00 104.24 ? 1077 TRP B CG  1 
ATOM   22554 C  CD1 . TRP C 1 1077 ? -13.904  45.000  98.617  1.00 106.15 ? 1077 TRP B CD1 1 
ATOM   22555 C  CD2 . TRP C 1 1077 ? -13.177  45.083  96.504  1.00 106.12 ? 1077 TRP B CD2 1 
ATOM   22556 N  NE1 . TRP C 1 1077 ? -12.686  44.365  98.568  1.00 107.23 ? 1077 TRP B NE1 1 
ATOM   22557 C  CE2 . TRP C 1 1077 ? -12.218  44.400  97.280  1.00 106.89 ? 1077 TRP B CE2 1 
ATOM   22558 C  CE3 . TRP C 1 1077 ? -12.931  45.265  95.139  1.00 106.78 ? 1077 TRP B CE3 1 
ATOM   22559 C  CZ2 . TRP C 1 1077 ? -11.030  43.895  96.733  1.00 105.25 ? 1077 TRP B CZ2 1 
ATOM   22560 C  CZ3 . TRP C 1 1077 ? -11.751  44.757  94.601  1.00 106.95 ? 1077 TRP B CZ3 1 
ATOM   22561 C  CH2 . TRP C 1 1077 ? -10.819  44.082  95.397  1.00 105.26 ? 1077 TRP B CH2 1 
ATOM   22562 N  N   . LEU C 1 1078 ? -14.620  48.552  95.423  1.00 92.86  ? 1078 LEU B N   1 
ATOM   22563 C  CA  . LEU C 1 1078 ? -13.587  49.146  94.600  1.00 90.22  ? 1078 LEU B CA  1 
ATOM   22564 C  C   . LEU C 1 1078 ? -13.481  50.626  94.904  1.00 91.12  ? 1078 LEU B C   1 
ATOM   22565 O  O   . LEU C 1 1078 ? -12.396  51.202  94.860  1.00 90.94  ? 1078 LEU B O   1 
ATOM   22566 C  CB  . LEU C 1 1078 ? -13.821  48.862  93.121  1.00 87.07  ? 1078 LEU B CB  1 
ATOM   22567 C  CG  . LEU C 1 1078 ? -12.555  49.036  92.293  1.00 81.13  ? 1078 LEU B CG  1 
ATOM   22568 C  CD1 . LEU C 1 1078 ? -12.219  47.823  91.430  1.00 78.42  ? 1078 LEU B CD1 1 
ATOM   22569 C  CD2 . LEU C 1 1078 ? -12.708  50.288  91.465  1.00 81.23  ? 1078 LEU B CD2 1 
ATOM   22570 N  N   . THR C 1 1079 ? -14.603  51.232  95.263  1.00 92.43  ? 1079 THR B N   1 
ATOM   22571 C  CA  . THR C 1 1079 ? -14.569  52.624  95.698  1.00 93.18  ? 1079 THR B CA  1 
ATOM   22572 C  C   . THR C 1 1079 ? -13.589  52.795  96.879  1.00 91.93  ? 1079 THR B C   1 
ATOM   22573 O  O   . THR C 1 1079 ? -12.750  53.708  96.890  1.00 92.11  ? 1079 THR B O   1 
ATOM   22574 C  CB  . THR C 1 1079 ? -15.993  53.167  96.026  1.00 105.63 ? 1079 THR B CB  1 
ATOM   22575 O  OG1 . THR C 1 1079 ? -16.815  53.085  94.851  1.00 107.16 ? 1079 THR B OG1 1 
ATOM   22576 C  CG2 . THR C 1 1079 ? -15.936  54.618  96.481  1.00 104.61 ? 1079 THR B CG2 1 
ATOM   22577 N  N   . ALA C 1 1080 ? -13.676  51.907  97.862  1.00 87.72  ? 1080 ALA B N   1 
ATOM   22578 C  CA  . ALA C 1 1080 ? -12.760  51.984  98.977  1.00 85.13  ? 1080 ALA B CA  1 
ATOM   22579 C  C   . ALA C 1 1080 ? -11.353  51.899  98.425  1.00 82.09  ? 1080 ALA B C   1 
ATOM   22580 O  O   . ALA C 1 1080 ? -10.577  52.843  98.539  1.00 81.14  ? 1080 ALA B O   1 
ATOM   22581 C  CB  . ALA C 1 1080 ? -13.020  50.872  99.949  1.00 84.69  ? 1080 ALA B CB  1 
ATOM   22582 N  N   . PHE C 1 1081 ? -11.058  50.764  97.798  1.00 81.31  ? 1081 PHE B N   1 
ATOM   22583 C  CA  . PHE C 1 1081 ? -9.723   50.432  97.298  1.00 78.38  ? 1081 PHE B CA  1 
ATOM   22584 C  C   . PHE C 1 1081 ? -9.168   51.531  96.405  1.00 74.78  ? 1081 PHE B C   1 
ATOM   22585 O  O   . PHE C 1 1081 ? -7.964   51.766  96.351  1.00 70.61  ? 1081 PHE B O   1 
ATOM   22586 C  CB  . PHE C 1 1081 ? -9.774   49.113  96.520  1.00 80.79  ? 1081 PHE B CB  1 
ATOM   22587 C  CG  . PHE C 1 1081 ? -8.436   48.631  96.042  1.00 82.95  ? 1081 PHE B CG  1 
ATOM   22588 C  CD1 . PHE C 1 1081 ? -7.599   47.928  96.876  1.00 82.56  ? 1081 PHE B CD1 1 
ATOM   22589 C  CD2 . PHE C 1 1081 ? -8.023   48.868  94.751  1.00 86.12  ? 1081 PHE B CD2 1 
ATOM   22590 C  CE1 . PHE C 1 1081 ? -6.362   47.483  96.430  1.00 83.79  ? 1081 PHE B CE1 1 
ATOM   22591 C  CE2 . PHE C 1 1081 ? -6.796   48.421  94.305  1.00 87.36  ? 1081 PHE B CE2 1 
ATOM   22592 C  CZ  . PHE C 1 1081 ? -5.965   47.731  95.149  1.00 85.92  ? 1081 PHE B CZ  1 
ATOM   22593 N  N   . ALA C 1 1082 ? -10.055  52.202  95.688  1.00 76.52  ? 1082 ALA B N   1 
ATOM   22594 C  CA  . ALA C 1 1082 ? -9.642   53.328  94.858  1.00 76.88  ? 1082 ALA B CA  1 
ATOM   22595 C  C   . ALA C 1 1082 ? -9.199   54.479  95.753  1.00 76.00  ? 1082 ALA B C   1 
ATOM   22596 O  O   . ALA C 1 1082 ? -8.079   54.957  95.633  1.00 75.49  ? 1082 ALA B O   1 
ATOM   22597 C  CB  . ALA C 1 1082 ? -10.764  53.760  93.961  1.00 78.89  ? 1082 ALA B CB  1 
ATOM   22598 N  N   . LEU C 1 1083 ? -10.073  54.901  96.662  1.00 74.75  ? 1083 LEU B N   1 
ATOM   22599 C  CA  . LEU C 1 1083 ? -9.669   55.757  97.767  1.00 72.59  ? 1083 LEU B CA  1 
ATOM   22600 C  C   . LEU C 1 1083 ? -8.328   55.364  98.387  1.00 72.30  ? 1083 LEU B C   1 
ATOM   22601 O  O   . LEU C 1 1083 ? -7.386   56.159  98.369  1.00 73.70  ? 1083 LEU B O   1 
ATOM   22602 C  CB  . LEU C 1 1083 ? -10.735  55.705  98.827  1.00 68.55  ? 1083 LEU B CB  1 
ATOM   22603 C  CG  . LEU C 1 1083 ? -11.866  56.566  98.309  1.00 67.72  ? 1083 LEU B CG  1 
ATOM   22604 C  CD1 . LEU C 1 1083 ? -13.106  56.225  99.083  1.00 68.66  ? 1083 LEU B CD1 1 
ATOM   22605 C  CD2 . LEU C 1 1083 ? -11.495  58.055  98.413  1.00 65.77  ? 1083 LEU B CD2 1 
ATOM   22606 N  N   . ARG C 1 1084 ? -8.245   54.153  98.940  1.00 70.26  ? 1084 ARG B N   1 
ATOM   22607 C  CA  . ARG C 1 1084 ? -6.973   53.637  99.452  1.00 70.71  ? 1084 ARG B CA  1 
ATOM   22608 C  C   . ARG C 1 1084 ? -5.796   53.966  98.543  1.00 73.28  ? 1084 ARG B C   1 
ATOM   22609 O  O   . ARG C 1 1084 ? -4.822   54.540  99.001  1.00 74.21  ? 1084 ARG B O   1 
ATOM   22610 C  CB  . ARG C 1 1084 ? -7.018   52.119  99.684  1.00 72.16  ? 1084 ARG B CB  1 
ATOM   22611 C  CG  . ARG C 1 1084 ? -5.671   51.381  99.456  1.00 68.58  ? 1084 ARG B CG  1 
ATOM   22612 C  CD  . ARG C 1 1084 ? -5.110   50.863  100.727 1.00 69.52  ? 1084 ARG B CD  1 
ATOM   22613 N  NE  . ARG C 1 1084 ? -3.746   50.353  100.632 1.00 74.97  ? 1084 ARG B NE  1 
ATOM   22614 C  CZ  . ARG C 1 1084 ? -3.409   49.080  100.866 1.00 81.17  ? 1084 ARG B CZ  1 
ATOM   22615 N  NH1 . ARG C 1 1084 ? -4.364   48.196  101.165 1.00 84.58  ? 1084 ARG B NH1 1 
ATOM   22616 N  NH2 . ARG C 1 1084 ? -2.133   48.671  100.810 1.00 80.91  ? 1084 ARG B NH2 1 
ATOM   22617 N  N   . VAL C 1 1085 ? -5.859   53.606  97.263  1.00 76.32  ? 1085 VAL B N   1 
ATOM   22618 C  CA  . VAL C 1 1085 ? -4.686   53.825  96.399  1.00 79.31  ? 1085 VAL B CA  1 
ATOM   22619 C  C   . VAL C 1 1085 ? -4.492   55.297  96.002  1.00 79.99  ? 1085 VAL B C   1 
ATOM   22620 O  O   . VAL C 1 1085 ? -3.379   55.743  95.708  1.00 77.85  ? 1085 VAL B O   1 
ATOM   22621 C  CB  . VAL C 1 1085 ? -4.667   52.904  95.148  1.00 69.97  ? 1085 VAL B CB  1 
ATOM   22622 C  CG1 . VAL C 1 1085 ? -3.377   53.133  94.338  1.00 69.85  ? 1085 VAL B CG1 1 
ATOM   22623 C  CG2 . VAL C 1 1085 ? -4.797   51.425  95.552  1.00 67.46  ? 1085 VAL B CG2 1 
ATOM   22624 N  N   . LEU C 1 1086 ? -5.594   56.036  96.011  1.00 83.30  ? 1086 LEU B N   1 
ATOM   22625 C  CA  . LEU C 1 1086 ? -5.585   57.457  95.714  1.00 88.00  ? 1086 LEU B CA  1 
ATOM   22626 C  C   . LEU C 1 1086 ? -4.957   58.195  96.881  1.00 87.95  ? 1086 LEU B C   1 
ATOM   22627 O  O   . LEU C 1 1086 ? -4.095   59.066  96.685  1.00 89.20  ? 1086 LEU B O   1 
ATOM   22628 C  CB  . LEU C 1 1086 ? -7.023   57.973  95.518  1.00 93.28  ? 1086 LEU B CB  1 
ATOM   22629 C  CG  . LEU C 1 1086 ? -7.737   58.140  94.156  1.00 98.24  ? 1086 LEU B CG  1 
ATOM   22630 C  CD1 . LEU C 1 1086 ? -7.125   59.241  93.294  1.00 98.51  ? 1086 LEU B CD1 1 
ATOM   22631 C  CD2 . LEU C 1 1086 ? -7.819   56.834  93.408  1.00 99.67  ? 1086 LEU B CD2 1 
ATOM   22632 N  N   . GLY C 1 1087 ? -5.415   57.854  98.090  1.00 85.62  ? 1087 GLY B N   1 
ATOM   22633 C  CA  . GLY C 1 1087 ? -4.931   58.486  99.302  1.00 83.50  ? 1087 GLY B CA  1 
ATOM   22634 C  C   . GLY C 1 1087 ? -3.433   58.311  99.338  1.00 80.96  ? 1087 GLY B C   1 
ATOM   22635 O  O   . GLY C 1 1087 ? -2.672   59.272  99.443  1.00 82.52  ? 1087 GLY B O   1 
ATOM   22636 N  N   . GLN C 1 1088 ? -3.014   57.067  99.213  1.00 76.42  ? 1088 GLN B N   1 
ATOM   22637 C  CA  . GLN C 1 1088 ? -1.616   56.746  99.059  1.00 77.33  ? 1088 GLN B CA  1 
ATOM   22638 C  C   . GLN C 1 1088 ? -0.851   57.662  98.097  1.00 82.53  ? 1088 GLN B C   1 
ATOM   22639 O  O   . GLN C 1 1088 ? 0.197    58.200  98.457  1.00 82.36  ? 1088 GLN B O   1 
ATOM   22640 C  CB  . GLN C 1 1088 ? -1.505   55.299  98.611  1.00 76.52  ? 1088 GLN B CB  1 
ATOM   22641 C  CG  . GLN C 1 1088 ? -2.258   54.408  99.534  1.00 76.97  ? 1088 GLN B CG  1 
ATOM   22642 C  CD  . GLN C 1 1088 ? -1.917   52.948  99.401  1.00 77.02  ? 1088 GLN B CD  1 
ATOM   22643 O  OE1 . GLN C 1 1088 ? -2.805   52.097  99.489  1.00 76.29  ? 1088 GLN B OE1 1 
ATOM   22644 N  NE2 . GLN C 1 1088 ? -0.633   52.639  99.207  1.00 77.23  ? 1088 GLN B NE2 1 
ATOM   22645 N  N   . VAL C 1 1089 ? -1.358   57.836  96.876  1.00 86.37  ? 1089 VAL B N   1 
ATOM   22646 C  CA  . VAL C 1 1089 ? -0.589   58.534  95.833  1.00 87.63  ? 1089 VAL B CA  1 
ATOM   22647 C  C   . VAL C 1 1089 ? -0.735   60.051  95.939  1.00 91.36  ? 1089 VAL B C   1 
ATOM   22648 O  O   . VAL C 1 1089 ? -0.016   60.819  95.310  1.00 91.46  ? 1089 VAL B O   1 
ATOM   22649 C  CB  . VAL C 1 1089 ? -0.924   58.011  94.414  1.00 82.14  ? 1089 VAL B CB  1 
ATOM   22650 C  CG1 . VAL C 1 1089 ? 0.142    58.413  93.437  1.00 80.44  ? 1089 VAL B CG1 1 
ATOM   22651 C  CG2 . VAL C 1 1089 ? -1.014   56.492  94.415  1.00 80.90  ? 1089 VAL B CG2 1 
ATOM   22652 N  N   . ASN C 1 1090 ? -1.658   60.482  96.776  1.00 96.45  ? 1090 ASN B N   1 
ATOM   22653 C  CA  . ASN C 1 1090 ? -1.803   61.894  97.038  1.00 101.74 ? 1090 ASN B CA  1 
ATOM   22654 C  C   . ASN C 1 1090 ? -0.584   62.521  97.712  1.00 104.34 ? 1090 ASN B C   1 
ATOM   22655 O  O   . ASN C 1 1090 ? -0.328   63.706  97.567  1.00 105.74 ? 1090 ASN B O   1 
ATOM   22656 C  CB  . ASN C 1 1090 ? -3.028   62.129  97.888  1.00 103.77 ? 1090 ASN B CB  1 
ATOM   22657 C  CG  . ASN C 1 1090 ? -3.373   63.572  97.974  1.00 108.02 ? 1090 ASN B CG  1 
ATOM   22658 O  OD1 . ASN C 1 1090 ? -2.549   64.444  97.691  1.00 108.13 ? 1090 ASN B OD1 1 
ATOM   22659 N  ND2 . ASN C 1 1090 ? -4.603   63.851  98.348  1.00 110.90 ? 1090 ASN B ND2 1 
ATOM   22660 N  N   . LYS C 1 1091 ? 0.157    61.731  98.473  1.00 105.63 ? 1091 LYS B N   1 
ATOM   22661 C  CA  . LYS C 1 1091 ? 1.371    62.237  99.094  1.00 108.43 ? 1091 LYS B CA  1 
ATOM   22662 C  C   . LYS C 1 1091 ? 2.178    62.940  98.038  1.00 104.54 ? 1091 LYS B C   1 
ATOM   22663 O  O   . LYS C 1 1091 ? 2.589    64.073  98.227  1.00 106.30 ? 1091 LYS B O   1 
ATOM   22664 C  CB  . LYS C 1 1091 ? 2.243    61.103  99.640  1.00 115.65 ? 1091 LYS B CB  1 
ATOM   22665 C  CG  . LYS C 1 1091 ? 1.991    60.696  101.081 1.00 122.87 ? 1091 LYS B CG  1 
ATOM   22666 C  CD  . LYS C 1 1091 ? 3.315    60.329  101.736 1.00 128.50 ? 1091 LYS B CD  1 
ATOM   22667 C  CE  . LYS C 1 1091 ? 4.303    61.481  101.570 1.00 134.18 ? 1091 LYS B CE  1 
ATOM   22668 N  NZ  . LYS C 1 1091 ? 5.229    61.642  102.732 1.00 136.61 ? 1091 LYS B NZ  1 
ATOM   22669 N  N   . TYR C 1 1092 ? 2.400    62.251  96.924  1.00 100.50 ? 1092 TYR B N   1 
ATOM   22670 C  CA  . TYR C 1 1092 ? 3.314    62.731  95.902  1.00 100.59 ? 1092 TYR B CA  1 
ATOM   22671 C  C   . TYR C 1 1092 ? 2.671    63.303  94.640  1.00 106.36 ? 1092 TYR B C   1 
ATOM   22672 O  O   . TYR C 1 1092 ? 3.325    63.993  93.851  1.00 110.10 ? 1092 TYR B O   1 
ATOM   22673 C  CB  . TYR C 1 1092 ? 4.257    61.626  95.521  1.00 95.82  ? 1092 TYR B CB  1 
ATOM   22674 C  CG  . TYR C 1 1092 ? 4.835    60.968  96.711  1.00 93.38  ? 1092 TYR B CG  1 
ATOM   22675 C  CD1 . TYR C 1 1092 ? 5.572    61.689  97.610  1.00 93.96  ? 1092 TYR B CD1 1 
ATOM   22676 C  CD2 . TYR C 1 1092 ? 4.644    59.612  96.941  1.00 92.81  ? 1092 TYR B CD2 1 
ATOM   22677 C  CE1 . TYR C 1 1092 ? 6.117    61.080  98.713  1.00 94.99  ? 1092 TYR B CE1 1 
ATOM   22678 C  CE2 . TYR C 1 1092 ? 5.185    58.991  98.041  1.00 92.67  ? 1092 TYR B CE2 1 
ATOM   22679 C  CZ  . TYR C 1 1092 ? 5.922    59.730  98.931  1.00 93.77  ? 1092 TYR B CZ  1 
ATOM   22680 O  OH  . TYR C 1 1092 ? 6.477    59.129  100.042 1.00 92.98  ? 1092 TYR B OH  1 
ATOM   22681 N  N   . VAL C 1 1093 ? 1.391    63.026  94.437  1.00 107.08 ? 1093 VAL B N   1 
ATOM   22682 C  CA  . VAL C 1 1093 ? 0.674    63.664  93.339  1.00 107.86 ? 1093 VAL B CA  1 
ATOM   22683 C  C   . VAL C 1 1093 ? -0.721   64.092  93.811  1.00 105.73 ? 1093 VAL B C   1 
ATOM   22684 O  O   . VAL C 1 1093 ? -1.590   63.246  94.027  1.00 104.71 ? 1093 VAL B O   1 
ATOM   22685 C  CB  . VAL C 1 1093 ? 0.590    62.737  92.121  1.00 109.04 ? 1093 VAL B CB  1 
ATOM   22686 C  CG1 . VAL C 1 1093 ? -0.170   63.424  91.008  1.00 112.21 ? 1093 VAL B CG1 1 
ATOM   22687 C  CG2 . VAL C 1 1093 ? 1.998    62.308  91.655  1.00 108.10 ? 1093 VAL B CG2 1 
ATOM   22688 N  N   . GLU C 1 1094 ? -0.919   65.401  93.991  1.00 104.49 ? 1094 GLU B N   1 
ATOM   22689 C  CA  . GLU C 1 1094 ? -2.123   65.905  94.647  1.00 104.20 ? 1094 GLU B CA  1 
ATOM   22690 C  C   . GLU C 1 1094 ? -3.301   65.391  93.857  1.00 102.76 ? 1094 GLU B C   1 
ATOM   22691 O  O   . GLU C 1 1094 ? -3.275   65.437  92.641  1.00 106.17 ? 1094 GLU B O   1 
ATOM   22692 C  CB  . GLU C 1 1094 ? -2.104   67.430  94.673  1.00 109.58 ? 1094 GLU B CB  1 
ATOM   22693 C  CG  . GLU C 1 1094 ? -3.216   68.093  95.486  1.00 114.73 ? 1094 GLU B CG  1 
ATOM   22694 C  CD  . GLU C 1 1094 ? -3.191   69.635  95.384  1.00 122.25 ? 1094 GLU B CD  1 
ATOM   22695 O  OE1 . GLU C 1 1094 ? -2.337   70.190  94.651  1.00 124.71 ? 1094 GLU B OE1 1 
ATOM   22696 O  OE2 . GLU C 1 1094 ? -4.031   70.300  96.032  1.00 124.92 ? 1094 GLU B OE2 1 
ATOM   22697 N  N   . GLN C 1 1095 ? -4.311   64.837  94.505  1.00 99.47  ? 1095 GLN B N   1 
ATOM   22698 C  CA  . GLN C 1 1095 ? -5.466   64.404  93.741  1.00 100.49 ? 1095 GLN B CA  1 
ATOM   22699 C  C   . GLN C 1 1095 ? -6.564   65.402  94.020  1.00 106.36 ? 1095 GLN B C   1 
ATOM   22700 O  O   . GLN C 1 1095 ? -6.482   66.150  94.978  1.00 107.94 ? 1095 GLN B O   1 
ATOM   22701 C  CB  . GLN C 1 1095 ? -5.853   62.960  94.048  1.00 97.67  ? 1095 GLN B CB  1 
ATOM   22702 C  CG  . GLN C 1 1095 ? -4.657   61.986  93.937  1.00 99.13  ? 1095 GLN B CG  1 
ATOM   22703 C  CD  . GLN C 1 1095 ? -4.166   61.715  92.487  1.00 129.57 ? 1095 GLN B CD  1 
ATOM   22704 O  OE1 . GLN C 1 1095 ? -4.877   61.109  91.689  1.00 130.53 ? 1095 GLN B OE1 1 
ATOM   22705 N  NE2 . GLN C 1 1095 ? -2.936   62.125  92.169  1.00 128.85 ? 1095 GLN B NE2 1 
ATOM   22706 N  N   . ASN C 1 1096 ? -7.554   65.455  93.142  1.00 111.87 ? 1096 ASN B N   1 
ATOM   22707 C  CA  . ASN C 1 1096 ? -8.619   66.454  93.185  1.00 116.89 ? 1096 ASN B CA  1 
ATOM   22708 C  C   . ASN C 1 1096 ? -9.387   66.353  94.487  1.00 118.50 ? 1096 ASN B C   1 
ATOM   22709 O  O   . ASN C 1 1096 ? -9.928   65.299  94.801  1.00 116.88 ? 1096 ASN B O   1 
ATOM   22710 C  CB  . ASN C 1 1096 ? -9.542   66.205  91.984  1.00 121.80 ? 1096 ASN B CB  1 
ATOM   22711 C  CG  . ASN C 1 1096 ? -10.835  66.978  92.052  1.00 127.69 ? 1096 ASN B CG  1 
ATOM   22712 O  OD1 . ASN C 1 1096 ? -11.124  67.815  91.190  1.00 132.95 ? 1096 ASN B OD1 1 
ATOM   22713 N  ND2 . ASN C 1 1096 ? -11.639  66.682  93.051  1.00 127.95 ? 1096 ASN B ND2 1 
ATOM   22714 N  N   . GLN C 1 1097 ? -9.452   67.428  95.264  1.00 122.73 ? 1097 GLN B N   1 
ATOM   22715 C  CA  . GLN C 1 1097 ? -10.092  67.288  96.572  1.00 123.59 ? 1097 GLN B CA  1 
ATOM   22716 C  C   . GLN C 1 1097 ? -11.571  66.944  96.445  1.00 127.78 ? 1097 GLN B C   1 
ATOM   22717 O  O   . GLN C 1 1097 ? -12.009  65.872  96.855  1.00 124.44 ? 1097 GLN B O   1 
ATOM   22718 C  CB  . GLN C 1 1097 ? -9.891   68.520  97.452  1.00 124.34 ? 1097 GLN B CB  1 
ATOM   22719 C  CG  . GLN C 1 1097 ? -10.241  68.256  98.904  1.00 122.02 ? 1097 GLN B CG  1 
ATOM   22720 C  CD  . GLN C 1 1097 ? -10.274  69.516  99.751  1.00 124.29 ? 1097 GLN B CD  1 
ATOM   22721 O  OE1 . GLN C 1 1097 ? -9.923   70.610  99.294  1.00 126.06 ? 1097 GLN B OE1 1 
ATOM   22722 N  NE2 . GLN C 1 1097 ? -10.703  69.368  101.000 1.00 124.46 ? 1097 GLN B NE2 1 
ATOM   22723 N  N   . ASN C 1 1098 ? -12.324  67.859  95.846  1.00 133.66 ? 1098 ASN B N   1 
ATOM   22724 C  CA  . ASN C 1 1098 ? -13.758  67.679  95.600  1.00 138.23 ? 1098 ASN B CA  1 
ATOM   22725 C  C   . ASN C 1 1098 ? -14.183  66.250  95.148  1.00 122.15 ? 1098 ASN B C   1 
ATOM   22726 O  O   . ASN C 1 1098 ? -15.125  65.671  95.705  1.00 119.83 ? 1098 ASN B O   1 
ATOM   22727 C  CB  . ASN C 1 1098 ? -14.242  68.761  94.617  1.00 143.24 ? 1098 ASN B CB  1 
ATOM   22728 C  CG  . ASN C 1 1098 ? -15.705  68.604  94.233  1.00 148.59 ? 1098 ASN B CG  1 
ATOM   22729 O  OD1 . ASN C 1 1098 ? -16.024  68.228  93.108  1.00 150.61 ? 1098 ASN B OD1 1 
ATOM   22730 N  ND2 . ASN C 1 1098 ? -16.600  68.889  95.168  1.00 150.85 ? 1098 ASN B ND2 1 
ATOM   22731 N  N   . SER C 1 1099 ? -13.498  65.690  94.150  1.00 121.34 ? 1099 SER B N   1 
ATOM   22732 C  CA  . SER C 1 1099 ? -13.697  64.295  93.785  1.00 116.97 ? 1099 SER B CA  1 
ATOM   22733 C  C   . SER C 1 1099 ? -13.590  63.458  95.041  1.00 112.12 ? 1099 SER B C   1 
ATOM   22734 O  O   . SER C 1 1099 ? -14.574  62.910  95.508  1.00 114.12 ? 1099 SER B O   1 
ATOM   22735 C  CB  . SER C 1 1099 ? -12.650  63.827  92.767  1.00 114.63 ? 1099 SER B CB  1 
ATOM   22736 O  OG  . SER C 1 1099 ? -12.559  62.404  92.740  1.00 112.00 ? 1099 SER B OG  1 
ATOM   22737 N  N   . ILE C 1 1100 ? -12.395  63.398  95.613  1.00 105.26 ? 1100 ILE B N   1 
ATOM   22738 C  CA  . ILE C 1 1100 ? -12.135  62.486  96.717  1.00 98.34  ? 1100 ILE B CA  1 
ATOM   22739 C  C   . ILE C 1 1100 ? -13.134  62.634  97.858  1.00 100.84 ? 1100 ILE B C   1 
ATOM   22740 O  O   . ILE C 1 1100 ? -13.421  61.664  98.564  1.00 99.95  ? 1100 ILE B O   1 
ATOM   22741 C  CB  . ILE C 1 1100 ? -10.727  62.654  97.281  1.00 91.20  ? 1100 ILE B CB  1 
ATOM   22742 C  CG1 . ILE C 1 1100 ? -9.698   61.993  96.375  1.00 85.39  ? 1100 ILE B CG1 1 
ATOM   22743 C  CG2 . ILE C 1 1100 ? -10.640  61.975  98.619  1.00 89.14  ? 1100 ILE B CG2 1 
ATOM   22744 C  CD1 . ILE C 1 1100 ? -9.676   60.494  96.521  1.00 81.42  ? 1100 ILE B CD1 1 
ATOM   22745 N  N   . CYS C 1 1101 ? -13.648  63.847  98.052  1.00 103.84 ? 1101 CYS B N   1 
ATOM   22746 C  CA  . CYS C 1 1101 ? -14.645  64.089  99.101  1.00 104.63 ? 1101 CYS B CA  1 
ATOM   22747 C  C   . CYS C 1 1101 ? -15.894  63.259  98.810  1.00 104.19 ? 1101 CYS B C   1 
ATOM   22748 O  O   . CYS C 1 1101 ? -16.292  62.417  99.617  1.00 101.25 ? 1101 CYS B O   1 
ATOM   22749 C  CB  . CYS C 1 1101 ? -15.028  65.572  99.174  1.00 108.14 ? 1101 CYS B CB  1 
ATOM   22750 S  SG  . CYS C 1 1101 ? -13.976  66.597  100.228 1.00 132.73 ? 1101 CYS B SG  1 
ATOM   22751 N  N   . ASN C 1 1102 ? -16.488  63.500  97.638  1.00 105.11 ? 1102 ASN B N   1 
ATOM   22752 C  CA  . ASN C 1 1102 ? -17.695  62.808  97.194  1.00 104.08 ? 1102 ASN B CA  1 
ATOM   22753 C  C   . ASN C 1 1102 ? -17.516  61.307  97.021  1.00 102.11 ? 1102 ASN B C   1 
ATOM   22754 O  O   . ASN C 1 1102 ? -18.446  60.541  97.270  1.00 101.54 ? 1102 ASN B O   1 
ATOM   22755 C  CB  . ASN C 1 1102 ? -18.170  63.421  95.890  1.00 104.74 ? 1102 ASN B CB  1 
ATOM   22756 C  CG  . ASN C 1 1102 ? -18.750  64.776  96.091  1.00 105.67 ? 1102 ASN B CG  1 
ATOM   22757 O  OD1 . ASN C 1 1102 ? -19.364  65.037  97.122  1.00 107.16 ? 1102 ASN B OD1 1 
ATOM   22758 N  ND2 . ASN C 1 1102 ? -18.570  65.656  95.115  1.00 105.61 ? 1102 ASN B ND2 1 
ATOM   22759 N  N   . SER C 1 1103 ? -16.329  60.895  96.579  1.00 100.85 ? 1103 SER B N   1 
ATOM   22760 C  CA  . SER C 1 1103 ? -16.010  59.479  96.497  1.00 99.62  ? 1103 SER B CA  1 
ATOM   22761 C  C   . SER C 1 1103 ? -16.116  58.917  97.915  1.00 99.71  ? 1103 SER B C   1 
ATOM   22762 O  O   . SER C 1 1103 ? -16.743  57.877  98.110  1.00 99.40  ? 1103 SER B O   1 
ATOM   22763 C  CB  . SER C 1 1103 ? -14.599  59.240  95.923  1.00 97.58  ? 1103 SER B CB  1 
ATOM   22764 O  OG  . SER C 1 1103 ? -14.396  59.796  94.619  1.00 98.06  ? 1103 SER B OG  1 
ATOM   22765 N  N   . LEU C 1 1104 ? -15.514  59.622  98.892  1.00 101.01 ? 1104 LEU B N   1 
ATOM   22766 C  CA  . LEU C 1 1104 ? -15.585  59.283  100.325 1.00 101.08 ? 1104 LEU B CA  1 
ATOM   22767 C  C   . LEU C 1 1104 ? -17.012  59.378  100.848 1.00 106.96 ? 1104 LEU B C   1 
ATOM   22768 O  O   . LEU C 1 1104 ? -17.524  58.420  101.440 1.00 107.12 ? 1104 LEU B O   1 
ATOM   22769 C  CB  . LEU C 1 1104 ? -14.720  60.235  101.149 1.00 97.95  ? 1104 LEU B CB  1 
ATOM   22770 C  CG  . LEU C 1 1104 ? -13.247  59.916  101.380 1.00 94.19  ? 1104 LEU B CG  1 
ATOM   22771 C  CD1 . LEU C 1 1104 ? -12.541  61.058  102.110 1.00 94.38  ? 1104 LEU B CD1 1 
ATOM   22772 C  CD2 . LEU C 1 1104 ? -13.114  58.640  102.166 1.00 91.27  ? 1104 LEU B CD2 1 
ATOM   22773 N  N   . LEU C 1 1105 ? -17.630  60.546  100.620 1.00 112.53 ? 1105 LEU B N   1 
ATOM   22774 C  CA  . LEU C 1 1105 ? -19.008  60.870  101.037 1.00 115.46 ? 1105 LEU B CA  1 
ATOM   22775 C  C   . LEU C 1 1105 ? -20.051  59.939  100.433 1.00 117.43 ? 1105 LEU B C   1 
ATOM   22776 O  O   . LEU C 1 1105 ? -21.229  59.991  100.785 1.00 119.80 ? 1105 LEU B O   1 
ATOM   22777 C  CB  . LEU C 1 1105 ? -19.361  62.318  100.666 1.00 117.65 ? 1105 LEU B CB  1 
ATOM   22778 C  CG  . LEU C 1 1105 ? -18.846  63.428  101.592 1.00 119.69 ? 1105 LEU B CG  1 
ATOM   22779 C  CD1 . LEU C 1 1105 ? -18.451  64.697  100.813 1.00 121.44 ? 1105 LEU B CD1 1 
ATOM   22780 C  CD2 . LEU C 1 1105 ? -19.838  63.737  102.724 1.00 121.28 ? 1105 LEU B CD2 1 
ATOM   22781 N  N   . TRP C 1 1106 ? -19.614  59.097  99.511  1.00 115.84 ? 1106 TRP B N   1 
ATOM   22782 C  CA  . TRP C 1 1106 ? -20.508  58.162  98.877  1.00 116.35 ? 1106 TRP B CA  1 
ATOM   22783 C  C   . TRP C 1 1106 ? -20.651  56.934  99.746  1.00 116.17 ? 1106 TRP B C   1 
ATOM   22784 O  O   . TRP C 1 1106 ? -21.764  56.492  100.018 1.00 117.46 ? 1106 TRP B O   1 
ATOM   22785 C  CB  . TRP C 1 1106 ? -19.945  57.778  97.522  1.00 116.56 ? 1106 TRP B CB  1 
ATOM   22786 C  CG  . TRP C 1 1106 ? -20.767  56.792  96.784  1.00 116.20 ? 1106 TRP B CG  1 
ATOM   22787 C  CD1 . TRP C 1 1106 ? -21.843  57.050  96.007  1.00 116.75 ? 1106 TRP B CD1 1 
ATOM   22788 C  CD2 . TRP C 1 1106 ? -20.557  55.385  96.728  1.00 116.12 ? 1106 TRP B CD2 1 
ATOM   22789 N  NE1 . TRP C 1 1106 ? -22.324  55.894  95.472  1.00 116.79 ? 1106 TRP B NE1 1 
ATOM   22790 C  CE2 . TRP C 1 1106 ? -21.553  54.851  95.904  1.00 116.80 ? 1106 TRP B CE2 1 
ATOM   22791 C  CE3 . TRP C 1 1106 ? -19.619  54.522  97.300  1.00 116.75 ? 1106 TRP B CE3 1 
ATOM   22792 C  CZ2 . TRP C 1 1106 ? -21.651  53.490  95.633  1.00 119.21 ? 1106 TRP B CZ2 1 
ATOM   22793 C  CZ3 . TRP C 1 1106 ? -19.713  53.166  97.032  1.00 117.62 ? 1106 TRP B CZ3 1 
ATOM   22794 C  CH2 . TRP C 1 1106 ? -20.725  52.663  96.206  1.00 118.64 ? 1106 TRP B CH2 1 
ATOM   22795 N  N   . LEU C 1 1107 ? -19.522  56.377  100.176 1.00 114.30 ? 1107 LEU B N   1 
ATOM   22796 C  CA  . LEU C 1 1107 ? -19.558  55.143  100.941 1.00 114.82 ? 1107 LEU B CA  1 
ATOM   22797 C  C   . LEU C 1 1107 ? -20.344  55.398  102.199 1.00 120.72 ? 1107 LEU B C   1 
ATOM   22798 O  O   . LEU C 1 1107 ? -21.301  54.686  102.510 1.00 122.77 ? 1107 LEU B O   1 
ATOM   22799 C  CB  . LEU C 1 1107 ? -18.161  54.671  101.330 1.00 108.16 ? 1107 LEU B CB  1 
ATOM   22800 C  CG  . LEU C 1 1107 ? -17.223  54.152  100.257 1.00 103.39 ? 1107 LEU B CG  1 
ATOM   22801 C  CD1 . LEU C 1 1107 ? -16.275  55.250  99.941  1.00 102.44 ? 1107 LEU B CD1 1 
ATOM   22802 C  CD2 . LEU C 1 1107 ? -16.454  52.971  100.771 1.00 100.67 ? 1107 LEU B CD2 1 
ATOM   22803 N  N   . VAL C 1 1108 ? -19.934  56.444  102.905 1.00 123.85 ? 1108 VAL B N   1 
ATOM   22804 C  CA  . VAL C 1 1108 ? -20.402  56.694  104.259 1.00 126.67 ? 1108 VAL B CA  1 
ATOM   22805 C  C   . VAL C 1 1108 ? -21.864  57.145  104.351 1.00 131.35 ? 1108 VAL B C   1 
ATOM   22806 O  O   . VAL C 1 1108 ? -22.556  56.786  105.301 1.00 133.20 ? 1108 VAL B O   1 
ATOM   22807 C  CB  . VAL C 1 1108 ? -19.485  57.689  104.989 1.00 125.30 ? 1108 VAL B CB  1 
ATOM   22808 C  CG1 . VAL C 1 1108 ? -19.093  58.810  104.060 1.00 125.96 ? 1108 VAL B CG1 1 
ATOM   22809 C  CG2 . VAL C 1 1108 ? -20.178  58.231  106.202 1.00 126.44 ? 1108 VAL B CG2 1 
ATOM   22810 N  N   . GLU C 1 1109 ? -22.348  57.908  103.377 1.00 134.10 ? 1109 GLU B N   1 
ATOM   22811 C  CA  . GLU C 1 1109 ? -23.740  58.366  103.435 1.00 138.48 ? 1109 GLU B CA  1 
ATOM   22812 C  C   . GLU C 1 1109 ? -24.764  57.322  102.974 1.00 140.89 ? 1109 GLU B C   1 
ATOM   22813 O  O   . GLU C 1 1109 ? -25.922  57.370  103.385 1.00 143.12 ? 1109 GLU B O   1 
ATOM   22814 C  CB  . GLU C 1 1109 ? -23.936  59.672  102.661 1.00 140.91 ? 1109 GLU B CB  1 
ATOM   22815 C  CG  . GLU C 1 1109 ? -23.088  60.821  103.175 1.00 140.29 ? 1109 GLU B CG  1 
ATOM   22816 C  CD  . GLU C 1 1109 ? -23.434  62.144  102.527 1.00 141.21 ? 1109 GLU B CD  1 
ATOM   22817 O  OE1 . GLU C 1 1109 ? -22.508  62.858  102.095 1.00 140.02 ? 1109 GLU B OE1 1 
ATOM   22818 O  OE2 . GLU C 1 1109 ? -24.633  62.467  102.450 1.00 143.20 ? 1109 GLU B OE2 1 
ATOM   22819 N  N   . ASN C 1 1110 ? -24.343  56.388  102.124 1.00 139.71 ? 1110 ASN B N   1 
ATOM   22820 C  CA  . ASN C 1 1110 ? -25.266  55.400  101.565 1.00 140.12 ? 1110 ASN B CA  1 
ATOM   22821 C  C   . ASN C 1 1110 ? -25.016  53.968  102.043 1.00 137.85 ? 1110 ASN B C   1 
ATOM   22822 O  O   . ASN C 1 1110 ? -25.940  53.156  102.111 1.00 138.81 ? 1110 ASN B O   1 
ATOM   22823 C  CB  . ASN C 1 1110 ? -25.242  55.455  100.030 1.00 141.40 ? 1110 ASN B CB  1 
ATOM   22824 C  CG  . ASN C 1 1110 ? -25.478  56.860  99.483  1.00 144.10 ? 1110 ASN B CG  1 
ATOM   22825 O  OD1 . ASN C 1 1110 ? -24.549  57.518  99.010  1.00 143.76 ? 1110 ASN B OD1 1 
ATOM   22826 N  ND2 . ASN C 1 1110 ? -26.721  57.324  99.546  1.00 146.69 ? 1110 ASN B ND2 1 
ATOM   22827 N  N   . TYR C 1 1111 ? -23.776  53.670  102.408 1.00 134.60 ? 1111 TYR B N   1 
ATOM   22828 C  CA  . TYR C 1 1111 ? -23.359  52.282  102.544 1.00 133.97 ? 1111 TYR B CA  1 
ATOM   22829 C  C   . TYR C 1 1111 ? -22.745  51.887  103.890 1.00 133.59 ? 1111 TYR B C   1 
ATOM   22830 O  O   . TYR C 1 1111 ? -21.859  51.032  103.965 1.00 131.46 ? 1111 TYR B O   1 
ATOM   22831 C  CB  . TYR C 1 1111 ? -22.430  51.947  101.390 1.00 131.56 ? 1111 TYR B CB  1 
ATOM   22832 C  CG  . TYR C 1 1111 ? -23.192  51.908  100.093 1.00 132.56 ? 1111 TYR B CG  1 
ATOM   22833 C  CD1 . TYR C 1 1111 ? -23.665  50.703  99.590  1.00 133.94 ? 1111 TYR B CD1 1 
ATOM   22834 C  CD2 . TYR C 1 1111 ? -23.477  53.070  99.390  1.00 132.82 ? 1111 TYR B CD2 1 
ATOM   22835 C  CE1 . TYR C 1 1111 ? -24.383  50.646  98.424  1.00 135.13 ? 1111 TYR B CE1 1 
ATOM   22836 C  CE2 . TYR C 1 1111 ? -24.196  53.021  98.213  1.00 134.20 ? 1111 TYR B CE2 1 
ATOM   22837 C  CZ  . TYR C 1 1111 ? -24.644  51.799  97.742  1.00 135.75 ? 1111 TYR B CZ  1 
ATOM   22838 O  OH  . TYR C 1 1111 ? -25.362  51.696  96.583  1.00 138.16 ? 1111 TYR B OH  1 
ATOM   22839 N  N   . GLN C 1 1112 ? -23.248  52.503  104.951 1.00 135.95 ? 1112 GLN B N   1 
ATOM   22840 C  CA  . GLN C 1 1112 ? -22.843  52.172  106.305 1.00 136.20 ? 1112 GLN B CA  1 
ATOM   22841 C  C   . GLN C 1 1112 ? -24.109  51.897  107.082 1.00 142.36 ? 1112 GLN B C   1 
ATOM   22842 O  O   . GLN C 1 1112 ? -24.936  52.783  107.277 1.00 145.19 ? 1112 GLN B O   1 
ATOM   22843 C  CB  . GLN C 1 1112 ? -22.089  53.340  106.942 1.00 132.85 ? 1112 GLN B CB  1 
ATOM   22844 C  CG  . GLN C 1 1112 ? -21.679  53.120  108.404 1.00 129.38 ? 1112 GLN B CG  1 
ATOM   22845 C  CD  . GLN C 1 1112 ? -20.715  54.192  108.908 1.00 126.46 ? 1112 GLN B CD  1 
ATOM   22846 O  OE1 . GLN C 1 1112 ? -20.917  55.381  108.662 1.00 127.12 ? 1112 GLN B OE1 1 
ATOM   22847 N  NE2 . GLN C 1 1112 ? -19.662  53.773  109.613 1.00 122.95 ? 1112 GLN B NE2 1 
ATOM   22848 N  N   . LEU C 1 1113 ? -24.261  50.654  107.510 1.00 145.20 ? 1113 LEU B N   1 
ATOM   22849 C  CA  . LEU C 1 1113 ? -25.456  50.220  108.205 1.00 148.57 ? 1113 LEU B CA  1 
ATOM   22850 C  C   . LEU C 1 1113 ? -25.586  50.888  109.574 1.00 151.57 ? 1113 LEU B C   1 
ATOM   22851 O  O   . LEU C 1 1113 ? -24.628  51.464  110.091 1.00 149.20 ? 1113 LEU B O   1 
ATOM   22852 C  CB  . LEU C 1 1113 ? -25.445  48.697  108.340 1.00 146.92 ? 1113 LEU B CB  1 
ATOM   22853 C  CG  . LEU C 1 1113 ? -25.430  47.928  107.017 1.00 144.59 ? 1113 LEU B CG  1 
ATOM   22854 C  CD1 . LEU C 1 1113 ? -24.627  46.644  107.142 1.00 142.79 ? 1113 LEU B CD1 1 
ATOM   22855 C  CD2 . LEU C 1 1113 ? -26.846  47.643  106.548 1.00 146.46 ? 1113 LEU B CD2 1 
ATOM   22856 N  N   . ASP C 1 1114 ? -26.788  50.806  110.142 1.00 156.55 ? 1114 ASP B N   1 
ATOM   22857 C  CA  . ASP C 1 1114 ? -27.087  51.383  111.448 1.00 159.35 ? 1114 ASP B CA  1 
ATOM   22858 C  C   . ASP C 1 1114 ? -26.403  50.626  112.565 1.00 156.65 ? 1114 ASP B C   1 
ATOM   22859 O  O   . ASP C 1 1114 ? -26.929  50.526  113.671 1.00 158.03 ? 1114 ASP B O   1 
ATOM   22860 C  CB  . ASP C 1 1114 ? -28.594  51.425  111.693 1.00 166.86 ? 1114 ASP B CB  1 
ATOM   22861 C  CG  . ASP C 1 1114 ? -29.202  52.756  111.310 1.00 172.59 ? 1114 ASP B CG  1 
ATOM   22862 O  OD1 . ASP C 1 1114 ? -28.520  53.791  111.504 1.00 173.00 ? 1114 ASP B OD1 1 
ATOM   22863 O  OD2 . ASP C 1 1114 ? -30.354  52.771  110.821 1.00 176.50 ? 1114 ASP B OD2 1 
ATOM   22864 N  N   . ASN C 1 1115 ? -25.232  50.084  112.259 1.00 152.16 ? 1115 ASN B N   1 
ATOM   22865 C  CA  . ASN C 1 1115 ? -24.364  49.486  113.261 1.00 147.48 ? 1115 ASN B CA  1 
ATOM   22866 C  C   . ASN C 1 1115 ? -22.955  49.981  113.030 1.00 139.04 ? 1115 ASN B C   1 
ATOM   22867 O  O   . ASN C 1 1115 ? -22.072  49.760  113.837 1.00 134.94 ? 1115 ASN B O   1 
ATOM   22868 C  CB  . ASN C 1 1115 ? -24.437  47.946  113.233 1.00 150.24 ? 1115 ASN B CB  1 
ATOM   22869 C  CG  . ASN C 1 1115 ? -23.960  47.342  111.910 1.00 150.58 ? 1115 ASN B CG  1 
ATOM   22870 O  OD1 . ASN C 1 1115 ? -23.960  46.120  111.740 1.00 150.72 ? 1115 ASN B OD1 1 
ATOM   22871 N  ND2 . ASN C 1 1115 ? -23.552  48.195  110.974 1.00 149.69 ? 1115 ASN B ND2 1 
ATOM   22872 N  N   . GLY C 1 1116 ? -22.762  50.671  111.917 1.00 135.38 ? 1116 GLY B N   1 
ATOM   22873 C  CA  . GLY C 1 1116 ? -21.454  51.155  111.549 1.00 130.61 ? 1116 GLY B CA  1 
ATOM   22874 C  C   . GLY C 1 1116 ? -20.724  50.296  110.540 1.00 123.57 ? 1116 GLY B C   1 
ATOM   22875 O  O   . GLY C 1 1116 ? -19.689  50.709  110.052 1.00 123.10 ? 1116 GLY B O   1 
ATOM   22876 N  N   . SER C 1 1117 ? -21.235  49.107  110.234 1.00 120.96 ? 1117 SER B N   1 
ATOM   22877 C  CA  . SER C 1 1117 ? -20.610  48.262  109.208 1.00 118.71 ? 1117 SER B CA  1 
ATOM   22878 C  C   . SER C 1 1117 ? -21.015  48.727  107.799 1.00 120.46 ? 1117 SER B C   1 
ATOM   22879 O  O   . SER C 1 1117 ? -21.979  49.476  107.648 1.00 123.81 ? 1117 SER B O   1 
ATOM   22880 C  CB  . SER C 1 1117 ? -20.934  46.772  109.417 1.00 118.50 ? 1117 SER B CB  1 
ATOM   22881 O  OG  . SER C 1 1117 ? -22.268  46.451  109.053 1.00 120.32 ? 1117 SER B OG  1 
ATOM   22882 N  N   . PHE C 1 1118 ? -20.278  48.307  106.772 1.00 117.73 ? 1118 PHE B N   1 
ATOM   22883 C  CA  . PHE C 1 1118 ? -20.537  48.778  105.416 1.00 115.59 ? 1118 PHE B CA  1 
ATOM   22884 C  C   . PHE C 1 1118 ? -21.155  47.708  104.516 1.00 115.56 ? 1118 PHE B C   1 
ATOM   22885 O  O   . PHE C 1 1118 ? -20.692  46.584  104.495 1.00 114.81 ? 1118 PHE B O   1 
ATOM   22886 C  CB  . PHE C 1 1118 ? -19.231  49.284  104.817 1.00 114.75 ? 1118 PHE B CB  1 
ATOM   22887 C  CG  . PHE C 1 1118 ? -18.912  50.701  105.188 1.00 115.05 ? 1118 PHE B CG  1 
ATOM   22888 C  CD1 . PHE C 1 1118 ? -18.924  51.105  106.503 1.00 114.43 ? 1118 PHE B CD1 1 
ATOM   22889 C  CD2 . PHE C 1 1118 ? -18.607  51.638  104.216 1.00 115.63 ? 1118 PHE B CD2 1 
ATOM   22890 C  CE1 . PHE C 1 1118 ? -18.639  52.421  106.844 1.00 113.85 ? 1118 PHE B CE1 1 
ATOM   22891 C  CE2 . PHE C 1 1118 ? -18.318  52.954  104.559 1.00 114.65 ? 1118 PHE B CE2 1 
ATOM   22892 C  CZ  . PHE C 1 1118 ? -18.336  53.341  105.870 1.00 113.62 ? 1118 PHE B CZ  1 
ATOM   22893 N  N   . LYS C 1 1119 ? -22.208  48.043  103.778 1.00 116.80 ? 1119 LYS B N   1 
ATOM   22894 C  CA  . LYS C 1 1119 ? -22.785  47.069  102.845 1.00 117.22 ? 1119 LYS B CA  1 
ATOM   22895 C  C   . LYS C 1 1119 ? -22.151  47.199  101.488 1.00 115.81 ? 1119 LYS B C   1 
ATOM   22896 O  O   . LYS C 1 1119 ? -21.859  48.299  101.050 1.00 114.14 ? 1119 LYS B O   1 
ATOM   22897 C  CB  . LYS C 1 1119 ? -24.329  47.171  102.730 1.00 129.92 ? 1119 LYS B CB  1 
ATOM   22898 C  CG  . LYS C 1 1119 ? -24.959  48.600  102.673 1.00 138.30 ? 1119 LYS B CG  1 
ATOM   22899 C  CD  . LYS C 1 1119 ? -26.447  48.588  102.151 1.00 168.99 ? 1119 LYS B CD  1 
ATOM   22900 C  CE  . LYS C 1 1119 ? -27.532  48.722  103.247 1.00 169.56 ? 1119 LYS B CE  1 
ATOM   22901 N  NZ  . LYS C 1 1119 ? -28.031  50.118  103.447 1.00 169.52 ? 1119 LYS B NZ  1 
ATOM   22902 N  N   . GLU C 1 1120 ? -21.925  46.080  100.818 1.00 117.32 ? 1120 GLU B N   1 
ATOM   22903 C  CA  . GLU C 1 1120 ? -21.517  46.179  99.425  1.00 121.03 ? 1120 GLU B CA  1 
ATOM   22904 C  C   . GLU C 1 1120 ? -22.778  46.351  98.596  1.00 124.51 ? 1120 GLU B C   1 
ATOM   22905 O  O   . GLU C 1 1120 ? -23.822  45.805  98.940  1.00 127.72 ? 1120 GLU B O   1 
ATOM   22906 C  CB  . GLU C 1 1120 ? -20.684  44.971  98.973  1.00 120.35 ? 1120 GLU B CB  1 
ATOM   22907 C  CG  . GLU C 1 1120 ? -20.369  44.896  97.448  1.00 122.06 ? 1120 GLU B CG  1 
ATOM   22908 C  CD  . GLU C 1 1120 ? -19.737  46.156  96.834  1.00 119.69 ? 1120 GLU B CD  1 
ATOM   22909 O  OE1 . GLU C 1 1120 ? -18.498  46.207  96.665  1.00 117.53 ? 1120 GLU B OE1 1 
ATOM   22910 O  OE2 . GLU C 1 1120 ? -20.488  47.084  96.491  1.00 119.79 ? 1120 GLU B OE2 1 
ATOM   22911 N  N   . ASN C 1 1121 ? -22.676  47.142  97.532  1.00 125.38 ? 1121 ASN B N   1 
ATOM   22912 C  CA  . ASN C 1 1121 ? -23.791  47.447  96.645  1.00 128.62 ? 1121 ASN B CA  1 
ATOM   22913 C  C   . ASN C 1 1121 ? -23.996  46.395  95.555  1.00 133.24 ? 1121 ASN B C   1 
ATOM   22914 O  O   . ASN C 1 1121 ? -24.972  45.635  95.585  1.00 135.61 ? 1121 ASN B O   1 
ATOM   22915 C  CB  . ASN C 1 1121 ? -23.554  48.809  95.993  1.00 126.08 ? 1121 ASN B CB  1 
ATOM   22916 C  CG  . ASN C 1 1121 ? -24.583  49.143  94.935  1.00 123.92 ? 1121 ASN B CG  1 
ATOM   22917 O  OD1 . ASN C 1 1121 ? -25.772  49.226  95.232  1.00 125.50 ? 1121 ASN B OD1 1 
ATOM   22918 N  ND2 . ASN C 1 1121 ? -24.130  49.363  93.703  1.00 120.45 ? 1121 ASN B ND2 1 
ATOM   22919 N  N   . SER C 1 1122 ? -23.072  46.361  94.594  1.00 135.38 ? 1122 SER B N   1 
ATOM   22920 C  CA  . SER C 1 1122 ? -23.141  45.423  93.482  1.00 137.74 ? 1122 SER B CA  1 
ATOM   22921 C  C   . SER C 1 1122 ? -22.964  43.985  93.952  1.00 141.80 ? 1122 SER B C   1 
ATOM   22922 O  O   . SER C 1 1122 ? -22.758  43.709  95.135  1.00 141.70 ? 1122 SER B O   1 
ATOM   22923 C  CB  . SER C 1 1122 ? -22.051  45.728  92.470  1.00 134.53 ? 1122 SER B CB  1 
ATOM   22924 O  OG  . SER C 1 1122 ? -20.849  45.108  92.872  1.00 130.76 ? 1122 SER B OG  1 
ATOM   22925 N  N   . GLN C 1 1123 ? -23.032  43.062  93.007  1.00 144.65 ? 1123 GLN B N   1 
ATOM   22926 C  CA  . GLN C 1 1123 ? -22.926  41.654  93.336  1.00 147.76 ? 1123 GLN B CA  1 
ATOM   22927 C  C   . GLN C 1 1123 ? -21.471  41.184  93.449  1.00 139.97 ? 1123 GLN B C   1 
ATOM   22928 O  O   . GLN C 1 1123 ? -21.214  40.050  93.862  1.00 140.28 ? 1123 GLN B O   1 
ATOM   22929 C  CB  . GLN C 1 1123 ? -23.707  40.813  92.316  1.00 159.02 ? 1123 GLN B CB  1 
ATOM   22930 C  CG  . GLN C 1 1123 ? -25.172  41.220  92.210  1.00 169.85 ? 1123 GLN B CG  1 
ATOM   22931 C  CD  . GLN C 1 1123 ? -26.058  40.159  91.571  1.00 181.08 ? 1123 GLN B CD  1 
ATOM   22932 O  OE1 . GLN C 1 1123 ? -26.060  38.994  91.974  1.00 184.40 ? 1123 GLN B OE1 1 
ATOM   22933 N  NE2 . GLN C 1 1123 ? -26.844  40.572  90.584  1.00 186.27 ? 1123 GLN B NE2 1 
ATOM   22934 N  N   . TYR C 1 1124 ? -20.522  42.053  93.106  1.00 131.34 ? 1124 TYR B N   1 
ATOM   22935 C  CA  . TYR C 1 1124 ? -19.124  41.640  93.024  1.00 122.92 ? 1124 TYR B CA  1 
ATOM   22936 C  C   . TYR C 1 1124 ? -18.679  40.922  94.274  1.00 119.21 ? 1124 TYR B C   1 
ATOM   22937 O  O   . TYR C 1 1124 ? -18.628  41.509  95.344  1.00 117.12 ? 1124 TYR B O   1 
ATOM   22938 C  CB  . TYR C 1 1124 ? -18.210  42.833  92.812  1.00 115.51 ? 1124 TYR B CB  1 
ATOM   22939 C  CG  . TYR C 1 1124 ? -16.739  42.486  92.643  1.00 109.19 ? 1124 TYR B CG  1 
ATOM   22940 C  CD1 . TYR C 1 1124 ? -16.214  42.147  91.397  1.00 108.05 ? 1124 TYR B CD1 1 
ATOM   22941 C  CD2 . TYR C 1 1124 ? -15.866  42.519  93.720  1.00 104.93 ? 1124 TYR B CD2 1 
ATOM   22942 C  CE1 . TYR C 1 1124 ? -14.843  41.846  91.232  1.00 104.42 ? 1124 TYR B CE1 1 
ATOM   22943 C  CE2 . TYR C 1 1124 ? -14.496  42.220  93.571  1.00 100.89 ? 1124 TYR B CE2 1 
ATOM   22944 C  CZ  . TYR C 1 1124 ? -13.984  41.886  92.328  1.00 98.78  ? 1124 TYR B CZ  1 
ATOM   22945 O  OH  . TYR C 1 1124 ? -12.627  41.608  92.184  1.00 91.32  ? 1124 TYR B OH  1 
ATOM   22946 N  N   . GLN C 1 1125 ? -18.372  39.641  94.129  1.00 119.37 ? 1125 GLN B N   1 
ATOM   22947 C  CA  . GLN C 1 1125 ? -17.763  38.875  95.196  1.00 118.21 ? 1125 GLN B CA  1 
ATOM   22948 C  C   . GLN C 1 1125 ? -16.274  38.997  95.027  1.00 108.77 ? 1125 GLN B C   1 
ATOM   22949 O  O   . GLN C 1 1125 ? -15.742  38.537  94.030  1.00 105.87 ? 1125 GLN B O   1 
ATOM   22950 C  CB  . GLN C 1 1125 ? -18.152  37.411  95.069  1.00 127.46 ? 1125 GLN B CB  1 
ATOM   22951 C  CG  . GLN C 1 1125 ? -19.607  37.137  95.383  1.00 137.31 ? 1125 GLN B CG  1 
ATOM   22952 C  CD  . GLN C 1 1125 ? -19.917  37.262  96.874  1.00 143.13 ? 1125 GLN B CD  1 
ATOM   22953 O  OE1 . GLN C 1 1125 ? -19.472  38.211  97.541  1.00 142.57 ? 1125 GLN B OE1 1 
ATOM   22954 N  NE2 . GLN C 1 1125 ? -20.683  36.296  97.408  1.00 147.16 ? 1125 GLN B NE2 1 
ATOM   22955 N  N   . PRO C 1 1126 ? -15.591  39.614  95.996  1.00 106.20 ? 1126 PRO B N   1 
ATOM   22956 C  CA  . PRO C 1 1126 ? -14.166  39.836  95.781  1.00 104.07 ? 1126 PRO B CA  1 
ATOM   22957 C  C   . PRO C 1 1126 ? -13.407  38.641  96.308  1.00 107.70 ? 1126 PRO B C   1 
ATOM   22958 O  O   . PRO C 1 1126 ? -12.556  38.102  95.596  1.00 109.64 ? 1126 PRO B O   1 
ATOM   22959 C  CB  . PRO C 1 1126 ? -13.874  41.069  96.634  1.00 101.16 ? 1126 PRO B CB  1 
ATOM   22960 C  CG  . PRO C 1 1126 ? -15.208  41.422  97.321  1.00 102.62 ? 1126 PRO B CG  1 
ATOM   22961 C  CD  . PRO C 1 1126 ? -16.025  40.171  97.281  1.00 104.47 ? 1126 PRO B CD  1 
ATOM   22962 N  N   . ILE C 1 1127 ? -13.702  38.244  97.547  1.00 109.24 ? 1127 ILE B N   1 
ATOM   22963 C  CA  . ILE C 1 1127 ? -13.154  37.009  98.134  1.00 111.15 ? 1127 ILE B CA  1 
ATOM   22964 C  C   . ILE C 1 1127 ? -14.251  35.979  98.357  1.00 114.31 ? 1127 ILE B C   1 
ATOM   22965 O  O   . ILE C 1 1127 ? -15.435  36.309  98.438  1.00 114.34 ? 1127 ILE B O   1 
ATOM   22966 C  CB  . ILE C 1 1127 ? -12.352  37.217  99.494  1.00 115.05 ? 1127 ILE B CB  1 
ATOM   22967 C  CG1 . ILE C 1 1127 ? -12.796  38.478  100.227 1.00 113.71 ? 1127 ILE B CG1 1 
ATOM   22968 C  CG2 . ILE C 1 1127 ? -10.855  37.303  99.258  1.00 113.83 ? 1127 ILE B CG2 1 
ATOM   22969 C  CD1 . ILE C 1 1127 ? -14.305  38.630  100.323 1.00 116.18 ? 1127 ILE B CD1 1 
ATOM   22970 N  N   . LYS C 1 1128 ? -13.839  34.725  98.424  1.00 117.21 ? 1128 LYS B N   1 
ATOM   22971 C  CA  . LYS C 1 1128 ? -14.677  33.675  98.957  1.00 122.17 ? 1128 LYS B CA  1 
ATOM   22972 C  C   . LYS C 1 1128 ? -14.124  33.394  100.338 1.00 127.10 ? 1128 LYS B C   1 
ATOM   22973 O  O   . LYS C 1 1128 ? -12.955  33.012  100.460 1.00 127.62 ? 1128 LYS B O   1 
ATOM   22974 C  CB  . LYS C 1 1128 ? -14.525  32.435  98.089  1.00 122.47 ? 1128 LYS B CB  1 
ATOM   22975 C  CG  . LYS C 1 1128 ? -14.990  31.138  98.721  1.00 123.33 ? 1128 LYS B CG  1 
ATOM   22976 C  CD  . LYS C 1 1128 ? -16.476  30.865  98.502  1.00 124.37 ? 1128 LYS B CD  1 
ATOM   22977 C  CE  . LYS C 1 1128 ? -17.362  31.630  99.478  1.00 122.34 ? 1128 LYS B CE  1 
ATOM   22978 N  NZ  . LYS C 1 1128 ? -18.690  30.960  99.645  1.00 123.90 ? 1128 LYS B NZ  1 
ATOM   22979 N  N   . LEU C 1 1129 ? -14.920  33.608  101.385 1.00 131.46 ? 1129 LEU B N   1 
ATOM   22980 C  CA  . LEU C 1 1129 ? -14.451  33.277  102.743 1.00 133.75 ? 1129 LEU B CA  1 
ATOM   22981 C  C   . LEU C 1 1129 ? -14.997  31.908  103.179 1.00 141.79 ? 1129 LEU B C   1 
ATOM   22982 O  O   . LEU C 1 1129 ? -15.944  31.399  102.580 1.00 145.55 ? 1129 LEU B O   1 
ATOM   22983 C  CB  . LEU C 1 1129 ? -14.836  34.362  103.768 1.00 129.74 ? 1129 LEU B CB  1 
ATOM   22984 C  CG  . LEU C 1 1129 ? -14.584  35.849  103.479 1.00 125.74 ? 1129 LEU B CG  1 
ATOM   22985 C  CD1 . LEU C 1 1129 ? -14.956  36.693  104.682 1.00 123.63 ? 1129 LEU B CD1 1 
ATOM   22986 C  CD2 . LEU C 1 1129 ? -13.150  36.116  103.068 1.00 123.16 ? 1129 LEU B CD2 1 
ATOM   22987 N  N   . GLN C 1 1130 ? -14.406  31.299  104.203 1.00 142.31 ? 1130 GLN B N   1 
ATOM   22988 C  CA  . GLN C 1 1130 ? -14.941  30.038  104.694 1.00 145.22 ? 1130 GLN B CA  1 
ATOM   22989 C  C   . GLN C 1 1130 ? -16.059  30.330  105.668 1.00 140.17 ? 1130 GLN B C   1 
ATOM   22990 O  O   . GLN C 1 1130 ? -16.157  31.433  106.193 1.00 135.32 ? 1130 GLN B O   1 
ATOM   22991 C  CB  . GLN C 1 1130 ? -13.865  29.219  105.391 1.00 151.98 ? 1130 GLN B CB  1 
ATOM   22992 C  CG  . GLN C 1 1130 ? -12.454  29.424  104.866 1.00 155.48 ? 1130 GLN B CG  1 
ATOM   22993 C  CD  . GLN C 1 1130 ? -11.487  28.390  105.427 1.00 160.08 ? 1130 GLN B CD  1 
ATOM   22994 O  OE1 . GLN C 1 1130 ? -11.881  27.250  105.707 1.00 164.24 ? 1130 GLN B OE1 1 
ATOM   22995 N  NE2 . GLN C 1 1130 ? -10.222  28.781  105.603 1.00 158.40 ? 1130 GLN B NE2 1 
ATOM   22996 N  N   . GLY C 1 1131 ? -16.903  29.342  105.914 1.00 141.46 ? 1131 GLY B N   1 
ATOM   22997 C  CA  . GLY C 1 1131 ? -17.970  29.515  106.874 1.00 144.13 ? 1131 GLY B CA  1 
ATOM   22998 C  C   . GLY C 1 1131 ? -19.292  28.893  106.470 1.00 148.47 ? 1131 GLY B C   1 
ATOM   22999 O  O   . GLY C 1 1131 ? -19.445  28.356  105.371 1.00 153.26 ? 1131 GLY B O   1 
ATOM   23000 N  N   . THR C 1 1132 ? -20.257  28.959  107.380 1.00 149.05 ? 1132 THR B N   1 
ATOM   23001 C  CA  . THR C 1 1132 ? -21.610  28.502  107.111 1.00 149.84 ? 1132 THR B CA  1 
ATOM   23002 C  C   . THR C 1 1132 ? -22.336  29.627  106.408 1.00 146.73 ? 1132 THR B C   1 
ATOM   23003 O  O   . THR C 1 1132 ? -21.900  30.757  106.467 1.00 143.16 ? 1132 THR B O   1 
ATOM   23004 C  CB  . THR C 1 1132 ? -22.338  28.198  108.416 1.00 152.69 ? 1132 THR B CB  1 
ATOM   23005 O  OG1 . THR C 1 1132 ? -21.385  27.973  109.471 1.00 151.98 ? 1132 THR B OG1 1 
ATOM   23006 C  CG2 . THR C 1 1132 ? -23.232  26.972  108.242 1.00 158.32 ? 1132 THR B CG2 1 
ATOM   23007 N  N   . LEU C 1 1133 ? -23.447  29.355  105.752 1.00 150.15 ? 1133 LEU B N   1 
ATOM   23008 C  CA  . LEU C 1 1133 ? -24.111  30.451  105.076 1.00 152.96 ? 1133 LEU B CA  1 
ATOM   23009 C  C   . LEU C 1 1133 ? -24.287  31.691  105.944 1.00 155.02 ? 1133 LEU B C   1 
ATOM   23010 O  O   . LEU C 1 1133 ? -24.195  32.800  105.439 1.00 157.29 ? 1133 LEU B O   1 
ATOM   23011 C  CB  . LEU C 1 1133 ? -25.430  30.019  104.455 1.00 154.88 ? 1133 LEU B CB  1 
ATOM   23012 C  CG  . LEU C 1 1133 ? -25.205  29.506  103.033 1.00 153.30 ? 1133 LEU B CG  1 
ATOM   23013 C  CD1 . LEU C 1 1133 ? -24.592  28.109  103.072 1.00 154.16 ? 1133 LEU B CD1 1 
ATOM   23014 C  CD2 . LEU C 1 1133 ? -26.491  29.529  102.202 1.00 154.11 ? 1133 LEU B CD2 1 
ATOM   23015 N  N   . PRO C 1 1134 ? -24.541  31.508  107.247 1.00 156.04 ? 1134 PRO B N   1 
ATOM   23016 C  CA  . PRO C 1 1134 ? -24.636  32.579  108.251 1.00 155.65 ? 1134 PRO B CA  1 
ATOM   23017 C  C   . PRO C 1 1134 ? -23.277  33.163  108.629 1.00 155.65 ? 1134 PRO B C   1 
ATOM   23018 O  O   . PRO C 1 1134 ? -23.069  34.378  108.526 1.00 153.09 ? 1134 PRO B O   1 
ATOM   23019 C  CB  . PRO C 1 1134 ? -25.204  31.857  109.477 1.00 157.13 ? 1134 PRO B CB  1 
ATOM   23020 C  CG  . PRO C 1 1134 ? -25.827  30.639  108.944 1.00 160.30 ? 1134 PRO B CG  1 
ATOM   23021 C  CD  . PRO C 1 1134 ? -24.982  30.224  107.798 1.00 158.83 ? 1134 PRO B CD  1 
ATOM   23022 N  N   . VAL C 1 1135 ? -22.376  32.294  109.092 1.00 157.27 ? 1135 VAL B N   1 
ATOM   23023 C  CA  . VAL C 1 1135 ? -20.994  32.662  109.380 1.00 153.18 ? 1135 VAL B CA  1 
ATOM   23024 C  C   . VAL C 1 1135 ? -20.454  33.559  108.281 1.00 150.27 ? 1135 VAL B C   1 
ATOM   23025 O  O   . VAL C 1 1135 ? -20.118  34.713  108.519 1.00 147.77 ? 1135 VAL B O   1 
ATOM   23026 C  CB  . VAL C 1 1135 ? -20.107  31.421  109.423 1.00 153.01 ? 1135 VAL B CB  1 
ATOM   23027 C  CG1 . VAL C 1 1135 ? -18.675  31.793  109.107 1.00 149.85 ? 1135 VAL B CG1 1 
ATOM   23028 C  CG2 . VAL C 1 1135 ? -20.220  30.719  110.769 1.00 154.67 ? 1135 VAL B CG2 1 
ATOM   23029 N  N   . GLU C 1 1136 ? -20.392  33.017  107.070 1.00 150.28 ? 1136 GLU B N   1 
ATOM   23030 C  CA  . GLU C 1 1136 ? -19.923  33.763  105.916 1.00 147.49 ? 1136 GLU B CA  1 
ATOM   23031 C  C   . GLU C 1 1136 ? -20.409  35.200  105.956 1.00 148.09 ? 1136 GLU B C   1 
ATOM   23032 O  O   . GLU C 1 1136 ? -19.607  36.117  106.091 1.00 146.99 ? 1136 GLU B O   1 
ATOM   23033 C  CB  . GLU C 1 1136 ? -20.372  33.096  104.618 1.00 147.14 ? 1136 GLU B CB  1 
ATOM   23034 C  CG  . GLU C 1 1136 ? -20.012  33.896  103.393 1.00 144.91 ? 1136 GLU B CG  1 
ATOM   23035 C  CD  . GLU C 1 1136 ? -19.714  33.021  102.210 1.00 145.64 ? 1136 GLU B CD  1 
ATOM   23036 O  OE1 . GLU C 1 1136 ? -20.247  31.897  102.180 1.00 146.36 ? 1136 GLU B OE1 1 
ATOM   23037 O  OE2 . GLU C 1 1136 ? -18.949  33.461  101.320 1.00 145.06 ? 1136 GLU B OE2 1 
ATOM   23038 N  N   . ALA C 1 1137 ? -21.717  35.402  105.863 1.00 149.77 ? 1137 ALA B N   1 
ATOM   23039 C  CA  . ALA C 1 1137 ? -22.259  36.757  105.842 1.00 150.17 ? 1137 ALA B CA  1 
ATOM   23040 C  C   . ALA C 1 1137 ? -21.706  37.593  107.000 1.00 148.14 ? 1137 ALA B C   1 
ATOM   23041 O  O   . ALA C 1 1137 ? -21.371  38.772  106.844 1.00 145.74 ? 1137 ALA B O   1 
ATOM   23042 C  CB  . ALA C 1 1137 ? -23.779  36.727  105.868 1.00 153.16 ? 1137 ALA B CB  1 
ATOM   23043 N  N   . ARG C 1 1138 ? -21.600  36.975  108.165 1.00 148.50 ? 1138 ARG B N   1 
ATOM   23044 C  CA  . ARG C 1 1138 ? -20.977  37.645  109.286 1.00 147.71 ? 1138 ARG B CA  1 
ATOM   23045 C  C   . ARG C 1 1138 ? -19.570  38.034  108.849 1.00 140.63 ? 1138 ARG B C   1 
ATOM   23046 O  O   . ARG C 1 1138 ? -19.278  39.210  108.669 1.00 138.09 ? 1138 ARG B O   1 
ATOM   23047 C  CB  . ARG C 1 1138 ? -20.970  36.725  110.516 1.00 153.19 ? 1138 ARG B CB  1 
ATOM   23048 C  CG  . ARG C 1 1138 ? -20.425  37.360  111.780 1.00 156.21 ? 1138 ARG B CG  1 
ATOM   23049 C  CD  . ARG C 1 1138 ? -21.081  36.805  113.039 1.00 161.54 ? 1138 ARG B CD  1 
ATOM   23050 N  NE  . ARG C 1 1138 ? -20.690  37.595  114.207 1.00 164.49 ? 1138 ARG B NE  1 
ATOM   23051 C  CZ  . ARG C 1 1138 ? -21.266  37.532  115.405 1.00 168.38 ? 1138 ARG B CZ  1 
ATOM   23052 N  NH1 . ARG C 1 1138 ? -22.280  36.706  115.618 1.00 171.49 ? 1138 ARG B NH1 1 
ATOM   23053 N  NH2 . ARG C 1 1138 ? -20.825  38.303  116.394 1.00 168.16 ? 1138 ARG B NH2 1 
ATOM   23054 N  N   . GLU C 1 1139 ? -18.728  37.028  108.640 1.00 137.12 ? 1139 GLU B N   1 
ATOM   23055 C  CA  . GLU C 1 1139 ? -17.355  37.203  108.184 1.00 131.78 ? 1139 GLU B CA  1 
ATOM   23056 C  C   . GLU C 1 1139 ? -17.258  38.222  107.074 1.00 130.00 ? 1139 GLU B C   1 
ATOM   23057 O  O   . GLU C 1 1139 ? -16.541  39.218  107.159 1.00 128.99 ? 1139 GLU B O   1 
ATOM   23058 C  CB  . GLU C 1 1139 ? -16.855  35.890  107.599 1.00 128.95 ? 1139 GLU B CB  1 
ATOM   23059 C  CG  . GLU C 1 1139 ? -16.319  34.911  108.582 1.00 127.00 ? 1139 GLU B CG  1 
ATOM   23060 C  CD  . GLU C 1 1139 ? -14.976  35.312  109.104 1.00 123.53 ? 1139 GLU B CD  1 
ATOM   23061 O  OE1 . GLU C 1 1139 ? -13.996  34.608  108.797 1.00 123.84 ? 1139 GLU B OE1 1 
ATOM   23062 O  OE2 . GLU C 1 1139 ? -14.904  36.330  109.816 1.00 120.73 ? 1139 GLU B OE2 1 
ATOM   23063 N  N   . ASN C 1 1140 ? -17.970  37.925  106.003 1.00 131.83 ? 1140 ASN B N   1 
ATOM   23064 C  CA  . ASN C 1 1140 ? -17.945  38.736  104.814 1.00 131.03 ? 1140 ASN B CA  1 
ATOM   23065 C  C   . ASN C 1 1140 ? -18.110  40.190  105.188 1.00 125.21 ? 1140 ASN B C   1 
ATOM   23066 O  O   . ASN C 1 1140 ? -17.389  41.056  104.696 1.00 122.77 ? 1140 ASN B O   1 
ATOM   23067 C  CB  . ASN C 1 1140 ? -19.080  38.306  103.905 1.00 138.74 ? 1140 ASN B CB  1 
ATOM   23068 C  CG  . ASN C 1 1140 ? -18.931  38.837  102.516 1.00 145.64 ? 1140 ASN B CG  1 
ATOM   23069 O  OD1 . ASN C 1 1140 ? -19.842  38.704  101.700 1.00 150.73 ? 1140 ASN B OD1 1 
ATOM   23070 N  ND2 . ASN C 1 1140 ? -17.782  39.450  102.224 1.00 145.17 ? 1140 ASN B ND2 1 
ATOM   23071 N  N   . SER C 1 1141 ? -19.051  40.448  106.090 1.00 123.26 ? 1141 SER B N   1 
ATOM   23072 C  CA  . SER C 1 1141 ? -19.309  41.805  106.551 1.00 119.51 ? 1141 SER B CA  1 
ATOM   23073 C  C   . SER C 1 1141 ? -18.071  42.446  107.183 1.00 113.04 ? 1141 SER B C   1 
ATOM   23074 O  O   . SER C 1 1141 ? -17.673  43.543  106.798 1.00 109.84 ? 1141 SER B O   1 
ATOM   23075 C  CB  . SER C 1 1141 ? -20.491  41.829  107.526 1.00 122.80 ? 1141 SER B CB  1 
ATOM   23076 O  OG  . SER C 1 1141 ? -20.847  43.166  107.863 1.00 123.52 ? 1141 SER B OG  1 
ATOM   23077 N  N   . LEU C 1 1142 ? -17.472  41.761  108.155 1.00 109.59 ? 1142 LEU B N   1 
ATOM   23078 C  CA  . LEU C 1 1142 ? -16.234  42.239  108.758 1.00 104.13 ? 1142 LEU B CA  1 
ATOM   23079 C  C   . LEU C 1 1142 ? -15.371  42.626  107.584 1.00 102.04 ? 1142 LEU B C   1 
ATOM   23080 O  O   . LEU C 1 1142 ? -15.010  43.805  107.433 1.00 100.10 ? 1142 LEU B O   1 
ATOM   23081 C  CB  . LEU C 1 1142 ? -15.527  41.134  109.566 1.00 100.35 ? 1142 LEU B CB  1 
ATOM   23082 C  CG  . LEU C 1 1142 ? -15.044  41.378  111.009 1.00 94.96  ? 1142 LEU B CG  1 
ATOM   23083 C  CD1 . LEU C 1 1142 ? -14.748  40.061  111.713 1.00 94.16  ? 1142 LEU B CD1 1 
ATOM   23084 C  CD2 . LEU C 1 1142 ? -13.857  42.306  111.098 1.00 90.19  ? 1142 LEU B CD2 1 
ATOM   23085 N  N   . TYR C 1 1143 ? -15.092  41.634  106.723 1.00 101.73 ? 1143 TYR B N   1 
ATOM   23086 C  CA  . TYR C 1 1143 ? -14.091  41.804  105.656 1.00 99.06  ? 1143 TYR B CA  1 
ATOM   23087 C  C   . TYR C 1 1143 ? -14.282  43.101  104.878 1.00 96.61  ? 1143 TYR B C   1 
ATOM   23088 O  O   . TYR C 1 1143 ? -13.311  43.823  104.631 1.00 93.25  ? 1143 TYR B O   1 
ATOM   23089 C  CB  . TYR C 1 1143 ? -13.988  40.612  104.684 1.00 97.87  ? 1143 TYR B CB  1 
ATOM   23090 C  CG  . TYR C 1 1143 ? -13.122  40.947  103.469 1.00 95.92  ? 1143 TYR B CG  1 
ATOM   23091 C  CD1 . TYR C 1 1143 ? -11.760  40.693  103.472 1.00 94.37  ? 1143 TYR B CD1 1 
ATOM   23092 C  CD2 . TYR C 1 1143 ? -13.673  41.552  102.325 1.00 96.54  ? 1143 TYR B CD2 1 
ATOM   23093 C  CE1 . TYR C 1 1143 ? -10.970  41.012  102.372 1.00 94.07  ? 1143 TYR B CE1 1 
ATOM   23094 C  CE2 . TYR C 1 1143 ? -12.885  41.866  101.213 1.00 94.74  ? 1143 TYR B CE2 1 
ATOM   23095 C  CZ  . TYR C 1 1143 ? -11.537  41.593  101.245 1.00 94.07  ? 1143 TYR B CZ  1 
ATOM   23096 O  OH  . TYR C 1 1143 ? -10.747  41.905  100.158 1.00 92.54  ? 1143 TYR B OH  1 
ATOM   23097 N  N   . LEU C 1 1144 ? -15.526  43.400  104.509 1.00 97.64  ? 1144 LEU B N   1 
ATOM   23098 C  CA  . LEU C 1 1144 ? -15.794  44.663  103.850 1.00 97.65  ? 1144 LEU B CA  1 
ATOM   23099 C  C   . LEU C 1 1144 ? -15.521  45.826  104.800 1.00 97.85  ? 1144 LEU B C   1 
ATOM   23100 O  O   . LEU C 1 1144 ? -14.669  46.673  104.530 1.00 97.85  ? 1144 LEU B O   1 
ATOM   23101 C  CB  . LEU C 1 1144 ? -17.222  44.726  103.325 1.00 97.42  ? 1144 LEU B CB  1 
ATOM   23102 C  CG  . LEU C 1 1144 ? -17.459  45.828  102.295 1.00 95.03  ? 1144 LEU B CG  1 
ATOM   23103 C  CD1 . LEU C 1 1144 ? -16.961  45.340  100.947 1.00 94.57  ? 1144 LEU B CD1 1 
ATOM   23104 C  CD2 . LEU C 1 1144 ? -18.937  46.198  102.230 1.00 95.68  ? 1144 LEU B CD2 1 
ATOM   23105 N  N   . THR C 1 1145 ? -16.231  45.858  105.921 1.00 97.86  ? 1145 THR B N   1 
ATOM   23106 C  CA  . THR C 1 1145 ? -16.099  46.976  106.843 1.00 97.36  ? 1145 THR B CA  1 
ATOM   23107 C  C   . THR C 1 1145 ? -14.614  47.241  107.196 1.00 95.74  ? 1145 THR B C   1 
ATOM   23108 O  O   . THR C 1 1145 ? -14.167  48.390  107.164 1.00 94.94  ? 1145 THR B O   1 
ATOM   23109 C  CB  . THR C 1 1145 ? -17.014  46.802  108.095 1.00 102.48 ? 1145 THR B CB  1 
ATOM   23110 O  OG1 . THR C 1 1145 ? -18.353  46.533  107.668 1.00 102.66 ? 1145 THR B OG1 1 
ATOM   23111 C  CG2 . THR C 1 1145 ? -17.039  48.064  108.919 1.00 103.01 ? 1145 THR B CG2 1 
ATOM   23112 N  N   . ALA C 1 1146 ? -13.833  46.202  107.481 1.00 95.48  ? 1146 ALA B N   1 
ATOM   23113 C  CA  . ALA C 1 1146 ? -12.409  46.428  107.725 1.00 96.92  ? 1146 ALA B CA  1 
ATOM   23114 C  C   . ALA C 1 1146 ? -11.745  47.123  106.531 1.00 97.89  ? 1146 ALA B C   1 
ATOM   23115 O  O   . ALA C 1 1146 ? -11.118  48.172  106.674 1.00 95.61  ? 1146 ALA B O   1 
ATOM   23116 C  CB  . ALA C 1 1146 ? -11.717  45.132  108.042 1.00 97.85  ? 1146 ALA B CB  1 
ATOM   23117 N  N   . PHE C 1 1147 ? -11.913  46.510  105.361 1.00 99.42  ? 1147 PHE B N   1 
ATOM   23118 C  CA  . PHE C 1 1147 ? -11.386  46.977  104.070 1.00 97.76  ? 1147 PHE B CA  1 
ATOM   23119 C  C   . PHE C 1 1147 ? -11.766  48.422  103.785 1.00 97.08  ? 1147 PHE B C   1 
ATOM   23120 O  O   . PHE C 1 1147 ? -10.905  49.279  103.553 1.00 96.58  ? 1147 PHE B O   1 
ATOM   23121 C  CB  . PHE C 1 1147 ? -11.966  46.095  102.942 1.00 98.51  ? 1147 PHE B CB  1 
ATOM   23122 C  CG  . PHE C 1 1147 ? -11.313  46.283  101.583 1.00 96.39  ? 1147 PHE B CG  1 
ATOM   23123 C  CD1 . PHE C 1 1147 ? -10.891  45.184  100.856 1.00 93.90  ? 1147 PHE B CD1 1 
ATOM   23124 C  CD2 . PHE C 1 1147 ? -11.140  47.539  101.037 1.00 96.86  ? 1147 PHE B CD2 1 
ATOM   23125 C  CE1 . PHE C 1 1147 ? -10.301  45.330  99.647  1.00 92.83  ? 1147 PHE B CE1 1 
ATOM   23126 C  CE2 . PHE C 1 1147 ? -10.551  47.683  99.821  1.00 96.00  ? 1147 PHE B CE2 1 
ATOM   23127 C  CZ  . PHE C 1 1147 ? -10.137  46.572  99.125  1.00 94.26  ? 1147 PHE B CZ  1 
ATOM   23128 N  N   . THR C 1 1148 ? -13.066  48.681  103.757 1.00 97.30  ? 1148 THR B N   1 
ATOM   23129 C  CA  . THR C 1 1148 ? -13.535  50.025  103.487 1.00 99.00  ? 1148 THR B CA  1 
ATOM   23130 C  C   . THR C 1 1148 ? -13.052  51.028  104.584 1.00 93.11  ? 1148 THR B C   1 
ATOM   23131 O  O   . THR C 1 1148 ? -12.952  52.243  104.348 1.00 92.81  ? 1148 THR B O   1 
ATOM   23132 C  CB  . THR C 1 1148 ? -15.069  50.056  103.132 1.00 93.53  ? 1148 THR B CB  1 
ATOM   23133 O  OG1 . THR C 1 1148 ? -15.675  51.265  103.603 1.00 95.83  ? 1148 THR B OG1 1 
ATOM   23134 C  CG2 . THR C 1 1148 ? -15.811  48.872  103.712 1.00 93.00  ? 1148 THR B CG2 1 
ATOM   23135 N  N   . VAL C 1 1149 ? -12.693  50.536  105.768 1.00 90.88  ? 1149 VAL B N   1 
ATOM   23136 C  CA  . VAL C 1 1149 ? -12.073  51.457  106.719 1.00 89.36  ? 1149 VAL B CA  1 
ATOM   23137 C  C   . VAL C 1 1149 ? -10.696  51.864  106.159 1.00 85.98  ? 1149 VAL B C   1 
ATOM   23138 O  O   . VAL C 1 1149 ? -10.494  53.020  105.798 1.00 84.96  ? 1149 VAL B O   1 
ATOM   23139 C  CB  . VAL C 1 1149 ? -12.052  50.918  108.193 1.00 73.47  ? 1149 VAL B CB  1 
ATOM   23140 C  CG1 . VAL C 1 1149 ? -10.886  51.511  108.988 1.00 73.45  ? 1149 VAL B CG1 1 
ATOM   23141 C  CG2 . VAL C 1 1149 ? -13.384  51.202  108.909 1.00 71.08  ? 1149 VAL B CG2 1 
ATOM   23142 N  N   . ILE C 1 1150 ? -9.791   50.893  106.033 1.00 82.66  ? 1150 ILE B N   1 
ATOM   23143 C  CA  . ILE C 1 1150 ? -8.446   51.100  105.493 1.00 77.46  ? 1150 ILE B CA  1 
ATOM   23144 C  C   . ILE C 1 1150 ? -8.445   52.067  104.341 1.00 76.87  ? 1150 ILE B C   1 
ATOM   23145 O  O   . ILE C 1 1150 ? -7.499   52.817  104.162 1.00 77.93  ? 1150 ILE B O   1 
ATOM   23146 C  CB  . ILE C 1 1150 ? -7.891   49.787  104.942 1.00 74.27  ? 1150 ILE B CB  1 
ATOM   23147 C  CG1 . ILE C 1 1150 ? -8.531   48.632  105.717 1.00 76.34  ? 1150 ILE B CG1 1 
ATOM   23148 C  CG2 . ILE C 1 1150 ? -6.360   49.789  104.928 1.00 68.44  ? 1150 ILE B CG2 1 
ATOM   23149 C  CD1 . ILE C 1 1150 ? -7.721   47.385  105.801 1.00 77.19  ? 1150 ILE B CD1 1 
ATOM   23150 N  N   . GLY C 1 1151 ? -9.502   52.033  103.541 1.00 77.33  ? 1151 GLY B N   1 
ATOM   23151 C  CA  . GLY C 1 1151 ? -9.630   52.961  102.437 1.00 78.60  ? 1151 GLY B CA  1 
ATOM   23152 C  C   . GLY C 1 1151 ? -9.896   54.385  102.911 1.00 82.30  ? 1151 GLY B C   1 
ATOM   23153 O  O   . GLY C 1 1151 ? -9.125   55.308  102.598 1.00 81.78  ? 1151 GLY B O   1 
ATOM   23154 N  N   . ILE C 1 1152 ? -10.985  54.572  103.661 1.00 83.70  ? 1152 ILE B N   1 
ATOM   23155 C  CA  . ILE C 1 1152 ? -11.359  55.905  104.129 1.00 86.39  ? 1152 ILE B CA  1 
ATOM   23156 C  C   . ILE C 1 1152 ? -10.236  56.433  104.976 1.00 89.81  ? 1152 ILE B C   1 
ATOM   23157 O  O   . ILE C 1 1152 ? -9.809   57.575  104.843 1.00 90.67  ? 1152 ILE B O   1 
ATOM   23158 C  CB  . ILE C 1 1152 ? -12.609  55.843  104.991 1.00 83.05  ? 1152 ILE B CB  1 
ATOM   23159 C  CG1 . ILE C 1 1152 ? -13.726  55.163  104.189 1.00 78.19  ? 1152 ILE B CG1 1 
ATOM   23160 C  CG2 . ILE C 1 1152 ? -12.943  57.268  105.531 1.00 53.16  ? 1152 ILE B CG2 1 
ATOM   23161 C  CD1 . ILE C 1 1152 ? -14.848  54.590  104.983 1.00 74.91  ? 1152 ILE B CD1 1 
ATOM   23162 N  N   . ARG C 1 1153 ? -9.778   55.553  105.851 1.00 90.78  ? 1153 ARG B N   1 
ATOM   23163 C  CA  . ARG C 1 1153 ? -8.588   55.759  106.623 1.00 92.30  ? 1153 ARG B CA  1 
ATOM   23164 C  C   . ARG C 1 1153 ? -7.439   56.187  105.740 1.00 89.53  ? 1153 ARG B C   1 
ATOM   23165 O  O   . ARG C 1 1153 ? -6.799   57.181  106.026 1.00 92.01  ? 1153 ARG B O   1 
ATOM   23166 C  CB  . ARG C 1 1153 ? -8.223   54.462  107.337 1.00 97.69  ? 1153 ARG B CB  1 
ATOM   23167 C  CG  . ARG C 1 1153 ? -9.036   54.191  108.602 1.00 104.45 ? 1153 ARG B CG  1 
ATOM   23168 C  CD  . ARG C 1 1153 ? -8.874   55.346  109.598 1.00 109.13 ? 1153 ARG B CD  1 
ATOM   23169 N  NE  . ARG C 1 1153 ? -9.290   55.023  110.963 1.00 110.66 ? 1153 ARG B NE  1 
ATOM   23170 C  CZ  . ARG C 1 1153 ? -9.565   55.952  111.872 1.00 112.07 ? 1153 ARG B CZ  1 
ATOM   23171 N  NH1 . ARG C 1 1153 ? -9.479   57.240  111.555 1.00 111.71 ? 1153 ARG B NH1 1 
ATOM   23172 N  NH2 . ARG C 1 1153 ? -9.934   55.601  113.092 1.00 113.97 ? 1153 ARG B NH2 1 
ATOM   23173 N  N   . LYS C 1 1154 ? -7.171   55.448  104.669 1.00 86.17  ? 1154 LYS B N   1 
ATOM   23174 C  CA  . LYS C 1 1154 ? -5.952   55.668  103.893 1.00 85.66  ? 1154 LYS B CA  1 
ATOM   23175 C  C   . LYS C 1 1154 ? -5.917   57.037  103.261 1.00 89.01  ? 1154 LYS B C   1 
ATOM   23176 O  O   . LYS C 1 1154 ? -4.845   57.604  103.037 1.00 88.45  ? 1154 LYS B O   1 
ATOM   23177 C  CB  . LYS C 1 1154 ? -5.818   54.622  102.795 1.00 83.91  ? 1154 LYS B CB  1 
ATOM   23178 C  CG  . LYS C 1 1154 ? -5.033   53.397  103.181 1.00 83.09  ? 1154 LYS B CG  1 
ATOM   23179 C  CD  . LYS C 1 1154 ? -3.539   53.624  103.053 1.00 83.37  ? 1154 LYS B CD  1 
ATOM   23180 C  CE  . LYS C 1 1154 ? -2.795   52.313  103.276 1.00 82.74  ? 1154 LYS B CE  1 
ATOM   23181 N  NZ  . LYS C 1 1154 ? -1.587   52.242  102.412 1.00 83.03  ? 1154 LYS B NZ  1 
ATOM   23182 N  N   . ALA C 1 1155 ? -7.112   57.546  102.972 1.00 93.60  ? 1155 ALA B N   1 
ATOM   23183 C  CA  . ALA C 1 1155 ? -7.294   58.718  102.132 1.00 97.99  ? 1155 ALA B CA  1 
ATOM   23184 C  C   . ALA C 1 1155 ? -7.929   59.854  102.897 1.00 105.86 ? 1155 ALA B C   1 
ATOM   23185 O  O   . ALA C 1 1155 ? -8.026   60.961  102.369 1.00 108.92 ? 1155 ALA B O   1 
ATOM   23186 C  CB  . ALA C 1 1155 ? -8.163   58.369  100.943 1.00 96.66  ? 1155 ALA B CB  1 
ATOM   23187 N  N   . PHE C 1 1156 ? -8.370   59.583  104.127 1.00 109.61 ? 1156 PHE B N   1 
ATOM   23188 C  CA  . PHE C 1 1156 ? -9.155   60.548  104.913 1.00 113.55 ? 1156 PHE B CA  1 
ATOM   23189 C  C   . PHE C 1 1156 ? -8.519   61.922  104.935 1.00 113.39 ? 1156 PHE B C   1 
ATOM   23190 O  O   . PHE C 1 1156 ? -9.209   62.942  105.008 1.00 114.46 ? 1156 PHE B O   1 
ATOM   23191 C  CB  . PHE C 1 1156 ? -9.369   60.052  106.356 1.00 115.47 ? 1156 PHE B CB  1 
ATOM   23192 C  CG  . PHE C 1 1156 ? -9.843   61.128  107.320 1.00 118.63 ? 1156 PHE B CG  1 
ATOM   23193 C  CD1 . PHE C 1 1156 ? -11.191  61.419  107.454 1.00 120.32 ? 1156 PHE B CD1 1 
ATOM   23194 C  CD2 . PHE C 1 1156 ? -8.933   61.834  108.101 1.00 119.18 ? 1156 PHE B CD2 1 
ATOM   23195 C  CE1 . PHE C 1 1156 ? -11.620  62.402  108.331 1.00 122.05 ? 1156 PHE B CE1 1 
ATOM   23196 C  CE2 . PHE C 1 1156 ? -9.355   62.812  108.981 1.00 120.95 ? 1156 PHE B CE2 1 
ATOM   23197 C  CZ  . PHE C 1 1156 ? -10.702  63.095  109.096 1.00 122.57 ? 1156 PHE B CZ  1 
ATOM   23198 N  N   . ASP C 1 1157 ? -7.198   61.942  104.842 1.00 110.72 ? 1157 ASP B N   1 
ATOM   23199 C  CA  . ASP C 1 1157 ? -6.474   63.175  105.072 1.00 112.41 ? 1157 ASP B CA  1 
ATOM   23200 C  C   . ASP C 1 1157 ? -6.698   64.330  104.076 1.00 113.34 ? 1157 ASP B C   1 
ATOM   23201 O  O   . ASP C 1 1157 ? -6.387   65.471  104.412 1.00 113.93 ? 1157 ASP B O   1 
ATOM   23202 C  CB  . ASP C 1 1157 ? -4.990   62.895  105.309 1.00 115.93 ? 1157 ASP B CB  1 
ATOM   23203 C  CG  . ASP C 1 1157 ? -4.639   62.880  106.801 1.00 121.69 ? 1157 ASP B CG  1 
ATOM   23204 O  OD1 . ASP C 1 1157 ? -5.440   63.436  107.599 1.00 124.89 ? 1157 ASP B OD1 1 
ATOM   23205 O  OD2 . ASP C 1 1157 ? -3.572   62.328  107.178 1.00 122.49 ? 1157 ASP B OD2 1 
ATOM   23206 N  N   . ILE C 1 1158 ? -7.237   64.067  102.881 1.00 112.03 ? 1158 ILE B N   1 
ATOM   23207 C  CA  . ILE C 1 1158 ? -7.458   65.136  101.903 1.00 108.98 ? 1158 ILE B CA  1 
ATOM   23208 C  C   . ILE C 1 1158 ? -8.835   65.662  102.051 1.00 112.27 ? 1158 ILE B C   1 
ATOM   23209 O  O   . ILE C 1 1158 ? -9.238   66.576  101.345 1.00 116.80 ? 1158 ILE B O   1 
ATOM   23210 C  CB  . ILE C 1 1158 ? -7.423   64.651  100.489 1.00 100.00 ? 1158 ILE B CB  1 
ATOM   23211 C  CG1 . ILE C 1 1158 ? -6.824   63.249  100.437 1.00 93.92  ? 1158 ILE B CG1 1 
ATOM   23212 C  CG2 . ILE C 1 1158 ? -6.717   65.690  99.628  1.00 100.06 ? 1158 ILE B CG2 1 
ATOM   23213 C  CD1 . ILE C 1 1158 ? -7.260   62.449  99.275  1.00 91.44  ? 1158 ILE B CD1 1 
ATOM   23214 N  N   . CYS C 1 1159 ? -9.580   65.040  102.943 1.00 111.94 ? 1159 CYS B N   1 
ATOM   23215 C  CA  . CYS C 1 1159 ? -10.929  65.474  103.190 1.00 113.88 ? 1159 CYS B CA  1 
ATOM   23216 C  C   . CYS C 1 1159 ? -11.357  65.200  104.629 1.00 120.09 ? 1159 CYS B C   1 
ATOM   23217 O  O   . CYS C 1 1159 ? -12.485  64.748  104.850 1.00 121.28 ? 1159 CYS B O   1 
ATOM   23218 C  CB  . CYS C 1 1159 ? -11.889  64.794  102.205 1.00 111.26 ? 1159 CYS B CB  1 
ATOM   23219 S  SG  . CYS C 1 1159 ? -13.435  65.695  101.928 1.00 173.52 ? 1159 CYS B SG  1 
ATOM   23220 N  N   . PRO C 1 1160 ? -10.471  65.464  105.615 1.00 121.51 ? 1160 PRO B N   1 
ATOM   23221 C  CA  . PRO C 1 1160 ? -10.997  65.392  106.980 1.00 123.18 ? 1160 PRO B CA  1 
ATOM   23222 C  C   . PRO C 1 1160 ? -12.299  66.169  107.012 1.00 121.44 ? 1160 PRO B C   1 
ATOM   23223 O  O   . PRO C 1 1160 ? -12.337  67.356  106.682 1.00 121.72 ? 1160 PRO B O   1 
ATOM   23224 C  CB  . PRO C 1 1160 ? -9.912   66.094  107.812 1.00 124.73 ? 1160 PRO B CB  1 
ATOM   23225 C  CG  . PRO C 1 1160 ? -9.047   66.808  106.797 1.00 126.20 ? 1160 PRO B CG  1 
ATOM   23226 C  CD  . PRO C 1 1160 ? -9.070   65.908  105.614 1.00 124.24 ? 1160 PRO B CD  1 
ATOM   23227 N  N   . LEU C 1 1161 ? -13.368  65.484  107.379 1.00 120.91 ? 1161 LEU B N   1 
ATOM   23228 C  CA  . LEU C 1 1161 ? -14.697  66.018  107.184 1.00 122.44 ? 1161 LEU B CA  1 
ATOM   23229 C  C   . LEU C 1 1161 ? -15.497  65.556  108.368 1.00 125.80 ? 1161 LEU B C   1 
ATOM   23230 O  O   . LEU C 1 1161 ? -15.636  64.351  108.592 1.00 126.29 ? 1161 LEU B O   1 
ATOM   23231 C  CB  . LEU C 1 1161 ? -15.299  65.424  105.920 1.00 118.24 ? 1161 LEU B CB  1 
ATOM   23232 C  CG  . LEU C 1 1161 ? -16.484  66.148  105.302 1.00 115.54 ? 1161 LEU B CG  1 
ATOM   23233 C  CD1 . LEU C 1 1161 ? -16.991  67.288  106.212 1.00 114.27 ? 1161 LEU B CD1 1 
ATOM   23234 C  CD2 . LEU C 1 1161 ? -16.093  66.672  103.943 1.00 113.63 ? 1161 LEU B CD2 1 
ATOM   23235 N  N   . VAL C 1 1162 ? -16.022  66.502  109.136 1.00 129.03 ? 1162 VAL B N   1 
ATOM   23236 C  CA  . VAL C 1 1162 ? -16.651  66.139  110.390 1.00 132.29 ? 1162 VAL B CA  1 
ATOM   23237 C  C   . VAL C 1 1162 ? -17.459  64.902  110.115 1.00 130.96 ? 1162 VAL B C   1 
ATOM   23238 O  O   . VAL C 1 1162 ? -17.276  63.866  110.754 1.00 128.66 ? 1162 VAL B O   1 
ATOM   23239 C  CB  . VAL C 1 1162 ? -17.581  67.236  110.923 1.00 138.60 ? 1162 VAL B CB  1 
ATOM   23240 C  CG1 . VAL C 1 1162 ? -16.937  67.962  112.124 1.00 140.46 ? 1162 VAL B CG1 1 
ATOM   23241 C  CG2 . VAL C 1 1162 ? -17.997  68.197  109.790 1.00 142.51 ? 1162 VAL B CG2 1 
ATOM   23242 N  N   . LYS C 1 1163 ? -18.315  65.001  109.107 1.00 133.56 ? 1163 LYS B N   1 
ATOM   23243 C  CA  . LYS C 1 1163 ? -19.310  63.976  108.891 1.00 134.25 ? 1163 LYS B CA  1 
ATOM   23244 C  C   . LYS C 1 1163 ? -18.700  62.605  108.702 1.00 132.48 ? 1163 LYS B C   1 
ATOM   23245 O  O   . LYS C 1 1163 ? -19.306  61.600  109.055 1.00 132.26 ? 1163 LYS B O   1 
ATOM   23246 C  CB  . LYS C 1 1163 ? -20.207  64.326  107.714 1.00 135.36 ? 1163 LYS B CB  1 
ATOM   23247 C  CG  . LYS C 1 1163 ? -21.589  63.748  107.876 1.00 135.39 ? 1163 LYS B CG  1 
ATOM   23248 C  CD  . LYS C 1 1163 ? -22.432  64.003  106.659 1.00 136.16 ? 1163 LYS B CD  1 
ATOM   23249 C  CE  . LYS C 1 1163 ? -23.748  63.273  106.771 1.00 136.37 ? 1163 LYS B CE  1 
ATOM   23250 N  NZ  . LYS C 1 1163 ? -24.223  62.881  105.421 1.00 136.49 ? 1163 LYS B NZ  1 
ATOM   23251 N  N   . ILE C 1 1164 ? -17.501  62.555  108.145 1.00 132.21 ? 1164 ILE B N   1 
ATOM   23252 C  CA  . ILE C 1 1164 ? -16.914  61.261  107.846 1.00 132.02 ? 1164 ILE B CA  1 
ATOM   23253 C  C   . ILE C 1 1164 ? -15.964  60.796  108.937 1.00 133.32 ? 1164 ILE B C   1 
ATOM   23254 O  O   . ILE C 1 1164 ? -15.455  59.679  108.878 1.00 132.34 ? 1164 ILE B O   1 
ATOM   23255 C  CB  . ILE C 1 1164 ? -16.283  61.179  106.409 1.00 107.79 ? 1164 ILE B CB  1 
ATOM   23256 C  CG1 . ILE C 1 1164 ? -14.763  61.104  106.444 1.00 105.68 ? 1164 ILE B CG1 1 
ATOM   23257 C  CG2 . ILE C 1 1164 ? -16.776  62.322  105.488 1.00 108.68 ? 1164 ILE B CG2 1 
ATOM   23258 C  CD1 . ILE C 1 1164 ? -14.203  61.067  105.049 1.00 105.57 ? 1164 ILE B CD1 1 
ATOM   23259 N  N   . ASP C 1 1165 ? -15.737  61.646  109.937 1.00 135.64 ? 1165 ASP B N   1 
ATOM   23260 C  CA  . ASP C 1 1165 ? -14.957  61.240  111.117 1.00 137.10 ? 1165 ASP B CA  1 
ATOM   23261 C  C   . ASP C 1 1165 ? -15.840  60.403  112.019 1.00 135.81 ? 1165 ASP B C   1 
ATOM   23262 O  O   . ASP C 1 1165 ? -15.458  59.316  112.448 1.00 134.25 ? 1165 ASP B O   1 
ATOM   23263 C  CB  . ASP C 1 1165 ? -14.413  62.450  111.885 1.00 139.53 ? 1165 ASP B CB  1 
ATOM   23264 C  CG  . ASP C 1 1165 ? -13.623  62.057  113.128 1.00 139.33 ? 1165 ASP B CG  1 
ATOM   23265 O  OD1 . ASP C 1 1165 ? -12.740  61.164  113.053 1.00 136.94 ? 1165 ASP B OD1 1 
ATOM   23266 O  OD2 . ASP C 1 1165 ? -13.889  62.671  114.182 1.00 141.72 ? 1165 ASP B OD2 1 
ATOM   23267 N  N   . THR C 1 1166 ? -17.027  60.937  112.291 1.00 137.84 ? 1166 THR B N   1 
ATOM   23268 C  CA  . THR C 1 1166 ? -18.119  60.179  112.886 1.00 138.15 ? 1166 THR B CA  1 
ATOM   23269 C  C   . THR C 1 1166 ? -18.228  58.798  112.255 1.00 136.16 ? 1166 THR B C   1 
ATOM   23270 O  O   . THR C 1 1166 ? -18.121  57.770  112.938 1.00 136.31 ? 1166 THR B O   1 
ATOM   23271 C  CB  . THR C 1 1166 ? -19.460  60.872  112.635 1.00 141.00 ? 1166 THR B CB  1 
ATOM   23272 O  OG1 . THR C 1 1166 ? -19.509  62.095  113.376 1.00 142.93 ? 1166 THR B OG1 1 
ATOM   23273 C  CG2 . THR C 1 1166 ? -20.618  59.959  113.043 1.00 141.52 ? 1166 THR B CG2 1 
ATOM   23274 N  N   . ALA C 1 1167 ? -18.454  58.779  110.945 1.00 133.66 ? 1167 ALA B N   1 
ATOM   23275 C  CA  . ALA C 1 1167 ? -18.558  57.527  110.213 1.00 128.39 ? 1167 ALA B CA  1 
ATOM   23276 C  C   . ALA C 1 1167 ? -17.361  56.618  110.497 1.00 122.13 ? 1167 ALA B C   1 
ATOM   23277 O  O   . ALA C 1 1167 ? -17.538  55.430  110.794 1.00 119.25 ? 1167 ALA B O   1 
ATOM   23278 C  CB  . ALA C 1 1167 ? -18.676  57.802  108.727 1.00 129.19 ? 1167 ALA B CB  1 
ATOM   23279 N  N   . LEU C 1 1168 ? -16.153  57.177  110.409 1.00 117.32 ? 1168 LEU B N   1 
ATOM   23280 C  CA  . LEU C 1 1168 ? -14.950  56.388  110.599 1.00 114.34 ? 1168 LEU B CA  1 
ATOM   23281 C  C   . LEU C 1 1168 ? -14.996  55.674  111.929 1.00 119.86 ? 1168 LEU B C   1 
ATOM   23282 O  O   . LEU C 1 1168 ? -14.543  54.535  112.066 1.00 121.14 ? 1168 LEU B O   1 
ATOM   23283 C  CB  . LEU C 1 1168 ? -13.710  57.255  110.521 1.00 108.71 ? 1168 LEU B CB  1 
ATOM   23284 C  CG  . LEU C 1 1168 ? -12.951  56.857  109.265 1.00 105.40 ? 1168 LEU B CG  1 
ATOM   23285 C  CD1 . LEU C 1 1168 ? -11.586  57.518  109.212 1.00 105.24 ? 1168 LEU B CD1 1 
ATOM   23286 C  CD2 . LEU C 1 1168 ? -12.835  55.343  109.225 1.00 102.93 ? 1168 LEU B CD2 1 
ATOM   23287 N  N   . ILE C 1 1169 ? -15.555  56.360  112.914 1.00 122.74 ? 1169 ILE B N   1 
ATOM   23288 C  CA  . ILE C 1 1169 ? -15.649  55.840  114.264 1.00 121.33 ? 1169 ILE B CA  1 
ATOM   23289 C  C   . ILE C 1 1169 ? -16.727  54.775  114.351 1.00 121.57 ? 1169 ILE B C   1 
ATOM   23290 O  O   . ILE C 1 1169 ? -16.428  53.632  114.661 1.00 121.05 ? 1169 ILE B O   1 
ATOM   23291 C  CB  . ILE C 1 1169 ? -15.889  56.987  115.251 1.00 119.75 ? 1169 ILE B CB  1 
ATOM   23292 C  CG1 . ILE C 1 1169 ? -14.537  57.508  115.763 1.00 117.11 ? 1169 ILE B CG1 1 
ATOM   23293 C  CG2 . ILE C 1 1169 ? -16.797  56.541  116.372 1.00 121.05 ? 1169 ILE B CG2 1 
ATOM   23294 C  CD1 . ILE C 1 1169 ? -14.475  58.995  115.930 1.00 116.71 ? 1169 ILE B CD1 1 
ATOM   23295 N  N   . LYS C 1 1170 ? -17.966  55.145  114.042 1.00 124.86 ? 1170 LYS B N   1 
ATOM   23296 C  CA  . LYS C 1 1170 ? -19.067  54.188  114.007 1.00 128.15 ? 1170 LYS B CA  1 
ATOM   23297 C  C   . LYS C 1 1170 ? -18.598  52.916  113.336 1.00 123.52 ? 1170 LYS B C   1 
ATOM   23298 O  O   . LYS C 1 1170 ? -18.992  51.815  113.704 1.00 121.34 ? 1170 LYS B O   1 
ATOM   23299 C  CB  . LYS C 1 1170 ? -20.246  54.752  113.212 1.00 136.55 ? 1170 LYS B CB  1 
ATOM   23300 C  CG  . LYS C 1 1170 ? -20.905  55.973  113.830 1.00 145.14 ? 1170 LYS B CG  1 
ATOM   23301 C  CD  . LYS C 1 1170 ? -21.270  55.707  115.285 1.00 152.57 ? 1170 LYS B CD  1 
ATOM   23302 C  CE  . LYS C 1 1170 ? -22.454  54.737  115.412 1.00 158.26 ? 1170 LYS B CE  1 
ATOM   23303 N  NZ  . LYS C 1 1170 ? -22.786  54.406  116.845 1.00 160.40 ? 1170 LYS B NZ  1 
ATOM   23304 N  N   . ALA C 1 1171 ? -17.755  53.090  112.332 1.00 121.93 ? 1171 ALA B N   1 
ATOM   23305 C  CA  . ALA C 1 1171 ? -17.150  51.971  111.644 1.00 121.92 ? 1171 ALA B CA  1 
ATOM   23306 C  C   . ALA C 1 1171 ? -16.144  51.284  112.550 1.00 121.35 ? 1171 ALA B C   1 
ATOM   23307 O  O   . ALA C 1 1171 ? -16.303  50.120  112.884 1.00 121.47 ? 1171 ALA B O   1 
ATOM   23308 C  CB  . ALA C 1 1171 ? -16.477  52.447  110.397 1.00 122.38 ? 1171 ALA B CB  1 
ATOM   23309 N  N   . ASP C 1 1172 ? -15.104  52.013  112.937 1.00 121.03 ? 1172 ASP B N   1 
ATOM   23310 C  CA  . ASP C 1 1172 ? -14.081  51.498  113.840 1.00 121.60 ? 1172 ASP B CA  1 
ATOM   23311 C  C   . ASP C 1 1172 ? -14.711  50.747  115.005 1.00 122.06 ? 1172 ASP B C   1 
ATOM   23312 O  O   . ASP C 1 1172 ? -14.203  49.711  115.453 1.00 120.65 ? 1172 ASP B O   1 
ATOM   23313 C  CB  . ASP C 1 1172 ? -13.265  52.658  114.395 1.00 122.80 ? 1172 ASP B CB  1 
ATOM   23314 C  CG  . ASP C 1 1172 ? -11.891  52.754  113.778 1.00 123.94 ? 1172 ASP B CG  1 
ATOM   23315 O  OD1 . ASP C 1 1172 ? -11.561  51.968  112.864 1.00 123.91 ? 1172 ASP B OD1 1 
ATOM   23316 O  OD2 . ASP C 1 1172 ? -11.125  53.623  114.228 1.00 125.94 ? 1172 ASP B OD2 1 
ATOM   23317 N  N   . ASN C 1 1173 ? -15.821  51.298  115.494 1.00 125.80 ? 1173 ASN B N   1 
ATOM   23318 C  CA  . ASN C 1 1173 ? -16.558  50.748  116.626 1.00 128.32 ? 1173 ASN B CA  1 
ATOM   23319 C  C   . ASN C 1 1173 ? -16.976  49.317  116.340 1.00 126.92 ? 1173 ASN B C   1 
ATOM   23320 O  O   . ASN C 1 1173 ? -16.557  48.398  117.046 1.00 126.77 ? 1173 ASN B O   1 
ATOM   23321 C  CB  . ASN C 1 1173 ? -17.783  51.614  116.963 1.00 135.12 ? 1173 ASN B CB  1 
ATOM   23322 C  CG  . ASN C 1 1173 ? -17.511  52.618  118.092 1.00 141.66 ? 1173 ASN B CG  1 
ATOM   23323 O  OD1 . ASN C 1 1173 ? -18.410  52.931  118.872 1.00 145.94 ? 1173 ASN B OD1 1 
ATOM   23324 N  ND2 . ASN C 1 1173 ? -16.275  53.120  118.182 1.00 141.24 ? 1173 ASN B ND2 1 
ATOM   23325 N  N   . PHE C 1 1174 ? -17.774  49.130  115.291 1.00 125.53 ? 1174 PHE B N   1 
ATOM   23326 C  CA  . PHE C 1 1174 ? -18.219  47.799  114.890 1.00 123.44 ? 1174 PHE B CA  1 
ATOM   23327 C  C   . PHE C 1 1174 ? -17.088  46.783  114.923 1.00 120.33 ? 1174 PHE B C   1 
ATOM   23328 O  O   . PHE C 1 1174 ? -17.260  45.681  115.428 1.00 121.48 ? 1174 PHE B O   1 
ATOM   23329 C  CB  . PHE C 1 1174 ? -18.829  47.852  113.498 1.00 123.19 ? 1174 PHE B CB  1 
ATOM   23330 C  CG  . PHE C 1 1174 ? -19.174  46.509  112.926 1.00 122.15 ? 1174 PHE B CG  1 
ATOM   23331 C  CD1 . PHE C 1 1174 ? -20.387  45.916  113.200 1.00 123.44 ? 1174 PHE B CD1 1 
ATOM   23332 C  CD2 . PHE C 1 1174 ? -18.297  45.854  112.080 1.00 120.49 ? 1174 PHE B CD2 1 
ATOM   23333 C  CE1 . PHE C 1 1174 ? -20.715  44.688  112.647 1.00 124.34 ? 1174 PHE B CE1 1 
ATOM   23334 C  CE2 . PHE C 1 1174 ? -18.622  44.627  111.525 1.00 121.06 ? 1174 PHE B CE2 1 
ATOM   23335 C  CZ  . PHE C 1 1174 ? -19.830  44.044  111.810 1.00 122.76 ? 1174 PHE B CZ  1 
ATOM   23336 N  N   . LEU C 1 1175 ? -15.926  47.160  114.409 1.00 115.64 ? 1175 LEU B N   1 
ATOM   23337 C  CA  . LEU C 1 1175 ? -14.810  46.227  114.327 1.00 114.43 ? 1175 LEU B CA  1 
ATOM   23338 C  C   . LEU C 1 1175 ? -14.286  45.798  115.708 1.00 114.23 ? 1175 LEU B C   1 
ATOM   23339 O  O   . LEU C 1 1175 ? -14.132  44.605  115.982 1.00 113.83 ? 1175 LEU B O   1 
ATOM   23340 C  CB  . LEU C 1 1175 ? -13.684  46.805  113.467 1.00 113.09 ? 1175 LEU B CB  1 
ATOM   23341 C  CG  . LEU C 1 1175 ? -14.006  47.007  111.984 1.00 113.05 ? 1175 LEU B CG  1 
ATOM   23342 C  CD1 . LEU C 1 1175 ? -12.842  47.687  111.277 1.00 111.95 ? 1175 LEU B CD1 1 
ATOM   23343 C  CD2 . LEU C 1 1175 ? -14.358  45.692  111.301 1.00 113.25 ? 1175 LEU B CD2 1 
ATOM   23344 N  N   . LEU C 1 1176 ? -14.014  46.767  116.575 1.00 114.83 ? 1176 LEU B N   1 
ATOM   23345 C  CA  . LEU C 1 1176 ? -13.696  46.461  117.962 1.00 115.67 ? 1176 LEU B CA  1 
ATOM   23346 C  C   . LEU C 1 1176 ? -14.752  45.532  118.540 1.00 121.78 ? 1176 LEU B C   1 
ATOM   23347 O  O   . LEU C 1 1176 ? -14.453  44.464  119.103 1.00 123.41 ? 1176 LEU B O   1 
ATOM   23348 C  CB  . LEU C 1 1176 ? -13.715  47.735  118.776 1.00 110.69 ? 1176 LEU B CB  1 
ATOM   23349 C  CG  . LEU C 1 1176 ? -12.628  48.711  118.428 1.00 105.93 ? 1176 LEU B CG  1 
ATOM   23350 C  CD1 . LEU C 1 1176 ? -12.722  49.835  119.408 1.00 105.81 ? 1176 LEU B CD1 1 
ATOM   23351 C  CD2 . LEU C 1 1176 ? -11.295  48.019  118.544 1.00 103.69 ? 1176 LEU B CD2 1 
ATOM   23352 N  N   . GLU C 1 1177 ? -15.999  45.973  118.394 1.00 125.39 ? 1177 GLU B N   1 
ATOM   23353 C  CA  . GLU C 1 1177 ? -17.145  45.309  118.986 1.00 129.70 ? 1177 GLU B CA  1 
ATOM   23354 C  C   . GLU C 1 1177 ? -17.508  43.998  118.298 1.00 130.14 ? 1177 GLU B C   1 
ATOM   23355 O  O   . GLU C 1 1177 ? -18.349  43.270  118.816 1.00 133.37 ? 1177 GLU B O   1 
ATOM   23356 C  CB  . GLU C 1 1177 ? -18.367  46.235  118.977 1.00 135.57 ? 1177 GLU B CB  1 
ATOM   23357 C  CG  . GLU C 1 1177 ? -18.416  47.270  120.099 1.00 141.25 ? 1177 GLU B CG  1 
ATOM   23358 C  CD  . GLU C 1 1177 ? -19.843  47.702  120.405 1.00 148.77 ? 1177 GLU B CD  1 
ATOM   23359 O  OE1 . GLU C 1 1177 ? -20.205  47.783  121.605 1.00 151.66 ? 1177 GLU B OE1 1 
ATOM   23360 O  OE2 . GLU C 1 1177 ? -20.612  47.940  119.439 1.00 151.36 ? 1177 GLU B OE2 1 
ATOM   23361 N  N   . ASN C 1 1178 ? -16.877  43.682  117.162 1.00 126.89 ? 1178 ASN B N   1 
ATOM   23362 C  CA  . ASN C 1 1178 ? -17.306  42.527  116.346 1.00 125.01 ? 1178 ASN B CA  1 
ATOM   23363 C  C   . ASN C 1 1178 ? -16.257  41.595  115.722 1.00 122.06 ? 1178 ASN B C   1 
ATOM   23364 O  O   . ASN C 1 1178 ? -16.605  40.682  114.965 1.00 123.20 ? 1178 ASN B O   1 
ATOM   23365 C  CB  . ASN C 1 1178 ? -18.268  42.977  115.249 1.00 124.25 ? 1178 ASN B CB  1 
ATOM   23366 C  CG  . ASN C 1 1178 ? -19.675  42.520  115.496 1.00 124.15 ? 1178 ASN B CG  1 
ATOM   23367 O  OD1 . ASN C 1 1178 ? -19.962  41.321  115.498 1.00 124.20 ? 1178 ASN B OD1 1 
ATOM   23368 N  ND2 . ASN C 1 1178 ? -20.571  43.475  115.695 1.00 124.46 ? 1178 ASN B ND2 1 
ATOM   23369 N  N   . THR C 1 1179 ? -14.990  41.815  116.034 1.00 117.56 ? 1179 THR B N   1 
ATOM   23370 C  CA  . THR C 1 1179 ? -13.929  40.935  115.575 1.00 114.46 ? 1179 THR B CA  1 
ATOM   23371 C  C   . THR C 1 1179 ? -13.812  39.694  116.454 1.00 112.72 ? 1179 THR B C   1 
ATOM   23372 O  O   . THR C 1 1179 ? -13.941  38.567  115.983 1.00 111.12 ? 1179 THR B O   1 
ATOM   23373 C  CB  . THR C 1 1179 ? -12.563  41.677  115.667 1.00 97.04  ? 1179 THR B CB  1 
ATOM   23374 O  OG1 . THR C 1 1179 ? -12.684  42.981  115.094 1.00 98.89  ? 1179 THR B OG1 1 
ATOM   23375 C  CG2 . THR C 1 1179 ? -11.408  40.891  115.006 1.00 92.27  ? 1179 THR B CG2 1 
ATOM   23376 N  N   . LEU C 1 1180 ? -13.630  39.937  117.752 1.00 113.35 ? 1180 LEU B N   1 
ATOM   23377 C  CA  . LEU C 1 1180 ? -12.657  39.169  118.539 1.00 113.64 ? 1180 LEU B CA  1 
ATOM   23378 C  C   . LEU C 1 1180 ? -12.836  37.695  118.809 1.00 119.76 ? 1180 LEU B C   1 
ATOM   23379 O  O   . LEU C 1 1180 ? -11.822  36.989  118.918 1.00 121.41 ? 1180 LEU B O   1 
ATOM   23380 C  CB  . LEU C 1 1180 ? -12.201  39.908  119.794 1.00 108.46 ? 1180 LEU B CB  1 
ATOM   23381 C  CG  . LEU C 1 1180 ? -10.796  40.414  119.461 1.00 103.05 ? 1180 LEU B CG  1 
ATOM   23382 C  CD1 . LEU C 1 1180 ? -10.158  41.137  120.615 1.00 101.42 ? 1180 LEU B CD1 1 
ATOM   23383 C  CD2 . LEU C 1 1180 ? -9.942   39.258  118.983 1.00 100.92 ? 1180 LEU B CD2 1 
ATOM   23384 N  N   . PRO C 1 1181 ? -14.095  37.225  118.953 1.00 122.28 ? 1181 PRO B N   1 
ATOM   23385 C  CA  . PRO C 1 1181 ? -14.299  35.778  118.821 1.00 121.73 ? 1181 PRO B CA  1 
ATOM   23386 C  C   . PRO C 1 1181 ? -13.972  35.494  117.367 1.00 121.76 ? 1181 PRO B C   1 
ATOM   23387 O  O   . PRO C 1 1181 ? -14.875  35.349  116.534 1.00 121.61 ? 1181 PRO B O   1 
ATOM   23388 C  CB  . PRO C 1 1181 ? -15.790  35.606  119.087 1.00 122.11 ? 1181 PRO B CB  1 
ATOM   23389 C  CG  . PRO C 1 1181 ? -16.196  36.833  119.824 1.00 121.51 ? 1181 PRO B CG  1 
ATOM   23390 C  CD  . PRO C 1 1181 ? -15.337  37.934  119.305 1.00 120.64 ? 1181 PRO B CD  1 
ATOM   23391 N  N   . ALA C 1 1182 ? -12.670  35.474  117.074 1.00 120.59 ? 1182 ALA B N   1 
ATOM   23392 C  CA  . ALA C 1 1182 ? -12.158  35.539  115.711 1.00 117.79 ? 1182 ALA B CA  1 
ATOM   23393 C  C   . ALA C 1 1182 ? -12.586  34.316  114.888 1.00 122.29 ? 1182 ALA B C   1 
ATOM   23394 O  O   . ALA C 1 1182 ? -12.445  33.171  115.341 1.00 124.99 ? 1182 ALA B O   1 
ATOM   23395 C  CB  . ALA C 1 1182 ? -10.633  35.714  115.724 1.00 112.35 ? 1182 ALA B CB  1 
ATOM   23396 N  N   . GLN C 1 1183 ? -13.119  34.568  113.689 1.00 119.84 ? 1183 GLN B N   1 
ATOM   23397 C  CA  . GLN C 1 1183 ? -13.631  33.509  112.834 1.00 118.54 ? 1183 GLN B CA  1 
ATOM   23398 C  C   . GLN C 1 1183 ? -12.618  33.015  111.807 1.00 113.60 ? 1183 GLN B C   1 
ATOM   23399 O  O   . GLN C 1 1183 ? -12.531  31.814  111.542 1.00 115.93 ? 1183 GLN B O   1 
ATOM   23400 C  CB  . GLN C 1 1183 ? -14.909  33.962  112.155 1.00 121.77 ? 1183 GLN B CB  1 
ATOM   23401 C  CG  . GLN C 1 1183 ? -15.659  32.824  111.503 1.00 127.04 ? 1183 GLN B CG  1 
ATOM   23402 C  CD  . GLN C 1 1183 ? -15.874  31.664  112.449 1.00 130.26 ? 1183 GLN B CD  1 
ATOM   23403 O  OE1 . GLN C 1 1183 ? -15.610  31.780  113.650 1.00 130.65 ? 1183 GLN B OE1 1 
ATOM   23404 N  NE2 . GLN C 1 1183 ? -16.356  30.536  111.919 1.00 132.25 ? 1183 GLN B NE2 1 
ATOM   23405 N  N   . SER C 1 1184 ? -11.857  33.943  111.234 1.00 107.12 ? 1184 SER B N   1 
ATOM   23406 C  CA  . SER C 1 1184 ? -10.654  33.572  110.482 1.00 105.39 ? 1184 SER B CA  1 
ATOM   23407 C  C   . SER C 1 1184 ? -9.438   34.475  110.709 1.00 102.35 ? 1184 SER B C   1 
ATOM   23408 O  O   . SER C 1 1184 ? -9.567   35.697  110.809 1.00 101.23 ? 1184 SER B O   1 
ATOM   23409 C  CB  . SER C 1 1184 ? -10.921  33.567  108.993 1.00 106.47 ? 1184 SER B CB  1 
ATOM   23410 O  OG  . SER C 1 1184 ? -9.740   33.984  108.321 1.00 105.67 ? 1184 SER B OG  1 
ATOM   23411 N  N   . THR C 1 1185 ? -8.255   33.872  110.742 1.00 100.79 ? 1185 THR B N   1 
ATOM   23412 C  CA  . THR C 1 1185 ? -7.003   34.617  110.762 1.00 96.98  ? 1185 THR B CA  1 
ATOM   23413 C  C   . THR C 1 1185 ? -6.939   35.749  109.736 1.00 95.28  ? 1185 THR B C   1 
ATOM   23414 O  O   . THR C 1 1185 ? -6.575   36.870  110.063 1.00 91.35  ? 1185 THR B O   1 
ATOM   23415 C  CB  . THR C 1 1185 ? -5.861   33.684  110.475 1.00 96.25  ? 1185 THR B CB  1 
ATOM   23416 O  OG1 . THR C 1 1185 ? -5.774   32.713  111.530 1.00 97.04  ? 1185 THR B OG1 1 
ATOM   23417 C  CG2 . THR C 1 1185 ? -4.569   34.470  110.358 1.00 93.30  ? 1185 THR B CG2 1 
ATOM   23418 N  N   . PHE C 1 1186 ? -7.294   35.435  108.493 1.00 97.88  ? 1186 PHE B N   1 
ATOM   23419 C  CA  . PHE C 1 1186 ? -7.494   36.443  107.450 1.00 96.31  ? 1186 PHE B CA  1 
ATOM   23420 C  C   . PHE C 1 1186 ? -8.436   37.567  107.884 1.00 98.81  ? 1186 PHE B C   1 
ATOM   23421 O  O   . PHE C 1 1186 ? -8.038   38.725  107.891 1.00 99.77  ? 1186 PHE B O   1 
ATOM   23422 C  CB  . PHE C 1 1186 ? -8.082   35.830  106.182 1.00 94.80  ? 1186 PHE B CB  1 
ATOM   23423 C  CG  . PHE C 1 1186 ? -8.346   36.838  105.105 1.00 91.30  ? 1186 PHE B CG  1 
ATOM   23424 C  CD1 . PHE C 1 1186 ? -7.384   37.112  104.149 1.00 90.24  ? 1186 PHE B CD1 1 
ATOM   23425 C  CD2 . PHE C 1 1186 ? -9.536   37.529  105.059 1.00 90.30  ? 1186 PHE B CD2 1 
ATOM   23426 C  CE1 . PHE C 1 1186 ? -7.609   38.054  103.162 1.00 89.12  ? 1186 PHE B CE1 1 
ATOM   23427 C  CE2 . PHE C 1 1186 ? -9.763   38.467  104.069 1.00 90.16  ? 1186 PHE B CE2 1 
ATOM   23428 C  CZ  . PHE C 1 1186 ? -8.796   38.732  103.128 1.00 89.14  ? 1186 PHE B CZ  1 
ATOM   23429 N  N   . THR C 1 1187 ? -9.692   37.239  108.202 1.00 98.83  ? 1187 THR B N   1 
ATOM   23430 C  CA  . THR C 1 1187 ? -10.623  38.234  108.744 1.00 97.53  ? 1187 THR B CA  1 
ATOM   23431 C  C   . THR C 1 1187 ? -9.972   39.049  109.860 1.00 95.02  ? 1187 THR B C   1 
ATOM   23432 O  O   . THR C 1 1187 ? -10.029  40.285  109.852 1.00 95.22  ? 1187 THR B O   1 
ATOM   23433 C  CB  . THR C 1 1187 ? -11.877  37.585  109.358 1.00 97.56  ? 1187 THR B CB  1 
ATOM   23434 O  OG1 . THR C 1 1187 ? -12.397  36.581  108.478 1.00 97.84  ? 1187 THR B OG1 1 
ATOM   23435 C  CG2 . THR C 1 1187 ? -12.938  38.650  109.619 1.00 97.69  ? 1187 THR B CG2 1 
ATOM   23436 N  N   . LEU C 1 1188 ? -9.357   38.346  110.809 1.00 91.65  ? 1188 LEU B N   1 
ATOM   23437 C  CA  . LEU C 1 1188 ? -8.763   38.972  111.973 1.00 90.91  ? 1188 LEU B CA  1 
ATOM   23438 C  C   . LEU C 1 1188 ? -7.774   40.007  111.528 1.00 88.90  ? 1188 LEU B C   1 
ATOM   23439 O  O   . LEU C 1 1188 ? -7.878   41.187  111.853 1.00 88.58  ? 1188 LEU B O   1 
ATOM   23440 C  CB  . LEU C 1 1188 ? -8.028   37.924  112.795 1.00 91.66  ? 1188 LEU B CB  1 
ATOM   23441 C  CG  . LEU C 1 1188 ? -7.536   38.282  114.197 1.00 86.85  ? 1188 LEU B CG  1 
ATOM   23442 C  CD1 . LEU C 1 1188 ? -8.697   38.511  115.191 1.00 86.00  ? 1188 LEU B CD1 1 
ATOM   23443 C  CD2 . LEU C 1 1188 ? -6.631   37.173  114.640 1.00 85.22  ? 1188 LEU B CD2 1 
ATOM   23444 N  N   . ALA C 1 1189 ? -6.803   39.538  110.765 1.00 89.97  ? 1189 ALA B N   1 
ATOM   23445 C  CA  . ALA C 1 1189 ? -5.697   40.376  110.311 1.00 89.88  ? 1189 ALA B CA  1 
ATOM   23446 C  C   . ALA C 1 1189 ? -6.115   41.706  109.660 1.00 90.98  ? 1189 ALA B C   1 
ATOM   23447 O  O   . ALA C 1 1189 ? -5.490   42.743  109.930 1.00 88.74  ? 1189 ALA B O   1 
ATOM   23448 C  CB  . ALA C 1 1189 ? -4.797   39.586  109.349 1.00 91.31  ? 1189 ALA B CB  1 
ATOM   23449 N  N   . ILE C 1 1190 ? -7.139   41.694  108.800 1.00 91.77  ? 1190 ILE B N   1 
ATOM   23450 C  CA  . ILE C 1 1190 ? -7.592   42.952  108.218 1.00 92.11  ? 1190 ILE B CA  1 
ATOM   23451 C  C   . ILE C 1 1190 ? -8.177   43.770  109.356 1.00 94.22  ? 1190 ILE B C   1 
ATOM   23452 O  O   . ILE C 1 1190 ? -7.694   44.879  109.661 1.00 92.67  ? 1190 ILE B O   1 
ATOM   23453 C  CB  . ILE C 1 1190 ? -8.570   42.770  107.051 1.00 92.74  ? 1190 ILE B CB  1 
ATOM   23454 C  CG1 . ILE C 1 1190 ? -7.858   42.106  105.877 1.00 91.61  ? 1190 ILE B CG1 1 
ATOM   23455 C  CG2 . ILE C 1 1190 ? -9.084   44.121  106.556 1.00 91.60  ? 1190 ILE B CG2 1 
ATOM   23456 C  CD1 . ILE C 1 1190 ? -8.570   42.275  104.565 1.00 91.88  ? 1190 ILE B CD1 1 
ATOM   23457 N  N   . SER C 1 1191 ? -9.168   43.198  110.030 1.00 94.54  ? 1191 SER B N   1 
ATOM   23458 C  CA  . SER C 1 1191 ? -9.695   43.851  111.207 1.00 93.07  ? 1191 SER B CA  1 
ATOM   23459 C  C   . SER C 1 1191 ? -8.559   44.501  111.983 1.00 89.95  ? 1191 SER B C   1 
ATOM   23460 O  O   . SER C 1 1191 ? -8.602   45.692  112.266 1.00 88.96  ? 1191 SER B O   1 
ATOM   23461 C  CB  . SER C 1 1191 ? -10.429  42.867  112.085 1.00 92.67  ? 1191 SER B CB  1 
ATOM   23462 O  OG  . SER C 1 1191 ? -11.434  43.578  112.770 1.00 93.61  ? 1191 SER B OG  1 
ATOM   23463 N  N   . ALA C 1 1192 ? -7.527   43.724  112.290 1.00 89.10  ? 1192 ALA B N   1 
ATOM   23464 C  CA  . ALA C 1 1192 ? -6.369   44.253  112.991 1.00 87.52  ? 1192 ALA B CA  1 
ATOM   23465 C  C   . ALA C 1 1192 ? -5.763   45.440  112.236 1.00 89.27  ? 1192 ALA B C   1 
ATOM   23466 O  O   . ALA C 1 1192 ? -5.781   46.567  112.734 1.00 91.82  ? 1192 ALA B O   1 
ATOM   23467 C  CB  . ALA C 1 1192 ? -5.335   43.161  113.216 1.00 84.10  ? 1192 ALA B CB  1 
ATOM   23468 N  N   . TYR C 1 1193 ? -5.240   45.197  111.035 1.00 89.83  ? 1193 TYR B N   1 
ATOM   23469 C  CA  . TYR C 1 1193 ? -4.545   46.255  110.295 1.00 90.33  ? 1193 TYR B CA  1 
ATOM   23470 C  C   . TYR C 1 1193 ? -5.423   47.523  110.184 1.00 90.24  ? 1193 TYR B C   1 
ATOM   23471 O  O   . TYR C 1 1193 ? -4.918   48.652  110.117 1.00 91.79  ? 1193 TYR B O   1 
ATOM   23472 C  CB  . TYR C 1 1193 ? -4.049   45.783  108.896 1.00 89.71  ? 1193 TYR B CB  1 
ATOM   23473 C  CG  . TYR C 1 1193 ? -3.476   46.925  108.062 1.00 88.63  ? 1193 TYR B CG  1 
ATOM   23474 C  CD1 . TYR C 1 1193 ? -2.251   47.488  108.390 1.00 89.22  ? 1193 TYR B CD1 1 
ATOM   23475 C  CD2 . TYR C 1 1193 ? -4.181   47.474  106.990 1.00 86.65  ? 1193 TYR B CD2 1 
ATOM   23476 C  CE1 . TYR C 1 1193 ? -1.720   48.557  107.670 1.00 88.83  ? 1193 TYR B CE1 1 
ATOM   23477 C  CE2 . TYR C 1 1193 ? -3.657   48.550  106.260 1.00 86.85  ? 1193 TYR B CE2 1 
ATOM   23478 C  CZ  . TYR C 1 1193 ? -2.411   49.089  106.611 1.00 87.22  ? 1193 TYR B CZ  1 
ATOM   23479 O  OH  . TYR C 1 1193 ? -1.833   50.155  105.931 1.00 84.68  ? 1193 TYR B OH  1 
ATOM   23480 N  N   . ALA C 1 1194 ? -6.738   47.342  110.186 1.00 87.69  ? 1194 ALA B N   1 
ATOM   23481 C  CA  . ALA C 1 1194 ? -7.623   48.471  109.949 1.00 85.81  ? 1194 ALA B CA  1 
ATOM   23482 C  C   . ALA C 1 1194 ? -7.724   49.377  111.162 1.00 85.05  ? 1194 ALA B C   1 
ATOM   23483 O  O   . ALA C 1 1194 ? -7.875   50.598  111.035 1.00 85.34  ? 1194 ALA B O   1 
ATOM   23484 C  CB  . ALA C 1 1194 ? -9.002   47.986  109.522 1.00 87.52  ? 1194 ALA B CB  1 
ATOM   23485 N  N   . LEU C 1 1195 ? -7.668   48.768  112.340 1.00 83.08  ? 1195 LEU B N   1 
ATOM   23486 C  CA  . LEU C 1 1195 ? -7.741   49.520  113.583 1.00 82.21  ? 1195 LEU B CA  1 
ATOM   23487 C  C   . LEU C 1 1195 ? -6.391   50.181  113.725 1.00 83.28  ? 1195 LEU B C   1 
ATOM   23488 O  O   . LEU C 1 1195 ? -6.286   51.396  113.886 1.00 83.45  ? 1195 LEU B O   1 
ATOM   23489 C  CB  . LEU C 1 1195 ? -8.064   48.581  114.755 1.00 79.91  ? 1195 LEU B CB  1 
ATOM   23490 C  CG  . LEU C 1 1195 ? -9.364   47.786  114.502 1.00 81.21  ? 1195 LEU B CG  1 
ATOM   23491 C  CD1 . LEU C 1 1195 ? -9.451   46.545  115.355 1.00 81.96  ? 1195 LEU B CD1 1 
ATOM   23492 C  CD2 . LEU C 1 1195 ? -10.638  48.635  114.654 1.00 81.87  ? 1195 LEU B CD2 1 
ATOM   23493 N  N   . SER C 1 1196 ? -5.362   49.355  113.592 1.00 83.65  ? 1196 SER B N   1 
ATOM   23494 C  CA  . SER C 1 1196 ? -3.982   49.800  113.494 1.00 85.51  ? 1196 SER B CA  1 
ATOM   23495 C  C   . SER C 1 1196 ? -3.869   51.216  112.899 1.00 88.23  ? 1196 SER B C   1 
ATOM   23496 O  O   . SER C 1 1196 ? -2.962   51.988  113.215 1.00 85.31  ? 1196 SER B O   1 
ATOM   23497 C  CB  . SER C 1 1196 ? -3.203   48.769  112.668 1.00 84.79  ? 1196 SER B CB  1 
ATOM   23498 O  OG  . SER C 1 1196 ? -2.047   49.327  112.094 1.00 85.89  ? 1196 SER B OG  1 
ATOM   23499 N  N   . LEU C 1 1197 ? -4.806   51.556  112.032 1.00 96.58  ? 1197 LEU B N   1 
ATOM   23500 C  CA  . LEU C 1 1197 ? -4.790   52.864  111.388 1.00 106.24 ? 1197 LEU B CA  1 
ATOM   23501 C  C   . LEU C 1 1197 ? -5.780   53.826  112.041 1.00 112.69 ? 1197 LEU B C   1 
ATOM   23502 O  O   . LEU C 1 1197 ? -6.581   54.477  111.371 1.00 113.37 ? 1197 LEU B O   1 
ATOM   23503 C  CB  . LEU C 1 1197 ? -5.065   52.731  109.880 1.00 109.28 ? 1197 LEU B CB  1 
ATOM   23504 C  CG  . LEU C 1 1197 ? -4.328   51.626  109.111 1.00 111.84 ? 1197 LEU B CG  1 
ATOM   23505 C  CD1 . LEU C 1 1197 ? -4.736   51.665  107.657 1.00 114.51 ? 1197 LEU B CD1 1 
ATOM   23506 C  CD2 . LEU C 1 1197 ? -2.809   51.729  109.233 1.00 112.15 ? 1197 LEU B CD2 1 
ATOM   23507 N  N   . GLY C 1 1198 ? -5.726   53.917  113.357 1.00 118.26 ? 1198 GLY B N   1 
ATOM   23508 C  CA  . GLY C 1 1198 ? -6.652   54.774  114.062 1.00 124.31 ? 1198 GLY B CA  1 
ATOM   23509 C  C   . GLY C 1 1198 ? -6.117   55.012  115.451 1.00 127.22 ? 1198 GLY B C   1 
ATOM   23510 O  O   . GLY C 1 1198 ? -5.001   55.538  115.615 1.00 128.78 ? 1198 GLY B O   1 
ATOM   23511 N  N   . ASP C 1 1199 ? -6.915   54.628  116.450 1.00 125.55 ? 1199 ASP B N   1 
ATOM   23512 C  CA  . ASP C 1 1199 ? -6.428   54.570  117.825 1.00 122.10 ? 1199 ASP B CA  1 
ATOM   23513 C  C   . ASP C 1 1199 ? -5.864   53.195  118.118 1.00 112.51 ? 1199 ASP B C   1 
ATOM   23514 O  O   . ASP C 1 1199 ? -6.619   52.222  118.189 1.00 111.46 ? 1199 ASP B O   1 
ATOM   23515 C  CB  . ASP C 1 1199 ? -7.538   54.860  118.820 1.00 127.79 ? 1199 ASP B CB  1 
ATOM   23516 C  CG  . ASP C 1 1199 ? -7.123   54.537  120.231 1.00 132.45 ? 1199 ASP B CG  1 
ATOM   23517 O  OD1 . ASP C 1 1199 ? -5.894   54.478  120.481 1.00 131.60 ? 1199 ASP B OD1 1 
ATOM   23518 O  OD2 . ASP C 1 1199 ? -8.021   54.336  121.078 1.00 136.46 ? 1199 ASP B OD2 1 
ATOM   23519 N  N   . LYS C 1 1200 ? -4.550   53.113  118.285 1.00 104.19 ? 1200 LYS B N   1 
ATOM   23520 C  CA  . LYS C 1 1200 ? -3.925   51.827  118.501 1.00 99.49  ? 1200 LYS B CA  1 
ATOM   23521 C  C   . LYS C 1 1200 ? -3.619   51.654  119.994 1.00 103.44 ? 1200 LYS B C   1 
ATOM   23522 O  O   . LYS C 1 1200 ? -2.570   51.119  120.383 1.00 107.28 ? 1200 LYS B O   1 
ATOM   23523 C  CB  . LYS C 1 1200 ? -2.691   51.689  117.622 1.00 94.92  ? 1200 LYS B CB  1 
ATOM   23524 C  CG  . LYS C 1 1200 ? -2.113   53.025  117.264 1.00 96.86  ? 1200 LYS B CG  1 
ATOM   23525 C  CD  . LYS C 1 1200 ? -1.363   53.008  115.938 1.00 100.54 ? 1200 LYS B CD  1 
ATOM   23526 C  CE  . LYS C 1 1200 ? 0.134    52.671  116.079 1.00 101.99 ? 1200 LYS B CE  1 
ATOM   23527 N  NZ  . LYS C 1 1200 ? 0.967    53.352  115.013 1.00 103.02 ? 1200 LYS B NZ  1 
ATOM   23528 N  N   . THR C 1 1201 ? -4.535   52.105  120.851 1.00 100.77 ? 1201 THR B N   1 
ATOM   23529 C  CA  . THR C 1 1201 ? -4.397   51.825  122.280 1.00 97.63  ? 1201 THR B CA  1 
ATOM   23530 C  C   . THR C 1 1201 ? -5.696   51.412  122.938 1.00 98.82  ? 1201 THR B C   1 
ATOM   23531 O  O   . THR C 1 1201 ? -5.702   50.983  124.089 1.00 98.63  ? 1201 THR B O   1 
ATOM   23532 C  CB  . THR C 1 1201 ? -3.861   53.004  123.052 1.00 95.11  ? 1201 THR B CB  1 
ATOM   23533 O  OG1 . THR C 1 1201 ? -4.715   54.130  122.821 1.00 95.40  ? 1201 THR B OG1 1 
ATOM   23534 C  CG2 . THR C 1 1201 ? -2.406   53.305  122.669 1.00 92.09  ? 1201 THR B CG2 1 
ATOM   23535 N  N   . HIS C 1 1202 ? -6.803   51.541  122.224 1.00 102.89 ? 1202 HIS B N   1 
ATOM   23536 C  CA  . HIS C 1 1202 ? -8.025   50.983  122.759 1.00 106.48 ? 1202 HIS B CA  1 
ATOM   23537 C  C   . HIS C 1 1202 ? -7.657   49.598  123.226 1.00 110.04 ? 1202 HIS B C   1 
ATOM   23538 O  O   . HIS C 1 1202 ? -7.025   48.830  122.500 1.00 109.16 ? 1202 HIS B O   1 
ATOM   23539 C  CB  . HIS C 1 1202 ? -9.151   50.895  121.743 1.00 106.06 ? 1202 HIS B CB  1 
ATOM   23540 C  CG  . HIS C 1 1202 ? -10.467  50.577  122.364 1.00 107.40 ? 1202 HIS B CG  1 
ATOM   23541 N  ND1 . HIS C 1 1202 ? -11.595  51.332  122.151 1.00 110.20 ? 1202 HIS B ND1 1 
ATOM   23542 C  CD2 . HIS C 1 1202 ? -10.826  49.602  123.230 1.00 108.37 ? 1202 HIS B CD2 1 
ATOM   23543 C  CE1 . HIS C 1 1202 ? -12.604  50.826  122.838 1.00 110.56 ? 1202 HIS B CE1 1 
ATOM   23544 N  NE2 . HIS C 1 1202 ? -12.162  49.777  123.504 1.00 110.36 ? 1202 HIS B NE2 1 
ATOM   23545 N  N   . PRO C 1 1203 ? -8.034   49.287  124.462 1.00 113.32 ? 1203 PRO B N   1 
ATOM   23546 C  CA  . PRO C 1 1203 ? -7.695   48.051  125.172 1.00 114.82 ? 1203 PRO B CA  1 
ATOM   23547 C  C   . PRO C 1 1203 ? -8.078   46.894  124.287 1.00 111.29 ? 1203 PRO B C   1 
ATOM   23548 O  O   . PRO C 1 1203 ? -7.295   45.975  124.043 1.00 112.57 ? 1203 PRO B O   1 
ATOM   23549 C  CB  . PRO C 1 1203 ? -8.640   48.079  126.369 1.00 117.44 ? 1203 PRO B CB  1 
ATOM   23550 C  CG  . PRO C 1 1203 ? -8.943   49.550  126.574 1.00 117.81 ? 1203 PRO B CG  1 
ATOM   23551 C  CD  . PRO C 1 1203 ? -8.940   50.158  125.229 1.00 115.19 ? 1203 PRO B CD  1 
ATOM   23552 N  N   . GLN C 1 1204 ? -9.309   46.982  123.805 1.00 106.56 ? 1204 GLN B N   1 
ATOM   23553 C  CA  . GLN C 1 1204 ? -9.879   46.056  122.849 1.00 101.41 ? 1204 GLN B CA  1 
ATOM   23554 C  C   . GLN C 1 1204 ? -8.987   45.804  121.617 1.00 95.61  ? 1204 GLN B C   1 
ATOM   23555 O  O   . GLN C 1 1204 ? -8.692   44.658  121.310 1.00 92.26  ? 1204 GLN B O   1 
ATOM   23556 C  CB  . GLN C 1 1204 ? -11.246  46.599  122.457 1.00 102.34 ? 1204 GLN B CB  1 
ATOM   23557 C  CG  . GLN C 1 1204 ? -11.988  45.795  121.478 1.00 100.19 ? 1204 GLN B CG  1 
ATOM   23558 C  CD  . GLN C 1 1204 ? -12.137  44.398  121.934 1.00 98.67  ? 1204 GLN B CD  1 
ATOM   23559 O  OE1 . GLN C 1 1204 ? -11.740  44.032  123.050 1.00 96.00  ? 1204 GLN B OE1 1 
ATOM   23560 N  NE2 . GLN C 1 1204 ? -12.716  43.578  121.066 1.00 100.15 ? 1204 GLN B NE2 1 
ATOM   23561 N  N   . PHE C 1 1205 ? -8.555   46.859  120.924 1.00 92.87  ? 1205 PHE B N   1 
ATOM   23562 C  CA  . PHE C 1 1205 ? -7.581   46.692  119.845 1.00 89.59  ? 1205 PHE B CA  1 
ATOM   23563 C  C   . PHE C 1 1205 ? -6.439   45.790  120.311 1.00 89.96  ? 1205 PHE B C   1 
ATOM   23564 O  O   . PHE C 1 1205 ? -6.131   44.797  119.642 1.00 90.00  ? 1205 PHE B O   1 
ATOM   23565 C  CB  . PHE C 1 1205 ? -7.048   48.044  119.324 1.00 82.71  ? 1205 PHE B CB  1 
ATOM   23566 C  CG  . PHE C 1 1205 ? -5.844   47.933  118.371 1.00 77.95  ? 1205 PHE B CG  1 
ATOM   23567 C  CD1 . PHE C 1 1205 ? -5.968   47.355  117.111 1.00 77.99  ? 1205 PHE B CD1 1 
ATOM   23568 C  CD2 . PHE C 1 1205 ? -4.603   48.458  118.727 1.00 73.20  ? 1205 PHE B CD2 1 
ATOM   23569 C  CE1 . PHE C 1 1205 ? -4.857   47.279  116.254 1.00 76.79  ? 1205 PHE B CE1 1 
ATOM   23570 C  CE2 . PHE C 1 1205 ? -3.495   48.384  117.879 1.00 71.58  ? 1205 PHE B CE2 1 
ATOM   23571 C  CZ  . PHE C 1 1205 ? -3.613   47.795  116.658 1.00 73.72  ? 1205 PHE B CZ  1 
ATOM   23572 N  N   . ARG C 1 1206 ? -5.833   46.121  121.458 1.00 89.82  ? 1206 ARG B N   1 
ATOM   23573 C  CA  . ARG C 1 1206 ? -4.711   45.337  122.002 1.00 91.30  ? 1206 ARG B CA  1 
ATOM   23574 C  C   . ARG C 1 1206 ? -5.081   43.860  122.226 1.00 89.31  ? 1206 ARG B C   1 
ATOM   23575 O  O   . ARG C 1 1206 ? -4.218   42.966  122.179 1.00 87.27  ? 1206 ARG B O   1 
ATOM   23576 C  CB  . ARG C 1 1206 ? -4.158   45.956  123.295 1.00 94.41  ? 1206 ARG B CB  1 
ATOM   23577 C  CG  . ARG C 1 1206 ? -3.729   47.408  123.182 1.00 99.56  ? 1206 ARG B CG  1 
ATOM   23578 C  CD  . ARG C 1 1206 ? -2.450   47.659  123.973 1.00 105.81 ? 1206 ARG B CD  1 
ATOM   23579 N  NE  . ARG C 1 1206 ? -2.063   49.071  124.141 1.00 111.08 ? 1206 ARG B NE  1 
ATOM   23580 C  CZ  . ARG C 1 1206 ? -2.560   49.893  125.076 1.00 114.30 ? 1206 ARG B CZ  1 
ATOM   23581 N  NH1 . ARG C 1 1206 ? -3.511   49.475  125.921 1.00 114.98 ? 1206 ARG B NH1 1 
ATOM   23582 N  NH2 . ARG C 1 1206 ? -2.120   51.148  125.159 1.00 114.70 ? 1206 ARG B NH2 1 
ATOM   23583 N  N   . SER C 1 1207 ? -6.373   43.629  122.471 1.00 89.20  ? 1207 SER B N   1 
ATOM   23584 C  CA  . SER C 1 1207 ? -6.932   42.284  122.601 1.00 87.88  ? 1207 SER B CA  1 
ATOM   23585 C  C   . SER C 1 1207 ? -6.822   41.614  121.244 1.00 85.49  ? 1207 SER B C   1 
ATOM   23586 O  O   . SER C 1 1207 ? -6.267   40.512  121.124 1.00 85.57  ? 1207 SER B O   1 
ATOM   23587 C  CB  . SER C 1 1207 ? -8.415   42.345  123.031 1.00 89.31  ? 1207 SER B CB  1 
ATOM   23588 O  OG  . SER C 1 1207 ? -8.913   41.103  123.542 1.00 90.21  ? 1207 SER B OG  1 
ATOM   23589 N  N   . ILE C 1 1208 ? -7.335   42.308  120.223 1.00 81.36  ? 1208 ILE B N   1 
ATOM   23590 C  CA  . ILE C 1 1208 ? -7.394   41.772  118.872 1.00 74.78  ? 1208 ILE B CA  1 
ATOM   23591 C  C   . ILE C 1 1208 ? -5.987   41.463  118.366 1.00 68.28  ? 1208 ILE B C   1 
ATOM   23592 O  O   . ILE C 1 1208 ? -5.727   40.367  117.837 1.00 65.15  ? 1208 ILE B O   1 
ATOM   23593 C  CB  . ILE C 1 1208 ? -8.103   42.737  117.906 1.00 72.31  ? 1208 ILE B CB  1 
ATOM   23594 C  CG1 . ILE C 1 1208 ? -9.046   43.679  118.642 1.00 69.81  ? 1208 ILE B CG1 1 
ATOM   23595 C  CG2 . ILE C 1 1208 ? -8.903   41.951  116.881 1.00 74.52  ? 1208 ILE B CG2 1 
ATOM   23596 C  CD1 . ILE C 1 1208 ? -10.310  43.990  117.840 1.00 68.25  ? 1208 ILE B CD1 1 
ATOM   23597 N  N   . VAL C 1 1209 ? -5.085   42.426  118.544 1.00 66.05  ? 1209 VAL B N   1 
ATOM   23598 C  CA  . VAL C 1 1209 ? -3.693   42.215  118.208 1.00 69.24  ? 1209 VAL B CA  1 
ATOM   23599 C  C   . VAL C 1 1209 ? -3.104   41.049  118.984 1.00 76.54  ? 1209 VAL B C   1 
ATOM   23600 O  O   . VAL C 1 1209 ? -2.200   40.355  118.497 1.00 76.78  ? 1209 VAL B O   1 
ATOM   23601 C  CB  . VAL C 1 1209 ? -2.875   43.421  118.548 1.00 68.68  ? 1209 VAL B CB  1 
ATOM   23602 C  CG1 . VAL C 1 1209 ? -1.435   43.194  118.109 1.00 69.22  ? 1209 VAL B CG1 1 
ATOM   23603 C  CG2 . VAL C 1 1209 ? -3.455   44.655  117.912 1.00 67.76  ? 1209 VAL B CG2 1 
ATOM   23604 N  N   . SER C 1 1210 ? -3.589   40.868  120.212 1.00 83.13  ? 1210 SER B N   1 
ATOM   23605 C  CA  . SER C 1 1210 ? -3.289   39.655  120.962 1.00 89.03  ? 1210 SER B CA  1 
ATOM   23606 C  C   . SER C 1 1210 ? -3.808   38.458  120.167 1.00 92.46  ? 1210 SER B C   1 
ATOM   23607 O  O   . SER C 1 1210 ? -3.030   37.616  119.686 1.00 94.38  ? 1210 SER B O   1 
ATOM   23608 C  CB  . SER C 1 1210 ? -3.950   39.657  122.338 1.00 91.69  ? 1210 SER B CB  1 
ATOM   23609 O  OG  . SER C 1 1210 ? -4.080   38.313  122.806 1.00 94.44  ? 1210 SER B OG  1 
ATOM   23610 N  N   . ALA C 1 1211 ? -5.127   38.403  120.012 1.00 92.79  ? 1211 ALA B N   1 
ATOM   23611 C  CA  . ALA C 1 1211 ? -5.737   37.382  119.187 1.00 93.37  ? 1211 ALA B CA  1 
ATOM   23612 C  C   . ALA C 1 1211 ? -4.810   37.034  118.040 1.00 92.41  ? 1211 ALA B C   1 
ATOM   23613 O  O   . ALA C 1 1211 ? -4.272   35.925  117.960 1.00 91.03  ? 1211 ALA B O   1 
ATOM   23614 C  CB  . ALA C 1 1211 ? -7.049   37.896  118.654 1.00 94.51  ? 1211 ALA B CB  1 
ATOM   23615 N  N   . LEU C 1 1212 ? -4.618   38.019  117.169 1.00 91.70  ? 1212 LEU B N   1 
ATOM   23616 C  CA  . LEU C 1 1212 ? -3.880   37.815  115.930 1.00 91.98  ? 1212 LEU B CA  1 
ATOM   23617 C  C   . LEU C 1 1212 ? -2.508   37.232  116.215 1.00 90.97  ? 1212 LEU B C   1 
ATOM   23618 O  O   . LEU C 1 1212 ? -2.063   36.268  115.571 1.00 92.05  ? 1212 LEU B O   1 
ATOM   23619 C  CB  . LEU C 1 1212 ? -3.735   39.135  115.157 1.00 89.01  ? 1212 LEU B CB  1 
ATOM   23620 C  CG  . LEU C 1 1212 ? -2.727   39.131  114.002 1.00 86.48  ? 1212 LEU B CG  1 
ATOM   23621 C  CD1 . LEU C 1 1212 ? -2.997   37.984  113.093 1.00 87.16  ? 1212 LEU B CD1 1 
ATOM   23622 C  CD2 . LEU C 1 1212 ? -2.819   40.408  113.237 1.00 85.70  ? 1212 LEU B CD2 1 
ATOM   23623 N  N   . LYS C 1 1213 ? -1.848   37.827  117.197 1.00 87.75  ? 1213 LYS B N   1 
ATOM   23624 C  CA  . LYS C 1 1213 ? -0.438   37.584  117.385 1.00 86.15  ? 1213 LYS B CA  1 
ATOM   23625 C  C   . LYS C 1 1213 ? -0.263   36.194  117.942 1.00 90.81  ? 1213 LYS B C   1 
ATOM   23626 O  O   . LYS C 1 1213 ? 0.806    35.583  117.852 1.00 90.02  ? 1213 LYS B O   1 
ATOM   23627 C  CB  . LYS C 1 1213 ? 0.144    38.642  118.301 1.00 79.89  ? 1213 LYS B CB  1 
ATOM   23628 C  CG  . LYS C 1 1213 ? 1.635    38.744  118.193 1.00 78.16  ? 1213 LYS B CG  1 
ATOM   23629 C  CD  . LYS C 1 1213 ? 2.044    40.171  118.446 1.00 78.69  ? 1213 LYS B CD  1 
ATOM   23630 C  CE  . LYS C 1 1213 ? 3.509    40.298  118.832 1.00 79.75  ? 1213 LYS B CE  1 
ATOM   23631 N  NZ  . LYS C 1 1213 ? 3.941    41.678  118.515 1.00 78.90  ? 1213 LYS B NZ  1 
ATOM   23632 N  N   . ARG C 1 1214 ? -1.348   35.703  118.512 1.00 96.55  ? 1214 ARG B N   1 
ATOM   23633 C  CA  . ARG C 1 1214 ? -1.364   34.388  119.079 1.00 107.04 ? 1214 ARG B CA  1 
ATOM   23634 C  C   . ARG C 1 1214 ? -1.572   33.414  117.930 1.00 109.68 ? 1214 ARG B C   1 
ATOM   23635 O  O   . ARG C 1 1214 ? -1.159   32.258  117.986 1.00 111.63 ? 1214 ARG B O   1 
ATOM   23636 C  CB  . ARG C 1 1214 ? -2.488   34.308  120.112 1.00 118.35 ? 1214 ARG B CB  1 
ATOM   23637 C  CG  . ARG C 1 1214 ? -2.993   32.906  120.433 1.00 131.96 ? 1214 ARG B CG  1 
ATOM   23638 C  CD  . ARG C 1 1214 ? -3.994   32.923  121.599 1.00 142.00 ? 1214 ARG B CD  1 
ATOM   23639 N  NE  . ARG C 1 1214 ? -4.952   34.026  121.486 1.00 147.47 ? 1214 ARG B NE  1 
ATOM   23640 C  CZ  . ARG C 1 1214 ? -5.656   34.520  122.503 1.00 151.74 ? 1214 ARG B CZ  1 
ATOM   23641 N  NH1 . ARG C 1 1214 ? -5.508   34.012  123.717 1.00 154.71 ? 1214 ARG B NH1 1 
ATOM   23642 N  NH2 . ARG C 1 1214 ? -6.502   35.528  122.317 1.00 151.79 ? 1214 ARG B NH2 1 
ATOM   23643 N  N   . GLU C 1 1215 ? -2.189   33.885  116.854 1.00 109.44 ? 1215 GLU B N   1 
ATOM   23644 C  CA  . GLU C 1 1215 ? -2.558   32.962  115.780 1.00 107.66 ? 1215 GLU B CA  1 
ATOM   23645 C  C   . GLU C 1 1215 ? -1.392   32.483  114.924 1.00 103.67 ? 1215 GLU B C   1 
ATOM   23646 O  O   . GLU C 1 1215 ? -1.470   31.408  114.329 1.00 105.78 ? 1215 GLU B O   1 
ATOM   23647 C  CB  . GLU C 1 1215 ? -3.699   33.533  114.943 1.00 105.77 ? 1215 GLU B CB  1 
ATOM   23648 C  CG  . GLU C 1 1215 ? -5.022   33.280  115.631 1.00 107.21 ? 1215 GLU B CG  1 
ATOM   23649 C  CD  . GLU C 1 1215 ? -5.299   31.794  115.758 1.00 111.51 ? 1215 GLU B CD  1 
ATOM   23650 O  OE1 . GLU C 1 1215 ? -4.744   31.026  114.942 1.00 113.37 ? 1215 GLU B OE1 1 
ATOM   23651 O  OE2 . GLU C 1 1215 ? -6.060   31.389  116.663 1.00 113.11 ? 1215 GLU B OE2 1 
ATOM   23652 N  N   . ALA C 1 1216 ? -0.310   33.265  114.920 1.00 96.10  ? 1216 ALA B N   1 
ATOM   23653 C  CA  . ALA C 1 1216 ? 0.804    33.116  113.987 1.00 90.43  ? 1216 ALA B CA  1 
ATOM   23654 C  C   . ALA C 1 1216 ? 1.571    31.803  114.087 1.00 91.10  ? 1216 ALA B C   1 
ATOM   23655 O  O   . ALA C 1 1216 ? 1.294    30.996  114.987 1.00 93.96  ? 1216 ALA B O   1 
ATOM   23656 C  CB  . ALA C 1 1216 ? 1.735    34.269  114.138 1.00 87.35  ? 1216 ALA B CB  1 
ATOM   23657 N  N   . LEU C 1 1217 ? 2.523    31.599  113.161 1.00 87.38  ? 1217 LEU B N   1 
ATOM   23658 C  CA  . LEU C 1 1217 ? 3.365    30.393  113.126 1.00 87.12  ? 1217 LEU B CA  1 
ATOM   23659 C  C   . LEU C 1 1217 ? 4.824    30.717  112.788 1.00 85.76  ? 1217 LEU B C   1 
ATOM   23660 O  O   . LEU C 1 1217 ? 5.137    31.801  112.278 1.00 80.53  ? 1217 LEU B O   1 
ATOM   23661 C  CB  . LEU C 1 1217 ? 2.823    29.382  112.129 1.00 87.29  ? 1217 LEU B CB  1 
ATOM   23662 C  CG  . LEU C 1 1217 ? 1.314    29.444  111.930 1.00 86.72  ? 1217 LEU B CG  1 
ATOM   23663 C  CD1 . LEU C 1 1217 ? 1.003    29.541  110.461 1.00 85.92  ? 1217 LEU B CD1 1 
ATOM   23664 C  CD2 . LEU C 1 1217 ? 0.561    28.270  112.611 1.00 88.84  ? 1217 LEU B CD2 1 
ATOM   23665 N  N   . VAL C 1 1218 ? 5.717    29.765  113.041 1.00 89.06  ? 1218 VAL B N   1 
ATOM   23666 C  CA  . VAL C 1 1218 ? 7.132    30.090  113.034 1.00 91.02  ? 1218 VAL B CA  1 
ATOM   23667 C  C   . VAL C 1 1218 ? 7.937    28.950  112.525 1.00 91.26  ? 1218 VAL B C   1 
ATOM   23668 O  O   . VAL C 1 1218 ? 7.595    27.817  112.743 1.00 89.98  ? 1218 VAL B O   1 
ATOM   23669 C  CB  . VAL C 1 1218 ? 7.567    30.256  114.424 1.00 97.06  ? 1218 VAL B CB  1 
ATOM   23670 C  CG1 . VAL C 1 1218 ? 7.616    31.724  114.816 1.00 95.41  ? 1218 VAL B CG1 1 
ATOM   23671 C  CG2 . VAL C 1 1218 ? 6.571    29.509  115.271 1.00 103.15 ? 1218 VAL B CG2 1 
ATOM   23672 N  N   . LYS C 1 1219 ? 9.016    29.253  111.837 1.00 97.22  ? 1219 LYS B N   1 
ATOM   23673 C  CA  . LYS C 1 1219 ? 9.832    28.210  111.264 1.00 109.07 ? 1219 LYS B CA  1 
ATOM   23674 C  C   . LYS C 1 1219 ? 11.196   28.288  111.927 1.00 117.12 ? 1219 LYS B C   1 
ATOM   23675 O  O   . LYS C 1 1219 ? 11.816   29.361  111.968 1.00 118.17 ? 1219 LYS B O   1 
ATOM   23676 C  CB  . LYS C 1 1219 ? 9.917    28.333  109.718 1.00 116.69 ? 1219 LYS B CB  1 
ATOM   23677 C  CG  . LYS C 1 1219 ? 9.096    27.286  108.861 1.00 178.00 ? 1219 LYS B CG  1 
ATOM   23678 C  CD  . LYS C 1 1219 ? 8.405    27.895  107.581 1.00 163.42 ? 1219 LYS B CD  1 
ATOM   23679 C  CE  . LYS C 1 1219 ? 8.925    27.409  106.198 1.00 147.35 ? 1219 LYS B CE  1 
ATOM   23680 N  NZ  . LYS C 1 1219 ? 8.286    28.177  105.040 1.00 145.05 ? 1219 LYS B NZ  1 
ATOM   23681 N  N   . GLY C 1 1220 ? 11.636   27.143  112.461 1.00 122.49 ? 1220 GLY B N   1 
ATOM   23682 C  CA  . GLY C 1 1220 ? 12.939   26.997  113.096 1.00 123.69 ? 1220 GLY B CA  1 
ATOM   23683 C  C   . GLY C 1 1220 ? 13.002   27.594  114.488 1.00 126.04 ? 1220 GLY B C   1 
ATOM   23684 O  O   . GLY C 1 1220 ? 12.279   28.543  114.790 1.00 124.22 ? 1220 GLY B O   1 
ATOM   23685 N  N   . ASN C 1 1221 ? 13.848   27.042  115.352 1.00 128.45 ? 1221 ASN B N   1 
ATOM   23686 C  CA  . ASN C 1 1221 ? 13.954   27.589  116.706 1.00 128.30 ? 1221 ASN B CA  1 
ATOM   23687 C  C   . ASN C 1 1221 ? 15.273   28.272  117.011 1.00 123.91 ? 1221 ASN B C   1 
ATOM   23688 O  O   . ASN C 1 1221 ? 16.322   27.631  116.976 1.00 125.62 ? 1221 ASN B O   1 
ATOM   23689 C  CB  . ASN C 1 1221 ? 13.704   26.536  117.777 1.00 132.77 ? 1221 ASN B CB  1 
ATOM   23690 C  CG  . ASN C 1 1221 ? 13.850   27.105  119.158 1.00 132.26 ? 1221 ASN B CG  1 
ATOM   23691 O  OD1 . ASN C 1 1221 ? 14.762   26.746  119.895 1.00 133.00 ? 1221 ASN B OD1 1 
ATOM   23692 N  ND2 . ASN C 1 1221 ? 12.980   28.052  119.497 1.00 130.70 ? 1221 ASN B ND2 1 
ATOM   23693 N  N   . PRO C 1 1222 ? 15.222   29.561  117.373 1.00 116.89 ? 1222 PRO B N   1 
ATOM   23694 C  CA  . PRO C 1 1222 ? 14.022   30.367  117.608 1.00 112.97 ? 1222 PRO B CA  1 
ATOM   23695 C  C   . PRO C 1 1222 ? 13.365   30.707  116.280 1.00 110.80 ? 1222 PRO B C   1 
ATOM   23696 O  O   . PRO C 1 1222 ? 13.809   30.185  115.262 1.00 114.08 ? 1222 PRO B O   1 
ATOM   23697 C  CB  . PRO C 1 1222 ? 14.586   31.644  118.226 1.00 110.75 ? 1222 PRO B CB  1 
ATOM   23698 C  CG  . PRO C 1 1222 ? 16.074   31.444  118.329 1.00 112.60 ? 1222 PRO B CG  1 
ATOM   23699 C  CD  . PRO C 1 1222 ? 16.442   30.377  117.398 1.00 115.14 ? 1222 PRO B CD  1 
ATOM   23700 N  N   . PRO C 1 1223 ? 12.339   31.585  116.275 1.00 105.86 ? 1223 PRO B N   1 
ATOM   23701 C  CA  . PRO C 1 1223 ? 11.812   32.047  114.998 1.00 98.04  ? 1223 PRO B CA  1 
ATOM   23702 C  C   . PRO C 1 1223 ? 12.940   32.485  114.122 1.00 91.76  ? 1223 PRO B C   1 
ATOM   23703 O  O   . PRO C 1 1223 ? 13.710   33.365  114.538 1.00 87.20  ? 1223 PRO B O   1 
ATOM   23704 C  CB  . PRO C 1 1223 ? 11.017   33.300  115.383 1.00 95.26  ? 1223 PRO B CB  1 
ATOM   23705 C  CG  . PRO C 1 1223 ? 10.494   32.994  116.660 1.00 98.58  ? 1223 PRO B CG  1 
ATOM   23706 C  CD  . PRO C 1 1223 ? 11.612   32.226  117.380 1.00 104.35 ? 1223 PRO B CD  1 
ATOM   23707 N  N   . ILE C 1 1224 ? 13.051   31.854  112.954 1.00 91.04  ? 1224 ILE B N   1 
ATOM   23708 C  CA  . ILE C 1 1224 ? 13.736   32.480  111.841 1.00 88.67  ? 1224 ILE B CA  1 
ATOM   23709 C  C   . ILE C 1 1224 ? 12.744   33.007  110.810 1.00 87.57  ? 1224 ILE B C   1 
ATOM   23710 O  O   . ILE C 1 1224 ? 13.038   34.030  110.136 1.00 86.78  ? 1224 ILE B O   1 
ATOM   23711 C  CB  . ILE C 1 1224 ? 14.754   31.589  111.203 1.00 87.56  ? 1224 ILE B CB  1 
ATOM   23712 C  CG1 . ILE C 1 1224 ? 15.698   31.136  112.310 1.00 91.82  ? 1224 ILE B CG1 1 
ATOM   23713 C  CG2 . ILE C 1 1224 ? 15.446   32.372  110.090 1.00 83.79  ? 1224 ILE B CG2 1 
ATOM   23714 C  CD1 . ILE C 1 1224 ? 17.097   30.779  111.877 1.00 95.34  ? 1224 ILE B CD1 1 
ATOM   23715 N  N   . TYR C 1 1225 ? 11.579   32.336  110.735 1.00 85.03  ? 1225 TYR B N   1 
ATOM   23716 C  CA  . TYR C 1 1225 ? 10.469   32.745  109.879 1.00 82.22  ? 1225 TYR B CA  1 
ATOM   23717 C  C   . TYR C 1 1225 ? 9.217    32.776  110.684 1.00 79.54  ? 1225 TYR B C   1 
ATOM   23718 O  O   . TYR C 1 1225 ? 8.972    31.871  111.448 1.00 81.40  ? 1225 TYR B O   1 
ATOM   23719 C  CB  . TYR C 1 1225 ? 10.215   31.728  108.765 1.00 85.14  ? 1225 TYR B CB  1 
ATOM   23720 C  CG  . TYR C 1 1225 ? 11.350   31.545  107.816 1.00 87.08  ? 1225 TYR B CG  1 
ATOM   23721 C  CD1 . TYR C 1 1225 ? 11.777   32.579  107.010 1.00 86.62  ? 1225 TYR B CD1 1 
ATOM   23722 C  CD2 . TYR C 1 1225 ? 12.011   30.344  107.738 1.00 90.71  ? 1225 TYR B CD2 1 
ATOM   23723 C  CE1 . TYR C 1 1225 ? 12.851   32.416  106.147 1.00 88.92  ? 1225 TYR B CE1 1 
ATOM   23724 C  CE2 . TYR C 1 1225 ? 13.077   30.166  106.878 1.00 93.16  ? 1225 TYR B CE2 1 
ATOM   23725 C  CZ  . TYR C 1 1225 ? 13.497   31.205  106.084 1.00 91.60  ? 1225 TYR B CZ  1 
ATOM   23726 O  OH  . TYR C 1 1225 ? 14.560   31.020  105.231 1.00 92.13  ? 1225 TYR B OH  1 
ATOM   23727 N  N   . ARG C 1 1226 ? 8.397    33.784  110.461 1.00 78.49  ? 1226 ARG B N   1 
ATOM   23728 C  CA  . ARG C 1 1226 ? 7.040    33.796  110.969 1.00 83.39  ? 1226 ARG B CA  1 
ATOM   23729 C  C   . ARG C 1 1226 ? 6.131    34.103  109.795 1.00 85.41  ? 1226 ARG B C   1 
ATOM   23730 O  O   . ARG C 1 1226 ? 6.592    34.731  108.837 1.00 86.50  ? 1226 ARG B O   1 
ATOM   23731 C  CB  . ARG C 1 1226 ? 6.891    34.917  111.997 1.00 86.60  ? 1226 ARG B CB  1 
ATOM   23732 C  CG  . ARG C 1 1226 ? 5.468    35.091  112.572 1.00 88.29  ? 1226 ARG B CG  1 
ATOM   23733 C  CD  . ARG C 1 1226 ? 5.365    36.225  113.605 1.00 85.84  ? 1226 ARG B CD  1 
ATOM   23734 N  NE  . ARG C 1 1226 ? 6.639    36.460  114.287 1.00 84.36  ? 1226 ARG B NE  1 
ATOM   23735 C  CZ  . ARG C 1 1226 ? 7.078    35.781  115.349 1.00 80.04  ? 1226 ARG B CZ  1 
ATOM   23736 N  NH1 . ARG C 1 1226 ? 6.338    34.787  115.908 1.00 77.70  ? 1226 ARG B NH1 1 
ATOM   23737 N  NH2 . ARG C 1 1226 ? 8.269    36.111  115.848 1.00 77.33  ? 1226 ARG B NH2 1 
ATOM   23738 N  N   . PHE C 1 1227 ? 4.860    33.682  109.863 1.00 85.22  ? 1227 PHE B N   1 
ATOM   23739 C  CA  . PHE C 1 1227 ? 3.804    34.085  108.909 1.00 82.42  ? 1227 PHE B CA  1 
ATOM   23740 C  C   . PHE C 1 1227 ? 2.522    33.558  109.478 1.00 81.95  ? 1227 PHE B C   1 
ATOM   23741 O  O   . PHE C 1 1227 ? 2.571    32.661  110.331 1.00 83.11  ? 1227 PHE B O   1 
ATOM   23742 C  CB  . PHE C 1 1227 ? 3.974    33.375  107.583 1.00 84.52  ? 1227 PHE B CB  1 
ATOM   23743 C  CG  . PHE C 1 1227 ? 4.246    31.903  107.733 1.00 88.08  ? 1227 PHE B CG  1 
ATOM   23744 C  CD1 . PHE C 1 1227 ? 3.218    30.984  107.693 1.00 88.75  ? 1227 PHE B CD1 1 
ATOM   23745 C  CD2 . PHE C 1 1227 ? 5.535    31.450  107.954 1.00 88.44  ? 1227 PHE B CD2 1 
ATOM   23746 C  CE1 . PHE C 1 1227 ? 3.471    29.644  107.849 1.00 89.14  ? 1227 PHE B CE1 1 
ATOM   23747 C  CE2 . PHE C 1 1227 ? 5.796    30.126  108.100 1.00 88.83  ? 1227 PHE B CE2 1 
ATOM   23748 C  CZ  . PHE C 1 1227 ? 4.759    29.216  108.050 1.00 89.74  ? 1227 PHE B CZ  1 
ATOM   23749 N  N   . TRP C 1 1228 ? 1.375    34.063  109.020 1.00 81.48  ? 1228 TRP B N   1 
ATOM   23750 C  CA  . TRP C 1 1228 ? 0.090    33.412  109.370 1.00 83.87  ? 1228 TRP B CA  1 
ATOM   23751 C  C   . TRP C 1 1228 ? -0.551   32.573  108.230 1.00 102.90 ? 1228 TRP B C   1 
ATOM   23752 O  O   . TRP C 1 1228 ? -0.274   32.765  107.049 1.00 102.58 ? 1228 TRP B O   1 
ATOM   23753 C  CB  . TRP C 1 1228 ? -0.929   34.408  109.940 1.00 81.61  ? 1228 TRP B CB  1 
ATOM   23754 C  CG  . TRP C 1 1228 ? -0.448   35.261  111.100 1.00 81.23  ? 1228 TRP B CG  1 
ATOM   23755 C  CD1 . TRP C 1 1228 ? -1.110   35.485  112.281 1.00 82.57  ? 1228 TRP B CD1 1 
ATOM   23756 C  CD2 . TRP C 1 1228 ? 0.770    36.022  111.179 1.00 78.59  ? 1228 TRP B CD2 1 
ATOM   23757 N  NE1 . TRP C 1 1228 ? -0.382   36.340  113.081 1.00 80.69  ? 1228 TRP B NE1 1 
ATOM   23758 C  CE2 . TRP C 1 1228 ? 0.771    36.683  112.425 1.00 79.08  ? 1228 TRP B CE2 1 
ATOM   23759 C  CE3 . TRP C 1 1228 ? 1.852    36.209  110.323 1.00 75.66  ? 1228 TRP B CE3 1 
ATOM   23760 C  CZ2 . TRP C 1 1228 ? 1.819    37.506  112.832 1.00 77.89  ? 1228 TRP B CZ2 1 
ATOM   23761 C  CZ3 . TRP C 1 1228 ? 2.885    37.021  110.734 1.00 75.14  ? 1228 TRP B CZ3 1 
ATOM   23762 C  CH2 . TRP C 1 1228 ? 2.865    37.660  111.974 1.00 75.84  ? 1228 TRP B CH2 1 
ATOM   23763 N  N   . LYS C 1 1229 ? -1.382   31.618  108.610 1.00 105.04 ? 1229 LYS B N   1 
ATOM   23764 C  CA  . LYS C 1 1229 ? -2.070   30.776  107.666 1.00 108.90 ? 1229 LYS B CA  1 
ATOM   23765 C  C   . LYS C 1 1229 ? -3.479   31.331  107.626 1.00 117.43 ? 1229 LYS B C   1 
ATOM   23766 O  O   . LYS C 1 1229 ? -3.896   31.971  108.574 1.00 117.00 ? 1229 LYS B O   1 
ATOM   23767 C  CB  . LYS C 1 1229 ? -2.102   29.374  108.229 1.00 109.81 ? 1229 LYS B CB  1 
ATOM   23768 C  CG  . LYS C 1 1229 ? -1.698   28.280  107.275 1.00 112.87 ? 1229 LYS B CG  1 
ATOM   23769 C  CD  . LYS C 1 1229 ? -1.485   26.916  107.999 1.00 149.19 ? 1229 LYS B CD  1 
ATOM   23770 C  CE  . LYS C 1 1229 ? -2.770   26.073  108.181 1.00 146.26 ? 1229 LYS B CE  1 
ATOM   23771 N  NZ  . LYS C 1 1229 ? -3.493   25.623  106.926 1.00 142.85 ? 1229 LYS B NZ  1 
ATOM   23772 N  N   . ASP C 1 1230 ? -4.220   31.090  106.549 1.00 126.29 ? 1230 ASP B N   1 
ATOM   23773 C  CA  . ASP C 1 1230 ? -5.549   31.685  106.356 1.00 134.58 ? 1230 ASP B CA  1 
ATOM   23774 C  C   . ASP C 1 1230 ? -6.620   31.227  107.347 1.00 141.11 ? 1230 ASP B C   1 
ATOM   23775 O  O   . ASP C 1 1230 ? -7.319   32.052  107.928 1.00 140.09 ? 1230 ASP B O   1 
ATOM   23776 C  CB  . ASP C 1 1230 ? -6.040   31.415  104.940 1.00 138.94 ? 1230 ASP B CB  1 
ATOM   23777 C  CG  . ASP C 1 1230 ? -7.493   31.787  104.763 1.00 143.20 ? 1230 ASP B CG  1 
ATOM   23778 O  OD1 . ASP C 1 1230 ? -7.971   32.604  105.575 1.00 144.04 ? 1230 ASP B OD1 1 
ATOM   23779 O  OD2 . ASP C 1 1230 ? -8.161   31.280  103.830 1.00 146.48 ? 1230 ASP B OD2 1 
ATOM   23780 N  N   . ASN C 1 1231 ? -6.774   29.910  107.476 1.00 152.25 ? 1231 ASN B N   1 
ATOM   23781 C  CA  . ASN C 1 1231 ? -7.563   29.266  108.527 1.00 161.83 ? 1231 ASN B CA  1 
ATOM   23782 C  C   . ASN C 1 1231 ? -7.468   30.004  109.860 1.00 167.01 ? 1231 ASN B C   1 
ATOM   23783 O  O   . ASN C 1 1231 ? -6.818   31.038  109.960 1.00 165.03 ? 1231 ASN B O   1 
ATOM   23784 C  CB  . ASN C 1 1231 ? -7.009   27.860  108.759 1.00 168.35 ? 1231 ASN B CB  1 
ATOM   23785 C  CG  . ASN C 1 1231 ? -5.783   27.856  109.701 1.00 172.29 ? 1231 ASN B CG  1 
ATOM   23786 O  OD1 . ASN C 1 1231 ? -4.635   27.891  109.256 1.00 173.21 ? 1231 ASN B OD1 1 
ATOM   23787 N  ND2 . ASN C 1 1231 ? -6.036   27.833  111.006 1.00 173.47 ? 1231 ASN B ND2 1 
ATOM   23788 N  N   . LEU C 1 1232 ? -8.073   29.438  110.899 1.00 174.27 ? 1232 LEU B N   1 
ATOM   23789 C  CA  . LEU C 1 1232 ? -7.962   29.985  112.247 1.00 175.33 ? 1232 LEU B CA  1 
ATOM   23790 C  C   . LEU C 1 1232 ? -7.938   28.855  113.267 1.00 187.33 ? 1232 LEU B C   1 
ATOM   23791 O  O   . LEU C 1 1232 ? -8.968   28.227  113.495 1.00 191.88 ? 1232 LEU B O   1 
ATOM   23792 C  CB  . LEU C 1 1232 ? -9.160   30.876  112.526 1.00 166.63 ? 1232 LEU B CB  1 
ATOM   23793 C  CG  . LEU C 1 1232 ? -9.435   31.164  113.989 1.00 156.14 ? 1232 LEU B CG  1 
ATOM   23794 C  CD1 . LEU C 1 1232 ? -8.837   32.495  114.339 1.00 150.27 ? 1232 LEU B CD1 1 
ATOM   23795 C  CD2 . LEU C 1 1232 ? -10.931  31.162  114.194 1.00 153.67 ? 1232 LEU B CD2 1 
ATOM   23796 N  N   . GLN C 1 1233 ? -6.772   28.592  113.865 1.00 191.28 ? 1233 GLN B N   1 
ATOM   23797 C  CA  . GLN C 1 1233 ? -6.590   27.524  114.868 1.00 200.01 ? 1233 GLN B CA  1 
ATOM   23798 C  C   . GLN C 1 1233 ? -7.246   26.146  114.575 1.00 213.63 ? 1233 GLN B C   1 
ATOM   23799 O  O   . GLN C 1 1233 ? -7.395   25.323  115.481 1.00 213.08 ? 1233 GLN B O   1 
ATOM   23800 C  CB  . GLN C 1 1233 ? -6.972   28.030  116.269 1.00 207.72 ? 1233 GLN B CB  1 
ATOM   23801 C  CG  . GLN C 1 1233 ? -8.407   28.528  116.372 1.00 217.03 ? 1233 GLN B CG  1 
ATOM   23802 C  CD  . GLN C 1 1233 ? -8.789   29.051  117.748 1.00 223.37 ? 1233 GLN B CD  1 
ATOM   23803 O  OE1 . GLN C 1 1233 ? -8.610   28.372  118.761 1.00 227.59 ? 1233 GLN B OE1 1 
ATOM   23804 N  NE2 . GLN C 1 1233 ? -9.345   30.258  117.784 1.00 223.46 ? 1233 GLN B NE2 1 
ATOM   23805 N  N   . HIS C 1 1234 ? -7.646   25.912  113.322 1.00 217.35 ? 1234 HIS B N   1 
ATOM   23806 C  CA  . HIS C 1 1234 ? -8.201   24.623  112.879 1.00 221.20 ? 1234 HIS B CA  1 
ATOM   23807 C  C   . HIS C 1 1234 ? -7.090   23.736  112.380 1.00 227.38 ? 1234 HIS B C   1 
ATOM   23808 O  O   . HIS C 1 1234 ? -7.317   22.629  111.898 1.00 228.69 ? 1234 HIS B O   1 
ATOM   23809 C  CB  . HIS C 1 1234 ? -9.236   24.820  111.779 1.00 218.08 ? 1234 HIS B CB  1 
ATOM   23810 C  CG  . HIS C 1 1234 ? -10.401  25.644  112.216 1.00 214.39 ? 1234 HIS B CG  1 
ATOM   23811 N  ND1 . HIS C 1 1234 ? -11.162  25.317  113.315 1.00 214.73 ? 1234 HIS B ND1 1 
ATOM   23812 C  CD2 . HIS C 1 1234 ? -10.918  26.794  111.726 1.00 211.15 ? 1234 HIS B CD2 1 
ATOM   23813 C  CE1 . HIS C 1 1234 ? -12.108  26.224  113.478 1.00 213.15 ? 1234 HIS B CE1 1 
ATOM   23814 N  NE2 . HIS C 1 1234 ? -11.982  27.132  112.528 1.00 211.10 ? 1234 HIS B NE2 1 
ATOM   23815 N  N   . LYS C 1 1235 ? -5.891   24.296  112.447 1.00 231.34 ? 1235 LYS B N   1 
ATOM   23816 C  CA  . LYS C 1 1235 ? -4.643   23.558  112.417 1.00 239.19 ? 1235 LYS B CA  1 
ATOM   23817 C  C   . LYS C 1 1235 ? -4.681   22.218  111.690 1.00 251.49 ? 1235 LYS B C   1 
ATOM   23818 O  O   . LYS C 1 1235 ? -4.232   21.209  112.235 1.00 255.32 ? 1235 LYS B O   1 
ATOM   23819 C  CB  . LYS C 1 1235 ? -4.151   23.352  113.852 1.00 236.78 ? 1235 LYS B CB  1 
ATOM   23820 C  CG  . LYS C 1 1235 ? -4.033   24.641  114.659 1.00 230.92 ? 1235 LYS B CG  1 
ATOM   23821 C  CD  . LYS C 1 1235 ? -2.801   25.432  114.263 1.00 225.78 ? 1235 LYS B CD  1 
ATOM   23822 C  CE  . LYS C 1 1235 ? -2.658   26.682  115.105 1.00 220.72 ? 1235 LYS B CE  1 
ATOM   23823 N  NZ  . LYS C 1 1235 ? -3.802   27.604  114.915 1.00 217.86 ? 1235 LYS B NZ  1 
ATOM   23824 N  N   . ASP C 1 1236 ? -5.209   22.189  110.470 1.00 259.47 ? 1236 ASP B N   1 
ATOM   23825 C  CA  . ASP C 1 1236 ? -5.001   21.005  109.654 1.00 270.36 ? 1236 ASP B CA  1 
ATOM   23826 C  C   . ASP C 1 1236 ? -3.503   20.967  109.361 1.00 274.82 ? 1236 ASP B C   1 
ATOM   23827 O  O   . ASP C 1 1236 ? -2.931   19.911  109.093 1.00 277.02 ? 1236 ASP B O   1 
ATOM   23828 C  CB  . ASP C 1 1236 ? -5.829   21.041  108.368 1.00 273.68 ? 1236 ASP B CB  1 
ATOM   23829 C  CG  . ASP C 1 1236 ? -5.958   19.667  107.719 1.00 280.39 ? 1236 ASP B CG  1 
ATOM   23830 O  OD1 . ASP C 1 1236 ? -5.022   18.852  107.856 1.00 282.73 ? 1236 ASP B OD1 1 
ATOM   23831 O  OD2 . ASP C 1 1236 ? -6.995   19.398  107.074 1.00 282.90 ? 1236 ASP B OD2 1 
ATOM   23832 N  N   . SER C 1 1237 ? -2.884   22.145  109.443 1.00 276.31 ? 1237 SER B N   1 
ATOM   23833 C  CA  . SER C 1 1237 ? -1.434   22.325  109.325 1.00 277.98 ? 1237 SER B CA  1 
ATOM   23834 C  C   . SER C 1 1237 ? -0.868   22.022  107.945 1.00 279.39 ? 1237 SER B C   1 
ATOM   23835 O  O   . SER C 1 1237 ? 0.351    21.953  107.771 1.00 282.85 ? 1237 SER B O   1 
ATOM   23836 C  CB  . SER C 1 1237 ? -0.672   21.532  110.388 1.00 279.84 ? 1237 SER B CB  1 
ATOM   23837 O  OG  . SER C 1 1237 ? 0.704    21.876  110.366 1.00 277.95 ? 1237 SER B OG  1 
ATOM   23838 N  N   . SER C 1 1238 ? -1.750   21.832  106.970 1.00 275.04 ? 1238 SER B N   1 
ATOM   23839 C  CA  . SER C 1 1238 ? -1.312   21.736  105.587 1.00 270.49 ? 1238 SER B CA  1 
ATOM   23840 C  C   . SER C 1 1238 ? -0.845   23.114  105.121 1.00 261.05 ? 1238 SER B C   1 
ATOM   23841 O  O   . SER C 1 1238 ? -1.617   23.886  104.547 1.00 253.61 ? 1238 SER B O   1 
ATOM   23842 C  CB  . SER C 1 1238 ? -2.425   21.191  104.680 1.00 278.94 ? 1238 SER B CB  1 
ATOM   23843 O  OG  . SER C 1 1238 ? -3.575   22.023  104.706 1.00 281.84 ? 1238 SER B OG  1 
ATOM   23844 N  N   . VAL C 1 1239 ? 0.418    23.425  105.401 1.00 244.45 ? 1239 VAL B N   1 
ATOM   23845 C  CA  . VAL C 1 1239 ? 1.077    24.596  104.840 1.00 237.08 ? 1239 VAL B CA  1 
ATOM   23846 C  C   . VAL C 1 1239 ? 1.959    24.087  103.710 1.00 234.60 ? 1239 VAL B C   1 
ATOM   23847 O  O   . VAL C 1 1239 ? 3.063    24.585  103.505 1.00 231.58 ? 1239 VAL B O   1 
ATOM   23848 C  CB  . VAL C 1 1239 ? 1.937    25.320  105.899 1.00 237.04 ? 1239 VAL B CB  1 
ATOM   23849 C  CG1 . VAL C 1 1239 ? 1.164    25.476  107.176 1.00 238.48 ? 1239 VAL B CG1 1 
ATOM   23850 C  CG2 . VAL C 1 1239 ? 3.202    24.544  106.188 1.00 241.51 ? 1239 VAL B CG2 1 
ATOM   23851 N  N   . PRO C 1 1240 ? 1.434    23.117  102.938 1.00 237.04 ? 1240 PRO B N   1 
ATOM   23852 C  CA  . PRO C 1 1240 ? 2.183    22.103  102.188 1.00 238.80 ? 1240 PRO B CA  1 
ATOM   23853 C  C   . PRO C 1 1240 ? 3.363    22.667  101.420 1.00 231.11 ? 1240 PRO B C   1 
ATOM   23854 O  O   . PRO C 1 1240 ? 3.333    22.706  100.191 1.00 234.36 ? 1240 PRO B O   1 
ATOM   23855 C  CB  . PRO C 1 1240 ? 1.135    21.552  101.202 1.00 243.83 ? 1240 PRO B CB  1 
ATOM   23856 C  CG  . PRO C 1 1240 ? 0.157    22.664  101.056 1.00 242.02 ? 1240 PRO B CG  1 
ATOM   23857 C  CD  . PRO C 1 1240 ? 0.047    23.197  102.445 1.00 239.54 ? 1240 PRO B CD  1 
ATOM   23858 N  N   . ASN C 1 1241 ? 4.393    23.098  102.136 1.00 218.73 ? 1241 ASN B N   1 
ATOM   23859 C  CA  . ASN C 1 1241 ? 5.578    23.622  101.483 1.00 207.25 ? 1241 ASN B CA  1 
ATOM   23860 C  C   . ASN C 1 1241 ? 5.184    24.637  100.416 1.00 183.85 ? 1241 ASN B C   1 
ATOM   23861 O  O   . ASN C 1 1241 ? 5.874    24.772  99.406  1.00 180.48 ? 1241 ASN B O   1 
ATOM   23862 C  CB  . ASN C 1 1241 ? 6.381    22.489  100.817 1.00 219.62 ? 1241 ASN B CB  1 
ATOM   23863 C  CG  . ASN C 1 1241 ? 6.948    21.474  101.820 1.00 229.39 ? 1241 ASN B CG  1 
ATOM   23864 O  OD1 . ASN C 1 1241 ? 7.235    21.807  102.975 1.00 230.59 ? 1241 ASN B OD1 1 
ATOM   23865 N  ND2 . ASN C 1 1241 ? 7.132    20.230  101.363 1.00 235.14 ? 1241 ASN B ND2 1 
ATOM   23866 N  N   . THR C 1 1242 ? 4.071    25.338  100.617 1.00 166.26 ? 1242 THR B N   1 
ATOM   23867 C  CA  . THR C 1 1242 ? 3.599    26.252  99.585  1.00 148.13 ? 1242 THR B CA  1 
ATOM   23868 C  C   . THR C 1 1242 ? 2.788    27.438  100.065 1.00 124.40 ? 1242 THR B C   1 
ATOM   23869 O  O   . THR C 1 1242 ? 1.804    27.301  100.797 1.00 118.89 ? 1242 THR B O   1 
ATOM   23870 C  CB  . THR C 1 1242 ? 2.753    25.529  98.561  1.00 153.14 ? 1242 THR B CB  1 
ATOM   23871 O  OG1 . THR C 1 1242 ? 1.713    24.823  99.246  1.00 156.32 ? 1242 THR B OG1 1 
ATOM   23872 C  CG2 . THR C 1 1242 ? 3.604    24.559  97.730  1.00 156.02 ? 1242 THR B CG2 1 
ATOM   23873 N  N   . GLY C 1 1243 ? 3.216    28.603  99.595  1.00 111.14 ? 1243 GLY B N   1 
ATOM   23874 C  CA  . GLY C 1 1243 ? 2.570    29.862  99.887  1.00 99.78  ? 1243 GLY B CA  1 
ATOM   23875 C  C   . GLY C 1 1243 ? 1.303    30.038  99.078  1.00 94.01  ? 1243 GLY B C   1 
ATOM   23876 O  O   . GLY C 1 1243 ? 0.876    29.118  98.380  1.00 94.95  ? 1243 GLY B O   1 
ATOM   23877 N  N   . THR C 1 1244 ? 0.714    31.226  99.150  1.00 85.91  ? 1244 THR B N   1 
ATOM   23878 C  CA  . THR C 1 1244 ? -0.646   31.376  98.717  1.00 84.73  ? 1244 THR B CA  1 
ATOM   23879 C  C   . THR C 1 1244 ? -1.044   32.814  98.724  1.00 90.37  ? 1244 THR B C   1 
ATOM   23880 O  O   . THR C 1 1244 ? -0.740   33.527  99.661  1.00 90.52  ? 1244 THR B O   1 
ATOM   23881 C  CB  . THR C 1 1244 ? -1.566   30.740  99.716  1.00 80.74  ? 1244 THR B CB  1 
ATOM   23882 O  OG1 . THR C 1 1244 ? -1.818   29.385  99.347  1.00 81.78  ? 1244 THR B OG1 1 
ATOM   23883 C  CG2 . THR C 1 1244 ? -2.871   31.499  99.761  1.00 78.92  ? 1244 THR B CG2 1 
ATOM   23884 N  N   . ALA C 1 1245 ? -1.769   33.224  97.691  1.00 96.55  ? 1245 ALA B N   1 
ATOM   23885 C  CA  . ALA C 1 1245 ? -2.349   34.567  97.618  1.00 97.36  ? 1245 ALA B CA  1 
ATOM   23886 C  C   . ALA C 1 1245 ? -2.904   35.069  98.954  1.00 97.45  ? 1245 ALA B C   1 
ATOM   23887 O  O   . ALA C 1 1245 ? -2.599   36.198  99.353  1.00 93.60  ? 1245 ALA B O   1 
ATOM   23888 C  CB  . ALA C 1 1245 ? -3.450   34.596  96.569  1.00 98.44  ? 1245 ALA B CB  1 
ATOM   23889 N  N   . ARG C 1 1246 ? -3.726   34.247  99.621  1.00 101.74 ? 1246 ARG B N   1 
ATOM   23890 C  CA  . ARG C 1 1246 ? -4.333   34.625  100.905 1.00 101.85 ? 1246 ARG B CA  1 
ATOM   23891 C  C   . ARG C 1 1246 ? -3.374   34.464  102.081 1.00 98.86  ? 1246 ARG B C   1 
ATOM   23892 O  O   . ARG C 1 1246 ? -3.371   35.267  103.018 1.00 96.13  ? 1246 ARG B O   1 
ATOM   23893 C  CB  . ARG C 1 1246 ? -5.631   33.869  101.172 1.00 103.92 ? 1246 ARG B CB  1 
ATOM   23894 C  CG  . ARG C 1 1246 ? -6.497   34.578  102.198 1.00 104.01 ? 1246 ARG B CG  1 
ATOM   23895 C  CD  . ARG C 1 1246 ? -7.813   33.892  102.371 1.00 109.68 ? 1246 ARG B CD  1 
ATOM   23896 N  NE  . ARG C 1 1246 ? -8.524   33.804  101.107 1.00 117.98 ? 1246 ARG B NE  1 
ATOM   23897 C  CZ  . ARG C 1 1246 ? -9.731   34.316  100.884 1.00 124.18 ? 1246 ARG B CZ  1 
ATOM   23898 N  NH1 . ARG C 1 1246 ? -10.370  34.940  101.862 1.00 125.62 ? 1246 ARG B NH1 1 
ATOM   23899 N  NH2 . ARG C 1 1246 ? -10.308  34.194  99.685  1.00 126.83 ? 1246 ARG B NH2 1 
ATOM   23900 N  N   . MET C 1 1247 ? -2.557   33.425  102.030 1.00 97.42  ? 1247 MET B N   1 
ATOM   23901 C  CA  . MET C 1 1247 ? -1.474   33.316  102.980 1.00 93.41  ? 1247 MET B CA  1 
ATOM   23902 C  C   . MET C 1 1247 ? -0.670   34.604  103.037 1.00 91.11  ? 1247 MET B C   1 
ATOM   23903 O  O   . MET C 1 1247 ? -0.666   35.300  104.052 1.00 89.17  ? 1247 MET B O   1 
ATOM   23904 C  CB  . MET C 1 1247 ? -0.552   32.207  102.569 1.00 92.81  ? 1247 MET B CB  1 
ATOM   23905 C  CG  . MET C 1 1247 ? 0.341    31.780  103.670 1.00 91.53  ? 1247 MET B CG  1 
ATOM   23906 S  SD  . MET C 1 1247 ? 0.485    30.020  103.452 1.00 106.62 ? 1247 MET B SD  1 
ATOM   23907 C  CE  . MET C 1 1247 ? -1.242   29.615  103.132 1.00 88.82  ? 1247 MET B CE  1 
ATOM   23908 N  N   . VAL C 1 1248 ? 0.015    34.916  101.936 1.00 90.85  ? 1248 VAL B N   1 
ATOM   23909 C  CA  . VAL C 1 1248 ? 0.789    36.165  101.837 1.00 87.95  ? 1248 VAL B CA  1 
ATOM   23910 C  C   . VAL C 1 1248 ? -0.085   37.365  102.154 1.00 81.57  ? 1248 VAL B C   1 
ATOM   23911 O  O   . VAL C 1 1248 ? 0.402    38.372  102.640 1.00 79.19  ? 1248 VAL B O   1 
ATOM   23912 C  CB  . VAL C 1 1248 ? 1.500    36.385  100.438 1.00 62.73  ? 1248 VAL B CB  1 
ATOM   23913 C  CG1 . VAL C 1 1248 ? 2.072    37.816  100.318 1.00 57.65  ? 1248 VAL B CG1 1 
ATOM   23914 C  CG2 . VAL C 1 1248 ? 2.595    35.317  100.175 1.00 64.96  ? 1248 VAL B CG2 1 
ATOM   23915 N  N   . GLU C 1 1249 ? -1.376   37.265  101.892 1.00 81.05  ? 1249 GLU B N   1 
ATOM   23916 C  CA  . GLU C 1 1249 ? -2.213   38.392  102.212 1.00 83.36  ? 1249 GLU B CA  1 
ATOM   23917 C  C   . GLU C 1 1249 ? -2.271   38.591  103.704 1.00 83.21  ? 1249 GLU B C   1 
ATOM   23918 O  O   . GLU C 1 1249 ? -1.930   39.650  104.211 1.00 83.08  ? 1249 GLU B O   1 
ATOM   23919 C  CB  . GLU C 1 1249 ? -3.621   38.238  101.676 1.00 88.19  ? 1249 GLU B CB  1 
ATOM   23920 C  CG  . GLU C 1 1249 ? -4.526   39.330  102.198 1.00 92.26  ? 1249 GLU B CG  1 
ATOM   23921 C  CD  . GLU C 1 1249 ? -5.321   39.948  101.100 1.00 98.38  ? 1249 GLU B CD  1 
ATOM   23922 O  OE1 . GLU C 1 1249 ? -5.144   39.472  99.962  1.00 103.45 ? 1249 GLU B OE1 1 
ATOM   23923 O  OE2 . GLU C 1 1249 ? -6.109   40.890  101.353 1.00 98.96  ? 1249 GLU B OE2 1 
ATOM   23924 N  N   . THR C 1 1250 ? -2.718   37.565  104.416 1.00 83.65  ? 1250 THR B N   1 
ATOM   23925 C  CA  . THR C 1 1250 ? -2.964   37.718  105.856 1.00 80.81  ? 1250 THR B CA  1 
ATOM   23926 C  C   . THR C 1 1250 ? -1.680   38.127  106.589 1.00 72.81  ? 1250 THR B C   1 
ATOM   23927 O  O   . THR C 1 1250 ? -1.670   39.072  107.384 1.00 67.46  ? 1250 THR B O   1 
ATOM   23928 C  CB  . THR C 1 1250 ? -3.581   36.448  106.506 1.00 85.09  ? 1250 THR B CB  1 
ATOM   23929 O  OG1 . THR C 1 1250 ? -2.570   35.444  106.641 1.00 88.03  ? 1250 THR B OG1 1 
ATOM   23930 C  CG2 . THR C 1 1250 ? -4.741   35.908  105.673 1.00 83.76  ? 1250 THR B CG2 1 
ATOM   23931 N  N   . THR C 1 1251 ? -0.597   37.423  106.304 1.00 71.01  ? 1251 THR B N   1 
ATOM   23932 C  CA  . THR C 1 1251 ? 0.647    37.736  106.961 1.00 71.80  ? 1251 THR B CA  1 
ATOM   23933 C  C   . THR C 1 1251 ? 1.085    39.181  106.646 1.00 71.00  ? 1251 THR B C   1 
ATOM   23934 O  O   . THR C 1 1251 ? 1.669    39.866  107.478 1.00 71.53  ? 1251 THR B O   1 
ATOM   23935 C  CB  . THR C 1 1251 ? 1.738    36.662  106.691 1.00 73.09  ? 1251 THR B CB  1 
ATOM   23936 O  OG1 . THR C 1 1251 ? 2.542    37.041  105.577 1.00 74.99  ? 1251 THR B OG1 1 
ATOM   23937 C  CG2 . THR C 1 1251 ? 1.115    35.321  106.408 1.00 72.71  ? 1251 THR B CG2 1 
ATOM   23938 N  N   . ALA C 1 1252 ? 0.765    39.679  105.468 1.00 71.01  ? 1252 ALA B N   1 
ATOM   23939 C  CA  . ALA C 1 1252 ? 1.012    41.092  105.235 1.00 71.61  ? 1252 ALA B CA  1 
ATOM   23940 C  C   . ALA C 1 1252 ? 0.121    41.934  106.157 1.00 72.44  ? 1252 ALA B C   1 
ATOM   23941 O  O   . ALA C 1 1252 ? 0.554    42.950  106.675 1.00 69.88  ? 1252 ALA B O   1 
ATOM   23942 C  CB  . ALA C 1 1252 ? 0.806    41.460  103.777 1.00 73.07  ? 1252 ALA B CB  1 
ATOM   23943 N  N   . TYR C 1 1253 ? -1.117   41.517  106.383 1.00 75.96  ? 1253 TYR B N   1 
ATOM   23944 C  CA  . TYR C 1 1253 ? -1.956   42.242  107.338 1.00 78.61  ? 1253 TYR B CA  1 
ATOM   23945 C  C   . TYR C 1 1253 ? -1.426   42.251  108.768 1.00 78.54  ? 1253 TYR B C   1 
ATOM   23946 O  O   . TYR C 1 1253 ? -1.508   43.281  109.436 1.00 80.43  ? 1253 TYR B O   1 
ATOM   23947 C  CB  . TYR C 1 1253 ? -3.367   41.698  107.349 1.00 82.03  ? 1253 TYR B CB  1 
ATOM   23948 C  CG  . TYR C 1 1253 ? -4.128   42.210  106.186 1.00 84.20  ? 1253 TYR B CG  1 
ATOM   23949 C  CD1 . TYR C 1 1253 ? -4.346   43.569  106.033 1.00 83.81  ? 1253 TYR B CD1 1 
ATOM   23950 C  CD2 . TYR C 1 1253 ? -4.594   41.348  105.215 1.00 85.19  ? 1253 TYR B CD2 1 
ATOM   23951 C  CE1 . TYR C 1 1253 ? -5.036   44.038  104.962 1.00 83.23  ? 1253 TYR B CE1 1 
ATOM   23952 C  CE2 . TYR C 1 1253 ? -5.278   41.817  104.141 1.00 84.98  ? 1253 TYR B CE2 1 
ATOM   23953 C  CZ  . TYR C 1 1253 ? -5.496   43.155  104.015 1.00 84.18  ? 1253 TYR B CZ  1 
ATOM   23954 O  OH  . TYR C 1 1253 ? -6.166   43.595  102.904 1.00 86.53  ? 1253 TYR B OH  1 
ATOM   23955 N  N   . ALA C 1 1254 ? -0.923   41.108  109.245 1.00 74.37  ? 1254 ALA B N   1 
ATOM   23956 C  CA  . ALA C 1 1254 ? -0.170   41.073  110.500 1.00 68.16  ? 1254 ALA B CA  1 
ATOM   23957 C  C   . ALA C 1 1254 ? 1.048    41.989  110.409 1.00 65.67  ? 1254 ALA B C   1 
ATOM   23958 O  O   . ALA C 1 1254 ? 1.115    43.011  111.103 1.00 61.39  ? 1254 ALA B O   1 
ATOM   23959 C  CB  . ALA C 1 1254 ? 0.241    39.647  110.868 1.00 65.37  ? 1254 ALA B CB  1 
ATOM   23960 N  N   . LEU C 1 1255 ? 1.983    41.642  109.527 1.00 68.57  ? 1255 LEU B N   1 
ATOM   23961 C  CA  . LEU C 1 1255 ? 3.173    42.483  109.306 1.00 72.98  ? 1255 LEU B CA  1 
ATOM   23962 C  C   . LEU C 1 1255 ? 2.879    43.979  109.221 1.00 70.41  ? 1255 LEU B C   1 
ATOM   23963 O  O   . LEU C 1 1255 ? 3.705    44.806  109.623 1.00 66.49  ? 1255 LEU B O   1 
ATOM   23964 C  CB  . LEU C 1 1255 ? 3.940    42.090  108.034 1.00 77.04  ? 1255 LEU B CB  1 
ATOM   23965 C  CG  . LEU C 1 1255 ? 5.032    43.118  107.669 1.00 76.67  ? 1255 LEU B CG  1 
ATOM   23966 C  CD1 . LEU C 1 1255 ? 6.091    43.223  108.767 1.00 76.07  ? 1255 LEU B CD1 1 
ATOM   23967 C  CD2 . LEU C 1 1255 ? 5.691    42.877  106.301 1.00 76.30  ? 1255 LEU B CD2 1 
ATOM   23968 N  N   . LEU C 1 1256 ? 1.726    44.322  108.659 1.00 72.94  ? 1256 LEU B N   1 
ATOM   23969 C  CA  . LEU C 1 1256 ? 1.406    45.720  108.450 1.00 77.87  ? 1256 LEU B CA  1 
ATOM   23970 C  C   . LEU C 1 1256 ? 0.898    46.330  109.740 1.00 80.56  ? 1256 LEU B C   1 
ATOM   23971 O  O   . LEU C 1 1256 ? 1.247    47.483  110.043 1.00 82.22  ? 1256 LEU B O   1 
ATOM   23972 C  CB  . LEU C 1 1256 ? 0.400    45.917  107.313 1.00 79.97  ? 1256 LEU B CB  1 
ATOM   23973 C  CG  . LEU C 1 1256 ? 0.880    46.152  105.877 1.00 80.45  ? 1256 LEU B CG  1 
ATOM   23974 C  CD1 . LEU C 1 1256 ? -0.315   46.578  105.077 1.00 83.22  ? 1256 LEU B CD1 1 
ATOM   23975 C  CD2 . LEU C 1 1256 ? 1.989    47.184  105.721 1.00 77.38  ? 1256 LEU B CD2 1 
ATOM   23976 N  N   . THR C 1 1257 ? 0.081    45.561  110.482 1.00 80.39  ? 1257 THR B N   1 
ATOM   23977 C  CA  . THR C 1 1257 ? -0.401   45.945  111.823 1.00 76.11  ? 1257 THR B CA  1 
ATOM   23978 C  C   . THR C 1 1257 ? 0.806    46.175  112.715 1.00 74.06  ? 1257 THR B C   1 
ATOM   23979 O  O   . THR C 1 1257 ? 1.076    47.306  113.159 1.00 71.32  ? 1257 THR B O   1 
ATOM   23980 C  CB  . THR C 1 1257 ? -1.278   44.853  112.468 1.00 70.62  ? 1257 THR B CB  1 
ATOM   23981 O  OG1 . THR C 1 1257 ? -2.312   44.499  111.551 1.00 71.01  ? 1257 THR B OG1 1 
ATOM   23982 C  CG2 . THR C 1 1257 ? -1.935   45.378  113.730 1.00 67.59  ? 1257 THR B CG2 1 
ATOM   23983 N  N   . SER C 1 1258 ? 1.559    45.103  112.931 1.00 73.64  ? 1258 SER B N   1 
ATOM   23984 C  CA  . SER C 1 1258 ? 2.839    45.216  113.615 1.00 76.85  ? 1258 SER B CA  1 
ATOM   23985 C  C   . SER C 1 1258 ? 3.734    46.400  113.162 1.00 76.95  ? 1258 SER B C   1 
ATOM   23986 O  O   . SER C 1 1258 ? 4.126    47.221  113.995 1.00 74.21  ? 1258 SER B O   1 
ATOM   23987 C  CB  . SER C 1 1258 ? 3.585    43.890  113.517 1.00 78.55  ? 1258 SER B CB  1 
ATOM   23988 O  OG  . SER C 1 1258 ? 2.849    42.886  114.185 1.00 79.18  ? 1258 SER B OG  1 
ATOM   23989 N  N   . LEU C 1 1259 ? 4.057    46.482  111.867 1.00 77.88  ? 1259 LEU B N   1 
ATOM   23990 C  CA  . LEU C 1 1259 ? 4.904    47.571  111.378 1.00 75.50  ? 1259 LEU B CA  1 
ATOM   23991 C  C   . LEU C 1 1259 ? 4.389    48.933  111.859 1.00 75.52  ? 1259 LEU B C   1 
ATOM   23992 O  O   . LEU C 1 1259 ? 5.174    49.902  112.029 1.00 74.36  ? 1259 LEU B O   1 
ATOM   23993 C  CB  . LEU C 1 1259 ? 5.071    47.518  109.856 1.00 70.62  ? 1259 LEU B CB  1 
ATOM   23994 C  CG  . LEU C 1 1259 ? 6.300    46.702  109.451 1.00 66.85  ? 1259 LEU B CG  1 
ATOM   23995 C  CD1 . LEU C 1 1259 ? 6.384    46.575  107.961 1.00 68.17  ? 1259 LEU B CD1 1 
ATOM   23996 C  CD2 . LEU C 1 1259 ? 7.580    47.325  109.999 1.00 63.35  ? 1259 LEU B CD2 1 
ATOM   23997 N  N   . ASN C 1 1260 ? 3.079    48.992  112.100 1.00 75.67  ? 1260 ASN B N   1 
ATOM   23998 C  CA  . ASN C 1 1260 ? 2.468    50.200  112.621 1.00 77.44  ? 1260 ASN B CA  1 
ATOM   23999 C  C   . ASN C 1 1260 ? 2.875    50.465  114.068 1.00 80.23  ? 1260 ASN B C   1 
ATOM   24000 O  O   . ASN C 1 1260 ? 3.313    51.576  114.419 1.00 83.89  ? 1260 ASN B O   1 
ATOM   24001 C  CB  . ASN C 1 1260 ? 0.950    50.168  112.447 1.00 75.43  ? 1260 ASN B CB  1 
ATOM   24002 C  CG  . ASN C 1 1260 ? 0.490    51.082  111.332 1.00 76.66  ? 1260 ASN B CG  1 
ATOM   24003 O  OD1 . ASN C 1 1260 ? 0.986    52.197  111.205 1.00 79.81  ? 1260 ASN B OD1 1 
ATOM   24004 N  ND2 . ASN C 1 1260 ? -0.427   50.618  110.509 1.00 75.29  ? 1260 ASN B ND2 1 
ATOM   24005 N  N   . LEU C 1 1261 ? 2.767    49.425  114.888 1.00 77.27  ? 1261 LEU B N   1 
ATOM   24006 C  CA  . LEU C 1 1261 ? 3.113    49.493  116.305 1.00 73.11  ? 1261 LEU B CA  1 
ATOM   24007 C  C   . LEU C 1 1261 ? 4.635    49.364  116.540 1.00 72.66  ? 1261 LEU B C   1 
ATOM   24008 O  O   . LEU C 1 1261 ? 5.072    48.817  117.535 1.00 71.56  ? 1261 LEU B O   1 
ATOM   24009 C  CB  . LEU C 1 1261 ? 2.334    48.410  117.057 1.00 69.93  ? 1261 LEU B CB  1 
ATOM   24010 C  CG  . LEU C 1 1261 ? 0.841    48.228  116.712 1.00 67.21  ? 1261 LEU B CG  1 
ATOM   24011 C  CD1 . LEU C 1 1261 ? 0.211    47.038  117.463 1.00 66.37  ? 1261 LEU B CD1 1 
ATOM   24012 C  CD2 . LEU C 1 1261 ? 0.026    49.527  116.918 1.00 64.16  ? 1261 LEU B CD2 1 
ATOM   24013 N  N   . LYS C 1 1262 ? 5.422    49.881  115.601 1.00 72.89  ? 1262 LYS B N   1 
ATOM   24014 C  CA  . LYS C 1 1262 ? 6.883    49.759  115.594 1.00 71.32  ? 1262 LYS B CA  1 
ATOM   24015 C  C   . LYS C 1 1262 ? 7.385    48.510  116.278 1.00 66.85  ? 1262 LYS B C   1 
ATOM   24016 O  O   . LYS C 1 1262 ? 8.429    48.519  116.892 1.00 65.22  ? 1262 LYS B O   1 
ATOM   24017 C  CB  . LYS C 1 1262 ? 7.512    51.026  116.136 1.00 75.71  ? 1262 LYS B CB  1 
ATOM   24018 C  CG  . LYS C 1 1262 ? 6.633    52.227  115.745 1.00 84.59  ? 1262 LYS B CG  1 
ATOM   24019 C  CD  . LYS C 1 1262 ? 7.398    53.427  115.171 1.00 93.27  ? 1262 LYS B CD  1 
ATOM   24020 C  CE  . LYS C 1 1262 ? 6.588    54.088  114.054 1.00 97.13  ? 1262 LYS B CE  1 
ATOM   24021 N  NZ  . LYS C 1 1262 ? 5.961    53.044  113.151 1.00 97.73  ? 1262 LYS B NZ  1 
ATOM   24022 N  N   . ASP C 1 1263 ? 6.629    47.430  116.095 1.00 65.45  ? 1263 ASP B N   1 
ATOM   24023 C  CA  . ASP C 1 1263 ? 6.844    46.143  116.732 1.00 65.69  ? 1263 ASP B CA  1 
ATOM   24024 C  C   . ASP C 1 1263 ? 8.129    45.483  116.283 1.00 66.82  ? 1263 ASP B C   1 
ATOM   24025 O  O   . ASP C 1 1263 ? 8.278    44.271  116.392 1.00 68.92  ? 1263 ASP B O   1 
ATOM   24026 C  CB  . ASP C 1 1263 ? 5.675    45.218  116.387 1.00 68.08  ? 1263 ASP B CB  1 
ATOM   24027 C  CG  . ASP C 1 1263 ? 5.299    44.253  117.544 1.00 97.13  ? 1263 ASP B CG  1 
ATOM   24028 O  OD1 . ASP C 1 1263 ? 6.227    43.888  118.346 1.00 96.43  ? 1263 ASP B OD1 1 
ATOM   24029 O  OD2 . ASP C 1 1263 ? 4.073    43.875  117.619 1.00 95.42  ? 1263 ASP B OD2 1 
ATOM   24030 N  N   . ILE C 1 1264 ? 9.071    46.303  115.849 1.00 63.40  ? 1264 ILE B N   1 
ATOM   24031 C  CA  . ILE C 1 1264 ? 10.287   45.893  115.141 1.00 62.79  ? 1264 ILE B CA  1 
ATOM   24032 C  C   . ILE C 1 1264 ? 10.893   44.498  115.216 1.00 68.13  ? 1264 ILE B C   1 
ATOM   24033 O  O   . ILE C 1 1264 ? 11.126   43.874  114.191 1.00 70.73  ? 1264 ILE B O   1 
ATOM   24034 C  CB  . ILE C 1 1264 ? 11.357   46.857  115.425 1.00 59.54  ? 1264 ILE B CB  1 
ATOM   24035 C  CG1 . ILE C 1 1264 ? 10.781   48.227  115.091 1.00 56.52  ? 1264 ILE B CG1 1 
ATOM   24036 C  CG2 . ILE C 1 1264 ? 12.601   46.464  114.647 1.00 46.45  ? 1264 ILE B CG2 1 
ATOM   24037 C  CD1 . ILE C 1 1264 ? 11.720   49.300  115.216 1.00 58.46  ? 1264 ILE B CD1 1 
ATOM   24038 N  N   . ASN C 1 1265 ? 11.201   44.008  116.396 1.00 72.27  ? 1265 ASN B N   1 
ATOM   24039 C  CA  . ASN C 1 1265 ? 11.767   42.672  116.445 1.00 77.20  ? 1265 ASN B CA  1 
ATOM   24040 C  C   . ASN C 1 1265 ? 10.817   41.597  115.957 1.00 78.27  ? 1265 ASN B C   1 
ATOM   24041 O  O   . ASN C 1 1265 ? 11.230   40.708  115.223 1.00 79.54  ? 1265 ASN B O   1 
ATOM   24042 C  CB  . ASN C 1 1265 ? 12.313   42.333  117.834 1.00 82.81  ? 1265 ASN B CB  1 
ATOM   24043 C  CG  . ASN C 1 1265 ? 13.767   42.692  117.969 1.00 87.25  ? 1265 ASN B CG  1 
ATOM   24044 O  OD1 . ASN C 1 1265 ? 14.622   42.058  117.356 1.00 91.23  ? 1265 ASN B OD1 1 
ATOM   24045 N  ND2 . ASN C 1 1265 ? 14.062   43.725  118.755 1.00 86.76  ? 1265 ASN B ND2 1 
ATOM   24046 N  N   . TYR C 1 1266 ? 9.550    41.689  116.362 1.00 78.29  ? 1266 TYR B N   1 
ATOM   24047 C  CA  . TYR C 1 1266 ? 8.544    40.655  116.059 1.00 78.78  ? 1266 TYR B CA  1 
ATOM   24048 C  C   . TYR C 1 1266 ? 8.608    40.333  114.608 1.00 82.21  ? 1266 TYR B C   1 
ATOM   24049 O  O   . TYR C 1 1266 ? 8.560    39.163  114.204 1.00 85.88  ? 1266 TYR B O   1 
ATOM   24050 C  CB  . TYR C 1 1266 ? 7.127    41.186  116.308 1.00 74.07  ? 1266 TYR B CB  1 
ATOM   24051 C  CG  . TYR C 1 1266 ? 6.042    40.139  116.226 1.00 70.58  ? 1266 TYR B CG  1 
ATOM   24052 C  CD1 . TYR C 1 1266 ? 6.234    38.902  116.787 1.00 70.82  ? 1266 TYR B CD1 1 
ATOM   24053 C  CD2 . TYR C 1 1266 ? 4.814    40.401  115.604 1.00 68.20  ? 1266 TYR B CD2 1 
ATOM   24054 C  CE1 . TYR C 1 1266 ? 5.249    37.949  116.734 1.00 73.03  ? 1266 TYR B CE1 1 
ATOM   24055 C  CE2 . TYR C 1 1266 ? 3.812    39.431  115.539 1.00 67.84  ? 1266 TYR B CE2 1 
ATOM   24056 C  CZ  . TYR C 1 1266 ? 4.044    38.208  116.114 1.00 71.15  ? 1266 TYR B CZ  1 
ATOM   24057 O  OH  . TYR C 1 1266 ? 3.100    37.211  116.104 1.00 72.63  ? 1266 TYR B OH  1 
ATOM   24058 N  N   . VAL C 1 1267 ? 8.746    41.430  113.863 1.00 78.70  ? 1267 VAL B N   1 
ATOM   24059 C  CA  . VAL C 1 1267 ? 8.444    41.564  112.461 1.00 72.80  ? 1267 VAL B CA  1 
ATOM   24060 C  C   . VAL C 1 1267 ? 9.556    41.017  111.612 1.00 71.78  ? 1267 VAL B C   1 
ATOM   24061 O  O   . VAL C 1 1267 ? 9.289    40.441  110.586 1.00 72.42  ? 1267 VAL B O   1 
ATOM   24062 C  CB  . VAL C 1 1267 ? 8.162    43.043  112.167 1.00 68.97  ? 1267 VAL B CB  1 
ATOM   24063 C  CG1 . VAL C 1 1267 ? 8.999    43.561  111.022 1.00 68.40  ? 1267 VAL B CG1 1 
ATOM   24064 C  CG2 . VAL C 1 1267 ? 6.659    43.270  111.975 1.00 68.40  ? 1267 VAL B CG2 1 
ATOM   24065 N  N   . ASN C 1 1268 ? 10.794   41.134  112.058 1.00 74.75  ? 1268 ASN B N   1 
ATOM   24066 C  CA  . ASN C 1 1268 ? 11.898   40.614  111.266 1.00 82.52  ? 1268 ASN B CA  1 
ATOM   24067 C  C   . ASN C 1 1268 ? 11.616   39.299  110.527 1.00 87.59  ? 1268 ASN B C   1 
ATOM   24068 O  O   . ASN C 1 1268 ? 11.564   39.312  109.312 1.00 91.05  ? 1268 ASN B O   1 
ATOM   24069 C  CB  . ASN C 1 1268 ? 13.179   40.530  112.083 1.00 90.95  ? 1268 ASN B CB  1 
ATOM   24070 C  CG  . ASN C 1 1268 ? 13.650   41.899  112.580 1.00 95.88  ? 1268 ASN B CG  1 
ATOM   24071 O  OD1 . ASN C 1 1268 ? 13.531   42.914  111.879 1.00 96.85  ? 1268 ASN B OD1 1 
ATOM   24072 N  ND2 . ASN C 1 1268 ? 14.205   41.927  113.795 1.00 99.02  ? 1268 ASN B ND2 1 
ATOM   24073 N  N   . PRO C 1 1269 ? 11.396   38.176  111.240 1.00 87.58  ? 1269 PRO B N   1 
ATOM   24074 C  CA  . PRO C 1 1269 ? 11.206   36.850  110.617 1.00 88.22  ? 1269 PRO B CA  1 
ATOM   24075 C  C   . PRO C 1 1269 ? 9.978    36.826  109.726 1.00 82.45  ? 1269 PRO B C   1 
ATOM   24076 O  O   . PRO C 1 1269 ? 9.848    36.001  108.821 1.00 83.08  ? 1269 PRO B O   1 
ATOM   24077 C  CB  . PRO C 1 1269 ? 10.926   35.919  111.800 1.00 90.82  ? 1269 PRO B CB  1 
ATOM   24078 C  CG  . PRO C 1 1269 ? 11.121   36.727  113.025 1.00 93.17  ? 1269 PRO B CG  1 
ATOM   24079 C  CD  . PRO C 1 1269 ? 10.965   38.167  112.639 1.00 91.30  ? 1269 PRO B CD  1 
ATOM   24080 N  N   . VAL C 1 1270 ? 9.054    37.722  110.014 1.00 77.39  ? 1270 VAL B N   1 
ATOM   24081 C  CA  . VAL C 1 1270 ? 7.987    37.979  109.086 1.00 71.89  ? 1270 VAL B CA  1 
ATOM   24082 C  C   . VAL C 1 1270 ? 8.546    38.451  107.743 1.00 68.22  ? 1270 VAL B C   1 
ATOM   24083 O  O   . VAL C 1 1270 ? 8.373    37.784  106.733 1.00 68.50  ? 1270 VAL B O   1 
ATOM   24084 C  CB  . VAL C 1 1270 ? 7.018    38.975  109.694 1.00 70.79  ? 1270 VAL B CB  1 
ATOM   24085 C  CG1 . VAL C 1 1270 ? 6.413    39.878  108.633 1.00 67.79  ? 1270 VAL B CG1 1 
ATOM   24086 C  CG2 . VAL C 1 1270 ? 5.976    38.227  110.488 1.00 71.46  ? 1270 VAL B CG2 1 
ATOM   24087 N  N   . ILE C 1 1271 ? 9.240    39.579  107.704 1.00 63.80  ? 1271 ILE B N   1 
ATOM   24088 C  CA  . ILE C 1 1271 ? 9.764    39.975  106.410 1.00 62.62  ? 1271 ILE B CA  1 
ATOM   24089 C  C   . ILE C 1 1271 ? 10.821   39.002  105.897 1.00 62.79  ? 1271 ILE B C   1 
ATOM   24090 O  O   . ILE C 1 1271 ? 10.994   38.882  104.711 1.00 65.73  ? 1271 ILE B O   1 
ATOM   24091 C  CB  . ILE C 1 1271 ? 10.173   41.505  106.242 1.00 62.55  ? 1271 ILE B CB  1 
ATOM   24092 C  CG1 . ILE C 1 1271 ? 11.622   41.741  106.590 1.00 61.77  ? 1271 ILE B CG1 1 
ATOM   24093 C  CG2 . ILE C 1 1271 ? 9.243    42.443  106.977 1.00 63.06  ? 1271 ILE B CG2 1 
ATOM   24094 C  CD1 . ILE C 1 1271 ? 12.539   41.399  105.445 1.00 63.04  ? 1271 ILE B CD1 1 
ATOM   24095 N  N   . LYS C 1 1272 ? 11.530   38.275  106.736 1.00 63.19  ? 1272 LYS B N   1 
ATOM   24096 C  CA  . LYS C 1 1272 ? 12.470   37.328  106.128 1.00 70.45  ? 1272 LYS B CA  1 
ATOM   24097 C  C   . LYS C 1 1272 ? 11.682   36.413  105.159 1.00 74.50  ? 1272 LYS B C   1 
ATOM   24098 O  O   . LYS C 1 1272 ? 12.186   36.023  104.101 1.00 77.09  ? 1272 LYS B O   1 
ATOM   24099 C  CB  . LYS C 1 1272 ? 13.259   36.532  107.187 1.00 73.61  ? 1272 LYS B CB  1 
ATOM   24100 C  CG  . LYS C 1 1272 ? 13.992   35.277  106.720 1.00 74.80  ? 1272 LYS B CG  1 
ATOM   24101 C  CD  . LYS C 1 1272 ? 15.444   35.478  106.409 1.00 74.34  ? 1272 LYS B CD  1 
ATOM   24102 C  CE  . LYS C 1 1272 ? 16.091   34.109  106.360 1.00 78.52  ? 1272 LYS B CE  1 
ATOM   24103 N  NZ  . LYS C 1 1272 ? 17.443   34.122  105.735 1.00 82.56  ? 1272 LYS B NZ  1 
ATOM   24104 N  N   . TRP C 1 1273 ? 10.428   36.122  105.515 1.00 73.85  ? 1273 TRP B N   1 
ATOM   24105 C  CA  . TRP C 1 1273 ? 9.573    35.186  104.769 1.00 71.36  ? 1273 TRP B CA  1 
ATOM   24106 C  C   . TRP C 1 1273 ? 8.827    35.853  103.602 1.00 66.90  ? 1273 TRP B C   1 
ATOM   24107 O  O   . TRP C 1 1273 ? 8.672    35.226  102.564 1.00 69.15  ? 1273 TRP B O   1 
ATOM   24108 C  CB  . TRP C 1 1273 ? 8.643    34.449  105.751 1.00 70.81  ? 1273 TRP B CB  1 
ATOM   24109 C  CG  . TRP C 1 1273 ? 7.497    33.617  105.215 1.00 71.66  ? 1273 TRP B CG  1 
ATOM   24110 C  CD1 . TRP C 1 1273 ? 7.401    32.237  105.186 1.00 74.84  ? 1273 TRP B CD1 1 
ATOM   24111 C  CD2 . TRP C 1 1273 ? 6.260    34.106  104.730 1.00 70.50  ? 1273 TRP B CD2 1 
ATOM   24112 N  NE1 . TRP C 1 1273 ? 6.173    31.843  104.679 1.00 74.14  ? 1273 TRP B NE1 1 
ATOM   24113 C  CE2 . TRP C 1 1273 ? 5.455    32.980  104.387 1.00 72.73  ? 1273 TRP B CE2 1 
ATOM   24114 C  CE3 . TRP C 1 1273 ? 5.741    35.385  104.523 1.00 69.25  ? 1273 TRP B CE3 1 
ATOM   24115 C  CZ2 . TRP C 1 1273 ? 4.189    33.109  103.858 1.00 73.95  ? 1273 TRP B CZ2 1 
ATOM   24116 C  CZ3 . TRP C 1 1273 ? 4.480    35.503  104.004 1.00 70.42  ? 1273 TRP B CZ3 1 
ATOM   24117 C  CH2 . TRP C 1 1273 ? 3.717    34.378  103.673 1.00 72.51  ? 1273 TRP B CH2 1 
ATOM   24118 N  N   . LEU C 1 1274 ? 8.393    37.106  103.728 1.00 61.40  ? 1274 LEU B N   1 
ATOM   24119 C  CA  . LEU C 1 1274 ? 7.985    37.815  102.516 1.00 64.80  ? 1274 LEU B CA  1 
ATOM   24120 C  C   . LEU C 1 1274 ? 9.145    37.974  101.495 1.00 70.42  ? 1274 LEU B C   1 
ATOM   24121 O  O   . LEU C 1 1274 ? 9.108    37.441  100.414 1.00 73.50  ? 1274 LEU B O   1 
ATOM   24122 C  CB  . LEU C 1 1274 ? 7.278    39.137  102.825 1.00 67.99  ? 1274 LEU B CB  1 
ATOM   24123 C  CG  . LEU C 1 1274 ? 5.858    38.964  103.351 1.00 71.96  ? 1274 LEU B CG  1 
ATOM   24124 C  CD1 . LEU C 1 1274 ? 5.100    40.276  103.487 1.00 72.17  ? 1274 LEU B CD1 1 
ATOM   24125 C  CD2 . LEU C 1 1274 ? 5.131    38.087  102.404 1.00 74.42  ? 1274 LEU B CD2 1 
ATOM   24126 N  N   . SER C 1 1275 ? 10.200   38.673  101.846 1.00 69.78  ? 1275 SER B N   1 
ATOM   24127 C  CA  . SER C 1 1275 ? 11.330   38.879  100.937 1.00 74.44  ? 1275 SER B CA  1 
ATOM   24128 C  C   . SER C 1 1275 ? 11.979   37.587  100.470 1.00 76.15  ? 1275 SER B C   1 
ATOM   24129 O  O   . SER C 1 1275 ? 13.174   37.572  100.117 1.00 75.61  ? 1275 SER B O   1 
ATOM   24130 C  CB  . SER C 1 1275 ? 12.407   39.724  101.628 1.00 83.58  ? 1275 SER B CB  1 
ATOM   24131 O  OG  . SER C 1 1275 ? 12.833   40.828  100.858 1.00 88.99  ? 1275 SER B OG  1 
ATOM   24132 N  N   . GLU C 1 1276 ? 11.198   36.509  100.488 1.00 79.86  ? 1276 GLU B N   1 
ATOM   24133 C  CA  . GLU C 1 1276 ? 11.642   35.165  100.103 1.00 86.01  ? 1276 GLU B CA  1 
ATOM   24134 C  C   . GLU C 1 1276 ? 10.421   34.420  99.656  1.00 86.53  ? 1276 GLU B C   1 
ATOM   24135 O  O   . GLU C 1 1276 ? 10.453   33.189  99.553  1.00 90.05  ? 1276 GLU B O   1 
ATOM   24136 C  CB  . GLU C 1 1276 ? 12.174   34.375  101.303 1.00 90.83  ? 1276 GLU B CB  1 
ATOM   24137 C  CG  . GLU C 1 1276 ? 13.631   34.626  101.674 1.00 93.51  ? 1276 GLU B CG  1 
ATOM   24138 C  CD  . GLU C 1 1276 ? 14.249   33.474  102.448 1.00 93.74  ? 1276 GLU B CD  1 
ATOM   24139 O  OE1 . GLU C 1 1276 ? 13.491   32.537  102.805 1.00 93.06  ? 1276 GLU B OE1 1 
ATOM   24140 O  OE2 . GLU C 1 1276 ? 15.488   33.517  102.675 1.00 93.65  ? 1276 GLU B OE2 1 
ATOM   24141 N  N   . GLU C 1 1277 ? 9.333    35.168  99.475  1.00 83.95  ? 1277 GLU B N   1 
ATOM   24142 C  CA  . GLU C 1 1277 ? 8.047    34.646  99.031  1.00 85.44  ? 1277 GLU B CA  1 
ATOM   24143 C  C   . GLU C 1 1277 ? 7.719    35.227  97.667  1.00 85.57  ? 1277 GLU B C   1 
ATOM   24144 O  O   . GLU C 1 1277 ? 7.588    34.491  96.673  1.00 86.08  ? 1277 GLU B O   1 
ATOM   24145 C  CB  . GLU C 1 1277 ? 6.950    35.011  100.037 1.00 85.09  ? 1277 GLU B CB  1 
ATOM   24146 C  CG  . GLU C 1 1277 ? 5.709    34.117  100.002 1.00 86.78  ? 1277 GLU B CG  1 
ATOM   24147 C  CD  . GLU C 1 1277 ? 6.058    32.649  100.195 1.00 89.79  ? 1277 GLU B CD  1 
ATOM   24148 O  OE1 . GLU C 1 1277 ? 5.168    31.781  100.048 1.00 91.12  ? 1277 GLU B OE1 1 
ATOM   24149 O  OE2 . GLU C 1 1277 ? 7.241    32.359  100.469 1.00 90.90  ? 1277 GLU B OE2 1 
ATOM   24150 N  N   . GLN C 1 1278 ? 7.598    36.555  97.650  1.00 86.32  ? 1278 GLN B N   1 
ATOM   24151 C  CA  . GLN C 1 1278 ? 7.493    37.348  96.421  1.00 89.99  ? 1278 GLN B CA  1 
ATOM   24152 C  C   . GLN C 1 1278 ? 8.419    36.735  95.352  1.00 94.38  ? 1278 GLN B C   1 
ATOM   24153 O  O   . GLN C 1 1278 ? 9.508    36.224  95.673  1.00 95.30  ? 1278 GLN B O   1 
ATOM   24154 C  CB  . GLN C 1 1278 ? 7.795    38.859  96.664  1.00 95.79  ? 1278 GLN B CB  1 
ATOM   24155 C  CG  . GLN C 1 1278 ? 7.017    39.546  97.854  1.00 126.53 ? 1278 GLN B CG  1 
ATOM   24156 C  CD  . GLN C 1 1278 ? 5.455    39.387  97.858  1.00 80.26  ? 1278 GLN B CD  1 
ATOM   24157 O  OE1 . GLN C 1 1278 ? 4.732    40.380  97.958  1.00 77.00  ? 1278 GLN B OE1 1 
ATOM   24158 N  NE2 . GLN C 1 1278 ? 4.956    38.143  97.768  1.00 81.36  ? 1278 GLN B NE2 1 
ATOM   24159 N  N   . ARG C 1 1279 ? 7.960    36.740  94.096  1.00 94.11  ? 1279 ARG B N   1 
ATOM   24160 C  CA  . ARG C 1 1279 ? 8.631    35.997  93.035  1.00 93.12  ? 1279 ARG B CA  1 
ATOM   24161 C  C   . ARG C 1 1279 ? 9.427    36.985  92.264  1.00 86.48  ? 1279 ARG B C   1 
ATOM   24162 O  O   . ARG C 1 1279 ? 9.240    38.160  92.481  1.00 83.59  ? 1279 ARG B O   1 
ATOM   24163 C  CB  . ARG C 1 1279 ? 7.601    35.334  92.132  1.00 98.08  ? 1279 ARG B CB  1 
ATOM   24164 C  CG  . ARG C 1 1279 ? 6.665    34.448  92.889  1.00 102.15 ? 1279 ARG B CG  1 
ATOM   24165 C  CD  . ARG C 1 1279 ? 6.569    33.039  92.326  1.00 108.99 ? 1279 ARG B CD  1 
ATOM   24166 N  NE  . ARG C 1 1279 ? 6.634    32.980  90.870  1.00 113.84 ? 1279 ARG B NE  1 
ATOM   24167 C  CZ  . ARG C 1 1279 ? 6.377    31.881  90.163  1.00 116.73 ? 1279 ARG B CZ  1 
ATOM   24168 N  NH1 . ARG C 1 1279 ? 6.024    30.766  90.788  1.00 116.23 ? 1279 ARG B NH1 1 
ATOM   24169 N  NH2 . ARG C 1 1279 ? 6.460    31.906  88.837  1.00 119.47 ? 1279 ARG B NH2 1 
ATOM   24170 N  N   . TYR C 1 1280 ? 10.295   36.530  91.367  1.00 86.57  ? 1280 TYR B N   1 
ATOM   24171 C  CA  . TYR C 1 1280 ? 11.075   37.441  90.516  1.00 86.96  ? 1280 TYR B CA  1 
ATOM   24172 C  C   . TYR C 1 1280 ? 10.236   38.591  89.882  1.00 68.87  ? 1280 TYR B C   1 
ATOM   24173 O  O   . TYR C 1 1280 ? 9.204    38.357  89.291  1.00 67.49  ? 1280 TYR B O   1 
ATOM   24174 C  CB  . TYR C 1 1280 ? 11.791   36.622  89.455  1.00 87.69  ? 1280 TYR B CB  1 
ATOM   24175 C  CG  . TYR C 1 1280 ? 12.260   37.414  88.283  1.00 87.62  ? 1280 TYR B CG  1 
ATOM   24176 C  CD1 . TYR C 1 1280 ? 12.495   36.792  87.066  1.00 92.86  ? 1280 TYR B CD1 1 
ATOM   24177 C  CD2 . TYR C 1 1280 ? 12.463   38.776  88.367  1.00 84.28  ? 1280 TYR B CD2 1 
ATOM   24178 C  CE1 . TYR C 1 1280 ? 12.937   37.498  85.949  1.00 94.07  ? 1280 TYR B CE1 1 
ATOM   24179 C  CE2 . TYR C 1 1280 ? 12.896   39.496  87.257  1.00 87.45  ? 1280 TYR B CE2 1 
ATOM   24180 C  CZ  . TYR C 1 1280 ? 13.133   38.844  86.050  1.00 92.50  ? 1280 TYR B CZ  1 
ATOM   24181 O  OH  . TYR C 1 1280 ? 13.566   39.531  84.948  1.00 95.97  ? 1280 TYR B OH  1 
ATOM   24182 N  N   . GLY C 1 1281 ? 10.657   39.842  90.019  1.00 67.73  ? 1281 GLY B N   1 
ATOM   24183 C  CA  . GLY C 1 1281 ? 9.817    40.926  89.552  1.00 70.01  ? 1281 GLY B CA  1 
ATOM   24184 C  C   . GLY C 1 1281 ? 8.831    41.560  90.520  1.00 74.08  ? 1281 GLY B C   1 
ATOM   24185 O  O   . GLY C 1 1281 ? 8.924    42.736  90.730  1.00 78.34  ? 1281 GLY B O   1 
ATOM   24186 N  N   . GLY C 1 1282 ? 7.884    40.821  91.098  1.00 79.56  ? 1282 GLY B N   1 
ATOM   24187 C  CA  . GLY C 1 1282 ? 6.965    41.382  92.100  1.00 84.56  ? 1282 GLY B CA  1 
ATOM   24188 C  C   . GLY C 1 1282 ? 6.135    40.323  92.830  1.00 97.48  ? 1282 GLY B C   1 
ATOM   24189 O  O   . GLY C 1 1282 ? 6.410    39.112  92.722  1.00 96.27  ? 1282 GLY B O   1 
ATOM   24190 N  N   . GLY C 1 1283 ? 5.094    40.758  93.542  1.00 109.94 ? 1283 GLY B N   1 
ATOM   24191 C  CA  . GLY C 1 1283 ? 4.406    39.897  94.520  1.00 119.34 ? 1283 GLY B CA  1 
ATOM   24192 C  C   . GLY C 1 1283 ? 3.762    38.530  94.265  1.00 122.65 ? 1283 GLY B C   1 
ATOM   24193 O  O   . GLY C 1 1283 ? 2.911    38.092  95.032  1.00 118.22 ? 1283 GLY B O   1 
ATOM   24194 N  N   . PHE C 1 1284 ? 4.210    37.848  93.224  1.00 131.39 ? 1284 PHE B N   1 
ATOM   24195 C  CA  . PHE C 1 1284 ? 3.508    36.698  92.619  1.00 144.09 ? 1284 PHE B CA  1 
ATOM   24196 C  C   . PHE C 1 1284 ? 2.045    36.408  92.949  1.00 134.22 ? 1284 PHE B C   1 
ATOM   24197 O  O   . PHE C 1 1284 ? 1.220    36.378  92.035  1.00 137.86 ? 1284 PHE B O   1 
ATOM   24198 C  CB  . PHE C 1 1284 ? 4.283    35.398  92.755  1.00 166.79 ? 1284 PHE B CB  1 
ATOM   24199 C  CG  . PHE C 1 1284 ? 3.919    34.350  91.723  1.00 191.12 ? 1284 PHE B CG  1 
ATOM   24200 C  CD1 . PHE C 1 1284 ? 4.124    34.583  90.363  1.00 202.26 ? 1284 PHE B CD1 1 
ATOM   24201 C  CD2 . PHE C 1 1284 ? 3.393    33.121  92.116  1.00 202.66 ? 1284 PHE B CD2 1 
ATOM   24202 C  CE1 . PHE C 1 1284 ? 3.795    33.611  89.416  1.00 213.85 ? 1284 PHE B CE1 1 
ATOM   24203 C  CE2 . PHE C 1 1284 ? 3.063    32.144  91.173  1.00 213.44 ? 1284 PHE B CE2 1 
ATOM   24204 C  CZ  . PHE C 1 1284 ? 3.265    32.392  89.825  1.00 219.53 ? 1284 PHE B CZ  1 
ATOM   24205 N  N   . TYR C 1 1285 ? 1.694    36.108  94.192  1.00 121.70 ? 1285 TYR B N   1 
ATOM   24206 C  CA  . TYR C 1 1285 ? 0.338    35.611  94.361  1.00 112.62 ? 1285 TYR B CA  1 
ATOM   24207 C  C   . TYR C 1 1285 ? -0.655   36.720  94.080  1.00 107.13 ? 1285 TYR B C   1 
ATOM   24208 O  O   . TYR C 1 1285 ? -0.674   37.694  94.815  1.00 109.83 ? 1285 TYR B O   1 
ATOM   24209 C  CB  . TYR C 1 1285 ? 0.126    34.968  95.732  1.00 107.49 ? 1285 TYR B CB  1 
ATOM   24210 C  CG  . TYR C 1 1285 ? 1.157    33.907  96.013  1.00 106.36 ? 1285 TYR B CG  1 
ATOM   24211 C  CD1 . TYR C 1 1285 ? 1.610    33.078  95.008  1.00 106.80 ? 1285 TYR B CD1 1 
ATOM   24212 C  CD2 . TYR C 1 1285 ? 1.704    33.757  97.274  1.00 104.90 ? 1285 TYR B CD2 1 
ATOM   24213 C  CE1 . TYR C 1 1285 ? 2.579    32.135  95.246  1.00 107.06 ? 1285 TYR B CE1 1 
ATOM   24214 C  CE2 . TYR C 1 1285 ? 2.679    32.812  97.527  1.00 103.84 ? 1285 TYR B CE2 1 
ATOM   24215 C  CZ  . TYR C 1 1285 ? 3.109    32.008  96.507  1.00 105.20 ? 1285 TYR B CZ  1 
ATOM   24216 O  OH  . TYR C 1 1285 ? 4.062    31.062  96.753  1.00 106.53 ? 1285 TYR B OH  1 
ATOM   24217 N  N   . SER C 1 1286 ? -1.445   36.604  93.007  1.00 99.11  ? 1286 SER B N   1 
ATOM   24218 C  CA  . SER C 1 1286 ? -2.543   37.559  92.768  1.00 93.06  ? 1286 SER B CA  1 
ATOM   24219 C  C   . SER C 1 1286 ? -2.218   39.053  93.044  1.00 85.92  ? 1286 SER B C   1 
ATOM   24220 O  O   . SER C 1 1286 ? -1.081   39.506  92.928  1.00 84.89  ? 1286 SER B O   1 
ATOM   24221 C  CB  . SER C 1 1286 ? -3.818   37.111  93.506  1.00 91.33  ? 1286 SER B CB  1 
ATOM   24222 O  OG  . SER C 1 1286 ? -4.719   38.156  93.797  1.00 88.43  ? 1286 SER B OG  1 
ATOM   24223 N  N   . THR C 1 1287 ? -3.236   39.827  93.377  1.00 86.56  ? 1287 THR B N   1 
ATOM   24224 C  CA  . THR C 1 1287 ? -3.101   41.268  93.433  1.00 88.90  ? 1287 THR B CA  1 
ATOM   24225 C  C   . THR C 1 1287 ? -3.093   41.716  94.857  1.00 96.21  ? 1287 THR B C   1 
ATOM   24226 O  O   . THR C 1 1287 ? -2.108   42.276  95.350  1.00 98.58  ? 1287 THR B O   1 
ATOM   24227 C  CB  . THR C 1 1287 ? -4.350   41.926  92.876  1.00 86.78  ? 1287 THR B CB  1 
ATOM   24228 O  OG1 . THR C 1 1287 ? -5.492   41.118  93.207  1.00 86.53  ? 1287 THR B OG1 1 
ATOM   24229 C  CG2 . THR C 1 1287 ? -4.257   42.045  91.393  1.00 88.54  ? 1287 THR B CG2 1 
ATOM   24230 N  N   . GLN C 1 1288 ? -4.229   41.457  95.505  1.00 99.96  ? 1288 GLN B N   1 
ATOM   24231 C  CA  . GLN C 1 1288 ? -4.576   42.061  96.776  1.00 100.86 ? 1288 GLN B CA  1 
ATOM   24232 C  C   . GLN C 1 1288 ? -3.526   41.848  97.844  1.00 104.45 ? 1288 GLN B C   1 
ATOM   24233 O  O   . GLN C 1 1288 ? -3.234   42.762  98.614  1.00 106.39 ? 1288 GLN B O   1 
ATOM   24234 C  CB  . GLN C 1 1288 ? -5.928   41.548  97.242  1.00 101.05 ? 1288 GLN B CB  1 
ATOM   24235 C  CG  . GLN C 1 1288 ? -7.059   42.270  96.581  1.00 102.12 ? 1288 GLN B CG  1 
ATOM   24236 C  CD  . GLN C 1 1288 ? -7.218   43.701  97.067  1.00 100.95 ? 1288 GLN B CD  1 
ATOM   24237 O  OE1 . GLN C 1 1288 ? -7.166   43.964  98.275  1.00 102.05 ? 1288 GLN B OE1 1 
ATOM   24238 N  NE2 . GLN C 1 1288 ? -7.442   44.629  96.134  1.00 98.36  ? 1288 GLN B NE2 1 
ATOM   24239 N  N   . ASP C 1 1289 ? -2.954   40.654  97.913  1.00 103.68 ? 1289 ASP B N   1 
ATOM   24240 C  CA  . ASP C 1 1289 ? -1.841   40.481  98.822  1.00 102.73 ? 1289 ASP B CA  1 
ATOM   24241 C  C   . ASP C 1 1289 ? -0.715   41.371  98.310  1.00 101.94 ? 1289 ASP B C   1 
ATOM   24242 O  O   . ASP C 1 1289 ? -0.175   42.205  99.056  1.00 104.22 ? 1289 ASP B O   1 
ATOM   24243 C  CB  . ASP C 1 1289 ? -1.365   39.055  98.801  1.00 104.35 ? 1289 ASP B CB  1 
ATOM   24244 C  CG  . ASP C 1 1289 ? -1.107   38.606  97.428  1.00 105.97 ? 1289 ASP B CG  1 
ATOM   24245 O  OD1 . ASP C 1 1289 ? -2.097   38.604  96.674  1.00 105.35 ? 1289 ASP B OD1 1 
ATOM   24246 O  OD2 . ASP C 1 1289 ? 0.062    38.316  97.093  1.00 107.78 ? 1289 ASP B OD2 1 
ATOM   24247 N  N   . THR C 1 1290 ? -0.368   41.208  97.036  1.00 95.08  ? 1290 THR B N   1 
ATOM   24248 C  CA  . THR C 1 1290 ? 0.810    41.885  96.519  1.00 87.80  ? 1290 THR B CA  1 
ATOM   24249 C  C   . THR C 1 1290 ? 0.876    43.389  96.812  1.00 79.69  ? 1290 THR B C   1 
ATOM   24250 O  O   . THR C 1 1290 ? 1.964    43.946  96.920  1.00 77.41  ? 1290 THR B O   1 
ATOM   24251 C  CB  . THR C 1 1290 ? 1.075    41.575  95.036  1.00 87.61  ? 1290 THR B CB  1 
ATOM   24252 O  OG1 . THR C 1 1290 ? 1.294    40.161  94.881  1.00 89.94  ? 1290 THR B OG1 1 
ATOM   24253 C  CG2 . THR C 1 1290 ? 2.330    42.327  94.548  1.00 84.61  ? 1290 THR B CG2 1 
ATOM   24254 N  N   . ILE C 1 1291 ? -0.255   44.057  96.973  1.00 74.79  ? 1291 ILE B N   1 
ATOM   24255 C  CA  . ILE C 1 1291 ? -0.140   45.469  97.312  1.00 71.75  ? 1291 ILE B CA  1 
ATOM   24256 C  C   . ILE C 1 1291 ? 0.276    45.608  98.749  1.00 71.88  ? 1291 ILE B C   1 
ATOM   24257 O  O   . ILE C 1 1291 ? 1.100    46.446  99.076  1.00 74.56  ? 1291 ILE B O   1 
ATOM   24258 C  CB  . ILE C 1 1291 ? -1.426   46.282  97.064  1.00 64.78  ? 1291 ILE B CB  1 
ATOM   24259 C  CG1 . ILE C 1 1291 ? -1.247   47.724  97.545  1.00 58.07  ? 1291 ILE B CG1 1 
ATOM   24260 C  CG2 . ILE C 1 1291 ? -2.603   45.613  97.713  1.00 63.98  ? 1291 ILE B CG2 1 
ATOM   24261 C  CD1 . ILE C 1 1291 ? -2.544   48.481  97.589  1.00 55.27  ? 1291 ILE B CD1 1 
ATOM   24262 N  N   . ASN C 1 1292 ? -0.281   44.761  99.602  1.00 69.18  ? 1292 ASN B N   1 
ATOM   24263 C  CA  . ASN C 1 1292 ? -0.026   44.832  101.025 1.00 66.31  ? 1292 ASN B CA  1 
ATOM   24264 C  C   . ASN C 1 1292 ? 1.369    44.410  101.305 1.00 67.43  ? 1292 ASN B C   1 
ATOM   24265 O  O   . ASN C 1 1292 ? 2.153    45.194  101.807 1.00 69.96  ? 1292 ASN B O   1 
ATOM   24266 C  CB  . ASN C 1 1292 ? -1.046   44.003  101.761 1.00 65.28  ? 1292 ASN B CB  1 
ATOM   24267 C  CG  . ASN C 1 1292 ? -2.410   44.629  101.657 1.00 66.42  ? 1292 ASN B CG  1 
ATOM   24268 O  OD1 . ASN C 1 1292 ? -2.523   45.863  101.704 1.00 64.19  ? 1292 ASN B OD1 1 
ATOM   24269 N  ND2 . ASN C 1 1292 ? -3.449   43.812  101.474 1.00 66.77  ? 1292 ASN B ND2 1 
ATOM   24270 N  N   . ALA C 1 1293 ? 1.699    43.190  100.927 1.00 66.52  ? 1293 ALA B N   1 
ATOM   24271 C  CA  . ALA C 1 1293 ? 3.062    42.721  101.049 1.00 68.98  ? 1293 ALA B CA  1 
ATOM   24272 C  C   . ALA C 1 1293 ? 4.067    43.708  100.462 1.00 70.30  ? 1293 ALA B C   1 
ATOM   24273 O  O   . ALA C 1 1293 ? 5.160    43.877  101.005 1.00 69.44  ? 1293 ALA B O   1 
ATOM   24274 C  CB  . ALA C 1 1293 ? 3.213    41.369  100.433 1.00 72.82  ? 1293 ALA B CB  1 
ATOM   24275 N  N   . ILE C 1 1294 ? 3.743    44.356  99.350  1.00 73.20  ? 1294 ILE B N   1 
ATOM   24276 C  CA  . ILE C 1 1294 ? 4.683    45.384  98.876  1.00 76.42  ? 1294 ILE B CA  1 
ATOM   24277 C  C   . ILE C 1 1294 ? 4.753    46.532  99.883  1.00 78.14  ? 1294 ILE B C   1 
ATOM   24278 O  O   . ILE C 1 1294 ? 5.834    46.915  100.325 1.00 79.64  ? 1294 ILE B O   1 
ATOM   24279 C  CB  . ILE C 1 1294 ? 4.353    45.996  97.498  1.00 74.56  ? 1294 ILE B CB  1 
ATOM   24280 C  CG1 . ILE C 1 1294 ? 4.567    44.978  96.376  1.00 72.97  ? 1294 ILE B CG1 1 
ATOM   24281 C  CG2 . ILE C 1 1294 ? 5.253    47.217  97.271  1.00 72.79  ? 1294 ILE B CG2 1 
ATOM   24282 C  CD1 . ILE C 1 1294 ? 5.778    45.255  95.555  1.00 71.34  ? 1294 ILE B CD1 1 
ATOM   24283 N  N   . GLU C 1 1295 ? 3.601    47.073  100.255 1.00 76.65  ? 1295 GLU B N   1 
ATOM   24284 C  CA  . GLU C 1 1295 ? 3.602    48.154  101.200 1.00 74.86  ? 1295 GLU B CA  1 
ATOM   24285 C  C   . GLU C 1 1295 ? 4.434    47.753  102.381 1.00 68.77  ? 1295 GLU B C   1 
ATOM   24286 O  O   . GLU C 1 1295 ? 5.341    48.475  102.766 1.00 68.32  ? 1295 GLU B O   1 
ATOM   24287 C  CB  . GLU C 1 1295 ? 2.212    48.469  101.670 1.00 80.24  ? 1295 GLU B CB  1 
ATOM   24288 C  CG  . GLU C 1 1295 ? 2.236    49.729  102.440 1.00 85.94  ? 1295 GLU B CG  1 
ATOM   24289 C  CD  . GLU C 1 1295 ? 0.875    50.189  102.838 1.00 90.52  ? 1295 GLU B CD  1 
ATOM   24290 O  OE1 . GLU C 1 1295 ? -0.003   50.270  101.944 1.00 88.42  ? 1295 GLU B OE1 1 
ATOM   24291 O  OE2 . GLU C 1 1295 ? 0.701    50.474  104.055 1.00 94.37  ? 1295 GLU B OE2 1 
ATOM   24292 N  N   . GLY C 1 1296 ? 4.133    46.592  102.948 1.00 66.21  ? 1296 GLY B N   1 
ATOM   24293 C  CA  . GLY C 1 1296 ? 4.942    46.047  104.028 1.00 66.60  ? 1296 GLY B CA  1 
ATOM   24294 C  C   . GLY C 1 1296 ? 6.444    46.134  103.763 1.00 66.31  ? 1296 GLY B C   1 
ATOM   24295 O  O   . GLY C 1 1296 ? 7.150    46.988  104.287 1.00 66.31  ? 1296 GLY B O   1 
ATOM   24296 N  N   . LEU C 1 1297 ? 6.938    45.243  102.931 1.00 65.95  ? 1297 LEU B N   1 
ATOM   24297 C  CA  . LEU C 1 1297 ? 8.302    45.340  102.466 1.00 66.97  ? 1297 LEU B CA  1 
ATOM   24298 C  C   . LEU C 1 1297 ? 8.873    46.765  102.318 1.00 69.77  ? 1297 LEU B C   1 
ATOM   24299 O  O   . LEU C 1 1297 ? 10.055   47.009  102.587 1.00 68.76  ? 1297 LEU B O   1 
ATOM   24300 C  CB  . LEU C 1 1297 ? 8.417    44.578  101.152 1.00 64.79  ? 1297 LEU B CB  1 
ATOM   24301 C  CG  . LEU C 1 1297 ? 9.005    43.235  101.537 1.00 63.50  ? 1297 LEU B CG  1 
ATOM   24302 C  CD1 . LEU C 1 1297 ? 7.964    42.123  101.596 1.00 61.89  ? 1297 LEU B CD1 1 
ATOM   24303 C  CD2 . LEU C 1 1297 ? 10.115   42.928  100.577 1.00 64.52  ? 1297 LEU B CD2 1 
ATOM   24304 N  N   . THR C 1 1298 ? 8.060    47.709  101.856 1.00 73.96  ? 1298 THR B N   1 
ATOM   24305 C  CA  . THR C 1 1298 ? 8.611    49.048  101.629 1.00 74.48  ? 1298 THR B CA  1 
ATOM   24306 C  C   . THR C 1 1298 ? 8.727    49.660  102.993 1.00 74.95  ? 1298 THR B C   1 
ATOM   24307 O  O   . THR C 1 1298 ? 9.843    49.939  103.476 1.00 72.06  ? 1298 THR B O   1 
ATOM   24308 C  CB  . THR C 1 1298 ? 7.721    49.970  100.754 1.00 71.65  ? 1298 THR B CB  1 
ATOM   24309 O  OG1 . THR C 1 1298 ? 7.056    49.193  99.754  1.00 74.12  ? 1298 THR B OG1 1 
ATOM   24310 C  CG2 . THR C 1 1298 ? 8.567    51.019  100.066 1.00 69.63  ? 1298 THR B CG2 1 
ATOM   24311 N  N   . GLU C 1 1299 ? 7.547    49.792  103.609 1.00 75.28  ? 1299 GLU B N   1 
ATOM   24312 C  CA  . GLU C 1 1299 ? 7.325    50.527  104.845 1.00 77.66  ? 1299 GLU B CA  1 
ATOM   24313 C  C   . GLU C 1 1299 ? 8.288    50.123  105.980 1.00 77.45  ? 1299 GLU B C   1 
ATOM   24314 O  O   . GLU C 1 1299 ? 8.765    50.983  106.754 1.00 79.60  ? 1299 GLU B O   1 
ATOM   24315 C  CB  . GLU C 1 1299 ? 5.860    50.381  105.254 1.00 79.15  ? 1299 GLU B CB  1 
ATOM   24316 C  CG  . GLU C 1 1299 ? 5.347    51.571  106.036 1.00 84.76  ? 1299 GLU B CG  1 
ATOM   24317 C  CD  . GLU C 1 1299 ? 5.026    52.792  105.172 1.00 90.10  ? 1299 GLU B CD  1 
ATOM   24318 O  OE1 . GLU C 1 1299 ? 4.113    52.688  104.332 1.00 92.33  ? 1299 GLU B OE1 1 
ATOM   24319 O  OE2 . GLU C 1 1299 ? 5.653    53.863  105.361 1.00 91.13  ? 1299 GLU B OE2 1 
ATOM   24320 N  N   . TYR C 1 1300 ? 8.576    48.824  106.050 1.00 72.29  ? 1300 TYR B N   1 
ATOM   24321 C  CA  . TYR C 1 1300 ? 9.608    48.286  106.924 1.00 69.30  ? 1300 TYR B CA  1 
ATOM   24322 C  C   . TYR C 1 1300 ? 11.028   48.662  106.536 1.00 65.95  ? 1300 TYR B C   1 
ATOM   24323 O  O   . TYR C 1 1300 ? 11.848   48.797  107.391 1.00 62.07  ? 1300 TYR B O   1 
ATOM   24324 C  CB  . TYR C 1 1300 ? 9.484    46.757  107.012 1.00 72.38  ? 1300 TYR B CB  1 
ATOM   24325 C  CG  . TYR C 1 1300 ? 10.703   46.043  107.585 1.00 72.92  ? 1300 TYR B CG  1 
ATOM   24326 C  CD1 . TYR C 1 1300 ? 10.673   45.507  108.865 1.00 73.84  ? 1300 TYR B CD1 1 
ATOM   24327 C  CD2 . TYR C 1 1300 ? 11.869   45.897  106.840 1.00 71.34  ? 1300 TYR B CD2 1 
ATOM   24328 C  CE1 . TYR C 1 1300 ? 11.769   44.867  109.395 1.00 75.01  ? 1300 TYR B CE1 1 
ATOM   24329 C  CE2 . TYR C 1 1300 ? 12.967   45.259  107.354 1.00 72.78  ? 1300 TYR B CE2 1 
ATOM   24330 C  CZ  . TYR C 1 1300 ? 12.920   44.743  108.638 1.00 75.58  ? 1300 TYR B CZ  1 
ATOM   24331 O  OH  . TYR C 1 1300 ? 14.026   44.108  109.175 1.00 78.27  ? 1300 TYR B OH  1 
ATOM   24332 N  N   . SER C 1 1301 ? 11.352   48.783  105.256 1.00 70.13  ? 1301 SER B N   1 
ATOM   24333 C  CA  . SER C 1 1301 ? 12.749   49.065  104.885 1.00 73.41  ? 1301 SER B CA  1 
ATOM   24334 C  C   . SER C 1 1301 ? 12.957   50.520  105.132 1.00 69.33  ? 1301 SER B C   1 
ATOM   24335 O  O   . SER C 1 1301 ? 14.065   51.024  105.151 1.00 65.49  ? 1301 SER B O   1 
ATOM   24336 C  CB  . SER C 1 1301 ? 13.067   48.703  103.426 1.00 79.10  ? 1301 SER B CB  1 
ATOM   24337 O  OG  . SER C 1 1301 ? 13.789   47.475  103.353 1.00 82.19  ? 1301 SER B OG  1 
ATOM   24338 N  N   . LEU C 1 1302 ? 11.821   51.165  105.323 1.00 71.02  ? 1302 LEU B N   1 
ATOM   24339 C  CA  . LEU C 1 1302 ? 11.707   52.536  105.759 1.00 76.00  ? 1302 LEU B CA  1 
ATOM   24340 C  C   . LEU C 1 1302 ? 11.851   52.696  107.262 1.00 78.25  ? 1302 LEU B C   1 
ATOM   24341 O  O   . LEU C 1 1302 ? 12.635   53.538  107.711 1.00 84.20  ? 1302 LEU B O   1 
ATOM   24342 C  CB  . LEU C 1 1302 ? 10.331   53.041  105.374 1.00 78.87  ? 1302 LEU B CB  1 
ATOM   24343 C  CG  . LEU C 1 1302 ? 10.362   53.515  103.939 1.00 81.63  ? 1302 LEU B CG  1 
ATOM   24344 C  CD1 . LEU C 1 1302 ? 8.947    53.770  103.446 1.00 81.02  ? 1302 LEU B CD1 1 
ATOM   24345 C  CD2 . LEU C 1 1302 ? 11.242   54.767  103.927 1.00 83.53  ? 1302 LEU B CD2 1 
ATOM   24346 N  N   . LEU C 1 1303 ? 11.065   51.916  108.020 1.00 71.99  ? 1303 LEU B N   1 
ATOM   24347 C  CA  . LEU C 1 1303 ? 11.129   51.857  109.498 1.00 66.58  ? 1303 LEU B CA  1 
ATOM   24348 C  C   . LEU C 1 1303 ? 12.454   51.348  110.101 1.00 61.11  ? 1303 LEU B C   1 
ATOM   24349 O  O   . LEU C 1 1303 ? 12.949   51.917  111.035 1.00 60.62  ? 1303 LEU B O   1 
ATOM   24350 C  CB  . LEU C 1 1303 ? 9.921    51.079  110.037 1.00 66.38  ? 1303 LEU B CB  1 
ATOM   24351 C  CG  . LEU C 1 1303 ? 9.720    50.413  111.400 1.00 63.10  ? 1303 LEU B CG  1 
ATOM   24352 C  CD1 . LEU C 1 1303 ? 10.942   49.667  111.812 1.00 60.12  ? 1303 LEU B CD1 1 
ATOM   24353 C  CD2 . LEU C 1 1303 ? 9.306    51.409  112.454 1.00 64.72  ? 1303 LEU B CD2 1 
ATOM   24354 N  N   . VAL C 1 1304 ? 13.004   50.265  109.582 1.00 60.80  ? 1304 VAL B N   1 
ATOM   24355 C  CA  . VAL C 1 1304 ? 14.333   49.768  109.978 1.00 64.59  ? 1304 VAL B CA  1 
ATOM   24356 C  C   . VAL C 1 1304 ? 15.431   50.406  109.128 1.00 65.37  ? 1304 VAL B C   1 
ATOM   24357 O  O   . VAL C 1 1304 ? 15.220   50.575  107.945 1.00 70.00  ? 1304 VAL B O   1 
ATOM   24358 C  CB  . VAL C 1 1304 ? 14.445   48.257  109.703 1.00 68.04  ? 1304 VAL B CB  1 
ATOM   24359 C  CG1 . VAL C 1 1304 ? 15.877   47.799  109.862 1.00 72.14  ? 1304 VAL B CG1 1 
ATOM   24360 C  CG2 . VAL C 1 1304 ? 13.480   47.408  110.557 1.00 65.93  ? 1304 VAL B CG2 1 
ATOM   24361 N  N   . LYS C 1 1305 ? 16.621   50.683  109.646 1.00 91.72  ? 1305 LYS B N   1 
ATOM   24362 C  CA  . LYS C 1 1305 ? 17.605   51.300  108.753 1.00 94.97  ? 1305 LYS B CA  1 
ATOM   24363 C  C   . LYS C 1 1305 ? 18.130   50.436  107.604 1.00 98.02  ? 1305 LYS B C   1 
ATOM   24364 O  O   . LYS C 1 1305 ? 18.131   49.223  107.705 1.00 99.28  ? 1305 LYS B O   1 
ATOM   24365 C  CB  . LYS C 1 1305 ? 18.769   51.848  109.518 1.00 97.64  ? 1305 LYS B CB  1 
ATOM   24366 C  CG  . LYS C 1 1305 ? 19.367   53.028  108.807 1.00 101.41 ? 1305 LYS B CG  1 
ATOM   24367 C  CD  . LYS C 1 1305 ? 19.731   54.171  109.788 1.00 123.30 ? 1305 LYS B CD  1 
ATOM   24368 C  CE  . LYS C 1 1305 ? 18.533   55.053  110.236 1.00 130.12 ? 1305 LYS B CE  1 
ATOM   24369 N  NZ  . LYS C 1 1305 ? 18.964   56.042  111.275 1.00 130.36 ? 1305 LYS B NZ  1 
ATOM   24370 N  N   . GLN C 1 1306 ? 18.572   51.056  106.503 1.00 100.07 ? 1306 GLN B N   1 
ATOM   24371 C  CA  . GLN C 1 1306 ? 19.121   50.284  105.355 1.00 100.46 ? 1306 GLN B CA  1 
ATOM   24372 C  C   . GLN C 1 1306 ? 20.421   49.644  105.803 1.00 100.47 ? 1306 GLN B C   1 
ATOM   24373 O  O   . GLN C 1 1306 ? 20.792   49.806  106.958 1.00 103.86 ? 1306 GLN B O   1 
ATOM   24374 C  CB  . GLN C 1 1306 ? 19.324   51.148  104.075 1.00 139.77 ? 1306 GLN B CB  1 
ATOM   24375 C  CG  . GLN C 1 1306 ? 18.326   50.813  102.887 1.00 189.53 ? 1306 GLN B CG  1 
ATOM   24376 C  CD  . GLN C 1 1306 ? 18.687   51.433  101.504 1.00 119.40 ? 1306 GLN B CD  1 
ATOM   24377 O  OE1 . GLN C 1 1306 ? 19.653   51.043  100.841 1.00 118.70 ? 1306 GLN B OE1 1 
ATOM   24378 N  NE2 . GLN C 1 1306 ? 17.873   52.371  101.069 1.00 120.60 ? 1306 GLN B NE2 1 
ATOM   24379 N  N   . LEU C 1 1307 ? 21.110   48.904  104.942 1.00 98.71  ? 1307 LEU B N   1 
ATOM   24380 C  CA  . LEU C 1 1307 ? 22.455   48.455  105.313 1.00 97.30  ? 1307 LEU B CA  1 
ATOM   24381 C  C   . LEU C 1 1307 ? 23.394   48.346  104.133 1.00 97.41  ? 1307 LEU B C   1 
ATOM   24382 O  O   . LEU C 1 1307 ? 23.411   47.340  103.403 1.00 97.16  ? 1307 LEU B O   1 
ATOM   24383 C  CB  . LEU C 1 1307 ? 22.458   47.104  106.026 1.00 98.21  ? 1307 LEU B CB  1 
ATOM   24384 C  CG  . LEU C 1 1307 ? 21.451   46.607  107.056 1.00 98.44  ? 1307 LEU B CG  1 
ATOM   24385 C  CD1 . LEU C 1 1307 ? 20.056   46.375  106.421 1.00 99.90  ? 1307 LEU B CD1 1 
ATOM   24386 C  CD2 . LEU C 1 1307 ? 22.042   45.324  107.657 1.00 97.04  ? 1307 LEU B CD2 1 
ATOM   24387 N  N   . ARG C 1 1308 ? 24.204   49.381  103.993 1.00 95.71  ? 1308 ARG B N   1 
ATOM   24388 C  CA  . ARG C 1 1308 ? 25.236   49.463  102.978 1.00 91.80  ? 1308 ARG B CA  1 
ATOM   24389 C  C   . ARG C 1 1308 ? 25.625   48.103  102.414 1.00 87.08  ? 1308 ARG B C   1 
ATOM   24390 O  O   . ARG C 1 1308 ? 26.264   47.296  103.091 1.00 82.76  ? 1308 ARG B O   1 
ATOM   24391 C  CB  . ARG C 1 1308 ? 26.442   50.192  103.573 1.00 92.15  ? 1308 ARG B CB  1 
ATOM   24392 C  CG  . ARG C 1 1308 ? 27.762   49.821  103.006 1.00 92.82  ? 1308 ARG B CG  1 
ATOM   24393 C  CD  . ARG C 1 1308 ? 28.697   50.992  103.125 1.00 96.20  ? 1308 ARG B CD  1 
ATOM   24394 N  NE  . ARG C 1 1308 ? 29.819   50.888  102.204 1.00 99.09  ? 1308 ARG B NE  1 
ATOM   24395 C  CZ  . ARG C 1 1308 ? 30.634   49.841  102.179 1.00 101.29 ? 1308 ARG B CZ  1 
ATOM   24396 N  NH1 . ARG C 1 1308 ? 30.450   48.821  103.043 1.00 99.03  ? 1308 ARG B NH1 1 
ATOM   24397 N  NH2 . ARG C 1 1308 ? 31.625   49.809  101.293 1.00 103.79 ? 1308 ARG B NH2 1 
ATOM   24398 N  N   . LEU C 1 1309 ? 25.205   47.872  101.167 1.00 86.54  ? 1309 LEU B N   1 
ATOM   24399 C  CA  . LEU C 1 1309 ? 25.521   46.651  100.419 1.00 86.53  ? 1309 LEU B CA  1 
ATOM   24400 C  C   . LEU C 1 1309 ? 26.992   46.514  100.031 1.00 87.55  ? 1309 LEU B C   1 
ATOM   24401 O  O   . LEU C 1 1309 ? 27.610   47.446  99.502  1.00 87.32  ? 1309 LEU B O   1 
ATOM   24402 C  CB  . LEU C 1 1309 ? 24.695   46.603  99.137  1.00 83.81  ? 1309 LEU B CB  1 
ATOM   24403 C  CG  . LEU C 1 1309 ? 23.241   46.185  99.208  1.00 81.98  ? 1309 LEU B CG  1 
ATOM   24404 C  CD1 . LEU C 1 1309 ? 22.575   46.707  98.002  1.00 82.18  ? 1309 LEU B CD1 1 
ATOM   24405 C  CD2 . LEU C 1 1309 ? 23.122   44.687  99.232  1.00 79.74  ? 1309 LEU B CD2 1 
ATOM   24406 N  N   . SER C 1 1310 ? 27.544   45.336  100.260 1.00 82.37  ? 1310 SER B N   1 
ATOM   24407 C  CA  . SER C 1 1310 ? 28.879   45.080  99.782  1.00 83.52  ? 1310 SER B CA  1 
ATOM   24408 C  C   . SER C 1 1310 ? 29.248   43.622  99.862  1.00 89.88  ? 1310 SER B C   1 
ATOM   24409 O  O   . SER C 1 1310 ? 30.321   43.274  100.347 1.00 84.00  ? 1310 SER B O   1 
ATOM   24410 C  CB  . SER C 1 1310 ? 29.911   45.938  100.502 1.00 87.55  ? 1310 SER B CB  1 
ATOM   24411 O  OG  . SER C 1 1310 ? 31.203   45.341  100.431 1.00 89.31  ? 1310 SER B OG  1 
ATOM   24412 N  N   . MET C 1 1311 ? 28.340   42.778  99.386  1.00 89.76  ? 1311 MET B N   1 
ATOM   24413 C  CA  . MET C 1 1311 ? 28.678   41.419  99.005  1.00 93.09  ? 1311 MET B CA  1 
ATOM   24414 C  C   . MET C 1 1311 ? 29.560   41.327  97.769  1.00 94.53  ? 1311 MET B C   1 
ATOM   24415 O  O   . MET C 1 1311 ? 30.010   42.329  97.211  1.00 95.54  ? 1311 MET B O   1 
ATOM   24416 C  CB  . MET C 1 1311 ? 27.423   40.644  98.726  1.00 81.31  ? 1311 MET B CB  1 
ATOM   24417 C  CG  . MET C 1 1311 ? 26.817   40.117  99.940  1.00 80.37  ? 1311 MET B CG  1 
ATOM   24418 S  SD  . MET C 1 1311 ? 25.061   40.071  99.755  1.00 97.26  ? 1311 MET B SD  1 
ATOM   24419 C  CE  . MET C 1 1311 ? 24.656   41.692  100.393 1.00 100.75 ? 1311 MET B CE  1 
ATOM   24420 N  N   . ASP C 1 1312 ? 29.779   40.088  97.349  1.00 99.34  ? 1312 ASP B N   1 
ATOM   24421 C  CA  . ASP C 1 1312 ? 30.721   39.741  96.295  1.00 101.42 ? 1312 ASP B CA  1 
ATOM   24422 C  C   . ASP C 1 1312 ? 30.234   38.454  95.667  1.00 98.21  ? 1312 ASP B C   1 
ATOM   24423 O  O   . ASP C 1 1312 ? 30.906   37.415  95.701  1.00 97.29  ? 1312 ASP B O   1 
ATOM   24424 C  CB  . ASP C 1 1312 ? 32.091   39.511  96.893  1.00 108.25 ? 1312 ASP B CB  1 
ATOM   24425 C  CG  . ASP C 1 1312 ? 33.187   39.836  95.932  1.00 115.94 ? 1312 ASP B CG  1 
ATOM   24426 O  OD1 . ASP C 1 1312 ? 32.922   39.815  94.693  1.00 117.64 ? 1312 ASP B OD1 1 
ATOM   24427 O  OD2 . ASP C 1 1312 ? 34.304   40.120  96.430  1.00 119.01 ? 1312 ASP B OD2 1 
ATOM   24428 N  N   . ILE C 1 1313 ? 29.028   38.537  95.126  1.00 95.92  ? 1313 ILE B N   1 
ATOM   24429 C  CA  . ILE C 1 1313 ? 28.276   37.361  94.759  1.00 94.12  ? 1313 ILE B CA  1 
ATOM   24430 C  C   . ILE C 1 1313 ? 28.924   36.564  93.674  1.00 99.00  ? 1313 ILE B C   1 
ATOM   24431 O  O   . ILE C 1 1313 ? 29.719   37.073  92.887  1.00 105.42 ? 1313 ILE B O   1 
ATOM   24432 C  CB  . ILE C 1 1313 ? 26.942   37.752  94.270  1.00 89.78  ? 1313 ILE B CB  1 
ATOM   24433 C  CG1 . ILE C 1 1313 ? 26.510   38.986  95.031  1.00 89.70  ? 1313 ILE B CG1 1 
ATOM   24434 C  CG2 . ILE C 1 1313 ? 25.987   36.615  94.471  1.00 88.51  ? 1313 ILE B CG2 1 
ATOM   24435 C  CD1 . ILE C 1 1313 ? 25.223   38.786  95.729  1.00 90.32  ? 1313 ILE B CD1 1 
ATOM   24436 N  N   . ASP C 1 1314 ? 28.574   35.296  93.621  1.00 95.52  ? 1314 ASP B N   1 
ATOM   24437 C  CA  . ASP C 1 1314 ? 29.123   34.452  92.598  1.00 93.91  ? 1314 ASP B CA  1 
ATOM   24438 C  C   . ASP C 1 1314 ? 28.136   33.394  92.256  1.00 92.63  ? 1314 ASP B C   1 
ATOM   24439 O  O   . ASP C 1 1314 ? 27.869   32.488  93.040  1.00 92.03  ? 1314 ASP B O   1 
ATOM   24440 C  CB  . ASP C 1 1314 ? 30.396   33.775  93.053  1.00 96.46  ? 1314 ASP B CB  1 
ATOM   24441 C  CG  . ASP C 1 1314 ? 30.671   32.521  92.270  1.00 99.53  ? 1314 ASP B CG  1 
ATOM   24442 O  OD1 . ASP C 1 1314 ? 30.029   31.478  92.539  1.00 98.46  ? 1314 ASP B OD1 1 
ATOM   24443 O  OD2 . ASP C 1 1314 ? 31.518   32.589  91.361  1.00 103.70 ? 1314 ASP B OD2 1 
ATOM   24444 N  N   . VAL C 1 1315 ? 27.599   33.512  91.058  1.00 91.40  ? 1315 VAL B N   1 
ATOM   24445 C  CA  . VAL C 1 1315 ? 26.688   32.520  90.541  1.00 89.54  ? 1315 VAL B CA  1 
ATOM   24446 C  C   . VAL C 1 1315 ? 27.539   31.546  89.717  1.00 91.62  ? 1315 VAL B C   1 
ATOM   24447 O  O   . VAL C 1 1315 ? 28.480   31.976  89.051  1.00 93.07  ? 1315 VAL B O   1 
ATOM   24448 C  CB  . VAL C 1 1315 ? 25.555   33.215  89.787  1.00 87.97  ? 1315 VAL B CB  1 
ATOM   24449 C  CG1 . VAL C 1 1315 ? 26.110   34.146  88.726  1.00 84.48  ? 1315 VAL B CG1 1 
ATOM   24450 C  CG2 . VAL C 1 1315 ? 24.554   32.209  89.264  1.00 83.61  ? 1315 VAL B CG2 1 
ATOM   24451 N  N   . SER C 1 1316 ? 27.266   30.244  89.819  1.00 94.76  ? 1316 SER B N   1 
ATOM   24452 C  CA  . SER C 1 1316 ? 28.193   29.232  89.293  1.00 100.31 ? 1316 SER B CA  1 
ATOM   24453 C  C   . SER C 1 1316 ? 27.592   27.827  89.155  1.00 105.18 ? 1316 SER B C   1 
ATOM   24454 O  O   . SER C 1 1316 ? 26.795   27.397  89.986  1.00 105.34 ? 1316 SER B O   1 
ATOM   24455 C  CB  . SER C 1 1316 ? 29.437   29.153  90.175  1.00 101.63 ? 1316 SER B CB  1 
ATOM   24456 O  OG  . SER C 1 1316 ? 30.510   28.597  89.438  1.00 103.78 ? 1316 SER B OG  1 
ATOM   24457 N  N   . TYR C 1 1317 ? 27.977   27.100  88.112  1.00 109.80 ? 1317 TYR B N   1 
ATOM   24458 C  CA  . TYR C 1 1317 ? 27.426   25.766  87.908  1.00 114.23 ? 1317 TYR B CA  1 
ATOM   24459 C  C   . TYR C 1 1317 ? 28.178   24.752  88.737  1.00 115.30 ? 1317 TYR B C   1 
ATOM   24460 O  O   . TYR C 1 1317 ? 29.406   24.734  88.716  1.00 115.59 ? 1317 TYR B O   1 
ATOM   24461 C  CB  . TYR C 1 1317 ? 27.543   25.374  86.450  1.00 119.78 ? 1317 TYR B CB  1 
ATOM   24462 C  CG  . TYR C 1 1317 ? 26.710   26.225  85.565  1.00 124.26 ? 1317 TYR B CG  1 
ATOM   24463 C  CD1 . TYR C 1 1317 ? 27.243   27.339  84.943  1.00 127.37 ? 1317 TYR B CD1 1 
ATOM   24464 C  CD2 . TYR C 1 1317 ? 25.379   25.931  85.369  1.00 126.37 ? 1317 TYR B CD2 1 
ATOM   24465 C  CE1 . TYR C 1 1317 ? 26.465   28.140  84.130  1.00 130.58 ? 1317 TYR B CE1 1 
ATOM   24466 C  CE2 . TYR C 1 1317 ? 24.588   26.711  84.560  1.00 129.94 ? 1317 TYR B CE2 1 
ATOM   24467 C  CZ  . TYR C 1 1317 ? 25.127   27.825  83.933  1.00 132.04 ? 1317 TYR B CZ  1 
ATOM   24468 O  OH  . TYR C 1 1317 ? 24.321   28.609  83.106  1.00 133.14 ? 1317 TYR B OH  1 
ATOM   24469 N  N   . LYS C 1 1318 ? 27.451   23.889  89.441  1.00 115.52 ? 1318 LYS B N   1 
ATOM   24470 C  CA  . LYS C 1 1318 ? 28.088   22.871  90.271  1.00 117.06 ? 1318 LYS B CA  1 
ATOM   24471 C  C   . LYS C 1 1318 ? 29.223   22.086  89.600  1.00 123.53 ? 1318 LYS B C   1 
ATOM   24472 O  O   . LYS C 1 1318 ? 30.264   21.892  90.219  1.00 123.45 ? 1318 LYS B O   1 
ATOM   24473 C  CB  . LYS C 1 1318 ? 27.067   21.910  90.876  1.00 115.90 ? 1318 LYS B CB  1 
ATOM   24474 C  CG  . LYS C 1 1318 ? 27.690   20.588  91.292  1.00 118.56 ? 1318 LYS B CG  1 
ATOM   24475 C  CD  . LYS C 1 1318 ? 27.378   20.207  92.739  1.00 120.17 ? 1318 LYS B CD  1 
ATOM   24476 C  CE  . LYS C 1 1318 ? 25.934   19.760  92.925  1.00 120.78 ? 1318 LYS B CE  1 
ATOM   24477 N  NZ  . LYS C 1 1318 ? 25.676   19.303  94.324  1.00 120.49 ? 1318 LYS B NZ  1 
ATOM   24478 N  N   . HIS C 1 1319 ? 29.038   21.627  88.360  1.00 130.57 ? 1319 HIS B N   1 
ATOM   24479 C  CA  . HIS C 1 1319 ? 30.107   20.908  87.646  1.00 137.22 ? 1319 HIS B CA  1 
ATOM   24480 C  C   . HIS C 1 1319 ? 30.709   21.677  86.475  1.00 148.57 ? 1319 HIS B C   1 
ATOM   24481 O  O   . HIS C 1 1319 ? 31.918   21.628  86.258  1.00 150.22 ? 1319 HIS B O   1 
ATOM   24482 C  CB  . HIS C 1 1319 ? 29.635   19.540  87.185  1.00 132.64 ? 1319 HIS B CB  1 
ATOM   24483 C  CG  . HIS C 1 1319 ? 28.841   18.814  88.214  1.00 130.36 ? 1319 HIS B CG  1 
ATOM   24484 N  ND1 . HIS C 1 1319 ? 27.472   18.927  88.307  1.00 129.23 ? 1319 HIS B ND1 1 
ATOM   24485 C  CD2 . HIS C 1 1319 ? 29.220   17.981  89.210  1.00 131.37 ? 1319 HIS B CD2 1 
ATOM   24486 C  CE1 . HIS C 1 1319 ? 27.036   18.184  89.309  1.00 129.30 ? 1319 HIS B CE1 1 
ATOM   24487 N  NE2 . HIS C 1 1319 ? 28.078   17.601  89.876  1.00 130.67 ? 1319 HIS B NE2 1 
ATOM   24488 N  N   . LYS C 1 1320 ? 29.870   22.373  85.714  1.00 159.03 ? 1320 LYS B N   1 
ATOM   24489 C  CA  . LYS C 1 1320 ? 30.366   23.225  84.636  1.00 171.77 ? 1320 LYS B CA  1 
ATOM   24490 C  C   . LYS C 1 1320 ? 31.197   24.388  85.181  1.00 178.89 ? 1320 LYS B C   1 
ATOM   24491 O  O   . LYS C 1 1320 ? 30.971   24.852  86.304  1.00 180.01 ? 1320 LYS B O   1 
ATOM   24492 C  CB  . LYS C 1 1320 ? 29.214   23.781  83.800  1.00 175.69 ? 1320 LYS B CB  1 
ATOM   24493 C  CG  . LYS C 1 1320 ? 29.637   24.893  82.837  1.00 180.78 ? 1320 LYS B CG  1 
ATOM   24494 C  CD  . LYS C 1 1320 ? 30.635   24.389  81.786  1.00 186.53 ? 1320 LYS B CD  1 
ATOM   24495 C  CE  . LYS C 1 1320 ? 31.076   25.496  80.818  1.00 189.19 ? 1320 LYS B CE  1 
ATOM   24496 N  NZ  . LYS C 1 1320 ? 31.930   24.993  79.689  1.00 191.32 ? 1320 LYS B NZ  1 
ATOM   24497 N  N   . GLY C 1 1321 ? 32.148   24.864  84.378  1.00 182.75 ? 1321 GLY B N   1 
ATOM   24498 C  CA  . GLY C 1 1321 ? 32.951   26.022  84.736  1.00 182.42 ? 1321 GLY B CA  1 
ATOM   24499 C  C   . GLY C 1 1321 ? 32.118   27.147  85.323  1.00 179.60 ? 1321 GLY B C   1 
ATOM   24500 O  O   . GLY C 1 1321 ? 30.894   27.184  85.182  1.00 182.12 ? 1321 GLY B O   1 
ATOM   24501 N  N   . ALA C 1 1322 ? 32.785   28.073  85.996  1.00 174.31 ? 1322 ALA B N   1 
ATOM   24502 C  CA  . ALA C 1 1322 ? 32.091   29.180  86.638  1.00 164.95 ? 1322 ALA B CA  1 
ATOM   24503 C  C   . ALA C 1 1322 ? 31.319   30.023  85.634  1.00 163.28 ? 1322 ALA B C   1 
ATOM   24504 O  O   . ALA C 1 1322 ? 31.829   30.388  84.577  1.00 159.44 ? 1322 ALA B O   1 
ATOM   24505 C  CB  . ALA C 1 1322 ? 33.081   30.061  87.417  1.00 164.95 ? 1322 ALA B CB  1 
ATOM   24506 N  N   . LEU C 1 1323 ? 30.078   30.323  85.964  1.00 159.98 ? 1323 LEU B N   1 
ATOM   24507 C  CA  . LEU C 1 1323 ? 29.386   31.382  85.279  1.00 152.11 ? 1323 LEU B CA  1 
ATOM   24508 C  C   . LEU C 1 1323 ? 29.735   32.661  86.044  1.00 159.17 ? 1323 LEU B C   1 
ATOM   24509 O  O   . LEU C 1 1323 ? 30.660   32.659  86.868  1.00 164.63 ? 1323 LEU B O   1 
ATOM   24510 C  CB  . LEU C 1 1323 ? 27.902   31.055  85.242  1.00 135.52 ? 1323 LEU B CB  1 
ATOM   24511 C  CG  . LEU C 1 1323 ? 26.787   32.086  85.145  1.00 108.93 ? 1323 LEU B CG  1 
ATOM   24512 C  CD1 . LEU C 1 1323 ? 27.054   33.140  84.116  1.00 105.73 ? 1323 LEU B CD1 1 
ATOM   24513 C  CD2 . LEU C 1 1323 ? 25.491   31.365  84.857  1.00 102.59 ? 1323 LEU B CD2 1 
ATOM   24514 N  N   . HIS C 1 1324 ? 29.027   33.749  85.764  1.00 155.12 ? 1324 HIS B N   1 
ATOM   24515 C  CA  . HIS C 1 1324 ? 29.391   35.070  86.276  1.00 152.13 ? 1324 HIS B CA  1 
ATOM   24516 C  C   . HIS C 1 1324 ? 29.396   35.228  87.812  1.00 150.77 ? 1324 HIS B C   1 
ATOM   24517 O  O   . HIS C 1 1324 ? 28.815   34.428  88.541  1.00 147.75 ? 1324 HIS B O   1 
ATOM   24518 C  CB  . HIS C 1 1324 ? 28.525   36.149  85.612  1.00 154.86 ? 1324 HIS B CB  1 
ATOM   24519 C  CG  . HIS C 1 1324 ? 27.154   36.284  86.201  1.00 159.36 ? 1324 HIS B CG  1 
ATOM   24520 N  ND1 . HIS C 1 1324 ? 26.884   37.115  87.269  1.00 162.24 ? 1324 HIS B ND1 1 
ATOM   24521 C  CD2 . HIS C 1 1324 ? 25.973   35.712  85.863  1.00 162.33 ? 1324 HIS B CD2 1 
ATOM   24522 C  CE1 . HIS C 1 1324 ? 25.600   37.044  87.569  1.00 163.23 ? 1324 HIS B CE1 1 
ATOM   24523 N  NE2 . HIS C 1 1324 ? 25.025   36.197  86.733  1.00 163.70 ? 1324 HIS B NE2 1 
ATOM   24524 N  N   . ASN C 1 1325 ? 30.060   36.283  88.280  1.00 153.01 ? 1325 ASN B N   1 
ATOM   24525 C  CA  . ASN C 1 1325 ? 30.228   36.553  89.706  1.00 154.88 ? 1325 ASN B CA  1 
ATOM   24526 C  C   . ASN C 1 1325 ? 30.676   37.978  89.916  1.00 149.97 ? 1325 ASN B C   1 
ATOM   24527 O  O   . ASN C 1 1325 ? 31.753   38.366  89.478  1.00 149.35 ? 1325 ASN B O   1 
ATOM   24528 C  CB  . ASN C 1 1325 ? 31.260   35.605  90.329  1.00 162.89 ? 1325 ASN B CB  1 
ATOM   24529 C  CG  . ASN C 1 1325 ? 32.576   35.562  89.555  1.00 168.37 ? 1325 ASN B CG  1 
ATOM   24530 O  OD1 . ASN C 1 1325 ? 32.740   34.772  88.613  1.00 169.94 ? 1325 ASN B OD1 1 
ATOM   24531 N  ND2 . ASN C 1 1325 ? 33.532   36.391  89.974  1.00 169.78 ? 1325 ASN B ND2 1 
ATOM   24532 N  N   . TYR C 1 1326 ? 29.871   38.753  90.621  1.00 147.26 ? 1326 TYR B N   1 
ATOM   24533 C  CA  . TYR C 1 1326 ? 30.094   40.187  90.627  1.00 147.55 ? 1326 TYR B CA  1 
ATOM   24534 C  C   . TYR C 1 1326 ? 30.022   40.890  91.964  1.00 138.65 ? 1326 TYR B C   1 
ATOM   24535 O  O   . TYR C 1 1326 ? 29.126   40.646  92.763  1.00 135.92 ? 1326 TYR B O   1 
ATOM   24536 C  CB  . TYR C 1 1326 ? 29.074   40.851  89.729  1.00 156.90 ? 1326 TYR B CB  1 
ATOM   24537 C  CG  . TYR C 1 1326 ? 27.673   40.487  90.106  1.00 163.90 ? 1326 TYR B CG  1 
ATOM   24538 C  CD1 . TYR C 1 1326 ? 26.804   41.432  90.647  1.00 166.41 ? 1326 TYR B CD1 1 
ATOM   24539 C  CD2 . TYR C 1 1326 ? 27.219   39.186  89.926  1.00 166.90 ? 1326 TYR B CD2 1 
ATOM   24540 C  CE1 . TYR C 1 1326 ? 25.513   41.086  90.982  1.00 168.42 ? 1326 TYR B CE1 1 
ATOM   24541 C  CE2 . TYR C 1 1326 ? 25.941   38.831  90.253  1.00 168.79 ? 1326 TYR B CE2 1 
ATOM   24542 C  CZ  . TYR C 1 1326 ? 25.088   39.776  90.781  1.00 169.55 ? 1326 TYR B CZ  1 
ATOM   24543 O  OH  . TYR C 1 1326 ? 23.806   39.393  91.100  1.00 169.87 ? 1326 TYR B OH  1 
ATOM   24544 N  N   . LYS C 1 1327 ? 30.952   41.817  92.158  1.00 131.78 ? 1327 LYS B N   1 
ATOM   24545 C  CA  . LYS C 1 1327 ? 30.940   42.696  93.304  1.00 124.23 ? 1327 LYS B CA  1 
ATOM   24546 C  C   . LYS C 1 1327 ? 29.675   43.577  93.331  1.00 114.50 ? 1327 LYS B C   1 
ATOM   24547 O  O   . LYS C 1 1327 ? 29.512   44.474  92.512  1.00 112.92 ? 1327 LYS B O   1 
ATOM   24548 C  CB  . LYS C 1 1327 ? 32.228   43.531  93.348  1.00 128.42 ? 1327 LYS B CB  1 
ATOM   24549 C  CG  . LYS C 1 1327 ? 32.417   44.246  94.685  1.00 132.49 ? 1327 LYS B CG  1 
ATOM   24550 C  CD  . LYS C 1 1327 ? 33.875   44.299  95.184  1.00 136.47 ? 1327 LYS B CD  1 
ATOM   24551 C  CE  . LYS C 1 1327 ? 33.952   44.593  96.715  1.00 134.38 ? 1327 LYS B CE  1 
ATOM   24552 N  NZ  . LYS C 1 1327 ? 33.434   43.477  97.608  1.00 131.01 ? 1327 LYS B NZ  1 
ATOM   24553 N  N   . MET C 1 1328 ? 28.785   43.283  94.286  1.00 106.67 ? 1328 MET B N   1 
ATOM   24554 C  CA  . MET C 1 1328 ? 27.574   44.062  94.581  1.00 96.88  ? 1328 MET B CA  1 
ATOM   24555 C  C   . MET C 1 1328 ? 27.880   45.210  95.523  1.00 97.20  ? 1328 MET B C   1 
ATOM   24556 O  O   . MET C 1 1328 ? 28.701   45.058  96.415  1.00 97.29  ? 1328 MET B O   1 
ATOM   24557 C  CB  . MET C 1 1328 ? 26.540   43.170  95.239  1.00 87.42  ? 1328 MET B CB  1 
ATOM   24558 C  CG  . MET C 1 1328 ? 25.355   43.906  95.747  1.00 83.07  ? 1328 MET B CG  1 
ATOM   24559 S  SD  . MET C 1 1328 ? 23.947   42.796  95.762  1.00 80.98  ? 1328 MET B SD  1 
ATOM   24560 C  CE  . MET C 1 1328 ? 23.216   43.193  94.162  1.00 130.50 ? 1328 MET B CE  1 
ATOM   24561 N  N   . THR C 1 1329 ? 27.210   46.346  95.337  1.00 98.43  ? 1329 THR B N   1 
ATOM   24562 C  CA  . THR C 1 1329 ? 27.518   47.589  96.064  1.00 99.06  ? 1329 THR B CA  1 
ATOM   24563 C  C   . THR C 1 1329 ? 26.353   48.544  95.974  1.00 97.67  ? 1329 THR B C   1 
ATOM   24564 O  O   . THR C 1 1329 ? 25.407   48.282  95.258  1.00 98.09  ? 1329 THR B O   1 
ATOM   24565 C  CB  . THR C 1 1329 ? 28.728   48.301  95.475  1.00 101.56 ? 1329 THR B CB  1 
ATOM   24566 O  OG1 . THR C 1 1329 ? 28.614   48.358  94.043  1.00 103.09 ? 1329 THR B OG1 1 
ATOM   24567 C  CG2 . THR C 1 1329 ? 29.987   47.551  95.846  1.00 103.18 ? 1329 THR B CG2 1 
ATOM   24568 N  N   . ASP C 1 1330 ? 26.367   49.655  96.681  1.00 98.00  ? 1330 ASP B N   1 
ATOM   24569 C  CA  . ASP C 1 1330 ? 25.190   50.491  96.519  1.00 100.46 ? 1330 ASP B CA  1 
ATOM   24570 C  C   . ASP C 1 1330 ? 25.207   51.160  95.143  1.00 104.48 ? 1330 ASP B C   1 
ATOM   24571 O  O   . ASP C 1 1330 ? 24.266   51.853  94.773  1.00 107.13 ? 1330 ASP B O   1 
ATOM   24572 C  CB  . ASP C 1 1330 ? 25.019   51.507  97.649  1.00 102.49 ? 1330 ASP B CB  1 
ATOM   24573 C  CG  . ASP C 1 1330 ? 25.271   50.908  99.018  1.00 102.59 ? 1330 ASP B CG  1 
ATOM   24574 O  OD1 . ASP C 1 1330 ? 24.503   50.012  99.488  1.00 98.64  ? 1330 ASP B OD1 1 
ATOM   24575 O  OD2 . ASP C 1 1330 ? 26.256   51.381  99.623  1.00 105.35 ? 1330 ASP B OD2 1 
ATOM   24576 N  N   . LYS C 1 1331 ? 26.274   50.952  94.380  1.00 105.27 ? 1331 LYS B N   1 
ATOM   24577 C  CA  . LYS C 1 1331 ? 26.366   51.545  93.054  1.00 106.50 ? 1331 LYS B CA  1 
ATOM   24578 C  C   . LYS C 1 1331 ? 25.373   50.868  92.117  1.00 106.52 ? 1331 LYS B C   1 
ATOM   24579 O  O   . LYS C 1 1331 ? 24.362   51.463  91.730  1.00 106.68 ? 1331 LYS B O   1 
ATOM   24580 C  CB  . LYS C 1 1331 ? 27.790   51.405  92.552  1.00 107.53 ? 1331 LYS B CB  1 
ATOM   24581 C  CG  . LYS C 1 1331 ? 28.763   52.025  93.518  1.00 107.06 ? 1331 LYS B CG  1 
ATOM   24582 C  CD  . LYS C 1 1331 ? 28.277   53.421  93.865  1.00 107.74 ? 1331 LYS B CD  1 
ATOM   24583 C  CE  . LYS C 1 1331 ? 29.354   54.228  94.566  1.00 110.37 ? 1331 LYS B CE  1 
ATOM   24584 N  NZ  . LYS C 1 1331 ? 29.483   55.592  93.983  1.00 111.97 ? 1331 LYS B NZ  1 
ATOM   24585 N  N   . ASN C 1 1332 ? 25.674   49.619  91.770  1.00 105.78 ? 1332 ASN B N   1 
ATOM   24586 C  CA  . ASN C 1 1332 ? 24.715   48.714  91.157  1.00 107.80 ? 1332 ASN B CA  1 
ATOM   24587 C  C   . ASN C 1 1332 ? 24.225   47.706  92.168  1.00 109.25 ? 1332 ASN B C   1 
ATOM   24588 O  O   . ASN C 1 1332 ? 25.030   47.019  92.788  1.00 109.92 ? 1332 ASN B O   1 
ATOM   24589 C  CB  . ASN C 1 1332 ? 25.416   47.879  90.104  1.00 110.43 ? 1332 ASN B CB  1 
ATOM   24590 C  CG  . ASN C 1 1332 ? 26.110   46.654  90.705  1.00 110.56 ? 1332 ASN B CG  1 
ATOM   24591 O  OD1 . ASN C 1 1332 ? 27.040   46.795  91.512  1.00 108.67 ? 1332 ASN B OD1 1 
ATOM   24592 N  ND2 . ASN C 1 1332 ? 25.643   45.449  90.333  1.00 110.73 ? 1332 ASN B ND2 1 
ATOM   24593 N  N   . PHE C 1 1333 ? 22.922   47.557  92.338  1.00 108.75 ? 1333 PHE B N   1 
ATOM   24594 C  CA  . PHE C 1 1333 ? 22.464   46.355  93.027  1.00 105.96 ? 1333 PHE B CA  1 
ATOM   24595 C  C   . PHE C 1 1333 ? 21.379   45.751  92.199  1.00 109.91 ? 1333 PHE B C   1 
ATOM   24596 O  O   . PHE C 1 1333 ? 21.181   44.543  92.242  1.00 112.84 ? 1333 PHE B O   1 
ATOM   24597 C  CB  . PHE C 1 1333 ? 22.027   46.557  94.492  1.00 95.59  ? 1333 PHE B CB  1 
ATOM   24598 C  CG  . PHE C 1 1333 ? 21.224   47.812  94.752  1.00 89.50  ? 1333 PHE B CG  1 
ATOM   24599 C  CD1 . PHE C 1 1333 ? 19.869   47.748  94.972  1.00 84.59  ? 1333 PHE B CD1 1 
ATOM   24600 C  CD2 . PHE C 1 1333 ? 21.835   49.054  94.830  1.00 89.83  ? 1333 PHE B CD2 1 
ATOM   24601 C  CE1 . PHE C 1 1333 ? 19.142   48.908  95.230  1.00 85.18  ? 1333 PHE B CE1 1 
ATOM   24602 C  CE2 . PHE C 1 1333 ? 21.096   50.208  95.084  1.00 83.70  ? 1333 PHE B CE2 1 
ATOM   24603 C  CZ  . PHE C 1 1333 ? 19.762   50.131  95.281  1.00 83.20  ? 1333 PHE B CZ  1 
ATOM   24604 N  N   . LEU C 1 1334 ? 20.704   46.588  91.411  1.00 108.35 ? 1334 LEU B N   1 
ATOM   24605 C  CA  . LEU C 1 1334 ? 19.614   46.097  90.587  1.00 104.08 ? 1334 LEU B CA  1 
ATOM   24606 C  C   . LEU C 1 1334 ? 20.175   45.692  89.241  1.00 109.48 ? 1334 LEU B C   1 
ATOM   24607 O  O   . LEU C 1 1334 ? 19.643   46.048  88.192  1.00 113.35 ? 1334 LEU B O   1 
ATOM   24608 C  CB  . LEU C 1 1334 ? 18.478   47.105  90.416  1.00 95.38  ? 1334 LEU B CB  1 
ATOM   24609 C  CG  . LEU C 1 1334 ? 18.325   48.394  91.221  1.00 88.31  ? 1334 LEU B CG  1 
ATOM   24610 C  CD1 . LEU C 1 1334 ? 17.457   48.191  92.437  1.00 85.19  ? 1334 LEU B CD1 1 
ATOM   24611 C  CD2 . LEU C 1 1334 ? 19.691   49.028  91.542  1.00 87.92  ? 1334 LEU B CD2 1 
ATOM   24612 N  N   . GLY C 1 1335 ? 21.265   44.940  89.290  1.00 114.48 ? 1335 GLY B N   1 
ATOM   24613 C  CA  . GLY C 1 1335 ? 21.794   44.261  88.120  1.00 120.88 ? 1335 GLY B CA  1 
ATOM   24614 C  C   . GLY C 1 1335 ? 20.860   43.481  87.183  1.00 127.52 ? 1335 GLY B C   1 
ATOM   24615 O  O   . GLY C 1 1335 ? 19.645   43.375  87.370  1.00 126.98 ? 1335 GLY B O   1 
ATOM   24616 N  N   . ARG C 1 1336 ? 21.474   42.948  86.137  1.00 132.08 ? 1336 ARG B N   1 
ATOM   24617 C  CA  . ARG C 1 1336 ? 20.801   42.224  85.088  1.00 138.75 ? 1336 ARG B CA  1 
ATOM   24618 C  C   . ARG C 1 1336 ? 20.264   40.943  85.678  1.00 130.57 ? 1336 ARG B C   1 
ATOM   24619 O  O   . ARG C 1 1336 ? 20.821   40.465  86.676  1.00 129.31 ? 1336 ARG B O   1 
ATOM   24620 C  CB  . ARG C 1 1336 ? 21.877   41.857  84.088  1.00 153.66 ? 1336 ARG B CB  1 
ATOM   24621 C  CG  . ARG C 1 1336 ? 23.182   41.508  84.807  1.00 164.72 ? 1336 ARG B CG  1 
ATOM   24622 C  CD  . ARG C 1 1336 ? 24.055   40.571  84.006  1.00 175.42 ? 1336 ARG B CD  1 
ATOM   24623 N  NE  . ARG C 1 1336 ? 25.189   40.107  84.797  1.00 183.73 ? 1336 ARG B NE  1 
ATOM   24624 C  CZ  . ARG C 1 1336 ? 26.301   39.612  84.267  1.00 191.08 ? 1336 ARG B CZ  1 
ATOM   24625 N  NH1 . ARG C 1 1336 ? 26.419   39.525  82.945  1.00 194.13 ? 1336 ARG B NH1 1 
ATOM   24626 N  NH2 . ARG C 1 1336 ? 27.296   39.213  85.054  1.00 192.93 ? 1336 ARG B NH2 1 
ATOM   24627 N  N   . PRO C 1 1337 ? 19.170   40.397  85.103  1.00 122.25 ? 1337 PRO B N   1 
ATOM   24628 C  CA  . PRO C 1 1337 ? 18.865   38.983  85.353  1.00 116.13 ? 1337 PRO B CA  1 
ATOM   24629 C  C   . PRO C 1 1337 ? 19.799   38.140  84.527  1.00 110.52 ? 1337 PRO B C   1 
ATOM   24630 O  O   . PRO C 1 1337 ? 20.678   38.698  83.894  1.00 109.98 ? 1337 PRO B O   1 
ATOM   24631 C  CB  . PRO C 1 1337 ? 17.424   38.839  84.886  1.00 116.35 ? 1337 PRO B CB  1 
ATOM   24632 C  CG  . PRO C 1 1337 ? 16.867   40.202  85.007  1.00 119.76 ? 1337 PRO B CG  1 
ATOM   24633 C  CD  . PRO C 1 1337 ? 17.991   41.124  84.612  1.00 122.10 ? 1337 PRO B CD  1 
ATOM   24634 N  N   . VAL C 1 1338 ? 19.634   36.828  84.553  1.00 111.33 ? 1338 VAL B N   1 
ATOM   24635 C  CA  . VAL C 1 1338 ? 20.553   35.920  83.860  1.00 116.04 ? 1338 VAL B CA  1 
ATOM   24636 C  C   . VAL C 1 1338 ? 19.859   34.588  83.633  1.00 122.85 ? 1338 VAL B C   1 
ATOM   24637 O  O   . VAL C 1 1338 ? 19.420   33.954  84.595  1.00 124.71 ? 1338 VAL B O   1 
ATOM   24638 C  CB  . VAL C 1 1338 ? 21.876   35.690  84.666  1.00 156.88 ? 1338 VAL B CB  1 
ATOM   24639 C  CG1 . VAL C 1 1338 ? 22.288   34.217  84.702  1.00 156.23 ? 1338 VAL B CG1 1 
ATOM   24640 C  CG2 . VAL C 1 1338 ? 23.004   36.536  84.107  1.00 158.16 ? 1338 VAL B CG2 1 
ATOM   24641 N  N   . GLU C 1 1339 ? 19.732   34.162  82.378  1.00 127.20 ? 1339 GLU B N   1 
ATOM   24642 C  CA  . GLU C 1 1339 ? 19.109   32.872  82.117  1.00 131.28 ? 1339 GLU B CA  1 
ATOM   24643 C  C   . GLU C 1 1339 ? 20.154   31.820  82.261  1.00 130.95 ? 1339 GLU B C   1 
ATOM   24644 O  O   . GLU C 1 1339 ? 21.205   31.887  81.635  1.00 129.40 ? 1339 GLU B O   1 
ATOM   24645 C  CB  . GLU C 1 1339 ? 18.472   32.812  80.742  1.00 139.00 ? 1339 GLU B CB  1 
ATOM   24646 C  CG  . GLU C 1 1339 ? 17.006   33.189  80.790  1.00 144.89 ? 1339 GLU B CG  1 
ATOM   24647 C  CD  . GLU C 1 1339 ? 16.437   33.564  79.431  1.00 150.14 ? 1339 GLU B CD  1 
ATOM   24648 O  OE1 . GLU C 1 1339 ? 16.404   32.667  78.558  1.00 152.71 ? 1339 GLU B OE1 1 
ATOM   24649 O  OE2 . GLU C 1 1339 ? 16.016   34.741  79.248  1.00 150.78 ? 1339 GLU B OE2 1 
ATOM   24650 N  N   . VAL C 1 1340 ? 19.883   30.868  83.132  1.00 132.23 ? 1340 VAL B N   1 
ATOM   24651 C  CA  . VAL C 1 1340 ? 20.877   29.883  83.458  1.00 135.25 ? 1340 VAL B CA  1 
ATOM   24652 C  C   . VAL C 1 1340 ? 20.755   28.882  82.373  1.00 137.10 ? 1340 VAL B C   1 
ATOM   24653 O  O   . VAL C 1 1340 ? 19.729   28.216  82.275  1.00 139.65 ? 1340 VAL B O   1 
ATOM   24654 C  CB  . VAL C 1 1340 ? 20.580   29.218  84.798  1.00 136.11 ? 1340 VAL B CB  1 
ATOM   24655 C  CG1 . VAL C 1 1340 ? 21.370   27.930  84.930  1.00 137.71 ? 1340 VAL B CG1 1 
ATOM   24656 C  CG2 . VAL C 1 1340 ? 20.904   30.177  85.938  1.00 135.42 ? 1340 VAL B CG2 1 
ATOM   24657 N  N   . LEU C 1 1341 ? 21.777   28.793  81.531  1.00 137.41 ? 1341 LEU B N   1 
ATOM   24658 C  CA  . LEU C 1 1341 ? 21.661   27.948  80.349  1.00 141.01 ? 1341 LEU B CA  1 
ATOM   24659 C  C   . LEU C 1 1341 ? 21.897   26.479  80.692  1.00 144.46 ? 1341 LEU B C   1 
ATOM   24660 O  O   . LEU C 1 1341 ? 21.013   25.616  80.543  1.00 145.04 ? 1341 LEU B O   1 
ATOM   24661 C  CB  . LEU C 1 1341 ? 22.616   28.396  79.218  1.00 139.87 ? 1341 LEU B CB  1 
ATOM   24662 C  CG  . LEU C 1 1341 ? 22.210   29.268  78.003  1.00 158.76 ? 1341 LEU B CG  1 
ATOM   24663 C  CD1 . LEU C 1 1341 ? 20.788   28.974  77.481  1.00 158.77 ? 1341 LEU B CD1 1 
ATOM   24664 C  CD2 . LEU C 1 1341 ? 22.416   30.776  78.245  1.00 157.83 ? 1341 LEU B CD2 1 
ATOM   24665 N  N   . LEU C 1 1342 ? 23.092   26.199  81.177  1.00 147.39 ? 1342 LEU B N   1 
ATOM   24666 C  CA  . LEU C 1 1342 ? 23.577   24.839  81.128  1.00 148.05 ? 1342 LEU B CA  1 
ATOM   24667 C  C   . LEU C 1 1342 ? 22.786   23.867  82.001  1.00 147.04 ? 1342 LEU B C   1 
ATOM   24668 O  O   . LEU C 1 1342 ? 21.995   24.257  82.861  1.00 145.00 ? 1342 LEU B O   1 
ATOM   24669 C  CB  . LEU C 1 1342 ? 25.081   24.822  81.388  1.00 146.96 ? 1342 LEU B CB  1 
ATOM   24670 C  CG  . LEU C 1 1342 ? 25.705   26.137  80.868  1.00 144.44 ? 1342 LEU B CG  1 
ATOM   24671 C  CD1 . LEU C 1 1342 ? 27.213   26.211  81.078  1.00 143.95 ? 1342 LEU B CD1 1 
ATOM   24672 C  CD2 . LEU C 1 1342 ? 25.367   26.422  79.401  1.00 143.92 ? 1342 LEU B CD2 1 
ATOM   24673 N  N   . ASN C 1 1343 ? 22.972   22.590  81.706  1.00 149.36 ? 1343 ASN B N   1 
ATOM   24674 C  CA  . ASN C 1 1343 ? 22.306   21.513  82.425  1.00 154.14 ? 1343 ASN B CA  1 
ATOM   24675 C  C   . ASN C 1 1343 ? 23.122   21.062  83.641  1.00 153.52 ? 1343 ASN B C   1 
ATOM   24676 O  O   . ASN C 1 1343 ? 23.812   20.037  83.595  1.00 153.71 ? 1343 ASN B O   1 
ATOM   24677 C  CB  . ASN C 1 1343 ? 22.016   20.326  81.484  1.00 162.56 ? 1343 ASN B CB  1 
ATOM   24678 C  CG  . ASN C 1 1343 ? 20.869   20.615  80.496  1.00 170.95 ? 1343 ASN B CG  1 
ATOM   24679 O  OD1 . ASN C 1 1343 ? 19.958   19.798  80.327  1.00 174.43 ? 1343 ASN B OD1 1 
ATOM   24680 N  ND2 . ASN C 1 1343 ? 20.900   21.793  79.868  1.00 173.65 ? 1343 ASN B ND2 1 
ATOM   24681 N  N   . ASP C 1 1344 ? 23.029   21.823  84.730  1.00 151.58 ? 1344 ASP B N   1 
ATOM   24682 C  CA  . ASP C 1 1344 ? 23.851   21.585  85.912  1.00 147.82 ? 1344 ASP B CA  1 
ATOM   24683 C  C   . ASP C 1 1344 ? 23.138   22.172  87.120  1.00 145.53 ? 1344 ASP B C   1 
ATOM   24684 O  O   . ASP C 1 1344 ? 22.233   22.988  86.978  1.00 147.32 ? 1344 ASP B O   1 
ATOM   24685 C  CB  . ASP C 1 1344 ? 25.212   22.260  85.733  1.00 142.36 ? 1344 ASP B CB  1 
ATOM   24686 C  CG  . ASP C 1 1344 ? 26.330   21.500  86.394  1.00 135.77 ? 1344 ASP B CG  1 
ATOM   24687 O  OD1 . ASP C 1 1344 ? 26.030   20.653  87.254  1.00 133.79 ? 1344 ASP B OD1 1 
ATOM   24688 O  OD2 . ASP C 1 1344 ? 27.505   21.750  86.052  1.00 132.85 ? 1344 ASP B OD2 1 
ATOM   24689 N  N   . ASP C 1 1345 ? 23.523   21.754  88.314  1.00 142.20 ? 1345 ASP B N   1 
ATOM   24690 C  CA  . ASP C 1 1345 ? 23.000   22.402  89.503  1.00 138.72 ? 1345 ASP B CA  1 
ATOM   24691 C  C   . ASP C 1 1345 ? 23.667   23.805  89.617  1.00 110.04 ? 1345 ASP B C   1 
ATOM   24692 O  O   . ASP C 1 1345 ? 24.885   23.947  89.444  1.00 110.92 ? 1345 ASP B O   1 
ATOM   24693 C  CB  . ASP C 1 1345 ? 23.249   21.534  90.752  1.00 137.81 ? 1345 ASP B CB  1 
ATOM   24694 C  CG  . ASP C 1 1345 ? 22.938   20.029  90.525  1.00 146.02 ? 1345 ASP B CG  1 
ATOM   24695 O  OD1 . ASP C 1 1345 ? 22.595   19.333  91.512  1.00 146.58 ? 1345 ASP B OD1 1 
ATOM   24696 O  OD2 . ASP C 1 1345 ? 23.053   19.520  89.382  1.00 147.19 ? 1345 ASP B OD2 1 
ATOM   24697 N  N   . LEU C 1 1346 ? 22.878   24.847  89.877  1.00 107.39 ? 1346 LEU B N   1 
ATOM   24698 C  CA  . LEU C 1 1346 ? 23.416   26.201  90.042  1.00 103.54 ? 1346 LEU B CA  1 
ATOM   24699 C  C   . LEU C 1 1346 ? 23.805   26.504  91.495  1.00 105.07 ? 1346 LEU B C   1 
ATOM   24700 O  O   . LEU C 1 1346 ? 23.277   25.867  92.404  1.00 107.93 ? 1346 LEU B O   1 
ATOM   24701 C  CB  . LEU C 1 1346 ? 22.377   27.215  89.611  1.00 98.63  ? 1346 LEU B CB  1 
ATOM   24702 C  CG  . LEU C 1 1346 ? 23.019   28.582  89.522  1.00 96.17  ? 1346 LEU B CG  1 
ATOM   24703 C  CD1 . LEU C 1 1346 ? 24.143   28.521  88.515  1.00 96.98  ? 1346 LEU B CD1 1 
ATOM   24704 C  CD2 . LEU C 1 1346 ? 22.002   29.595  89.127  1.00 95.38  ? 1346 LEU B CD2 1 
ATOM   24705 N  N   . ILE C 1 1347 ? 24.708   27.473  91.720  1.00 101.64 ? 1347 ILE B N   1 
ATOM   24706 C  CA  . ILE C 1 1347 ? 25.060   27.934  93.085  1.00 94.61  ? 1347 ILE B CA  1 
ATOM   24707 C  C   . ILE C 1 1347 ? 25.443   29.409  93.293  1.00 88.23  ? 1347 ILE B C   1 
ATOM   24708 O  O   . ILE C 1 1347 ? 26.614   29.767  93.136  1.00 87.00  ? 1347 ILE B O   1 
ATOM   24709 C  CB  . ILE C 1 1347 ? 26.261   27.201  93.688  1.00 94.91  ? 1347 ILE B CB  1 
ATOM   24710 C  CG1 . ILE C 1 1347 ? 26.445   25.804  93.129  1.00 96.09  ? 1347 ILE B CG1 1 
ATOM   24711 C  CG2 . ILE C 1 1347 ? 26.124   27.162  95.198  1.00 94.45  ? 1347 ILE B CG2 1 
ATOM   24712 C  CD1 . ILE C 1 1347 ? 27.644   25.118  93.758  1.00 98.27  ? 1347 ILE B CD1 1 
ATOM   24713 N  N   . VAL C 1 1348 ? 24.477   30.229  93.708  1.00 84.33  ? 1348 VAL B N   1 
ATOM   24714 C  CA  . VAL C 1 1348 ? 24.732   31.573  94.229  1.00 83.89  ? 1348 VAL B CA  1 
ATOM   24715 C  C   . VAL C 1 1348 ? 25.545   31.460  95.549  1.00 93.35  ? 1348 VAL B C   1 
ATOM   24716 O  O   . VAL C 1 1348 ? 25.309   30.532  96.306  1.00 95.06  ? 1348 VAL B O   1 
ATOM   24717 C  CB  . VAL C 1 1348 ? 23.377   32.274  94.481  1.00 80.80  ? 1348 VAL B CB  1 
ATOM   24718 C  CG1 . VAL C 1 1348 ? 23.560   33.770  94.735  1.00 80.25  ? 1348 VAL B CG1 1 
ATOM   24719 C  CG2 . VAL C 1 1348 ? 22.459   32.044  93.320  1.00 80.75  ? 1348 VAL B CG2 1 
ATOM   24720 N  N   . SER C 1 1349 ? 26.482   32.372  95.836  1.00 92.09  ? 1349 SER B N   1 
ATOM   24721 C  CA  . SER C 1 1349 ? 27.376   32.183  96.991  1.00 92.60  ? 1349 SER B CA  1 
ATOM   24722 C  C   . SER C 1 1349 ? 28.340   33.317  97.372  1.00 96.82  ? 1349 SER B C   1 
ATOM   24723 O  O   . SER C 1 1349 ? 29.570   33.150  97.321  1.00 97.31  ? 1349 SER B O   1 
ATOM   24724 C  CB  . SER C 1 1349 ? 28.190   30.920  96.823  1.00 90.71  ? 1349 SER B CB  1 
ATOM   24725 O  OG  . SER C 1 1349 ? 28.783   30.882  95.552  1.00 90.94  ? 1349 SER B OG  1 
ATOM   24726 N  N   . THR C 1 1350 ? 27.758   34.447  97.784  1.00 100.80 ? 1350 THR B N   1 
ATOM   24727 C  CA  . THR C 1 1350 ? 28.475   35.601  98.349  1.00 102.13 ? 1350 THR B CA  1 
ATOM   24728 C  C   . THR C 1 1350 ? 29.593   35.315  99.362  1.00 99.47  ? 1350 THR B C   1 
ATOM   24729 O  O   . THR C 1 1350 ? 29.495   34.429  100.223 1.00 96.21  ? 1350 THR B O   1 
ATOM   24730 C  CB  . THR C 1 1350 ? 27.507   36.579  99.056  1.00 109.19 ? 1350 THR B CB  1 
ATOM   24731 O  OG1 . THR C 1 1350 ? 28.177   37.824  99.285  1.00 112.10 ? 1350 THR B OG1 1 
ATOM   24732 C  CG2 . THR C 1 1350 ? 27.062   36.026  100.414 1.00 108.35 ? 1350 THR B CG2 1 
ATOM   24733 N  N   . GLY C 1 1351 ? 30.629   36.142  99.274  1.00 99.71  ? 1351 GLY B N   1 
ATOM   24734 C  CA  . GLY C 1 1351 ? 31.754   36.094  100.189 1.00 98.52  ? 1351 GLY B CA  1 
ATOM   24735 C  C   . GLY C 1 1351 ? 31.364   36.507  101.588 1.00 96.03  ? 1351 GLY B C   1 
ATOM   24736 O  O   . GLY C 1 1351 ? 30.211   36.330  101.985 1.00 92.29  ? 1351 GLY B O   1 
ATOM   24737 N  N   . PHE C 1 1352 ? 32.318   37.033  102.354 1.00 95.78  ? 1352 PHE B N   1 
ATOM   24738 C  CA  . PHE C 1 1352 ? 31.938   37.599  103.633 1.00 93.32  ? 1352 PHE B CA  1 
ATOM   24739 C  C   . PHE C 1 1352 ? 31.064   38.841  103.380 1.00 92.85  ? 1352 PHE B C   1 
ATOM   24740 O  O   . PHE C 1 1352 ? 29.877   38.684  103.121 1.00 92.99  ? 1352 PHE B O   1 
ATOM   24741 C  CB  . PHE C 1 1352 ? 33.115   37.835  104.595 1.00 92.14  ? 1352 PHE B CB  1 
ATOM   24742 C  CG  . PHE C 1 1352 ? 32.708   38.566  105.854 1.00 90.10  ? 1352 PHE B CG  1 
ATOM   24743 C  CD1 . PHE C 1 1352 ? 31.540   38.226  106.519 1.00 87.19  ? 1352 PHE B CD1 1 
ATOM   24744 C  CD2 . PHE C 1 1352 ? 33.464   39.600  106.355 1.00 89.81  ? 1352 PHE B CD2 1 
ATOM   24745 C  CE1 . PHE C 1 1352 ? 31.137   38.903  107.643 1.00 84.52  ? 1352 PHE B CE1 1 
ATOM   24746 C  CE2 . PHE C 1 1352 ? 33.069   40.278  107.484 1.00 86.96  ? 1352 PHE B CE2 1 
ATOM   24747 C  CZ  . PHE C 1 1352 ? 31.905   39.930  108.123 1.00 84.88  ? 1352 PHE B CZ  1 
ATOM   24748 N  N   . GLY C 1 1353 ? 31.623   40.049  103.431 1.00 90.61  ? 1353 GLY B N   1 
ATOM   24749 C  CA  . GLY C 1 1353 ? 30.875   41.255  103.083 1.00 91.25  ? 1353 GLY B CA  1 
ATOM   24750 C  C   . GLY C 1 1353 ? 29.725   41.673  103.993 1.00 89.68  ? 1353 GLY B C   1 
ATOM   24751 O  O   . GLY C 1 1353 ? 29.756   41.382  105.176 1.00 89.16  ? 1353 GLY B O   1 
ATOM   24752 N  N   . SER C 1 1354 ? 28.705   42.332  103.426 1.00 90.71  ? 1354 SER B N   1 
ATOM   24753 C  CA  . SER C 1 1354 ? 27.671   43.026  104.194 1.00 88.84  ? 1354 SER B CA  1 
ATOM   24754 C  C   . SER C 1 1354 ? 26.475   43.495  103.357 1.00 86.51  ? 1354 SER B C   1 
ATOM   24755 O  O   . SER C 1 1354 ? 26.613   43.762  102.162 1.00 86.84  ? 1354 SER B O   1 
ATOM   24756 C  CB  . SER C 1 1354 ? 28.296   44.260  104.813 1.00 90.62  ? 1354 SER B CB  1 
ATOM   24757 O  OG  . SER C 1 1354 ? 28.084   45.391  103.983 1.00 91.65  ? 1354 SER B OG  1 
ATOM   24758 N  N   . GLY C 1 1355 ? 25.316   43.647  104.001 1.00 87.15  ? 1355 GLY B N   1 
ATOM   24759 C  CA  . GLY C 1 1355 ? 24.093   44.062  103.312 1.00 88.05  ? 1355 GLY B CA  1 
ATOM   24760 C  C   . GLY C 1 1355 ? 23.093   42.921  103.126 1.00 88.78  ? 1355 GLY B C   1 
ATOM   24761 O  O   . GLY C 1 1355 ? 23.208   41.857  103.763 1.00 93.92  ? 1355 GLY B O   1 
ATOM   24762 N  N   . LEU C 1 1356 ? 22.122   43.113  102.241 1.00 82.34  ? 1356 LEU B N   1 
ATOM   24763 C  CA  . LEU C 1 1356 ? 21.123   42.077  102.026 1.00 85.88  ? 1356 LEU B CA  1 
ATOM   24764 C  C   . LEU C 1 1356 ? 20.721   41.919  100.554 1.00 91.16  ? 1356 LEU B C   1 
ATOM   24765 O  O   . LEU C 1 1356 ? 20.055   42.788  99.985  1.00 98.97  ? 1356 LEU B O   1 
ATOM   24766 C  CB  . LEU C 1 1356 ? 19.893   42.421  102.840 1.00 81.93  ? 1356 LEU B CB  1 
ATOM   24767 C  CG  . LEU C 1 1356 ? 19.809   41.776  104.203 1.00 79.02  ? 1356 LEU B CG  1 
ATOM   24768 C  CD1 . LEU C 1 1356 ? 18.832   42.513  105.074 1.00 75.73  ? 1356 LEU B CD1 1 
ATOM   24769 C  CD2 . LEU C 1 1356 ? 19.343   40.397  103.944 1.00 77.19  ? 1356 LEU B CD2 1 
ATOM   24770 N  N   . ALA C 1 1357 ? 21.112   40.814  99.923  1.00 89.70  ? 1357 ALA B N   1 
ATOM   24771 C  CA  . ALA C 1 1357 ? 20.798   40.616  98.497  1.00 83.23  ? 1357 ALA B CA  1 
ATOM   24772 C  C   . ALA C 1 1357 ? 19.789   39.493  98.288  1.00 79.15  ? 1357 ALA B C   1 
ATOM   24773 O  O   . ALA C 1 1357 ? 20.019   38.376  98.729  1.00 77.50  ? 1357 ALA B O   1 
ATOM   24774 C  CB  . ALA C 1 1357 ? 22.070   40.364  97.683  1.00 78.88  ? 1357 ALA B CB  1 
ATOM   24775 N  N   . THR C 1 1358 ? 18.676   39.801  97.626  1.00 77.93  ? 1358 THR B N   1 
ATOM   24776 C  CA  . THR C 1 1358 ? 17.656   38.805  97.326  1.00 77.88  ? 1358 THR B CA  1 
ATOM   24777 C  C   . THR C 1 1358 ? 17.890   38.018  96.021  1.00 78.46  ? 1358 THR B C   1 
ATOM   24778 O  O   . THR C 1 1358 ? 17.724   38.546  94.911  1.00 79.08  ? 1358 THR B O   1 
ATOM   24779 C  CB  . THR C 1 1358 ? 16.182   39.394  97.349  1.00 94.79  ? 1358 THR B CB  1 
ATOM   24780 O  OG1 . THR C 1 1358 ? 16.046   40.594  96.556  1.00 94.09  ? 1358 THR B OG1 1 
ATOM   24781 C  CG2 . THR C 1 1358 ? 15.731   39.649  98.781  1.00 93.27  ? 1358 THR B CG2 1 
ATOM   24782 N  N   . VAL C 1 1359 ? 18.257   36.748  96.175  1.00 78.34  ? 1359 VAL B N   1 
ATOM   24783 C  CA  . VAL C 1 1359 ? 18.244   35.781  95.081  1.00 78.89  ? 1359 VAL B CA  1 
ATOM   24784 C  C   . VAL C 1 1359 ? 16.845   35.171  94.838  1.00 86.21  ? 1359 VAL B C   1 
ATOM   24785 O  O   . VAL C 1 1359 ? 16.317   34.467  95.697  1.00 84.37  ? 1359 VAL B O   1 
ATOM   24786 C  CB  . VAL C 1 1359 ? 19.190   34.601  95.387  1.00 78.84  ? 1359 VAL B CB  1 
ATOM   24787 C  CG1 . VAL C 1 1359 ? 19.148   33.609  94.255  1.00 79.49  ? 1359 VAL B CG1 1 
ATOM   24788 C  CG2 . VAL C 1 1359 ? 20.599   35.075  95.620  1.00 78.91  ? 1359 VAL B CG2 1 
ATOM   24789 N  N   . HIS C 1 1360 ? 16.238   35.454  93.686  1.00 85.58  ? 1360 HIS B N   1 
ATOM   24790 C  CA  . HIS C 1 1360 ? 15.119   34.639  93.186  1.00 88.45  ? 1360 HIS B CA  1 
ATOM   24791 C  C   . HIS C 1 1360 ? 15.507   33.927  91.919  1.00 88.87  ? 1360 HIS B C   1 
ATOM   24792 O  O   . HIS C 1 1360 ? 16.338   34.430  91.151  1.00 91.43  ? 1360 HIS B O   1 
ATOM   24793 C  CB  . HIS C 1 1360 ? 13.903   35.463  92.839  1.00 91.70  ? 1360 HIS B CB  1 
ATOM   24794 C  CG  . HIS C 1 1360 ? 13.265   36.098  94.015  1.00 91.96  ? 1360 HIS B CG  1 
ATOM   24795 N  ND1 . HIS C 1 1360 ? 13.826   37.180  94.658  1.00 90.58  ? 1360 HIS B ND1 1 
ATOM   24796 C  CD2 . HIS C 1 1360 ? 12.106   35.822  94.654  1.00 92.46  ? 1360 HIS B CD2 1 
ATOM   24797 C  CE1 . HIS C 1 1360 ? 13.039   37.541  95.654  1.00 91.30  ? 1360 HIS B CE1 1 
ATOM   24798 N  NE2 . HIS C 1 1360 ? 11.992   36.732  95.676  1.00 92.66  ? 1360 HIS B NE2 1 
ATOM   24799 N  N   . VAL C 1 1361 ? 14.855   32.799  91.656  1.00 86.26  ? 1361 VAL B N   1 
ATOM   24800 C  CA  . VAL C 1 1361 ? 15.249   31.988  90.519  1.00 87.91  ? 1361 VAL B CA  1 
ATOM   24801 C  C   . VAL C 1 1361 ? 14.048   31.277  89.937  1.00 89.41  ? 1361 VAL B C   1 
ATOM   24802 O  O   . VAL C 1 1361 ? 13.713   30.156  90.303  1.00 91.21  ? 1361 VAL B O   1 
ATOM   24803 C  CB  . VAL C 1 1361 ? 16.393   31.024  90.892  1.00 81.94  ? 1361 VAL B CB  1 
ATOM   24804 C  CG1 . VAL C 1 1361 ? 16.095   29.640  90.460  1.00 82.60  ? 1361 VAL B CG1 1 
ATOM   24805 C  CG2 . VAL C 1 1361 ? 17.672   31.474  90.270  1.00 82.07  ? 1361 VAL B CG2 1 
ATOM   24806 N  N   . THR C 1 1362 ? 13.397   31.963  89.012  1.00 90.01  ? 1362 THR B N   1 
ATOM   24807 C  CA  . THR C 1 1362 ? 12.062   31.584  88.585  1.00 90.80  ? 1362 THR B CA  1 
ATOM   24808 C  C   . THR C 1 1362 ? 12.128   30.707  87.338  1.00 88.56  ? 1362 THR B C   1 
ATOM   24809 O  O   . THR C 1 1362 ? 12.531   31.154  86.269  1.00 87.72  ? 1362 THR B O   1 
ATOM   24810 C  CB  . THR C 1 1362 ? 11.177   32.843  88.473  1.00 92.31  ? 1362 THR B CB  1 
ATOM   24811 O  OG1 . THR C 1 1362 ? 9.812    32.482  88.240  1.00 93.41  ? 1362 THR B OG1 1 
ATOM   24812 C  CG2 . THR C 1 1362 ? 11.699   33.761  87.402  1.00 94.32  ? 1362 THR B CG2 1 
ATOM   24813 N  N   . THR C 1 1363 ? 11.773   29.436  87.527  1.00 91.27  ? 1363 THR B N   1 
ATOM   24814 C  CA  . THR C 1 1363 ? 12.063   28.365  86.563  1.00 97.08  ? 1363 THR B CA  1 
ATOM   24815 C  C   . THR C 1 1363 ? 10.829   27.848  85.805  1.00 104.72 ? 1363 THR B C   1 
ATOM   24816 O  O   . THR C 1 1363 ? 9.927    27.244  86.401  1.00 105.98 ? 1363 THR B O   1 
ATOM   24817 C  CB  . THR C 1 1363 ? 12.803   27.146  87.221  1.00 154.43 ? 1363 THR B CB  1 
ATOM   24818 O  OG1 . THR C 1 1363 ? 11.935   26.016  87.297  1.00 154.63 ? 1363 THR B OG1 1 
ATOM   24819 C  CG2 . THR C 1 1363 ? 13.302   27.471  88.610  1.00 153.49 ? 1363 THR B CG2 1 
ATOM   24820 N  N   . VAL C 1 1364 ? 10.820   28.064  84.487  1.00 107.17 ? 1364 VAL B N   1 
ATOM   24821 C  CA  . VAL C 1 1364 ? 9.716    27.688  83.613  1.00 106.71 ? 1364 VAL B CA  1 
ATOM   24822 C  C   . VAL C 1 1364 ? 9.892    26.346  82.941  1.00 110.73 ? 1364 VAL B C   1 
ATOM   24823 O  O   . VAL C 1 1364 ? 10.975   25.995  82.472  1.00 112.91 ? 1364 VAL B O   1 
ATOM   24824 C  CB  . VAL C 1 1364 ? 9.609    28.660  82.503  1.00 103.68 ? 1364 VAL B CB  1 
ATOM   24825 C  CG1 . VAL C 1 1364 ? 8.942    27.995  81.314  1.00 106.12 ? 1364 VAL B CG1 1 
ATOM   24826 C  CG2 . VAL C 1 1364 ? 8.850    29.853  82.988  1.00 102.23 ? 1364 VAL B CG2 1 
ATOM   24827 N  N   . VAL C 1 1365 ? 8.819    25.591  82.858  1.00 112.31 ? 1365 VAL B N   1 
ATOM   24828 C  CA  . VAL C 1 1365 ? 8.943    24.336  82.170  1.00 114.47 ? 1365 VAL B CA  1 
ATOM   24829 C  C   . VAL C 1 1365 ? 7.603    23.981  81.521  1.00 123.02 ? 1365 VAL B C   1 
ATOM   24830 O  O   . VAL C 1 1365 ? 6.565    24.491  81.946  1.00 126.14 ? 1365 VAL B O   1 
ATOM   24831 C  CB  . VAL C 1 1365 ? 9.486    23.273  83.133  1.00 108.92 ? 1365 VAL B CB  1 
ATOM   24832 C  CG1 . VAL C 1 1365 ? 8.348    22.550  83.873  1.00 107.97 ? 1365 VAL B CG1 1 
ATOM   24833 C  CG2 . VAL C 1 1365 ? 10.382   22.322  82.379  1.00 108.26 ? 1365 VAL B CG2 1 
ATOM   24834 N  N   . HIS C 1 1366 ? 7.624    23.178  80.453  1.00 124.99 ? 1366 HIS B N   1 
ATOM   24835 C  CA  . HIS C 1 1366 ? 6.379    22.749  79.816  1.00 125.98 ? 1366 HIS B CA  1 
ATOM   24836 C  C   . HIS C 1 1366 ? 6.141    21.302  80.116  1.00 123.74 ? 1366 HIS B C   1 
ATOM   24837 O  O   . HIS C 1 1366 ? 7.020    20.470  79.876  1.00 122.75 ? 1366 HIS B O   1 
ATOM   24838 C  CB  . HIS C 1 1366 ? 6.457    22.876  78.305  1.00 130.83 ? 1366 HIS B CB  1 
ATOM   24839 C  CG  . HIS C 1 1366 ? 6.668    24.269  77.821  1.00 132.94 ? 1366 HIS B CG  1 
ATOM   24840 N  ND1 . HIS C 1 1366 ? 7.562    25.133  78.417  1.00 132.31 ? 1366 HIS B ND1 1 
ATOM   24841 C  CD2 . HIS C 1 1366 ? 6.125    24.942  76.781  1.00 135.32 ? 1366 HIS B CD2 1 
ATOM   24842 C  CE1 . HIS C 1 1366 ? 7.549    26.286  77.774  1.00 133.46 ? 1366 HIS B CE1 1 
ATOM   24843 N  NE2 . HIS C 1 1366 ? 6.689    26.194  76.774  1.00 135.81 ? 1366 HIS B NE2 1 
ATOM   24844 N  N   . LYS C 1 1367 ? 4.961    20.986  80.631  1.00 122.60 ? 1367 LYS B N   1 
ATOM   24845 C  CA  . LYS C 1 1367 ? 4.630    19.581  80.828  1.00 126.19 ? 1367 LYS B CA  1 
ATOM   24846 C  C   . LYS C 1 1367 ? 3.558    19.084  79.879  1.00 127.32 ? 1367 LYS B C   1 
ATOM   24847 O  O   . LYS C 1 1367 ? 2.906    19.875  79.212  1.00 127.57 ? 1367 LYS B O   1 
ATOM   24848 C  CB  . LYS C 1 1367 ? 4.279    19.257  82.284  1.00 129.22 ? 1367 LYS B CB  1 
ATOM   24849 C  CG  . LYS C 1 1367 ? 3.416    20.248  83.025  1.00 131.25 ? 1367 LYS B CG  1 
ATOM   24850 C  CD  . LYS C 1 1367 ? 3.462    19.923  84.514  1.00 131.66 ? 1367 LYS B CD  1 
ATOM   24851 C  CE  . LYS C 1 1367 ? 4.909    19.790  84.989  1.00 130.59 ? 1367 LYS B CE  1 
ATOM   24852 N  NZ  . LYS C 1 1367 ? 4.998    18.921  86.183  1.00 130.53 ? 1367 LYS B NZ  1 
ATOM   24853 N  N   . THR C 1 1368 ? 3.391    17.768  79.807  1.00 121.43 ? 1368 THR B N   1 
ATOM   24854 C  CA  . THR C 1 1368 ? 2.420    17.194  78.893  1.00 121.14 ? 1368 THR B CA  1 
ATOM   24855 C  C   . THR C 1 1368 ? 1.088    16.920  79.562  1.00 120.54 ? 1368 THR B C   1 
ATOM   24856 O  O   . THR C 1 1368 ? 0.153    16.474  78.906  1.00 123.69 ? 1368 THR B O   1 
ATOM   24857 C  CB  . THR C 1 1368 ? 2.931    15.898  78.252  1.00 122.11 ? 1368 THR B CB  1 
ATOM   24858 O  OG1 . THR C 1 1368 ? 2.694    14.803  79.140  1.00 124.45 ? 1368 THR B OG1 1 
ATOM   24859 C  CG2 . THR C 1 1368 ? 4.414    16.003  77.948  1.00 120.92 ? 1368 THR B CG2 1 
ATOM   24860 N  N   . SER C 1 1369 ? 0.984    17.201  80.857  1.00 119.00 ? 1369 SER B N   1 
ATOM   24861 C  CA  . SER C 1 1369 ? -0.184   16.742  81.605  1.00 121.00 ? 1369 SER B CA  1 
ATOM   24862 C  C   . SER C 1 1369 ? -0.577   17.542  82.835  1.00 120.23 ? 1369 SER B C   1 
ATOM   24863 O  O   . SER C 1 1369 ? 0.241    18.196  83.484  1.00 115.88 ? 1369 SER B O   1 
ATOM   24864 C  CB  . SER C 1 1369 ? 0.013    15.287  82.033  1.00 124.08 ? 1369 SER B CB  1 
ATOM   24865 O  OG  . SER C 1 1369 ? 0.427    14.484  80.940  1.00 126.79 ? 1369 SER B OG  1 
ATOM   24866 N  N   . THR C 1 1370 ? -1.856   17.445  83.154  1.00 126.26 ? 1370 THR B N   1 
ATOM   24867 C  CA  . THR C 1 1370 ? -2.377   18.058  84.344  1.00 130.62 ? 1370 THR B CA  1 
ATOM   24868 C  C   . THR C 1 1370 ? -2.718   16.985  85.362  1.00 142.79 ? 1370 THR B C   1 
ATOM   24869 O  O   . THR C 1 1370 ? -2.785   17.272  86.551  1.00 144.34 ? 1370 THR B O   1 
ATOM   24870 C  CB  . THR C 1 1370 ? -3.607   18.906  84.012  1.00 125.20 ? 1370 THR B CB  1 
ATOM   24871 O  OG1 . THR C 1 1370 ? -3.178   20.074  83.314  1.00 119.89 ? 1370 THR B OG1 1 
ATOM   24872 C  CG2 . THR C 1 1370 ? -4.337   19.342  85.271  1.00 124.40 ? 1370 THR B CG2 1 
ATOM   24873 N  N   . SER C 1 1371 ? -2.906   15.750  84.898  1.00 152.69 ? 1371 SER B N   1 
ATOM   24874 C  CA  . SER C 1 1371 ? -3.354   14.661  85.768  1.00 162.34 ? 1371 SER B CA  1 
ATOM   24875 C  C   . SER C 1 1371 ? -2.890   14.828  87.219  1.00 167.35 ? 1371 SER B C   1 
ATOM   24876 O  O   . SER C 1 1371 ? -3.672   14.653  88.158  1.00 169.79 ? 1371 SER B O   1 
ATOM   24877 C  CB  . SER C 1 1371 ? -2.872   13.316  85.224  1.00 168.17 ? 1371 SER B CB  1 
ATOM   24878 O  OG  . SER C 1 1371 ? -1.467   13.173  85.355  1.00 169.87 ? 1371 SER B OG  1 
ATOM   24879 N  N   . GLU C 1 1372 ? -1.612   15.167  87.384  1.00 169.59 ? 1372 GLU B N   1 
ATOM   24880 C  CA  . GLU C 1 1372 ? -1.018   15.444  88.690  1.00 171.93 ? 1372 GLU B CA  1 
ATOM   24881 C  C   . GLU C 1 1372 ? -1.805   16.500  89.477  1.00 162.39 ? 1372 GLU B C   1 
ATOM   24882 O  O   . GLU C 1 1372 ? -2.430   16.179  90.486  1.00 162.71 ? 1372 GLU B O   1 
ATOM   24883 C  CB  . GLU C 1 1372 ? 0.443    15.898  88.518  1.00 182.26 ? 1372 GLU B CB  1 
ATOM   24884 C  CG  . GLU C 1 1372 ? 0.644    16.914  87.379  1.00 191.05 ? 1372 GLU B CG  1 
ATOM   24885 C  CD  . GLU C 1 1372 ? 1.981    17.660  87.418  1.00 197.81 ? 1372 GLU B CD  1 
ATOM   24886 O  OE1 . GLU C 1 1372 ? 2.925    17.186  88.091  1.00 201.72 ? 1372 GLU B OE1 1 
ATOM   24887 O  OE2 . GLU C 1 1372 ? 2.079    18.723  86.757  1.00 198.02 ? 1372 GLU B OE2 1 
ATOM   24888 N  N   . GLU C 1 1373 ? -1.789   17.740  88.979  1.00 152.13 ? 1373 GLU B N   1 
ATOM   24889 C  CA  . GLU C 1 1373 ? -2.297   18.943  89.671  1.00 140.93 ? 1373 GLU B CA  1 
ATOM   24890 C  C   . GLU C 1 1373 ? -3.634   18.819  90.420  1.00 137.86 ? 1373 GLU B C   1 
ATOM   24891 O  O   . GLU C 1 1373 ? -4.372   17.843  90.270  1.00 138.45 ? 1373 GLU B O   1 
ATOM   24892 C  CB  . GLU C 1 1373 ? -2.375   20.121  88.687  1.00 133.32 ? 1373 GLU B CB  1 
ATOM   24893 C  CG  . GLU C 1 1373 ? -1.061   20.388  87.941  1.00 126.82 ? 1373 GLU B CG  1 
ATOM   24894 C  CD  . GLU C 1 1373 ? -1.187   21.433  86.835  1.00 118.92 ? 1373 GLU B CD  1 
ATOM   24895 O  OE1 . GLU C 1 1373 ? -2.336   21.868  86.557  1.00 115.85 ? 1373 GLU B OE1 1 
ATOM   24896 O  OE2 . GLU C 1 1373 ? -0.131   21.807  86.253  1.00 114.57 ? 1373 GLU B OE2 1 
ATOM   24897 N  N   . VAL C 1 1374 ? -3.932   19.834  91.224  1.00 131.92 ? 1374 VAL B N   1 
ATOM   24898 C  CA  . VAL C 1 1374 ? -5.129   19.840  92.046  1.00 127.91 ? 1374 VAL B CA  1 
ATOM   24899 C  C   . VAL C 1 1374 ? -6.260   20.634  91.438  1.00 126.16 ? 1374 VAL B C   1 
ATOM   24900 O  O   . VAL C 1 1374 ? -6.161   21.864  91.296  1.00 125.10 ? 1374 VAL B O   1 
ATOM   24901 C  CB  . VAL C 1 1374 ? -4.860   20.504  93.373  1.00 125.00 ? 1374 VAL B CB  1 
ATOM   24902 C  CG1 . VAL C 1 1374 ? -5.933   20.090  94.353  1.00 126.00 ? 1374 VAL B CG1 1 
ATOM   24903 C  CG2 . VAL C 1 1374 ? -3.462   20.177  93.869  1.00 123.55 ? 1374 VAL B CG2 1 
ATOM   24904 N  N   . CYS C 1 1375 ? -7.353   19.954  91.111  1.00 125.84 ? 1375 CYS B N   1 
ATOM   24905 C  CA  . CYS C 1 1375 ? -8.474   20.655  90.472  1.00 123.94 ? 1375 CYS B CA  1 
ATOM   24906 C  C   . CYS C 1 1375 ? -9.526   21.242  91.433  1.00 123.73 ? 1375 CYS B C   1 
ATOM   24907 O  O   . CYS C 1 1375 ? -10.195  20.520  92.169  1.00 124.00 ? 1375 CYS B O   1 
ATOM   24908 C  CB  . CYS C 1 1375 ? -9.102   19.832  89.327  1.00 122.52 ? 1375 CYS B CB  1 
ATOM   24909 S  SG  . CYS C 1 1375 ? -8.475   20.306  87.676  1.00 200.63 ? 1375 CYS B SG  1 
ATOM   24910 N  N   . SER C 1 1376 ? -9.647   22.565  91.396  1.00 123.19 ? 1376 SER B N   1 
ATOM   24911 C  CA  . SER C 1 1376 ? -10.509  23.297  92.287  1.00 124.41 ? 1376 SER B CA  1 
ATOM   24912 C  C   . SER C 1 1376 ? -11.818  23.660  91.557  1.00 127.35 ? 1376 SER B C   1 
ATOM   24913 O  O   . SER C 1 1376 ? -12.755  24.197  92.153  1.00 129.86 ? 1376 SER B O   1 
ATOM   24914 C  CB  . SER C 1 1376 ? -9.739   24.523  92.772  1.00 119.74 ? 1376 SER B CB  1 
ATOM   24915 O  OG  . SER C 1 1376 ? -8.339   24.322  92.603  1.00 116.67 ? 1376 SER B OG  1 
ATOM   24916 N  N   . PHE C 1 1377 ? -11.866  23.341  90.259  1.00 127.61 ? 1377 PHE B N   1 
ATOM   24917 C  CA  . PHE C 1 1377 ? -13.017  23.593  89.368  1.00 125.21 ? 1377 PHE B CA  1 
ATOM   24918 C  C   . PHE C 1 1377 ? -13.356  22.387  88.472  1.00 128.96 ? 1377 PHE B C   1 
ATOM   24919 O  O   . PHE C 1 1377 ? -12.466  21.796  87.851  1.00 130.54 ? 1377 PHE B O   1 
ATOM   24920 C  CB  . PHE C 1 1377 ? -12.696  24.746  88.438  1.00 119.94 ? 1377 PHE B CB  1 
ATOM   24921 C  CG  . PHE C 1 1377 ? -12.905  26.064  89.039  1.00 119.89 ? 1377 PHE B CG  1 
ATOM   24922 C  CD1 . PHE C 1 1377 ? -14.174  26.536  89.244  1.00 120.40 ? 1377 PHE B CD1 1 
ATOM   24923 C  CD2 . PHE C 1 1377 ? -11.838  26.845  89.403  1.00 120.44 ? 1377 PHE B CD2 1 
ATOM   24924 C  CE1 . PHE C 1 1377 ? -14.382  27.769  89.794  1.00 119.72 ? 1377 PHE B CE1 1 
ATOM   24925 C  CE2 . PHE C 1 1377 ? -12.045  28.079  89.962  1.00 119.70 ? 1377 PHE B CE2 1 
ATOM   24926 C  CZ  . PHE C 1 1377 ? -13.321  28.536  90.155  1.00 119.11 ? 1377 PHE B CZ  1 
ATOM   24927 N  N   . TYR C 1 1378 ? -14.635  22.024  88.387  1.00 129.81 ? 1378 TYR B N   1 
ATOM   24928 C  CA  . TYR C 1 1378 ? -15.042  20.932  87.509  1.00 128.38 ? 1378 TYR B CA  1 
ATOM   24929 C  C   . TYR C 1 1378 ? -15.200  21.499  86.105  1.00 126.07 ? 1378 TYR B C   1 
ATOM   24930 O  O   . TYR C 1 1378 ? -15.950  22.453  85.895  1.00 123.30 ? 1378 TYR B O   1 
ATOM   24931 C  CB  . TYR C 1 1378 ? -16.359  20.287  87.980  1.00 128.68 ? 1378 TYR B CB  1 
ATOM   24932 C  CG  . TYR C 1 1378 ? -16.278  19.407  89.230  1.00 127.14 ? 1378 TYR B CG  1 
ATOM   24933 C  CD1 . TYR C 1 1378 ? -15.425  18.322  89.285  1.00 127.12 ? 1378 TYR B CD1 1 
ATOM   24934 C  CD2 . TYR C 1 1378 ? -17.093  19.647  90.338  1.00 126.77 ? 1378 TYR B CD2 1 
ATOM   24935 C  CE1 . TYR C 1 1378 ? -15.356  17.511  90.418  1.00 128.46 ? 1378 TYR B CE1 1 
ATOM   24936 C  CE2 . TYR C 1 1378 ? -17.034  18.842  91.478  1.00 127.59 ? 1378 TYR B CE2 1 
ATOM   24937 C  CZ  . TYR C 1 1378 ? -16.162  17.774  91.513  1.00 128.56 ? 1378 TYR B CZ  1 
ATOM   24938 O  OH  . TYR C 1 1378 ? -16.091  16.975  92.638  1.00 129.40 ? 1378 TYR B OH  1 
ATOM   24939 N  N   . LEU C 1 1379 ? -14.502  20.925  85.136  1.00 128.69 ? 1379 LEU B N   1 
ATOM   24940 C  CA  . LEU C 1 1379 ? -14.591  21.464  83.788  1.00 131.62 ? 1379 LEU B CA  1 
ATOM   24941 C  C   . LEU C 1 1379 ? -15.084  20.486  82.729  1.00 141.65 ? 1379 LEU B C   1 
ATOM   24942 O  O   . LEU C 1 1379 ? -15.042  19.258  82.891  1.00 146.67 ? 1379 LEU B O   1 
ATOM   24943 C  CB  . LEU C 1 1379 ? -13.241  22.000  83.364  1.00 128.62 ? 1379 LEU B CB  1 
ATOM   24944 C  CG  . LEU C 1 1379 ? -12.806  23.130  84.271  1.00 126.59 ? 1379 LEU B CG  1 
ATOM   24945 C  CD1 . LEU C 1 1379 ? -11.422  23.652  83.878  1.00 123.98 ? 1379 LEU B CD1 1 
ATOM   24946 C  CD2 . LEU C 1 1379 ? -13.871  24.194  84.180  1.00 125.81 ? 1379 LEU B CD2 1 
ATOM   24947 N  N   . LYS C 1 1380 ? -15.562  21.059  81.635  1.00 142.92 ? 1380 LYS B N   1 
ATOM   24948 C  CA  . LYS C 1 1380 ? -15.873  20.300  80.445  1.00 144.58 ? 1380 LYS B CA  1 
ATOM   24949 C  C   . LYS C 1 1380 ? -15.759  21.285  79.298  1.00 142.20 ? 1380 LYS B C   1 
ATOM   24950 O  O   . LYS C 1 1380 ? -15.986  22.484  79.469  1.00 138.91 ? 1380 LYS B O   1 
ATOM   24951 C  CB  . LYS C 1 1380 ? -17.243  19.576  80.524  1.00 132.75 ? 1380 LYS B CB  1 
ATOM   24952 C  CG  . LYS C 1 1380 ? -18.475  20.382  81.044  1.00 138.79 ? 1380 LYS B CG  1 
ATOM   24953 C  CD  . LYS C 1 1380 ? -19.773  19.499  81.185  1.00 139.53 ? 1380 LYS B CD  1 
ATOM   24954 C  CE  . LYS C 1 1380 ? -21.090  20.323  81.298  1.00 121.73 ? 1380 LYS B CE  1 
ATOM   24955 N  NZ  . LYS C 1 1380 ? -22.369  19.573  81.039  1.00 124.18 ? 1380 LYS B NZ  1 
ATOM   24956 N  N   . ILE C 1 1381 ? -15.333  20.779  78.151  1.00 141.11 ? 1381 ILE B N   1 
ATOM   24957 C  CA  . ILE C 1 1381 ? -15.175  21.592  76.957  1.00 137.24 ? 1381 ILE B CA  1 
ATOM   24958 C  C   . ILE C 1 1381 ? -15.196  20.670  75.742  1.00 145.61 ? 1381 ILE B C   1 
ATOM   24959 O  O   . ILE C 1 1381 ? -14.773  19.507  75.836  1.00 151.30 ? 1381 ILE B O   1 
ATOM   24960 C  CB  . ILE C 1 1381 ? -13.844  22.346  76.970  1.00 126.37 ? 1381 ILE B CB  1 
ATOM   24961 C  CG1 . ILE C 1 1381 ? -13.986  23.641  76.213  1.00 122.78 ? 1381 ILE B CG1 1 
ATOM   24962 C  CG2 . ILE C 1 1381 ? -12.739  21.546  76.312  1.00 123.08 ? 1381 ILE B CG2 1 
ATOM   24963 C  CD1 . ILE C 1 1381 ? -12.707  24.099  75.664  1.00 120.62 ? 1381 ILE B CD1 1 
ATOM   24964 N  N   . ASP C 1 1382 ? -15.705  21.169  74.616  1.00 145.35 ? 1382 ASP B N   1 
ATOM   24965 C  CA  . ASP C 1 1382 ? -15.557  20.473  73.336  1.00 148.80 ? 1382 ASP B CA  1 
ATOM   24966 C  C   . ASP C 1 1382 ? -16.001  21.346  72.167  1.00 148.15 ? 1382 ASP B C   1 
ATOM   24967 O  O   . ASP C 1 1382 ? -16.534  22.433  72.367  1.00 145.01 ? 1382 ASP B O   1 
ATOM   24968 C  CB  . ASP C 1 1382 ? -16.275  19.110  73.327  1.00 154.89 ? 1382 ASP B CB  1 
ATOM   24969 C  CG  . ASP C 1 1382 ? -17.672  19.172  73.925  1.00 159.52 ? 1382 ASP B CG  1 
ATOM   24970 O  OD1 . ASP C 1 1382 ? -17.785  19.467  75.134  1.00 159.23 ? 1382 ASP B OD1 1 
ATOM   24971 O  OD2 . ASP C 1 1382 ? -18.658  18.902  73.195  1.00 163.36 ? 1382 ASP B OD2 1 
ATOM   24972 N  N   . THR C 1 1383 ? -15.743  20.873  70.949  1.00 152.20 ? 1383 THR B N   1 
ATOM   24973 C  CA  . THR C 1 1383 ? -16.165  21.570  69.731  1.00 152.44 ? 1383 THR B CA  1 
ATOM   24974 C  C   . THR C 1 1383 ? -17.426  20.981  69.082  1.00 154.02 ? 1383 THR B C   1 
ATOM   24975 O  O   . THR C 1 1383 ? -17.437  19.849  68.597  1.00 154.87 ? 1383 THR B O   1 
ATOM   24976 C  CB  . THR C 1 1383 ? -15.017  21.691  68.693  1.00 151.16 ? 1383 THR B CB  1 
ATOM   24977 O  OG1 . THR C 1 1383 ? -14.090  20.614  68.865  1.00 153.36 ? 1383 THR B OG1 1 
ATOM   24978 C  CG2 . THR C 1 1383 ? -14.269  22.998  68.870  1.00 146.92 ? 1383 THR B CG2 1 
ATOM   24979 N  N   . GLN C 1 1384 ? -18.484  21.779  69.088  1.00 156.18 ? 1384 GLN B N   1 
ATOM   24980 C  CA  . GLN C 1 1384 ? -19.735  21.436  68.433  1.00 162.50 ? 1384 GLN B CA  1 
ATOM   24981 C  C   . GLN C 1 1384 ? -19.741  21.908  66.986  1.00 164.53 ? 1384 GLN B C   1 
ATOM   24982 O  O   . GLN C 1 1384 ? -18.991  22.810  66.610  1.00 161.99 ? 1384 GLN B O   1 
ATOM   24983 C  CB  . GLN C 1 1384 ? -20.901  22.097  69.158  1.00 165.06 ? 1384 GLN B CB  1 
ATOM   24984 C  CG  . GLN C 1 1384 ? -21.006  21.724  70.616  1.00 168.80 ? 1384 GLN B CG  1 
ATOM   24985 C  CD  . GLN C 1 1384 ? -22.287  22.233  71.246  1.00 172.25 ? 1384 GLN B CD  1 
ATOM   24986 O  OE1 . GLN C 1 1384 ? -22.728  23.351  70.973  1.00 172.07 ? 1384 GLN B OE1 1 
ATOM   24987 N  NE2 . GLN C 1 1384 ? -22.891  21.413  72.100  1.00 174.91 ? 1384 GLN B NE2 1 
ATOM   24988 N  N   . ASP C 1 1385 ? -20.606  21.304  66.178  1.00 169.49 ? 1385 ASP B N   1 
ATOM   24989 C  CA  . ASP C 1 1385 ? -20.762  21.719  64.786  1.00 171.19 ? 1385 ASP B CA  1 
ATOM   24990 C  C   . ASP C 1 1385 ? -22.008  22.601  64.555  1.00 172.48 ? 1385 ASP B C   1 
ATOM   24991 O  O   . ASP C 1 1385 ? -22.006  23.496  63.697  1.00 171.02 ? 1385 ASP B O   1 
ATOM   24992 C  CB  . ASP C 1 1385 ? -20.731  20.503  63.855  1.00 174.39 ? 1385 ASP B CB  1 
ATOM   24993 C  CG  . ASP C 1 1385 ? -19.348  19.881  63.762  1.00 174.31 ? 1385 ASP B CG  1 
ATOM   24994 O  OD1 . ASP C 1 1385 ? -18.428  20.543  63.233  1.00 172.68 ? 1385 ASP B OD1 1 
ATOM   24995 O  OD2 . ASP C 1 1385 ? -19.174  18.731  64.218  1.00 175.97 ? 1385 ASP B OD2 1 
ATOM   24996 N  N   . ILE C 1 1386 ? -23.056  22.362  65.343  1.00 173.76 ? 1386 ILE B N   1 
ATOM   24997 C  CA  . ILE C 1 1386 ? -24.316  23.107  65.220  1.00 173.66 ? 1386 ILE B CA  1 
ATOM   24998 C  C   . ILE C 1 1386 ? -24.127  24.621  65.442  1.00 167.89 ? 1386 ILE B C   1 
ATOM   24999 O  O   . ILE C 1 1386 ? -23.585  25.341  64.596  1.00 164.25 ? 1386 ILE B O   1 
ATOM   25000 C  CB  . ILE C 1 1386 ? -25.398  22.566  66.214  1.00 237.90 ? 1386 ILE B CB  1 
ATOM   25001 C  CG1 . ILE C 1 1386 ? -25.216  21.065  66.473  1.00 240.34 ? 1386 ILE B CG1 1 
ATOM   25002 C  CG2 . ILE C 1 1386 ? -26.807  22.855  65.701  1.00 239.64 ? 1386 ILE B CG2 1 
ATOM   25003 C  CD1 . ILE C 1 1386 ? -26.199  20.487  67.479  1.00 241.95 ? 1386 ILE B CD1 1 
ATOM   25004 N  N   . TYR C 1 1399 ? -20.947  25.910  61.489  1.00 217.59 ? 1399 TYR B N   1 
ATOM   25005 C  CA  . TYR C 1 1399 ? -19.622  25.561  60.989  1.00 217.93 ? 1399 TYR B CA  1 
ATOM   25006 C  C   . TYR C 1 1399 ? -18.894  24.789  62.091  1.00 203.81 ? 1399 TYR B C   1 
ATOM   25007 O  O   . TYR C 1 1399 ? -18.735  23.572  62.000  1.00 204.93 ? 1399 TYR B O   1 
ATOM   25008 C  CB  . TYR C 1 1399 ? -18.869  26.836  60.568  1.00 229.36 ? 1399 TYR B CB  1 
ATOM   25009 C  CG  . TYR C 1 1399 ? -17.448  26.663  60.027  1.00 241.71 ? 1399 TYR B CG  1 
ATOM   25010 C  CD1 . TYR C 1 1399 ? -17.146  25.707  59.054  1.00 249.47 ? 1399 TYR B CD1 1 
ATOM   25011 C  CD2 . TYR C 1 1399 ? -16.413  27.497  60.465  1.00 244.11 ? 1399 TYR B CD2 1 
ATOM   25012 C  CE1 . TYR C 1 1399 ? -15.840  25.568  58.558  1.00 252.10 ? 1399 TYR B CE1 1 
ATOM   25013 C  CE2 . TYR C 1 1399 ? -15.111  27.367  59.975  1.00 246.52 ? 1399 TYR B CE2 1 
ATOM   25014 C  CZ  . TYR C 1 1399 ? -14.831  26.403  59.024  1.00 250.40 ? 1399 TYR B CZ  1 
ATOM   25015 O  OH  . TYR C 1 1399 ? -13.546  26.278  58.540  1.00 250.71 ? 1399 TYR B OH  1 
ATOM   25016 N  N   . LYS C 1 1400 ? -18.476  25.499  63.138  1.00 188.32 ? 1400 LYS B N   1 
ATOM   25017 C  CA  . LYS C 1 1400 ? -17.961  24.883  64.362  1.00 172.31 ? 1400 LYS B CA  1 
ATOM   25018 C  C   . LYS C 1 1400 ? -17.958  25.909  65.501  1.00 158.08 ? 1400 LYS B C   1 
ATOM   25019 O  O   . LYS C 1 1400 ? -17.840  27.115  65.266  1.00 154.47 ? 1400 LYS B O   1 
ATOM   25020 C  CB  . LYS C 1 1400 ? -16.583  24.229  64.157  1.00 169.53 ? 1400 LYS B CB  1 
ATOM   25021 C  CG  . LYS C 1 1400 ? -15.675  24.909  63.127  1.00 165.88 ? 1400 LYS B CG  1 
ATOM   25022 C  CD  . LYS C 1 1400 ? -14.206  24.449  63.233  1.00 163.77 ? 1400 LYS B CD  1 
ATOM   25023 C  CE  . LYS C 1 1400 ? -13.965  23.029  62.689  1.00 165.63 ? 1400 LYS B CE  1 
ATOM   25024 N  NZ  . LYS C 1 1400 ? -12.508  22.663  62.657  1.00 163.88 ? 1400 LYS B NZ  1 
ATOM   25025 N  N   . ARG C 1 1401 ? -18.102  25.427  66.732  1.00 147.54 ? 1401 ARG B N   1 
ATOM   25026 C  CA  . ARG C 1 1401 ? -18.247  26.305  67.901  1.00 134.96 ? 1401 ARG B CA  1 
ATOM   25027 C  C   . ARG C 1 1401 ? -17.801  25.652  69.229  1.00 133.98 ? 1401 ARG B C   1 
ATOM   25028 O  O   . ARG C 1 1401 ? -18.027  24.457  69.443  1.00 135.95 ? 1401 ARG B O   1 
ATOM   25029 C  CB  . ARG C 1 1401 ? -19.705  26.725  68.018  1.00 126.81 ? 1401 ARG B CB  1 
ATOM   25030 C  CG  . ARG C 1 1401 ? -20.156  26.952  69.436  1.00 118.80 ? 1401 ARG B CG  1 
ATOM   25031 C  CD  . ARG C 1 1401 ? -21.448  26.227  69.728  1.00 117.07 ? 1401 ARG B CD  1 
ATOM   25032 N  NE  . ARG C 1 1401 ? -22.470  27.172  70.165  1.00 113.95 ? 1401 ARG B NE  1 
ATOM   25033 C  CZ  . ARG C 1 1401 ? -23.552  26.854  70.867  1.00 113.74 ? 1401 ARG B CZ  1 
ATOM   25034 N  NH1 . ARG C 1 1401 ? -23.771  25.600  71.241  1.00 115.00 ? 1401 ARG B NH1 1 
ATOM   25035 N  NH2 . ARG C 1 1401 ? -24.411  27.802  71.207  1.00 112.74 ? 1401 ARG B NH2 1 
ATOM   25036 N  N   . ILE C 1 1402 ? -17.194  26.439  70.122  1.00 129.20 ? 1402 ILE B N   1 
ATOM   25037 C  CA  . ILE C 1 1402 ? -16.726  25.924  71.414  1.00 125.65 ? 1402 ILE B CA  1 
ATOM   25038 C  C   . ILE C 1 1402 ? -17.697  26.101  72.571  1.00 126.22 ? 1402 ILE B C   1 
ATOM   25039 O  O   . ILE C 1 1402 ? -18.232  27.182  72.789  1.00 124.66 ? 1402 ILE B O   1 
ATOM   25040 C  CB  . ILE C 1 1402 ? -15.455  26.604  71.858  1.00 118.01 ? 1402 ILE B CB  1 
ATOM   25041 C  CG1 . ILE C 1 1402 ? -14.361  26.381  70.833  1.00 116.18 ? 1402 ILE B CG1 1 
ATOM   25042 C  CG2 . ILE C 1 1402 ? -15.062  26.052  73.185  1.00 117.43 ? 1402 ILE B CG2 1 
ATOM   25043 C  CD1 . ILE C 1 1402 ? -13.070  26.992  71.211  1.00 113.19 ? 1402 ILE B CD1 1 
ATOM   25044 N  N   . VAL C 1 1403 ? -17.882  25.042  73.344  1.00 130.33 ? 1403 VAL B N   1 
ATOM   25045 C  CA  . VAL C 1 1403 ? -18.766  25.100  74.495  1.00 133.78 ? 1403 VAL B CA  1 
ATOM   25046 C  C   . VAL C 1 1403 ? -18.003  24.695  75.756  1.00 137.83 ? 1403 VAL B C   1 
ATOM   25047 O  O   . VAL C 1 1403 ? -17.891  23.497  76.093  1.00 141.24 ? 1403 VAL B O   1 
ATOM   25048 C  CB  . VAL C 1 1403 ? -20.015  24.206  74.306  1.00 135.99 ? 1403 VAL B CB  1 
ATOM   25049 C  CG1 . VAL C 1 1403 ? -20.760  24.032  75.617  1.00 136.40 ? 1403 VAL B CG1 1 
ATOM   25050 C  CG2 . VAL C 1 1403 ? -20.928  24.802  73.272  1.00 136.28 ? 1403 VAL B CG2 1 
ATOM   25051 N  N   . ALA C 1 1404 ? -17.468  25.710  76.438  1.00 136.56 ? 1404 ALA B N   1 
ATOM   25052 C  CA  . ALA C 1 1404 ? -16.728  25.513  77.679  1.00 135.81 ? 1404 ALA B CA  1 
ATOM   25053 C  C   . ALA C 1 1404 ? -17.608  25.763  78.900  1.00 137.20 ? 1404 ALA B C   1 
ATOM   25054 O  O   . ALA C 1 1404 ? -18.410  26.706  78.916  1.00 133.60 ? 1404 ALA B O   1 
ATOM   25055 C  CB  . ALA C 1 1404 ? -15.501  26.405  77.718  1.00 132.05 ? 1404 ALA B CB  1 
ATOM   25056 N  N   . CYS C 1 1405 ? -17.447  24.907  79.911  1.00 140.33 ? 1405 CYS B N   1 
ATOM   25057 C  CA  . CYS C 1 1405 ? -18.217  24.995  81.142  1.00 141.29 ? 1405 CYS B CA  1 
ATOM   25058 C  C   . CYS C 1 1405 ? -17.309  24.829  82.333  1.00 140.57 ? 1405 CYS B C   1 
ATOM   25059 O  O   . CYS C 1 1405 ? -16.141  24.440  82.200  1.00 141.73 ? 1405 CYS B O   1 
ATOM   25060 C  CB  . CYS C 1 1405 ? -19.285  23.907  81.204  1.00 144.85 ? 1405 CYS B CB  1 
ATOM   25061 S  SG  . CYS C 1 1405 ? -19.960  23.451  79.630  1.00 163.03 ? 1405 CYS B SG  1 
ATOM   25062 N  N   . ALA C 1 1406 ? -17.875  25.106  83.502  1.00 137.56 ? 1406 ALA B N   1 
ATOM   25063 C  CA  . ALA C 1 1406 ? -17.175  24.935  84.767  1.00 135.22 ? 1406 ALA B CA  1 
ATOM   25064 C  C   . ALA C 1 1406 ? -18.163  24.878  85.937  1.00 137.57 ? 1406 ALA B C   1 
ATOM   25065 O  O   . ALA C 1 1406 ? -19.278  25.395  85.845  1.00 136.69 ? 1406 ALA B O   1 
ATOM   25066 C  CB  . ALA C 1 1406 ? -16.189  26.077  84.976  1.00 129.13 ? 1406 ALA B CB  1 
ATOM   25067 N  N   . SER C 1 1407 ? -17.756  24.240  87.028  1.00 140.93 ? 1407 SER B N   1 
ATOM   25068 C  CA  . SER C 1 1407 ? -18.440  24.400  88.298  1.00 142.44 ? 1407 SER B CA  1 
ATOM   25069 C  C   . SER C 1 1407 ? -17.387  24.530  89.366  1.00 143.09 ? 1407 SER B C   1 
ATOM   25070 O  O   . SER C 1 1407 ? -16.290  23.985  89.233  1.00 145.27 ? 1407 SER B O   1 
ATOM   25071 C  CB  . SER C 1 1407 ? -19.315  23.207  88.620  1.00 144.04 ? 1407 SER B CB  1 
ATOM   25072 O  OG  . SER C 1 1407 ? -19.674  23.244  89.993  1.00 142.81 ? 1407 SER B OG  1 
ATOM   25073 N  N   . TYR C 1 1408 ? -17.706  25.269  90.421  1.00 140.64 ? 1408 TYR B N   1 
ATOM   25074 C  CA  . TYR C 1 1408 ? -16.739  25.480  91.483  1.00 137.87 ? 1408 TYR B CA  1 
ATOM   25075 C  C   . TYR C 1 1408 ? -16.827  24.355  92.500  1.00 138.55 ? 1408 TYR B C   1 
ATOM   25076 O  O   . TYR C 1 1408 ? -17.906  24.069  93.008  1.00 141.09 ? 1408 TYR B O   1 
ATOM   25077 C  CB  . TYR C 1 1408 ? -16.951  26.832  92.161  1.00 137.92 ? 1408 TYR B CB  1 
ATOM   25078 C  CG  . TYR C 1 1408 ? -16.008  27.036  93.306  1.00 140.27 ? 1408 TYR B CG  1 
ATOM   25079 C  CD1 . TYR C 1 1408 ? -14.701  26.582  93.222  1.00 141.54 ? 1408 TYR B CD1 1 
ATOM   25080 C  CD2 . TYR C 1 1408 ? -16.416  27.673  94.467  1.00 141.90 ? 1408 TYR B CD2 1 
ATOM   25081 C  CE1 . TYR C 1 1408 ? -13.829  26.745  94.256  1.00 143.36 ? 1408 TYR B CE1 1 
ATOM   25082 C  CE2 . TYR C 1 1408 ? -15.547  27.849  95.513  1.00 143.72 ? 1408 TYR B CE2 1 
ATOM   25083 C  CZ  . TYR C 1 1408 ? -14.248  27.379  95.403  1.00 145.08 ? 1408 TYR B CZ  1 
ATOM   25084 O  OH  . TYR C 1 1408 ? -13.352  27.534  96.441  1.00 146.49 ? 1408 TYR B OH  1 
ATOM   25085 N  N   . LYS C 1 1409 ? -15.696  23.710  92.779  1.00 136.03 ? 1409 LYS B N   1 
ATOM   25086 C  CA  . LYS C 1 1409 ? -15.639  22.670  93.804  1.00 137.27 ? 1409 LYS B CA  1 
ATOM   25087 C  C   . LYS C 1 1409 ? -15.389  23.337  95.159  1.00 140.02 ? 1409 LYS B C   1 
ATOM   25088 O  O   . LYS C 1 1409 ? -14.283  23.822  95.406  1.00 139.88 ? 1409 LYS B O   1 
ATOM   25089 C  CB  . LYS C 1 1409 ? -14.497  21.679  93.516  1.00 132.69 ? 1409 LYS B CB  1 
ATOM   25090 C  CG  . LYS C 1 1409 ? -14.477  21.039  92.135  1.00 128.54 ? 1409 LYS B CG  1 
ATOM   25091 C  CD  . LYS C 1 1409 ? -13.223  20.176  91.909  1.00 125.49 ? 1409 LYS B CD  1 
ATOM   25092 C  CE  . LYS C 1 1409 ? -13.363  18.769  92.496  1.00 127.14 ? 1409 LYS B CE  1 
ATOM   25093 N  NZ  . LYS C 1 1409 ? -12.221  17.851  92.182  1.00 127.57 ? 1409 LYS B NZ  1 
ATOM   25094 N  N   . PRO C 1 1410 ? -16.400  23.386  96.044  1.00 144.38 ? 1410 PRO B N   1 
ATOM   25095 C  CA  . PRO C 1 1410 ? -16.118  24.058  97.316  1.00 147.44 ? 1410 PRO B CA  1 
ATOM   25096 C  C   . PRO C 1 1410 ? -15.117  23.302  98.187  1.00 156.21 ? 1410 PRO B C   1 
ATOM   25097 O  O   . PRO C 1 1410 ? -15.132  22.075  98.273  1.00 157.51 ? 1410 PRO B O   1 
ATOM   25098 C  CB  . PRO C 1 1410 ? -17.498  24.136  97.979  1.00 145.54 ? 1410 PRO B CB  1 
ATOM   25099 C  CG  . PRO C 1 1410 ? -18.421  24.165  96.854  1.00 144.69 ? 1410 PRO B CG  1 
ATOM   25100 C  CD  . PRO C 1 1410 ? -17.841  23.170  95.878  1.00 145.79 ? 1410 PRO B CD  1 
ATOM   25101 N  N   . SER C 1 1411 ? -14.218  24.060  98.798  1.00 164.67 ? 1411 SER B N   1 
ATOM   25102 C  CA  . SER C 1 1411 ? -13.262  23.512  99.731  1.00 177.38 ? 1411 SER B CA  1 
ATOM   25103 C  C   . SER C 1 1411 ? -14.027  23.257  101.005 1.00 190.90 ? 1411 SER B C   1 
ATOM   25104 O  O   . SER C 1 1411 ? -15.037  23.906  101.263 1.00 191.62 ? 1411 SER B O   1 
ATOM   25105 C  CB  . SER C 1 1411 ? -12.134  24.512  99.992  1.00 175.97 ? 1411 SER B CB  1 
ATOM   25106 O  OG  . SER C 1 1411 ? -11.681  25.121  98.789  1.00 175.41 ? 1411 SER B OG  1 
ATOM   25107 N  N   . ARG C 1 1412 ? -13.552  22.308  101.798 1.00 205.09 ? 1412 ARG B N   1 
ATOM   25108 C  CA  . ARG C 1 1412 ? -14.186  21.991  103.067 1.00 218.78 ? 1412 ARG B CA  1 
ATOM   25109 C  C   . ARG C 1 1412 ? -14.421  23.276  103.850 1.00 217.22 ? 1412 ARG B C   1 
ATOM   25110 O  O   . ARG C 1 1412 ? -13.637  24.220  103.747 1.00 216.40 ? 1412 ARG B O   1 
ATOM   25111 C  CB  . ARG C 1 1412 ? -13.297  21.045  103.876 1.00 232.73 ? 1412 ARG B CB  1 
ATOM   25112 C  CG  . ARG C 1 1412 ? -11.943  21.646  104.233 1.00 242.36 ? 1412 ARG B CG  1 
ATOM   25113 C  CD  . ARG C 1 1412 ? -11.256  20.883  105.358 1.00 254.12 ? 1412 ARG B CD  1 
ATOM   25114 N  NE  . ARG C 1 1412 ? -10.287  21.728  106.049 1.00 260.35 ? 1412 ARG B NE  1 
ATOM   25115 C  CZ  . ARG C 1 1412 ? -9.548   21.331  107.079 1.00 267.00 ? 1412 ARG B CZ  1 
ATOM   25116 N  NH1 . ARG C 1 1412 ? -9.666   20.091  107.539 1.00 271.24 ? 1412 ARG B NH1 1 
ATOM   25117 N  NH2 . ARG C 1 1412 ? -8.692   22.174  107.645 1.00 267.40 ? 1412 ARG B NH2 1 
ATOM   25118 N  N   . GLU C 1 1413 ? -15.497  23.303  104.630 1.00 216.10 ? 1413 GLU B N   1 
ATOM   25119 C  CA  . GLU C 1 1413 ? -15.842  24.473  105.432 1.00 212.30 ? 1413 GLU B CA  1 
ATOM   25120 C  C   . GLU C 1 1413 ? -16.523  25.546  104.591 1.00 196.88 ? 1413 GLU B C   1 
ATOM   25121 O  O   . GLU C 1 1413 ? -17.103  26.487  105.133 1.00 194.02 ? 1413 GLU B O   1 
ATOM   25122 C  CB  . GLU C 1 1413 ? -14.596  25.076  106.095 1.00 221.63 ? 1413 GLU B CB  1 
ATOM   25123 C  CG  . GLU C 1 1413 ? -13.742  24.088  106.881 1.00 232.41 ? 1413 GLU B CG  1 
ATOM   25124 C  CD  . GLU C 1 1413 ? -14.272  23.828  108.281 1.00 240.88 ? 1413 GLU B CD  1 
ATOM   25125 O  OE1 . GLU C 1 1413 ? -14.784  24.779  108.907 1.00 243.02 ? 1413 GLU B OE1 1 
ATOM   25126 O  OE2 . GLU C 1 1413 ? -14.167  22.677  108.759 1.00 244.82 ? 1413 GLU B OE2 1 
ATOM   25127 N  N   . GLU C 1 1414 ? -16.450  25.412  103.269 1.00 183.46 ? 1414 GLU B N   1 
ATOM   25128 C  CA  . GLU C 1 1414 ? -16.926  26.467  102.376 1.00 167.12 ? 1414 GLU B CA  1 
ATOM   25129 C  C   . GLU C 1 1414 ? -18.413  26.462  102.086 1.00 160.77 ? 1414 GLU B C   1 
ATOM   25130 O  O   . GLU C 1 1414 ? -19.066  25.431  102.088 1.00 162.29 ? 1414 GLU B O   1 
ATOM   25131 C  CB  . GLU C 1 1414 ? -16.155  26.467  101.062 1.00 157.49 ? 1414 GLU B CB  1 
ATOM   25132 C  CG  . GLU C 1 1414 ? -15.195  27.616  100.927 1.00 147.16 ? 1414 GLU B CG  1 
ATOM   25133 C  CD  . GLU C 1 1414 ? -14.243  27.421  99.775  1.00 140.81 ? 1414 GLU B CD  1 
ATOM   25134 O  OE1 . GLU C 1 1414 ? -14.439  26.463  99.007  1.00 139.74 ? 1414 GLU B OE1 1 
ATOM   25135 O  OE2 . GLU C 1 1414 ? -13.291  28.213  99.637  1.00 137.76 ? 1414 GLU B OE2 1 
ATOM   25136 N  N   . SER C 1 1415 ? -18.925  27.649  101.810 1.00 154.72 ? 1415 SER B N   1 
ATOM   25137 C  CA  . SER C 1 1415 ? -20.326  27.858  101.485 1.00 153.09 ? 1415 SER B CA  1 
ATOM   25138 C  C   . SER C 1 1415 ? -20.719  27.353  100.087 1.00 153.47 ? 1415 SER B C   1 
ATOM   25139 O  O   . SER C 1 1415 ? -19.921  27.361  99.155  1.00 154.10 ? 1415 SER B O   1 
ATOM   25140 C  CB  . SER C 1 1415 ? -20.625  29.346  101.622 1.00 150.04 ? 1415 SER B CB  1 
ATOM   25141 O  OG  . SER C 1 1415 ? -21.659  29.756  100.766 1.00 149.67 ? 1415 SER B OG  1 
ATOM   25142 N  N   . SER C 1 1416 ? -21.969  26.933  99.939  1.00 154.52 ? 1416 SER B N   1 
ATOM   25143 C  CA  . SER C 1 1416 ? -22.457  26.385  98.667  1.00 156.08 ? 1416 SER B CA  1 
ATOM   25144 C  C   . SER C 1 1416 ? -22.754  27.408  97.558  1.00 154.30 ? 1416 SER B C   1 
ATOM   25145 O  O   . SER C 1 1416 ? -23.290  27.044  96.506  1.00 153.48 ? 1416 SER B O   1 
ATOM   25146 C  CB  . SER C 1 1416 ? -23.714  25.544  98.914  1.00 159.64 ? 1416 SER B CB  1 
ATOM   25147 O  OG  . SER C 1 1416 ? -24.665  26.266  99.678  1.00 160.04 ? 1416 SER B OG  1 
ATOM   25148 N  N   . SER C 1 1417 ? -22.417  28.673  97.798  1.00 153.12 ? 1417 SER B N   1 
ATOM   25149 C  CA  . SER C 1 1417 ? -22.815  29.762  96.905  1.00 152.23 ? 1417 SER B CA  1 
ATOM   25150 C  C   . SER C 1 1417 ? -22.029  29.767  95.602  1.00 148.53 ? 1417 SER B C   1 
ATOM   25151 O  O   . SER C 1 1417 ? -22.503  30.256  94.567  1.00 152.87 ? 1417 SER B O   1 
ATOM   25152 C  CB  . SER C 1 1417 ? -22.637  31.110  97.601  1.00 151.05 ? 1417 SER B CB  1 
ATOM   25153 O  OG  . SER C 1 1417 ? -21.304  31.262  98.062  1.00 150.45 ? 1417 SER B OG  1 
ATOM   25154 N  N   . GLY C 1 1418 ? -20.819  29.226  95.661  1.00 142.16 ? 1418 GLY B N   1 
ATOM   25155 C  CA  . GLY C 1 1418 ? -19.939  29.234  94.508  1.00 134.80 ? 1418 GLY B CA  1 
ATOM   25156 C  C   . GLY C 1 1418 ? -18.855  30.290  94.590  1.00 129.82 ? 1418 GLY B C   1 
ATOM   25157 O  O   . GLY C 1 1418 ? -18.791  31.068  95.540  1.00 127.25 ? 1418 GLY B O   1 
ATOM   25158 N  N   . SER C 1 1419 ? -18.011  30.335  93.572  1.00 129.02 ? 1419 SER B N   1 
ATOM   25159 C  CA  . SER C 1 1419 ? -16.769  31.074  93.671  1.00 123.88 ? 1419 SER B CA  1 
ATOM   25160 C  C   . SER C 1 1419 ? -16.864  32.580  93.825  1.00 116.92 ? 1419 SER B C   1 
ATOM   25161 O  O   . SER C 1 1419 ? -17.948  33.171  93.812  1.00 115.97 ? 1419 SER B O   1 
ATOM   25162 C  CB  . SER C 1 1419 ? -15.874  30.767  92.488  1.00 124.50 ? 1419 SER B CB  1 
ATOM   25163 O  OG  . SER C 1 1419 ? -14.659  31.483  92.634  1.00 121.26 ? 1419 SER B OG  1 
ATOM   25164 N  N   . SER C 1 1420 ? -15.681  33.166  94.007  1.00 109.82 ? 1420 SER B N   1 
ATOM   25165 C  CA  . SER C 1 1420 ? -15.467  34.609  94.043  1.00 104.46 ? 1420 SER B CA  1 
ATOM   25166 C  C   . SER C 1 1420 ? -15.167  35.061  92.642  1.00 104.47 ? 1420 SER B C   1 
ATOM   25167 O  O   . SER C 1 1420 ? -15.103  34.245  91.728  1.00 107.52 ? 1420 SER B O   1 
ATOM   25168 C  CB  . SER C 1 1420 ? -14.240  34.964  94.877  1.00 100.61 ? 1420 SER B CB  1 
ATOM   25169 O  OG  . SER C 1 1420 ? -13.100  35.131  94.029  1.00 97.98  ? 1420 SER B OG  1 
ATOM   25170 N  N   . HIS C 1 1421 ? -14.945  36.357  92.473  1.00 100.84 ? 1421 HIS B N   1 
ATOM   25171 C  CA  . HIS C 1 1421 ? -14.599  36.870  91.161  1.00 98.26  ? 1421 HIS B CA  1 
ATOM   25172 C  C   . HIS C 1 1421 ? -13.518  35.995  90.551  1.00 92.40  ? 1421 HIS B C   1 
ATOM   25173 O  O   . HIS C 1 1421 ? -12.436  35.835  91.139  1.00 88.95  ? 1421 HIS B O   1 
ATOM   25174 C  CB  . HIS C 1 1421 ? -14.193  38.341  91.274  1.00 99.38  ? 1421 HIS B CB  1 
ATOM   25175 C  CG  . HIS C 1 1421 ? -13.224  38.798  90.234  1.00 98.53  ? 1421 HIS B CG  1 
ATOM   25176 N  ND1 . HIS C 1 1421 ? -12.350  39.842  90.450  1.00 97.58  ? 1421 HIS B ND1 1 
ATOM   25177 C  CD2 . HIS C 1 1421 ? -12.981  38.353  88.983  1.00 98.66  ? 1421 HIS B CD2 1 
ATOM   25178 C  CE1 . HIS C 1 1421 ? -11.607  40.017  89.375  1.00 97.47  ? 1421 HIS B CE1 1 
ATOM   25179 N  NE2 . HIS C 1 1421 ? -11.970  39.125  88.471  1.00 98.16  ? 1421 HIS B NE2 1 
ATOM   25180 N  N   . ALA C 1 1422 ? -13.844  35.410  89.393  1.00 92.84  ? 1422 ALA B N   1 
ATOM   25181 C  CA  . ALA C 1 1422 ? -12.981  34.414  88.750  1.00 93.18  ? 1422 ALA B CA  1 
ATOM   25182 C  C   . ALA C 1 1422 ? -12.939  34.546  87.250  1.00 96.75  ? 1422 ALA B C   1 
ATOM   25183 O  O   . ALA C 1 1422 ? -13.808  35.183  86.650  1.00 97.47  ? 1422 ALA B O   1 
ATOM   25184 C  CB  . ALA C 1 1422 ? -13.422  33.045  89.083  1.00 95.42  ? 1422 ALA B CB  1 
ATOM   25185 N  N   . VAL C 1 1423 ? -11.924  33.931  86.647  1.00 100.11 ? 1423 VAL B N   1 
ATOM   25186 C  CA  . VAL C 1 1423 ? -11.744  34.021  85.207  1.00 102.77 ? 1423 VAL B CA  1 
ATOM   25187 C  C   . VAL C 1 1423 ? -11.617  32.629  84.639  1.00 107.92 ? 1423 VAL B C   1 
ATOM   25188 O  O   . VAL C 1 1423 ? -11.152  31.739  85.343  1.00 106.74 ? 1423 VAL B O   1 
ATOM   25189 C  CB  . VAL C 1 1423 ? -10.492  34.845  84.781  1.00 74.60  ? 1423 VAL B CB  1 
ATOM   25190 C  CG1 . VAL C 1 1423 ? -10.124  35.846  85.826  1.00 79.63  ? 1423 VAL B CG1 1 
ATOM   25191 C  CG2 . VAL C 1 1423 ? -9.340   33.949  84.453  1.00 75.37  ? 1423 VAL B CG2 1 
ATOM   25192 N  N   . MET C 1 1424 ? -12.122  32.458  83.403  1.00 103.84 ? 1424 MET B N   1 
ATOM   25193 C  CA  . MET C 1 1424 ? -11.883  31.306  82.518  1.00 99.80  ? 1424 MET B CA  1 
ATOM   25194 C  C   . MET C 1 1424 ? -10.981  31.771  81.369  1.00 102.91 ? 1424 MET B C   1 
ATOM   25195 O  O   . MET C 1 1424 ? -11.106  32.892  80.868  1.00 101.99 ? 1424 MET B O   1 
ATOM   25196 C  CB  . MET C 1 1424 ? -13.203  30.771  81.976  1.00 95.71  ? 1424 MET B CB  1 
ATOM   25197 C  CG  . MET C 1 1424 ? -14.363  31.134  82.869  1.00 92.81  ? 1424 MET B CG  1 
ATOM   25198 S  SD  . MET C 1 1424 ? -15.980  30.522  82.371  1.00 100.93 ? 1424 MET B SD  1 
ATOM   25199 C  CE  . MET C 1 1424 ? -15.597  28.860  81.808  1.00 91.59  ? 1424 MET B CE  1 
ATOM   25200 N  N   . ASP C 1 1425 ? -10.065  30.915  80.951  1.00 103.94 ? 1425 ASP B N   1 
ATOM   25201 C  CA  . ASP C 1 1425 ? -9.038   31.323  80.009  1.00 105.98 ? 1425 ASP B CA  1 
ATOM   25202 C  C   . ASP C 1 1425 ? -8.864   30.199  78.998  1.00 110.17 ? 1425 ASP B C   1 
ATOM   25203 O  O   . ASP C 1 1425 ? -8.253   29.163  79.299  1.00 113.53 ? 1425 ASP B O   1 
ATOM   25204 C  CB  . ASP C 1 1425 ? -7.743   31.591  80.781  1.00 107.14 ? 1425 ASP B CB  1 
ATOM   25205 C  CG  . ASP C 1 1425 ? -6.522   31.776  79.890  1.00 109.76 ? 1425 ASP B CG  1 
ATOM   25206 O  OD1 . ASP C 1 1425 ? -5.540   32.378  80.373  1.00 109.79 ? 1425 ASP B OD1 1 
ATOM   25207 O  OD2 . ASP C 1 1425 ? -6.512   31.313  78.735  1.00 112.22 ? 1425 ASP B OD2 1 
ATOM   25208 N  N   . ILE C 1 1426 ? -9.420   30.407  77.805  1.00 108.14 ? 1426 ILE B N   1 
ATOM   25209 C  CA  . ILE C 1 1426 ? -9.281   29.459  76.715  1.00 105.96 ? 1426 ILE B CA  1 
ATOM   25210 C  C   . ILE C 1 1426 ? -8.209   29.847  75.712  1.00 103.18 ? 1426 ILE B C   1 
ATOM   25211 O  O   . ILE C 1 1426 ? -8.318   30.874  75.044  1.00 101.23 ? 1426 ILE B O   1 
ATOM   25212 C  CB  . ILE C 1 1426 ? -10.568  29.344  75.959  1.00 105.55 ? 1426 ILE B CB  1 
ATOM   25213 C  CG1 . ILE C 1 1426 ? -11.719  29.335  76.946  1.00 104.87 ? 1426 ILE B CG1 1 
ATOM   25214 C  CG2 . ILE C 1 1426 ? -10.551  28.086  75.085  1.00 108.47 ? 1426 ILE B CG2 1 
ATOM   25215 C  CD1 . ILE C 1 1426 ? -12.902  28.568  76.454  1.00 106.25 ? 1426 ILE B CD1 1 
ATOM   25216 N  N   . SER C 1 1427 ? -7.172   29.018  75.641  1.00 102.93 ? 1427 SER B N   1 
ATOM   25217 C  CA  . SER C 1 1427 ? -6.141   29.084  74.616  1.00 101.26 ? 1427 SER B CA  1 
ATOM   25218 C  C   . SER C 1 1427 ? -6.845   28.625  73.336  1.00 100.75 ? 1427 SER B C   1 
ATOM   25219 O  O   . SER C 1 1427 ? -7.614   27.661  73.371  1.00 103.20 ? 1427 SER B O   1 
ATOM   25220 C  CB  . SER C 1 1427 ? -4.979   28.150  75.042  1.00 93.25  ? 1427 SER B CB  1 
ATOM   25221 O  OG  . SER C 1 1427 ? -4.005   27.863  74.042  1.00 93.66  ? 1427 SER B OG  1 
ATOM   25222 N  N   . LEU C 1 1428 ? -6.650   29.340  72.229  1.00 97.64  ? 1428 LEU B N   1 
ATOM   25223 C  CA  . LEU C 1 1428 ? -7.192   28.892  70.939  1.00 97.48  ? 1428 LEU B CA  1 
ATOM   25224 C  C   . LEU C 1 1428 ? -6.102   28.150  70.221  1.00 99.47  ? 1428 LEU B C   1 
ATOM   25225 O  O   . LEU C 1 1428 ? -4.934   28.554  70.317  1.00 97.72  ? 1428 LEU B O   1 
ATOM   25226 C  CB  . LEU C 1 1428 ? -7.684   30.055  70.075  1.00 93.29  ? 1428 LEU B CB  1 
ATOM   25227 C  CG  . LEU C 1 1428 ? -8.770   30.800  70.847  1.00 90.21  ? 1428 LEU B CG  1 
ATOM   25228 C  CD1 . LEU C 1 1428 ? -9.151   32.103  70.181  1.00 90.01  ? 1428 LEU B CD1 1 
ATOM   25229 C  CD2 . LEU C 1 1428 ? -9.972   29.892  71.051  1.00 90.11  ? 1428 LEU B CD2 1 
ATOM   25230 N  N   . PRO C 1 1429 ? -6.467   27.034  69.546  1.00 99.94  ? 1429 PRO B N   1 
ATOM   25231 C  CA  . PRO C 1 1429 ? -5.557   26.225  68.722  1.00 100.18 ? 1429 PRO B CA  1 
ATOM   25232 C  C   . PRO C 1 1429 ? -4.996   27.042  67.580  1.00 99.04  ? 1429 PRO B C   1 
ATOM   25233 O  O   . PRO C 1 1429 ? -5.610   28.015  67.156  1.00 96.39  ? 1429 PRO B O   1 
ATOM   25234 C  CB  . PRO C 1 1429 ? -6.451   25.096  68.203  1.00 100.77 ? 1429 PRO B CB  1 
ATOM   25235 C  CG  . PRO C 1 1429 ? -7.453   24.948  69.261  1.00 101.22 ? 1429 PRO B CG  1 
ATOM   25236 C  CD  . PRO C 1 1429 ? -7.738   26.331  69.773  1.00 99.53  ? 1429 PRO B CD  1 
ATOM   25237 N  N   . THR C 1 1430 ? -3.818   26.657  67.120  1.00 100.41 ? 1430 THR B N   1 
ATOM   25238 C  CA  . THR C 1 1430 ? -3.042   27.502  66.242  1.00 100.05 ? 1430 THR B CA  1 
ATOM   25239 C  C   . THR C 1 1430 ? -3.863   27.828  64.991  1.00 104.57 ? 1430 THR B C   1 
ATOM   25240 O  O   . THR C 1 1430 ? -4.303   26.934  64.260  1.00 108.59 ? 1430 THR B O   1 
ATOM   25241 C  CB  . THR C 1 1430 ? -1.684   26.838  65.921  1.00 99.24  ? 1430 THR B CB  1 
ATOM   25242 O  OG1 . THR C 1 1430 ? -1.313   25.942  66.982  1.00 98.44  ? 1430 THR B OG1 1 
ATOM   25243 C  CG2 . THR C 1 1430 ? -0.600   27.873  65.758  1.00 96.69  ? 1430 THR B CG2 1 
ATOM   25244 N  N   . GLY C 1 1431 ? -4.100   29.124  64.789  1.00 104.43 ? 1431 GLY B N   1 
ATOM   25245 C  CA  . GLY C 1 1431 ? -4.947   29.631  63.712  1.00 105.52 ? 1431 GLY B CA  1 
ATOM   25246 C  C   . GLY C 1 1431 ? -6.409   29.203  63.752  1.00 106.42 ? 1431 GLY B C   1 
ATOM   25247 O  O   . GLY C 1 1431 ? -6.819   28.373  62.968  1.00 104.66 ? 1431 GLY B O   1 
ATOM   25248 N  N   . ILE C 1 1432 ? -7.188   29.783  64.662  1.00 111.57 ? 1432 ILE B N   1 
ATOM   25249 C  CA  . ILE C 1 1432 ? -8.588   29.436  64.856  1.00 115.74 ? 1432 ILE B CA  1 
ATOM   25250 C  C   . ILE C 1 1432 ? -9.288   30.588  65.562  1.00 117.29 ? 1432 ILE B C   1 
ATOM   25251 O  O   . ILE C 1 1432 ? -9.738   30.417  66.681  1.00 119.66 ? 1432 ILE B O   1 
ATOM   25252 C  CB  . ILE C 1 1432 ? -8.739   28.225  65.814  1.00 99.92  ? 1432 ILE B CB  1 
ATOM   25253 C  CG1 . ILE C 1 1432 ? -7.776   27.086  65.436  1.00 105.89 ? 1432 ILE B CG1 1 
ATOM   25254 C  CG2 . ILE C 1 1432 ? -10.198  27.771  65.909  1.00 98.30  ? 1432 ILE B CG2 1 
ATOM   25255 C  CD1 . ILE C 1 1432 ? -8.250   26.140  64.318  1.00 111.61 ? 1432 ILE B CD1 1 
ATOM   25256 N  N   . SER C 1 1433 ? -9.372   31.759  64.926  1.00 115.21 ? 1433 SER B N   1 
ATOM   25257 C  CA  . SER C 1 1433 ? -9.985   32.976  65.515  1.00 112.96 ? 1433 SER B CA  1 
ATOM   25258 C  C   . SER C 1 1433 ? -11.315  32.734  66.227  1.00 111.67 ? 1433 SER B C   1 
ATOM   25259 O  O   . SER C 1 1433 ? -12.125  31.947  65.769  1.00 112.48 ? 1433 SER B O   1 
ATOM   25260 C  CB  . SER C 1 1433 ? -10.241  34.029  64.422  1.00 113.89 ? 1433 SER B CB  1 
ATOM   25261 O  OG  . SER C 1 1433 ? -9.114   34.217  63.574  1.00 114.91 ? 1433 SER B OG  1 
ATOM   25262 N  N   . ALA C 1 1434 ? -11.561  33.415  67.335  1.00 111.74 ? 1434 ALA B N   1 
ATOM   25263 C  CA  . ALA C 1 1434 ? -12.837  33.233  68.013  1.00 116.00 ? 1434 ALA B CA  1 
ATOM   25264 C  C   . ALA C 1 1434 ? -13.805  34.270  67.522  1.00 116.92 ? 1434 ALA B C   1 
ATOM   25265 O  O   . ALA C 1 1434 ? -13.402  35.203  66.836  1.00 118.04 ? 1434 ALA B O   1 
ATOM   25266 C  CB  . ALA C 1 1434 ? -12.677  33.335  69.502  1.00 117.42 ? 1434 ALA B CB  1 
ATOM   25267 N  N   . ASN C 1 1435 ? -15.078  34.118  67.880  1.00 118.09 ? 1435 ASN B N   1 
ATOM   25268 C  CA  . ASN C 1 1435 ? -16.134  34.987  67.346  1.00 117.90 ? 1435 ASN B CA  1 
ATOM   25269 C  C   . ASN C 1 1435 ? -16.415  36.259  68.163  1.00 116.79 ? 1435 ASN B C   1 
ATOM   25270 O  O   . ASN C 1 1435 ? -17.413  36.345  68.880  1.00 115.04 ? 1435 ASN B O   1 
ATOM   25271 C  CB  . ASN C 1 1435 ? -17.432  34.197  67.136  1.00 121.14 ? 1435 ASN B CB  1 
ATOM   25272 C  CG  . ASN C 1 1435 ? -18.467  34.987  66.357  1.00 123.23 ? 1435 ASN B CG  1 
ATOM   25273 O  OD1 . ASN C 1 1435 ? -18.277  36.169  66.090  1.00 121.98 ? 1435 ASN B OD1 1 
ATOM   25274 N  ND2 . ASN C 1 1435 ? -19.565  34.336  65.980  1.00 126.32 ? 1435 ASN B ND2 1 
ATOM   25275 N  N   . GLU C 1 1436 ? -15.551  37.257  68.019  1.00 117.02 ? 1436 GLU B N   1 
ATOM   25276 C  CA  . GLU C 1 1436 ? -15.651  38.458  68.829  1.00 117.52 ? 1436 GLU B CA  1 
ATOM   25277 C  C   . GLU C 1 1436 ? -17.103  38.796  69.162  1.00 117.06 ? 1436 GLU B C   1 
ATOM   25278 O  O   . GLU C 1 1436 ? -17.434  39.064  70.306  1.00 116.01 ? 1436 GLU B O   1 
ATOM   25279 C  CB  . GLU C 1 1436 ? -14.979  39.627  68.114  1.00 120.35 ? 1436 GLU B CB  1 
ATOM   25280 C  CG  . GLU C 1 1436 ? -14.814  40.878  68.968  1.00 121.80 ? 1436 GLU B CG  1 
ATOM   25281 C  CD  . GLU C 1 1436 ? -13.374  41.101  69.450  1.00 122.85 ? 1436 GLU B CD  1 
ATOM   25282 O  OE1 . GLU C 1 1436 ? -12.559  40.142  69.391  1.00 124.74 ? 1436 GLU B OE1 1 
ATOM   25283 O  OE2 . GLU C 1 1436 ? -13.058  42.244  69.875  1.00 120.78 ? 1436 GLU B OE2 1 
ATOM   25284 N  N   . GLU C 1 1437 ? -17.974  38.753  68.161  1.00 117.35 ? 1437 GLU B N   1 
ATOM   25285 C  CA  . GLU C 1 1437 ? -19.358  39.199  68.324  1.00 117.03 ? 1437 GLU B CA  1 
ATOM   25286 C  C   . GLU C 1 1437 ? -20.103  38.287  69.282  1.00 118.64 ? 1437 GLU B C   1 
ATOM   25287 O  O   . GLU C 1 1437 ? -20.869  38.755  70.112  1.00 119.31 ? 1437 GLU B O   1 
ATOM   25288 C  CB  . GLU C 1 1437 ? -20.097  39.271  66.972  1.00 115.46 ? 1437 GLU B CB  1 
ATOM   25289 C  CG  . GLU C 1 1437 ? -19.174  39.392  65.732  1.00 164.38 ? 1437 GLU B CG  1 
ATOM   25290 C  CD  . GLU C 1 1437 ? -18.466  40.744  65.613  1.00 158.78 ? 1437 GLU B CD  1 
ATOM   25291 O  OE1 . GLU C 1 1437 ? -19.130  41.766  65.918  1.00 157.04 ? 1437 GLU B OE1 1 
ATOM   25292 O  OE2 . GLU C 1 1437 ? -17.266  40.776  65.205  1.00 155.02 ? 1437 GLU B OE2 1 
ATOM   25293 N  N   . ASP C 1 1438 ? -19.873  36.985  69.170  1.00 121.37 ? 1438 ASP B N   1 
ATOM   25294 C  CA  . ASP C 1 1438 ? -20.537  36.026  70.042  1.00 123.23 ? 1438 ASP B CA  1 
ATOM   25295 C  C   . ASP C 1 1438 ? -20.294  36.388  71.497  1.00 119.60 ? 1438 ASP B C   1 
ATOM   25296 O  O   . ASP C 1 1438 ? -21.214  36.333  72.309  1.00 120.95 ? 1438 ASP B O   1 
ATOM   25297 C  CB  . ASP C 1 1438 ? -20.020  34.603  69.785  1.00 125.95 ? 1438 ASP B CB  1 
ATOM   25298 C  CG  . ASP C 1 1438 ? -20.640  33.957  68.563  1.00 127.84 ? 1438 ASP B CG  1 
ATOM   25299 O  OD1 . ASP C 1 1438 ? -21.661  34.464  68.074  1.00 128.03 ? 1438 ASP B OD1 1 
ATOM   25300 O  OD2 . ASP C 1 1438 ? -20.105  32.934  68.090  1.00 128.55 ? 1438 ASP B OD2 1 
ATOM   25301 N  N   . LEU C 1 1439 ? -19.043  36.747  71.803  1.00 113.91 ? 1439 LEU B N   1 
ATOM   25302 C  CA  . LEU C 1 1439 ? -18.589  37.021  73.158  1.00 107.89 ? 1439 LEU B CA  1 
ATOM   25303 C  C   . LEU C 1 1439 ? -19.137  38.343  73.656  1.00 106.96 ? 1439 LEU B C   1 
ATOM   25304 O  O   . LEU C 1 1439 ? -19.617  38.438  74.782  1.00 106.68 ? 1439 LEU B O   1 
ATOM   25305 C  CB  . LEU C 1 1439 ? -17.063  37.045  73.197  1.00 104.66 ? 1439 LEU B CB  1 
ATOM   25306 C  CG  . LEU C 1 1439 ? -16.319  35.762  72.811  1.00 103.34 ? 1439 LEU B CG  1 
ATOM   25307 C  CD1 . LEU C 1 1439 ? -14.830  36.008  72.620  1.00 101.40 ? 1439 LEU B CD1 1 
ATOM   25308 C  CD2 . LEU C 1 1439 ? -16.529  34.702  73.868  1.00 103.41 ? 1439 LEU B CD2 1 
ATOM   25309 N  N   . LYS C 1 1440 ? -19.054  39.365  72.806  1.00 107.36 ? 1440 LYS B N   1 
ATOM   25310 C  CA  . LYS C 1 1440 ? -19.703  40.653  73.058  1.00 107.73 ? 1440 LYS B CA  1 
ATOM   25311 C  C   . LYS C 1 1440 ? -21.120  40.362  73.501  1.00 107.16 ? 1440 LYS B C   1 
ATOM   25312 O  O   . LYS C 1 1440 ? -21.656  41.019  74.381  1.00 104.55 ? 1440 LYS B O   1 
ATOM   25313 C  CB  . LYS C 1 1440 ? -19.769  41.504  71.781  1.00 113.17 ? 1440 LYS B CB  1 
ATOM   25314 C  CG  . LYS C 1 1440 ? -18.451  42.125  71.287  1.00 117.79 ? 1440 LYS B CG  1 
ATOM   25315 C  CD  . LYS C 1 1440 ? -18.110  43.446  71.996  1.00 120.34 ? 1440 LYS B CD  1 
ATOM   25316 C  CE  . LYS C 1 1440 ? -17.736  44.597  71.023  1.00 131.36 ? 1440 LYS B CE  1 
ATOM   25317 N  NZ  . LYS C 1 1440 ? -16.857  44.259  69.851  1.00 131.57 ? 1440 LYS B NZ  1 
ATOM   25318 N  N   . ALA C 1 1441 ? -21.716  39.357  72.872  1.00 109.22 ? 1441 ALA B N   1 
ATOM   25319 C  CA  . ALA C 1 1441 ? -23.089  38.965  73.135  1.00 113.03 ? 1441 ALA B CA  1 
ATOM   25320 C  C   . ALA C 1 1441 ? -23.283  38.606  74.584  1.00 116.58 ? 1441 ALA B C   1 
ATOM   25321 O  O   . ALA C 1 1441 ? -24.333  38.870  75.156  1.00 118.87 ? 1441 ALA B O   1 
ATOM   25322 C  CB  . ALA C 1 1441 ? -23.462  37.776  72.268  1.00 114.01 ? 1441 ALA B CB  1 
ATOM   25323 N  N   . LEU C 1 1442 ? -22.271  37.983  75.171  1.00 118.22 ? 1442 LEU B N   1 
ATOM   25324 C  CA  . LEU C 1 1442 ? -22.414  37.414  76.493  1.00 120.42 ? 1442 LEU B CA  1 
ATOM   25325 C  C   . LEU C 1 1442 ? -22.319  38.442  77.590  1.00 124.95 ? 1442 LEU B C   1 
ATOM   25326 O  O   . LEU C 1 1442 ? -23.116  38.420  78.519  1.00 129.86 ? 1442 LEU B O   1 
ATOM   25327 C  CB  . LEU C 1 1442 ? -21.380  36.337  76.691  1.00 116.06 ? 1442 LEU B CB  1 
ATOM   25328 C  CG  . LEU C 1 1442 ? -21.964  35.150  75.968  1.00 116.19 ? 1442 LEU B CG  1 
ATOM   25329 C  CD1 . LEU C 1 1442 ? -20.870  34.181  75.612  1.00 116.83 ? 1442 LEU B CD1 1 
ATOM   25330 C  CD2 . LEU C 1 1442 ? -23.043  34.523  76.843  1.00 117.62 ? 1442 LEU B CD2 1 
ATOM   25331 N  N   . VAL C 1 1443 ? -21.355  39.351  77.475  1.00 126.58 ? 1443 VAL B N   1 
ATOM   25332 C  CA  . VAL C 1 1443 ? -21.093  40.337  78.524  1.00 126.41 ? 1443 VAL B CA  1 
ATOM   25333 C  C   . VAL C 1 1443 ? -21.925  41.626  78.401  1.00 129.18 ? 1443 VAL B C   1 
ATOM   25334 O  O   . VAL C 1 1443 ? -22.093  42.357  79.376  1.00 127.90 ? 1443 VAL B O   1 
ATOM   25335 C  CB  . VAL C 1 1443 ? -19.593  40.730  78.556  1.00 128.19 ? 1443 VAL B CB  1 
ATOM   25336 C  CG1 . VAL C 1 1443 ? -18.775  39.757  77.733  1.00 128.65 ? 1443 VAL B CG1 1 
ATOM   25337 C  CG2 . VAL C 1 1443 ? -19.389  42.142  78.027  1.00 126.94 ? 1443 VAL B CG2 1 
ATOM   25338 N  N   . GLU C 1 1444 ? -22.448  41.899  77.213  1.00 130.59 ? 1444 GLU B N   1 
ATOM   25339 C  CA  . GLU C 1 1444 ? -22.897  43.239  76.884  1.00 133.28 ? 1444 GLU B CA  1 
ATOM   25340 C  C   . GLU C 1 1444 ? -24.356  43.466  77.192  1.00 131.63 ? 1444 GLU B C   1 
ATOM   25341 O  O   . GLU C 1 1444 ? -24.908  44.500  76.837  1.00 128.90 ? 1444 GLU B O   1 
ATOM   25342 C  CB  . GLU C 1 1444 ? -22.626  43.494  75.409  1.00 141.69 ? 1444 GLU B CB  1 
ATOM   25343 C  CG  . GLU C 1 1444 ? -22.754  44.930  74.957  1.00 147.75 ? 1444 GLU B CG  1 
ATOM   25344 C  CD  . GLU C 1 1444 ? -21.923  45.205  73.708  1.00 152.31 ? 1444 GLU B CD  1 
ATOM   25345 O  OE1 . GLU C 1 1444 ? -20.717  44.853  73.723  1.00 152.56 ? 1444 GLU B OE1 1 
ATOM   25346 O  OE2 . GLU C 1 1444 ? -22.472  45.772  72.724  1.00 154.19 ? 1444 GLU B OE2 1 
ATOM   25347 N  N   . GLY C 1 1445 ? -24.983  42.511  77.863  1.00 133.63 ? 1445 GLY B N   1 
ATOM   25348 C  CA  . GLY C 1 1445 ? -26.416  42.588  78.061  1.00 137.89 ? 1445 GLY B CA  1 
ATOM   25349 C  C   . GLY C 1 1445 ? -26.868  42.419  79.490  1.00 139.39 ? 1445 GLY B C   1 
ATOM   25350 O  O   . GLY C 1 1445 ? -26.190  41.783  80.287  1.00 140.86 ? 1445 GLY B O   1 
ATOM   25351 N  N   . VAL C 1 1446 ? -28.022  42.995  79.816  1.00 140.66 ? 1446 VAL B N   1 
ATOM   25352 C  CA  . VAL C 1 1446 ? -28.589  42.866  81.157  1.00 141.41 ? 1446 VAL B CA  1 
ATOM   25353 C  C   . VAL C 1 1446 ? -28.627  41.413  81.596  1.00 140.85 ? 1446 VAL B C   1 
ATOM   25354 O  O   . VAL C 1 1446 ? -28.589  41.110  82.783  1.00 140.18 ? 1446 VAL B O   1 
ATOM   25355 C  CB  . VAL C 1 1446 ? -30.029  43.400  81.227  1.00 143.74 ? 1446 VAL B CB  1 
ATOM   25356 C  CG1 . VAL C 1 1446 ? -30.506  43.420  82.679  1.00 145.07 ? 1446 VAL B CG1 1 
ATOM   25357 C  CG2 . VAL C 1 1446 ? -30.122  44.781  80.594  1.00 142.70 ? 1446 VAL B CG2 1 
ATOM   25358 N  N   . ASP C 1 1447 ? -28.727  40.519  80.624  1.00 141.68 ? 1447 ASP B N   1 
ATOM   25359 C  CA  . ASP C 1 1447 ? -28.668  39.102  80.903  1.00 143.63 ? 1447 ASP B CA  1 
ATOM   25360 C  C   . ASP C 1 1447 ? -27.215  38.672  81.036  1.00 141.36 ? 1447 ASP B C   1 
ATOM   25361 O  O   . ASP C 1 1447 ? -26.899  37.489  80.962  1.00 142.34 ? 1447 ASP B O   1 
ATOM   25362 C  CB  . ASP C 1 1447 ? -29.391  38.297  79.812  1.00 148.32 ? 1447 ASP B CB  1 
ATOM   25363 C  CG  . ASP C 1 1447 ? -28.862  38.581  78.409  1.00 149.69 ? 1447 ASP B CG  1 
ATOM   25364 O  OD1 . ASP C 1 1447 ? -28.169  39.608  78.221  1.00 147.85 ? 1447 ASP B OD1 1 
ATOM   25365 O  OD2 . ASP C 1 1447 ? -29.151  37.770  77.494  1.00 152.61 ? 1447 ASP B OD2 1 
ATOM   25366 N  N   . GLN C 1 1448 ? -26.327  39.635  81.249  1.00 137.93 ? 1448 GLN B N   1 
ATOM   25367 C  CA  . GLN C 1 1448 ? -24.906  39.344  81.156  1.00 136.05 ? 1448 GLN B CA  1 
ATOM   25368 C  C   . GLN C 1 1448 ? -24.548  38.084  81.904  1.00 135.25 ? 1448 GLN B C   1 
ATOM   25369 O  O   . GLN C 1 1448 ? -24.804  37.956  83.091  1.00 136.12 ? 1448 GLN B O   1 
ATOM   25370 C  CB  . GLN C 1 1448 ? -24.037  40.516  81.612  1.00 134.54 ? 1448 GLN B CB  1 
ATOM   25371 C  CG  . GLN C 1 1448 ? -24.156  40.914  83.055  1.00 135.74 ? 1448 GLN B CG  1 
ATOM   25372 C  CD  . GLN C 1 1448 ? -23.080  41.913  83.457  1.00 135.72 ? 1448 GLN B CD  1 
ATOM   25373 O  OE1 . GLN C 1 1448 ? -21.903  41.738  83.128  1.00 135.46 ? 1448 GLN B OE1 1 
ATOM   25374 N  NE2 . GLN C 1 1448 ? -23.477  42.967  84.172  1.00 135.92 ? 1448 GLN B NE2 1 
ATOM   25375 N  N   . LEU C 1 1449 ? -23.985  37.139  81.170  1.00 135.15 ? 1449 LEU B N   1 
ATOM   25376 C  CA  . LEU C 1 1449 ? -23.490  35.899  81.736  1.00 137.18 ? 1449 LEU B CA  1 
ATOM   25377 C  C   . LEU C 1 1449 ? -22.065  36.133  82.227  1.00 131.50 ? 1449 LEU B C   1 
ATOM   25378 O  O   . LEU C 1 1449 ? -21.691  35.725  83.331  1.00 129.91 ? 1449 LEU B O   1 
ATOM   25379 C  CB  . LEU C 1 1449 ? -23.539  34.797  80.670  1.00 144.06 ? 1449 LEU B CB  1 
ATOM   25380 C  CG  . LEU C 1 1449 ? -22.914  33.423  80.928  1.00 149.22 ? 1449 LEU B CG  1 
ATOM   25381 C  CD1 . LEU C 1 1449 ? -23.326  32.880  82.290  1.00 151.48 ? 1449 LEU B CD1 1 
ATOM   25382 C  CD2 . LEU C 1 1449 ? -23.273  32.454  79.797  1.00 152.82 ? 1449 LEU B CD2 1 
ATOM   25383 N  N   . PHE C 1 1450 ? -21.272  36.795  81.392  1.00 128.24 ? 1450 PHE B N   1 
ATOM   25384 C  CA  . PHE C 1 1450 ? -19.943  37.226  81.785  1.00 124.47 ? 1450 PHE B CA  1 
ATOM   25385 C  C   . PHE C 1 1450 ? -19.934  38.736  81.944  1.00 122.04 ? 1450 PHE B C   1 
ATOM   25386 O  O   . PHE C 1 1450 ? -20.920  39.408  81.624  1.00 122.38 ? 1450 PHE B O   1 
ATOM   25387 C  CB  . PHE C 1 1450 ? -18.910  36.754  80.775  1.00 121.75 ? 1450 PHE B CB  1 
ATOM   25388 C  CG  . PHE C 1 1450 ? -18.919  35.284  80.590  1.00 122.37 ? 1450 PHE B CG  1 
ATOM   25389 C  CD1 . PHE C 1 1450 ? -19.885  34.681  79.804  1.00 124.21 ? 1450 PHE B CD1 1 
ATOM   25390 C  CD2 . PHE C 1 1450 ? -18.001  34.490  81.232  1.00 121.33 ? 1450 PHE B CD2 1 
ATOM   25391 C  CE1 . PHE C 1 1450 ? -19.920  33.295  79.632  1.00 125.55 ? 1450 PHE B CE1 1 
ATOM   25392 C  CE2 . PHE C 1 1450 ? -18.029  33.110  81.068  1.00 123.72 ? 1450 PHE B CE2 1 
ATOM   25393 C  CZ  . PHE C 1 1450 ? -18.996  32.513  80.261  1.00 125.12 ? 1450 PHE B CZ  1 
ATOM   25394 N  N   . THR C 1 1451 ? -18.831  39.267  82.458  1.00 118.89 ? 1451 THR B N   1 
ATOM   25395 C  CA  . THR C 1 1451 ? -18.763  40.683  82.752  1.00 114.20 ? 1451 THR B CA  1 
ATOM   25396 C  C   . THR C 1 1451 ? -17.602  41.234  81.972  1.00 112.29 ? 1451 THR B C   1 
ATOM   25397 O  O   . THR C 1 1451 ? -17.420  42.452  81.879  1.00 110.05 ? 1451 THR B O   1 
ATOM   25398 C  CB  . THR C 1 1451 ? -18.521  40.948  84.258  1.00 111.43 ? 1451 THR B CB  1 
ATOM   25399 O  OG1 . THR C 1 1451 ? -17.113  40.988  84.519  1.00 109.23 ? 1451 THR B OG1 1 
ATOM   25400 C  CG2 . THR C 1 1451 ? -19.174  39.868  85.124  1.00 111.96 ? 1451 THR B CG2 1 
ATOM   25401 N  N   . ASP C 1 1452 ? -16.812  40.331  81.405  1.00 112.71 ? 1452 ASP B N   1 
ATOM   25402 C  CA  . ASP C 1 1452 ? -15.655  40.798  80.680  1.00 110.96 ? 1452 ASP B CA  1 
ATOM   25403 C  C   . ASP C 1 1452 ? -14.873  39.777  79.868  1.00 114.00 ? 1452 ASP B C   1 
ATOM   25404 O  O   . ASP C 1 1452 ? -14.230  38.874  80.413  1.00 114.15 ? 1452 ASP B O   1 
ATOM   25405 C  CB  . ASP C 1 1452 ? -14.704  41.487  81.631  1.00 106.57 ? 1452 ASP B CB  1 
ATOM   25406 C  CG  . ASP C 1 1452 ? -13.862  42.475  80.930  1.00 101.42 ? 1452 ASP B CG  1 
ATOM   25407 O  OD1 . ASP C 1 1452 ? -12.669  42.189  80.708  1.00 101.35 ? 1452 ASP B OD1 1 
ATOM   25408 O  OD2 . ASP C 1 1452 ? -14.416  43.525  80.568  1.00 97.52  ? 1452 ASP B OD2 1 
ATOM   25409 N  N   . TYR C 1 1453 ? -14.914  39.975  78.551  1.00 115.25 ? 1453 TYR B N   1 
ATOM   25410 C  CA  . TYR C 1 1453 ? -14.174  39.165  77.590  1.00 115.88 ? 1453 TYR B CA  1 
ATOM   25411 C  C   . TYR C 1 1453 ? -12.990  39.952  77.025  1.00 114.18 ? 1453 TYR B C   1 
ATOM   25412 O  O   . TYR C 1 1453 ? -12.937  41.176  77.130  1.00 112.58 ? 1453 TYR B O   1 
ATOM   25413 C  CB  . TYR C 1 1453 ? -15.098  38.697  76.444  1.00 116.98 ? 1453 TYR B CB  1 
ATOM   25414 C  CG  . TYR C 1 1453 ? -15.118  39.645  75.285  1.00 116.76 ? 1453 TYR B CG  1 
ATOM   25415 C  CD1 . TYR C 1 1453 ? -15.778  40.843  75.381  1.00 117.82 ? 1453 TYR B CD1 1 
ATOM   25416 C  CD2 . TYR C 1 1453 ? -14.444  39.361  74.114  1.00 117.48 ? 1453 TYR B CD2 1 
ATOM   25417 C  CE1 . TYR C 1 1453 ? -15.785  41.746  74.340  1.00 119.36 ? 1453 TYR B CE1 1 
ATOM   25418 C  CE2 . TYR C 1 1453 ? -14.442  40.253  73.059  1.00 119.27 ? 1453 TYR B CE2 1 
ATOM   25419 C  CZ  . TYR C 1 1453 ? -15.124  41.456  73.176  1.00 118.35 ? 1453 TYR B CZ  1 
ATOM   25420 O  OH  . TYR C 1 1453 ? -15.157  42.386  72.151  1.00 115.34 ? 1453 TYR B OH  1 
ATOM   25421 N  N   . GLN C 1 1454 ? -12.045  39.234  76.433  1.00 113.44 ? 1454 GLN B N   1 
ATOM   25422 C  CA  . GLN C 1 1454 ? -10.932  39.845  75.728  1.00 112.25 ? 1454 GLN B CA  1 
ATOM   25423 C  C   . GLN C 1 1454 ? -10.103  38.773  75.025  1.00 111.45 ? 1454 GLN B C   1 
ATOM   25424 O  O   . GLN C 1 1454 ? -9.833   37.716  75.600  1.00 112.42 ? 1454 GLN B O   1 
ATOM   25425 C  CB  . GLN C 1 1454 ? -10.059  40.625  76.702  1.00 111.37 ? 1454 GLN B CB  1 
ATOM   25426 C  CG  . GLN C 1 1454 ? -9.679   39.860  77.951  1.00 113.30 ? 1454 GLN B CG  1 
ATOM   25427 C  CD  . GLN C 1 1454 ? -8.547   40.529  78.709  1.00 113.99 ? 1454 GLN B CD  1 
ATOM   25428 O  OE1 . GLN C 1 1454 ? -7.591   41.032  78.109  1.00 112.77 ? 1454 GLN B OE1 1 
ATOM   25429 N  NE2 . GLN C 1 1454 ? -8.649   40.537  80.035  1.00 114.88 ? 1454 GLN B NE2 1 
ATOM   25430 N  N   . ILE C 1 1455 ? -9.728   39.019  73.771  1.00 111.13 ? 1455 ILE B N   1 
ATOM   25431 C  CA  . ILE C 1 1455 ? -8.809   38.112  73.083  1.00 110.34 ? 1455 ILE B CA  1 
ATOM   25432 C  C   . ILE C 1 1455 ? -7.407   38.685  73.038  1.00 109.60 ? 1455 ILE B C   1 
ATOM   25433 O  O   . ILE C 1 1455 ? -7.070   39.437  72.115  1.00 108.16 ? 1455 ILE B O   1 
ATOM   25434 C  CB  . ILE C 1 1455 ? -9.217   37.780  71.621  1.00 118.18 ? 1455 ILE B CB  1 
ATOM   25435 C  CG1 . ILE C 1 1455 ? -10.461  36.896  71.583  1.00 120.27 ? 1455 ILE B CG1 1 
ATOM   25436 C  CG2 . ILE C 1 1455 ? -8.085   37.042  70.912  1.00 118.91 ? 1455 ILE B CG2 1 
ATOM   25437 C  CD1 . ILE C 1 1455 ? -11.753  37.672  71.620  1.00 120.72 ? 1455 ILE B CD1 1 
ATOM   25438 N  N   . LYS C 1 1456 ? -6.599   38.333  74.037  1.00 109.08 ? 1456 LYS B N   1 
ATOM   25439 C  CA  . LYS C 1 1456 ? -5.182   38.653  74.019  1.00 108.27 ? 1456 LYS B CA  1 
ATOM   25440 C  C   . LYS C 1 1456 ? -4.359   37.438  73.640  1.00 105.15 ? 1456 LYS B C   1 
ATOM   25441 O  O   . LYS C 1 1456 ? -4.646   36.317  74.048  1.00 103.80 ? 1456 LYS B O   1 
ATOM   25442 C  CB  . LYS C 1 1456 ? -4.708   39.207  75.359  1.00 112.24 ? 1456 LYS B CB  1 
ATOM   25443 C  CG  . LYS C 1 1456 ? -3.256   39.668  75.309  1.00 117.60 ? 1456 LYS B CG  1 
ATOM   25444 C  CD  . LYS C 1 1456 ? -2.787   40.301  76.619  1.00 121.34 ? 1456 LYS B CD  1 
ATOM   25445 C  CE  . LYS C 1 1456 ? -1.746   41.425  76.392  1.00 122.59 ? 1456 LYS B CE  1 
ATOM   25446 N  NZ  . LYS C 1 1456 ? -2.321   42.684  75.781  1.00 121.80 ? 1456 LYS B NZ  1 
ATOM   25447 N  N   . ASP C 1 1457 ? -3.346   37.680  72.828  1.00 103.88 ? 1457 ASP B N   1 
ATOM   25448 C  CA  . ASP C 1 1457 ? -2.354   36.669  72.503  1.00 105.44 ? 1457 ASP B CA  1 
ATOM   25449 C  C   . ASP C 1 1457 ? -2.860   35.228  72.386  1.00 103.64 ? 1457 ASP B C   1 
ATOM   25450 O  O   . ASP C 1 1457 ? -2.289   34.313  72.959  1.00 102.83 ? 1457 ASP B O   1 
ATOM   25451 C  CB  . ASP C 1 1457 ? -1.165   36.775  73.455  1.00 108.31 ? 1457 ASP B CB  1 
ATOM   25452 C  CG  . ASP C 1 1457 ? -0.374   38.040  73.224  1.00 111.59 ? 1457 ASP B CG  1 
ATOM   25453 O  OD1 . ASP C 1 1457 ? -0.530   38.620  72.123  1.00 114.12 ? 1457 ASP B OD1 1 
ATOM   25454 O  OD2 . ASP C 1 1457 ? 0.380    38.467  74.131  1.00 111.74 ? 1457 ASP B OD2 1 
ATOM   25455 N  N   . GLY C 1 1458 ? -3.911   35.028  71.607  1.00 101.37 ? 1458 GLY B N   1 
ATOM   25456 C  CA  . GLY C 1 1458 ? -4.324   33.685  71.278  1.00 99.22  ? 1458 GLY B CA  1 
ATOM   25457 C  C   . GLY C 1 1458 ? -5.134   33.061  72.382  1.00 96.77  ? 1458 GLY B C   1 
ATOM   25458 O  O   . GLY C 1 1458 ? -5.235   31.837  72.449  1.00 97.84  ? 1458 GLY B O   1 
ATOM   25459 N  N   . HIS C 1 1459 ? -5.721   33.899  73.235  1.00 94.47  ? 1459 HIS B N   1 
ATOM   25460 C  CA  . HIS C 1 1459 ? -6.484   33.428  74.387  1.00 95.02  ? 1459 HIS B CA  1 
ATOM   25461 C  C   . HIS C 1 1459 ? -7.757   34.224  74.529  1.00 92.07  ? 1459 HIS B C   1 
ATOM   25462 O  O   . HIS C 1 1459 ? -7.709   35.440  74.618  1.00 89.29  ? 1459 HIS B O   1 
ATOM   25463 C  CB  . HIS C 1 1459 ? -5.680   33.599  75.693  1.00 97.03  ? 1459 HIS B CB  1 
ATOM   25464 C  CG  . HIS C 1 1459 ? -4.420   32.777  75.768  1.00 101.82 ? 1459 HIS B CG  1 
ATOM   25465 N  ND1 . HIS C 1 1459 ? -4.391   31.491  76.270  1.00 104.56 ? 1459 HIS B ND1 1 
ATOM   25466 C  CD2 . HIS C 1 1459 ? -3.138   33.070  75.433  1.00 103.01 ? 1459 HIS B CD2 1 
ATOM   25467 C  CE1 . HIS C 1 1459 ? -3.154   31.023  76.217  1.00 105.14 ? 1459 HIS B CE1 1 
ATOM   25468 N  NE2 . HIS C 1 1459 ? -2.374   31.962  75.714  1.00 103.99 ? 1459 HIS B NE2 1 
ATOM   25469 N  N   . VAL C 1 1460 ? -8.900   33.551  74.553  1.00 94.84  ? 1460 VAL B N   1 
ATOM   25470 C  CA  . VAL C 1 1460 ? -10.137  34.216  74.961  1.00 97.44  ? 1460 VAL B CA  1 
ATOM   25471 C  C   . VAL C 1 1460 ? -10.164  34.203  76.475  1.00 101.41 ? 1460 VAL B C   1 
ATOM   25472 O  O   . VAL C 1 1460 ? -9.879   33.161  77.087  1.00 104.12 ? 1460 VAL B O   1 
ATOM   25473 C  CB  . VAL C 1 1460 ? -11.396  33.506  74.436  1.00 98.48  ? 1460 VAL B CB  1 
ATOM   25474 C  CG1 . VAL C 1 1460 ? -12.634  33.972  75.191  1.00 98.04  ? 1460 VAL B CG1 1 
ATOM   25475 C  CG2 . VAL C 1 1460 ? -11.543  33.771  72.951  1.00 99.39  ? 1460 VAL B CG2 1 
ATOM   25476 N  N   . ILE C 1 1461 ? -10.504  35.343  77.082  1.00 100.50 ? 1461 ILE B N   1 
ATOM   25477 C  CA  . ILE C 1 1461 ? -10.340  35.512  78.532  1.00 98.04  ? 1461 ILE B CA  1 
ATOM   25478 C  C   . ILE C 1 1461 ? -11.536  36.169  79.213  1.00 99.06  ? 1461 ILE B C   1 
ATOM   25479 O  O   . ILE C 1 1461 ? -11.720  37.396  79.172  1.00 96.67  ? 1461 ILE B O   1 
ATOM   25480 C  CB  . ILE C 1 1461 ? -9.077   36.310  78.851  1.00 92.70  ? 1461 ILE B CB  1 
ATOM   25481 C  CG1 . ILE C 1 1461 ? -7.896   35.362  78.985  1.00 92.16  ? 1461 ILE B CG1 1 
ATOM   25482 C  CG2 . ILE C 1 1461 ? -9.251   37.092  80.117  1.00 89.64  ? 1461 ILE B CG2 1 
ATOM   25483 C  CD1 . ILE C 1 1461 ? -6.569   36.035  78.773  1.00 91.04  ? 1461 ILE B CD1 1 
ATOM   25484 N  N   . LEU C 1 1462 ? -12.334  35.325  79.858  1.00 101.29 ? 1462 LEU B N   1 
ATOM   25485 C  CA  . LEU C 1 1462 ? -13.587  35.745  80.464  1.00 100.58 ? 1462 LEU B CA  1 
ATOM   25486 C  C   . LEU C 1 1462 ? -13.452  35.943  81.973  1.00 104.15 ? 1462 LEU B C   1 
ATOM   25487 O  O   . LEU C 1 1462 ? -12.607  35.329  82.605  1.00 104.62 ? 1462 LEU B O   1 
ATOM   25488 C  CB  . LEU C 1 1462 ? -14.685  34.737  80.124  1.00 95.81  ? 1462 LEU B CB  1 
ATOM   25489 C  CG  . LEU C 1 1462 ? -14.973  34.713  78.629  1.00 82.39  ? 1462 LEU B CG  1 
ATOM   25490 C  CD1 . LEU C 1 1462 ? -16.078  33.752  78.310  1.00 83.70  ? 1462 LEU B CD1 1 
ATOM   25491 C  CD2 . LEU C 1 1462 ? -15.367  36.086  78.223  1.00 78.69  ? 1462 LEU B CD2 1 
ATOM   25492 N  N   . GLN C 1 1463 ? -14.288  36.812  82.533  1.00 103.91 ? 1463 GLN B N   1 
ATOM   25493 C  CA  . GLN C 1 1463 ? -14.230  37.154  83.942  1.00 101.95 ? 1463 GLN B CA  1 
ATOM   25494 C  C   . GLN C 1 1463 ? -15.660  37.376  84.436  1.00 100.05 ? 1463 GLN B C   1 
ATOM   25495 O  O   . GLN C 1 1463 ? -16.410  38.150  83.827  1.00 97.90  ? 1463 GLN B O   1 
ATOM   25496 C  CB  . GLN C 1 1463 ? -13.448  38.464  84.135  1.00 102.96 ? 1463 GLN B CB  1 
ATOM   25497 C  CG  . GLN C 1 1463 ? -11.911  38.399  84.273  1.00 104.24 ? 1463 GLN B CG  1 
ATOM   25498 C  CD  . GLN C 1 1463 ? -11.329  39.771  84.654  1.00 105.23 ? 1463 GLN B CD  1 
ATOM   25499 O  OE1 . GLN C 1 1463 ? -10.113  39.980  84.681  1.00 104.78 ? 1463 GLN B OE1 1 
ATOM   25500 N  NE2 . GLN C 1 1463 ? -12.219  40.712  84.950  1.00 106.28 ? 1463 GLN B NE2 1 
ATOM   25501 N  N   . LEU C 1 1464 ? -16.035  36.711  85.530  1.00 100.70 ? 1464 LEU B N   1 
ATOM   25502 C  CA  . LEU C 1 1464 ? -17.308  36.975  86.225  1.00 101.73 ? 1464 LEU B CA  1 
ATOM   25503 C  C   . LEU C 1 1464 ? -17.128  36.893  87.737  1.00 103.80 ? 1464 LEU B C   1 
ATOM   25504 O  O   . LEU C 1 1464 ? -16.089  36.445  88.229  1.00 102.46 ? 1464 LEU B O   1 
ATOM   25505 C  CB  . LEU C 1 1464 ? -18.429  36.022  85.796  1.00 102.07 ? 1464 LEU B CB  1 
ATOM   25506 C  CG  . LEU C 1 1464 ? -18.194  34.681  85.072  1.00 102.21 ? 1464 LEU B CG  1 
ATOM   25507 C  CD1 . LEU C 1 1464 ? -16.804  34.043  85.248  1.00 101.27 ? 1464 LEU B CD1 1 
ATOM   25508 C  CD2 . LEU C 1 1464 ? -19.277  33.707  85.477  1.00 103.96 ? 1464 LEU B CD2 1 
ATOM   25509 N  N   . ASN C 1 1465 ? -18.142  37.332  88.476  1.00 108.40 ? 1465 ASN B N   1 
ATOM   25510 C  CA  . ASN C 1 1465 ? -18.065  37.370  89.945  1.00 111.94 ? 1465 ASN B CA  1 
ATOM   25511 C  C   . ASN C 1 1465 ? -18.144  36.016  90.673  1.00 114.88 ? 1465 ASN B C   1 
ATOM   25512 O  O   . ASN C 1 1465 ? -17.864  35.945  91.865  1.00 114.72 ? 1465 ASN B O   1 
ATOM   25513 C  CB  . ASN C 1 1465 ? -19.138  38.299  90.535  1.00 113.78 ? 1465 ASN B CB  1 
ATOM   25514 C  CG  . ASN C 1 1465 ? -19.395  39.512  89.684  1.00 112.59 ? 1465 ASN B CG  1 
ATOM   25515 O  OD1 . ASN C 1 1465 ? -19.110  40.636  90.106  1.00 109.99 ? 1465 ASN B OD1 1 
ATOM   25516 N  ND2 . ASN C 1 1465 ? -19.948  39.298  88.475  1.00 113.83 ? 1465 ASN B ND2 1 
ATOM   25517 N  N   . SER C 1 1466 ? -18.544  34.959  89.968  1.00 119.75 ? 1466 SER B N   1 
ATOM   25518 C  CA  . SER C 1 1466 ? -18.754  33.649  90.584  1.00 123.34 ? 1466 SER B CA  1 
ATOM   25519 C  C   . SER C 1 1466 ? -18.877  32.527  89.556  1.00 124.80 ? 1466 SER B C   1 
ATOM   25520 O  O   . SER C 1 1466 ? -19.210  32.771  88.397  1.00 122.22 ? 1466 SER B O   1 
ATOM   25521 C  CB  . SER C 1 1466 ? -20.026  33.661  91.432  1.00 128.17 ? 1466 SER B CB  1 
ATOM   25522 O  OG  . SER C 1 1466 ? -20.368  32.340  91.832  1.00 132.43 ? 1466 SER B OG  1 
ATOM   25523 N  N   . ILE C 1 1467 ? -18.645  31.294  89.992  1.00 126.44 ? 1467 ILE B N   1 
ATOM   25524 C  CA  . ILE C 1 1467 ? -18.858  30.151  89.122  1.00 128.46 ? 1467 ILE B CA  1 
ATOM   25525 C  C   . ILE C 1 1467 ? -19.702  29.082  89.811  1.00 135.46 ? 1467 ILE B C   1 
ATOM   25526 O  O   . ILE C 1 1467 ? -19.261  27.949  89.966  1.00 138.82 ? 1467 ILE B O   1 
ATOM   25527 C  CB  . ILE C 1 1467 ? -17.537  29.543  88.659  1.00 125.08 ? 1467 ILE B CB  1 
ATOM   25528 C  CG1 . ILE C 1 1467 ? -16.665  30.586  87.981  1.00 117.00 ? 1467 ILE B CG1 1 
ATOM   25529 C  CG2 . ILE C 1 1467 ? -17.787  28.428  87.670  1.00 127.61 ? 1467 ILE B CG2 1 
ATOM   25530 C  CD1 . ILE C 1 1467 ? -15.496  29.972  87.291  1.00 114.65 ? 1467 ILE B CD1 1 
ATOM   25531 N  N   . PRO C 1 1468 ? -20.941  29.439  90.191  1.00 135.11 ? 1468 PRO B N   1 
ATOM   25532 C  CA  . PRO C 1 1468 ? -21.862  28.651  91.021  1.00 138.29 ? 1468 PRO B CA  1 
ATOM   25533 C  C   . PRO C 1 1468 ? -21.512  27.168  91.085  1.00 140.07 ? 1468 PRO B C   1 
ATOM   25534 O  O   . PRO C 1 1468 ? -21.094  26.593  90.076  1.00 138.59 ? 1468 PRO B O   1 
ATOM   25535 C  CB  . PRO C 1 1468 ? -23.198  28.817  90.284  1.00 137.53 ? 1468 PRO B CB  1 
ATOM   25536 C  CG  . PRO C 1 1468 ? -23.127  30.199  89.724  1.00 135.01 ? 1468 PRO B CG  1 
ATOM   25537 C  CD  . PRO C 1 1468 ? -21.650  30.555  89.545  1.00 134.14 ? 1468 PRO B CD  1 
ATOM   25538 N  N   . SER C 1 1469 ? -21.671  26.553  92.253  1.00 143.40 ? 1469 SER B N   1 
ATOM   25539 C  CA  . SER C 1 1469 ? -21.438  25.128  92.371  1.00 147.07 ? 1469 SER B CA  1 
ATOM   25540 C  C   . SER C 1 1469 ? -22.721  24.395  92.135  1.00 151.04 ? 1469 SER B C   1 
ATOM   25541 O  O   . SER C 1 1469 ? -22.712  23.207  91.848  1.00 156.01 ? 1469 SER B O   1 
ATOM   25542 C  CB  . SER C 1 1469 ? -20.902  24.790  93.740  1.00 147.50 ? 1469 SER B CB  1 
ATOM   25543 O  OG  . SER C 1 1469 ? -19.679  25.460  93.929  1.00 146.04 ? 1469 SER B OG  1 
ATOM   25544 N  N   . SER C 1 1470 ? -23.830  25.114  92.256  1.00 149.67 ? 1470 SER B N   1 
ATOM   25545 C  CA  . SER C 1 1470 ? -25.152  24.537  92.021  1.00 151.12 ? 1470 SER B CA  1 
ATOM   25546 C  C   . SER C 1 1470 ? -25.136  23.651  90.789  1.00 150.70 ? 1470 SER B C   1 
ATOM   25547 O  O   . SER C 1 1470 ? -25.643  22.524  90.790  1.00 153.20 ? 1470 SER B O   1 
ATOM   25548 C  CB  . SER C 1 1470 ? -26.188  25.650  91.826  1.00 152.86 ? 1470 SER B CB  1 
ATOM   25549 O  OG  . SER C 1 1470 ? -25.788  26.550  90.799  1.00 152.26 ? 1470 SER B OG  1 
ATOM   25550 N  N   . ASP C 1 1471 ? -24.534  24.179  89.736  1.00 146.58 ? 1471 ASP B N   1 
ATOM   25551 C  CA  . ASP C 1 1471 ? -24.436  23.473  88.477  1.00 147.56 ? 1471 ASP B CA  1 
ATOM   25552 C  C   . ASP C 1 1471 ? -23.262  24.048  87.708  1.00 137.35 ? 1471 ASP B C   1 
ATOM   25553 O  O   . ASP C 1 1471 ? -22.353  24.619  88.295  1.00 133.23 ? 1471 ASP B O   1 
ATOM   25554 C  CB  . ASP C 1 1471 ? -25.750  23.576  87.680  1.00 154.88 ? 1471 ASP B CB  1 
ATOM   25555 C  CG  . ASP C 1 1471 ? -26.270  25.008  87.574  1.00 157.16 ? 1471 ASP B CG  1 
ATOM   25556 O  OD1 . ASP C 1 1471 ? -27.507  25.179  87.487  1.00 160.70 ? 1471 ASP B OD1 1 
ATOM   25557 O  OD2 . ASP C 1 1471 ? -25.451  25.959  87.573  1.00 155.69 ? 1471 ASP B OD2 1 
ATOM   25558 N  N   . PHE C 1 1472 ? -23.273  23.876  86.398  1.00 133.63 ? 1472 PHE B N   1 
ATOM   25559 C  CA  . PHE C 1 1472 ? -22.216  24.408  85.574  1.00 127.11 ? 1472 PHE B CA  1 
ATOM   25560 C  C   . PHE C 1 1472 ? -22.516  25.786  85.055  1.00 123.19 ? 1472 PHE B C   1 
ATOM   25561 O  O   . PHE C 1 1472 ? -23.658  26.267  85.070  1.00 123.11 ? 1472 PHE B O   1 
ATOM   25562 C  CB  . PHE C 1 1472 ? -21.963  23.503  84.395  1.00 126.85 ? 1472 PHE B CB  1 
ATOM   25563 C  CG  . PHE C 1 1472 ? -21.058  22.407  84.706  1.00 128.08 ? 1472 PHE B CG  1 
ATOM   25564 C  CD1 . PHE C 1 1472 ? -21.417  21.454  85.625  1.00 131.90 ? 1472 PHE B CD1 1 
ATOM   25565 C  CD2 . PHE C 1 1472 ? -19.826  22.329  84.112  1.00 127.32 ? 1472 PHE B CD2 1 
ATOM   25566 C  CE1 . PHE C 1 1472 ? -20.558  20.415  85.939  1.00 134.14 ? 1472 PHE B CE1 1 
ATOM   25567 C  CE2 . PHE C 1 1472 ? -18.957  21.294  84.413  1.00 129.21 ? 1472 PHE B CE2 1 
ATOM   25568 C  CZ  . PHE C 1 1472 ? -19.322  20.337  85.323  1.00 132.29 ? 1472 PHE B CZ  1 
ATOM   25569 N  N   . LEU C 1 1473 ? -21.467  26.411  84.559  1.00 121.01 ? 1473 LEU B N   1 
ATOM   25570 C  CA  . LEU C 1 1473 ? -21.613  27.695  83.932  1.00 118.92 ? 1473 LEU B CA  1 
ATOM   25571 C  C   . LEU C 1 1473 ? -20.876  27.596  82.616  1.00 121.91 ? 1473 LEU B C   1 
ATOM   25572 O  O   . LEU C 1 1473 ? -19.687  27.227  82.595  1.00 120.79 ? 1473 LEU B O   1 
ATOM   25573 C  CB  . LEU C 1 1473 ? -21.024  28.780  84.816  1.00 114.52 ? 1473 LEU B CB  1 
ATOM   25574 C  CG  . LEU C 1 1473 ? -21.121  30.175  84.217  1.00 112.19 ? 1473 LEU B CG  1 
ATOM   25575 C  CD1 . LEU C 1 1473 ? -21.673  31.157  85.234  1.00 111.41 ? 1473 LEU B CD1 1 
ATOM   25576 C  CD2 . LEU C 1 1473 ? -19.772  30.625  83.645  1.00 109.98 ? 1473 LEU B CD2 1 
ATOM   25577 N  N   . CYS C 1 1474 ? -21.586  27.920  81.527  1.00 122.49 ? 1474 CYS B N   1 
ATOM   25578 C  CA  . CYS C 1 1474 ? -21.076  27.685  80.183  1.00 119.86 ? 1474 CYS B CA  1 
ATOM   25579 C  C   . CYS C 1 1474 ? -20.973  28.916  79.319  1.00 120.61 ? 1474 CYS B C   1 
ATOM   25580 O  O   . CYS C 1 1474 ? -21.929  29.670  79.198  1.00 121.78 ? 1474 CYS B O   1 
ATOM   25581 C  CB  . CYS C 1 1474 ? -21.903  26.624  79.498  1.00 119.16 ? 1474 CYS B CB  1 
ATOM   25582 S  SG  . CYS C 1 1474 ? -21.207  25.034  79.916  1.00 131.07 ? 1474 CYS B SG  1 
ATOM   25583 N  N   . VAL C 1 1475 ? -19.785  29.141  78.765  1.00 120.40 ? 1475 VAL B N   1 
ATOM   25584 C  CA  . VAL C 1 1475 ? -19.615  30.106  77.693  1.00 120.44 ? 1475 VAL B CA  1 
ATOM   25585 C  C   . VAL C 1 1475 ? -19.680  29.276  76.435  1.00 125.31 ? 1475 VAL B C   1 
ATOM   25586 O  O   . VAL C 1 1475 ? -19.229  28.119  76.443  1.00 126.26 ? 1475 VAL B O   1 
ATOM   25587 C  CB  . VAL C 1 1475 ? -18.229  30.788  77.716  1.00 115.96 ? 1475 VAL B CB  1 
ATOM   25588 C  CG1 . VAL C 1 1475 ? -17.161  29.767  77.908  1.00 116.46 ? 1475 VAL B CG1 1 
ATOM   25589 C  CG2 . VAL C 1 1475 ? -17.968  31.511  76.411  1.00 114.12 ? 1475 VAL B CG2 1 
ATOM   25590 N  N   . ARG C 1 1476 ? -20.260  29.845  75.375  1.00 125.37 ? 1476 ARG B N   1 
ATOM   25591 C  CA  . ARG C 1 1476 ? -20.143  29.265  74.041  1.00 125.65 ? 1476 ARG B CA  1 
ATOM   25592 C  C   . ARG C 1 1476 ? -19.823  30.365  73.022  1.00 119.00 ? 1476 ARG B C   1 
ATOM   25593 O  O   . ARG C 1 1476 ? -20.180  31.526  73.212  1.00 114.97 ? 1476 ARG B O   1 
ATOM   25594 C  CB  . ARG C 1 1476 ? -21.371  28.423  73.658  1.00 131.23 ? 1476 ARG B CB  1 
ATOM   25595 C  CG  . ARG C 1 1476 ? -22.709  28.985  74.098  1.00 136.46 ? 1476 ARG B CG  1 
ATOM   25596 C  CD  . ARG C 1 1476 ? -23.267  28.348  75.373  1.00 143.73 ? 1476 ARG B CD  1 
ATOM   25597 N  NE  . ARG C 1 1476 ? -23.912  29.375  76.192  1.00 149.00 ? 1476 ARG B NE  1 
ATOM   25598 C  CZ  . ARG C 1 1476 ? -24.620  29.159  77.303  1.00 154.77 ? 1476 ARG B CZ  1 
ATOM   25599 N  NH1 . ARG C 1 1476 ? -24.820  27.917  77.773  1.00 157.99 ? 1476 ARG B NH1 1 
ATOM   25600 N  NH2 . ARG C 1 1476 ? -25.136  30.210  77.944  1.00 154.56 ? 1476 ARG B NH2 1 
ATOM   25601 N  N   . PHE C 1 1477 ? -19.091  29.997  71.976  1.00 117.80 ? 1477 PHE B N   1 
ATOM   25602 C  CA  . PHE C 1 1477 ? -18.666  30.947  70.947  1.00 114.97 ? 1477 PHE B CA  1 
ATOM   25603 C  C   . PHE C 1 1477 ? -18.061  30.223  69.736  1.00 116.19 ? 1477 PHE B C   1 
ATOM   25604 O  O   . PHE C 1 1477 ? -17.522  29.119  69.859  1.00 117.87 ? 1477 PHE B O   1 
ATOM   25605 C  CB  . PHE C 1 1477 ? -17.688  31.982  71.518  1.00 111.33 ? 1477 PHE B CB  1 
ATOM   25606 C  CG  . PHE C 1 1477 ? -16.328  31.421  71.860  1.00 110.79 ? 1477 PHE B CG  1 
ATOM   25607 C  CD1 . PHE C 1 1477 ? -15.268  31.520  70.972  1.00 110.39 ? 1477 PHE B CD1 1 
ATOM   25608 C  CD2 . PHE C 1 1477 ? -16.113  30.809  73.073  1.00 111.62 ? 1477 PHE B CD2 1 
ATOM   25609 C  CE1 . PHE C 1 1477 ? -14.039  31.006  71.282  1.00 109.74 ? 1477 PHE B CE1 1 
ATOM   25610 C  CE2 . PHE C 1 1477 ? -14.887  30.303  73.382  1.00 111.68 ? 1477 PHE B CE2 1 
ATOM   25611 C  CZ  . PHE C 1 1477 ? -13.849  30.399  72.483  1.00 110.94 ? 1477 PHE B CZ  1 
ATOM   25612 N  N   . ARG C 1 1478 ? -18.152  30.845  68.566  1.00 114.07 ? 1478 ARG B N   1 
ATOM   25613 C  CA  . ARG C 1 1478 ? -17.796  30.156  67.344  1.00 114.70 ? 1478 ARG B CA  1 
ATOM   25614 C  C   . ARG C 1 1478 ? -16.428  30.560  66.872  1.00 113.26 ? 1478 ARG B C   1 
ATOM   25615 O  O   . ARG C 1 1478 ? -15.973  31.645  67.203  1.00 107.36 ? 1478 ARG B O   1 
ATOM   25616 C  CB  . ARG C 1 1478 ? -18.817  30.472  66.278  1.00 116.82 ? 1478 ARG B CB  1 
ATOM   25617 C  CG  . ARG C 1 1478 ? -20.239  30.433  66.771  1.00 119.05 ? 1478 ARG B CG  1 
ATOM   25618 C  CD  . ARG C 1 1478 ? -21.183  30.732  65.624  1.00 122.23 ? 1478 ARG B CD  1 
ATOM   25619 N  NE  . ARG C 1 1478 ? -21.463  32.151  65.490  1.00 120.81 ? 1478 ARG B NE  1 
ATOM   25620 C  CZ  . ARG C 1 1478 ? -22.635  32.682  65.792  1.00 122.60 ? 1478 ARG B CZ  1 
ATOM   25621 N  NH1 . ARG C 1 1478 ? -23.619  31.897  66.224  1.00 126.82 ? 1478 ARG B NH1 1 
ATOM   25622 N  NH2 . ARG C 1 1478 ? -22.825  33.983  65.655  1.00 120.52 ? 1478 ARG B NH2 1 
ATOM   25623 N  N   . ILE C 1 1479 ? -15.799  29.701  66.067  1.00 120.12 ? 1479 ILE B N   1 
ATOM   25624 C  CA  . ILE C 1 1479 ? -14.395  29.864  65.673  1.00 124.65 ? 1479 ILE B CA  1 
ATOM   25625 C  C   . ILE C 1 1479 ? -14.110  29.577  64.197  1.00 130.63 ? 1479 ILE B C   1 
ATOM   25626 O  O   . ILE C 1 1479 ? -14.533  28.553  63.682  1.00 134.86 ? 1479 ILE B O   1 
ATOM   25627 C  CB  . ILE C 1 1479 ? -13.513  28.922  66.491  1.00 127.28 ? 1479 ILE B CB  1 
ATOM   25628 C  CG1 . ILE C 1 1479 ? -13.930  27.479  66.250  1.00 129.52 ? 1479 ILE B CG1 1 
ATOM   25629 C  CG2 . ILE C 1 1479 ? -13.638  29.226  67.966  1.00 126.70 ? 1479 ILE B CG2 1 
ATOM   25630 C  CD1 . ILE C 1 1479 ? -13.383  26.526  67.272  1.00 130.39 ? 1479 ILE B CD1 1 
ATOM   25631 N  N   . PHE C 1 1480 ? -13.383  30.468  63.523  1.00 132.99 ? 1480 PHE B N   1 
ATOM   25632 C  CA  . PHE C 1 1480 ? -13.098  30.281  62.092  1.00 138.25 ? 1480 PHE B CA  1 
ATOM   25633 C  C   . PHE C 1 1480 ? -11.642  29.985  61.740  1.00 137.74 ? 1480 PHE B C   1 
ATOM   25634 O  O   . PHE C 1 1480 ? -10.757  30.793  61.979  1.00 135.42 ? 1480 PHE B O   1 
ATOM   25635 C  CB  . PHE C 1 1480 ? -13.662  31.418  61.202  1.00 170.13 ? 1480 PHE B CB  1 
ATOM   25636 C  CG  . PHE C 1 1480 ? -13.966  32.720  61.941  1.00 172.39 ? 1480 PHE B CG  1 
ATOM   25637 C  CD1 . PHE C 1 1480 ? -12.968  33.409  62.639  1.00 169.66 ? 1480 PHE B CD1 1 
ATOM   25638 C  CD2 . PHE C 1 1480 ? -15.258  33.283  61.890  1.00 174.11 ? 1480 PHE B CD2 1 
ATOM   25639 C  CE1 . PHE C 1 1480 ? -13.255  34.615  63.297  1.00 166.89 ? 1480 PHE B CE1 1 
ATOM   25640 C  CE2 . PHE C 1 1480 ? -15.556  34.490  62.546  1.00 170.81 ? 1480 PHE B CE2 1 
ATOM   25641 C  CZ  . PHE C 1 1480 ? -14.553  35.154  63.252  1.00 167.23 ? 1480 PHE B CZ  1 
ATOM   25642 N  N   . GLU C 1 1481 ? -11.423  28.825  61.132  1.00 138.17 ? 1481 GLU B N   1 
ATOM   25643 C  CA  . GLU C 1 1481 ? -10.091  28.386  60.740  1.00 136.83 ? 1481 GLU B CA  1 
ATOM   25644 C  C   . GLU C 1 1481 ? -9.358   29.458  59.933  1.00 134.83 ? 1481 GLU B C   1 
ATOM   25645 O  O   . GLU C 1 1481 ? -9.306   29.396  58.704  1.00 136.81 ? 1481 GLU B O   1 
ATOM   25646 C  CB  . GLU C 1 1481 ? -10.167  27.064  59.937  1.00 139.24 ? 1481 GLU B CB  1 
ATOM   25647 C  CG  . GLU C 1 1481 ? -10.549  25.796  60.754  1.00 173.15 ? 1481 GLU B CG  1 
ATOM   25648 C  CD  . GLU C 1 1481 ? -10.418  24.469  59.969  1.00 174.57 ? 1481 GLU B CD  1 
ATOM   25649 O  OE1 . GLU C 1 1481 ? -9.927   24.476  58.814  1.00 174.35 ? 1481 GLU B OE1 1 
ATOM   25650 O  OE2 . GLU C 1 1481 ? -10.810  23.409  60.516  1.00 175.47 ? 1481 GLU B OE2 1 
ATOM   25651 N  N   . LEU C 1 1482 ? -8.764   30.425  60.620  1.00 130.44 ? 1482 LEU B N   1 
ATOM   25652 C  CA  . LEU C 1 1482 ? -8.104   31.522  59.924  1.00 127.45 ? 1482 LEU B CA  1 
ATOM   25653 C  C   . LEU C 1 1482 ? -7.134   31.038  58.843  1.00 124.81 ? 1482 LEU B C   1 
ATOM   25654 O  O   . LEU C 1 1482 ? -7.067   31.616  57.758  1.00 124.95 ? 1482 LEU B O   1 
ATOM   25655 C  CB  . LEU C 1 1482 ? -7.407   32.461  60.905  1.00 126.35 ? 1482 LEU B CB  1 
ATOM   25656 C  CG  . LEU C 1 1482 ? -6.516   33.530  60.269  1.00 126.46 ? 1482 LEU B CG  1 
ATOM   25657 C  CD1 . LEU C 1 1482 ? -6.624   34.846  61.028  1.00 124.47 ? 1482 LEU B CD1 1 
ATOM   25658 C  CD2 . LEU C 1 1482 ? -5.055   33.054  60.181  1.00 127.87 ? 1482 LEU B CD2 1 
ATOM   25659 N  N   . PHE C 1 1483 ? -6.415   29.953  59.143  1.00 122.99 ? 1483 PHE B N   1 
ATOM   25660 C  CA  . PHE C 1 1483 ? -5.552   29.329  58.139  1.00 121.57 ? 1483 PHE B CA  1 
ATOM   25661 C  C   . PHE C 1 1483 ? -5.378   27.826  58.389  1.00 126.32 ? 1483 PHE B C   1 
ATOM   25662 O  O   . PHE C 1 1483 ? -5.792   27.308  59.424  1.00 126.01 ? 1483 PHE B O   1 
ATOM   25663 C  CB  . PHE C 1 1483 ? -4.236   30.062  57.989  1.00 116.64 ? 1483 PHE B CB  1 
ATOM   25664 C  CG  . PHE C 1 1483 ? -3.430   30.219  59.225  1.00 112.53 ? 1483 PHE B CG  1 
ATOM   25665 C  CD1 . PHE C 1 1483 ? -3.630   29.391  60.321  1.00 111.02 ? 1483 PHE B CD1 1 
ATOM   25666 C  CD2 . PHE C 1 1483 ? -2.466   31.198  59.308  1.00 108.66 ? 1483 PHE B CD2 1 
ATOM   25667 C  CE1 . PHE C 1 1483 ? -2.898   29.544  61.478  1.00 107.15 ? 1483 PHE B CE1 1 
ATOM   25668 C  CE2 . PHE C 1 1483 ? -1.735   31.351  60.452  1.00 106.40 ? 1483 PHE B CE2 1 
ATOM   25669 C  CZ  . PHE C 1 1483 ? -1.955   30.521  61.545  1.00 105.00 ? 1483 PHE B CZ  1 
ATOM   25670 N  N   . GLU C 1 1484 ? -4.785   27.149  57.423  1.00 129.96 ? 1484 GLU B N   1 
ATOM   25671 C  CA  . GLU C 1 1484 ? -4.697   25.708  57.509  1.00 137.16 ? 1484 GLU B CA  1 
ATOM   25672 C  C   . GLU C 1 1484 ? -3.587   25.151  58.378  1.00 135.85 ? 1484 GLU B C   1 
ATOM   25673 O  O   . GLU C 1 1484 ? -2.398   25.323  58.078  1.00 135.73 ? 1484 GLU B O   1 
ATOM   25674 C  CB  . GLU C 1 1484 ? -4.598   25.129  56.099  1.00 145.96 ? 1484 GLU B CB  1 
ATOM   25675 C  CG  . GLU C 1 1484 ? -5.633   25.720  55.158  1.00 153.21 ? 1484 GLU B CG  1 
ATOM   25676 C  CD  . GLU C 1 1484 ? -5.287   27.139  54.704  1.00 156.36 ? 1484 GLU B CD  1 
ATOM   25677 O  OE1 . GLU C 1 1484 ? -4.250   27.663  55.173  1.00 156.32 ? 1484 GLU B OE1 1 
ATOM   25678 O  OE2 . GLU C 1 1484 ? -6.044   27.696  53.888  1.00 157.38 ? 1484 GLU B OE2 1 
ATOM   25679 N  N   . VAL C 1 1485 ? -3.983   24.476  59.475  1.00 134.20 ? 1485 VAL B N   1 
ATOM   25680 C  CA  . VAL C 1 1485 ? -3.016   23.863  60.386  1.00 131.18 ? 1485 VAL B CA  1 
ATOM   25681 C  C   . VAL C 1 1485 ? -2.958   22.362  60.252  1.00 128.17 ? 1485 VAL B C   1 
ATOM   25682 O  O   . VAL C 1 1485 ? -3.948   21.650  60.104  1.00 130.22 ? 1485 VAL B O   1 
ATOM   25683 C  CB  . VAL C 1 1485 ? -3.242   24.272  61.838  1.00 148.57 ? 1485 VAL B CB  1 
ATOM   25684 C  CG1 . VAL C 1 1485 ? -3.931   25.624  61.908  1.00 145.08 ? 1485 VAL B CG1 1 
ATOM   25685 C  CG2 . VAL C 1 1485 ? -4.054   23.212  62.574  1.00 150.44 ? 1485 VAL B CG2 1 
ATOM   25686 N  N   . GLY C 1 1486 ? -1.694   21.907  60.308  1.00 127.42 ? 1486 GLY B N   1 
ATOM   25687 C  CA  . GLY C 1 1486 ? -1.318   20.513  60.226  1.00 127.31 ? 1486 GLY B CA  1 
ATOM   25688 C  C   . GLY C 1 1486 ? -1.122   19.912  61.601  1.00 127.70 ? 1486 GLY B C   1 
ATOM   25689 O  O   . GLY C 1 1486 ? -0.905   20.627  62.577  1.00 128.87 ? 1486 GLY B O   1 
ATOM   25690 N  N   . PHE C 1 1487 ? -1.233   18.628  61.682  1.00 125.09 ? 1487 PHE B N   1 
ATOM   25691 C  CA  . PHE C 1 1487 ? -1.088   18.025  62.989  1.00 125.96 ? 1487 PHE B CA  1 
ATOM   25692 C  C   . PHE C 1 1487 ? -1.126   19.084  64.102  1.00 120.88 ? 1487 PHE B C   1 
ATOM   25693 O  O   . PHE C 1 1487 ? -0.156   19.256  64.842  1.00 119.40 ? 1487 PHE B O   1 
ATOM   25694 C  CB  . PHE C 1 1487 ? 0.232    17.291  63.155  1.00 131.44 ? 1487 PHE B CB  1 
ATOM   25695 C  CG  . PHE C 1 1487 ? 1.041    16.997  61.928  1.00 134.84 ? 1487 PHE B CG  1 
ATOM   25696 C  CD1 . PHE C 1 1487 ? 1.713    17.980  61.190  1.00 138.83 ? 1487 PHE B CD1 1 
ATOM   25697 C  CD2 . PHE C 1 1487 ? 1.165    15.684  61.484  1.00 133.61 ? 1487 PHE B CD2 1 
ATOM   25698 C  CE1 . PHE C 1 1487 ? 2.452    17.661  60.061  1.00 139.97 ? 1487 PHE B CE1 1 
ATOM   25699 C  CE2 . PHE C 1 1487 ? 1.897    15.364  60.358  1.00 135.02 ? 1487 PHE B CE2 1 
ATOM   25700 C  CZ  . PHE C 1 1487 ? 2.542    16.357  59.648  1.00 138.03 ? 1487 PHE B CZ  1 
ATOM   25701 N  N   . LEU C 1 1488 ? -2.248   19.784  64.288  1.00 118.31 ? 1488 LEU B N   1 
ATOM   25702 C  CA  . LEU C 1 1488 ? -2.318   20.780  65.351  1.00 115.71 ? 1488 LEU B CA  1 
ATOM   25703 C  C   . LEU C 1 1488 ? -2.333   20.172  66.758  1.00 116.40 ? 1488 LEU B C   1 
ATOM   25704 O  O   . LEU C 1 1488 ? -3.084   19.224  67.019  1.00 119.82 ? 1488 LEU B O   1 
ATOM   25705 C  CB  . LEU C 1 1488 ? -3.544   21.717  65.125  1.00 113.32 ? 1488 LEU B CB  1 
ATOM   25706 C  CG  . LEU C 1 1488 ? -4.915   21.355  65.736  1.00 113.92 ? 1488 LEU B CG  1 
ATOM   25707 C  CD1 . LEU C 1 1488 ? -4.750   20.631  67.064  1.00 113.75 ? 1488 LEU B CD1 1 
ATOM   25708 C  CD2 . LEU C 1 1488 ? -5.772   22.595  65.917  1.00 111.51 ? 1488 LEU B CD2 1 
ATOM   25709 N  N   . SER C 1 1489 ? -1.512   20.712  67.697  1.00 112.53 ? 1489 SER B N   1 
ATOM   25710 C  CA  . SER C 1 1489 ? -1.496   20.239  69.108  1.00 107.55 ? 1489 SER B CA  1 
ATOM   25711 C  C   . SER C 1 1489 ? -2.525   21.087  69.862  1.00 106.52 ? 1489 SER B C   1 
ATOM   25712 O  O   . SER C 1 1489 ? -2.862   22.187  69.401  1.00 105.35 ? 1489 SER B O   1 
ATOM   25713 C  CB  . SER C 1 1489 ? -0.105   20.339  69.713  1.00 104.05 ? 1489 SER B CB  1 
ATOM   25714 O  OG  . SER C 1 1489 ? -0.003   21.485  70.535  1.00 100.66 ? 1489 SER B OG  1 
ATOM   25715 N  N   . PRO C 1 1490 ? -3.028   20.624  71.007  1.00 103.55 ? 1490 PRO B N   1 
ATOM   25716 C  CA  . PRO C 1 1490 ? -4.135   21.259  71.715  1.00 102.97 ? 1490 PRO B CA  1 
ATOM   25717 C  C   . PRO C 1 1490 ? -3.672   22.436  72.483  1.00 101.72 ? 1490 PRO B C   1 
ATOM   25718 O  O   . PRO C 1 1490 ? -2.548   22.490  72.975  1.00 99.90  ? 1490 PRO B O   1 
ATOM   25719 C  CB  . PRO C 1 1490 ? -4.564   20.213  72.739  1.00 102.74 ? 1490 PRO B CB  1 
ATOM   25720 C  CG  . PRO C 1 1490 ? -3.848   19.007  72.392  1.00 105.60 ? 1490 PRO B CG  1 
ATOM   25721 C  CD  . PRO C 1 1490 ? -2.592   19.428  71.715  1.00 104.81 ? 1490 PRO B CD  1 
ATOM   25722 N  N   . ALA C 1 1491 ? -4.569   23.395  72.564  1.00 103.49 ? 1491 ALA B N   1 
ATOM   25723 C  CA  . ALA C 1 1491 ? -4.437   24.474  73.488  1.00 102.96 ? 1491 ALA B CA  1 
ATOM   25724 C  C   . ALA C 1 1491 ? -5.140   23.986  74.739  1.00 106.71 ? 1491 ALA B C   1 
ATOM   25725 O  O   . ALA C 1 1491 ? -5.423   22.779  74.878  1.00 107.38 ? 1491 ALA B O   1 
ATOM   25726 C  CB  . ALA C 1 1491 ? -5.108   25.683  72.949  1.00 99.21  ? 1491 ALA B CB  1 
ATOM   25727 N  N   . THR C 1 1492 ? -5.441   24.940  75.620  1.00 107.87 ? 1492 THR B N   1 
ATOM   25728 C  CA  . THR C 1 1492 ? -5.789   24.656  77.001  1.00 108.88 ? 1492 THR B CA  1 
ATOM   25729 C  C   . THR C 1 1492 ? -6.916   25.523  77.508  1.00 109.55 ? 1492 THR B C   1 
ATOM   25730 O  O   . THR C 1 1492 ? -7.048   26.687  77.139  1.00 109.86 ? 1492 THR B O   1 
ATOM   25731 C  CB  . THR C 1 1492 ? -4.596   24.868  77.897  1.00 104.64 ? 1492 THR B CB  1 
ATOM   25732 O  OG1 . THR C 1 1492 ? -3.741   25.840  77.300  1.00 87.75  ? 1492 THR B OG1 1 
ATOM   25733 C  CG2 . THR C 1 1492 ? -3.835   23.620  77.982  1.00 91.15  ? 1492 THR B CG2 1 
ATOM   25734 N  N   . PHE C 1 1493 ? -7.722   24.930  78.375  1.00 110.58 ? 1493 PHE B N   1 
ATOM   25735 C  CA  . PHE C 1 1493 ? -8.841   25.621  78.969  1.00 107.24 ? 1493 PHE B CA  1 
ATOM   25736 C  C   . PHE C 1 1493 ? -8.648   25.621  80.447  1.00 111.47 ? 1493 PHE B C   1 
ATOM   25737 O  O   . PHE C 1 1493 ? -8.944   24.626  81.123  1.00 113.31 ? 1493 PHE B O   1 
ATOM   25738 C  CB  . PHE C 1 1493 ? -10.118  24.881  78.708  1.00 102.76 ? 1493 PHE B CB  1 
ATOM   25739 C  CG  . PHE C 1 1493 ? -11.257  25.383  79.507  1.00 95.51  ? 1493 PHE B CG  1 
ATOM   25740 C  CD1 . PHE C 1 1493 ? -11.317  26.714  79.843  1.00 88.52  ? 1493 PHE B CD1 1 
ATOM   25741 C  CD2 . PHE C 1 1493 ? -12.289  24.533  79.884  1.00 96.96  ? 1493 PHE B CD2 1 
ATOM   25742 C  CE1 . PHE C 1 1493 ? -12.370  27.193  80.565  1.00 90.14  ? 1493 PHE B CE1 1 
ATOM   25743 C  CE2 . PHE C 1 1493 ? -13.356  24.995  80.598  1.00 95.88  ? 1493 PHE B CE2 1 
ATOM   25744 C  CZ  . PHE C 1 1493 ? -13.400  26.333  80.949  1.00 93.99  ? 1493 PHE B CZ  1 
ATOM   25745 N  N   . THR C 1 1494 ? -8.168   26.755  80.943  1.00 111.65 ? 1494 THR B N   1 
ATOM   25746 C  CA  . THR C 1 1494 ? -7.860   26.914  82.347  1.00 110.33 ? 1494 THR B CA  1 
ATOM   25747 C  C   . THR C 1 1494 ? -8.839   27.907  83.032  1.00 93.15  ? 1494 THR B C   1 
ATOM   25748 O  O   . THR C 1 1494 ? -9.288   28.871  82.419  1.00 83.86  ? 1494 THR B O   1 
ATOM   25749 C  CB  . THR C 1 1494 ? -6.374   27.267  82.483  1.00 106.49 ? 1494 THR B CB  1 
ATOM   25750 O  OG1 . THR C 1 1494 ? -6.161   27.995  83.688  1.00 105.57 ? 1494 THR B OG1 1 
ATOM   25751 C  CG2 . THR C 1 1494 ? -5.890   28.069  81.255  1.00 102.84 ? 1494 THR B CG2 1 
ATOM   25752 N  N   . VAL C 1 1495 ? -9.220   27.617  84.274  1.00 99.03  ? 1495 VAL B N   1 
ATOM   25753 C  CA  . VAL C 1 1495 ? -10.077  28.509  85.057  1.00 106.99 ? 1495 VAL B CA  1 
ATOM   25754 C  C   . VAL C 1 1495 ? -9.734   28.494  86.552  1.00 111.16 ? 1495 VAL B C   1 
ATOM   25755 O  O   . VAL C 1 1495 ? -9.890   27.476  87.228  1.00 113.81 ? 1495 VAL B O   1 
ATOM   25756 C  CB  . VAL C 1 1495 ? -11.586  28.233  84.871  1.00 84.73  ? 1495 VAL B CB  1 
ATOM   25757 C  CG1 . VAL C 1 1495 ? -11.822  26.799  84.603  1.00 106.85 ? 1495 VAL B CG1 1 
ATOM   25758 C  CG2 . VAL C 1 1495 ? -12.365  28.677  86.111  1.00 84.28  ? 1495 VAL B CG2 1 
ATOM   25759 N  N   . TYR C 1 1496 ? -9.262   29.651  87.032  1.00 109.65 ? 1496 TYR B N   1 
ATOM   25760 C  CA  . TYR C 1 1496 ? -8.852   29.898  88.411  1.00 108.98 ? 1496 TYR B CA  1 
ATOM   25761 C  C   . TYR C 1 1496 ? -9.638   31.108  88.964  1.00 108.84 ? 1496 TYR B C   1 
ATOM   25762 O  O   . TYR C 1 1496 ? -10.323  31.825  88.211  1.00 107.31 ? 1496 TYR B O   1 
ATOM   25763 C  CB  . TYR C 1 1496 ? -7.348   30.192  88.459  1.00 106.18 ? 1496 TYR B CB  1 
ATOM   25764 C  CG  . TYR C 1 1496 ? -6.914   31.303  87.504  1.00 105.65 ? 1496 TYR B CG  1 
ATOM   25765 C  CD1 . TYR C 1 1496 ? -7.833   32.244  87.066  1.00 103.89 ? 1496 TYR B CD1 1 
ATOM   25766 C  CD2 . TYR C 1 1496 ? -5.583   31.433  87.067  1.00 105.72 ? 1496 TYR B CD2 1 
ATOM   25767 C  CE1 . TYR C 1 1496 ? -7.478   33.244  86.234  1.00 101.48 ? 1496 TYR B CE1 1 
ATOM   25768 C  CE2 . TYR C 1 1496 ? -5.211   32.464  86.210  1.00 104.00 ? 1496 TYR B CE2 1 
ATOM   25769 C  CZ  . TYR C 1 1496 ? -6.192   33.358  85.797  1.00 102.11 ? 1496 TYR B CZ  1 
ATOM   25770 O  OH  . TYR C 1 1496 ? -5.944   34.394  84.942  1.00 100.98 ? 1496 TYR B OH  1 
ATOM   25771 N  N   . GLU C 1 1497 ? -9.532   31.325  90.275  1.00 109.16 ? 1497 GLU B N   1 
ATOM   25772 C  CA  . GLU C 1 1497 ? -10.148  32.459  90.969  1.00 106.59 ? 1497 GLU B CA  1 
ATOM   25773 C  C   . GLU C 1 1497 ? -9.192   33.661  91.021  1.00 104.60 ? 1497 GLU B C   1 
ATOM   25774 O  O   . GLU C 1 1497 ? -8.027   33.527  91.403  1.00 101.40 ? 1497 GLU B O   1 
ATOM   25775 C  CB  . GLU C 1 1497 ? -10.500  32.016  92.381  1.00 106.23 ? 1497 GLU B CB  1 
ATOM   25776 C  CG  . GLU C 1 1497 ? -11.638  32.738  93.044  1.00 105.03 ? 1497 GLU B CG  1 
ATOM   25777 C  CD  . GLU C 1 1497 ? -12.180  31.938  94.210  1.00 105.76 ? 1497 GLU B CD  1 
ATOM   25778 O  OE1 . GLU C 1 1497 ? -11.751  30.782  94.392  1.00 104.46 ? 1497 GLU B OE1 1 
ATOM   25779 O  OE2 . GLU C 1 1497 ? -13.032  32.454  94.951  1.00 107.77 ? 1497 GLU B OE2 1 
ATOM   25780 N  N   . TYR C 1 1498 ? -9.688   34.840  90.662  1.00 106.22 ? 1498 TYR B N   1 
ATOM   25781 C  CA  . TYR C 1 1498 ? -8.800   35.983  90.468  1.00 106.61 ? 1498 TYR B CA  1 
ATOM   25782 C  C   . TYR C 1 1498 ? -7.913   36.217  91.682  1.00 105.66 ? 1498 TYR B C   1 
ATOM   25783 O  O   . TYR C 1 1498 ? -6.677   36.252  91.566  1.00 103.50 ? 1498 TYR B O   1 
ATOM   25784 C  CB  . TYR C 1 1498 ? -9.572   37.268  90.115  1.00 106.69 ? 1498 TYR B CB  1 
ATOM   25785 C  CG  . TYR C 1 1498 ? -8.686   38.344  89.500  1.00 107.82 ? 1498 TYR B CG  1 
ATOM   25786 C  CD1 . TYR C 1 1498 ? -7.923   38.070  88.383  1.00 109.97 ? 1498 TYR B CD1 1 
ATOM   25787 C  CD2 . TYR C 1 1498 ? -8.609   39.623  90.038  1.00 108.54 ? 1498 TYR B CD2 1 
ATOM   25788 C  CE1 . TYR C 1 1498 ? -7.109   39.024  87.812  1.00 110.53 ? 1498 TYR B CE1 1 
ATOM   25789 C  CE2 . TYR C 1 1498 ? -7.789   40.592  89.471  1.00 109.27 ? 1498 TYR B CE2 1 
ATOM   25790 C  CZ  . TYR C 1 1498 ? -7.037   40.281  88.354  1.00 110.42 ? 1498 TYR B CZ  1 
ATOM   25791 O  OH  . TYR C 1 1498 ? -6.215   41.217  87.759  1.00 110.98 ? 1498 TYR B OH  1 
ATOM   25792 N  N   . HIS C 1 1499 ? -8.549   36.355  92.841  1.00 105.05 ? 1499 HIS B N   1 
ATOM   25793 C  CA  . HIS C 1 1499 ? -7.827   36.689  94.051  1.00 102.92 ? 1499 HIS B CA  1 
ATOM   25794 C  C   . HIS C 1 1499 ? -7.136   35.504  94.715  1.00 107.55 ? 1499 HIS B C   1 
ATOM   25795 O  O   . HIS C 1 1499 ? -6.264   35.692  95.575  1.00 110.14 ? 1499 HIS B O   1 
ATOM   25796 C  CB  . HIS C 1 1499 ? -8.748   37.402  95.016  1.00 98.13  ? 1499 HIS B CB  1 
ATOM   25797 C  CG  . HIS C 1 1499 ? -9.117   38.767  94.560  1.00 93.84  ? 1499 HIS B CG  1 
ATOM   25798 N  ND1 . HIS C 1 1499 ? -10.378  39.291  94.727  1.00 93.87  ? 1499 HIS B ND1 1 
ATOM   25799 C  CD2 . HIS C 1 1499 ? -8.396   39.715  93.911  1.00 92.36  ? 1499 HIS B CD2 1 
ATOM   25800 C  CE1 . HIS C 1 1499 ? -10.415  40.514  94.217  1.00 93.09  ? 1499 HIS B CE1 1 
ATOM   25801 N  NE2 . HIS C 1 1499 ? -9.226   40.792  93.710  1.00 91.57  ? 1499 HIS B NE2 1 
ATOM   25802 N  N   . ARG C 1 1500 ? -7.513   34.290  94.325  1.00 107.16 ? 1500 ARG B N   1 
ATOM   25803 C  CA  . ARG C 1 1500 ? -6.764   33.126  94.768  1.00 107.32 ? 1500 ARG B CA  1 
ATOM   25804 C  C   . ARG C 1 1500 ? -6.569   32.115  93.642  1.00 104.90 ? 1500 ARG B C   1 
ATOM   25805 O  O   . ARG C 1 1500 ? -7.246   31.086  93.574  1.00 108.53 ? 1500 ARG B O   1 
ATOM   25806 C  CB  . ARG C 1 1500 ? -7.385   32.479  96.016  1.00 109.93 ? 1500 ARG B CB  1 
ATOM   25807 C  CG  . ARG C 1 1500 ? -8.817   32.866  96.307  1.00 112.26 ? 1500 ARG B CG  1 
ATOM   25808 C  CD  . ARG C 1 1500 ? -9.656   31.601  96.467  1.00 116.79 ? 1500 ARG B CD  1 
ATOM   25809 N  NE  . ARG C 1 1500 ? -10.019  31.283  97.842  1.00 119.20 ? 1500 ARG B NE  1 
ATOM   25810 C  CZ  . ARG C 1 1500 ? -10.671  30.177  98.192  1.00 121.46 ? 1500 ARG B CZ  1 
ATOM   25811 N  NH1 . ARG C 1 1500 ? -11.007  29.278  97.270  1.00 121.50 ? 1500 ARG B NH1 1 
ATOM   25812 N  NH2 . ARG C 1 1500 ? -10.971  29.960  99.467  1.00 123.38 ? 1500 ARG B NH2 1 
ATOM   25813 N  N   . PRO C 1 1501 ? -5.611   32.409  92.767  1.00 100.56 ? 1501 PRO B N   1 
ATOM   25814 C  CA  . PRO C 1 1501 ? -5.038   31.633  91.666  1.00 100.43 ? 1501 PRO B CA  1 
ATOM   25815 C  C   . PRO C 1 1501 ? -4.589   30.261  92.115  1.00 105.45 ? 1501 PRO B C   1 
ATOM   25816 O  O   . PRO C 1 1501 ? -4.011   29.531  91.327  1.00 105.46 ? 1501 PRO B O   1 
ATOM   25817 C  CB  . PRO C 1 1501 ? -3.773   32.404  91.328  1.00 98.92  ? 1501 PRO B CB  1 
ATOM   25818 C  CG  . PRO C 1 1501 ? -4.007   33.765  91.806  1.00 97.65  ? 1501 PRO B CG  1 
ATOM   25819 C  CD  . PRO C 1 1501 ? -4.975   33.720  92.917  1.00 97.46  ? 1501 PRO B CD  1 
ATOM   25820 N  N   . ASP C 1 1502 ? -4.772   29.945  93.389  1.00 111.02 ? 1502 ASP B N   1 
ATOM   25821 C  CA  . ASP C 1 1502 ? -4.289   28.684  93.930  1.00 116.21 ? 1502 ASP B CA  1 
ATOM   25822 C  C   . ASP C 1 1502 ? -5.332   27.686  93.484  1.00 122.13 ? 1502 ASP B C   1 
ATOM   25823 O  O   . ASP C 1 1502 ? -5.222   26.495  93.750  1.00 125.85 ? 1502 ASP B O   1 
ATOM   25824 C  CB  . ASP C 1 1502 ? -4.153   28.713  95.476  1.00 117.43 ? 1502 ASP B CB  1 
ATOM   25825 C  CG  . ASP C 1 1502 ? -4.064   30.153  96.062  1.00 113.52 ? 1502 ASP B CG  1 
ATOM   25826 O  OD1 . ASP C 1 1502 ? -3.235   30.994  95.586  1.00 109.29 ? 1502 ASP B OD1 1 
ATOM   25827 O  OD2 . ASP C 1 1502 ? -4.837   30.427  97.028  1.00 114.27 ? 1502 ASP B OD2 1 
ATOM   25828 N  N   . LYS C 1 1503 ? -6.347   28.190  92.788  1.00 125.12 ? 1503 LYS B N   1 
ATOM   25829 C  CA  . LYS C 1 1503 ? -7.465   27.367  92.328  1.00 132.40 ? 1503 LYS B CA  1 
ATOM   25830 C  C   . LYS C 1 1503 ? -7.494   27.004  90.784  1.00 118.68 ? 1503 LYS B C   1 
ATOM   25831 O  O   . LYS C 1 1503 ? -8.565   26.892  90.159  1.00 115.25 ? 1503 LYS B O   1 
ATOM   25832 C  CB  . LYS C 1 1503 ? -8.757   28.026  92.805  1.00 136.05 ? 1503 LYS B CB  1 
ATOM   25833 C  CG  . LYS C 1 1503 ? -9.172   27.651  94.243  1.00 139.85 ? 1503 LYS B CG  1 
ATOM   25834 C  CD  . LYS C 1 1503 ? -8.057   27.690  95.260  1.00 141.99 ? 1503 LYS B CD  1 
ATOM   25835 C  CE  . LYS C 1 1503 ? -8.392   26.756  96.443  1.00 147.43 ? 1503 LYS B CE  1 
ATOM   25836 N  NZ  . LYS C 1 1503 ? -7.220   26.416  97.341  1.00 150.06 ? 1503 LYS B NZ  1 
ATOM   25837 N  N   . GLN C 1 1504 ? -6.304   26.771  90.209  1.00 116.43 ? 1504 GLN B N   1 
ATOM   25838 C  CA  . GLN C 1 1504 ? -6.100   26.557  88.770  1.00 118.43 ? 1504 GLN B CA  1 
ATOM   25839 C  C   . GLN C 1 1504 ? -6.383   25.151  88.386  1.00 118.48 ? 1504 GLN B C   1 
ATOM   25840 O  O   . GLN C 1 1504 ? -5.498   24.309  88.432  1.00 87.95  ? 1504 GLN B O   1 
ATOM   25841 C  CB  . GLN C 1 1504 ? -4.660   26.936  88.319  1.00 108.22 ? 1504 GLN B CB  1 
ATOM   25842 C  CG  . GLN C 1 1504 ? -4.552   28.374  87.629  1.00 150.55 ? 1504 GLN B CG  1 
ATOM   25843 C  CD  . GLN C 1 1504 ? -3.127   29.039  87.605  1.00 127.47 ? 1504 GLN B CD  1 
ATOM   25844 O  OE1 . GLN C 1 1504 ? -2.955   30.241  87.244  1.00 120.44 ? 1504 GLN B OE1 1 
ATOM   25845 N  NE2 . GLN C 1 1504 ? -2.119   28.254  87.990  1.00 130.80 ? 1504 GLN B NE2 1 
ATOM   25846 N  N   . CYS C 1 1505 ? -7.637   24.918  88.015  1.00 114.33 ? 1505 CYS B N   1 
ATOM   25847 C  CA  . CYS C 1 1505 ? -7.977   23.752  87.203  1.00 110.63 ? 1505 CYS B CA  1 
ATOM   25848 C  C   . CYS C 1 1505 ? -7.656   23.991  85.725  1.00 109.19 ? 1505 CYS B C   1 
ATOM   25849 O  O   . CYS C 1 1505 ? -8.096   24.964  85.117  1.00 106.75 ? 1505 CYS B O   1 
ATOM   25850 C  CB  . CYS C 1 1505 ? -9.435   23.311  87.363  1.00 112.66 ? 1505 CYS B CB  1 
ATOM   25851 S  SG  . CYS C 1 1505 ? -9.673   21.626  86.712  1.00 168.19 ? 1505 CYS B SG  1 
ATOM   25852 N  N   . THR C 1 1506 ? -6.882   23.086  85.155  1.00 114.01 ? 1506 THR B N   1 
ATOM   25853 C  CA  . THR C 1 1506 ? -6.388   23.285  83.824  1.00 115.32 ? 1506 THR B CA  1 
ATOM   25854 C  C   . THR C 1 1506 ? -6.680   22.012  83.094  1.00 118.19 ? 1506 THR B C   1 
ATOM   25855 O  O   . THR C 1 1506 ? -6.640   20.929  83.695  1.00 120.06 ? 1506 THR B O   1 
ATOM   25856 C  CB  . THR C 1 1506 ? -4.892   23.517  83.840  1.00 116.91 ? 1506 THR B CB  1 
ATOM   25857 O  OG1 . THR C 1 1506 ? -4.598   24.551  84.780  1.00 119.48 ? 1506 THR B OG1 1 
ATOM   25858 C  CG2 . THR C 1 1506 ? -4.413   23.951  82.481  1.00 115.30 ? 1506 THR B CG2 1 
ATOM   25859 N  N   . MET C 1 1507 ? -6.984   22.160  81.799  1.00 118.42 ? 1507 MET B N   1 
ATOM   25860 C  CA  . MET C 1 1507 ? -7.349   21.045  80.915  1.00 116.61 ? 1507 MET B CA  1 
ATOM   25861 C  C   . MET C 1 1507 ? -6.922   21.268  79.457  1.00 112.46 ? 1507 MET B C   1 
ATOM   25862 O  O   . MET C 1 1507 ? -7.167   22.338  78.887  1.00 107.35 ? 1507 MET B O   1 
ATOM   25863 C  CB  . MET C 1 1507 ? -8.851   20.860  80.950  1.00 115.81 ? 1507 MET B CB  1 
ATOM   25864 C  CG  . MET C 1 1507 ? -9.335   19.560  80.392  1.00 118.77 ? 1507 MET B CG  1 
ATOM   25865 S  SD  . MET C 1 1507 ? -11.080  19.843  80.140  1.00 107.27 ? 1507 MET B SD  1 
ATOM   25866 C  CE  . MET C 1 1507 ? -11.169  21.470  80.887  1.00 97.55  ? 1507 MET B CE  1 
ATOM   25867 N  N   . PHE C 1 1508 ? -6.273   20.266  78.867  1.00 114.23 ? 1508 PHE B N   1 
ATOM   25868 C  CA  . PHE C 1 1508 ? -6.030   20.274  77.434  1.00 116.75 ? 1508 PHE B CA  1 
ATOM   25869 C  C   . PHE C 1 1508 ? -7.340   19.915  76.714  1.00 126.92 ? 1508 PHE B C   1 
ATOM   25870 O  O   . PHE C 1 1508 ? -8.139   19.120  77.235  1.00 133.99 ? 1508 PHE B O   1 
ATOM   25871 C  CB  . PHE C 1 1508 ? -5.028   19.195  77.085  1.00 111.77 ? 1508 PHE B CB  1 
ATOM   25872 C  CG  . PHE C 1 1508 ? -3.616   19.557  77.324  1.00 103.91 ? 1508 PHE B CG  1 
ATOM   25873 C  CD1 . PHE C 1 1508 ? -3.049   20.628  76.694  1.00 101.43 ? 1508 PHE B CD1 1 
ATOM   25874 C  CD2 . PHE C 1 1508 ? -2.826   18.769  78.124  1.00 101.94 ? 1508 PHE B CD2 1 
ATOM   25875 C  CE1 . PHE C 1 1508 ? -1.709   20.941  76.901  1.00 100.74 ? 1508 PHE B CE1 1 
ATOM   25876 C  CE2 . PHE C 1 1508 ? -1.500   19.067  78.331  1.00 101.07 ? 1508 PHE B CE2 1 
ATOM   25877 C  CZ  . PHE C 1 1508 ? -0.937   20.158  77.722  1.00 99.79  ? 1508 PHE B CZ  1 
ATOM   25878 N  N   . TYR C 1 1509 ? -7.562   20.467  75.521  1.00 125.56 ? 1509 TYR B N   1 
ATOM   25879 C  CA  . TYR C 1 1509 ? -8.662   20.016  74.655  1.00 125.25 ? 1509 TYR B CA  1 
ATOM   25880 C  C   . TYR C 1 1509 ? -8.213   20.300  73.245  1.00 127.66 ? 1509 TYR B C   1 
ATOM   25881 O  O   . TYR C 1 1509 ? -7.224   21.011  73.032  1.00 127.71 ? 1509 TYR B O   1 
ATOM   25882 C  CB  . TYR C 1 1509 ? -9.961   20.783  74.902  1.00 117.97 ? 1509 TYR B CB  1 
ATOM   25883 C  CG  . TYR C 1 1509 ? -9.902   22.164  74.320  1.00 111.22 ? 1509 TYR B CG  1 
ATOM   25884 C  CD1 . TYR C 1 1509 ? -10.965  22.708  73.653  1.00 108.95 ? 1509 TYR B CD1 1 
ATOM   25885 C  CD2 . TYR C 1 1509 ? -8.740   22.916  74.419  1.00 110.02 ? 1509 TYR B CD2 1 
ATOM   25886 C  CE1 . TYR C 1 1509 ? -10.886  23.984  73.114  1.00 107.27 ? 1509 TYR B CE1 1 
ATOM   25887 C  CE2 . TYR C 1 1509 ? -8.646   24.187  73.886  1.00 107.69 ? 1509 TYR B CE2 1 
ATOM   25888 C  CZ  . TYR C 1 1509 ? -9.723   24.717  73.235  1.00 106.47 ? 1509 TYR B CZ  1 
ATOM   25889 O  OH  . TYR C 1 1509 ? -9.627   25.984  72.712  1.00 104.24 ? 1509 TYR B OH  1 
ATOM   25890 N  N   . SER C 1 1510 ? -8.936   19.766  72.275  1.00 128.26 ? 1510 SER B N   1 
ATOM   25891 C  CA  . SER C 1 1510 ? -8.584   20.059  70.907  1.00 127.83 ? 1510 SER B CA  1 
ATOM   25892 C  C   . SER C 1 1510 ? -9.807   20.500  70.149  1.00 129.19 ? 1510 SER B C   1 
ATOM   25893 O  O   . SER C 1 1510 ? -10.943  20.231  70.532  1.00 128.99 ? 1510 SER B O   1 
ATOM   25894 C  CB  . SER C 1 1510 ? -7.928   18.866  70.216  1.00 128.42 ? 1510 SER B CB  1 
ATOM   25895 O  OG  . SER C 1 1510 ? -7.218   19.298  69.061  1.00 126.59 ? 1510 SER B OG  1 
ATOM   25896 N  N   . THR C 1 1511 ? -9.552   21.193  69.060  1.00 131.08 ? 1511 THR B N   1 
ATOM   25897 C  CA  . THR C 1 1511 ? -10.590  21.857  68.334  1.00 131.55 ? 1511 THR B CA  1 
ATOM   25898 C  C   . THR C 1 1511 ? -10.934  21.041  67.123  1.00 142.13 ? 1511 THR B C   1 
ATOM   25899 O  O   . THR C 1 1511 ? -11.531  21.556  66.189  1.00 144.18 ? 1511 THR B O   1 
ATOM   25900 C  CB  . THR C 1 1511 ? -10.090  23.198  67.881  1.00 123.61 ? 1511 THR B CB  1 
ATOM   25901 O  OG1 . THR C 1 1511 ? -11.203  24.053  67.647  1.00 122.15 ? 1511 THR B OG1 1 
ATOM   25902 C  CG2 . THR C 1 1511 ? -9.245   23.057  66.624  1.00 122.41 ? 1511 THR B CG2 1 
ATOM   25903 N  N   . SER C 1 1512 ? -10.545  19.769  67.126  1.00 151.77 ? 1512 SER B N   1 
ATOM   25904 C  CA  . SER C 1 1512 ? -10.852  18.886  66.006  1.00 162.62 ? 1512 SER B CA  1 
ATOM   25905 C  C   . SER C 1 1512 ? -10.668  17.415  66.340  1.00 175.68 ? 1512 SER B C   1 
ATOM   25906 O  O   . SER C 1 1512 ? -9.833   17.045  67.167  1.00 175.97 ? 1512 SER B O   1 
ATOM   25907 C  CB  . SER C 1 1512 ? -9.995   19.239  64.795  1.00 161.84 ? 1512 SER B CB  1 
ATOM   25908 O  OG  . SER C 1 1512 ? -8.646   18.855  64.985  1.00 161.58 ? 1512 SER B OG  1 
ATOM   25909 N  N   . ASN C 1 1513 ? -11.452  16.547  65.673  1.00 188.44 ? 1513 ASN B N   1 
ATOM   25910 C  CA  . ASN C 1 1513 ? -11.428  15.113  65.922  1.00 201.20 ? 1513 ASN B CA  1 
ATOM   25911 C  C   . ASN C 1 1513 ? -10.568  14.297  64.975  1.00 209.20 ? 1513 ASN B C   1 
ATOM   25912 O  O   . ASN C 1 1513 ? -10.383  13.112  65.204  1.00 213.59 ? 1513 ASN B O   1 
ATOM   25913 C  CB  . ASN C 1 1513 ? -12.851  14.575  65.873  1.00 207.36 ? 1513 ASN B CB  1 
ATOM   25914 C  CG  . ASN C 1 1513 ? -13.914  15.600  66.196  1.00 208.46 ? 1513 ASN B CG  1 
ATOM   25915 O  OD1 . ASN C 1 1513 ? -13.824  16.281  67.216  1.00 206.74 ? 1513 ASN B OD1 1 
ATOM   25916 N  ND2 . ASN C 1 1513 ? -14.929  15.711  65.349  1.00 211.05 ? 1513 ASN B ND2 1 
ATOM   25917 N  N   . ILE C 1 1514 ? -10.050  14.906  63.952  1.00 210.61 ? 1514 ILE B N   1 
ATOM   25918 C  CA  . ILE C 1 1514 ? -9.263   14.238  62.954  1.00 213.72 ? 1514 ILE B CA  1 
ATOM   25919 C  C   . ILE C 1 1514 ? -8.167   13.321  63.436  1.00 215.12 ? 1514 ILE B C   1 
ATOM   25920 O  O   . ILE C 1 1514 ? -7.594   13.460  64.516  1.00 212.83 ? 1514 ILE B O   1 
ATOM   25921 C  CB  . ILE C 1 1514 ? -8.553   15.305  62.098  1.00 225.12 ? 1514 ILE B CB  1 
ATOM   25922 C  CG1 . ILE C 1 1514 ? -9.527   16.220  61.364  1.00 222.47 ? 1514 ILE B CG1 1 
ATOM   25923 C  CG2 . ILE C 1 1514 ? -7.618   14.644  61.086  1.00 228.01 ? 1514 ILE B CG2 1 
ATOM   25924 C  CD1 . ILE C 1 1514 ? -8.873   17.420  60.716  1.00 219.37 ? 1514 ILE B CD1 1 
ATOM   25925 N  N   . LYS C 1 1515 ? -7.904   12.383  62.548  1.00 236.34 ? 1515 LYS B N   1 
ATOM   25926 C  CA  . LYS C 1 1515 ? -6.775   11.474  62.589  1.00 237.68 ? 1515 LYS B CA  1 
ATOM   25927 C  C   . LYS C 1 1515 ? -6.313   11.417  61.120  1.00 235.52 ? 1515 LYS B C   1 
ATOM   25928 O  O   . LYS C 1 1515 ? -6.803   10.584  60.364  1.00 233.89 ? 1515 LYS B O   1 
ATOM   25929 C  CB  . LYS C 1 1515 ? -7.099   10.112  63.218  1.00 238.29 ? 1515 LYS B CB  1 
ATOM   25930 C  CG  . LYS C 1 1515 ? -8.070   9.221   62.457  1.00 240.46 ? 1515 LYS B CG  1 
ATOM   25931 C  CD  . LYS C 1 1515 ? -8.183   7.852   63.132  1.00 242.18 ? 1515 LYS B CD  1 
ATOM   25932 C  CE  . LYS C 1 1515 ? -8.765   7.960   64.531  1.00 245.19 ? 1515 LYS B CE  1 
ATOM   25933 N  NZ  . LYS C 1 1515 ? -8.913   6.626   65.174  1.00 248.24 ? 1515 LYS B NZ  1 
ATOM   25934 N  N   . ILE C 1 1516 ? -5.376   12.293  60.692  1.00 251.02 ? 1516 ILE B N   1 
ATOM   25935 C  CA  . ILE C 1 1516 ? -4.854   12.308  59.301  1.00 252.12 ? 1516 ILE B CA  1 
ATOM   25936 C  C   . ILE C 1 1516 ? -3.573   11.549  59.152  1.00 255.68 ? 1516 ILE B C   1 
ATOM   25937 O  O   . ILE C 1 1516 ? -2.629   11.671  59.922  1.00 258.89 ? 1516 ILE B O   1 
ATOM   25938 C  CB  . ILE C 1 1516 ? -4.478   13.685  58.724  1.00 166.78 ? 1516 ILE B CB  1 
ATOM   25939 C  CG1 . ILE C 1 1516 ? -4.885   14.815  59.667  1.00 166.39 ? 1516 ILE B CG1 1 
ATOM   25940 C  CG2 . ILE C 1 1516 ? -5.127   13.865  57.356  1.00 165.05 ? 1516 ILE B CG2 1 
ATOM   25941 C  CD1 . ILE C 1 1516 ? -4.332   16.164  59.262  1.00 166.86 ? 1516 ILE B CD1 1 
ATOM   25942 N  N   . GLN C 1 1517 ? -3.623   10.780  58.076  1.00 255.82 ? 1517 GLN B N   1 
ATOM   25943 C  CA  . GLN C 1 1517 ? -2.598   9.912   57.582  1.00 258.35 ? 1517 GLN B CA  1 
ATOM   25944 C  C   . GLN C 1 1517 ? -2.183   10.316  56.150  1.00 255.54 ? 1517 GLN B C   1 
ATOM   25945 O  O   . GLN C 1 1517 ? -3.036   10.543  55.302  1.00 251.44 ? 1517 GLN B O   1 
ATOM   25946 C  CB  . GLN C 1 1517 ? -3.066   8.457   57.619  1.00 261.04 ? 1517 GLN B CB  1 
ATOM   25947 C  CG  . GLN C 1 1517 ? -3.310   7.919   59.018  1.00 268.80 ? 1517 GLN B CG  1 
ATOM   25948 C  CD  . GLN C 1 1517 ? -4.698   8.245   59.534  1.00 276.71 ? 1517 GLN B CD  1 
ATOM   25949 O  OE1 . GLN C 1 1517 ? -5.056   7.880   60.652  1.00 277.49 ? 1517 GLN B OE1 1 
ATOM   25950 N  NE2 . GLN C 1 1517 ? -5.640   8.920   58.887  1.00 282.57 ? 1517 GLN B NE2 1 
ATOM   25951 N  N   . LYS C 1 1518 ? -0.855   10.415  55.873  1.00 257.19 ? 1518 LYS B N   1 
ATOM   25952 C  CA  . LYS C 1 1518 ? -0.344   10.843  54.541  1.00 254.39 ? 1518 LYS B CA  1 
ATOM   25953 C  C   . LYS C 1 1518 ? 0.844    9.972   54.073  1.00 260.39 ? 1518 LYS B C   1 
ATOM   25954 O  O   . LYS C 1 1518 ? 1.609    9.477   54.902  1.00 264.61 ? 1518 LYS B O   1 
ATOM   25955 C  CB  . LYS C 1 1518 ? 0.070    12.324  54.565  1.00 246.84 ? 1518 LYS B CB  1 
ATOM   25956 C  CG  . LYS C 1 1518 ? -1.027   13.309  54.959  1.00 233.23 ? 1518 LYS B CG  1 
ATOM   25957 C  CD  . LYS C 1 1518 ? -0.474   14.721  55.119  1.00 225.23 ? 1518 LYS B CD  1 
ATOM   25958 C  CE  . LYS C 1 1518 ? -1.268   15.507  56.154  1.00 217.58 ? 1518 LYS B CE  1 
ATOM   25959 N  NZ  . LYS C 1 1518 ? -0.467   16.597  56.766  1.00 217.23 ? 1518 LYS B NZ  1 
ATOM   25960 N  N   . VAL C 1 1519 ? 0.997    9.801   52.752  1.00 261.15 ? 1519 VAL B N   1 
ATOM   25961 C  CA  . VAL C 1 1519 ? 2.015    8.896   52.171  1.00 265.93 ? 1519 VAL B CA  1 
ATOM   25962 C  C   . VAL C 1 1519 ? 3.434    9.469   52.098  1.00 270.07 ? 1519 VAL B C   1 
ATOM   25963 O  O   . VAL C 1 1519 ? 4.285    9.142   52.927  1.00 276.19 ? 1519 VAL B O   1 
ATOM   25964 C  CB  . VAL C 1 1519 ? 1.615    8.402   50.765  1.00 265.75 ? 1519 VAL B CB  1 
ATOM   25965 C  CG1 . VAL C 1 1519 ? 2.708    7.515   50.187  1.00 270.97 ? 1519 VAL B CG1 1 
ATOM   25966 C  CG2 . VAL C 1 1519 ? 0.309    7.650   50.838  1.00 261.98 ? 1519 VAL B CG2 1 
ATOM   25967 N  N   . CYS C 1 1520 ? 3.692    10.290  51.079  1.00 265.84 ? 1520 CYS B N   1 
ATOM   25968 C  CA  . CYS C 1 1520 ? 4.910    11.113  51.030  1.00 264.11 ? 1520 CYS B CA  1 
ATOM   25969 C  C   . CYS C 1 1520 ? 4.732    12.268  50.053  1.00 256.38 ? 1520 CYS B C   1 
ATOM   25970 O  O   . CYS C 1 1520 ? 5.258    12.249  48.939  1.00 256.70 ? 1520 CYS B O   1 
ATOM   25971 C  CB  . CYS C 1 1520 ? 6.172    10.290  50.697  1.00 270.21 ? 1520 CYS B CB  1 
ATOM   25972 S  SG  . CYS C 1 1520 ? 7.521    10.339  51.971  1.00 242.36 ? 1520 CYS B SG  1 
ATOM   25973 N  N   . GLU C 1 1521 ? 3.961    13.258  50.493  1.00 247.94 ? 1521 GLU B N   1 
ATOM   25974 C  CA  . GLU C 1 1521 ? 3.689    14.451  49.709  1.00 239.76 ? 1521 GLU B CA  1 
ATOM   25975 C  C   . GLU C 1 1521 ? 4.607    15.587  50.112  1.00 234.76 ? 1521 GLU B C   1 
ATOM   25976 O  O   . GLU C 1 1521 ? 5.238    15.551  51.168  1.00 237.00 ? 1521 GLU B O   1 
ATOM   25977 C  CB  . GLU C 1 1521 ? 2.240    14.889  49.893  1.00 233.23 ? 1521 GLU B CB  1 
ATOM   25978 C  CG  . GLU C 1 1521 ? 1.252    13.755  49.787  1.00 227.45 ? 1521 GLU B CG  1 
ATOM   25979 C  CD  . GLU C 1 1521 ? -0.144   14.246  49.528  1.00 218.56 ? 1521 GLU B CD  1 
ATOM   25980 O  OE1 . GLU C 1 1521 ? -0.313   15.473  49.380  1.00 214.86 ? 1521 GLU B OE1 1 
ATOM   25981 O  OE2 . GLU C 1 1521 ? -1.066   13.406  49.469  1.00 215.44 ? 1521 GLU B OE2 1 
ATOM   25982 N  N   . GLY C 1 1522 ? 4.671    16.604  49.264  1.00 226.82 ? 1522 GLY B N   1 
ATOM   25983 C  CA  . GLY C 1 1522 ? 5.475    17.771  49.549  1.00 221.15 ? 1522 GLY B CA  1 
ATOM   25984 C  C   . GLY C 1 1522 ? 4.899    18.577  50.691  1.00 213.10 ? 1522 GLY B C   1 
ATOM   25985 O  O   . GLY C 1 1522 ? 3.767    18.348  51.138  1.00 209.58 ? 1522 GLY B O   1 
ATOM   25986 N  N   . ALA C 1 1523 ? 5.693    19.527  51.167  1.00 209.47 ? 1523 ALA B N   1 
ATOM   25987 C  CA  . ALA C 1 1523 ? 5.248    20.408  52.222  1.00 202.33 ? 1523 ALA B CA  1 
ATOM   25988 C  C   . ALA C 1 1523 ? 4.766    19.583  53.409  1.00 197.37 ? 1523 ALA B C   1 
ATOM   25989 O  O   . ALA C 1 1523 ? 4.002    20.059  54.233  1.00 194.45 ? 1523 ALA B O   1 
ATOM   25990 C  CB  . ALA C 1 1523 ? 4.139    21.326  51.706  1.00 198.04 ? 1523 ALA B CB  1 
ATOM   25991 N  N   . ALA C 1 1524 ? 5.207    18.337  53.503  1.00 196.70 ? 1524 ALA B N   1 
ATOM   25992 C  CA  . ALA C 1 1524 ? 4.796    17.510  54.629  1.00 195.03 ? 1524 ALA B CA  1 
ATOM   25993 C  C   . ALA C 1 1524 ? 5.785    16.378  54.947  1.00 198.83 ? 1524 ALA B C   1 
ATOM   25994 O  O   . ALA C 1 1524 ? 6.715    16.566  55.728  1.00 201.23 ? 1524 ALA B O   1 
ATOM   25995 C  CB  . ALA C 1 1524 ? 3.382    16.973  54.411  1.00 191.18 ? 1524 ALA B CB  1 
ATOM   25996 N  N   . CYS C 1 1525 ? 5.597    15.210  54.344  1.00 199.98 ? 1525 CYS B N   1 
ATOM   25997 C  CA  . CYS C 1 1525 ? 6.447    14.059  54.646  1.00 205.93 ? 1525 CYS B CA  1 
ATOM   25998 C  C   . CYS C 1 1525 ? 7.929    14.366  54.440  1.00 212.30 ? 1525 CYS B C   1 
ATOM   25999 O  O   . CYS C 1 1525 ? 8.297    15.480  54.057  1.00 212.49 ? 1525 CYS B O   1 
ATOM   26000 C  CB  . CYS C 1 1525 ? 6.018    12.839  53.817  1.00 206.60 ? 1525 CYS B CB  1 
ATOM   26001 S  SG  . CYS C 1 1525 ? 7.226    11.465  53.648  1.00 340.65 ? 1525 CYS B SG  1 
ATOM   26002 N  N   . LYS C 1 1526 ? 8.765    13.363  54.707  1.00 218.59 ? 1526 LYS B N   1 
ATOM   26003 C  CA  . LYS C 1 1526 ? 10.219   13.468  54.594  1.00 226.44 ? 1526 LYS B CA  1 
ATOM   26004 C  C   . LYS C 1 1526 ? 10.722   14.625  55.453  1.00 224.39 ? 1526 LYS B C   1 
ATOM   26005 O  O   . LYS C 1 1526 ? 11.765   15.229  55.186  1.00 226.35 ? 1526 LYS B O   1 
ATOM   26006 C  CB  . LYS C 1 1526 ? 10.660   13.593  53.123  1.00 233.53 ? 1526 LYS B CB  1 
ATOM   26007 C  CG  . LYS C 1 1526 ? 10.611   15.007  52.535  1.00 236.64 ? 1526 LYS B CG  1 
ATOM   26008 C  CD  . LYS C 1 1526 ? 11.022   15.014  51.066  1.00 242.66 ? 1526 LYS B CD  1 
ATOM   26009 C  CE  . LYS C 1 1526 ? 11.498   16.389  50.636  1.00 244.07 ? 1526 LYS B CE  1 
ATOM   26010 N  NZ  . LYS C 1 1526 ? 12.714   16.807  51.395  1.00 248.80 ? 1526 LYS B NZ  1 
ATOM   26011 N  N   . CYS C 1 1527 ? 9.966    14.925  56.500  1.00 220.10 ? 1527 CYS B N   1 
ATOM   26012 C  CA  . CYS C 1 1527 ? 10.330   16.030  57.353  1.00 218.62 ? 1527 CYS B CA  1 
ATOM   26013 C  C   . CYS C 1 1527 ? 9.405    16.155  58.564  1.00 212.28 ? 1527 CYS B C   1 
ATOM   26014 O  O   . CYS C 1 1527 ? 9.538    17.092  59.345  1.00 210.91 ? 1527 CYS B O   1 
ATOM   26015 C  CB  . CYS C 1 1527 ? 10.349   17.324  56.540  1.00 217.69 ? 1527 CYS B CB  1 
ATOM   26016 S  SG  . CYS C 1 1527 ? 11.923   18.217  56.597  1.00 314.36 ? 1527 CYS B SG  1 
ATOM   26017 N  N   . VAL C 1 1528 ? 8.456    15.235  58.720  1.00 207.86 ? 1528 VAL B N   1 
ATOM   26018 C  CA  . VAL C 1 1528 ? 7.731    15.127  59.995  1.00 203.79 ? 1528 VAL B CA  1 
ATOM   26019 C  C   . VAL C 1 1528 ? 7.927    13.754  60.657  1.00 208.94 ? 1528 VAL B C   1 
ATOM   26020 O  O   . VAL C 1 1528 ? 8.419    13.660  61.788  1.00 212.21 ? 1528 VAL B O   1 
ATOM   26021 C  CB  . VAL C 1 1528 ? 6.234    15.473  59.870  1.00 193.02 ? 1528 VAL B CB  1 
ATOM   26022 C  CG1 . VAL C 1 1528 ? 5.546    15.362  61.224  1.00 189.69 ? 1528 VAL B CG1 1 
ATOM   26023 C  CG2 . VAL C 1 1528 ? 6.083    16.869  59.342  1.00 189.10 ? 1528 VAL B CG2 1 
ATOM   26024 N  N   . GLU C 1 1529 ? 7.541    12.698  59.945  1.00 210.00 ? 1529 GLU B N   1 
ATOM   26025 C  CA  . GLU C 1 1529 ? 7.855    11.329  60.356  1.00 215.55 ? 1529 GLU B CA  1 
ATOM   26026 C  C   . GLU C 1 1529 ? 9.366    11.148  60.291  1.00 224.20 ? 1529 GLU B C   1 
ATOM   26027 O  O   . GLU C 1 1529 ? 9.930    10.186  60.823  1.00 226.70 ? 1529 GLU B O   1 
ATOM   26028 C  CB  . GLU C 1 1529 ? 7.166    10.319  59.429  1.00 213.94 ? 1529 GLU B CB  1 
ATOM   26029 C  CG  . GLU C 1 1529 ? 7.466    8.856   59.745  1.00 217.67 ? 1529 GLU B CG  1 
ATOM   26030 C  CD  . GLU C 1 1529 ? 6.727    8.363   60.973  1.00 216.01 ? 1529 GLU B CD  1 
ATOM   26031 O  OE1 . GLU C 1 1529 ? 5.498    8.135   60.874  1.00 211.08 ? 1529 GLU B OE1 1 
ATOM   26032 O  OE2 . GLU C 1 1529 ? 7.379    8.203   62.031  1.00 219.38 ? 1529 GLU B OE2 1 
ATOM   26033 N  N   . ALA C 1 1530 ? 10.007   12.091  59.611  1.00 229.66 ? 1530 ALA B N   1 
ATOM   26034 C  CA  . ALA C 1 1530 ? 11.446   12.100  59.457  1.00 240.65 ? 1530 ALA B CA  1 
ATOM   26035 C  C   . ALA C 1 1530 ? 12.089   12.907  60.569  1.00 246.02 ? 1530 ALA B C   1 
ATOM   26036 O  O   . ALA C 1 1530 ? 12.833   13.843  60.298  1.00 247.19 ? 1530 ALA B O   1 
ATOM   26037 C  CB  . ALA C 1 1530 ? 11.825   12.672  58.101  1.00 241.39 ? 1530 ALA B CB  1 
ATOM   26038 N  N   . ASP C 1 1531 ? 11.777   12.549  61.813  1.00 249.66 ? 1531 ASP B N   1 
ATOM   26039 C  CA  . ASP C 1 1531 ? 12.460   13.098  62.989  1.00 255.71 ? 1531 ASP B CA  1 
ATOM   26040 C  C   . ASP C 1 1531 ? 12.118   12.353  64.292  1.00 260.05 ? 1531 ASP B C   1 
ATOM   26041 O  O   . ASP C 1 1531 ? 12.685   12.637  65.353  1.00 263.16 ? 1531 ASP B O   1 
ATOM   26042 C  CB  . ASP C 1 1531 ? 12.211   14.607  63.122  1.00 251.26 ? 1531 ASP B CB  1 
ATOM   26043 C  CG  . ASP C 1 1531 ? 13.283   15.440  62.426  1.00 252.90 ? 1531 ASP B CG  1 
ATOM   26044 O  OD1 . ASP C 1 1531 ? 14.379   15.618  63.004  1.00 257.42 ? 1531 ASP B OD1 1 
ATOM   26045 O  OD2 . ASP C 1 1531 ? 13.029   15.916  61.300  1.00 249.64 ? 1531 ASP B OD2 1 
ATOM   26046 N  N   . CYS C 1 1532 ? 11.207   11.386  64.188  1.00 260.62 ? 1532 CYS B N   1 
ATOM   26047 C  CA  . CYS C 1 1532 ? 10.747   10.583  65.328  1.00 263.12 ? 1532 CYS B CA  1 
ATOM   26048 C  C   . CYS C 1 1532 ? 11.844   9.672   65.930  1.00 270.13 ? 1532 CYS B C   1 
ATOM   26049 O  O   . CYS C 1 1532 ? 12.048   9.600   67.147  1.00 272.00 ? 1532 CYS B O   1 
ATOM   26050 C  CB  . CYS C 1 1532 ? 9.503    9.756   64.929  1.00 259.48 ? 1532 CYS B CB  1 
ATOM   26051 S  SG  . CYS C 1 1532 ? 8.011    10.712  64.394  1.00 245.56 ? 1532 CYS B SG  1 
ATOM   26052 N  N   . LEU D 2 40   ? 20.554   117.457 51.367  1.00 211.21 ? 40   LEU Y N   1 
ATOM   26053 C  CA  . LEU D 2 40   ? 20.837   116.964 50.023  1.00 211.18 ? 40   LEU Y CA  1 
ATOM   26054 C  C   . LEU D 2 40   ? 19.586   116.978 49.134  1.00 213.49 ? 40   LEU Y C   1 
ATOM   26055 O  O   . LEU D 2 40   ? 19.678   117.191 47.922  1.00 213.69 ? 40   LEU Y O   1 
ATOM   26056 C  CB  . LEU D 2 40   ? 21.479   115.578 50.091  1.00 209.60 ? 40   LEU Y CB  1 
ATOM   26057 C  CG  . LEU D 2 40   ? 22.838   115.573 50.805  1.00 208.08 ? 40   LEU Y CG  1 
ATOM   26058 C  CD1 . LEU D 2 40   ? 23.422   114.170 50.871  1.00 208.67 ? 40   LEU Y CD1 1 
ATOM   26059 C  CD2 . LEU D 2 40   ? 23.818   116.539 50.132  1.00 207.62 ? 40   LEU Y CD2 1 
ATOM   26060 N  N   . HIS D 2 41   ? 18.432   116.722 49.754  1.00 214.56 ? 41   HIS Y N   1 
ATOM   26061 C  CA  . HIS D 2 41   ? 17.100   117.084 49.226  1.00 218.46 ? 41   HIS Y CA  1 
ATOM   26062 C  C   . HIS D 2 41   ? 16.685   116.541 47.827  1.00 237.44 ? 41   HIS Y C   1 
ATOM   26063 O  O   . HIS D 2 41   ? 17.393   116.720 46.836  1.00 237.89 ? 41   HIS Y O   1 
ATOM   26064 C  CB  . HIS D 2 41   ? 16.907   118.619 49.304  1.00 229.74 ? 41   HIS Y CB  1 
ATOM   26065 C  CG  . HIS D 2 41   ? 17.506   119.260 50.529  1.00 235.56 ? 41   HIS Y CG  1 
ATOM   26066 N  ND1 . HIS D 2 41   ? 18.839   119.616 50.613  1.00 238.37 ? 41   HIS Y ND1 1 
ATOM   26067 C  CD2 . HIS D 2 41   ? 16.950   119.636 51.707  1.00 235.12 ? 41   HIS Y CD2 1 
ATOM   26068 C  CE1 . HIS D 2 41   ? 19.078   120.163 51.790  1.00 237.86 ? 41   HIS Y CE1 1 
ATOM   26069 N  NE2 . HIS D 2 41   ? 17.947   120.189 52.475  1.00 235.95 ? 41   HIS Y NE2 1 
ATOM   26070 N  N   . ASP D 2 42   ? 15.519   115.893 47.776  1.00 235.86 ? 42   ASP Y N   1 
ATOM   26071 C  CA  . ASP D 2 42   ? 14.897   115.389 46.539  1.00 235.10 ? 42   ASP Y CA  1 
ATOM   26072 C  C   . ASP D 2 42   ? 13.856   114.326 46.913  1.00 230.28 ? 42   ASP Y C   1 
ATOM   26073 O  O   . ASP D 2 42   ? 13.963   113.718 47.972  1.00 232.45 ? 42   ASP Y O   1 
ATOM   26074 C  CB  . ASP D 2 42   ? 15.934   114.793 45.581  1.00 239.63 ? 42   ASP Y CB  1 
ATOM   26075 C  CG  . ASP D 2 42   ? 15.391   114.606 44.163  1.00 239.89 ? 42   ASP Y CG  1 
ATOM   26076 O  OD1 . ASP D 2 42   ? 14.301   114.015 43.991  1.00 238.87 ? 42   ASP Y OD1 1 
ATOM   26077 O  OD2 . ASP D 2 42   ? 16.068   115.047 43.212  1.00 240.93 ? 42   ASP Y OD2 1 
ATOM   26078 N  N   . ILE D 2 43   ? 12.852   114.102 46.065  1.00 223.99 ? 43   ILE Y N   1 
ATOM   26079 C  CA  . ILE D 2 43   ? 11.839   113.086 46.369  1.00 219.76 ? 43   ILE Y CA  1 
ATOM   26080 C  C   . ILE D 2 43   ? 12.155   111.698 45.794  1.00 218.54 ? 43   ILE Y C   1 
ATOM   26081 O  O   . ILE D 2 43   ? 11.896   110.679 46.440  1.00 217.03 ? 43   ILE Y O   1 
ATOM   26082 C  CB  . ILE D 2 43   ? 10.409   113.520 45.960  1.00 216.94 ? 43   ILE Y CB  1 
ATOM   26083 C  CG1 . ILE D 2 43   ? 9.382    112.540 46.551  1.00 213.60 ? 43   ILE Y CG1 1 
ATOM   26084 C  CG2 . ILE D 2 43   ? 10.289   113.638 44.438  1.00 219.72 ? 43   ILE Y CG2 1 
ATOM   26085 C  CD1 . ILE D 2 43   ? 7.941    112.905 46.308  1.00 208.86 ? 43   ILE Y CD1 1 
ATOM   26086 N  N   . ARG D 2 44   ? 12.712   111.660 44.587  1.00 219.97 ? 44   ARG Y N   1 
ATOM   26087 C  CA  . ARG D 2 44   ? 13.064   110.389 43.956  1.00 222.55 ? 44   ARG Y CA  1 
ATOM   26088 C  C   . ARG D 2 44   ? 14.057   109.579 44.798  1.00 229.80 ? 44   ARG Y C   1 
ATOM   26089 O  O   . ARG D 2 44   ? 13.861   108.381 45.020  1.00 231.35 ? 44   ARG Y O   1 
ATOM   26090 C  CB  . ARG D 2 44   ? 13.590   110.610 42.528  1.00 219.66 ? 44   ARG Y CB  1 
ATOM   26091 C  CG  . ARG D 2 44   ? 12.559   110.307 41.446  1.00 214.05 ? 44   ARG Y CG  1 
ATOM   26092 C  CD  . ARG D 2 44   ? 12.710   111.203 40.225  1.00 210.39 ? 44   ARG Y CD  1 
ATOM   26093 N  NE  . ARG D 2 44   ? 12.587   112.623 40.564  1.00 206.51 ? 44   ARG Y NE  1 
ATOM   26094 C  CZ  . ARG D 2 44   ? 12.173   113.572 39.723  1.00 202.60 ? 44   ARG Y CZ  1 
ATOM   26095 N  NH1 . ARG D 2 44   ? 11.818   113.264 38.480  1.00 200.83 ? 44   ARG Y NH1 1 
ATOM   26096 N  NH2 . ARG D 2 44   ? 12.105   114.835 40.129  1.00 200.63 ? 44   ARG Y NH2 1 
ATOM   26097 N  N   . ASP D 2 45   ? 15.105   110.246 45.279  1.00 233.83 ? 45   ASP Y N   1 
ATOM   26098 C  CA  . ASP D 2 45   ? 16.175   109.603 46.053  1.00 238.85 ? 45   ASP Y CA  1 
ATOM   26099 C  C   . ASP D 2 45   ? 15.714   109.053 47.408  1.00 239.66 ? 45   ASP Y C   1 
ATOM   26100 O  O   . ASP D 2 45   ? 16.044   107.924 47.773  1.00 240.62 ? 45   ASP Y O   1 
ATOM   26101 C  CB  . ASP D 2 45   ? 17.333   110.584 46.284  1.00 241.31 ? 45   ASP Y CB  1 
ATOM   26102 C  CG  . ASP D 2 45   ? 18.014   111.006 44.999  1.00 243.76 ? 45   ASP Y CG  1 
ATOM   26103 O  OD1 . ASP D 2 45   ? 17.761   110.374 43.949  1.00 244.82 ? 45   ASP Y OD1 1 
ATOM   26104 O  OD2 . ASP D 2 45   ? 18.805   111.973 45.046  1.00 244.85 ? 45   ASP Y OD2 1 
ATOM   26105 N  N   . LEU D 2 46   ? 14.965   109.860 48.153  1.00 240.00 ? 46   LEU Y N   1 
ATOM   26106 C  CA  . LEU D 2 46   ? 14.536   109.483 49.497  1.00 241.42 ? 46   LEU Y CA  1 
ATOM   26107 C  C   . LEU D 2 46   ? 13.665   108.224 49.483  1.00 240.98 ? 46   LEU Y C   1 
ATOM   26108 O  O   . LEU D 2 46   ? 13.429   107.611 50.527  1.00 240.95 ? 46   LEU Y O   1 
ATOM   26109 C  CB  . LEU D 2 46   ? 13.804   110.645 50.183  1.00 240.37 ? 46   LEU Y CB  1 
ATOM   26110 C  CG  . LEU D 2 46   ? 14.415   112.056 50.135  1.00 241.22 ? 46   LEU Y CG  1 
ATOM   26111 C  CD1 . LEU D 2 46   ? 13.686   112.998 51.091  1.00 239.31 ? 46   LEU Y CD1 1 
ATOM   26112 C  CD2 . LEU D 2 46   ? 15.915   112.066 50.416  1.00 243.92 ? 46   LEU Y CD2 1 
ATOM   26113 N  N   . HIS D 2 47   ? 13.191   107.851 48.294  1.00 240.62 ? 47   HIS Y N   1 
ATOM   26114 C  CA  . HIS D 2 47   ? 12.404   106.628 48.102  1.00 239.40 ? 47   HIS Y CA  1 
ATOM   26115 C  C   . HIS D 2 47   ? 13.292   105.421 47.785  1.00 239.67 ? 47   HIS Y C   1 
ATOM   26116 O  O   . HIS D 2 47   ? 12.838   104.276 47.817  1.00 239.53 ? 47   HIS Y O   1 
ATOM   26117 C  CB  . HIS D 2 47   ? 11.386   106.814 46.971  1.00 238.47 ? 47   HIS Y CB  1 
ATOM   26118 C  CG  . HIS D 2 47   ? 10.333   105.749 46.922  1.00 237.22 ? 47   HIS Y CG  1 
ATOM   26119 N  ND1 . HIS D 2 47   ? 9.002    106.029 46.707  1.00 235.15 ? 47   HIS Y ND1 1 
ATOM   26120 C  CD2 . HIS D 2 47   ? 10.415   104.407 47.074  1.00 237.97 ? 47   HIS Y CD2 1 
ATOM   26121 C  CE1 . HIS D 2 47   ? 8.309    104.905 46.721  1.00 234.34 ? 47   HIS Y CE1 1 
ATOM   26122 N  NE2 . HIS D 2 47   ? 9.143    103.907 46.944  1.00 236.15 ? 47   HIS Y NE2 1 
ATOM   26123 N  N   . ARG D 2 48   ? 14.554   105.688 47.465  1.00 239.49 ? 48   ARG Y N   1 
ATOM   26124 C  CA  . ARG D 2 48   ? 15.499   104.635 47.095  1.00 238.78 ? 48   ARG Y CA  1 
ATOM   26125 C  C   . ARG D 2 48   ? 16.447   104.252 48.236  1.00 236.08 ? 48   ARG Y C   1 
ATOM   26126 O  O   . ARG D 2 48   ? 16.854   103.096 48.358  1.00 237.50 ? 48   ARG Y O   1 
ATOM   26127 C  CB  . ARG D 2 48   ? 16.304   105.057 45.863  1.00 242.17 ? 48   ARG Y CB  1 
ATOM   26128 C  CG  . ARG D 2 48   ? 15.444   105.490 44.682  1.00 242.04 ? 48   ARG Y CG  1 
ATOM   26129 C  CD  . ARG D 2 48   ? 16.307   105.976 43.530  1.00 244.92 ? 48   ARG Y CD  1 
ATOM   26130 N  NE  . ARG D 2 48   ? 17.345   106.897 43.983  1.00 246.90 ? 48   ARG Y NE  1 
ATOM   26131 C  CZ  . ARG D 2 48   ? 18.340   107.332 43.219  1.00 248.82 ? 48   ARG Y CZ  1 
ATOM   26132 N  NH1 . ARG D 2 48   ? 19.242   108.166 43.715  1.00 249.81 ? 48   ARG Y NH1 1 
ATOM   26133 N  NH2 . ARG D 2 48   ? 18.435   106.929 41.958  1.00 249.67 ? 48   ARG Y NH2 1 
ATOM   26134 N  N   . TYR D 2 49   ? 16.800   105.229 49.065  1.00 230.53 ? 49   TYR Y N   1 
ATOM   26135 C  CA  . TYR D 2 49   ? 17.729   104.995 50.165  1.00 226.65 ? 49   TYR Y CA  1 
ATOM   26136 C  C   . TYR D 2 49   ? 17.060   104.294 51.350  1.00 220.88 ? 49   TYR Y C   1 
ATOM   26137 O  O   . TYR D 2 49   ? 17.668   103.445 51.999  1.00 221.45 ? 49   TYR Y O   1 
ATOM   26138 C  CB  . TYR D 2 49   ? 18.355   106.316 50.624  1.00 226.80 ? 49   TYR Y CB  1 
ATOM   26139 C  CG  . TYR D 2 49   ? 19.249   107.006 49.600  1.00 227.78 ? 49   TYR Y CG  1 
ATOM   26140 C  CD1 . TYR D 2 49   ? 20.639   106.920 49.686  1.00 230.25 ? 49   TYR Y CD1 1 
ATOM   26141 C  CD2 . TYR D 2 49   ? 18.706   107.763 48.567  1.00 225.86 ? 49   TYR Y CD2 1 
ATOM   26142 C  CE1 . TYR D 2 49   ? 21.461   107.558 48.766  1.00 231.35 ? 49   TYR Y CE1 1 
ATOM   26143 C  CE2 . TYR D 2 49   ? 19.520   108.401 47.641  1.00 227.15 ? 49   TYR Y CE2 1 
ATOM   26144 C  CZ  . TYR D 2 49   ? 20.895   108.295 47.747  1.00 229.94 ? 49   TYR Y CZ  1 
ATOM   26145 O  OH  . TYR D 2 49   ? 21.707   108.927 46.831  1.00 231.38 ? 49   TYR Y OH  1 
ATOM   26146 N  N   . TYR D 2 50   ? 15.812   104.658 51.630  1.00 214.24 ? 50   TYR Y N   1 
ATOM   26147 C  CA  . TYR D 2 50   ? 15.096   104.119 52.785  1.00 210.39 ? 50   TYR Y CA  1 
ATOM   26148 C  C   . TYR D 2 50   ? 14.343   102.823 52.497  1.00 206.17 ? 50   TYR Y C   1 
ATOM   26149 O  O   . TYR D 2 50   ? 13.756   102.223 53.398  1.00 203.70 ? 50   TYR Y O   1 
ATOM   26150 C  CB  . TYR D 2 50   ? 14.158   105.171 53.386  1.00 209.25 ? 50   TYR Y CB  1 
ATOM   26151 C  CG  . TYR D 2 50   ? 14.857   106.096 54.359  1.00 211.68 ? 50   TYR Y CG  1 
ATOM   26152 C  CD1 . TYR D 2 50   ? 15.823   105.603 55.229  1.00 214.13 ? 50   TYR Y CD1 1 
ATOM   26153 C  CD2 . TYR D 2 50   ? 14.549   107.449 54.422  1.00 211.24 ? 50   TYR Y CD2 1 
ATOM   26154 C  CE1 . TYR D 2 50   ? 16.472   106.426 56.126  1.00 215.10 ? 50   TYR Y CE1 1 
ATOM   26155 C  CE2 . TYR D 2 50   ? 15.196   108.285 55.322  1.00 212.44 ? 50   TYR Y CE2 1 
ATOM   26156 C  CZ  . TYR D 2 50   ? 16.158   107.764 56.170  1.00 214.58 ? 50   TYR Y CZ  1 
ATOM   26157 O  OH  . TYR D 2 50   ? 16.811   108.575 57.070  1.00 215.90 ? 50   TYR Y OH  1 
ATOM   26158 N  N   . SER D 2 51   ? 14.358   102.404 51.237  1.00 205.88 ? 51   SER Y N   1 
ATOM   26159 C  CA  . SER D 2 51   ? 13.742   101.143 50.833  1.00 204.73 ? 51   SER Y CA  1 
ATOM   26160 C  C   . SER D 2 51   ? 14.790   100.036 50.820  1.00 206.79 ? 51   SER Y C   1 
ATOM   26161 O  O   . SER D 2 51   ? 14.494   98.858  50.598  1.00 208.27 ? 51   SER Y O   1 
ATOM   26162 C  CB  . SER D 2 51   ? 13.077   101.286 49.457  1.00 202.09 ? 51   SER Y CB  1 
ATOM   26163 O  OG  . SER D 2 51   ? 13.895   102.006 48.550  1.00 202.62 ? 51   SER Y OG  1 
ATOM   26164 N  N   . SER D 2 52   ? 16.023   100.444 51.086  1.00 207.99 ? 52   SER Y N   1 
ATOM   26165 C  CA  . SER D 2 52   ? 17.192   99.585  50.974  1.00 210.43 ? 52   SER Y CA  1 
ATOM   26166 C  C   . SER D 2 52   ? 17.202   98.384  51.919  1.00 210.74 ? 52   SER Y C   1 
ATOM   26167 O  O   . SER D 2 52   ? 16.324   98.232  52.773  1.00 206.74 ? 52   SER Y O   1 
ATOM   26168 C  CB  . SER D 2 52   ? 18.452   100.426 51.207  1.00 213.14 ? 52   SER Y CB  1 
ATOM   26169 O  OG  . SER D 2 52   ? 18.353   101.178 52.412  1.00 212.88 ? 52   SER Y OG  1 
ATOM   26170 N  N   . GLU D 2 53   ? 18.213   97.535  51.747  1.00 216.59 ? 53   GLU Y N   1 
ATOM   26171 C  CA  . GLU D 2 53   ? 18.443   96.412  52.646  1.00 219.56 ? 53   GLU Y CA  1 
ATOM   26172 C  C   . GLU D 2 53   ? 19.266   96.813  53.865  1.00 228.93 ? 53   GLU Y C   1 
ATOM   26173 O  O   . GLU D 2 53   ? 20.470   97.057  53.768  1.00 230.73 ? 53   GLU Y O   1 
ATOM   26174 C  CB  . GLU D 2 53   ? 19.110   95.246  51.911  1.00 215.76 ? 53   GLU Y CB  1 
ATOM   26175 C  CG  . GLU D 2 53   ? 18.139   94.390  51.111  1.00 208.79 ? 53   GLU Y CG  1 
ATOM   26176 C  CD  . GLU D 2 53   ? 17.054   93.761  51.975  1.00 202.21 ? 53   GLU Y CD  1 
ATOM   26177 O  OE1 . GLU D 2 53   ? 17.359   92.780  52.689  1.00 200.35 ? 53   GLU Y OE1 1 
ATOM   26178 O  OE2 . GLU D 2 53   ? 15.894   94.238  51.927  1.00 199.00 ? 53   GLU Y OE2 1 
ATOM   26179 N  N   . SER D 2 54   ? 18.593   96.876  55.009  1.00 235.56 ? 54   SER Y N   1 
ATOM   26180 C  CA  . SER D 2 54   ? 19.234   97.141  56.291  1.00 245.95 ? 54   SER Y CA  1 
ATOM   26181 C  C   . SER D 2 54   ? 19.952   95.903  56.839  1.00 258.51 ? 54   SER Y C   1 
ATOM   26182 O  O   . SER D 2 54   ? 19.652   94.773  56.455  1.00 257.76 ? 54   SER Y O   1 
ATOM   26183 C  CB  . SER D 2 54   ? 18.192   97.625  57.300  1.00 243.73 ? 54   SER Y CB  1 
ATOM   26184 O  OG  . SER D 2 54   ? 18.661   97.466  58.625  1.00 244.98 ? 54   SER Y OG  1 
ATOM   26185 N  N   . PHE D 2 55   ? 20.895   96.127  57.747  1.00 270.68 ? 55   PHE Y N   1 
ATOM   26186 C  CA  . PHE D 2 55   ? 21.629   95.042  58.384  1.00 282.47 ? 55   PHE Y CA  1 
ATOM   26187 C  C   . PHE D 2 55   ? 22.078   95.509  59.761  1.00 289.08 ? 55   PHE Y C   1 
ATOM   26188 O  O   . PHE D 2 55   ? 22.124   96.708  60.030  1.00 289.78 ? 55   PHE Y O   1 
ATOM   26189 C  CB  . PHE D 2 55   ? 22.838   94.642  57.532  1.00 287.65 ? 55   PHE Y CB  1 
ATOM   26190 C  CG  . PHE D 2 55   ? 23.534   93.386  57.997  1.00 290.30 ? 55   PHE Y CG  1 
ATOM   26191 C  CD1 . PHE D 2 55   ? 23.027   92.138  57.677  1.00 290.56 ? 55   PHE Y CD1 1 
ATOM   26192 C  CD2 . PHE D 2 55   ? 24.710   93.455  58.733  1.00 292.44 ? 55   PHE Y CD2 1 
ATOM   26193 C  CE1 . PHE D 2 55   ? 23.671   90.982  58.094  1.00 291.75 ? 55   PHE Y CE1 1 
ATOM   26194 C  CE2 . PHE D 2 55   ? 25.361   92.305  59.155  1.00 293.50 ? 55   PHE Y CE2 1 
ATOM   26195 C  CZ  . PHE D 2 55   ? 24.840   91.067  58.835  1.00 293.30 ? 55   PHE Y CZ  1 
ATOM   26196 N  N   . GLU D 2 56   ? 22.405   94.560  60.629  1.00 295.01 ? 56   GLU Y N   1 
ATOM   26197 C  CA  . GLU D 2 56   ? 22.842   94.874  61.985  1.00 300.47 ? 56   GLU Y CA  1 
ATOM   26198 C  C   . GLU D 2 56   ? 23.892   93.860  62.438  1.00 298.73 ? 56   GLU Y C   1 
ATOM   26199 O  O   . GLU D 2 56   ? 23.824   92.686  62.076  1.00 299.48 ? 56   GLU Y O   1 
ATOM   26200 C  CB  . GLU D 2 56   ? 21.644   94.879  62.940  1.00 305.88 ? 56   GLU Y CB  1 
ATOM   26201 C  CG  . GLU D 2 56   ? 21.950   95.386  64.343  1.00 312.79 ? 56   GLU Y CG  1 
ATOM   26202 C  CD  . GLU D 2 56   ? 22.543   94.317  65.240  1.00 318.43 ? 56   GLU Y CD  1 
ATOM   26203 O  OE1 . GLU D 2 56   ? 22.255   93.122  65.015  1.00 319.35 ? 56   GLU Y OE1 1 
ATOM   26204 O  OE2 . GLU D 2 56   ? 23.293   94.675  66.172  1.00 321.34 ? 56   GLU Y OE2 1 
ATOM   26205 N  N   . TYR D 2 57   ? 24.860   94.309  63.232  1.00 295.46 ? 57   TYR Y N   1 
ATOM   26206 C  CA  . TYR D 2 57   ? 25.963   93.437  63.625  1.00 291.49 ? 57   TYR Y CA  1 
ATOM   26207 C  C   . TYR D 2 57   ? 26.378   93.654  65.085  1.00 287.56 ? 57   TYR Y C   1 
ATOM   26208 O  O   . TYR D 2 57   ? 26.037   94.671  65.692  1.00 287.92 ? 57   TYR Y O   1 
ATOM   26209 C  CB  . TYR D 2 57   ? 27.160   93.647  62.691  1.00 291.73 ? 57   TYR Y CB  1 
ATOM   26210 C  CG  . TYR D 2 57   ? 27.982   92.401  62.445  1.00 290.85 ? 57   TYR Y CG  1 
ATOM   26211 C  CD1 . TYR D 2 57   ? 28.763   92.276  61.307  1.00 291.37 ? 57   TYR Y CD1 1 
ATOM   26212 C  CD2 . TYR D 2 57   ? 27.962   91.343  63.344  1.00 289.50 ? 57   TYR Y CD2 1 
ATOM   26213 C  CE1 . TYR D 2 57   ? 29.516   91.140  61.082  1.00 292.24 ? 57   TYR Y CE1 1 
ATOM   26214 C  CE2 . TYR D 2 57   ? 28.708   90.204  63.127  1.00 290.09 ? 57   TYR Y CE2 1 
ATOM   26215 C  CZ  . TYR D 2 57   ? 29.483   90.106  61.996  1.00 291.34 ? 57   TYR Y CZ  1 
ATOM   26216 O  OH  . TYR D 2 57   ? 30.224   88.967  61.779  1.00 292.20 ? 57   TYR Y OH  1 
ATOM   26217 N  N   . SER D 2 58   ? 27.110   92.685  65.636  1.00 282.04 ? 58   SER Y N   1 
ATOM   26218 C  CA  . SER D 2 58   ? 27.579   92.730  67.023  1.00 275.44 ? 58   SER Y CA  1 
ATOM   26219 C  C   . SER D 2 58   ? 28.842   91.888  67.223  1.00 269.44 ? 58   SER Y C   1 
ATOM   26220 O  O   . SER D 2 58   ? 29.295   91.200  66.308  1.00 268.33 ? 58   SER Y O   1 
ATOM   26221 C  CB  . SER D 2 58   ? 26.484   92.252  67.977  1.00 274.30 ? 58   SER Y CB  1 
ATOM   26222 O  OG  . SER D 2 58   ? 26.111   90.916  67.692  1.00 274.35 ? 58   SER Y OG  1 
ATOM   26223 N  N   . ASN D 2 59   ? 29.401   91.943  68.426  1.00 264.42 ? 59   ASN Y N   1 
ATOM   26224 C  CA  . ASN D 2 59   ? 30.645   91.246  68.722  1.00 261.01 ? 59   ASN Y CA  1 
ATOM   26225 C  C   . ASN D 2 59   ? 31.802   91.811  67.915  1.00 263.20 ? 59   ASN Y C   1 
ATOM   26226 O  O   . ASN D 2 59   ? 32.870   91.206  67.845  1.00 265.51 ? 59   ASN Y O   1 
ATOM   26227 C  CB  . ASN D 2 59   ? 30.516   89.747  68.453  1.00 254.82 ? 59   ASN Y CB  1 
ATOM   26228 C  CG  . ASN D 2 59   ? 29.429   89.099  69.278  1.00 246.78 ? 59   ASN Y CG  1 
ATOM   26229 O  OD1 . ASN D 2 59   ? 29.698   88.229  70.108  1.00 244.73 ? 59   ASN Y OD1 1 
ATOM   26230 N  ND2 . ASN D 2 59   ? 28.190   89.525  69.061  1.00 242.60 ? 59   ASN Y ND2 1 
ATOM   26231 N  N   . VAL D 2 60   ? 31.579   92.970  67.300  1.00 263.00 ? 60   VAL Y N   1 
ATOM   26232 C  CA  . VAL D 2 60   ? 32.604   93.625  66.489  1.00 267.44 ? 60   VAL Y CA  1 
ATOM   26233 C  C   . VAL D 2 60   ? 33.452   94.640  67.278  1.00 272.82 ? 60   VAL Y C   1 
ATOM   26234 O  O   . VAL D 2 60   ? 32.965   95.711  67.652  1.00 271.94 ? 60   VAL Y O   1 
ATOM   26235 C  CB  . VAL D 2 60   ? 31.996   94.308  65.224  1.00 238.53 ? 60   VAL Y CB  1 
ATOM   26236 C  CG1 . VAL D 2 60   ? 31.520   93.267  64.217  1.00 237.65 ? 60   VAL Y CG1 1 
ATOM   26237 C  CG2 . VAL D 2 60   ? 30.869   95.257  65.600  1.00 235.83 ? 60   VAL Y CG2 1 
ATOM   26238 N  N   . SER D 2 61   ? 34.717   94.297  67.526  1.00 280.13 ? 61   SER Y N   1 
ATOM   26239 C  CA  . SER D 2 61   ? 35.671   95.222  68.150  1.00 286.75 ? 61   SER Y CA  1 
ATOM   26240 C  C   . SER D 2 61   ? 36.782   95.684  67.197  1.00 294.94 ? 61   SER Y C   1 
ATOM   26241 O  O   . SER D 2 61   ? 37.397   94.866  66.511  1.00 295.65 ? 61   SER Y O   1 
ATOM   26242 C  CB  . SER D 2 61   ? 36.295   94.595  69.396  1.00 287.52 ? 61   SER Y CB  1 
ATOM   26243 O  OG  . SER D 2 61   ? 37.342   95.412  69.894  1.00 289.61 ? 61   SER Y OG  1 
ATOM   26244 N  N   . GLY D 2 62   ? 37.055   96.989  67.179  1.00 301.86 ? 62   GLY Y N   1 
ATOM   26245 C  CA  . GLY D 2 62   ? 38.060   97.550  66.287  1.00 311.11 ? 62   GLY Y CA  1 
ATOM   26246 C  C   . GLY D 2 62   ? 38.903   98.656  66.904  1.00 319.29 ? 62   GLY Y C   1 
ATOM   26247 O  O   . GLY D 2 62   ? 38.680   99.047  68.049  1.00 318.15 ? 62   GLY Y O   1 
ATOM   26248 N  N   . LYS D 2 63   ? 39.869   99.168  66.141  1.00 328.32 ? 63   LYS Y N   1 
ATOM   26249 C  CA  . LYS D 2 63   ? 40.794   100.192 66.636  1.00 335.55 ? 63   LYS Y CA  1 
ATOM   26250 C  C   . LYS D 2 63   ? 40.993   101.359 65.659  1.00 339.47 ? 63   LYS Y C   1 
ATOM   26251 O  O   . LYS D 2 63   ? 41.497   101.186 64.547  1.00 342.86 ? 63   LYS Y O   1 
ATOM   26252 C  CB  . LYS D 2 63   ? 42.140   99.562  66.996  1.00 339.94 ? 63   LYS Y CB  1 
ATOM   26253 C  CG  . LYS D 2 63   ? 42.719   98.687  65.902  1.00 342.62 ? 63   LYS Y CG  1 
ATOM   26254 C  CD  . LYS D 2 63   ? 44.039   98.079  66.326  1.00 347.22 ? 63   LYS Y CD  1 
ATOM   26255 C  CE  . LYS D 2 63   ? 44.728   97.424  65.147  1.00 350.90 ? 63   LYS Y CE  1 
ATOM   26256 N  NZ  . LYS D 2 63   ? 44.794   98.354  63.990  1.00 352.55 ? 63   LYS Y NZ  1 
ATOM   26257 N  N   . VAL D 2 64   ? 40.626   102.549 66.125  1.00 338.40 ? 64   VAL Y N   1 
ATOM   26258 C  CA  . VAL D 2 64   ? 40.527   103.777 65.325  1.00 337.61 ? 64   VAL Y CA  1 
ATOM   26259 C  C   . VAL D 2 64   ? 41.605   104.078 64.271  1.00 335.81 ? 64   VAL Y C   1 
ATOM   26260 O  O   . VAL D 2 64   ? 42.778   103.747 64.436  1.00 338.31 ? 64   VAL Y O   1 
ATOM   26261 C  CB  . VAL D 2 64   ? 40.462   105.002 66.267  1.00 340.79 ? 64   VAL Y CB  1 
ATOM   26262 C  CG1 . VAL D 2 64   ? 41.675   105.015 67.184  1.00 344.89 ? 64   VAL Y CG1 1 
ATOM   26263 C  CG2 . VAL D 2 64   ? 40.374   106.299 65.471  1.00 341.82 ? 64   VAL Y CG2 1 
ATOM   26264 N  N   . GLU D 2 65   ? 41.159   104.703 63.182  1.00 330.30 ? 65   GLU Y N   1 
ATOM   26265 C  CA  . GLU D 2 65   ? 42.002   105.483 62.279  1.00 327.84 ? 65   GLU Y CA  1 
ATOM   26266 C  C   . GLU D 2 65   ? 41.191   106.613 61.639  1.00 320.61 ? 65   GLU Y C   1 
ATOM   26267 O  O   . GLU D 2 65   ? 40.086   106.390 61.153  1.00 317.69 ? 65   GLU Y O   1 
ATOM   26268 C  CB  . GLU D 2 65   ? 42.774   104.660 61.217  1.00 326.97 ? 65   GLU Y CB  1 
ATOM   26269 C  CG  . GLU D 2 65   ? 42.373   103.222 60.723  1.00 324.20 ? 65   GLU Y CG  1 
ATOM   26270 C  CD  . GLU D 2 65   ? 41.184   102.510 61.360  1.00 320.46 ? 65   GLU Y CD  1 
ATOM   26271 O  OE1 . GLU D 2 65   ? 40.264   103.159 61.887  1.00 317.59 ? 65   GLU Y OE1 1 
ATOM   26272 O  OE2 . GLU D 2 65   ? 41.158   101.262 61.268  1.00 320.41 ? 65   GLU Y OE2 1 
ATOM   26273 N  N   . ASN D 2 66   ? 41.723   107.832 61.660  1.00 317.09 ? 66   ASN Y N   1 
ATOM   26274 C  CA  . ASN D 2 66   ? 41.026   108.947 61.017  1.00 309.57 ? 66   ASN Y CA  1 
ATOM   26275 C  C   . ASN D 2 66   ? 41.358   109.125 59.524  1.00 307.51 ? 66   ASN Y C   1 
ATOM   26276 O  O   . ASN D 2 66   ? 42.488   109.464 59.165  1.00 309.02 ? 66   ASN Y O   1 
ATOM   26277 C  CB  . ASN D 2 66   ? 41.165   110.259 61.817  1.00 305.75 ? 66   ASN Y CB  1 
ATOM   26278 C  CG  . ASN D 2 66   ? 42.437   110.318 62.650  1.00 305.07 ? 66   ASN Y CG  1 
ATOM   26279 O  OD1 . ASN D 2 66   ? 42.834   109.339 63.286  1.00 304.93 ? 66   ASN Y OD1 1 
ATOM   26280 N  ND2 . ASN D 2 66   ? 43.067   111.486 62.669  1.00 304.62 ? 66   ASN Y ND2 1 
ATOM   26281 N  N   . TYR D 2 67   ? 40.363   108.864 58.672  1.00 303.51 ? 67   TYR Y N   1 
ATOM   26282 C  CA  . TYR D 2 67   ? 40.442   109.123 57.226  1.00 301.54 ? 67   TYR Y CA  1 
ATOM   26283 C  C   . TYR D 2 67   ? 40.705   110.613 56.958  1.00 298.58 ? 67   TYR Y C   1 
ATOM   26284 O  O   . TYR D 2 67   ? 41.829   110.980 56.600  1.00 303.28 ? 67   TYR Y O   1 
ATOM   26285 C  CB  . TYR D 2 67   ? 39.174   108.610 56.511  1.00 298.80 ? 67   TYR Y CB  1 
ATOM   26286 C  CG  . TYR D 2 67   ? 38.501   109.595 55.569  1.00 295.84 ? 67   TYR Y CG  1 
ATOM   26287 C  CD1 . TYR D 2 67   ? 39.109   109.979 54.374  1.00 296.60 ? 67   TYR Y CD1 1 
ATOM   26288 C  CD2 . TYR D 2 67   ? 37.252   110.137 55.879  1.00 291.68 ? 67   TYR Y CD2 1 
ATOM   26289 C  CE1 . TYR D 2 67   ? 38.499   110.885 53.515  1.00 293.09 ? 67   TYR Y CE1 1 
ATOM   26290 C  CE2 . TYR D 2 67   ? 36.629   111.040 55.028  1.00 288.30 ? 67   TYR Y CE2 1 
ATOM   26291 C  CZ  . TYR D 2 67   ? 37.261   111.410 53.847  1.00 288.73 ? 67   TYR Y CZ  1 
ATOM   26292 O  OH  . TYR D 2 67   ? 36.657   112.306 52.994  1.00 285.56 ? 67   TYR Y OH  1 
ATOM   26293 N  N   . ASN D 2 68   ? 39.690   111.465 57.138  1.00 292.37 ? 68   ASN Y N   1 
ATOM   26294 C  CA  . ASN D 2 68   ? 39.913   112.917 57.208  1.00 292.32 ? 68   ASN Y CA  1 
ATOM   26295 C  C   . ASN D 2 68   ? 39.658   113.577 58.587  1.00 306.38 ? 68   ASN Y C   1 
ATOM   26296 O  O   . ASN D 2 68   ? 40.562   113.635 59.429  1.00 310.22 ? 68   ASN Y O   1 
ATOM   26297 C  CB  . ASN D 2 68   ? 39.204   113.683 56.070  1.00 293.39 ? 68   ASN Y CB  1 
ATOM   26298 C  CG  . ASN D 2 68   ? 37.671   113.657 56.165  1.00 295.28 ? 68   ASN Y CG  1 
ATOM   26299 O  OD1 . ASN D 2 68   ? 37.090   113.211 57.153  1.00 296.54 ? 68   ASN Y OD1 1 
ATOM   26300 N  ND2 . ASN D 2 68   ? 37.014   114.145 55.109  1.00 295.46 ? 68   ASN Y ND2 1 
ATOM   26301 N  N   . GLY D 2 69   ? 38.428   114.041 58.823  1.00 301.61 ? 69   GLY Y N   1 
ATOM   26302 C  CA  . GLY D 2 69   ? 38.104   114.887 59.968  1.00 298.69 ? 69   GLY Y CA  1 
ATOM   26303 C  C   . GLY D 2 69   ? 38.464   114.377 61.356  1.00 297.14 ? 69   GLY Y C   1 
ATOM   26304 O  O   . GLY D 2 69   ? 39.167   115.065 62.104  1.00 298.36 ? 69   GLY Y O   1 
ATOM   26305 N  N   . SER D 2 70   ? 37.990   113.180 61.699  1.00 292.61 ? 70   SER Y N   1 
ATOM   26306 C  CA  . SER D 2 70   ? 38.082   112.698 63.066  1.00 287.71 ? 70   SER Y CA  1 
ATOM   26307 C  C   . SER D 2 70   ? 38.109   111.179 63.203  1.00 281.14 ? 70   SER Y C   1 
ATOM   26308 O  O   . SER D 2 70   ? 38.434   110.666 64.271  1.00 280.35 ? 70   SER Y O   1 
ATOM   26309 C  CB  . SER D 2 70   ? 36.926   113.253 63.895  1.00 285.18 ? 70   SER Y CB  1 
ATOM   26310 O  OG  . SER D 2 70   ? 37.047   114.621 64.143  1.00 285.10 ? 70   SER Y OG  1 
ATOM   26311 N  N   . ASN D 2 71   ? 37.751   110.456 62.148  1.00 275.60 ? 71   ASN Y N   1 
ATOM   26312 C  CA  . ASN D 2 71   ? 37.527   109.027 62.317  1.00 270.57 ? 71   ASN Y CA  1 
ATOM   26313 C  C   . ASN D 2 71   ? 37.245   108.255 61.030  1.00 267.86 ? 71   ASN Y C   1 
ATOM   26314 O  O   . ASN D 2 71   ? 37.013   108.845 59.979  1.00 268.43 ? 71   ASN Y O   1 
ATOM   26315 C  CB  . ASN D 2 71   ? 36.358   108.828 63.289  1.00 265.03 ? 71   ASN Y CB  1 
ATOM   26316 C  CG  . ASN D 2 71   ? 36.716   107.958 64.480  1.00 262.81 ? 71   ASN Y CG  1 
ATOM   26317 O  OD1 . ASN D 2 71   ? 37.762   107.314 64.508  1.00 263.78 ? 71   ASN Y OD1 1 
ATOM   26318 N  ND2 . ASN D 2 71   ? 35.841   107.947 65.481  1.00 259.67 ? 71   ASN Y ND2 1 
ATOM   26319 N  N   . VAL D 2 72   ? 37.274   106.927 61.149  1.00 265.17 ? 72   VAL Y N   1 
ATOM   26320 C  CA  . VAL D 2 72   ? 36.918   105.968 60.093  1.00 263.53 ? 72   VAL Y CA  1 
ATOM   26321 C  C   . VAL D 2 72   ? 37.310   104.573 60.579  1.00 265.03 ? 72   VAL Y C   1 
ATOM   26322 O  O   . VAL D 2 72   ? 38.294   104.420 61.296  1.00 264.65 ? 72   VAL Y O   1 
ATOM   26323 C  CB  . VAL D 2 72   ? 37.590   106.261 58.734  1.00 266.18 ? 72   VAL Y CB  1 
ATOM   26324 C  CG1 . VAL D 2 72   ? 38.099   104.973 58.095  1.00 268.21 ? 72   VAL Y CG1 1 
ATOM   26325 C  CG2 . VAL D 2 72   ? 36.614   106.959 57.802  1.00 264.27 ? 72   VAL Y CG2 1 
ATOM   26326 N  N   . VAL D 2 73   ? 36.561   103.556 60.170  1.00 266.28 ? 73   VAL Y N   1 
ATOM   26327 C  CA  . VAL D 2 73   ? 36.641   102.237 60.791  1.00 267.92 ? 73   VAL Y CA  1 
ATOM   26328 C  C   . VAL D 2 73   ? 36.576   101.156 59.704  1.00 266.92 ? 73   VAL Y C   1 
ATOM   26329 O  O   . VAL D 2 73   ? 36.524   101.471 58.514  1.00 266.07 ? 73   VAL Y O   1 
ATOM   26330 C  CB  . VAL D 2 73   ? 35.431   102.100 61.751  1.00 215.59 ? 73   VAL Y CB  1 
ATOM   26331 C  CG1 . VAL D 2 73   ? 35.107   100.679 62.167  1.00 214.82 ? 73   VAL Y CG1 1 
ATOM   26332 C  CG2 . VAL D 2 73   ? 35.457   103.134 62.885  1.00 215.15 ? 73   VAL Y CG2 1 
ATOM   26333 N  N   . ARG D 2 74   ? 36.597   99.889  60.109  1.00 266.33 ? 74   ARG Y N   1 
ATOM   26334 C  CA  . ARG D 2 74   ? 36.392   98.774  59.184  1.00 267.08 ? 74   ARG Y CA  1 
ATOM   26335 C  C   . ARG D 2 74   ? 36.101   97.456  59.916  1.00 268.73 ? 74   ARG Y C   1 
ATOM   26336 O  O   . ARG D 2 74   ? 36.422   97.308  61.096  1.00 270.13 ? 74   ARG Y O   1 
ATOM   26337 C  CB  . ARG D 2 74   ? 37.593   98.617  58.249  1.00 268.86 ? 74   ARG Y CB  1 
ATOM   26338 C  CG  . ARG D 2 74   ? 38.835   98.058  58.918  1.00 271.84 ? 74   ARG Y CG  1 
ATOM   26339 C  CD  . ARG D 2 74   ? 40.021   98.054  57.966  1.00 274.95 ? 74   ARG Y CD  1 
ATOM   26340 N  NE  . ARG D 2 74   ? 40.386   99.405  57.549  1.00 275.35 ? 74   ARG Y NE  1 
ATOM   26341 C  CZ  . ARG D 2 74   ? 41.330   100.139 58.129  1.00 276.74 ? 74   ARG Y CZ  1 
ATOM   26342 N  NH1 . ARG D 2 74   ? 42.012   99.655  59.156  1.00 278.04 ? 74   ARG Y NH1 1 
ATOM   26343 N  NH2 . ARG D 2 74   ? 41.594   101.359 57.681  1.00 276.85 ? 74   ARG Y NH2 1 
ATOM   26344 N  N   . PHE D 2 75   ? 35.491   96.507  59.203  1.00 270.13 ? 75   PHE Y N   1 
ATOM   26345 C  CA  . PHE D 2 75   ? 35.160   95.192  59.764  1.00 271.63 ? 75   PHE Y CA  1 
ATOM   26346 C  C   . PHE D 2 75   ? 34.908   94.095  58.730  1.00 266.66 ? 75   PHE Y C   1 
ATOM   26347 O  O   . PHE D 2 75   ? 34.282   94.333  57.699  1.00 265.20 ? 75   PHE Y O   1 
ATOM   26348 C  CB  . PHE D 2 75   ? 33.973   95.278  60.725  1.00 275.77 ? 75   PHE Y CB  1 
ATOM   26349 C  CG  . PHE D 2 75   ? 34.369   95.149  62.153  1.00 282.98 ? 75   PHE Y CG  1 
ATOM   26350 C  CD1 . PHE D 2 75   ? 34.618   93.904  62.695  1.00 285.98 ? 75   PHE Y CD1 1 
ATOM   26351 C  CD2 . PHE D 2 75   ? 34.531   96.268  62.945  1.00 285.75 ? 75   PHE Y CD2 1 
ATOM   26352 C  CE1 . PHE D 2 75   ? 35.006   93.776  64.002  1.00 287.91 ? 75   PHE Y CE1 1 
ATOM   26353 C  CE2 . PHE D 2 75   ? 34.917   96.146  64.254  1.00 287.68 ? 75   PHE Y CE2 1 
ATOM   26354 C  CZ  . PHE D 2 75   ? 35.156   94.899  64.780  1.00 288.45 ? 75   PHE Y CZ  1 
ATOM   26355 N  N   . ASN D 2 76   ? 35.400   92.895  59.035  1.00 263.46 ? 76   ASN Y N   1 
ATOM   26356 C  CA  . ASN D 2 76   ? 35.257   91.721  58.175  1.00 259.27 ? 76   ASN Y CA  1 
ATOM   26357 C  C   . ASN D 2 76   ? 34.029   90.896  58.574  1.00 252.64 ? 76   ASN Y C   1 
ATOM   26358 O  O   . ASN D 2 76   ? 34.109   90.044  59.460  1.00 252.05 ? 76   ASN Y O   1 
ATOM   26359 C  CB  . ASN D 2 76   ? 36.537   90.873  58.241  1.00 260.59 ? 76   ASN Y CB  1 
ATOM   26360 C  CG  . ASN D 2 76   ? 36.690   89.931  57.056  1.00 260.17 ? 76   ASN Y CG  1 
ATOM   26361 O  OD1 . ASN D 2 76   ? 35.852   89.059  56.831  1.00 257.73 ? 76   ASN Y OD1 1 
ATOM   26362 N  ND2 . ASN D 2 76   ? 37.778   90.092  56.306  1.00 262.29 ? 76   ASN Y ND2 1 
ATOM   26363 N  N   . PRO D 2 77   ? 32.886   91.160  57.917  1.00 248.81 ? 77   PRO Y N   1 
ATOM   26364 C  CA  . PRO D 2 77   ? 31.552   90.615  58.212  1.00 245.15 ? 77   PRO Y CA  1 
ATOM   26365 C  C   . PRO D 2 77   ? 31.320   89.130  57.882  1.00 246.87 ? 77   PRO Y C   1 
ATOM   26366 O  O   . PRO D 2 77   ? 30.287   88.612  58.301  1.00 244.26 ? 77   PRO Y O   1 
ATOM   26367 C  CB  . PRO D 2 77   ? 30.641   91.476  57.329  1.00 242.54 ? 77   PRO Y CB  1 
ATOM   26368 C  CG  . PRO D 2 77   ? 31.533   91.909  56.210  1.00 244.02 ? 77   PRO Y CG  1 
ATOM   26369 C  CD  . PRO D 2 77   ? 32.802   92.231  56.910  1.00 246.95 ? 77   PRO Y CD  1 
ATOM   26370 N  N   . LYS D 2 78   ? 32.245   88.492  57.158  1.00 251.61 ? 78   LYS Y N   1 
ATOM   26371 C  CA  . LYS D 2 78   ? 32.178   87.074  56.721  1.00 254.47 ? 78   LYS Y CA  1 
ATOM   26372 C  C   . LYS D 2 78   ? 32.093   86.882  55.190  1.00 263.75 ? 78   LYS Y C   1 
ATOM   26373 O  O   . LYS D 2 78   ? 32.059   85.745  54.700  1.00 265.30 ? 78   LYS Y O   1 
ATOM   26374 C  CB  . LYS D 2 78   ? 31.093   86.247  57.456  1.00 246.17 ? 78   LYS Y CB  1 
ATOM   26375 C  CG  . LYS D 2 78   ? 29.643   86.496  57.038  1.00 238.62 ? 78   LYS Y CG  1 
ATOM   26376 C  CD  . LYS D 2 78   ? 29.319   85.915  55.685  1.00 235.74 ? 78   LYS Y CD  1 
ATOM   26377 C  CE  . LYS D 2 78   ? 28.232   86.722  55.016  1.00 231.87 ? 78   LYS Y CE  1 
ATOM   26378 N  NZ  . LYS D 2 78   ? 28.134   86.392  53.573  1.00 231.44 ? 78   LYS Y NZ  1 
ATOM   26379 N  N   . ASP D 2 79   ? 32.095   87.993  54.450  1.00 270.52 ? 79   ASP Y N   1 
ATOM   26380 C  CA  . ASP D 2 79   ? 31.911   87.976  52.994  1.00 276.68 ? 79   ASP Y CA  1 
ATOM   26381 C  C   . ASP D 2 79   ? 32.715   89.088  52.286  1.00 283.60 ? 79   ASP Y C   1 
ATOM   26382 O  O   . ASP D 2 79   ? 33.019   88.982  51.095  1.00 284.41 ? 79   ASP Y O   1 
ATOM   26383 C  CB  . ASP D 2 79   ? 30.414   88.080  52.661  1.00 274.10 ? 79   ASP Y CB  1 
ATOM   26384 C  CG  . ASP D 2 79   ? 30.091   87.671  51.234  1.00 274.63 ? 79   ASP Y CG  1 
ATOM   26385 O  OD1 . ASP D 2 79   ? 30.592   88.324  50.296  1.00 276.02 ? 79   ASP Y OD1 1 
ATOM   26386 O  OD2 . ASP D 2 79   ? 29.315   86.708  51.053  1.00 273.46 ? 79   ASP Y OD2 1 
ATOM   26387 N  N   . GLN D 2 80   ? 33.063   90.143  53.024  1.00 288.85 ? 80   GLN Y N   1 
ATOM   26388 C  CA  . GLN D 2 80   ? 33.866   91.247  52.488  1.00 295.49 ? 80   GLN Y CA  1 
ATOM   26389 C  C   . GLN D 2 80   ? 34.591   92.011  53.596  1.00 298.91 ? 80   GLN Y C   1 
ATOM   26390 O  O   . GLN D 2 80   ? 34.988   91.428  54.603  1.00 299.23 ? 80   GLN Y O   1 
ATOM   26391 C  CB  . GLN D 2 80   ? 33.003   92.216  51.675  1.00 295.21 ? 80   GLN Y CB  1 
ATOM   26392 C  CG  . GLN D 2 80   ? 31.917   92.915  52.474  1.00 293.67 ? 80   GLN Y CG  1 
ATOM   26393 C  CD  . GLN D 2 80   ? 30.603   92.165  52.449  1.00 292.21 ? 80   GLN Y CD  1 
ATOM   26394 O  OE1 . GLN D 2 80   ? 29.578   92.670  52.902  1.00 290.48 ? 80   GLN Y OE1 1 
ATOM   26395 N  NE2 . GLN D 2 80   ? 30.623   90.957  51.904  1.00 292.89 ? 80   GLN Y NE2 1 
ATOM   26396 N  N   . ASN D 2 81   ? 34.767   93.314  53.400  1.00 302.00 ? 81   ASN Y N   1 
ATOM   26397 C  CA  . ASN D 2 81   ? 35.399   94.172  54.401  1.00 305.24 ? 81   ASN Y CA  1 
ATOM   26398 C  C   . ASN D 2 81   ? 34.850   95.592  54.343  1.00 308.19 ? 81   ASN Y C   1 
ATOM   26399 O  O   . ASN D 2 81   ? 35.197   96.363  53.452  1.00 309.40 ? 81   ASN Y O   1 
ATOM   26400 C  CB  . ASN D 2 81   ? 36.919   94.186  54.221  1.00 306.05 ? 81   ASN Y CB  1 
ATOM   26401 C  CG  . ASN D 2 81   ? 37.595   92.993  54.868  1.00 304.89 ? 81   ASN Y CG  1 
ATOM   26402 O  OD1 . ASN D 2 81   ? 37.812   92.969  56.079  1.00 303.91 ? 81   ASN Y OD1 1 
ATOM   26403 N  ND2 . ASN D 2 81   ? 37.942   91.999  54.059  1.00 305.21 ? 81   ASN Y ND2 1 
ATOM   26404 N  N   . HIS D 2 82   ? 34.007   95.933  55.314  1.00 310.15 ? 82   HIS Y N   1 
ATOM   26405 C  CA  . HIS D 2 82   ? 33.234   97.173  55.285  1.00 312.22 ? 82   HIS Y CA  1 
ATOM   26406 C  C   . HIS D 2 82   ? 33.962   98.413  55.800  1.00 309.57 ? 82   HIS Y C   1 
ATOM   26407 O  O   . HIS D 2 82   ? 35.186   98.434  55.932  1.00 310.45 ? 82   HIS Y O   1 
ATOM   26408 C  CB  . HIS D 2 82   ? 31.938   97.000  56.079  1.00 316.65 ? 82   HIS Y CB  1 
ATOM   26409 C  CG  . HIS D 2 82   ? 30.943   96.092  55.426  1.00 321.17 ? 82   HIS Y CG  1 
ATOM   26410 N  ND1 . HIS D 2 82   ? 30.222   96.457  54.310  1.00 322.35 ? 82   HIS Y ND1 1 
ATOM   26411 C  CD2 . HIS D 2 82   ? 30.537   94.840  55.744  1.00 322.79 ? 82   HIS Y CD2 1 
ATOM   26412 C  CE1 . HIS D 2 82   ? 29.421   95.466  53.962  1.00 321.93 ? 82   HIS Y CE1 1 
ATOM   26413 N  NE2 . HIS D 2 82   ? 29.592   94.474  54.817  1.00 322.22 ? 82   HIS Y NE2 1 
ATOM   26414 N  N   . GLN D 2 83   ? 33.172   99.445  56.090  1.00 306.01 ? 83   GLN Y N   1 
ATOM   26415 C  CA  . GLN D 2 83   ? 33.670   100.691 56.655  1.00 304.76 ? 83   GLN Y CA  1 
ATOM   26416 C  C   . GLN D 2 83   ? 32.582   101.332 57.514  1.00 302.91 ? 83   GLN Y C   1 
ATOM   26417 O  O   . GLN D 2 83   ? 31.399   101.071 57.316  1.00 301.12 ? 83   GLN Y O   1 
ATOM   26418 C  CB  . GLN D 2 83   ? 34.088   101.649 55.544  1.00 302.66 ? 83   GLN Y CB  1 
ATOM   26419 C  CG  . GLN D 2 83   ? 34.723   102.932 56.046  1.00 300.89 ? 83   GLN Y CG  1 
ATOM   26420 C  CD  . GLN D 2 83   ? 35.313   103.758 54.927  1.00 300.33 ? 83   GLN Y CD  1 
ATOM   26421 O  OE1 . GLN D 2 83   ? 35.052   103.501 53.753  1.00 300.10 ? 83   GLN Y OE1 1 
ATOM   26422 N  NE2 . GLN D 2 83   ? 36.115   104.757 55.282  1.00 300.43 ? 83   GLN Y NE2 1 
ATOM   26423 N  N   . LEU D 2 84   ? 32.984   102.171 58.464  1.00 302.92 ? 84   LEU Y N   1 
ATOM   26424 C  CA  . LEU D 2 84   ? 32.035   102.820 59.365  1.00 299.02 ? 84   LEU Y CA  1 
ATOM   26425 C  C   . LEU D 2 84   ? 32.537   104.193 59.805  1.00 295.35 ? 84   LEU Y C   1 
ATOM   26426 O  O   . LEU D 2 84   ? 33.654   104.329 60.305  1.00 298.76 ? 84   LEU Y O   1 
ATOM   26427 C  CB  . LEU D 2 84   ? 31.760   101.935 60.586  1.00 301.59 ? 84   LEU Y CB  1 
ATOM   26428 C  CG  . LEU D 2 84   ? 31.003   102.552 61.767  1.00 302.28 ? 84   LEU Y CG  1 
ATOM   26429 C  CD1 . LEU D 2 84   ? 29.662   103.120 61.331  1.00 300.10 ? 84   LEU Y CD1 1 
ATOM   26430 C  CD2 . LEU D 2 84   ? 30.817   101.526 62.877  1.00 302.80 ? 84   LEU Y CD2 1 
ATOM   26431 N  N   . PHE D 2 85   ? 31.706   105.210 59.610  1.00 286.51 ? 85   PHE Y N   1 
ATOM   26432 C  CA  . PHE D 2 85   ? 32.079   106.578 59.949  1.00 281.32 ? 85   PHE Y CA  1 
ATOM   26433 C  C   . PHE D 2 85   ? 31.437   107.051 61.254  1.00 274.59 ? 85   PHE Y C   1 
ATOM   26434 O  O   . PHE D 2 85   ? 30.237   107.327 61.305  1.00 273.36 ? 85   PHE Y O   1 
ATOM   26435 C  CB  . PHE D 2 85   ? 31.721   107.528 58.801  1.00 279.35 ? 85   PHE Y CB  1 
ATOM   26436 C  CG  . PHE D 2 85   ? 32.540   107.313 57.554  1.00 281.69 ? 85   PHE Y CG  1 
ATOM   26437 C  CD1 . PHE D 2 85   ? 32.520   106.096 56.892  1.00 282.53 ? 85   PHE Y CD1 1 
ATOM   26438 C  CD2 . PHE D 2 85   ? 33.319   108.336 57.037  1.00 283.73 ? 85   PHE Y CD2 1 
ATOM   26439 C  CE1 . PHE D 2 85   ? 33.266   105.902 55.745  1.00 284.98 ? 85   PHE Y CE1 1 
ATOM   26440 C  CE2 . PHE D 2 85   ? 34.069   108.147 55.888  1.00 286.11 ? 85   PHE Y CE2 1 
ATOM   26441 C  CZ  . PHE D 2 85   ? 34.042   106.928 55.243  1.00 286.91 ? 85   PHE Y CZ  1 
ATOM   26442 N  N   . LEU D 2 86   ? 32.248   107.134 62.305  1.00 270.23 ? 86   LEU Y N   1 
ATOM   26443 C  CA  . LEU D 2 86   ? 31.814   107.664 63.593  1.00 262.50 ? 86   LEU Y CA  1 
ATOM   26444 C  C   . LEU D 2 86   ? 32.004   109.185 63.576  1.00 257.88 ? 86   LEU Y C   1 
ATOM   26445 O  O   . LEU D 2 86   ? 33.097   109.670 63.282  1.00 258.78 ? 86   LEU Y O   1 
ATOM   26446 C  CB  . LEU D 2 86   ? 32.635   107.020 64.720  1.00 262.67 ? 86   LEU Y CB  1 
ATOM   26447 C  CG  . LEU D 2 86   ? 32.054   106.891 66.131  1.00 259.92 ? 86   LEU Y CG  1 
ATOM   26448 C  CD1 . LEU D 2 86   ? 30.647   106.341 66.082  1.00 256.88 ? 86   LEU Y CD1 1 
ATOM   26449 C  CD2 . LEU D 2 86   ? 32.946   106.014 67.004  1.00 261.26 ? 86   LEU Y CD2 1 
ATOM   26450 N  N   . LEU D 2 87   ? 30.947   109.939 63.866  1.00 252.80 ? 87   LEU Y N   1 
ATOM   26451 C  CA  . LEU D 2 87   ? 31.053   111.398 63.905  1.00 248.94 ? 87   LEU Y CA  1 
ATOM   26452 C  C   . LEU D 2 87   ? 29.882   112.059 64.640  1.00 251.12 ? 87   LEU Y C   1 
ATOM   26453 O  O   . LEU D 2 87   ? 29.520   113.204 64.358  1.00 250.06 ? 87   LEU Y O   1 
ATOM   26454 C  CB  . LEU D 2 87   ? 31.264   111.991 62.498  1.00 241.47 ? 87   LEU Y CB  1 
ATOM   26455 C  CG  . LEU D 2 87   ? 30.372   111.599 61.317  1.00 231.96 ? 87   LEU Y CG  1 
ATOM   26456 C  CD1 . LEU D 2 87   ? 29.101   112.427 61.315  1.00 226.70 ? 87   LEU Y CD1 1 
ATOM   26457 C  CD2 . LEU D 2 87   ? 31.113   111.785 60.002  1.00 230.14 ? 87   LEU Y CD2 1 
ATOM   26458 N  N   . GLY D 2 88   ? 29.300   111.324 65.585  1.00 253.85 ? 88   GLY Y N   1 
ATOM   26459 C  CA  . GLY D 2 88   ? 28.238   111.849 66.425  1.00 257.56 ? 88   GLY Y CA  1 
ATOM   26460 C  C   . GLY D 2 88   ? 28.813   112.437 67.695  1.00 266.26 ? 88   GLY Y C   1 
ATOM   26461 O  O   . GLY D 2 88   ? 29.993   112.251 67.976  1.00 269.23 ? 88   GLY Y O   1 
ATOM   26462 N  N   . LYS D 2 89   ? 27.993   113.147 68.465  1.00 271.89 ? 89   LYS Y N   1 
ATOM   26463 C  CA  . LYS D 2 89   ? 28.464   113.725 69.721  1.00 280.99 ? 89   LYS Y CA  1 
ATOM   26464 C  C   . LYS D 2 89   ? 28.963   112.628 70.661  1.00 289.91 ? 89   LYS Y C   1 
ATOM   26465 O  O   . LYS D 2 89   ? 29.700   112.900 71.615  1.00 292.44 ? 89   LYS Y O   1 
ATOM   26466 C  CB  . LYS D 2 89   ? 27.368   114.551 70.391  1.00 277.98 ? 89   LYS Y CB  1 
ATOM   26467 C  CG  . LYS D 2 89   ? 27.816   115.235 71.667  1.00 279.05 ? 89   LYS Y CG  1 
ATOM   26468 C  CD  . LYS D 2 89   ? 29.001   116.138 71.409  1.00 281.95 ? 89   LYS Y CD  1 
ATOM   26469 C  CE  . LYS D 2 89   ? 29.487   116.769 72.693  1.00 283.99 ? 89   LYS Y CE  1 
ATOM   26470 N  NZ  . LYS D 2 89   ? 30.583   117.731 72.424  1.00 286.79 ? 89   LYS Y NZ  1 
ATOM   26471 N  N   . ASP D 2 90   ? 28.552   111.392 70.377  1.00 295.41 ? 90   ASP Y N   1 
ATOM   26472 C  CA  . ASP D 2 90   ? 29.003   110.214 71.118  1.00 300.38 ? 90   ASP Y CA  1 
ATOM   26473 C  C   . ASP D 2 90   ? 30.357   109.700 70.628  1.00 301.90 ? 90   ASP Y C   1 
ATOM   26474 O  O   . ASP D 2 90   ? 30.975   108.856 71.279  1.00 303.74 ? 90   ASP Y O   1 
ATOM   26475 C  CB  . ASP D 2 90   ? 27.968   109.090 71.028  1.00 302.19 ? 90   ASP Y CB  1 
ATOM   26476 C  CG  . ASP D 2 90   ? 26.737   109.359 71.868  1.00 301.93 ? 90   ASP Y CG  1 
ATOM   26477 O  OD1 . ASP D 2 90   ? 26.745   110.334 72.648  1.00 302.52 ? 90   ASP Y OD1 1 
ATOM   26478 O  OD2 . ASP D 2 90   ? 25.760   108.590 71.753  1.00 301.08 ? 90   ASP Y OD2 1 
ATOM   26479 N  N   . LYS D 2 91   ? 30.804   110.197 69.475  1.00 300.64 ? 91   LYS Y N   1 
ATOM   26480 C  CA  . LYS D 2 91   ? 32.113   109.827 68.927  1.00 300.68 ? 91   LYS Y CA  1 
ATOM   26481 C  C   . LYS D 2 91   ? 33.276   110.533 69.622  1.00 298.32 ? 91   LYS Y C   1 
ATOM   26482 O  O   . LYS D 2 91   ? 34.366   109.969 69.745  1.00 300.90 ? 91   LYS Y O   1 
ATOM   26483 C  CB  . LYS D 2 91   ? 32.198   110.124 67.430  1.00 303.45 ? 91   LYS Y CB  1 
ATOM   26484 C  CG  . LYS D 2 91   ? 33.543   109.723 66.827  1.00 309.03 ? 91   LYS Y CG  1 
ATOM   26485 C  CD  . LYS D 2 91   ? 34.004   110.666 65.724  1.00 312.11 ? 91   LYS Y CD  1 
ATOM   26486 C  CE  . LYS D 2 91   ? 35.135   111.573 66.181  1.00 316.16 ? 91   LYS Y CE  1 
ATOM   26487 N  NZ  . LYS D 2 91   ? 34.659   112.695 67.032  1.00 315.53 ? 91   LYS Y NZ  1 
ATOM   26488 N  N   . GLU D 2 92   ? 33.056   111.777 70.043  1.00 291.10 ? 92   GLU Y N   1 
ATOM   26489 C  CA  . GLU D 2 92   ? 34.087   112.532 70.750  1.00 286.38 ? 92   GLU Y CA  1 
ATOM   26490 C  C   . GLU D 2 92   ? 34.405   111.841 72.076  1.00 286.69 ? 92   GLU Y C   1 
ATOM   26491 O  O   . GLU D 2 92   ? 35.371   112.184 72.759  1.00 287.89 ? 92   GLU Y O   1 
ATOM   26492 C  CB  . GLU D 2 92   ? 33.657   113.988 70.963  1.00 277.98 ? 92   GLU Y CB  1 
ATOM   26493 C  CG  . GLU D 2 92   ? 34.774   114.894 71.461  1.00 273.86 ? 92   GLU Y CG  1 
ATOM   26494 C  CD  . GLU D 2 92   ? 36.090   114.646 70.744  1.00 271.84 ? 92   GLU Y CD  1 
ATOM   26495 O  OE1 . GLU D 2 92   ? 36.083   114.529 69.501  1.00 269.86 ? 92   GLU Y OE1 1 
ATOM   26496 O  OE2 . GLU D 2 92   ? 37.134   114.571 71.423  1.00 272.75 ? 92   GLU Y OE2 1 
ATOM   26497 N  N   . GLN D 2 93   ? 33.571   110.864 72.425  1.00 285.29 ? 93   GLN Y N   1 
ATOM   26498 C  CA  . GLN D 2 93   ? 33.795   110.001 73.577  1.00 286.09 ? 93   GLN Y CA  1 
ATOM   26499 C  C   . GLN D 2 93   ? 34.325   108.627 73.141  1.00 288.89 ? 93   GLN Y C   1 
ATOM   26500 O  O   . GLN D 2 93   ? 34.530   107.742 73.974  1.00 290.15 ? 93   GLN Y O   1 
ATOM   26501 C  CB  . GLN D 2 93   ? 32.496   109.836 74.372  1.00 281.12 ? 93   GLN Y CB  1 
ATOM   26502 C  CG  . GLN D 2 93   ? 31.766   111.144 74.648  1.00 277.40 ? 93   GLN Y CG  1 
ATOM   26503 C  CD  . GLN D 2 93   ? 30.373   110.933 75.215  1.00 272.49 ? 93   GLN Y CD  1 
ATOM   26504 O  OE1 . GLN D 2 93   ? 29.906   109.800 75.345  1.00 270.68 ? 93   GLN Y OE1 1 
ATOM   26505 N  NE2 . GLN D 2 93   ? 29.700   112.028 75.555  1.00 270.28 ? 93   GLN Y NE2 1 
ATOM   26506 N  N   . TYR D 2 94   ? 34.550   108.457 71.838  1.00 290.86 ? 94   TYR Y N   1 
ATOM   26507 C  CA  . TYR D 2 94   ? 34.958   107.165 71.272  1.00 293.52 ? 94   TYR Y CA  1 
ATOM   26508 C  C   . TYR D 2 94   ? 35.872   107.251 70.047  1.00 290.30 ? 94   TYR Y C   1 
ATOM   26509 O  O   . TYR D 2 94   ? 35.664   106.534 69.066  1.00 289.21 ? 94   TYR Y O   1 
ATOM   26510 C  CB  . TYR D 2 94   ? 33.735   106.319 70.907  1.00 298.29 ? 94   TYR Y CB  1 
ATOM   26511 C  CG  . TYR D 2 94   ? 33.439   105.212 71.886  1.00 304.85 ? 94   TYR Y CG  1 
ATOM   26512 C  CD1 . TYR D 2 94   ? 34.361   104.199 72.113  1.00 309.38 ? 94   TYR Y CD1 1 
ATOM   26513 C  CD2 . TYR D 2 94   ? 32.235   105.171 72.574  1.00 305.48 ? 94   TYR Y CD2 1 
ATOM   26514 C  CE1 . TYR D 2 94   ? 34.097   103.183 73.003  1.00 310.53 ? 94   TYR Y CE1 1 
ATOM   26515 C  CE2 . TYR D 2 94   ? 31.960   104.159 73.466  1.00 306.60 ? 94   TYR Y CE2 1 
ATOM   26516 C  CZ  . TYR D 2 94   ? 32.895   103.167 73.677  1.00 308.84 ? 94   TYR Y CZ  1 
ATOM   26517 O  OH  . TYR D 2 94   ? 32.626   102.155 74.568  1.00 308.60 ? 94   TYR Y OH  1 
ATOM   26518 N  N   . LYS D 2 95   ? 36.872   108.126 70.096  1.00 287.92 ? 95   LYS Y N   1 
ATOM   26519 C  CA  . LYS D 2 95   ? 37.906   108.147 69.066  1.00 285.53 ? 95   LYS Y CA  1 
ATOM   26520 C  C   . LYS D 2 95   ? 38.894   107.008 69.296  1.00 285.84 ? 95   LYS Y C   1 
ATOM   26521 O  O   . LYS D 2 95   ? 39.842   106.839 68.533  1.00 288.99 ? 95   LYS Y O   1 
ATOM   26522 C  CB  . LYS D 2 95   ? 38.658   109.478 69.067  1.00 284.23 ? 95   LYS Y CB  1 
ATOM   26523 C  CG  . LYS D 2 95   ? 37.917   110.631 68.423  1.00 279.81 ? 95   LYS Y CG  1 
ATOM   26524 C  CD  . LYS D 2 95   ? 38.851   111.812 68.208  1.00 279.85 ? 95   LYS Y CD  1 
ATOM   26525 C  CE  . LYS D 2 95   ? 38.155   112.952 67.483  1.00 276.59 ? 95   LYS Y CE  1 
ATOM   26526 N  NZ  . LYS D 2 95   ? 39.104   114.033 67.097  1.00 277.65 ? 95   LYS Y NZ  1 
ATOM   26527 N  N   . GLU D 2 96   ? 38.668   106.240 70.360  1.00 282.00 ? 96   GLU Y N   1 
ATOM   26528 C  CA  . GLU D 2 96   ? 39.561   105.153 70.757  1.00 280.77 ? 96   GLU Y CA  1 
ATOM   26529 C  C   . GLU D 2 96   ? 39.325   103.877 69.945  1.00 278.33 ? 96   GLU Y C   1 
ATOM   26530 O  O   . GLU D 2 96   ? 40.269   103.284 69.416  1.00 280.24 ? 96   GLU Y O   1 
ATOM   26531 C  CB  . GLU D 2 96   ? 39.393   104.863 72.253  1.00 279.12 ? 96   GLU Y CB  1 
ATOM   26532 C  CG  . GLU D 2 96   ? 37.970   104.470 72.653  1.00 275.48 ? 96   GLU Y CG  1 
ATOM   26533 C  CD  . GLU D 2 96   ? 37.682   104.696 74.123  1.00 274.84 ? 96   GLU Y CD  1 
ATOM   26534 O  OE1 . GLU D 2 96   ? 38.191   105.690 74.683  1.00 275.98 ? 96   GLU Y OE1 1 
ATOM   26535 O  OE2 . GLU D 2 96   ? 36.940   103.882 74.713  1.00 273.16 ? 96   GLU Y OE2 1 
ATOM   26536 N  N   . GLY D 2 97   ? 38.064   103.460 69.859  1.00 274.09 ? 97   GLY Y N   1 
ATOM   26537 C  CA  . GLY D 2 97   ? 37.697   102.259 69.130  1.00 272.00 ? 97   GLY Y CA  1 
ATOM   26538 C  C   . GLY D 2 97   ? 36.415   101.624 69.639  1.00 267.63 ? 97   GLY Y C   1 
ATOM   26539 O  O   . GLY D 2 97   ? 35.849   102.067 70.642  1.00 266.05 ? 97   GLY Y O   1 
ATOM   26540 N  N   . LEU D 2 98   ? 35.957   100.587 68.940  1.00 265.61 ? 98   LEU Y N   1 
ATOM   26541 C  CA  . LEU D 2 98   ? 34.759   99.844  69.330  1.00 261.85 ? 98   LEU Y CA  1 
ATOM   26542 C  C   . LEU D 2 98   ? 35.082   98.583  70.130  1.00 262.17 ? 98   LEU Y C   1 
ATOM   26543 O  O   . LEU D 2 98   ? 35.905   97.772  69.711  1.00 263.64 ? 98   LEU Y O   1 
ATOM   26544 C  CB  . LEU D 2 98   ? 33.944   99.437  68.096  1.00 260.13 ? 98   LEU Y CB  1 
ATOM   26545 C  CG  . LEU D 2 98   ? 33.165   100.472 67.280  1.00 258.50 ? 98   LEU Y CG  1 
ATOM   26546 C  CD1 . LEU D 2 98   ? 32.207   99.745  66.342  1.00 256.45 ? 98   LEU Y CD1 1 
ATOM   26547 C  CD2 . LEU D 2 98   ? 32.412   101.460 68.169  1.00 256.50 ? 98   LEU Y CD2 1 
ATOM   26548 N  N   . GLN D 2 99   ? 34.435   98.426  71.282  1.00 260.81 ? 99   GLN Y N   1 
ATOM   26549 C  CA  . GLN D 2 99   ? 34.399   97.139  71.968  1.00 261.61 ? 99   GLN Y CA  1 
ATOM   26550 C  C   . GLN D 2 99   ? 33.062   96.469  71.635  1.00 261.28 ? 99   GLN Y C   1 
ATOM   26551 O  O   . GLN D 2 99   ? 32.001   96.992  71.981  1.00 258.26 ? 99   GLN Y O   1 
ATOM   26552 C  CB  . GLN D 2 99   ? 34.560   97.303  73.486  1.00 260.57 ? 99   GLN Y CB  1 
ATOM   26553 C  CG  . GLN D 2 99   ? 35.729   98.177  73.928  1.00 262.24 ? 99   GLN Y CG  1 
ATOM   26554 C  CD  . GLN D 2 99   ? 35.317   99.615  74.179  1.00 260.90 ? 99   GLN Y CD  1 
ATOM   26555 O  OE1 . GLN D 2 99   ? 34.147   99.967  74.035  1.00 258.78 ? 99   GLN Y OE1 1 
ATOM   26556 N  NE2 . GLN D 2 99   ? 36.276   100.452 74.562  1.00 262.47 ? 99   GLN Y NE2 1 
ATOM   26557 N  N   . GLY D 2 100  ? 33.123   95.313  70.976  1.00 263.77 ? 100  GLY Y N   1 
ATOM   26558 C  CA  . GLY D 2 100  ? 31.948   94.642  70.434  1.00 263.10 ? 100  GLY Y CA  1 
ATOM   26559 C  C   . GLY D 2 100  ? 30.578   95.227  70.749  1.00 260.54 ? 100  GLY Y C   1 
ATOM   26560 O  O   . GLY D 2 100  ? 29.867   94.732  71.622  1.00 258.69 ? 100  GLY Y O   1 
ATOM   26561 N  N   . GLN D 2 101  ? 30.208   96.283  70.027  1.00 261.73 ? 101  GLN Y N   1 
ATOM   26562 C  CA  . GLN D 2 101  ? 28.881   96.882  70.149  1.00 261.31 ? 101  GLN Y CA  1 
ATOM   26563 C  C   . GLN D 2 101  ? 27.929   96.367  69.073  1.00 262.81 ? 101  GLN Y C   1 
ATOM   26564 O  O   . GLN D 2 101  ? 28.310   95.554  68.229  1.00 262.31 ? 101  GLN Y O   1 
ATOM   26565 C  CB  . GLN D 2 101  ? 28.952   98.409  70.047  1.00 261.89 ? 101  GLN Y CB  1 
ATOM   26566 C  CG  . GLN D 2 101  ? 29.592   99.105  71.226  1.00 264.24 ? 101  GLN Y CG  1 
ATOM   26567 C  CD  . GLN D 2 101  ? 31.050   99.406  70.987  1.00 268.65 ? 101  GLN Y CD  1 
ATOM   26568 O  OE1 . GLN D 2 101  ? 31.639   98.931  70.016  1.00 270.35 ? 101  GLN Y OE1 1 
ATOM   26569 N  NE2 . GLN D 2 101  ? 31.645   100.202 71.869  1.00 270.62 ? 101  GLN Y NE2 1 
ATOM   26570 N  N   . ASN D 2 102  ? 26.688   96.849  69.115  1.00 265.24 ? 102  ASN Y N   1 
ATOM   26571 C  CA  . ASN D 2 102  ? 25.723   96.621  68.042  1.00 267.66 ? 102  ASN Y CA  1 
ATOM   26572 C  C   . ASN D 2 102  ? 25.762   97.753  67.021  1.00 275.68 ? 102  ASN Y C   1 
ATOM   26573 O  O   . ASN D 2 102  ? 25.627   98.924  67.376  1.00 275.78 ? 102  ASN Y O   1 
ATOM   26574 C  CB  . ASN D 2 102  ? 24.308   96.497  68.604  1.00 260.09 ? 102  ASN Y CB  1 
ATOM   26575 C  CG  . ASN D 2 102  ? 24.084   95.196  69.333  1.00 254.45 ? 102  ASN Y CG  1 
ATOM   26576 O  OD1 . ASN D 2 102  ? 23.867   95.178  70.541  1.00 252.07 ? 102  ASN Y OD1 1 
ATOM   26577 N  ND2 . ASN D 2 102  ? 24.140   94.094  68.601  1.00 252.91 ? 102  ASN Y ND2 1 
ATOM   26578 N  N   . VAL D 2 103  ? 25.935   97.403  65.753  1.00 284.13 ? 103  VAL Y N   1 
ATOM   26579 C  CA  . VAL D 2 103  ? 25.993   98.406  64.702  1.00 293.64 ? 103  VAL Y CA  1 
ATOM   26580 C  C   . VAL D 2 103  ? 24.948   98.136  63.635  1.00 300.78 ? 103  VAL Y C   1 
ATOM   26581 O  O   . VAL D 2 103  ? 25.081   97.215  62.829  1.00 301.02 ? 103  VAL Y O   1 
ATOM   26582 C  CB  . VAL D 2 103  ? 27.391   98.475  64.040  1.00 300.48 ? 103  VAL Y CB  1 
ATOM   26583 C  CG1 . VAL D 2 103  ? 27.352   99.390  62.820  1.00 301.14 ? 103  VAL Y CG1 1 
ATOM   26584 C  CG2 . VAL D 2 103  ? 28.434   98.955  65.034  1.00 303.39 ? 103  VAL Y CG2 1 
ATOM   26585 N  N   . PHE D 2 104  ? 23.898   98.948  63.657  1.00 307.91 ? 104  PHE Y N   1 
ATOM   26586 C  CA  . PHE D 2 104  ? 22.872   98.927  62.628  1.00 314.90 ? 104  PHE Y CA  1 
ATOM   26587 C  C   . PHE D 2 104  ? 23.516   99.334  61.309  1.00 315.25 ? 104  PHE Y C   1 
ATOM   26588 O  O   . PHE D 2 104  ? 23.418   100.483 60.887  1.00 314.98 ? 104  PHE Y O   1 
ATOM   26589 C  CB  . PHE D 2 104  ? 21.763   99.910  63.003  1.00 320.78 ? 104  PHE Y CB  1 
ATOM   26590 C  CG  . PHE D 2 104  ? 20.528   99.789  62.164  1.00 324.48 ? 104  PHE Y CG  1 
ATOM   26591 C  CD1 . PHE D 2 104  ? 19.752   98.644  62.214  1.00 325.41 ? 104  PHE Y CD1 1 
ATOM   26592 C  CD2 . PHE D 2 104  ? 20.131   100.828 61.342  1.00 325.67 ? 104  PHE Y CD2 1 
ATOM   26593 C  CE1 . PHE D 2 104  ? 18.610   98.533  61.450  1.00 324.34 ? 104  PHE Y CE1 1 
ATOM   26594 C  CE2 . PHE D 2 104  ? 18.988   100.726 60.579  1.00 324.51 ? 104  PHE Y CE2 1 
ATOM   26595 C  CZ  . PHE D 2 104  ? 18.228   99.576  60.631  1.00 323.71 ? 104  PHE Y CZ  1 
ATOM   26596 N  N   . VAL D 2 105  ? 24.183   98.385  60.662  1.00 314.64 ? 105  VAL Y N   1 
ATOM   26597 C  CA  . VAL D 2 105  ? 24.909   98.672  59.432  1.00 313.32 ? 105  VAL Y CA  1 
ATOM   26598 C  C   . VAL D 2 105  ? 24.003   98.634  58.202  1.00 307.22 ? 105  VAL Y C   1 
ATOM   26599 O  O   . VAL D 2 105  ? 23.841   97.594  57.562  1.00 307.98 ? 105  VAL Y O   1 
ATOM   26600 C  CB  . VAL D 2 105  ? 26.117   97.727  59.251  1.00 316.68 ? 105  VAL Y CB  1 
ATOM   26601 C  CG1 . VAL D 2 105  ? 25.720   96.289  59.533  1.00 316.72 ? 105  VAL Y CG1 1 
ATOM   26602 C  CG2 . VAL D 2 105  ? 26.716   97.874  57.860  1.00 318.12 ? 105  VAL Y CG2 1 
ATOM   26603 N  N   . VAL D 2 106  ? 23.403   99.778  57.890  1.00 299.83 ? 106  VAL Y N   1 
ATOM   26604 C  CA  . VAL D 2 106  ? 22.679   99.945  56.639  1.00 292.32 ? 106  VAL Y CA  1 
ATOM   26605 C  C   . VAL D 2 106  ? 23.542   100.782 55.710  1.00 286.27 ? 106  VAL Y C   1 
ATOM   26606 O  O   . VAL D 2 106  ? 24.193   101.728 56.145  1.00 286.77 ? 106  VAL Y O   1 
ATOM   26607 C  CB  . VAL D 2 106  ? 21.321   100.632 56.853  1.00 290.10 ? 106  VAL Y CB  1 
ATOM   26608 C  CG1 . VAL D 2 106  ? 20.568   99.955  57.973  1.00 289.33 ? 106  VAL Y CG1 1 
ATOM   26609 C  CG2 . VAL D 2 106  ? 21.510   102.106 57.159  1.00 290.12 ? 106  VAL Y CG2 1 
ATOM   26610 N  N   . GLN D 2 107  ? 23.561   100.430 54.431  1.00 279.78 ? 107  GLN Y N   1 
ATOM   26611 C  CA  . GLN D 2 107  ? 24.429   101.120 53.483  1.00 274.62 ? 107  GLN Y CA  1 
ATOM   26612 C  C   . GLN D 2 107  ? 23.903   102.503 53.092  1.00 268.89 ? 107  GLN Y C   1 
ATOM   26613 O  O   . GLN D 2 107  ? 22.712   102.666 52.819  1.00 266.61 ? 107  GLN Y O   1 
ATOM   26614 C  CB  . GLN D 2 107  ? 24.685   100.243 52.250  1.00 273.10 ? 107  GLN Y CB  1 
ATOM   26615 C  CG  . GLN D 2 107  ? 23.423   99.642  51.638  1.00 268.34 ? 107  GLN Y CG  1 
ATOM   26616 C  CD  . GLN D 2 107  ? 23.731   98.542  50.639  1.00 267.59 ? 107  GLN Y CD  1 
ATOM   26617 O  OE1 . GLN D 2 107  ? 24.606   97.705  50.871  1.00 269.06 ? 107  GLN Y OE1 1 
ATOM   26618 N  NE2 . GLN D 2 107  ? 23.009   98.532  49.526  1.00 265.33 ? 107  GLN Y NE2 1 
ATOM   26619 N  N   . GLU D 2 108  ? 24.795   103.496 53.089  1.00 265.99 ? 108  GLU Y N   1 
ATOM   26620 C  CA  . GLU D 2 108  ? 24.465   104.849 52.626  1.00 260.31 ? 108  GLU Y CA  1 
ATOM   26621 C  C   . GLU D 2 108  ? 25.069   105.066 51.231  1.00 259.33 ? 108  GLU Y C   1 
ATOM   26622 O  O   . GLU D 2 108  ? 24.532   105.810 50.412  1.00 257.74 ? 108  GLU Y O   1 
ATOM   26623 C  CB  . GLU D 2 108  ? 25.012   105.905 53.589  1.00 258.56 ? 108  GLU Y CB  1 
ATOM   26624 C  CG  . GLU D 2 108  ? 24.748   105.613 55.067  1.00 255.80 ? 108  GLU Y CG  1 
ATOM   26625 C  CD  . GLU D 2 108  ? 23.354   106.005 55.508  1.00 250.58 ? 108  GLU Y CD  1 
ATOM   26626 O  OE1 . GLU D 2 108  ? 22.881   107.084 55.099  1.00 248.50 ? 108  GLU Y OE1 1 
ATOM   26627 O  OE2 . GLU D 2 108  ? 22.737   105.239 56.274  1.00 249.10 ? 108  GLU Y OE2 1 
ATOM   26628 N  N   . LEU D 2 109  ? 26.195   104.402 50.987  1.00 260.20 ? 109  LEU Y N   1 
ATOM   26629 C  CA  . LEU D 2 109  ? 26.865   104.376 49.696  1.00 262.29 ? 109  LEU Y CA  1 
ATOM   26630 C  C   . LEU D 2 109  ? 27.768   103.155 49.735  1.00 271.36 ? 109  LEU Y C   1 
ATOM   26631 O  O   . LEU D 2 109  ? 27.981   102.590 50.804  1.00 272.77 ? 109  LEU Y O   1 
ATOM   26632 C  CB  . LEU D 2 109  ? 27.647   105.659 49.445  1.00 258.67 ? 109  LEU Y CB  1 
ATOM   26633 C  CG  . LEU D 2 109  ? 26.921   106.875 48.900  1.00 254.72 ? 109  LEU Y CG  1 
ATOM   26634 C  CD1 . LEU D 2 109  ? 27.837   108.099 48.820  1.00 255.95 ? 109  LEU Y CD1 1 
ATOM   26635 C  CD2 . LEU D 2 109  ? 26.335   106.573 47.532  1.00 251.71 ? 109  LEU Y CD2 1 
ATOM   26636 N  N   . ILE D 2 110  ? 28.319   102.753 48.595  1.00 280.02 ? 110  ILE Y N   1 
ATOM   26637 C  CA  . ILE D 2 110  ? 29.058   101.491 48.541  1.00 290.77 ? 110  ILE Y CA  1 
ATOM   26638 C  C   . ILE D 2 110  ? 30.305   101.511 47.645  1.00 301.09 ? 110  ILE Y C   1 
ATOM   26639 O  O   . ILE D 2 110  ? 30.459   102.383 46.788  1.00 301.42 ? 110  ILE Y O   1 
ATOM   26640 C  CB  . ILE D 2 110  ? 28.138   100.330 48.088  1.00 289.98 ? 110  ILE Y CB  1 
ATOM   26641 C  CG1 . ILE D 2 110  ? 26.875   100.280 48.938  1.00 286.71 ? 110  ILE Y CG1 1 
ATOM   26642 C  CG2 . ILE D 2 110  ? 28.854   98.987  48.162  1.00 293.44 ? 110  ILE Y CG2 1 
ATOM   26643 C  CD1 . ILE D 2 110  ? 26.112   98.996  48.772  1.00 285.30 ? 110  ILE Y CD1 1 
ATOM   26644 N  N   . ASP D 2 111  ? 31.200   100.552 47.878  1.00 311.00 ? 111  ASP Y N   1 
ATOM   26645 C  CA  . ASP D 2 111  ? 32.336   100.288 47.002  1.00 320.73 ? 111  ASP Y CA  1 
ATOM   26646 C  C   . ASP D 2 111  ? 32.060   98.991  46.234  1.00 324.19 ? 111  ASP Y C   1 
ATOM   26647 O  O   . ASP D 2 111  ? 31.326   98.130  46.719  1.00 323.60 ? 111  ASP Y O   1 
ATOM   26648 C  CB  . ASP D 2 111  ? 33.620   100.182 47.831  1.00 325.72 ? 111  ASP Y CB  1 
ATOM   26649 C  CG  . ASP D 2 111  ? 34.870   100.120 46.975  1.00 330.34 ? 111  ASP Y CG  1 
ATOM   26650 O  OD1 . ASP D 2 111  ? 35.177   99.031  46.448  1.00 332.96 ? 111  ASP Y OD1 1 
ATOM   26651 O  OD2 . ASP D 2 111  ? 35.556   101.157 46.845  1.00 331.14 ? 111  ASP Y OD2 1 
ATOM   26652 N  N   . PRO D 2 112  ? 32.635   98.850  45.027  1.00 327.50 ? 112  PRO Y N   1 
ATOM   26653 C  CA  . PRO D 2 112  ? 32.395   97.659  44.202  1.00 327.61 ? 112  PRO Y CA  1 
ATOM   26654 C  C   . PRO D 2 112  ? 32.638   96.325  44.918  1.00 327.52 ? 112  PRO Y C   1 
ATOM   26655 O  O   . PRO D 2 112  ? 31.997   95.334  44.569  1.00 327.36 ? 112  PRO Y O   1 
ATOM   26656 C  CB  . PRO D 2 112  ? 33.389   97.838  43.036  1.00 330.66 ? 112  PRO Y CB  1 
ATOM   26657 C  CG  . PRO D 2 112  ? 34.311   98.967  43.473  1.00 332.21 ? 112  PRO Y CG  1 
ATOM   26658 C  CD  . PRO D 2 112  ? 33.423   99.843  44.282  1.00 329.39 ? 112  PRO Y CD  1 
ATOM   26659 N  N   . ASN D 2 113  ? 33.536   96.301  45.900  1.00 327.05 ? 113  ASN Y N   1 
ATOM   26660 C  CA  . ASN D 2 113  ? 33.853   95.065  46.620  1.00 325.49 ? 113  ASN Y CA  1 
ATOM   26661 C  C   . ASN D 2 113  ? 32.760   94.624  47.596  1.00 319.49 ? 113  ASN Y C   1 
ATOM   26662 O  O   . ASN D 2 113  ? 32.901   93.613  48.286  1.00 319.41 ? 113  ASN Y O   1 
ATOM   26663 C  CB  . ASN D 2 113  ? 35.198   95.180  47.350  1.00 329.28 ? 113  ASN Y CB  1 
ATOM   26664 C  CG  . ASN D 2 113  ? 35.102   95.982  48.635  1.00 329.43 ? 113  ASN Y CG  1 
ATOM   26665 O  OD1 . ASN D 2 113  ? 35.704   95.629  49.651  1.00 330.75 ? 113  ASN Y OD1 1 
ATOM   26666 N  ND2 . ASN D 2 113  ? 34.339   97.067  48.598  1.00 328.03 ? 113  ASN Y ND2 1 
ATOM   26667 N  N   . GLY D 2 114  ? 31.672   95.384  47.647  1.00 313.95 ? 114  GLY Y N   1 
ATOM   26668 C  CA  . GLY D 2 114  ? 30.568   95.070  48.534  1.00 308.02 ? 114  GLY Y CA  1 
ATOM   26669 C  C   . GLY D 2 114  ? 30.613   95.823  49.849  1.00 303.97 ? 114  GLY Y C   1 
ATOM   26670 O  O   . GLY D 2 114  ? 29.593   95.950  50.532  1.00 301.93 ? 114  GLY Y O   1 
ATOM   26671 N  N   . ARG D 2 115  ? 31.793   96.321  50.210  1.00 302.44 ? 115  ARG Y N   1 
ATOM   26672 C  CA  . ARG D 2 115  ? 31.930   97.107  51.431  1.00 298.87 ? 115  ARG Y CA  1 
ATOM   26673 C  C   . ARG D 2 115  ? 31.131   98.389  51.282  1.00 296.44 ? 115  ARG Y C   1 
ATOM   26674 O  O   . ARG D 2 115  ? 31.083   98.984  50.206  1.00 295.07 ? 115  ARG Y O   1 
ATOM   26675 C  CB  . ARG D 2 115  ? 33.391   97.435  51.730  1.00 300.07 ? 115  ARG Y CB  1 
ATOM   26676 C  CG  . ARG D 2 115  ? 33.894   98.719  51.107  1.00 300.00 ? 115  ARG Y CG  1 
ATOM   26677 C  CD  . ARG D 2 115  ? 35.321   99.007  51.528  1.00 302.45 ? 115  ARG Y CD  1 
ATOM   26678 N  NE  . ARG D 2 115  ? 35.984   99.920  50.603  1.00 303.34 ? 115  ARG Y NE  1 
ATOM   26679 C  CZ  . ARG D 2 115  ? 36.804   99.530  49.633  1.00 304.98 ? 115  ARG Y CZ  1 
ATOM   26680 N  NH1 . ARG D 2 115  ? 37.071   98.240  49.467  1.00 306.01 ? 115  ARG Y NH1 1 
ATOM   26681 N  NH2 . ARG D 2 115  ? 37.361   100.431 48.834  1.00 305.70 ? 115  ARG Y NH2 1 
ATOM   26682 N  N   . LEU D 2 116  ? 30.511   98.816  52.371  1.00 296.40 ? 116  LEU Y N   1 
ATOM   26683 C  CA  . LEU D 2 116  ? 29.580   99.927  52.309  1.00 295.84 ? 116  LEU Y CA  1 
ATOM   26684 C  C   . LEU D 2 116  ? 29.823   100.913 53.440  1.00 299.30 ? 116  LEU Y C   1 
ATOM   26685 O  O   . LEU D 2 116  ? 30.017   100.520 54.590  1.00 300.06 ? 116  LEU Y O   1 
ATOM   26686 C  CB  . LEU D 2 116  ? 28.141   99.400  52.342  1.00 289.87 ? 116  LEU Y CB  1 
ATOM   26687 C  CG  . LEU D 2 116  ? 27.799   98.427  53.473  1.00 285.72 ? 116  LEU Y CG  1 
ATOM   26688 C  CD1 . LEU D 2 116  ? 27.228   99.176  54.664  1.00 282.88 ? 116  LEU Y CD1 1 
ATOM   26689 C  CD2 . LEU D 2 116  ? 26.819   97.377  52.991  1.00 282.69 ? 116  LEU Y CD2 1 
ATOM   26690 N  N   . SER D 2 117  ? 29.829   102.197 53.097  1.00 301.87 ? 117  SER Y N   1 
ATOM   26691 C  CA  . SER D 2 117  ? 29.943   103.258 54.088  1.00 303.85 ? 117  SER Y CA  1 
ATOM   26692 C  C   . SER D 2 117  ? 28.620   103.432 54.844  1.00 301.02 ? 117  SER Y C   1 
ATOM   26693 O  O   . SER D 2 117  ? 27.547   103.155 54.305  1.00 300.29 ? 117  SER Y O   1 
ATOM   26694 C  CB  . SER D 2 117  ? 30.369   104.570 53.421  1.00 306.13 ? 117  SER Y CB  1 
ATOM   26695 O  OG  . SER D 2 117  ? 29.556   104.860 52.295  1.00 305.61 ? 117  SER Y OG  1 
ATOM   26696 N  N   . THR D 2 118  ? 28.711   103.888 56.092  1.00 299.60 ? 118  THR Y N   1 
ATOM   26697 C  CA  . THR D 2 118  ? 27.546   104.061 56.963  1.00 295.09 ? 118  THR Y CA  1 
ATOM   26698 C  C   . THR D 2 118  ? 27.853   105.073 58.073  1.00 294.29 ? 118  THR Y C   1 
ATOM   26699 O  O   . THR D 2 118  ? 29.017   105.360 58.354  1.00 296.23 ? 118  THR Y O   1 
ATOM   26700 C  CB  . THR D 2 118  ? 27.096   102.714 57.584  1.00 312.00 ? 118  THR Y CB  1 
ATOM   26701 O  OG1 . THR D 2 118  ? 26.015   102.934 58.499  1.00 309.58 ? 118  THR Y OG1 1 
ATOM   26702 C  CG2 . THR D 2 118  ? 28.248   102.043 58.321  1.00 314.43 ? 118  THR Y CG2 1 
ATOM   26703 N  N   . VAL D 2 119  ? 26.818   105.613 58.708  1.00 289.53 ? 119  VAL Y N   1 
ATOM   26704 C  CA  . VAL D 2 119  ? 27.024   106.631 59.734  1.00 287.16 ? 119  VAL Y CA  1 
ATOM   26705 C  C   . VAL D 2 119  ? 26.147   106.410 60.963  1.00 283.67 ? 119  VAL Y C   1 
ATOM   26706 O  O   . VAL D 2 119  ? 24.921   106.375 60.870  1.00 281.20 ? 119  VAL Y O   1 
ATOM   26707 C  CB  . VAL D 2 119  ? 26.796   108.053 59.173  1.00 284.69 ? 119  VAL Y CB  1 
ATOM   26708 C  CG1 . VAL D 2 119  ? 25.510   108.110 58.366  1.00 281.02 ? 119  VAL Y CG1 1 
ATOM   26709 C  CG2 . VAL D 2 119  ? 26.783   109.076 60.297  1.00 283.81 ? 119  VAL Y CG2 1 
ATOM   26710 N  N   . GLY D 2 120  ? 26.791   106.266 62.116  1.00 282.88 ? 120  GLY Y N   1 
ATOM   26711 C  CA  . GLY D 2 120  ? 26.087   106.040 63.363  1.00 279.20 ? 120  GLY Y CA  1 
ATOM   26712 C  C   . GLY D 2 120  ? 25.515   104.641 63.450  1.00 276.07 ? 120  GLY Y C   1 
ATOM   26713 O  O   . GLY D 2 120  ? 26.054   103.700 62.866  1.00 278.77 ? 120  GLY Y O   1 
ATOM   26714 N  N   . GLY D 2 121  ? 24.419   104.508 64.191  1.00 271.39 ? 121  GLY Y N   1 
ATOM   26715 C  CA  . GLY D 2 121  ? 23.714   103.243 64.305  1.00 268.28 ? 121  GLY Y CA  1 
ATOM   26716 C  C   . GLY D 2 121  ? 24.223   102.327 65.404  1.00 268.70 ? 121  GLY Y C   1 
ATOM   26717 O  O   . GLY D 2 121  ? 23.717   101.218 65.587  1.00 267.56 ? 121  GLY Y O   1 
ATOM   26718 N  N   . VAL D 2 122  ? 25.225   102.791 66.142  1.00 268.97 ? 122  VAL Y N   1 
ATOM   26719 C  CA  . VAL D 2 122  ? 25.839   101.971 67.177  1.00 266.52 ? 122  VAL Y CA  1 
ATOM   26720 C  C   . VAL D 2 122  ? 25.075   102.001 68.501  1.00 259.59 ? 122  VAL Y C   1 
ATOM   26721 O  O   . VAL D 2 122  ? 24.520   103.030 68.900  1.00 259.54 ? 122  VAL Y O   1 
ATOM   26722 C  CB  . VAL D 2 122  ? 27.303   102.370 67.409  1.00 269.97 ? 122  VAL Y CB  1 
ATOM   26723 C  CG1 . VAL D 2 122  ? 27.988   101.361 68.318  1.00 271.17 ? 122  VAL Y CG1 1 
ATOM   26724 C  CG2 . VAL D 2 122  ? 28.030   102.477 66.078  1.00 271.06 ? 122  VAL Y CG2 1 
ATOM   26725 N  N   . THR D 2 123  ? 25.071   100.857 69.175  1.00 252.70 ? 123  THR Y N   1 
ATOM   26726 C  CA  . THR D 2 123  ? 24.358   100.678 70.434  1.00 245.18 ? 123  THR Y CA  1 
ATOM   26727 C  C   . THR D 2 123  ? 25.205   99.835  71.397  1.00 242.83 ? 123  THR Y C   1 
ATOM   26728 O  O   . THR D 2 123  ? 26.284   99.374  71.021  1.00 244.06 ? 123  THR Y O   1 
ATOM   26729 C  CB  . THR D 2 123  ? 22.946   100.067 70.201  1.00 262.94 ? 123  THR Y CB  1 
ATOM   26730 O  OG1 . THR D 2 123  ? 22.655   99.089  71.207  1.00 262.43 ? 123  THR Y OG1 1 
ATOM   26731 C  CG2 . THR D 2 123  ? 22.860   99.415  68.826  1.00 262.63 ? 123  THR Y CG2 1 
ATOM   26732 N  N   . LYS D 2 124  ? 24.724   99.641  72.627  1.00 236.62 ? 124  LYS Y N   1 
ATOM   26733 C  CA  . LYS D 2 124  ? 25.548   99.092  73.718  1.00 232.90 ? 124  LYS Y CA  1 
ATOM   26734 C  C   . LYS D 2 124  ? 26.191   97.705  73.506  1.00 232.23 ? 124  LYS Y C   1 
ATOM   26735 O  O   . LYS D 2 124  ? 27.397   97.611  73.252  1.00 235.34 ? 124  LYS Y O   1 
ATOM   26736 C  CB  . LYS D 2 124  ? 24.806   99.160  75.068  1.00 226.40 ? 124  LYS Y CB  1 
ATOM   26737 C  CG  . LYS D 2 124  ? 23.438   98.504  75.105  1.00 218.74 ? 124  LYS Y CG  1 
ATOM   26738 C  CD  . LYS D 2 124  ? 22.648   98.964  76.323  1.00 213.61 ? 124  LYS Y CD  1 
ATOM   26739 C  CE  . LYS D 2 124  ? 23.276   98.494  77.624  1.00 212.57 ? 124  LYS Y CE  1 
ATOM   26740 N  NZ  . LYS D 2 124  ? 23.010   97.057  77.876  1.00 211.46 ? 124  LYS Y NZ  1 
ATOM   26741 N  N   . LYS D 2 125  ? 25.399   96.641  73.618  1.00 228.06 ? 125  LYS Y N   1 
ATOM   26742 C  CA  . LYS D 2 125  ? 25.934   95.276  73.585  1.00 226.96 ? 125  LYS Y CA  1 
ATOM   26743 C  C   . LYS D 2 125  ? 26.878   95.052  74.767  1.00 229.29 ? 125  LYS Y C   1 
ATOM   26744 O  O   . LYS D 2 125  ? 27.944   95.674  74.834  1.00 230.10 ? 125  LYS Y O   1 
ATOM   26745 C  CB  . LYS D 2 125  ? 26.656   94.993  72.257  1.00 226.58 ? 125  LYS Y CB  1 
ATOM   26746 C  CG  . LYS D 2 125  ? 27.236   93.578  72.120  1.00 226.03 ? 125  LYS Y CG  1 
ATOM   26747 C  CD  . LYS D 2 125  ? 26.158   92.547  71.809  1.00 222.28 ? 125  LYS Y CD  1 
ATOM   26748 C  CE  . LYS D 2 125  ? 26.755   91.169  71.584  1.00 221.91 ? 125  LYS Y CE  1 
ATOM   26749 N  NZ  . LYS D 2 125  ? 27.330   90.612  72.832  1.00 221.55 ? 125  LYS Y NZ  1 
ATOM   26750 N  N   . ASN D 2 126  ? 26.505   94.165  75.691  1.00 230.06 ? 126  ASN Y N   1 
ATOM   26751 C  CA  . ASN D 2 126  ? 25.294   93.350  75.595  1.00 230.35 ? 126  ASN Y CA  1 
ATOM   26752 C  C   . ASN D 2 126  ? 23.990   94.147  75.578  1.00 236.08 ? 126  ASN Y C   1 
ATOM   26753 O  O   . ASN D 2 126  ? 23.590   94.743  76.581  1.00 237.28 ? 126  ASN Y O   1 
ATOM   26754 C  CB  . ASN D 2 126  ? 25.268   92.308  76.718  1.00 223.00 ? 126  ASN Y CB  1 
ATOM   26755 C  CG  . ASN D 2 126  ? 26.454   91.367  76.662  1.00 219.73 ? 126  ASN Y CG  1 
ATOM   26756 O  OD1 . ASN D 2 126  ? 27.004   91.113  75.593  1.00 214.90 ? 126  ASN Y OD1 1 
ATOM   26757 N  ND2 . ASN D 2 126  ? 26.855   90.845  77.818  1.00 220.16 ? 126  ASN Y ND2 1 
ATOM   26758 N  N   . ASN D 2 127  ? 23.344   94.145  74.416  1.00 241.75 ? 127  ASN Y N   1 
ATOM   26759 C  CA  . ASN D 2 127  ? 22.102   94.872  74.197  1.00 248.00 ? 127  ASN Y CA  1 
ATOM   26760 C  C   . ASN D 2 127  ? 20.898   93.987  74.482  1.00 250.85 ? 127  ASN Y C   1 
ATOM   26761 O  O   . ASN D 2 127  ? 20.637   93.028  73.748  1.00 250.68 ? 127  ASN Y O   1 
ATOM   26762 C  CB  . ASN D 2 127  ? 22.043   95.382  72.753  1.00 250.94 ? 127  ASN Y CB  1 
ATOM   26763 C  CG  . ASN D 2 127  ? 21.016   96.483  72.557  1.00 254.05 ? 127  ASN Y CG  1 
ATOM   26764 O  OD1 . ASN D 2 127  ? 20.363   96.923  73.505  1.00 254.66 ? 127  ASN Y OD1 1 
ATOM   26765 N  ND2 . ASN D 2 127  ? 20.873   96.940  71.317  1.00 255.51 ? 127  ASN Y ND2 1 
ATOM   26766 N  N   . LYS D 2 128  ? 20.169   94.315  75.547  1.00 255.81 ? 128  LYS Y N   1 
ATOM   26767 C  CA  . LYS D 2 128  ? 18.991   93.549  75.951  1.00 257.24 ? 128  LYS Y CA  1 
ATOM   26768 C  C   . LYS D 2 128  ? 18.051   93.320  74.758  1.00 259.99 ? 128  LYS Y C   1 
ATOM   26769 O  O   . LYS D 2 128  ? 17.776   94.251  73.999  1.00 260.64 ? 128  LYS Y O   1 
ATOM   26770 C  CB  . LYS D 2 128  ? 18.252   94.278  77.083  1.00 253.47 ? 128  LYS Y CB  1 
ATOM   26771 C  CG  . LYS D 2 128  ? 19.145   94.758  78.225  1.00 250.90 ? 128  LYS Y CG  1 
ATOM   26772 C  CD  . LYS D 2 128  ? 18.336   95.481  79.288  1.00 245.76 ? 128  LYS Y CD  1 
ATOM   26773 C  CE  . LYS D 2 128  ? 17.068   94.718  79.625  1.00 241.07 ? 128  LYS Y CE  1 
ATOM   26774 N  NZ  . LYS D 2 128  ? 17.357   93.313  80.008  1.00 240.35 ? 128  LYS Y NZ  1 
ATOM   26775 N  N   . THR D 2 129  ? 17.571   92.088  74.583  1.00 211.00 ? 129  THR Y N   1 
ATOM   26776 C  CA  . THR D 2 129  ? 16.665   91.772  73.471  1.00 211.06 ? 129  THR Y CA  1 
ATOM   26777 C  C   . THR D 2 129  ? 15.198   92.051  73.818  1.00 211.69 ? 129  THR Y C   1 
ATOM   26778 O  O   . THR D 2 129  ? 14.306   91.262  73.492  1.00 210.53 ? 129  THR Y O   1 
ATOM   26779 C  CB  . THR D 2 129  ? 16.834   90.320  72.969  1.00 212.09 ? 129  THR Y CB  1 
ATOM   26780 O  OG1 . THR D 2 129  ? 18.229   90.014  72.859  1.00 214.02 ? 129  THR Y OG1 1 
ATOM   26781 C  CG2 . THR D 2 129  ? 16.182   90.144  71.605  1.00 210.23 ? 129  THR Y CG2 1 
ATOM   26782 N  N   . SER D 2 130  ? 14.966   93.176  74.493  1.00 213.75 ? 130  SER Y N   1 
ATOM   26783 C  CA  . SER D 2 130  ? 13.618   93.663  74.767  1.00 215.15 ? 130  SER Y CA  1 
ATOM   26784 C  C   . SER D 2 130  ? 12.857   94.009  73.477  1.00 216.67 ? 130  SER Y C   1 
ATOM   26785 O  O   . SER D 2 130  ? 13.462   94.371  72.467  1.00 216.32 ? 130  SER Y O   1 
ATOM   26786 C  CB  . SER D 2 130  ? 13.676   94.884  75.679  1.00 213.67 ? 130  SER Y CB  1 
ATOM   26787 O  OG  . SER D 2 130  ? 12.554   95.717  75.459  1.00 211.61 ? 130  SER Y OG  1 
ATOM   26788 N  N   . GLU D 2 131  ? 11.528   93.908  73.529  1.00 218.24 ? 131  GLU Y N   1 
ATOM   26789 C  CA  . GLU D 2 131  ? 10.658   94.099  72.363  1.00 216.31 ? 131  GLU Y CA  1 
ATOM   26790 C  C   . GLU D 2 131  ? 9.449    94.944  72.741  1.00 215.88 ? 131  GLU Y C   1 
ATOM   26791 O  O   . GLU D 2 131  ? 8.457    94.422  73.248  1.00 217.03 ? 131  GLU Y O   1 
ATOM   26792 C  CB  . GLU D 2 131  ? 10.168   92.741  71.837  1.00 215.69 ? 131  GLU Y CB  1 
ATOM   26793 C  CG  . GLU D 2 131  ? 8.817    92.793  71.105  1.00 213.62 ? 131  GLU Y CG  1 
ATOM   26794 C  CD  . GLU D 2 131  ? 8.191    91.416  70.870  1.00 212.93 ? 131  GLU Y CD  1 
ATOM   26795 O  OE1 . GLU D 2 131  ? 8.877    90.527  70.327  1.00 212.62 ? 131  GLU Y OE1 1 
ATOM   26796 O  OE2 . GLU D 2 131  ? 7.003    91.222  71.212  1.00 212.51 ? 131  GLU Y OE2 1 
ATOM   26797 N  N   . THR D 2 132  ? 9.522    96.248  72.502  1.00 214.05 ? 132  THR Y N   1 
ATOM   26798 C  CA  . THR D 2 132  ? 8.402    97.111  72.860  1.00 213.13 ? 132  THR Y CA  1 
ATOM   26799 C  C   . THR D 2 132  ? 7.436    97.376  71.701  1.00 209.60 ? 132  THR Y C   1 
ATOM   26800 O  O   . THR D 2 132  ? 7.840    97.549  70.548  1.00 208.12 ? 132  THR Y O   1 
ATOM   26801 C  CB  . THR D 2 132  ? 8.865    98.438  73.499  1.00 214.09 ? 132  THR Y CB  1 
ATOM   26802 O  OG1 . THR D 2 132  ? 7.723    99.264  73.761  1.00 214.97 ? 132  THR Y OG1 1 
ATOM   26803 C  CG2 . THR D 2 132  ? 9.816    99.170  72.582  1.00 212.92 ? 132  THR Y CG2 1 
ATOM   26804 N  N   . ASN D 2 133  ? 6.149    97.380  72.029  1.00 206.82 ? 133  ASN Y N   1 
ATOM   26805 C  CA  . ASN D 2 133  ? 5.100    97.725  71.085  1.00 201.33 ? 133  ASN Y CA  1 
ATOM   26806 C  C   . ASN D 2 133  ? 4.663    99.170  71.328  1.00 197.57 ? 133  ASN Y C   1 
ATOM   26807 O  O   . ASN D 2 133  ? 3.817    99.422  72.186  1.00 200.33 ? 133  ASN Y O   1 
ATOM   26808 C  CB  . ASN D 2 133  ? 3.920    96.776  71.280  1.00 200.90 ? 133  ASN Y CB  1 
ATOM   26809 C  CG  . ASN D 2 133  ? 3.003    96.737  70.087  1.00 197.72 ? 133  ASN Y CG  1 
ATOM   26810 O  OD1 . ASN D 2 133  ? 3.452    96.581  68.955  1.00 195.80 ? 133  ASN Y OD1 1 
ATOM   26811 N  ND2 . ASN D 2 133  ? 1.707    96.873  70.334  1.00 197.74 ? 133  ASN Y ND2 1 
ATOM   26812 N  N   . THR D 2 134  ? 5.240    100.114 70.580  1.00 189.73 ? 134  THR Y N   1 
ATOM   26813 C  CA  . THR D 2 134  ? 5.043    101.549 70.847  1.00 183.92 ? 134  THR Y CA  1 
ATOM   26814 C  C   . THR D 2 134  ? 3.921    102.236 70.071  1.00 178.39 ? 134  THR Y C   1 
ATOM   26815 O  O   . THR D 2 134  ? 3.830    102.098 68.847  1.00 176.26 ? 134  THR Y O   1 
ATOM   26816 C  CB  . THR D 2 134  ? 6.337    102.378 70.608  1.00 206.21 ? 134  THR Y CB  1 
ATOM   26817 O  OG1 . THR D 2 134  ? 6.017    103.774 70.642  1.00 206.43 ? 134  THR Y OG1 1 
ATOM   26818 C  CG2 . THR D 2 134  ? 6.953    102.062 69.259  1.00 204.23 ? 134  THR Y CG2 1 
ATOM   26819 N  N   . PRO D 2 135  ? 3.079    103.007 70.784  1.00 177.13 ? 135  PRO Y N   1 
ATOM   26820 C  CA  . PRO D 2 135  ? 2.127    103.896 70.113  1.00 176.06 ? 135  PRO Y CA  1 
ATOM   26821 C  C   . PRO D 2 135  ? 2.846    104.743 69.055  1.00 174.08 ? 135  PRO Y C   1 
ATOM   26822 O  O   . PRO D 2 135  ? 4.079    104.767 69.043  1.00 173.88 ? 135  PRO Y O   1 
ATOM   26823 C  CB  . PRO D 2 135  ? 1.583    104.755 71.267  1.00 177.77 ? 135  PRO Y CB  1 
ATOM   26824 C  CG  . PRO D 2 135  ? 2.502    104.469 72.441  1.00 177.89 ? 135  PRO Y CG  1 
ATOM   26825 C  CD  . PRO D 2 135  ? 2.902    103.054 72.242  1.00 177.48 ? 135  PRO Y CD  1 
ATOM   26826 N  N   . LEU D 2 136  ? 2.092    105.413 68.185  1.00 172.03 ? 136  LEU Y N   1 
ATOM   26827 C  CA  . LEU D 2 136  ? 2.655    106.016 66.975  1.00 168.85 ? 136  LEU Y CA  1 
ATOM   26828 C  C   . LEU D 2 136  ? 1.553    106.428 66.013  1.00 169.61 ? 136  LEU Y C   1 
ATOM   26829 O  O   . LEU D 2 136  ? 0.923    105.580 65.380  1.00 169.69 ? 136  LEU Y O   1 
ATOM   26830 C  CB  . LEU D 2 136  ? 3.557    105.007 66.265  1.00 165.02 ? 136  LEU Y CB  1 
ATOM   26831 C  CG  . LEU D 2 136  ? 3.568    105.112 64.739  1.00 162.08 ? 136  LEU Y CG  1 
ATOM   26832 C  CD1 . LEU D 2 136  ? 4.240    106.402 64.311  1.00 160.59 ? 136  LEU Y CD1 1 
ATOM   26833 C  CD2 . LEU D 2 136  ? 4.236    103.898 64.103  1.00 160.33 ? 136  LEU Y CD2 1 
ATOM   26834 N  N   . PHE D 2 137  ? 1.321    107.727 65.889  1.00 170.94 ? 137  PHE Y N   1 
ATOM   26835 C  CA  . PHE D 2 137  ? 0.201    108.191 65.076  1.00 173.69 ? 137  PHE Y CA  1 
ATOM   26836 C  C   . PHE D 2 137  ? 0.654    108.682 63.714  1.00 172.35 ? 137  PHE Y C   1 
ATOM   26837 O  O   . PHE D 2 137  ? 1.846    108.849 63.466  1.00 171.28 ? 137  PHE Y O   1 
ATOM   26838 C  CB  . PHE D 2 137  ? -0.610   109.274 65.796  1.00 176.77 ? 137  PHE Y CB  1 
ATOM   26839 C  CG  . PHE D 2 137  ? -0.873   108.971 67.247  1.00 178.84 ? 137  PHE Y CG  1 
ATOM   26840 C  CD1 . PHE D 2 137  ? -0.453   107.777 67.816  1.00 179.03 ? 137  PHE Y CD1 1 
ATOM   26841 C  CD2 . PHE D 2 137  ? -1.564   109.870 68.033  1.00 181.86 ? 137  PHE Y CD2 1 
ATOM   26842 C  CE1 . PHE D 2 137  ? -0.692   107.498 69.134  1.00 179.76 ? 137  PHE Y CE1 1 
ATOM   26843 C  CE2 . PHE D 2 137  ? -1.812   109.592 69.354  1.00 182.92 ? 137  PHE Y CE2 1 
ATOM   26844 C  CZ  . PHE D 2 137  ? -1.377   108.402 69.906  1.00 182.30 ? 137  PHE Y CZ  1 
ATOM   26845 N  N   . VAL D 2 138  ? -0.304   108.913 62.830  1.00 173.23 ? 138  VAL Y N   1 
ATOM   26846 C  CA  . VAL D 2 138  ? 0.015    109.391 61.498  1.00 172.08 ? 138  VAL Y CA  1 
ATOM   26847 C  C   . VAL D 2 138  ? -1.165   110.158 60.924  1.00 174.41 ? 138  VAL Y C   1 
ATOM   26848 O  O   . VAL D 2 138  ? -2.225   109.588 60.642  1.00 176.84 ? 138  VAL Y O   1 
ATOM   26849 C  CB  . VAL D 2 138  ? 0.450    108.239 60.564  1.00 167.64 ? 138  VAL Y CB  1 
ATOM   26850 C  CG1 . VAL D 2 138  ? -0.131   108.414 59.169  1.00 168.15 ? 138  VAL Y CG1 1 
ATOM   26851 C  CG2 . VAL D 2 138  ? 1.975    108.147 60.513  1.00 164.76 ? 138  VAL Y CG2 1 
ATOM   26852 N  N   . ASN D 2 139  ? -0.971   111.469 60.794  1.00 174.25 ? 139  ASN Y N   1 
ATOM   26853 C  CA  . ASN D 2 139  ? -1.966   112.360 60.215  1.00 174.18 ? 139  ASN Y CA  1 
ATOM   26854 C  C   . ASN D 2 139  ? -1.493   112.862 58.849  1.00 174.53 ? 139  ASN Y C   1 
ATOM   26855 O  O   . ASN D 2 139  ? -0.420   113.455 58.735  1.00 172.78 ? 139  ASN Y O   1 
ATOM   26856 C  CB  . ASN D 2 139  ? -2.218   113.543 61.156  1.00 174.76 ? 139  ASN Y CB  1 
ATOM   26857 C  CG  . ASN D 2 139  ? -2.038   113.175 62.617  1.00 175.19 ? 139  ASN Y CG  1 
ATOM   26858 O  OD1 . ASN D 2 139  ? -1.022   113.506 63.223  1.00 175.15 ? 139  ASN Y OD1 1 
ATOM   26859 N  ND2 . ASN D 2 139  ? -3.016   112.476 63.186  1.00 176.80 ? 139  ASN Y ND2 1 
ATOM   26860 N  N   . LYS D 2 140  ? -2.273   112.613 57.804  1.00 175.54 ? 140  LYS Y N   1 
ATOM   26861 C  CA  . LYS D 2 140  ? -1.933   113.183 56.510  1.00 175.66 ? 140  LYS Y CA  1 
ATOM   26862 C  C   . LYS D 2 140  ? -2.641   114.521 56.349  1.00 176.43 ? 140  LYS Y C   1 
ATOM   26863 O  O   . LYS D 2 140  ? -3.859   114.614 56.473  1.00 176.74 ? 140  LYS Y O   1 
ATOM   26864 C  CB  . LYS D 2 140  ? -2.264   112.218 55.364  1.00 176.19 ? 140  LYS Y CB  1 
ATOM   26865 C  CG  . LYS D 2 140  ? -1.595   110.847 55.500  1.00 174.48 ? 140  LYS Y CG  1 
ATOM   26866 C  CD  . LYS D 2 140  ? -1.487   110.102 54.174  1.00 173.05 ? 140  LYS Y CD  1 
ATOM   26867 C  CE  . LYS D 2 140  ? -0.219   110.480 53.425  1.00 171.17 ? 140  LYS Y CE  1 
ATOM   26868 N  NZ  . LYS D 2 140  ? -0.020   109.593 52.250  1.00 171.14 ? 140  LYS Y NZ  1 
ATOM   26869 N  N   . VAL D 2 141  ? -1.861   115.567 56.116  1.00 177.23 ? 141  VAL Y N   1 
ATOM   26870 C  CA  . VAL D 2 141  ? -2.425   116.873 55.826  1.00 181.88 ? 141  VAL Y CA  1 
ATOM   26871 C  C   . VAL D 2 141  ? -2.729   116.973 54.328  1.00 184.15 ? 141  VAL Y C   1 
ATOM   26872 O  O   . VAL D 2 141  ? -2.017   116.416 53.489  1.00 182.10 ? 141  VAL Y O   1 
ATOM   26873 C  CB  . VAL D 2 141  ? -1.463   118.027 56.206  1.00 182.18 ? 141  VAL Y CB  1 
ATOM   26874 C  CG1 . VAL D 2 141  ? -2.235   119.327 56.375  1.00 184.84 ? 141  VAL Y CG1 1 
ATOM   26875 C  CG2 . VAL D 2 141  ? -0.674   117.701 57.467  1.00 181.22 ? 141  VAL Y CG2 1 
ATOM   26876 N  N   . ASN D 2 142  ? -3.797   117.686 54.003  1.00 189.15 ? 142  ASN Y N   1 
ATOM   26877 C  CA  . ASN D 2 142  ? -4.116   118.020 52.628  1.00 190.28 ? 142  ASN Y CA  1 
ATOM   26878 C  C   . ASN D 2 142  ? -4.796   119.368 52.676  1.00 193.60 ? 142  ASN Y C   1 
ATOM   26879 O  O   . ASN D 2 142  ? -5.944   119.527 52.261  1.00 196.46 ? 142  ASN Y O   1 
ATOM   26880 C  CB  . ASN D 2 142  ? -5.017   116.967 51.991  1.00 189.81 ? 142  ASN Y CB  1 
ATOM   26881 C  CG  . ASN D 2 142  ? -5.140   117.141 50.494  1.00 188.21 ? 142  ASN Y CG  1 
ATOM   26882 O  OD1 . ASN D 2 142  ? -5.995   117.887 50.011  1.00 189.33 ? 142  ASN Y OD1 1 
ATOM   26883 N  ND2 . ASN D 2 142  ? -4.286   116.449 49.746  1.00 185.65 ? 142  ASN Y ND2 1 
ATOM   26884 N  N   . GLY D 2 143  ? -4.066   120.334 53.224  1.00 193.91 ? 143  GLY Y N   1 
ATOM   26885 C  CA  . GLY D 2 143  ? -4.604   121.650 53.490  1.00 197.37 ? 143  GLY Y CA  1 
ATOM   26886 C  C   . GLY D 2 143  ? -5.644   121.579 54.590  1.00 201.63 ? 143  GLY Y C   1 
ATOM   26887 O  O   . GLY D 2 143  ? -5.308   121.544 55.775  1.00 201.88 ? 143  GLY Y O   1 
ATOM   26888 N  N   . GLU D 2 144  ? -6.912   121.551 54.197  1.00 204.60 ? 144  GLU Y N   1 
ATOM   26889 C  CA  . GLU D 2 144  ? -8.000   121.473 55.160  1.00 207.34 ? 144  GLU Y CA  1 
ATOM   26890 C  C   . GLU D 2 144  ? -8.301   120.028 55.499  1.00 203.56 ? 144  GLU Y C   1 
ATOM   26891 O  O   . GLU D 2 144  ? -9.016   119.744 56.457  1.00 204.19 ? 144  GLU Y O   1 
ATOM   26892 C  CB  . GLU D 2 144  ? -9.249   122.173 54.620  1.00 213.46 ? 144  GLU Y CB  1 
ATOM   26893 C  CG  . GLU D 2 144  ? -9.148   123.686 54.658  1.00 217.29 ? 144  GLU Y CG  1 
ATOM   26894 C  CD  . GLU D 2 144  ? -8.725   124.196 56.028  1.00 219.30 ? 144  GLU Y CD  1 
ATOM   26895 O  OE1 . GLU D 2 144  ? -8.995   123.499 57.031  1.00 220.13 ? 144  GLU Y OE1 1 
ATOM   26896 O  OE2 . GLU D 2 144  ? -8.121   125.291 56.102  1.00 219.92 ? 144  GLU Y OE2 1 
ATOM   26897 N  N   . ASP D 2 145  ? -7.743   119.122 54.700  1.00 199.40 ? 145  ASP Y N   1 
ATOM   26898 C  CA  . ASP D 2 145  ? -8.000   117.693 54.840  1.00 196.45 ? 145  ASP Y CA  1 
ATOM   26899 C  C   . ASP D 2 145  ? -6.989   117.006 55.772  1.00 189.96 ? 145  ASP Y C   1 
ATOM   26900 O  O   . ASP D 2 145  ? -5.841   117.448 55.905  1.00 187.55 ? 145  ASP Y O   1 
ATOM   26901 C  CB  . ASP D 2 145  ? -8.035   117.004 53.462  1.00 196.96 ? 145  ASP Y CB  1 
ATOM   26902 C  CG  . ASP D 2 145  ? -9.305   117.329 52.657  1.00 200.80 ? 145  ASP Y CG  1 
ATOM   26903 O  OD1 . ASP D 2 145  ? -10.222  117.994 53.192  1.00 204.16 ? 145  ASP Y OD1 1 
ATOM   26904 O  OD2 . ASP D 2 145  ? -9.388   116.912 51.478  1.00 200.37 ? 145  ASP Y OD2 1 
ATOM   26905 N  N   . LEU D 2 146  ? -7.437   115.931 56.425  1.00 186.89 ? 146  LEU Y N   1 
ATOM   26906 C  CA  . LEU D 2 146  ? -6.583   115.115 57.292  1.00 181.29 ? 146  LEU Y CA  1 
ATOM   26907 C  C   . LEU D 2 146  ? -7.066   113.672 57.354  1.00 179.25 ? 146  LEU Y C   1 
ATOM   26908 O  O   . LEU D 2 146  ? -8.115   113.377 57.936  1.00 178.19 ? 146  LEU Y O   1 
ATOM   26909 C  CB  . LEU D 2 146  ? -6.548   115.660 58.719  1.00 181.61 ? 146  LEU Y CB  1 
ATOM   26910 C  CG  . LEU D 2 146  ? -5.462   115.097 59.648  1.00 179.17 ? 146  LEU Y CG  1 
ATOM   26911 C  CD1 . LEU D 2 146  ? -6.046   114.859 61.024  1.00 180.35 ? 146  LEU Y CD1 1 
ATOM   26912 C  CD2 . LEU D 2 146  ? -4.831   113.815 59.128  1.00 176.81 ? 146  LEU Y CD2 1 
ATOM   26913 N  N   . ASP D 2 147  ? -6.277   112.781 56.762  1.00 177.93 ? 147  ASP Y N   1 
ATOM   26914 C  CA  . ASP D 2 147  ? -6.490   111.351 56.896  1.00 177.37 ? 147  ASP Y CA  1 
ATOM   26915 C  C   . ASP D 2 147  ? -5.496   110.796 57.902  1.00 179.96 ? 147  ASP Y C   1 
ATOM   26916 O  O   . ASP D 2 147  ? -4.333   110.541 57.584  1.00 179.74 ? 147  ASP Y O   1 
ATOM   26917 C  CB  . ASP D 2 147  ? -6.362   110.650 55.546  1.00 169.52 ? 147  ASP Y CB  1 
ATOM   26918 C  CG  . ASP D 2 147  ? -7.484   111.021 54.590  1.00 164.71 ? 147  ASP Y CG  1 
ATOM   26919 O  OD1 . ASP D 2 147  ? -8.602   111.338 55.050  1.00 164.24 ? 147  ASP Y OD1 1 
ATOM   26920 O  OD2 . ASP D 2 147  ? -7.245   110.999 53.368  1.00 162.42 ? 147  ASP Y OD2 1 
ATOM   26921 N  N   . ALA D 2 148  ? -5.974   110.635 59.130  1.00 184.12 ? 148  ALA Y N   1 
ATOM   26922 C  CA  . ALA D 2 148  ? -5.145   110.190 60.240  1.00 184.74 ? 148  ALA Y CA  1 
ATOM   26923 C  C   . ALA D 2 148  ? -5.381   108.725 60.609  1.00 187.53 ? 148  ALA Y C   1 
ATOM   26924 O  O   . ALA D 2 148  ? -6.421   108.141 60.286  1.00 191.57 ? 148  ALA Y O   1 
ATOM   26925 C  CB  . ALA D 2 148  ? -5.369   111.088 61.459  1.00 186.43 ? 148  ALA Y CB  1 
ATOM   26926 N  N   . SER D 2 149  ? -4.413   108.153 61.317  1.00 184.69 ? 149  SER Y N   1 
ATOM   26927 C  CA  . SER D 2 149  ? -4.449   106.750 61.698  1.00 182.12 ? 149  SER Y CA  1 
ATOM   26928 C  C   . SER D 2 149  ? -3.589   106.567 62.946  1.00 175.93 ? 149  SER Y C   1 
ATOM   26929 O  O   . SER D 2 149  ? -2.469   107.090 63.004  1.00 172.16 ? 149  SER Y O   1 
ATOM   26930 C  CB  . SER D 2 149  ? -3.881   105.893 60.561  1.00 184.68 ? 149  SER Y CB  1 
ATOM   26931 O  OG  . SER D 2 149  ? -4.327   106.345 59.290  1.00 186.61 ? 149  SER Y OG  1 
ATOM   26932 N  N   . ILE D 2 150  ? -4.109   105.857 63.949  1.00 170.43 ? 150  ILE Y N   1 
ATOM   26933 C  CA  . ILE D 2 150  ? -3.295   105.462 65.101  1.00 159.77 ? 150  ILE Y CA  1 
ATOM   26934 C  C   . ILE D 2 150  ? -2.605   104.161 64.718  1.00 157.43 ? 150  ILE Y C   1 
ATOM   26935 O  O   . ILE D 2 150  ? -3.180   103.346 64.001  1.00 157.99 ? 150  ILE Y O   1 
ATOM   26936 C  CB  . ILE D 2 150  ? -4.139   105.221 66.367  1.00 150.35 ? 150  ILE Y CB  1 
ATOM   26937 C  CG1 . ILE D 2 150  ? -4.361   103.729 66.575  1.00 138.32 ? 150  ILE Y CG1 1 
ATOM   26938 C  CG2 . ILE D 2 150  ? -5.470   105.950 66.298  1.00 151.72 ? 150  ILE Y CG2 1 
ATOM   26939 C  CD1 . ILE D 2 150  ? -3.202   103.023 67.228  1.00 132.21 ? 150  ILE Y CD1 1 
ATOM   26940 N  N   . ASP D 2 151  ? -1.388   103.937 65.190  1.00 153.74 ? 151  ASP Y N   1 
ATOM   26941 C  CA  . ASP D 2 151  ? -0.669   102.749 64.746  1.00 153.41 ? 151  ASP Y CA  1 
ATOM   26942 C  C   . ASP D 2 151  ? 0.308    102.230 65.790  1.00 159.07 ? 151  ASP Y C   1 
ATOM   26943 O  O   . ASP D 2 151  ? 0.037    102.292 66.989  1.00 158.81 ? 151  ASP Y O   1 
ATOM   26944 C  CB  . ASP D 2 151  ? 0.054    103.021 63.418  1.00 146.47 ? 151  ASP Y CB  1 
ATOM   26945 C  CG  . ASP D 2 151  ? 0.150    101.784 62.532  1.00 141.46 ? 151  ASP Y CG  1 
ATOM   26946 O  OD1 . ASP D 2 151  ? -0.241   100.688 62.997  1.00 141.22 ? 151  ASP Y OD1 1 
ATOM   26947 O  OD2 . ASP D 2 151  ? 0.614    101.909 61.374  1.00 137.45 ? 151  ASP Y OD2 1 
ATOM   26948 N  N   . SER D 2 152  ? 1.441    101.710 65.323  1.00 166.31 ? 152  SER Y N   1 
ATOM   26949 C  CA  . SER D 2 152  ? 2.418    101.077 66.202  1.00 176.33 ? 152  SER Y CA  1 
ATOM   26950 C  C   . SER D 2 152  ? 3.796    100.934 65.552  1.00 185.34 ? 152  SER Y C   1 
ATOM   26951 O  O   . SER D 2 152  ? 3.920    100.845 64.330  1.00 185.14 ? 152  SER Y O   1 
ATOM   26952 C  CB  . SER D 2 152  ? 1.918    99.693  66.651  1.00 176.20 ? 152  SER Y CB  1 
ATOM   26953 O  OG  . SER D 2 152  ? 0.774    99.787  67.487  1.00 177.47 ? 152  SER Y OG  1 
ATOM   26954 N  N   . PHE D 2 153  ? 4.826    100.914 66.396  1.00 197.05 ? 153  PHE Y N   1 
ATOM   26955 C  CA  . PHE D 2 153  ? 6.195    100.599 65.984  1.00 207.87 ? 153  PHE Y CA  1 
ATOM   26956 C  C   . PHE D 2 153  ? 6.840    99.578  66.936  1.00 212.49 ? 153  PHE Y C   1 
ATOM   26957 O  O   . PHE D 2 153  ? 6.626    99.611  68.150  1.00 213.74 ? 153  PHE Y O   1 
ATOM   26958 C  CB  . PHE D 2 153  ? 7.068    101.862 65.899  1.00 214.43 ? 153  PHE Y CB  1 
ATOM   26959 C  CG  . PHE D 2 153  ? 8.485    101.590 65.448  1.00 221.23 ? 153  PHE Y CG  1 
ATOM   26960 C  CD1 . PHE D 2 153  ? 8.891    101.906 64.162  1.00 223.26 ? 153  PHE Y CD1 1 
ATOM   26961 C  CD2 . PHE D 2 153  ? 9.406    101.004 66.308  1.00 225.40 ? 153  PHE Y CD2 1 
ATOM   26962 C  CE1 . PHE D 2 153  ? 10.184   101.649 63.746  1.00 224.92 ? 153  PHE Y CE1 1 
ATOM   26963 C  CE2 . PHE D 2 153  ? 10.701   100.740 65.895  1.00 226.82 ? 153  PHE Y CE2 1 
ATOM   26964 C  CZ  . PHE D 2 153  ? 11.090   101.064 64.614  1.00 226.54 ? 153  PHE Y CZ  1 
ATOM   26965 N  N   . LEU D 2 154  ? 7.631    98.671  66.372  1.00 215.94 ? 154  LEU Y N   1 
ATOM   26966 C  CA  . LEU D 2 154  ? 8.275    97.629  67.162  1.00 218.14 ? 154  LEU Y CA  1 
ATOM   26967 C  C   . LEU D 2 154  ? 9.772    97.877  67.357  1.00 220.28 ? 154  LEU Y C   1 
ATOM   26968 O  O   . LEU D 2 154  ? 10.577   97.668  66.446  1.00 219.18 ? 154  LEU Y O   1 
ATOM   26969 C  CB  . LEU D 2 154  ? 8.012    96.262  66.529  1.00 216.48 ? 154  LEU Y CB  1 
ATOM   26970 C  CG  . LEU D 2 154  ? 6.513    95.997  66.354  1.00 214.68 ? 154  LEU Y CG  1 
ATOM   26971 C  CD1 . LEU D 2 154  ? 6.245    94.941  65.296  1.00 213.49 ? 154  LEU Y CD1 1 
ATOM   26972 C  CD2 . LEU D 2 154  ? 5.870    95.625  67.684  1.00 214.94 ? 154  LEU Y CD2 1 
ATOM   26973 N  N   . ILE D 2 155  ? 10.127   98.335  68.554  1.00 223.65 ? 155  ILE Y N   1 
ATOM   26974 C  CA  . ILE D 2 155  ? 11.521   98.502  68.943  1.00 225.28 ? 155  ILE Y CA  1 
ATOM   26975 C  C   . ILE D 2 155  ? 12.059   97.189  69.493  1.00 230.87 ? 155  ILE Y C   1 
ATOM   26976 O  O   . ILE D 2 155  ? 11.593   96.696  70.522  1.00 230.81 ? 155  ILE Y O   1 
ATOM   26977 C  CB  . ILE D 2 155  ? 11.666   99.572  70.020  1.00 224.80 ? 155  ILE Y CB  1 
ATOM   26978 C  CG1 . ILE D 2 155  ? 10.718   100.732 69.732  1.00 221.78 ? 155  ILE Y CG1 1 
ATOM   26979 C  CG2 . ILE D 2 155  ? 13.111   100.039 70.122  1.00 224.77 ? 155  ILE Y CG2 1 
ATOM   26980 C  CD1 . ILE D 2 155  ? 10.816   101.838 70.736  1.00 222.16 ? 155  ILE Y CD1 1 
ATOM   26981 N  N   . GLN D 2 156  ? 13.048   96.630  68.807  1.00 235.76 ? 156  GLN Y N   1 
ATOM   26982 C  CA  . GLN D 2 156  ? 13.540   95.298  69.127  1.00 242.17 ? 156  GLN Y CA  1 
ATOM   26983 C  C   . GLN D 2 156  ? 14.761   95.296  70.044  1.00 247.54 ? 156  GLN Y C   1 
ATOM   26984 O  O   . GLN D 2 156  ? 15.500   94.313  70.093  1.00 248.19 ? 156  GLN Y O   1 
ATOM   26985 C  CB  . GLN D 2 156  ? 13.836   94.525  67.838  1.00 243.88 ? 156  GLN Y CB  1 
ATOM   26986 C  CG  . GLN D 2 156  ? 14.165   93.060  68.061  1.00 246.26 ? 156  GLN Y CG  1 
ATOM   26987 C  CD  . GLN D 2 156  ? 13.334   92.447  69.171  1.00 246.80 ? 156  GLN Y CD  1 
ATOM   26988 O  OE1 . GLN D 2 156  ? 12.103   92.487  69.136  1.00 246.29 ? 156  GLN Y OE1 1 
ATOM   26989 N  NE2 . GLN D 2 156  ? 14.005   91.876  70.167  1.00 248.27 ? 156  GLN Y NE2 1 
ATOM   26990 N  N   . LYS D 2 157  ? 14.968   96.383  70.782  1.00 251.43 ? 157  LYS Y N   1 
ATOM   26991 C  CA  . LYS D 2 157  ? 16.148   96.483  71.645  1.00 256.70 ? 157  LYS Y CA  1 
ATOM   26992 C  C   . LYS D 2 157  ? 15.936   97.310  72.921  1.00 259.63 ? 157  LYS Y C   1 
ATOM   26993 O  O   . LYS D 2 157  ? 14.858   97.854  73.155  1.00 259.37 ? 157  LYS Y O   1 
ATOM   26994 C  CB  . LYS D 2 157  ? 17.348   97.017  70.851  1.00 257.37 ? 157  LYS Y CB  1 
ATOM   26995 C  CG  . LYS D 2 157  ? 17.832   96.091  69.726  1.00 257.79 ? 157  LYS Y CG  1 
ATOM   26996 C  CD  . LYS D 2 157  ? 18.388   94.773  70.268  1.00 259.65 ? 157  LYS Y CD  1 
ATOM   26997 C  CE  . LYS D 2 157  ? 18.740   93.804  69.149  1.00 259.71 ? 157  LYS Y CE  1 
ATOM   26998 N  NZ  . LYS D 2 157  ? 19.237   92.509  69.682  1.00 261.61 ? 157  LYS Y NZ  1 
ATOM   26999 N  N   . GLU D 2 158  ? 16.977   97.368  73.748  1.00 263.20 ? 158  GLU Y N   1 
ATOM   27000 C  CA  . GLU D 2 158  ? 16.953   98.114  75.002  1.00 266.74 ? 158  GLU Y CA  1 
ATOM   27001 C  C   . GLU D 2 158  ? 17.409   99.548  74.768  1.00 265.04 ? 158  GLU Y C   1 
ATOM   27002 O  O   . GLU D 2 158  ? 16.801   100.493 75.270  1.00 265.86 ? 158  GLU Y O   1 
ATOM   27003 C  CB  . GLU D 2 158  ? 17.850   97.431  76.039  1.00 271.97 ? 158  GLU Y CB  1 
ATOM   27004 C  CG  . GLU D 2 158  ? 18.159   98.262  77.274  1.00 276.75 ? 158  GLU Y CG  1 
ATOM   27005 C  CD  . GLU D 2 158  ? 16.940   98.520  78.140  1.00 279.57 ? 158  GLU Y CD  1 
ATOM   27006 O  OE1 . GLU D 2 158  ? 15.868   97.940  77.867  1.00 279.69 ? 158  GLU Y OE1 1 
ATOM   27007 O  OE2 . GLU D 2 158  ? 17.059   99.309  79.101  1.00 281.95 ? 158  GLU Y OE2 1 
ATOM   27008 N  N   . GLU D 2 159  ? 18.485   99.697  74.000  1.00 262.98 ? 159  GLU Y N   1 
ATOM   27009 C  CA  . GLU D 2 159  ? 18.957   101.009 73.563  1.00 260.01 ? 159  GLU Y CA  1 
ATOM   27010 C  C   . GLU D 2 159  ? 18.979   101.010 72.047  1.00 254.39 ? 159  GLU Y C   1 
ATOM   27011 O  O   . GLU D 2 159  ? 19.383   100.026 71.425  1.00 254.24 ? 159  GLU Y O   1 
ATOM   27012 C  CB  . GLU D 2 159  ? 20.360   101.317 74.104  1.00 262.50 ? 159  GLU Y CB  1 
ATOM   27013 C  CG  . GLU D 2 159  ? 20.990   102.600 73.538  1.00 262.18 ? 159  GLU Y CG  1 
ATOM   27014 C  CD  . GLU D 2 159  ? 22.434   102.801 73.979  1.00 264.09 ? 159  GLU Y CD  1 
ATOM   27015 O  OE1 . GLU D 2 159  ? 23.227   103.366 73.197  1.00 264.31 ? 159  GLU Y OE1 1 
ATOM   27016 O  OE2 . GLU D 2 159  ? 22.779   102.387 75.105  1.00 265.26 ? 159  GLU Y OE2 1 
ATOM   27017 N  N   . ILE D 2 160  ? 18.551   102.113 71.447  1.00 250.01 ? 160  ILE Y N   1 
ATOM   27018 C  CA  . ILE D 2 160  ? 18.388   102.134 70.003  1.00 245.31 ? 160  ILE Y CA  1 
ATOM   27019 C  C   . ILE D 2 160  ? 18.898   103.428 69.367  1.00 243.78 ? 160  ILE Y C   1 
ATOM   27020 O  O   . ILE D 2 160  ? 18.598   104.534 69.826  1.00 243.03 ? 160  ILE Y O   1 
ATOM   27021 C  CB  . ILE D 2 160  ? 16.921   101.825 69.605  1.00 231.72 ? 160  ILE Y CB  1 
ATOM   27022 C  CG1 . ILE D 2 160  ? 16.765   101.787 68.087  1.00 228.25 ? 160  ILE Y CG1 1 
ATOM   27023 C  CG2 . ILE D 2 160  ? 15.957   102.813 70.257  1.00 231.73 ? 160  ILE Y CG2 1 
ATOM   27024 C  CD1 . ILE D 2 160  ? 15.407   101.320 67.647  1.00 226.11 ? 160  ILE Y CD1 1 
ATOM   27025 N  N   . SER D 2 161  ? 19.693   103.258 68.313  1.00 243.47 ? 161  SER Y N   1 
ATOM   27026 C  CA  . SER D 2 161  ? 20.323   104.364 67.603  1.00 242.86 ? 161  SER Y CA  1 
ATOM   27027 C  C   . SER D 2 161  ? 19.305   105.170 66.812  1.00 242.18 ? 161  SER Y C   1 
ATOM   27028 O  O   . SER D 2 161  ? 18.451   104.604 66.131  1.00 240.98 ? 161  SER Y O   1 
ATOM   27029 C  CB  . SER D 2 161  ? 21.404   103.830 66.659  1.00 243.34 ? 161  SER Y CB  1 
ATOM   27030 O  OG  . SER D 2 161  ? 20.891   102.803 65.819  1.00 241.70 ? 161  SER Y OG  1 
ATOM   27031 N  N   . LEU D 2 162  ? 19.409   106.493 66.896  1.00 242.14 ? 162  LEU Y N   1 
ATOM   27032 C  CA  . LEU D 2 162  ? 18.492   107.386 66.189  1.00 241.46 ? 162  LEU Y CA  1 
ATOM   27033 C  C   . LEU D 2 162  ? 18.573   107.211 64.671  1.00 239.52 ? 162  LEU Y C   1 
ATOM   27034 O  O   . LEU D 2 162  ? 17.626   107.526 63.951  1.00 237.41 ? 162  LEU Y O   1 
ATOM   27035 C  CB  . LEU D 2 162  ? 18.751   108.847 66.579  1.00 242.89 ? 162  LEU Y CB  1 
ATOM   27036 C  CG  . LEU D 2 162  ? 17.751   109.906 66.102  1.00 242.32 ? 162  LEU Y CG  1 
ATOM   27037 C  CD1 . LEU D 2 162  ? 16.333   109.539 66.514  1.00 241.44 ? 162  LEU Y CD1 1 
ATOM   27038 C  CD2 . LEU D 2 162  ? 18.128   111.288 66.631  1.00 243.85 ? 162  LEU Y CD2 1 
ATOM   27039 N  N   . LYS D 2 163  ? 19.705   106.717 64.184  1.00 240.68 ? 163  LYS Y N   1 
ATOM   27040 C  CA  . LYS D 2 163  ? 19.818   106.373 62.776  1.00 239.57 ? 163  LYS Y CA  1 
ATOM   27041 C  C   . LYS D 2 163  ? 18.848   105.246 62.481  1.00 239.79 ? 163  LYS Y C   1 
ATOM   27042 O  O   . LYS D 2 163  ? 17.977   105.371 61.621  1.00 240.52 ? 163  LYS Y O   1 
ATOM   27043 C  CB  . LYS D 2 163  ? 21.230   105.910 62.443  1.00 239.53 ? 163  LYS Y CB  1 
ATOM   27044 C  CG  . LYS D 2 163  ? 21.324   105.176 61.118  1.00 237.21 ? 163  LYS Y CG  1 
ATOM   27045 C  CD  . LYS D 2 163  ? 22.473   104.186 61.124  1.00 236.75 ? 163  LYS Y CD  1 
ATOM   27046 C  CE  . LYS D 2 163  ? 22.685   103.582 59.753  1.00 235.24 ? 163  LYS Y CE  1 
ATOM   27047 N  NZ  . LYS D 2 163  ? 23.035   104.631 58.761  1.00 234.68 ? 163  LYS Y NZ  1 
ATOM   27048 N  N   . GLU D 2 164  ? 19.005   104.144 63.209  1.00 239.55 ? 164  GLU Y N   1 
ATOM   27049 C  CA  . GLU D 2 164  ? 18.140   102.982 63.052  1.00 239.06 ? 164  GLU Y CA  1 
ATOM   27050 C  C   . GLU D 2 164  ? 16.694   103.319 63.387  1.00 231.25 ? 164  GLU Y C   1 
ATOM   27051 O  O   . GLU D 2 164  ? 15.769   102.777 62.790  1.00 227.67 ? 164  GLU Y O   1 
ATOM   27052 C  CB  . GLU D 2 164  ? 18.617   101.834 63.941  1.00 247.30 ? 164  GLU Y CB  1 
ATOM   27053 C  CG  . GLU D 2 164  ? 17.718   100.613 63.886  1.00 253.31 ? 164  GLU Y CG  1 
ATOM   27054 C  CD  . GLU D 2 164  ? 18.010   99.625  64.993  1.00 259.56 ? 164  GLU Y CD  1 
ATOM   27055 O  OE1 . GLU D 2 164  ? 18.944   99.878  65.788  1.00 262.80 ? 164  GLU Y OE1 1 
ATOM   27056 O  OE2 . GLU D 2 164  ? 17.300   98.598  65.067  1.00 261.06 ? 164  GLU Y OE2 1 
ATOM   27057 N  N   . LEU D 2 165  ? 16.506   104.208 64.354  1.00 227.56 ? 165  LEU Y N   1 
ATOM   27058 C  CA  . LEU D 2 165  ? 15.175   104.659 64.726  1.00 223.17 ? 165  LEU Y CA  1 
ATOM   27059 C  C   . LEU D 2 165  ? 14.544   105.373 63.537  1.00 221.80 ? 165  LEU Y C   1 
ATOM   27060 O  O   . LEU D 2 165  ? 13.364   105.200 63.244  1.00 221.26 ? 165  LEU Y O   1 
ATOM   27061 C  CB  . LEU D 2 165  ? 15.258   105.610 65.923  1.00 218.62 ? 165  LEU Y CB  1 
ATOM   27062 C  CG  . LEU D 2 165  ? 14.042   105.765 66.844  1.00 212.52 ? 165  LEU Y CG  1 
ATOM   27063 C  CD1 . LEU D 2 165  ? 13.945   104.587 67.797  1.00 211.11 ? 165  LEU Y CD1 1 
ATOM   27064 C  CD2 . LEU D 2 165  ? 14.107   107.066 67.632  1.00 210.94 ? 165  LEU Y CD2 1 
ATOM   27065 N  N   . ASP D 2 166  ? 15.351   106.169 62.845  1.00 223.08 ? 166  ASP Y N   1 
ATOM   27066 C  CA  . ASP D 2 166  ? 14.873   106.993 61.741  1.00 223.65 ? 166  ASP Y CA  1 
ATOM   27067 C  C   . ASP D 2 166  ? 14.683   106.182 60.466  1.00 224.22 ? 166  ASP Y C   1 
ATOM   27068 O  O   . ASP D 2 166  ? 13.811   106.487 59.656  1.00 223.42 ? 166  ASP Y O   1 
ATOM   27069 C  CB  . ASP D 2 166  ? 15.848   108.144 61.485  1.00 225.66 ? 166  ASP Y CB  1 
ATOM   27070 C  CG  . ASP D 2 166  ? 15.178   109.340 60.850  1.00 228.02 ? 166  ASP Y CG  1 
ATOM   27071 O  OD1 . ASP D 2 166  ? 13.937   109.315 60.710  1.00 228.45 ? 166  ASP Y OD1 1 
ATOM   27072 O  OD2 . ASP D 2 166  ? 15.886   110.308 60.503  1.00 229.56 ? 166  ASP Y OD2 1 
ATOM   27073 N  N   . PHE D 2 167  ? 15.506   105.152 60.294  1.00 227.41 ? 167  PHE Y N   1 
ATOM   27074 C  CA  . PHE D 2 167  ? 15.442   104.286 59.114  1.00 229.85 ? 167  PHE Y CA  1 
ATOM   27075 C  C   . PHE D 2 167  ? 14.157   103.443 59.077  1.00 226.29 ? 167  PHE Y C   1 
ATOM   27076 O  O   . PHE D 2 167  ? 13.540   103.294 58.018  1.00 227.07 ? 167  PHE Y O   1 
ATOM   27077 C  CB  . PHE D 2 167  ? 16.682   103.380 59.043  1.00 236.30 ? 167  PHE Y CB  1 
ATOM   27078 C  CG  . PHE D 2 167  ? 16.792   102.577 57.767  1.00 240.09 ? 167  PHE Y CG  1 
ATOM   27079 C  CD1 . PHE D 2 167  ? 16.354   101.261 57.715  1.00 241.51 ? 167  PHE Y CD1 1 
ATOM   27080 C  CD2 . PHE D 2 167  ? 17.349   103.133 56.627  1.00 242.19 ? 167  PHE Y CD2 1 
ATOM   27081 C  CE1 . PHE D 2 167  ? 16.458   100.517 56.547  1.00 242.64 ? 167  PHE Y CE1 1 
ATOM   27082 C  CE2 . PHE D 2 167  ? 17.457   102.396 55.456  1.00 243.47 ? 167  PHE Y CE2 1 
ATOM   27083 C  CZ  . PHE D 2 167  ? 17.010   101.087 55.418  1.00 243.62 ? 167  PHE Y CZ  1 
ATOM   27084 N  N   . LYS D 2 168  ? 13.761   102.895 60.229  1.00 220.31 ? 168  LYS Y N   1 
ATOM   27085 C  CA  . LYS D 2 168  ? 12.539   102.085 60.331  1.00 213.33 ? 168  LYS Y CA  1 
ATOM   27086 C  C   . LYS D 2 168  ? 11.265   102.952 60.432  1.00 208.07 ? 168  LYS Y C   1 
ATOM   27087 O  O   . LYS D 2 168  ? 10.196   102.544 59.959  1.00 206.29 ? 168  LYS Y O   1 
ATOM   27088 C  CB  . LYS D 2 168  ? 12.635   101.074 61.495  1.00 211.59 ? 168  LYS Y CB  1 
ATOM   27089 C  CG  . LYS D 2 168  ? 13.692   99.965  61.298  1.00 210.46 ? 168  LYS Y CG  1 
ATOM   27090 C  CD  . LYS D 2 168  ? 13.837   99.053  62.521  1.00 209.40 ? 168  LYS Y CD  1 
ATOM   27091 C  CE  . LYS D 2 168  ? 14.784   97.893  62.237  1.00 209.21 ? 168  LYS Y CE  1 
ATOM   27092 N  NZ  . LYS D 2 168  ? 14.814   96.896  63.340  1.00 209.50 ? 168  LYS Y NZ  1 
ATOM   27093 N  N   . ILE D 2 169  ? 11.398   104.140 61.035  1.00 204.62 ? 169  ILE Y N   1 
ATOM   27094 C  CA  . ILE D 2 169  ? 10.321   105.141 61.103  1.00 199.08 ? 169  ILE Y CA  1 
ATOM   27095 C  C   . ILE D 2 169  ? 9.910    105.656 59.723  1.00 199.51 ? 169  ILE Y C   1 
ATOM   27096 O  O   . ILE D 2 169  ? 8.765    106.056 59.508  1.00 200.43 ? 169  ILE Y O   1 
ATOM   27097 C  CB  . ILE D 2 169  ? 10.721   106.367 61.960  1.00 192.81 ? 169  ILE Y CB  1 
ATOM   27098 C  CG1 . ILE D 2 169  ? 10.685   106.028 63.451  1.00 188.46 ? 169  ILE Y CG1 1 
ATOM   27099 C  CG2 . ILE D 2 169  ? 9.807    107.545 61.665  1.00 190.38 ? 169  ILE Y CG2 1 
ATOM   27100 C  CD1 . ILE D 2 169  ? 9.482    105.230 63.865  1.00 186.34 ? 169  ILE Y CD1 1 
ATOM   27101 N  N   . ARG D 2 170  ? 10.861   105.656 58.797  1.00 199.74 ? 170  ARG Y N   1 
ATOM   27102 C  CA  . ARG D 2 170  ? 10.595   106.085 57.432  1.00 200.37 ? 170  ARG Y CA  1 
ATOM   27103 C  C   . ARG D 2 170  ? 10.367   104.905 56.470  1.00 198.23 ? 170  ARG Y C   1 
ATOM   27104 O  O   . ARG D 2 170  ? 9.591    105.018 55.522  1.00 197.24 ? 170  ARG Y O   1 
ATOM   27105 C  CB  . ARG D 2 170  ? 11.709   107.011 56.929  1.00 205.74 ? 170  ARG Y CB  1 
ATOM   27106 C  CG  . ARG D 2 170  ? 11.943   108.254 57.799  1.00 211.71 ? 170  ARG Y CG  1 
ATOM   27107 C  CD  . ARG D 2 170  ? 12.506   109.414 56.963  1.00 217.74 ? 170  ARG Y CD  1 
ATOM   27108 N  NE  . ARG D 2 170  ? 13.326   110.352 57.734  1.00 222.18 ? 170  ARG Y NE  1 
ATOM   27109 C  CZ  . ARG D 2 170  ? 13.900   111.441 57.224  1.00 224.65 ? 170  ARG Y CZ  1 
ATOM   27110 N  NH1 . ARG D 2 170  ? 13.741   111.738 55.940  1.00 225.60 ? 170  ARG Y NH1 1 
ATOM   27111 N  NH2 . ARG D 2 170  ? 14.632   112.237 57.995  1.00 225.38 ? 170  ARG Y NH2 1 
ATOM   27112 N  N   . GLN D 2 171  ? 11.036   103.779 56.717  1.00 197.36 ? 171  GLN Y N   1 
ATOM   27113 C  CA  . GLN D 2 171  ? 10.816   102.565 55.929  1.00 196.25 ? 171  GLN Y CA  1 
ATOM   27114 C  C   . GLN D 2 171  ? 9.342    102.196 55.972  1.00 195.36 ? 171  GLN Y C   1 
ATOM   27115 O  O   . GLN D 2 171  ? 8.765    101.760 54.970  1.00 193.50 ? 171  GLN Y O   1 
ATOM   27116 C  CB  . GLN D 2 171  ? 11.628   101.401 56.500  1.00 195.68 ? 171  GLN Y CB  1 
ATOM   27117 C  CG  . GLN D 2 171  ? 11.386   100.063 55.805  1.00 193.84 ? 171  GLN Y CG  1 
ATOM   27118 C  CD  . GLN D 2 171  ? 11.631   98.874  56.724  1.00 191.42 ? 171  GLN Y CD  1 
ATOM   27119 O  OE1 . GLN D 2 171  ? 11.227   98.885  57.889  1.00 190.30 ? 171  GLN Y OE1 1 
ATOM   27120 N  NE2 . GLN D 2 171  ? 12.288   97.843  56.201  1.00 190.97 ? 171  GLN Y NE2 1 
ATOM   27121 N  N   . GLN D 2 172  ? 8.750    102.380 57.153  1.00 194.82 ? 172  GLN Y N   1 
ATOM   27122 C  CA  . GLN D 2 172  ? 7.342    102.079 57.398  1.00 193.67 ? 172  GLN Y CA  1 
ATOM   27123 C  C   . GLN D 2 172  ? 6.377    103.042 56.688  1.00 195.67 ? 172  GLN Y C   1 
ATOM   27124 O  O   . GLN D 2 172  ? 5.379    102.613 56.091  1.00 195.83 ? 172  GLN Y O   1 
ATOM   27125 C  CB  . GLN D 2 172  ? 7.069    102.070 58.900  1.00 188.19 ? 172  GLN Y CB  1 
ATOM   27126 C  CG  . GLN D 2 172  ? 7.602    100.850 59.600  1.00 183.25 ? 172  GLN Y CG  1 
ATOM   27127 C  CD  . GLN D 2 172  ? 6.652    100.360 60.659  1.00 180.07 ? 172  GLN Y CD  1 
ATOM   27128 O  OE1 . GLN D 2 172  ? 6.165    101.133 61.482  1.00 179.08 ? 172  GLN Y OE1 1 
ATOM   27129 N  NE2 . GLN D 2 172  ? 6.365    99.069  60.637  1.00 178.90 ? 172  GLN Y NE2 1 
ATOM   27130 N  N   . LEU D 2 173  ? 6.680    104.337 56.763  1.00 196.85 ? 173  LEU Y N   1 
ATOM   27131 C  CA  . LEU D 2 173  ? 5.900    105.354 56.062  1.00 198.11 ? 173  LEU Y CA  1 
ATOM   27132 C  C   . LEU D 2 173  ? 5.949    105.144 54.540  1.00 198.92 ? 173  LEU Y C   1 
ATOM   27133 O  O   . LEU D 2 173  ? 4.943    105.329 53.847  1.00 199.84 ? 173  LEU Y O   1 
ATOM   27134 C  CB  . LEU D 2 173  ? 6.402    106.756 56.429  1.00 198.09 ? 173  LEU Y CB  1 
ATOM   27135 C  CG  . LEU D 2 173  ? 6.349    107.164 57.905  1.00 199.57 ? 173  LEU Y CG  1 
ATOM   27136 C  CD1 . LEU D 2 173  ? 7.116    108.457 58.165  1.00 200.24 ? 173  LEU Y CD1 1 
ATOM   27137 C  CD2 . LEU D 2 173  ? 4.910    107.298 58.369  1.00 200.30 ? 173  LEU Y CD2 1 
ATOM   27138 N  N   . VAL D 2 174  ? 7.123    104.749 54.040  1.00 197.88 ? 174  VAL Y N   1 
ATOM   27139 C  CA  . VAL D 2 174  ? 7.355    104.510 52.611  1.00 197.33 ? 174  VAL Y CA  1 
ATOM   27140 C  C   . VAL D 2 174  ? 6.517    103.363 52.059  1.00 195.82 ? 174  VAL Y C   1 
ATOM   27141 O  O   . VAL D 2 174  ? 6.136    103.370 50.888  1.00 197.06 ? 174  VAL Y O   1 
ATOM   27142 C  CB  . VAL D 2 174  ? 8.840    104.170 52.320  1.00 203.29 ? 174  VAL Y CB  1 
ATOM   27143 C  CG1 . VAL D 2 174  ? 9.019    103.777 50.865  1.00 204.30 ? 174  VAL Y CG1 1 
ATOM   27144 C  CG2 . VAL D 2 174  ? 9.737    105.342 52.655  1.00 203.03 ? 174  VAL Y CG2 1 
ATOM   27145 N  N   . ASN D 2 175  ? 6.242    102.374 52.906  1.00 195.08 ? 175  ASN Y N   1 
ATOM   27146 C  CA  . ASN D 2 175  ? 5.584    101.146 52.467  1.00 192.41 ? 175  ASN Y CA  1 
ATOM   27147 C  C   . ASN D 2 175  ? 4.131    101.020 52.898  1.00 189.73 ? 175  ASN Y C   1 
ATOM   27148 O  O   . ASN D 2 175  ? 3.430    100.092 52.477  1.00 190.11 ? 175  ASN Y O   1 
ATOM   27149 C  CB  . ASN D 2 175  ? 6.366    99.943  52.974  1.00 192.12 ? 175  ASN Y CB  1 
ATOM   27150 C  CG  . ASN D 2 175  ? 7.836    100.082 52.726  1.00 190.95 ? 175  ASN Y CG  1 
ATOM   27151 O  OD1 . ASN D 2 175  ? 8.656    99.490  53.423  1.00 190.89 ? 175  ASN Y OD1 1 
ATOM   27152 N  ND2 . ASN D 2 175  ? 8.187    100.887 51.732  1.00 190.35 ? 175  ASN Y ND2 1 
ATOM   27153 N  N   . ASN D 2 176  ? 3.678    101.947 53.740  1.00 186.10 ? 176  ASN Y N   1 
ATOM   27154 C  CA  . ASN D 2 176  ? 2.336    101.838 54.303  1.00 182.50 ? 176  ASN Y CA  1 
ATOM   27155 C  C   . ASN D 2 176  ? 1.553    103.152 54.430  1.00 178.87 ? 176  ASN Y C   1 
ATOM   27156 O  O   . ASN D 2 176  ? 0.344    103.128 54.682  1.00 177.65 ? 176  ASN Y O   1 
ATOM   27157 C  CB  . ASN D 2 176  ? 2.378    101.105 55.653  1.00 183.20 ? 176  ASN Y CB  1 
ATOM   27158 C  CG  . ASN D 2 176  ? 3.001    99.715  55.554  1.00 183.06 ? 176  ASN Y CG  1 
ATOM   27159 O  OD1 . ASN D 2 176  ? 2.301    98.698  55.589  1.00 183.19 ? 176  ASN Y OD1 1 
ATOM   27160 N  ND2 . ASN D 2 176  ? 4.325    99.671  55.431  1.00 182.27 ? 176  ASN Y ND2 1 
ATOM   27161 N  N   . TYR D 2 177  ? 2.220    104.290 54.241  1.00 175.60 ? 177  TYR Y N   1 
ATOM   27162 C  CA  . TYR D 2 177  ? 1.522    105.573 54.332  1.00 174.57 ? 177  TYR Y CA  1 
ATOM   27163 C  C   . TYR D 2 177  ? 1.721    106.470 53.123  1.00 179.00 ? 177  TYR Y C   1 
ATOM   27164 O  O   . TYR D 2 177  ? 1.462    107.671 53.182  1.00 180.37 ? 177  TYR Y O   1 
ATOM   27165 C  CB  . TYR D 2 177  ? 1.867    106.299 55.636  1.00 168.32 ? 177  TYR Y CB  1 
ATOM   27166 C  CG  . TYR D 2 177  ? 1.282    105.580 56.812  1.00 163.37 ? 177  TYR Y CG  1 
ATOM   27167 C  CD1 . TYR D 2 177  ? 2.009    104.597 57.476  1.00 160.90 ? 177  TYR Y CD1 1 
ATOM   27168 C  CD2 . TYR D 2 177  ? -0.020   105.829 57.223  1.00 161.95 ? 177  TYR Y CD2 1 
ATOM   27169 C  CE1 . TYR D 2 177  ? 1.466    103.895 58.546  1.00 159.37 ? 177  TYR Y CE1 1 
ATOM   27170 C  CE2 . TYR D 2 177  ? -0.575   105.137 58.293  1.00 161.15 ? 177  TYR Y CE2 1 
ATOM   27171 C  CZ  . TYR D 2 177  ? 0.176    104.167 58.951  1.00 159.18 ? 177  TYR Y CZ  1 
ATOM   27172 O  OH  . TYR D 2 177  ? -0.356   103.466 60.010  1.00 157.64 ? 177  TYR Y OH  1 
ATOM   27173 N  N   . GLY D 2 178  ? 2.161    105.870 52.024  1.00 181.63 ? 178  GLY Y N   1 
ATOM   27174 C  CA  . GLY D 2 178  ? 2.359    106.595 50.783  1.00 186.52 ? 178  GLY Y CA  1 
ATOM   27175 C  C   . GLY D 2 178  ? 3.439    107.661 50.863  1.00 191.01 ? 178  GLY Y C   1 
ATOM   27176 O  O   . GLY D 2 178  ? 3.266    108.767 50.350  1.00 190.55 ? 178  GLY Y O   1 
ATOM   27177 N  N   . LEU D 2 179  ? 4.552    107.335 51.510  1.00 196.67 ? 179  LEU Y N   1 
ATOM   27178 C  CA  . LEU D 2 179  ? 5.653    108.279 51.626  1.00 202.59 ? 179  LEU Y CA  1 
ATOM   27179 C  C   . LEU D 2 179  ? 6.610    108.188 50.443  1.00 209.42 ? 179  LEU Y C   1 
ATOM   27180 O  O   . LEU D 2 179  ? 6.851    107.105 49.906  1.00 209.03 ? 179  LEU Y O   1 
ATOM   27181 C  CB  . LEU D 2 179  ? 6.414    108.074 52.939  1.00 202.01 ? 179  LEU Y CB  1 
ATOM   27182 C  CG  . LEU D 2 179  ? 7.520    109.098 53.235  1.00 200.88 ? 179  LEU Y CG  1 
ATOM   27183 C  CD1 . LEU D 2 179  ? 6.961    110.519 53.225  1.00 201.12 ? 179  LEU Y CD1 1 
ATOM   27184 C  CD2 . LEU D 2 179  ? 8.225    108.799 54.554  1.00 199.20 ? 179  LEU Y CD2 1 
ATOM   27185 N  N   . TYR D 2 180  ? 7.152    109.341 50.056  1.00 216.05 ? 180  TYR Y N   1 
ATOM   27186 C  CA  . TYR D 2 180  ? 8.103    109.449 48.947  1.00 223.14 ? 180  TYR Y CA  1 
ATOM   27187 C  C   . TYR D 2 180  ? 7.541    108.947 47.620  1.00 228.94 ? 180  TYR Y C   1 
ATOM   27188 O  O   . TYR D 2 180  ? 8.254    108.347 46.821  1.00 230.47 ? 180  TYR Y O   1 
ATOM   27189 C  CB  . TYR D 2 180  ? 9.426    108.754 49.282  1.00 224.58 ? 180  TYR Y CB  1 
ATOM   27190 C  CG  . TYR D 2 180  ? 10.171   109.415 50.418  1.00 225.93 ? 180  TYR Y CG  1 
ATOM   27191 C  CD1 . TYR D 2 180  ? 10.182   110.800 50.551  1.00 227.06 ? 180  TYR Y CD1 1 
ATOM   27192 C  CD2 . TYR D 2 180  ? 10.867   108.661 51.354  1.00 226.41 ? 180  TYR Y CD2 1 
ATOM   27193 C  CE1 . TYR D 2 180  ? 10.858   111.414 51.589  1.00 227.11 ? 180  TYR Y CE1 1 
ATOM   27194 C  CE2 . TYR D 2 180  ? 11.551   109.266 52.395  1.00 226.41 ? 180  TYR Y CE2 1 
ATOM   27195 C  CZ  . TYR D 2 180  ? 11.543   110.641 52.508  1.00 226.65 ? 180  TYR Y CZ  1 
ATOM   27196 O  OH  . TYR D 2 180  ? 12.222   111.244 53.541  1.00 226.23 ? 180  TYR Y OH  1 
ATOM   27197 N  N   . LYS D 2 181  ? 6.259    109.217 47.390  1.00 232.78 ? 181  LYS Y N   1 
ATOM   27198 C  CA  . LYS D 2 181  ? 5.569    108.776 46.181  1.00 236.95 ? 181  LYS Y CA  1 
ATOM   27199 C  C   . LYS D 2 181  ? 4.492    109.794 45.801  1.00 236.85 ? 181  LYS Y C   1 
ATOM   27200 O  O   . LYS D 2 181  ? 3.347    109.692 46.244  1.00 236.69 ? 181  LYS Y O   1 
ATOM   27201 C  CB  . LYS D 2 181  ? 4.943    107.396 46.412  1.00 240.74 ? 181  LYS Y CB  1 
ATOM   27202 C  CG  . LYS D 2 181  ? 4.251    106.801 45.199  1.00 245.74 ? 181  LYS Y CG  1 
ATOM   27203 C  CD  . LYS D 2 181  ? 3.718    105.410 45.501  1.00 248.20 ? 181  LYS Y CD  1 
ATOM   27204 C  CE  . LYS D 2 181  ? 3.155    104.756 44.252  1.00 250.62 ? 181  LYS Y CE  1 
ATOM   27205 N  NZ  . LYS D 2 181  ? 2.664    103.384 44.530  1.00 251.00 ? 181  LYS Y NZ  1 
ATOM   27206 N  N   . GLY D 2 182  ? 4.864    110.770 44.975  1.00 236.74 ? 182  GLY Y N   1 
ATOM   27207 C  CA  . GLY D 2 182  ? 3.975    111.870 44.640  1.00 236.33 ? 182  GLY Y CA  1 
ATOM   27208 C  C   . GLY D 2 182  ? 4.194    113.098 45.509  1.00 233.50 ? 182  GLY Y C   1 
ATOM   27209 O  O   . GLY D 2 182  ? 5.328    113.484 45.787  1.00 231.39 ? 182  GLY Y O   1 
ATOM   27210 N  N   . THR D 2 183  ? 3.105    113.727 45.932  1.00 233.00 ? 183  THR Y N   1 
ATOM   27211 C  CA  . THR D 2 183  ? 3.212    114.900 46.789  1.00 232.57 ? 183  THR Y CA  1 
ATOM   27212 C  C   . THR D 2 183  ? 3.707    114.555 48.197  1.00 235.10 ? 183  THR Y C   1 
ATOM   27213 O  O   . THR D 2 183  ? 3.790    115.437 49.049  1.00 237.13 ? 183  THR Y O   1 
ATOM   27214 C  CB  . THR D 2 183  ? 1.877    115.675 46.884  1.00 227.68 ? 183  THR Y CB  1 
ATOM   27215 O  OG1 . THR D 2 183  ? 0.780    114.757 46.820  1.00 226.75 ? 183  THR Y OG1 1 
ATOM   27216 C  CG2 . THR D 2 183  ? 1.754    116.676 45.749  1.00 228.01 ? 183  THR Y CG2 1 
ATOM   27217 N  N   . SER D 2 184  ? 4.029    113.283 48.442  1.00 237.36 ? 184  SER Y N   1 
ATOM   27218 C  CA  . SER D 2 184  ? 4.498    112.840 49.767  1.00 238.31 ? 184  SER Y CA  1 
ATOM   27219 C  C   . SER D 2 184  ? 6.023    112.917 49.933  1.00 239.61 ? 184  SER Y C   1 
ATOM   27220 O  O   . SER D 2 184  ? 6.757    112.138 49.325  1.00 239.55 ? 184  SER Y O   1 
ATOM   27221 C  CB  . SER D 2 184  ? 4.016    111.414 50.073  1.00 237.77 ? 184  SER Y CB  1 
ATOM   27222 O  OG  . SER D 2 184  ? 2.611    111.357 50.261  1.00 238.56 ? 184  SER Y OG  1 
ATOM   27223 N  N   . LYS D 2 185  ? 6.490    113.842 50.773  1.00 241.49 ? 185  LYS Y N   1 
ATOM   27224 C  CA  . LYS D 2 185  ? 7.928    114.053 50.959  1.00 242.03 ? 185  LYS Y CA  1 
ATOM   27225 C  C   . LYS D 2 185  ? 8.293    115.044 52.075  1.00 238.84 ? 185  LYS Y C   1 
ATOM   27226 O  O   . LYS D 2 185  ? 9.424    115.032 52.556  1.00 238.65 ? 185  LYS Y O   1 
ATOM   27227 C  CB  . LYS D 2 185  ? 8.578    114.503 49.647  1.00 246.64 ? 185  LYS Y CB  1 
ATOM   27228 C  CG  . LYS D 2 185  ? 8.451    115.996 49.374  1.00 249.98 ? 185  LYS Y CG  1 
ATOM   27229 C  CD  . LYS D 2 185  ? 9.095    116.382 48.048  1.00 252.39 ? 185  LYS Y CD  1 
ATOM   27230 C  CE  . LYS D 2 185  ? 8.198    116.046 46.871  1.00 253.95 ? 185  LYS Y CE  1 
ATOM   27231 N  NZ  . LYS D 2 185  ? 8.899    116.246 45.576  1.00 255.27 ? 185  LYS Y NZ  1 
ATOM   27232 N  N   . TYR D 2 186  ? 7.357    115.908 52.466  1.00 235.76 ? 186  TYR Y N   1 
ATOM   27233 C  CA  . TYR D 2 186  ? 7.598    116.857 53.560  1.00 232.60 ? 186  TYR Y CA  1 
ATOM   27234 C  C   . TYR D 2 186  ? 6.852    116.496 54.849  1.00 229.67 ? 186  TYR Y C   1 
ATOM   27235 O  O   . TYR D 2 186  ? 5.687    116.098 54.802  1.00 228.04 ? 186  TYR Y O   1 
ATOM   27236 C  CB  . TYR D 2 186  ? 7.210    118.274 53.145  1.00 233.43 ? 186  TYR Y CB  1 
ATOM   27237 C  CG  . TYR D 2 186  ? 7.772    118.695 51.822  1.00 233.53 ? 186  TYR Y CG  1 
ATOM   27238 C  CD1 . TYR D 2 186  ? 6.937    119.110 50.800  1.00 233.96 ? 186  TYR Y CD1 1 
ATOM   27239 C  CD2 . TYR D 2 186  ? 9.137    118.672 51.588  1.00 233.25 ? 186  TYR Y CD2 1 
ATOM   27240 C  CE1 . TYR D 2 186  ? 7.444    119.500 49.583  1.00 234.80 ? 186  TYR Y CE1 1 
ATOM   27241 C  CE2 . TYR D 2 186  ? 9.656    119.058 50.371  1.00 234.10 ? 186  TYR Y CE2 1 
ATOM   27242 C  CZ  . TYR D 2 186  ? 8.804    119.472 49.369  1.00 234.53 ? 186  TYR Y CZ  1 
ATOM   27243 O  OH  . TYR D 2 186  ? 9.308    119.858 48.145  1.00 235.05 ? 186  TYR Y OH  1 
ATOM   27244 N  N   . GLY D 2 187  ? 7.514    116.656 55.997  1.00 226.96 ? 187  GLY Y N   1 
ATOM   27245 C  CA  . GLY D 2 187  ? 6.884    116.381 57.279  1.00 224.75 ? 187  GLY Y CA  1 
ATOM   27246 C  C   . GLY D 2 187  ? 7.836    116.368 58.457  1.00 220.52 ? 187  GLY Y C   1 
ATOM   27247 O  O   . GLY D 2 187  ? 9.034    116.588 58.301  1.00 220.24 ? 187  GLY Y O   1 
ATOM   27248 N  N   . LYS D 2 188  ? 7.296    116.085 59.639  1.00 220.27 ? 188  LYS Y N   1 
ATOM   27249 C  CA  . LYS D 2 188  ? 8.070    116.151 60.876  1.00 219.84 ? 188  LYS Y CA  1 
ATOM   27250 C  C   . LYS D 2 188  ? 7.675    115.057 61.883  1.00 219.67 ? 188  LYS Y C   1 
ATOM   27251 O  O   . LYS D 2 188  ? 6.524    114.995 62.322  1.00 220.88 ? 188  LYS Y O   1 
ATOM   27252 C  CB  . LYS D 2 188  ? 7.887    117.528 61.524  1.00 222.57 ? 188  LYS Y CB  1 
ATOM   27253 C  CG  . LYS D 2 188  ? 8.528    118.688 60.767  1.00 223.52 ? 188  LYS Y CG  1 
ATOM   27254 C  CD  . LYS D 2 188  ? 9.997    118.844 61.129  1.00 223.67 ? 188  LYS Y CD  1 
ATOM   27255 C  CE  . LYS D 2 188  ? 10.569   120.142 60.590  1.00 223.71 ? 188  LYS Y CE  1 
ATOM   27256 N  NZ  . LYS D 2 188  ? 10.487   120.206 59.111  1.00 222.60 ? 188  LYS Y NZ  1 
ATOM   27257 N  N   . ILE D 2 189  ? 8.634    114.208 62.256  1.00 216.87 ? 189  ILE Y N   1 
ATOM   27258 C  CA  . ILE D 2 189  ? 8.390    113.136 63.224  1.00 214.65 ? 189  ILE Y CA  1 
ATOM   27259 C  C   . ILE D 2 189  ? 8.645    113.597 64.653  1.00 216.17 ? 189  ILE Y C   1 
ATOM   27260 O  O   . ILE D 2 189  ? 9.792    113.826 65.030  1.00 215.72 ? 189  ILE Y O   1 
ATOM   27261 C  CB  . ILE D 2 189  ? 9.323    111.937 62.987  1.00 212.55 ? 189  ILE Y CB  1 
ATOM   27262 C  CG1 . ILE D 2 189  ? 9.579    111.723 61.494  1.00 211.17 ? 189  ILE Y CG1 1 
ATOM   27263 C  CG2 . ILE D 2 189  ? 8.757    110.690 63.645  1.00 212.20 ? 189  ILE Y CG2 1 
ATOM   27264 C  CD1 . ILE D 2 189  ? 10.662   110.703 61.207  1.00 210.19 ? 189  ILE Y CD1 1 
ATOM   27265 N  N   . ILE D 2 190  ? 7.593    113.718 65.456  1.00 217.19 ? 190  ILE Y N   1 
ATOM   27266 C  CA  . ILE D 2 190  ? 7.763    114.130 66.853  1.00 220.08 ? 190  ILE Y CA  1 
ATOM   27267 C  C   . ILE D 2 190  ? 7.822    112.943 67.833  1.00 221.21 ? 190  ILE Y C   1 
ATOM   27268 O  O   . ILE D 2 190  ? 6.796    112.479 68.339  1.00 221.49 ? 190  ILE Y O   1 
ATOM   27269 C  CB  . ILE D 2 190  ? 6.717    115.232 67.276  1.00 146.14 ? 190  ILE Y CB  1 
ATOM   27270 C  CG1 . ILE D 2 190  ? 6.210    115.019 68.718  1.00 146.57 ? 190  ILE Y CG1 1 
ATOM   27271 C  CG2 . ILE D 2 190  ? 5.582    115.325 66.241  1.00 145.86 ? 190  ILE Y CG2 1 
ATOM   27272 C  CD1 . ILE D 2 190  ? 5.048    115.917 69.134  1.00 147.33 ? 190  ILE Y CD1 1 
ATOM   27273 N  N   . ILE D 2 191  ? 9.035    112.446 68.083  1.00 223.27 ? 191  ILE Y N   1 
ATOM   27274 C  CA  . ILE D 2 191  ? 9.224    111.379 69.061  1.00 227.12 ? 191  ILE Y CA  1 
ATOM   27275 C  C   . ILE D 2 191  ? 8.988    111.951 70.440  1.00 232.24 ? 191  ILE Y C   1 
ATOM   27276 O  O   . ILE D 2 191  ? 9.585    112.959 70.801  1.00 235.37 ? 191  ILE Y O   1 
ATOM   27277 C  CB  . ILE D 2 191  ? 10.665   110.801 69.073  1.00 173.57 ? 191  ILE Y CB  1 
ATOM   27278 C  CG1 . ILE D 2 191  ? 11.277   110.770 67.676  1.00 168.45 ? 191  ILE Y CG1 1 
ATOM   27279 C  CG2 . ILE D 2 191  ? 10.684   109.410 69.714  1.00 175.94 ? 191  ILE Y CG2 1 
ATOM   27280 C  CD1 . ILE D 2 191  ? 12.630   110.090 67.630  1.00 164.84 ? 191  ILE Y CD1 1 
ATOM   27281 N  N   . ASN D 2 192  ? 8.122    111.318 71.217  1.00 235.74 ? 192  ASN Y N   1 
ATOM   27282 C  CA  . ASN D 2 192  ? 8.004    111.689 72.618  1.00 240.60 ? 192  ASN Y CA  1 
ATOM   27283 C  C   . ASN D 2 192  ? 9.002    110.897 73.473  1.00 244.57 ? 192  ASN Y C   1 
ATOM   27284 O  O   . ASN D 2 192  ? 9.340    109.756 73.154  1.00 243.19 ? 192  ASN Y O   1 
ATOM   27285 C  CB  . ASN D 2 192  ? 6.562    111.527 73.101  1.00 241.75 ? 192  ASN Y CB  1 
ATOM   27286 C  CG  . ASN D 2 192  ? 5.614    112.494 72.416  1.00 242.04 ? 192  ASN Y CG  1 
ATOM   27287 O  OD1 . ASN D 2 192  ? 5.878    113.694 72.345  1.00 242.66 ? 192  ASN Y OD1 1 
ATOM   27288 N  ND2 . ASN D 2 192  ? 4.505    111.975 71.906  1.00 241.97 ? 192  ASN Y ND2 1 
ATOM   27289 N  N   . LEU D 2 193  ? 9.484    111.514 74.546  1.00 250.31 ? 193  LEU Y N   1 
ATOM   27290 C  CA  . LEU D 2 193  ? 10.498   110.896 75.392  1.00 253.71 ? 193  LEU Y CA  1 
ATOM   27291 C  C   . LEU D 2 193  ? 10.205   111.183 76.857  1.00 259.59 ? 193  LEU Y C   1 
ATOM   27292 O  O   . LEU D 2 193  ? 10.559   110.404 77.745  1.00 261.16 ? 193  LEU Y O   1 
ATOM   27293 C  CB  . LEU D 2 193  ? 11.885   111.413 75.017  1.00 252.10 ? 193  LEU Y CB  1 
ATOM   27294 C  CG  . LEU D 2 193  ? 12.379   110.997 73.632  1.00 247.97 ? 193  LEU Y CG  1 
ATOM   27295 C  CD1 . LEU D 2 193  ? 13.661   111.727 73.272  1.00 247.00 ? 193  LEU Y CD1 1 
ATOM   27296 C  CD2 . LEU D 2 193  ? 12.578   109.490 73.575  1.00 246.46 ? 193  LEU Y CD2 1 
ATOM   27297 N  N   . LYS D 2 194  ? 9.553    112.314 77.095  1.00 262.82 ? 194  LYS Y N   1 
ATOM   27298 C  CA  . LYS D 2 194  ? 9.060    112.660 78.420  1.00 268.32 ? 194  LYS Y CA  1 
ATOM   27299 C  C   . LYS D 2 194  ? 8.090    113.829 78.323  1.00 269.22 ? 194  LYS Y C   1 
ATOM   27300 O  O   . LYS D 2 194  ? 7.931    114.427 77.255  1.00 265.80 ? 194  LYS Y O   1 
ATOM   27301 C  CB  . LYS D 2 194  ? 10.208   112.971 79.381  1.00 273.65 ? 194  LYS Y CB  1 
ATOM   27302 C  CG  . LYS D 2 194  ? 11.220   113.956 78.849  1.00 277.49 ? 194  LYS Y CG  1 
ATOM   27303 C  CD  . LYS D 2 194  ? 12.392   114.075 79.801  1.00 283.76 ? 194  LYS Y CD  1 
ATOM   27304 C  CE  . LYS D 2 194  ? 13.419   115.061 79.280  1.00 287.13 ? 194  LYS Y CE  1 
ATOM   27305 N  NZ  . LYS D 2 194  ? 12.853   116.432 79.158  1.00 289.84 ? 194  LYS Y NZ  1 
ATOM   27306 N  N   . ASP D 2 195  ? 7.447    114.144 79.443  1.00 273.20 ? 195  ASP Y N   1 
ATOM   27307 C  CA  . ASP D 2 195  ? 6.359    115.117 79.479  1.00 274.78 ? 195  ASP Y CA  1 
ATOM   27308 C  C   . ASP D 2 195  ? 6.651    116.377 78.672  1.00 280.63 ? 195  ASP Y C   1 
ATOM   27309 O  O   . ASP D 2 195  ? 5.730    117.063 78.226  1.00 283.35 ? 195  ASP Y O   1 
ATOM   27310 C  CB  . ASP D 2 195  ? 6.028    115.492 80.927  1.00 268.82 ? 195  ASP Y CB  1 
ATOM   27311 C  CG  . ASP D 2 195  ? 5.050    114.533 81.571  1.00 260.54 ? 195  ASP Y CG  1 
ATOM   27312 O  OD1 . ASP D 2 195  ? 3.945    114.349 81.024  1.00 256.55 ? 195  ASP Y OD1 1 
ATOM   27313 O  OD2 . ASP D 2 195  ? 5.382    113.972 82.632  1.00 258.81 ? 195  ASP Y OD2 1 
ATOM   27314 N  N   . GLU D 2 196  ? 7.929    116.667 78.461  1.00 284.20 ? 196  GLU Y N   1 
ATOM   27315 C  CA  . GLU D 2 196  ? 8.313    117.964 77.923  1.00 290.11 ? 196  GLU Y CA  1 
ATOM   27316 C  C   . GLU D 2 196  ? 9.418    117.909 76.873  1.00 282.79 ? 196  GLU Y C   1 
ATOM   27317 O  O   . GLU D 2 196  ? 10.000   118.938 76.537  1.00 283.35 ? 196  GLU Y O   1 
ATOM   27318 C  CB  . GLU D 2 196  ? 8.732    118.906 79.062  1.00 304.52 ? 196  GLU Y CB  1 
ATOM   27319 C  CG  . GLU D 2 196  ? 10.087   118.591 79.703  1.00 316.08 ? 196  GLU Y CG  1 
ATOM   27320 C  CD  . GLU D 2 196  ? 10.033   117.436 80.691  1.00 326.43 ? 196  GLU Y CD  1 
ATOM   27321 O  OE1 . GLU D 2 196  ? 8.953    116.830 80.855  1.00 329.94 ? 196  GLU Y OE1 1 
ATOM   27322 O  OE2 . GLU D 2 196  ? 11.077   117.136 81.310  1.00 330.34 ? 196  GLU Y OE2 1 
ATOM   27323 N  N   . ASN D 2 197  ? 9.707    116.727 76.340  1.00 275.59 ? 197  ASN Y N   1 
ATOM   27324 C  CA  . ASN D 2 197  ? 10.800   116.617 75.381  1.00 266.99 ? 197  ASN Y CA  1 
ATOM   27325 C  C   . ASN D 2 197  ? 10.387   115.918 74.099  1.00 256.19 ? 197  ASN Y C   1 
ATOM   27326 O  O   . ASN D 2 197  ? 9.474    115.095 74.095  1.00 254.76 ? 197  ASN Y O   1 
ATOM   27327 C  CB  . ASN D 2 197  ? 12.010   115.917 76.011  1.00 267.74 ? 197  ASN Y CB  1 
ATOM   27328 C  CG  . ASN D 2 197  ? 13.273   116.061 75.176  1.00 265.45 ? 197  ASN Y CG  1 
ATOM   27329 O  OD1 . ASN D 2 197  ? 13.328   115.618 74.029  1.00 262.97 ? 197  ASN Y OD1 1 
ATOM   27330 N  ND2 . ASN D 2 197  ? 14.302   116.672 75.757  1.00 266.09 ? 197  ASN Y ND2 1 
ATOM   27331 N  N   . LYS D 2 198  ? 11.065   116.267 73.010  1.00 247.10 ? 198  LYS Y N   1 
ATOM   27332 C  CA  . LYS D 2 198  ? 10.814   115.646 71.719  1.00 237.55 ? 198  LYS Y CA  1 
ATOM   27333 C  C   . LYS D 2 198  ? 11.976   115.829 70.738  1.00 234.38 ? 198  LYS Y C   1 
ATOM   27334 O  O   . LYS D 2 198  ? 12.550   116.913 70.638  1.00 235.49 ? 198  LYS Y O   1 
ATOM   27335 C  CB  . LYS D 2 198  ? 9.506    116.169 71.112  1.00 232.46 ? 198  LYS Y CB  1 
ATOM   27336 C  CG  . LYS D 2 198  ? 9.548    117.595 70.546  1.00 228.28 ? 198  LYS Y CG  1 
ATOM   27337 C  CD  . LYS D 2 198  ? 8.389    117.809 69.552  1.00 224.05 ? 198  LYS Y CD  1 
ATOM   27338 C  CE  . LYS D 2 198  ? 8.141    119.278 69.217  1.00 221.78 ? 198  LYS Y CE  1 
ATOM   27339 N  NZ  . LYS D 2 198  ? 6.960    119.453 68.316  1.00 219.48 ? 198  LYS Y NZ  1 
ATOM   27340 N  N   . VAL D 2 199  ? 12.317   114.752 70.029  1.00 230.53 ? 199  VAL Y N   1 
ATOM   27341 C  CA  . VAL D 2 199  ? 13.347   114.777 68.985  1.00 227.57 ? 199  VAL Y CA  1 
ATOM   27342 C  C   . VAL D 2 199  ? 12.754   114.674 67.577  1.00 223.52 ? 199  VAL Y C   1 
ATOM   27343 O  O   . VAL D 2 199  ? 12.281   113.610 67.174  1.00 223.14 ? 199  VAL Y O   1 
ATOM   27344 C  CB  . VAL D 2 199  ? 14.355   113.632 69.161  1.00 227.79 ? 199  VAL Y CB  1 
ATOM   27345 C  CG1 . VAL D 2 199  ? 15.471   113.748 68.128  1.00 227.56 ? 199  VAL Y CG1 1 
ATOM   27346 C  CG2 . VAL D 2 199  ? 14.914   113.634 70.575  1.00 229.74 ? 199  VAL Y CG2 1 
ATOM   27347 N  N   . GLU D 2 200  ? 12.803   115.776 66.829  1.00 220.26 ? 200  GLU Y N   1 
ATOM   27348 C  CA  . GLU D 2 200  ? 12.176   115.857 65.506  1.00 216.01 ? 200  GLU Y CA  1 
ATOM   27349 C  C   . GLU D 2 200  ? 13.099   115.429 64.363  1.00 213.05 ? 200  GLU Y C   1 
ATOM   27350 O  O   . GLU D 2 200  ? 14.323   115.440 64.503  1.00 212.29 ? 200  GLU Y O   1 
ATOM   27351 C  CB  . GLU D 2 200  ? 11.651   117.276 65.242  1.00 215.03 ? 200  GLU Y CB  1 
ATOM   27352 C  CG  . GLU D 2 200  ? 10.595   117.757 66.229  1.00 215.69 ? 200  GLU Y CG  1 
ATOM   27353 C  CD  . GLU D 2 200  ? 9.878    119.005 65.752  1.00 216.66 ? 200  GLU Y CD  1 
ATOM   27354 O  OE1 . GLU D 2 200  ? 10.177   119.473 64.632  1.00 216.31 ? 200  GLU Y OE1 1 
ATOM   27355 O  OE2 . GLU D 2 200  ? 9.013    119.514 66.494  1.00 218.17 ? 200  GLU Y OE2 1 
ATOM   27356 N  N   . ILE D 2 201  ? 12.502   115.062 63.231  1.00 212.01 ? 201  ILE Y N   1 
ATOM   27357 C  CA  . ILE D 2 201  ? 13.261   114.711 62.033  1.00 210.38 ? 201  ILE Y CA  1 
ATOM   27358 C  C   . ILE D 2 201  ? 12.549   115.181 60.778  1.00 213.62 ? 201  ILE Y C   1 
ATOM   27359 O  O   . ILE D 2 201  ? 11.566   114.571 60.357  1.00 213.48 ? 201  ILE Y O   1 
ATOM   27360 C  CB  . ILE D 2 201  ? 13.432   113.193 61.876  1.00 205.10 ? 201  ILE Y CB  1 
ATOM   27361 C  CG1 . ILE D 2 201  ? 13.829   112.543 63.198  1.00 202.05 ? 201  ILE Y CG1 1 
ATOM   27362 C  CG2 . ILE D 2 201  ? 14.452   112.898 60.792  1.00 203.48 ? 201  ILE Y CG2 1 
ATOM   27363 C  CD1 . ILE D 2 201  ? 13.855   111.033 63.143  1.00 199.44 ? 201  ILE Y CD1 1 
ATOM   27364 N  N   . ASP D 2 202  ? 13.048   116.253 60.169  1.00 218.01 ? 202  ASP Y N   1 
ATOM   27365 C  CA  . ASP D 2 202  ? 12.479   116.715 58.911  1.00 222.30 ? 202  ASP Y CA  1 
ATOM   27366 C  C   . ASP D 2 202  ? 12.534   115.544 57.948  1.00 225.68 ? 202  ASP Y C   1 
ATOM   27367 O  O   . ASP D 2 202  ? 13.465   114.737 57.991  1.00 224.17 ? 202  ASP Y O   1 
ATOM   27368 C  CB  . ASP D 2 202  ? 13.245   117.922 58.347  1.00 224.59 ? 202  ASP Y CB  1 
ATOM   27369 C  CG  . ASP D 2 202  ? 12.576   118.529 57.106  1.00 226.88 ? 202  ASP Y CG  1 
ATOM   27370 O  OD1 . ASP D 2 202  ? 13.231   119.337 56.411  1.00 227.70 ? 202  ASP Y OD1 1 
ATOM   27371 O  OD2 . ASP D 2 202  ? 11.400   118.205 56.824  1.00 227.55 ? 202  ASP Y OD2 1 
ATOM   27372 N  N   . LEU D 2 203  ? 11.516   115.438 57.105  1.00 230.57 ? 203  LEU Y N   1 
ATOM   27373 C  CA  . LEU D 2 203  ? 11.450   114.375 56.123  1.00 235.27 ? 203  LEU Y CA  1 
ATOM   27374 C  C   . LEU D 2 203  ? 11.916   114.880 54.766  1.00 243.79 ? 203  LEU Y C   1 
ATOM   27375 O  O   . LEU D 2 203  ? 12.106   114.098 53.835  1.00 243.93 ? 203  LEU Y O   1 
ATOM   27376 C  CB  . LEU D 2 203  ? 10.030   113.840 56.045  1.00 231.41 ? 203  LEU Y CB  1 
ATOM   27377 C  CG  . LEU D 2 203  ? 9.541    113.455 57.435  1.00 227.73 ? 203  LEU Y CG  1 
ATOM   27378 C  CD1 . LEU D 2 203  ? 8.073    113.082 57.418  1.00 227.09 ? 203  LEU Y CD1 1 
ATOM   27379 C  CD2 . LEU D 2 203  ? 10.382   112.311 57.954  1.00 226.25 ? 203  LEU Y CD2 1 
ATOM   27380 N  N   . GLY D 2 204  ? 12.104   116.193 54.667  1.00 252.30 ? 204  GLY Y N   1 
ATOM   27381 C  CA  . GLY D 2 204  ? 12.521   116.821 53.425  1.00 260.54 ? 204  GLY Y CA  1 
ATOM   27382 C  C   . GLY D 2 204  ? 13.956   116.535 53.013  1.00 268.66 ? 204  GLY Y C   1 
ATOM   27383 O  O   . GLY D 2 204  ? 14.358   116.844 51.889  1.00 270.08 ? 204  GLY Y O   1 
ATOM   27384 N  N   . ASP D 2 205  ? 14.728   115.944 53.920  1.00 274.95 ? 205  ASP Y N   1 
ATOM   27385 C  CA  . ASP D 2 205  ? 16.142   115.665 53.672  1.00 281.76 ? 205  ASP Y CA  1 
ATOM   27386 C  C   . ASP D 2 205  ? 16.705   114.746 54.753  1.00 282.23 ? 205  ASP Y C   1 
ATOM   27387 O  O   . ASP D 2 205  ? 16.258   114.771 55.901  1.00 282.28 ? 205  ASP Y O   1 
ATOM   27388 C  CB  . ASP D 2 205  ? 16.941   116.975 53.628  1.00 288.37 ? 205  ASP Y CB  1 
ATOM   27389 C  CG  . ASP D 2 205  ? 18.409   116.766 53.273  1.00 294.23 ? 205  ASP Y CG  1 
ATOM   27390 O  OD1 . ASP D 2 205  ? 18.746   115.706 52.700  1.00 295.70 ? 205  ASP Y OD1 1 
ATOM   27391 O  OD2 . ASP D 2 205  ? 19.223   117.674 53.560  1.00 296.84 ? 205  ASP Y OD2 1 
ATOM   27392 N  N   . LYS D 2 206  ? 17.683   113.929 54.379  1.00 281.59 ? 206  LYS Y N   1 
ATOM   27393 C  CA  . LYS D 2 206  ? 18.347   113.052 55.332  1.00 279.94 ? 206  LYS Y CA  1 
ATOM   27394 C  C   . LYS D 2 206  ? 19.724   113.596 55.699  1.00 278.64 ? 206  LYS Y C   1 
ATOM   27395 O  O   . LYS D 2 206  ? 20.703   112.857 55.698  1.00 280.36 ? 206  LYS Y O   1 
ATOM   27396 C  CB  . LYS D 2 206  ? 18.466   111.647 54.749  1.00 280.12 ? 206  LYS Y CB  1 
ATOM   27397 C  CG  . LYS D 2 206  ? 17.186   111.186 54.089  1.00 278.97 ? 206  LYS Y CG  1 
ATOM   27398 C  CD  . LYS D 2 206  ? 17.354   109.872 53.359  1.00 279.03 ? 206  LYS Y CD  1 
ATOM   27399 C  CE  . LYS D 2 206  ? 16.091   109.546 52.578  1.00 278.05 ? 206  LYS Y CE  1 
ATOM   27400 N  NZ  . LYS D 2 206  ? 16.084   108.170 52.008  1.00 278.29 ? 206  LYS Y NZ  1 
ATOM   27401 N  N   . LEU D 2 207  ? 19.791   114.890 56.008  1.00 274.83 ? 207  LEU Y N   1 
ATOM   27402 C  CA  . LEU D 2 207  ? 21.062   115.576 56.267  1.00 272.11 ? 207  LEU Y CA  1 
ATOM   27403 C  C   . LEU D 2 207  ? 21.570   115.426 57.710  1.00 268.25 ? 207  LEU Y C   1 
ATOM   27404 O  O   . LEU D 2 207  ? 22.488   116.140 58.124  1.00 269.58 ? 207  LEU Y O   1 
ATOM   27405 C  CB  . LEU D 2 207  ? 20.941   117.062 55.899  1.00 272.04 ? 207  LEU Y CB  1 
ATOM   27406 C  CG  . LEU D 2 207  ? 22.202   117.925 55.815  1.00 273.77 ? 207  LEU Y CG  1 
ATOM   27407 C  CD1 . LEU D 2 207  ? 23.134   117.408 54.735  1.00 275.03 ? 207  LEU Y CD1 1 
ATOM   27408 C  CD2 . LEU D 2 207  ? 21.832   119.372 55.552  1.00 273.76 ? 207  LEU Y CD2 1 
ATOM   27409 N  N   . GLN D 2 208  ? 20.979   114.501 58.467  1.00 262.92 ? 208  GLN Y N   1 
ATOM   27410 C  CA  . GLN D 2 208  ? 21.305   114.336 59.889  1.00 258.86 ? 208  GLN Y CA  1 
ATOM   27411 C  C   . GLN D 2 208  ? 22.398   113.296 60.161  1.00 257.09 ? 208  GLN Y C   1 
ATOM   27412 O  O   . GLN D 2 208  ? 22.212   112.376 60.953  1.00 255.63 ? 208  GLN Y O   1 
ATOM   27413 C  CB  . GLN D 2 208  ? 20.044   114.005 60.697  1.00 255.43 ? 208  GLN Y CB  1 
ATOM   27414 C  CG  . GLN D 2 208  ? 20.235   114.070 62.211  1.00 254.19 ? 208  GLN Y CG  1 
ATOM   27415 C  CD  . GLN D 2 208  ? 20.385   115.487 62.735  1.00 253.60 ? 208  GLN Y CD  1 
ATOM   27416 O  OE1 . GLN D 2 208  ? 21.451   115.874 63.216  1.00 254.21 ? 208  GLN Y OE1 1 
ATOM   27417 N  NE2 . GLN D 2 208  ? 19.315   116.267 62.647  1.00 252.72 ? 208  GLN Y NE2 1 
ATOM   27418 N  N   . PHE D 2 209  ? 23.540   113.455 59.507  1.00 257.57 ? 209  PHE Y N   1 
ATOM   27419 C  CA  . PHE D 2 209  ? 24.655   112.534 59.679  1.00 257.74 ? 209  PHE Y CA  1 
ATOM   27420 C  C   . PHE D 2 209  ? 25.203   112.506 61.113  1.00 263.26 ? 209  PHE Y C   1 
ATOM   27421 O  O   . PHE D 2 209  ? 25.540   111.439 61.629  1.00 264.25 ? 209  PHE Y O   1 
ATOM   27422 C  CB  . PHE D 2 209  ? 25.775   112.880 58.689  1.00 254.82 ? 209  PHE Y CB  1 
ATOM   27423 C  CG  . PHE D 2 209  ? 26.090   114.355 58.614  1.00 250.93 ? 209  PHE Y CG  1 
ATOM   27424 C  CD1 . PHE D 2 209  ? 27.091   114.903 59.401  1.00 250.89 ? 209  PHE Y CD1 1 
ATOM   27425 C  CD2 . PHE D 2 209  ? 25.385   115.190 57.757  1.00 247.43 ? 209  PHE Y CD2 1 
ATOM   27426 C  CE1 . PHE D 2 209  ? 27.380   116.250 59.337  1.00 250.35 ? 209  PHE Y CE1 1 
ATOM   27427 C  CE2 . PHE D 2 209  ? 25.671   116.540 57.689  1.00 246.83 ? 209  PHE Y CE2 1 
ATOM   27428 C  CZ  . PHE D 2 209  ? 26.669   117.069 58.479  1.00 248.58 ? 209  PHE Y CZ  1 
ATOM   27429 N  N   . GLU D 2 210  ? 25.270   113.676 61.753  1.00 267.22 ? 210  GLU Y N   1 
ATOM   27430 C  CA  . GLU D 2 210  ? 25.993   113.838 63.026  1.00 272.91 ? 210  GLU Y CA  1 
ATOM   27431 C  C   . GLU D 2 210  ? 25.236   113.401 64.296  1.00 270.62 ? 210  GLU Y C   1 
ATOM   27432 O  O   . GLU D 2 210  ? 25.859   113.017 65.288  1.00 273.01 ? 210  GLU Y O   1 
ATOM   27433 C  CB  . GLU D 2 210  ? 26.529   115.276 63.181  1.00 279.40 ? 210  GLU Y CB  1 
ATOM   27434 C  CG  . GLU D 2 210  ? 25.932   116.080 64.337  1.00 284.22 ? 210  GLU Y CG  1 
ATOM   27435 C  CD  . GLU D 2 210  ? 24.583   116.693 64.012  1.00 286.37 ? 210  GLU Y CD  1 
ATOM   27436 O  OE1 . GLU D 2 210  ? 24.294   116.910 62.817  1.00 286.88 ? 210  GLU Y OE1 1 
ATOM   27437 O  OE2 . GLU D 2 210  ? 23.815   116.965 64.957  1.00 287.65 ? 210  GLU Y OE2 1 
ATOM   27438 N  N   . ARG D 2 211  ? 23.907   113.471 64.278  1.00 264.88 ? 211  ARG Y N   1 
ATOM   27439 C  CA  . ARG D 2 211  ? 23.122   112.993 65.416  1.00 259.15 ? 211  ARG Y CA  1 
ATOM   27440 C  C   . ARG D 2 211  ? 22.839   111.503 65.273  1.00 257.02 ? 211  ARG Y C   1 
ATOM   27441 O  O   . ARG D 2 211  ? 22.371   110.860 66.211  1.00 255.58 ? 211  ARG Y O   1 
ATOM   27442 C  CB  . ARG D 2 211  ? 21.821   113.787 65.575  1.00 252.05 ? 211  ARG Y CB  1 
ATOM   27443 C  CG  . ARG D 2 211  ? 21.044   113.458 66.845  1.00 246.15 ? 211  ARG Y CG  1 
ATOM   27444 C  CD  . ARG D 2 211  ? 20.028   114.540 67.172  1.00 240.79 ? 211  ARG Y CD  1 
ATOM   27445 N  NE  . ARG D 2 211  ? 19.158   114.843 66.040  1.00 235.45 ? 211  ARG Y NE  1 
ATOM   27446 C  CZ  . ARG D 2 211  ? 18.322   115.875 65.994  1.00 232.70 ? 211  ARG Y CZ  1 
ATOM   27447 N  NH1 . ARG D 2 211  ? 18.240   116.709 67.017  1.00 233.16 ? 211  ARG Y NH1 1 
ATOM   27448 N  NH2 . ARG D 2 211  ? 17.569   116.076 64.922  1.00 230.55 ? 211  ARG Y NH2 1 
ATOM   27449 N  N   . MET D 2 212  ? 23.137   110.964 64.091  1.00 257.57 ? 212  MET Y N   1 
ATOM   27450 C  CA  . MET D 2 212  ? 22.994   109.536 63.825  1.00 255.35 ? 212  MET Y CA  1 
ATOM   27451 C  C   . MET D 2 212  ? 23.856   108.733 64.786  1.00 255.26 ? 212  MET Y C   1 
ATOM   27452 O  O   . MET D 2 212  ? 23.875   107.502 64.754  1.00 256.78 ? 212  MET Y O   1 
ATOM   27453 C  CB  . MET D 2 212  ? 23.352   109.217 62.372  1.00 255.74 ? 212  MET Y CB  1 
ATOM   27454 C  CG  . MET D 2 212  ? 22.221   109.530 61.407  1.00 253.70 ? 212  MET Y CG  1 
ATOM   27455 S  SD  . MET D 2 212  ? 22.551   109.203 59.668  1.00 231.77 ? 212  MET Y SD  1 
ATOM   27456 C  CE  . MET D 2 212  ? 20.906   109.409 58.980  1.00 131.70 ? 212  MET Y CE  1 
ATOM   27457 N  N   . GLY D 2 213  ? 24.572   109.458 65.638  1.00 252.73 ? 213  GLY Y N   1 
ATOM   27458 C  CA  . GLY D 2 213  ? 25.347   108.864 66.707  1.00 251.95 ? 213  GLY Y CA  1 
ATOM   27459 C  C   . GLY D 2 213  ? 24.560   108.797 68.002  1.00 250.89 ? 213  GLY Y C   1 
ATOM   27460 O  O   . GLY D 2 213  ? 24.710   107.841 68.768  1.00 249.88 ? 213  GLY Y O   1 
ATOM   27461 N  N   . ASP D 2 214  ? 23.729   109.812 68.243  1.00 249.37 ? 214  ASP Y N   1 
ATOM   27462 C  CA  . ASP D 2 214  ? 22.842   109.850 69.407  1.00 247.66 ? 214  ASP Y CA  1 
ATOM   27463 C  C   . ASP D 2 214  ? 22.250   108.447 69.656  1.00 247.46 ? 214  ASP Y C   1 
ATOM   27464 O  O   . ASP D 2 214  ? 22.095   107.664 68.714  1.00 250.07 ? 214  ASP Y O   1 
ATOM   27465 C  CB  . ASP D 2 214  ? 21.737   110.899 69.177  1.00 240.13 ? 214  ASP Y CB  1 
ATOM   27466 C  CG  . ASP D 2 214  ? 21.153   111.452 70.472  1.00 233.49 ? 214  ASP Y CG  1 
ATOM   27467 O  OD1 . ASP D 2 214  ? 20.891   110.678 71.413  1.00 230.97 ? 214  ASP Y OD1 1 
ATOM   27468 O  OD2 . ASP D 2 214  ? 20.933   112.675 70.539  1.00 231.51 ? 214  ASP Y OD2 1 
ATOM   27469 N  N   . VAL D 2 215  ? 21.945   108.122 70.917  1.00 244.65 ? 215  VAL Y N   1 
ATOM   27470 C  CA  . VAL D 2 215  ? 21.330   106.830 71.269  1.00 239.59 ? 215  VAL Y CA  1 
ATOM   27471 C  C   . VAL D 2 215  ? 20.117   107.016 72.200  1.00 236.29 ? 215  VAL Y C   1 
ATOM   27472 O  O   . VAL D 2 215  ? 19.991   108.046 72.872  1.00 235.42 ? 215  VAL Y O   1 
ATOM   27473 C  CB  . VAL D 2 215  ? 22.345   105.831 71.902  1.00 278.57 ? 215  VAL Y CB  1 
ATOM   27474 C  CG1 . VAL D 2 215  ? 23.369   105.364 70.866  1.00 278.68 ? 215  VAL Y CG1 1 
ATOM   27475 C  CG2 . VAL D 2 215  ? 23.034   106.444 73.112  1.00 280.88 ? 215  VAL Y CG2 1 
ATOM   27476 N  N   . LEU D 2 216  ? 19.227   106.024 72.235  1.00 232.98 ? 216  LEU Y N   1 
ATOM   27477 C  CA  . LEU D 2 216  ? 17.951   106.176 72.939  1.00 228.59 ? 216  LEU Y CA  1 
ATOM   27478 C  C   . LEU D 2 216  ? 17.592   105.007 73.856  1.00 225.58 ? 216  LEU Y C   1 
ATOM   27479 O  O   . LEU D 2 216  ? 17.823   103.843 73.528  1.00 224.45 ? 216  LEU Y O   1 
ATOM   27480 C  CB  . LEU D 2 216  ? 16.806   106.406 71.943  1.00 224.57 ? 216  LEU Y CB  1 
ATOM   27481 C  CG  . LEU D 2 216  ? 16.793   107.719 71.160  1.00 220.12 ? 216  LEU Y CG  1 
ATOM   27482 C  CD1 . LEU D 2 216  ? 17.181   108.885 72.071  1.00 220.44 ? 216  LEU Y CD1 1 
ATOM   27483 C  CD2 . LEU D 2 216  ? 17.709   107.635 69.948  1.00 217.71 ? 216  LEU Y CD2 1 
ATOM   27484 N  N   . ASN D 2 217  ? 17.015   105.344 75.006  1.00 223.51 ? 217  ASN Y N   1 
ATOM   27485 C  CA  . ASN D 2 217  ? 16.503   104.358 75.948  1.00 222.64 ? 217  ASN Y CA  1 
ATOM   27486 C  C   . ASN D 2 217  ? 15.138   103.847 75.507  1.00 221.41 ? 217  ASN Y C   1 
ATOM   27487 O  O   . ASN D 2 217  ? 14.181   104.610 75.453  1.00 219.06 ? 217  ASN Y O   1 
ATOM   27488 C  CB  . ASN D 2 217  ? 16.375   104.980 77.339  1.00 225.12 ? 217  ASN Y CB  1 
ATOM   27489 C  CG  . ASN D 2 217  ? 17.576   105.823 77.714  1.00 227.90 ? 217  ASN Y CG  1 
ATOM   27490 O  OD1 . ASN D 2 217  ? 18.636   105.714 77.102  1.00 229.32 ? 217  ASN Y OD1 1 
ATOM   27491 N  ND2 . ASN D 2 217  ? 17.415   106.672 78.725  1.00 229.03 ? 217  ASN Y ND2 1 
ATOM   27492 N  N   . SER D 2 218  ? 15.042   102.557 75.213  1.00 223.43 ? 218  SER Y N   1 
ATOM   27493 C  CA  . SER D 2 218  ? 13.806   101.992 74.689  1.00 224.79 ? 218  SER Y CA  1 
ATOM   27494 C  C   . SER D 2 218  ? 12.584   102.302 75.551  1.00 229.67 ? 218  SER Y C   1 
ATOM   27495 O  O   . SER D 2 218  ? 11.606   102.861 75.065  1.00 227.41 ? 218  SER Y O   1 
ATOM   27496 C  CB  . SER D 2 218  ? 13.951   100.483 74.503  1.00 223.40 ? 218  SER Y CB  1 
ATOM   27497 O  OG  . SER D 2 218  ? 14.902   100.194 73.497  1.00 221.01 ? 218  SER Y OG  1 
ATOM   27498 N  N   . LYS D 2 219  ? 12.643   101.945 76.828  1.00 235.96 ? 219  LYS Y N   1 
ATOM   27499 C  CA  . LYS D 2 219  ? 11.492   102.089 77.718  1.00 241.25 ? 219  LYS Y CA  1 
ATOM   27500 C  C   . LYS D 2 219  ? 11.064   103.538 77.947  1.00 237.42 ? 219  LYS Y C   1 
ATOM   27501 O  O   . LYS D 2 219  ? 9.964    103.797 78.437  1.00 240.24 ? 219  LYS Y O   1 
ATOM   27502 C  CB  . LYS D 2 219  ? 11.773   101.423 79.064  1.00 255.74 ? 219  LYS Y CB  1 
ATOM   27503 C  CG  . LYS D 2 219  ? 12.016   99.931  78.979  1.00 268.93 ? 219  LYS Y CG  1 
ATOM   27504 C  CD  . LYS D 2 219  ? 12.222   99.348  80.363  1.00 276.54 ? 219  LYS Y CD  1 
ATOM   27505 C  CE  . LYS D 2 219  ? 13.489   99.889  80.997  1.00 282.85 ? 219  LYS Y CE  1 
ATOM   27506 N  NZ  . LYS D 2 219  ? 14.691   99.447  80.243  1.00 287.52 ? 219  LYS Y NZ  1 
ATOM   27507 N  N   . ASP D 2 220  ? 11.935   104.480 77.607  1.00 230.86 ? 220  ASP Y N   1 
ATOM   27508 C  CA  . ASP D 2 220  ? 11.646   105.892 77.837  1.00 225.42 ? 220  ASP Y CA  1 
ATOM   27509 C  C   . ASP D 2 220  ? 10.583   106.442 76.882  1.00 220.46 ? 220  ASP Y C   1 
ATOM   27510 O  O   . ASP D 2 220  ? 9.713    107.205 77.305  1.00 222.15 ? 220  ASP Y O   1 
ATOM   27511 C  CB  . ASP D 2 220  ? 12.926   106.736 77.748  1.00 224.39 ? 220  ASP Y CB  1 
ATOM   27512 C  CG  . ASP D 2 220  ? 13.758   106.693 79.025  1.00 226.71 ? 220  ASP Y CG  1 
ATOM   27513 O  OD1 . ASP D 2 220  ? 13.232   106.275 80.077  1.00 228.55 ? 220  ASP Y OD1 1 
ATOM   27514 O  OD2 . ASP D 2 220  ? 14.941   107.089 78.979  1.00 227.03 ? 220  ASP Y OD2 1 
ATOM   27515 N  N   . ILE D 2 221  ? 10.656   106.048 75.605  1.00 213.84 ? 221  ILE Y N   1 
ATOM   27516 C  CA  . ILE D 2 221  ? 9.790    106.597 74.544  1.00 206.47 ? 221  ILE Y CA  1 
ATOM   27517 C  C   . ILE D 2 221  ? 8.300    106.412 74.826  1.00 201.93 ? 221  ILE Y C   1 
ATOM   27518 O  O   . ILE D 2 221  ? 7.786    105.292 74.805  1.00 202.95 ? 221  ILE Y O   1 
ATOM   27519 C  CB  . ILE D 2 221  ? 10.083   105.984 73.140  1.00 164.87 ? 221  ILE Y CB  1 
ATOM   27520 C  CG1 . ILE D 2 221  ? 11.582   105.812 72.887  1.00 161.90 ? 221  ILE Y CG1 1 
ATOM   27521 C  CG2 . ILE D 2 221  ? 9.464    106.839 72.045  1.00 165.69 ? 221  ILE Y CG2 1 
ATOM   27522 C  CD1 . ILE D 2 221  ? 11.918   105.303 71.481  1.00 157.90 ? 221  ILE Y CD1 1 
ATOM   27523 N  N   . ARG D 2 222  ? 7.607    107.522 75.064  1.00 196.08 ? 222  ARG Y N   1 
ATOM   27524 C  CA  . ARG D 2 222  ? 6.188    107.490 75.409  1.00 194.70 ? 222  ARG Y CA  1 
ATOM   27525 C  C   . ARG D 2 222  ? 5.274    107.240 74.204  1.00 190.08 ? 222  ARG Y C   1 
ATOM   27526 O  O   . ARG D 2 222  ? 4.315    106.471 74.303  1.00 188.12 ? 222  ARG Y O   1 
ATOM   27527 C  CB  . ARG D 2 222  ? 5.791    108.783 76.115  1.00 197.69 ? 222  ARG Y CB  1 
ATOM   27528 C  CG  . ARG D 2 222  ? 4.315    108.918 76.401  1.00 203.02 ? 222  ARG Y CG  1 
ATOM   27529 C  CD  . ARG D 2 222  ? 4.057    110.263 77.030  1.00 208.55 ? 222  ARG Y CD  1 
ATOM   27530 N  NE  . ARG D 2 222  ? 4.978    110.486 78.140  1.00 212.56 ? 222  ARG Y NE  1 
ATOM   27531 C  CZ  . ARG D 2 222  ? 5.008    111.587 78.883  1.00 215.54 ? 222  ARG Y CZ  1 
ATOM   27532 N  NH1 . ARG D 2 222  ? 4.165    112.581 78.636  1.00 216.37 ? 222  ARG Y NH1 1 
ATOM   27533 N  NH2 . ARG D 2 222  ? 5.883    111.689 79.877  1.00 217.12 ? 222  ARG Y NH2 1 
ATOM   27534 N  N   . GLY D 2 223  ? 5.566    107.891 73.075  1.00 189.86 ? 223  GLY Y N   1 
ATOM   27535 C  CA  . GLY D 2 223  ? 4.812    107.675 71.851  1.00 184.90 ? 223  GLY Y CA  1 
ATOM   27536 C  C   . GLY D 2 223  ? 5.175    108.600 70.709  1.00 178.13 ? 223  GLY Y C   1 
ATOM   27537 O  O   . GLY D 2 223  ? 5.175    109.816 70.872  1.00 176.72 ? 223  GLY Y O   1 
ATOM   27538 N  N   . ILE D 2 224  ? 5.477    108.013 69.551  1.00 173.00 ? 224  ILE Y N   1 
ATOM   27539 C  CA  . ILE D 2 224  ? 5.709    108.771 68.309  1.00 173.61 ? 224  ILE Y CA  1 
ATOM   27540 C  C   . ILE D 2 224  ? 4.434    109.399 67.716  1.00 178.21 ? 224  ILE Y C   1 
ATOM   27541 O  O   . ILE D 2 224  ? 3.316    108.913 67.925  1.00 179.29 ? 224  ILE Y O   1 
ATOM   27542 C  CB  . ILE D 2 224  ? 6.347    107.908 67.174  1.00 155.83 ? 224  ILE Y CB  1 
ATOM   27543 C  CG1 . ILE D 2 224  ? 7.510    107.064 67.675  1.00 154.24 ? 224  ILE Y CG1 1 
ATOM   27544 C  CG2 . ILE D 2 224  ? 6.847    108.788 66.037  1.00 154.98 ? 224  ILE Y CG2 1 
ATOM   27545 C  CD1 . ILE D 2 224  ? 8.295    106.464 66.528  1.00 151.82 ? 224  ILE Y CD1 1 
ATOM   27546 N  N   . SER D 2 225  ? 4.627    110.464 66.942  1.00 183.21 ? 225  SER Y N   1 
ATOM   27547 C  CA  . SER D 2 225  ? 3.529    111.148 66.276  1.00 188.71 ? 225  SER Y CA  1 
ATOM   27548 C  C   . SER D 2 225  ? 4.058    111.881 65.029  1.00 191.65 ? 225  SER Y C   1 
ATOM   27549 O  O   . SER D 2 225  ? 4.843    112.825 65.136  1.00 193.69 ? 225  SER Y O   1 
ATOM   27550 C  CB  . SER D 2 225  ? 2.855    112.121 67.251  1.00 189.26 ? 225  SER Y CB  1 
ATOM   27551 O  OG  . SER D 2 225  ? 1.442    112.050 67.176  1.00 189.41 ? 225  SER Y OG  1 
ATOM   27552 N  N   . VAL D 2 226  ? 3.642    111.419 63.848  1.00 192.96 ? 226  VAL Y N   1 
ATOM   27553 C  CA  . VAL D 2 226  ? 4.044    112.025 62.572  1.00 193.66 ? 226  VAL Y CA  1 
ATOM   27554 C  C   . VAL D 2 226  ? 2.926    112.883 61.968  1.00 197.54 ? 226  VAL Y C   1 
ATOM   27555 O  O   . VAL D 2 226  ? 1.740    112.642 62.212  1.00 196.38 ? 226  VAL Y O   1 
ATOM   27556 C  CB  . VAL D 2 226  ? 4.477    110.952 61.529  1.00 228.28 ? 226  VAL Y CB  1 
ATOM   27557 C  CG1 . VAL D 2 226  ? 4.923    111.601 60.216  1.00 227.38 ? 226  VAL Y CG1 1 
ATOM   27558 C  CG2 . VAL D 2 226  ? 5.586    110.081 62.086  1.00 227.56 ? 226  VAL Y CG2 1 
ATOM   27559 N  N   . THR D 2 227  ? 3.316    113.879 61.177  1.00 201.34 ? 227  THR Y N   1 
ATOM   27560 C  CA  . THR D 2 227  ? 2.366    114.693 60.430  1.00 204.90 ? 227  THR Y CA  1 
ATOM   27561 C  C   . THR D 2 227  ? 2.925    114.929 59.031  1.00 209.37 ? 227  THR Y C   1 
ATOM   27562 O  O   . THR D 2 227  ? 3.986    115.536 58.876  1.00 210.12 ? 227  THR Y O   1 
ATOM   27563 C  CB  . THR D 2 227  ? 2.097    116.045 61.123  1.00 202.77 ? 227  THR Y CB  1 
ATOM   27564 O  OG1 . THR D 2 227  ? 1.721    115.824 62.486  1.00 201.91 ? 227  THR Y OG1 1 
ATOM   27565 C  CG2 . THR D 2 227  ? 0.978    116.799 60.421  1.00 202.36 ? 227  THR Y CG2 1 
ATOM   27566 N  N   . ILE D 2 228  ? 2.215    114.420 58.023  1.00 212.59 ? 228  ILE Y N   1 
ATOM   27567 C  CA  . ILE D 2 228  ? 2.626    114.547 56.622  1.00 215.49 ? 228  ILE Y CA  1 
ATOM   27568 C  C   . ILE D 2 228  ? 1.897    115.660 55.873  1.00 218.61 ? 228  ILE Y C   1 
ATOM   27569 O  O   . ILE D 2 228  ? 0.675    115.617 55.717  1.00 220.26 ? 228  ILE Y O   1 
ATOM   27570 C  CB  . ILE D 2 228  ? 2.437    113.225 55.845  1.00 216.52 ? 228  ILE Y CB  1 
ATOM   27571 C  CG1 . ILE D 2 228  ? 3.706    112.375 55.928  1.00 215.97 ? 228  ILE Y CG1 1 
ATOM   27572 C  CG2 . ILE D 2 228  ? 2.102    113.494 54.381  1.00 218.12 ? 228  ILE Y CG2 1 
ATOM   27573 C  CD1 . ILE D 2 228  ? 3.760    111.268 54.893  1.00 215.93 ? 228  ILE Y CD1 1 
ATOM   27574 N  N   . ASN D 2 229  ? 2.663    116.652 55.414  1.00 219.48 ? 229  ASN Y N   1 
ATOM   27575 C  CA  . ASN D 2 229  ? 2.148    117.708 54.539  1.00 220.40 ? 229  ASN Y CA  1 
ATOM   27576 C  C   . ASN D 2 229  ? 2.545    117.524 53.063  1.00 213.16 ? 229  ASN Y C   1 
ATOM   27577 O  O   . ASN D 2 229  ? 3.720    117.611 52.701  1.00 210.51 ? 229  ASN Y O   1 
ATOM   27578 C  CB  . ASN D 2 229  ? 2.492    119.123 55.067  1.00 226.74 ? 229  ASN Y CB  1 
ATOM   27579 C  CG  . ASN D 2 229  ? 3.955    119.272 55.517  1.00 229.47 ? 229  ASN Y CG  1 
ATOM   27580 O  OD1 . ASN D 2 229  ? 4.595    118.313 55.952  1.00 229.45 ? 229  ASN Y OD1 1 
ATOM   27581 N  ND2 . ASN D 2 229  ? 4.474    120.498 55.434  1.00 231.19 ? 229  ASN Y ND2 1 
ATOM   27582 N  N   . GLN D 2 230  ? 1.550    117.261 52.221  1.00 208.82 ? 230  GLN Y N   1 
ATOM   27583 C  CA  . GLN D 2 230  ? 1.779    116.988 50.804  1.00 203.12 ? 230  GLN Y CA  1 
ATOM   27584 C  C   . GLN D 2 230  ? 1.668    118.252 49.948  1.00 202.53 ? 230  GLN Y C   1 
ATOM   27585 O  O   . GLN D 2 230  ? 1.244    118.202 48.791  1.00 201.97 ? 230  GLN Y O   1 
ATOM   27586 C  CB  . GLN D 2 230  ? 0.809    115.909 50.305  1.00 199.40 ? 230  GLN Y CB  1 
ATOM   27587 C  CG  . GLN D 2 230  ? 0.670    114.709 51.252  1.00 194.44 ? 230  GLN Y CG  1 
ATOM   27588 C  CD  . GLN D 2 230  ? -0.190   113.587 50.685  1.00 191.16 ? 230  GLN Y CD  1 
ATOM   27589 O  OE1 . GLN D 2 230  ? -1.278   113.309 51.187  1.00 190.70 ? 230  GLN Y OE1 1 
ATOM   27590 N  NE2 . GLN D 2 230  ? 0.299    112.937 49.637  1.00 189.60 ? 230  GLN Y NE2 1 
HETATM 27591 CD CD  . CD  E 3 .    ? -30.281  52.834  41.178  0.50 137.22 ? 1677 CD  A CD  1 
HETATM 27592 C  C1  . NAG F 4 .    ? -41.656  3.791   27.363  1.00 305.92 ? 2001 NAG A C1  1 
HETATM 27593 C  C2  . NAG F 4 .    ? -43.121  3.856   27.798  1.00 307.18 ? 2001 NAG A C2  1 
HETATM 27594 C  C3  . NAG F 4 .    ? -43.907  2.564   27.653  1.00 306.22 ? 2001 NAG A C3  1 
HETATM 27595 C  C4  . NAG F 4 .    ? -43.605  1.883   26.332  1.00 305.69 ? 2001 NAG A C4  1 
HETATM 27596 C  C5  . NAG F 4 .    ? -42.098  1.718   26.215  1.00 306.36 ? 2001 NAG A C5  1 
HETATM 27597 C  C6  . NAG F 4 .    ? -41.732  0.993   24.927  1.00 306.45 ? 2001 NAG A C6  1 
HETATM 27598 C  C7  . NAG F 4 .    ? -44.320  4.922   29.563  1.00 310.95 ? 2001 NAG A C7  1 
HETATM 27599 C  C8  . NAG F 4 .    ? -44.716  4.909   31.021  1.00 310.77 ? 2001 NAG A C8  1 
HETATM 27600 N  N2  . NAG F 4 .    ? -43.235  4.242   29.187  1.00 309.12 ? 2001 NAG A N2  1 
HETATM 27601 O  O3  . NAG F 4 .    ? -45.277  2.878   27.734  1.00 305.67 ? 2001 NAG A O3  1 
HETATM 27602 O  O4  . NAG F 4 .    ? -44.228  0.613   26.274  1.00 304.23 ? 2001 NAG A O4  1 
HETATM 27603 O  O5  . NAG F 4 .    ? -41.459  2.974   26.226  1.00 306.66 ? 2001 NAG A O5  1 
HETATM 27604 O  O6  . NAG F 4 .    ? -42.334  1.634   23.822  1.00 306.30 ? 2001 NAG A O6  1 
HETATM 27605 O  O7  . NAG F 4 .    ? -44.997  5.541   28.738  1.00 312.24 ? 2001 NAG A O7  1 
HETATM 27606 C  C1  . NAG G 4 .    ? -45.538  0.616   25.884  1.00 303.45 ? 2002 NAG A C1  1 
HETATM 27607 C  C2  . NAG G 4 .    ? -45.734  -0.728  25.183  1.00 303.72 ? 2002 NAG A C2  1 
HETATM 27608 C  C3  . NAG G 4 .    ? -47.089  -0.761  24.493  1.00 304.30 ? 2002 NAG A C3  1 
HETATM 27609 C  C4  . NAG G 4 .    ? -48.199  -0.432  25.468  1.00 303.75 ? 2002 NAG A C4  1 
HETATM 27610 C  C5  . NAG G 4 .    ? -47.930  0.903   26.155  1.00 303.41 ? 2002 NAG A C5  1 
HETATM 27611 C  C6  . NAG G 4 .    ? -48.987  1.209   27.221  1.00 303.04 ? 2002 NAG A C6  1 
HETATM 27612 C  C7  . NAG G 4 .    ? -43.926  -2.094  24.215  1.00 304.84 ? 2002 NAG A C7  1 
HETATM 27613 C  C8  . NAG G 4 .    ? -44.007  -2.961  22.987  1.00 304.06 ? 2002 NAG A C8  1 
HETATM 27614 N  N2  . NAG G 4 .    ? -44.669  -0.981  24.221  1.00 304.77 ? 2002 NAG A N2  1 
HETATM 27615 O  O3  . NAG G 4 .    ? -47.346  -2.034  23.952  1.00 305.64 ? 2002 NAG A O3  1 
HETATM 27616 O  O4  . NAG G 4 .    ? -49.400  -0.381  24.736  1.00 304.27 ? 2002 NAG A O4  1 
HETATM 27617 O  O5  . NAG G 4 .    ? -46.633  0.936   26.735  1.00 303.28 ? 2002 NAG A O5  1 
HETATM 27618 O  O6  . NAG G 4 .    ? -49.085  0.161   28.160  1.00 302.28 ? 2002 NAG A O6  1 
HETATM 27619 O  O7  . NAG G 4 .    ? -43.196  -2.413  25.157  1.00 305.13 ? 2002 NAG A O7  1 
HETATM 27620 CD CD  . CD  H 3 .    ? -77.616  57.982  37.954  1.00 261.05 ? 1678 CD  A CD  1 
HETATM 27621 CD CD  . CD  I 3 .    ? -15.871  43.742  23.322  1.00 270.94 ? 1679 CD  A CD  1 
HETATM 27622 CD CD  . CD  J 3 .    ? -31.167  41.062  15.090  1.00 241.23 ? 1680 CD  A CD  1 
HETATM 27623 CD CD  . CD  K 3 .    ? -27.838  19.395  40.970  1.00 263.81 ? 1681 CD  A CD  1 
HETATM 27624 C  C1  . NAG L 4 .    ? -3.991   55.294  20.733  1.00 313.73 ? 1682 NAG A C1  1 
HETATM 27625 C  C2  . NAG L 4 .    ? -3.666   55.174  22.235  1.00 303.70 ? 1682 NAG A C2  1 
HETATM 27626 C  C3  . NAG L 4 .    ? -3.139   56.451  22.891  1.00 301.33 ? 1682 NAG A C3  1 
HETATM 27627 C  C4  . NAG L 4 .    ? -2.331   57.324  21.950  1.00 303.01 ? 1682 NAG A C4  1 
HETATM 27628 C  C5  . NAG L 4 .    ? -3.098   57.494  20.658  1.00 306.28 ? 1682 NAG A C5  1 
HETATM 27629 C  C6  . NAG L 4 .    ? -2.398   58.482  19.737  1.00 301.37 ? 1682 NAG A C6  1 
HETATM 27630 C  C7  . NAG L 4 .    ? -4.809   53.935  24.039  1.00 291.63 ? 1682 NAG A C7  1 
HETATM 27631 C  C8  . NAG L 4 .    ? -5.816   54.197  25.122  1.00 292.11 ? 1682 NAG A C8  1 
HETATM 27632 N  N2  . NAG L 4 .    ? -4.847   54.744  22.976  1.00 300.33 ? 1682 NAG A N2  1 
HETATM 27633 O  O3  . NAG L 4 .    ? -2.319   56.104  23.981  1.00 295.24 ? 1682 NAG A O3  1 
HETATM 27634 O  O4  . NAG L 4 .    ? -2.115   58.586  22.537  1.00 304.75 ? 1682 NAG A O4  1 
HETATM 27635 O  O5  . NAG L 4 .    ? -3.185   56.232  20.042  1.00 311.16 ? 1682 NAG A O5  1 
HETATM 27636 O  O6  . NAG L 4 .    ? -1.183   57.920  19.308  1.00 291.46 ? 1682 NAG A O6  1 
HETATM 27637 O  O7  . NAG L 4 .    ? -4.011   53.008  24.160  1.00 285.61 ? 1682 NAG A O7  1 
HETATM 27638 C  C1  . NAG M 4 .    ? 17.564   37.878  54.712  1.00 323.00 ? 2001 NAG B C1  1 
HETATM 27639 C  C2  . NAG M 4 .    ? 18.190   39.263  54.555  1.00 320.33 ? 2001 NAG B C2  1 
HETATM 27640 C  C3  . NAG M 4 .    ? 19.709   39.291  54.652  1.00 318.94 ? 2001 NAG B C3  1 
HETATM 27641 C  C4  . NAG M 4 .    ? 20.198   38.409  55.788  1.00 317.84 ? 2001 NAG B C4  1 
HETATM 27642 C  C5  . NAG M 4 .    ? 19.641   37.026  55.495  1.00 319.21 ? 2001 NAG B C5  1 
HETATM 27643 C  C6  . NAG M 4 .    ? 20.220   35.948  56.396  1.00 317.43 ? 2001 NAG B C6  1 
HETATM 27644 C  C7  . NAG M 4 .    ? 17.778   41.163  53.108  1.00 319.27 ? 2001 NAG B C7  1 
HETATM 27645 C  C8  . NAG M 4 .    ? 17.760   41.683  51.692  1.00 318.68 ? 2001 NAG B C8  1 
HETATM 27646 N  N2  . NAG M 4 .    ? 17.817   39.838  53.282  1.00 320.22 ? 2001 NAG B N2  1 
HETATM 27647 O  O3  . NAG M 4 .    ? 20.099   40.626  54.856  1.00 318.21 ? 2001 NAG B O3  1 
HETATM 27648 O  O4  . NAG M 4 .    ? 21.613   38.372  55.860  1.00 315.39 ? 2001 NAG B O4  1 
HETATM 27649 O  O5  . NAG M 4 .    ? 18.242   37.068  55.654  1.00 321.12 ? 2001 NAG B O5  1 
HETATM 27650 O  O6  . NAG M 4 .    ? 19.676   36.114  57.681  1.00 315.93 ? 2001 NAG B O6  1 
HETATM 27651 O  O7  . NAG M 4 .    ? 17.762   41.958  54.051  1.00 318.93 ? 2001 NAG B O7  1 
HETATM 27652 C  C1  . NAG N 4 .    ? 22.236   39.521  56.262  1.00 313.28 ? 2002 NAG B C1  1 
HETATM 27653 C  C2  . NAG N 4 .    ? 23.366   39.158  57.213  1.00 312.59 ? 2002 NAG B C2  1 
HETATM 27654 C  C3  . NAG N 4 .    ? 23.692   40.361  58.083  1.00 312.29 ? 2002 NAG B C3  1 
HETATM 27655 C  C4  . NAG N 4 .    ? 24.051   41.561  57.228  1.00 311.68 ? 2002 NAG B C4  1 
HETATM 27656 C  C5  . NAG N 4 .    ? 22.979   41.823  56.172  1.00 311.77 ? 2002 NAG B C5  1 
HETATM 27657 C  C6  . NAG N 4 .    ? 23.406   42.905  55.171  1.00 310.85 ? 2002 NAG B C6  1 
HETATM 27658 C  C7  . NAG N 4 .    ? 23.625   36.854  57.995  1.00 314.18 ? 2002 NAG B C7  1 
HETATM 27659 C  C8  . NAG N 4 .    ? 24.680   36.623  59.041  1.00 313.62 ? 2002 NAG B C8  1 
HETATM 27660 N  N2  . NAG N 4 .    ? 22.987   38.024  58.037  1.00 313.74 ? 2002 NAG B N2  1 
HETATM 27661 O  O3  . NAG N 4 .    ? 24.761   40.075  58.959  1.00 312.82 ? 2002 NAG B O3  1 
HETATM 27662 O  O4  . NAG N 4 .    ? 24.170   42.668  58.090  1.00 311.83 ? 2002 NAG B O4  1 
HETATM 27663 O  O5  . NAG N 4 .    ? 22.610   40.641  55.472  1.00 312.56 ? 2002 NAG B O5  1 
HETATM 27664 O  O6  . NAG N 4 .    ? 24.575   42.540  54.471  1.00 309.84 ? 2002 NAG B O6  1 
HETATM 27665 O  O7  . NAG N 4 .    ? 23.369   35.992  57.154  1.00 314.62 ? 2002 NAG B O7  1 
HETATM 27666 CD CD  . CD  O 3 .    ? -11.356  96.267  44.145  1.00 255.58 ? 1677 CD  B CD  1 
HETATM 27667 CD CD  . CD  P 3 .    ? -30.063  35.670  58.887  1.00 271.68 ? 1678 CD  B CD  1 
HETATM 27668 CD CD  . CD  Q 3 .    ? -20.027  47.513  67.036  1.00 240.45 ? 1679 CD  B CD  1 
HETATM 27669 CD CD  . CD  R 3 .    ? -2.865   33.842  41.063  1.00 252.75 ? 1680 CD  B CD  1 
HETATM 27670 C  C1  . NAG S 4 .    ? -45.881  31.188  61.350  1.00 333.76 ? 1681 NAG B C1  1 
HETATM 27671 C  C2  . NAG S 4 .    ? -45.936  30.895  59.836  1.00 310.18 ? 1681 NAG B C2  1 
HETATM 27672 C  C3  . NAG S 4 .    ? -47.307  31.060  59.172  1.00 288.35 ? 1681 NAG B C3  1 
HETATM 27673 C  C4  . NAG S 4 .    ? -48.476  30.849  60.116  1.00 283.66 ? 1681 NAG B C4  1 
HETATM 27674 C  C5  . NAG S 4 .    ? -48.222  31.611  61.395  1.00 303.63 ? 1681 NAG B C5  1 
HETATM 27675 C  C6  . NAG S 4 .    ? -49.423  31.539  62.323  1.00 294.07 ? 1681 NAG B C6  1 
HETATM 27676 C  C7  . NAG S 4 .    ? -44.406  31.410  57.961  1.00 298.69 ? 1681 NAG B C7  1 
HETATM 27677 C  C8  . NAG S 4 .    ? -44.005  32.543  57.062  1.00 297.30 ? 1681 NAG B C8  1 
HETATM 27678 N  N2  . NAG S 4 .    ? -44.984  31.741  59.121  1.00 311.51 ? 1681 NAG B N2  1 
HETATM 27679 O  O3  . NAG S 4 .    ? -47.425  30.124  58.126  1.00 270.76 ? 1681 NAG B O3  1 
HETATM 27680 O  O4  . NAG S 4 .    ? -49.662  31.317  59.517  1.00 268.63 ? 1681 NAG B O4  1 
HETATM 27681 O  O5  . NAG S 4 .    ? -47.116  31.013  62.018  1.00 323.43 ? 1681 NAG B O5  1 
HETATM 27682 O  O6  . NAG S 4 .    ? -49.550  30.216  62.784  1.00 283.53 ? 1681 NAG B O6  1 
HETATM 27683 O  O7  . NAG S 4 .    ? -44.190  30.252  57.608  1.00 290.49 ? 1681 NAG B O7  1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1     N N   . THR A 22   ? 1.8610 3.0845 1.3823 1.0575  -0.2911 -0.2607 22   THR A N   
2     C CA  . THR A 22   ? 1.8508 3.0483 1.3554 1.0735  -0.2993 -0.2607 22   THR A CA  
3     C C   . THR A 22   ? 1.8000 2.9862 1.3027 1.0468  -0.3254 -0.2726 22   THR A C   
4     O O   . THR A 22   ? 1.7718 2.9612 1.2849 1.0146  -0.3335 -0.2802 22   THR A O   
5     C CB  . THR A 22   ? 1.8594 3.0097 1.3522 1.0814  -0.2777 -0.2493 22   THR A CB  
6     O OG1 . THR A 22   ? 1.8285 2.9656 1.3300 1.0548  -0.2627 -0.2451 22   THR A OG1 
7     C CG2 . THR A 22   ? 1.8770 3.0342 1.3622 1.1251  -0.2553 -0.2400 22   THR A CG2 
8     N N   . TYR A 23   ? 1.8048 2.9772 1.2944 1.0607  -0.3368 -0.2742 23   TYR A N   
9     C CA  . TYR A 23   ? 1.8515 3.0083 1.3374 1.0361  -0.3568 -0.2831 23   TYR A CA  
10    C C   . TYR A 23   ? 1.8542 2.9550 1.3262 1.0297  -0.3542 -0.2750 23   TYR A C   
11    O O   . TYR A 23   ? 1.8452 2.9203 1.3063 1.0535  -0.3413 -0.2651 23   TYR A O   
12    C CB  . TYR A 23   ? 1.9311 3.1157 1.4136 1.0494  -0.3737 -0.2923 23   TYR A CB  
13    C CG  . TYR A 23   ? 2.0338 3.2247 1.5065 1.0913  -0.3676 -0.2852 23   TYR A CG  
14    C CD1 . TYR A 23   ? 2.0649 3.2197 1.5274 1.1135  -0.3491 -0.2718 23   TYR A CD1 
15    C CD2 . TYR A 23   ? 2.0870 3.3212 1.5605 1.1092  -0.3794 -0.2931 23   TYR A CD2 
16    C CE1 . TYR A 23   ? 2.1100 3.2687 1.5631 1.1541  -0.3416 -0.2663 23   TYR A CE1 
17    C CE2 . TYR A 23   ? 2.1156 3.3570 1.5801 1.1492  -0.3737 -0.2866 23   TYR A CE2 
18    C CZ  . TYR A 23   ? 2.1380 3.3400 1.5921 1.1726  -0.3546 -0.2732 23   TYR A CZ  
19    O OH  . TYR A 23   ? 2.1607 3.3686 1.6054 1.2146  -0.3474 -0.2677 23   TYR A OH  
20    N N   . VAL A 24   ? 1.8544 2.9372 1.3266 0.9982  -0.3652 -0.2798 24   VAL A N   
21    C CA  . VAL A 24   ? 1.8267 2.8598 1.2859 0.9882  -0.3656 -0.2723 24   VAL A CA  
22    C C   . VAL A 24   ? 1.7957 2.8256 1.2511 0.9720  -0.3826 -0.2798 24   VAL A C   
23    O O   . VAL A 24   ? 1.7805 2.8355 1.2460 0.9502  -0.3906 -0.2915 24   VAL A O   
24    C CB  . VAL A 24   ? 1.8445 2.8556 1.3077 0.9625  -0.3557 -0.2671 24   VAL A CB  
25    C CG1 . VAL A 24   ? 1.8535 2.8243 1.3063 0.9432  -0.3614 -0.2623 24   VAL A CG1 
26    C CG2 . VAL A 24   ? 1.8380 2.8385 1.2997 0.9791  -0.3346 -0.2573 24   VAL A CG2 
27    N N   . ILE A 25   ? 1.8122 2.8089 1.2526 0.9830  -0.3861 -0.2732 25   ILE A N   
28    C CA  . ILE A 25   ? 1.8702 2.8592 1.3048 0.9701  -0.3989 -0.2778 25   ILE A CA  
29    C C   . ILE A 25   ? 1.8655 2.7986 1.2856 0.9650  -0.3961 -0.2646 25   ILE A C   
30    O O   . ILE A 25   ? 1.8848 2.7894 1.2922 0.9879  -0.3948 -0.2566 25   ILE A O   
31    C CB  . ILE A 25   ? 1.9481 2.9572 1.3781 0.9955  -0.4072 -0.2826 25   ILE A CB  
32    C CG1 . ILE A 25   ? 1.9873 3.0577 1.4316 1.0029  -0.4100 -0.2953 25   ILE A CG1 
33    C CG2 . ILE A 25   ? 1.9760 2.9691 1.3979 0.9813  -0.4175 -0.2853 25   ILE A CG2 
34    C CD1 . ILE A 25   ? 2.0063 3.1105 1.4585 0.9800  -0.4211 -0.3117 25   ILE A CD1 
35    N N   . SER A 26   ? 1.8277 2.7444 1.2494 0.9359  -0.3941 -0.2621 26   SER A N   
36    C CA  . SER A 26   ? 1.8085 2.6755 1.2172 0.9306  -0.3899 -0.2480 26   SER A CA  
37    C C   . SER A 26   ? 1.7524 2.5963 1.1506 0.9237  -0.3978 -0.2453 26   SER A C   
38    O O   . SER A 26   ? 1.7442 2.6130 1.1475 0.9125  -0.4045 -0.2559 26   SER A O   
39    C CB  . SER A 26   ? 1.8373 2.6990 1.2519 0.9036  -0.3831 -0.2447 26   SER A CB  
40    O OG  . SER A 26   ? 1.8454 2.7306 1.2711 0.9071  -0.3752 -0.2481 26   SER A OG  
41    N N   . ALA A 27   ? 1.6938 2.4899 1.0773 0.9298  -0.3956 -0.2314 27   ALA A N   
42    C CA  . ALA A 27   ? 1.6715 2.4375 1.0444 0.9185  -0.4002 -0.2250 27   ALA A CA  
43    C C   . ALA A 27   ? 1.6130 2.3234 0.9703 0.9246  -0.3960 -0.2079 27   ALA A C   
44    O O   . ALA A 27   ? 1.5921 2.2876 0.9453 0.9446  -0.3906 -0.2038 27   ALA A O   
45    C CB  . ALA A 27   ? 1.6841 2.4640 1.0551 0.9317  -0.4091 -0.2330 27   ALA A CB  
46    N N   . PRO A 28   ? 1.6279 2.3072 0.9764 0.9070  -0.3966 -0.1980 28   PRO A N   
47    C CA  . PRO A 28   ? 1.6617 2.2872 0.9954 0.9085  -0.3927 -0.1804 28   PRO A CA  
48    C C   . PRO A 28   ? 1.7311 2.3259 1.0543 0.9407  -0.3938 -0.1773 28   PRO A C   
49    O O   . PRO A 28   ? 1.7604 2.3726 1.0859 0.9627  -0.3983 -0.1871 28   PRO A O   
50    C CB  . PRO A 28   ? 1.6415 2.2453 0.9682 0.8898  -0.3942 -0.1731 28   PRO A CB  
51    C CG  . PRO A 28   ? 1.6209 2.2692 0.9609 0.8671  -0.3929 -0.1854 28   PRO A CG  
52    C CD  . PRO A 28   ? 1.6081 2.3032 0.9606 0.8827  -0.3983 -0.2033 28   PRO A CD  
53    N N   . LYS A 29   ? 1.7874 2.3376 1.0989 0.9443  -0.3885 -0.1642 29   LYS A N   
54    C CA  . LYS A 29   ? 1.8171 2.3287 1.1165 0.9745  -0.3874 -0.1614 29   LYS A CA  
55    C C   . LYS A 29   ? 1.8496 2.3282 1.1387 0.9807  -0.3963 -0.1568 29   LYS A C   
56    O O   . LYS A 29   ? 1.8430 2.3040 1.1257 1.0093  -0.3989 -0.1605 29   LYS A O   
57    C CB  . LYS A 29   ? 1.8386 2.3137 1.1289 0.9740  -0.3781 -0.1504 29   LYS A CB  
58    C CG  . LYS A 29   ? 1.9008 2.3261 1.1766 1.0037  -0.3743 -0.1477 29   LYS A CG  
59    C CD  . LYS A 29   ? 2.4474 2.8865 1.7253 1.0381  -0.3713 -0.1613 29   LYS A CD  
60    C CE  . LYS A 29   ? 2.3775 2.7668 1.6411 1.0646  -0.3758 -0.1589 29   LYS A CE  
61    N NZ  . LYS A 29   ? 2.3727 2.7659 1.6351 1.1030  -0.3692 -0.1701 29   LYS A NZ  
62    N N   . ILE A 30   ? 1.8387 2.3102 1.1265 0.9537  -0.3990 -0.1491 30   ILE A N   
63    C CA  . ILE A 30   ? 1.8442 2.2838 1.1227 0.9534  -0.4051 -0.1433 30   ILE A CA  
64    C C   . ILE A 30   ? 1.8116 2.2880 1.0991 0.9282  -0.4071 -0.1498 30   ILE A C   
65    O O   . ILE A 30   ? 1.7925 2.3043 1.0904 0.9071  -0.4024 -0.1540 30   ILE A O   
66    C CB  . ILE A 30   ? 1.7633 2.1389 1.0265 0.9436  -0.4013 -0.1224 30   ILE A CB  
67    C CG1 . ILE A 30   ? 1.7724 2.1090 1.0258 0.9677  -0.3980 -0.1178 30   ILE A CG1 
68    C CG2 . ILE A 30   ? 1.7639 2.1034 1.0177 0.9407  -0.4061 -0.1153 30   ILE A CG2 
69    C CD1 . ILE A 30   ? 1.7957 2.1145 1.0437 1.0032  -0.4024 -0.1265 30   ILE A CD1 
70    N N   . PHE A 31   ? 1.7903 2.2592 1.0739 0.9304  -0.4128 -0.1521 31   PHE A N   
71    C CA  . PHE A 31   ? 1.7531 2.2448 1.0419 0.9018  -0.4105 -0.1557 31   PHE A CA  
72    C C   . PHE A 31   ? 1.7569 2.1951 1.0331 0.8825  -0.4042 -0.1367 31   PHE A C   
73    O O   . PHE A 31   ? 1.7439 2.1247 1.0067 0.8935  -0.4049 -0.1211 31   PHE A O   
74    C CB  . PHE A 31   ? 1.7321 2.2646 1.0276 0.9098  -0.4183 -0.1734 31   PHE A CB  
75    C CG  . PHE A 31   ? 1.7287 2.3179 1.0371 0.9282  -0.4234 -0.1912 31   PHE A CG  
76    C CD1 . PHE A 31   ? 1.7350 2.3311 1.0419 0.9628  -0.4309 -0.1977 31   PHE A CD1 
77    C CD2 . PHE A 31   ? 1.7035 2.3384 1.0256 0.9121  -0.4192 -0.2009 31   PHE A CD2 
78    C CE1 . PHE A 31   ? 1.6984 2.3472 1.0170 0.9807  -0.4331 -0.2119 31   PHE A CE1 
79    C CE2 . PHE A 31   ? 1.6876 2.3725 1.0217 0.9286  -0.4230 -0.2158 31   PHE A CE2 
80    C CZ  . PHE A 31   ? 1.6806 2.3732 1.0129 0.9629  -0.4294 -0.2204 31   PHE A CZ  
81    N N   . ARG A 32   ? 1.7682 2.2253 1.0488 0.8531  -0.3962 -0.1386 32   ARG A N   
82    C CA  . ARG A 32   ? 1.7636 2.1755 1.0334 0.8309  -0.3859 -0.1205 32   ARG A CA  
83    C C   . ARG A 32   ? 1.7145 2.1521 0.9886 0.8129  -0.3819 -0.1319 32   ARG A C   
84    O O   . ARG A 32   ? 1.6728 2.1692 0.9600 0.8044  -0.3809 -0.1522 32   ARG A O   
85    C CB  . ARG A 32   ? 1.8162 2.2215 1.0860 0.8070  -0.3711 -0.1067 32   ARG A CB  
86    C CG  . ARG A 32   ? 1.8442 2.2154 1.1067 0.8187  -0.3718 -0.0905 32   ARG A CG  
87    C CD  . ARG A 32   ? 1.8616 2.2318 1.1240 0.7939  -0.3560 -0.0760 32   ARG A CD  
88    N NE  . ARG A 32   ? 1.8479 2.1763 1.0998 0.8018  -0.3552 -0.0560 32   ARG A NE  
89    C CZ  . ARG A 32   ? 1.8265 2.1711 1.0820 0.8051  -0.3543 -0.0551 32   ARG A CZ  
90    N NH1 . ARG A 32   ? 1.8115 2.2102 1.0814 0.8007  -0.3540 -0.0717 32   ARG A NH1 
91    N NH2 . ARG A 32   ? 1.8193 2.1248 1.0640 0.8120  -0.3532 -0.0375 32   ARG A NH2 
92    N N   . VAL A 33   ? 1.6966 2.0884 0.9593 0.8065  -0.3788 -0.1190 33   VAL A N   
93    C CA  . VAL A 33   ? 1.7131 2.1186 0.9771 0.7848  -0.3709 -0.1259 33   VAL A CA  
94    C C   . VAL A 33   ? 1.7343 2.1561 1.0026 0.7499  -0.3490 -0.1238 33   VAL A C   
95    O O   . VAL A 33   ? 1.7307 2.1242 0.9942 0.7407  -0.3383 -0.1055 33   VAL A O   
96    C CB  . VAL A 33   ? 1.7416 2.0821 0.9907 0.7852  -0.3706 -0.1075 33   VAL A CB  
97    C CG1 . VAL A 33   ? 1.7726 2.1288 1.0229 0.7671  -0.3650 -0.1173 33   VAL A CG1 
98    C CG2 . VAL A 33   ? 1.7412 2.0528 0.9840 0.8236  -0.3897 -0.1058 33   VAL A CG2 
99    N N   . GLY A 34   ? 1.7750 2.2446 1.0525 0.7314  -0.3408 -0.1436 34   GLY A N   
100   C CA  . GLY A 34   ? 1.8294 2.3181 1.1118 0.6998  -0.3170 -0.1457 34   GLY A CA  
101   C C   . GLY A 34   ? 1.8666 2.3840 1.1582 0.7038  -0.3174 -0.1509 34   GLY A C   
102   O O   . GLY A 34   ? 1.8783 2.4071 1.1736 0.6818  -0.2975 -0.1506 34   GLY A O   
103   N N   . ALA A 35   ? 1.8813 2.4090 1.1764 0.7324  -0.3383 -0.1555 35   ALA A N   
104   C CA  . ALA A 35   ? 1.8939 2.4452 1.1974 0.7365  -0.3393 -0.1591 35   ALA A CA  
105   C C   . ALA A 35   ? 1.9225 2.5397 1.2420 0.7406  -0.3469 -0.1883 35   ALA A C   
106   O O   . ALA A 35   ? 1.8981 2.5381 1.2210 0.7600  -0.3626 -0.2015 35   ALA A O   
107   C CB  . ALA A 35   ? 1.8851 2.4054 1.1824 0.7620  -0.3528 -0.1450 35   ALA A CB  
108   N N   . SER A 36   ? 1.9564 2.6029 1.2854 0.7231  -0.3347 -0.1975 36   SER A N   
109   C CA  . SER A 36   ? 1.9579 2.6640 1.3029 0.7251  -0.3404 -0.2243 36   SER A CA  
110   C C   . SER A 36   ? 1.9542 2.6656 1.3033 0.7499  -0.3565 -0.2224 36   SER A C   
111   O O   . SER A 36   ? 1.9623 2.6676 1.3135 0.7464  -0.3518 -0.2150 36   SER A O   
112   C CB  . SER A 36   ? 1.9419 2.6667 1.2944 0.6995  -0.3206 -0.2324 36   SER A CB  
113   O OG  . SER A 36   ? 1.9434 2.6282 1.2851 0.6795  -0.2992 -0.2131 36   SER A OG  
114   N N   . GLU A 37   ? 1.9678 2.6911 1.3177 0.7753  -0.3735 -0.2286 37   GLU A N   
115   C CA  . GLU A 37   ? 1.9878 2.7112 1.3399 0.8000  -0.3848 -0.2250 37   GLU A CA  
116   C C   . GLU A 37   ? 1.9535 2.7296 1.3220 0.8006  -0.3876 -0.2441 37   GLU A C   
117   O O   . GLU A 37   ? 1.9376 2.7584 1.3155 0.8062  -0.3941 -0.2636 37   GLU A O   
118   C CB  . GLU A 37   ? 2.0546 2.7615 1.3989 0.8301  -0.3981 -0.2208 37   GLU A CB  
119   C CG  . GLU A 37   ? 2.1397 2.7859 1.4671 0.8305  -0.3960 -0.2004 37   GLU A CG  
120   C CD  . GLU A 37   ? 2.2042 2.8027 1.5227 0.8264  -0.3891 -0.1783 37   GLU A CD  
121   O OE1 . GLU A 37   ? 2.2188 2.8256 1.5420 0.8068  -0.3788 -0.1757 37   GLU A OE1 
122   O OE2 . GLU A 37   ? 2.2354 2.7882 1.5419 0.8437  -0.3935 -0.1640 37   GLU A OE2 
123   N N   . ASN A 38   ? 1.9214 2.6919 1.2936 0.7940  -0.3820 -0.2379 38   ASN A N   
124   C CA  . ASN A 38   ? 1.8810 2.6928 1.2684 0.7925  -0.3833 -0.2531 38   ASN A CA  
125   C C   . ASN A 38   ? 1.8501 2.6781 1.2419 0.8203  -0.3945 -0.2560 38   ASN A C   
126   O O   . ASN A 38   ? 1.8468 2.6441 1.2302 0.8369  -0.3962 -0.2411 38   ASN A O   
127   C CB  . ASN A 38   ? 1.8623 2.6597 1.2511 0.7758  -0.3727 -0.2439 38   ASN A CB  
128   C CG  . ASN A 38   ? 1.8390 2.6482 1.2327 0.7481  -0.3589 -0.2530 38   ASN A CG  
129   O OD1 . ASN A 38   ? 1.8410 2.6389 1.2281 0.7358  -0.3506 -0.2520 38   ASN A OD1 
130   N ND2 . ASN A 38   ? 1.8186 2.6490 1.2237 0.7378  -0.3543 -0.2623 38   ASN A ND2 
131   N N   . ILE A 39   ? 1.8199 2.6965 1.2246 0.8250  -0.3999 -0.2753 39   ILE A N   
132   C CA  . ILE A 39   ? 1.7776 2.6768 1.1876 0.8518  -0.4076 -0.2790 39   ILE A CA  
133   C C   . ILE A 39   ? 1.7411 2.6861 1.1683 0.8456  -0.4075 -0.2952 39   ILE A C   
134   O O   . ILE A 39   ? 1.7251 2.7105 1.1609 0.8412  -0.4111 -0.3132 39   ILE A O   
135   C CB  . ILE A 39   ? 1.7650 2.6818 1.1718 0.8728  -0.4167 -0.2854 39   ILE A CB  
136   C CG1 . ILE A 39   ? 1.7552 2.6307 1.1467 0.8714  -0.4169 -0.2741 39   ILE A CG1 
137   C CG2 . ILE A 39   ? 1.7623 2.6898 1.1703 0.9057  -0.4208 -0.2828 39   ILE A CG2 
138   C CD1 . ILE A 39   ? 1.7340 2.5533 1.1122 0.8819  -0.4142 -0.2526 39   ILE A CD1 
139   N N   . VAL A 40   ? 1.7566 2.6956 1.1888 0.8444  -0.4028 -0.2893 40   VAL A N   
140   C CA  . VAL A 40   ? 1.7842 2.7622 1.2327 0.8403  -0.4025 -0.3028 40   VAL A CA  
141   C C   . VAL A 40   ? 1.8237 2.8304 1.2766 0.8684  -0.4076 -0.3060 40   VAL A C   
142   O O   . VAL A 40   ? 1.8060 2.7947 1.2493 0.8928  -0.4079 -0.2945 40   VAL A O   
143   C CB  . VAL A 40   ? 1.8413 2.8068 1.2959 0.8262  -0.3943 -0.2966 40   VAL A CB  
144   C CG1 . VAL A 40   ? 1.8490 2.7803 1.2962 0.8044  -0.3873 -0.2871 40   VAL A CG1 
145   C CG2 . VAL A 40   ? 1.8282 2.7833 1.2810 0.8462  -0.3911 -0.2844 40   VAL A CG2 
146   N N   . ILE A 41   ? 1.8568 2.9079 1.3240 0.8653  -0.4101 -0.3221 41   ILE A N   
147   C CA  . ILE A 41   ? 1.8776 2.9618 1.3515 0.8896  -0.4120 -0.3246 41   ILE A CA  
148   C C   . ILE A 41   ? 1.8495 2.9555 1.3390 0.8757  -0.4080 -0.3324 41   ILE A C   
149   O O   . ILE A 41   ? 1.8240 2.9395 1.3215 0.8510  -0.4084 -0.3454 41   ILE A O   
150   C CB  . ILE A 41   ? 1.9515 3.0778 1.4277 0.9014  -0.4211 -0.3382 41   ILE A CB  
151   C CG1 . ILE A 41   ? 1.9614 3.1291 1.4473 0.9242  -0.4211 -0.3410 41   ILE A CG1 
152   C CG2 . ILE A 41   ? 1.9597 3.1092 1.4435 0.8738  -0.4238 -0.3579 41   ILE A CG2 
153   C CD1 . ILE A 41   ? 1.9808 3.2009 1.4716 0.9345  -0.4301 -0.3561 41   ILE A CD1 
154   N N   . GLN A 42   ? 1.8771 2.9895 1.3709 0.8923  -0.4020 -0.3246 42   GLN A N   
155   C CA  . GLN A 42   ? 1.9406 3.0649 1.4484 0.8793  -0.3959 -0.3278 42   GLN A CA  
156   C C   . GLN A 42   ? 1.9943 3.1345 1.5039 0.9074  -0.3889 -0.3191 42   GLN A C   
157   O O   . GLN A 42   ? 1.9866 3.1089 1.4842 0.9305  -0.3852 -0.3074 42   GLN A O   
158   C CB  . GLN A 42   ? 1.9644 3.0480 1.4694 0.8595  -0.3878 -0.3175 42   GLN A CB  
159   C CG  . GLN A 42   ? 1.9763 3.0548 1.4874 0.8615  -0.3758 -0.3080 42   GLN A CG  
160   C CD  . GLN A 42   ? 1.9949 3.0322 1.4946 0.8607  -0.3671 -0.2920 42   GLN A CD  
161   O OE1 . GLN A 42   ? 2.0142 3.0438 1.5170 0.8609  -0.3547 -0.2836 42   GLN A OE1 
162   N NE2 . GLN A 42   ? 1.9943 3.0051 1.4807 0.8592  -0.3722 -0.2875 42   GLN A NE2 
163   N N   . VAL A 43   ? 2.0188 3.1906 1.5428 0.9067  -0.3854 -0.3246 43   VAL A N   
164   C CA  . VAL A 43   ? 1.9906 3.1836 1.5166 0.9356  -0.3762 -0.3161 43   VAL A CA  
165   C C   . VAL A 43   ? 2.0363 3.2500 1.5783 0.9276  -0.3672 -0.3168 43   VAL A C   
166   O O   . VAL A 43   ? 2.0470 3.2666 1.5999 0.9013  -0.3722 -0.3282 43   VAL A O   
167   C CB  . VAL A 43   ? 1.9132 3.1428 1.4360 0.9611  -0.3856 -0.3223 43   VAL A CB  
168   C CG1 . VAL A 43   ? 1.8792 3.1527 1.4145 0.9470  -0.3974 -0.3418 43   VAL A CG1 
169   C CG2 . VAL A 43   ? 1.8660 3.1116 1.3872 0.9957  -0.3732 -0.3104 43   VAL A CG2 
170   N N   . TYR A 44   ? 2.0827 3.3038 1.6252 0.9506  -0.3517 -0.3042 44   TYR A N   
171   C CA  . TYR A 44   ? 2.1503 3.3872 1.7070 0.9455  -0.3384 -0.3004 44   TYR A CA  
172   C C   . TYR A 44   ? 2.3711 3.6617 1.9381 0.9621  -0.3412 -0.3061 44   TYR A C   
173   O O   . TYR A 44   ? 2.3243 3.6300 1.9011 0.9664  -0.3267 -0.2986 44   TYR A O   
174   C CB  . TYR A 44   ? 2.2707 3.4818 1.8223 0.9572  -0.3138 -0.2820 44   TYR A CB  
175   C CG  . TYR A 44   ? 2.4204 3.6338 1.9856 0.9426  -0.2963 -0.2758 44   TYR A CG  
176   C CD1 . TYR A 44   ? 2.4784 3.6660 2.0502 0.9078  -0.2956 -0.2779 44   TYR A CD1 
177   C CD2 . TYR A 44   ? 2.4879 3.7286 2.0593 0.9637  -0.2789 -0.2669 44   TYR A CD2 
178   C CE1 . TYR A 44   ? 2.5049 3.6922 2.0893 0.8928  -0.2792 -0.2720 44   TYR A CE1 
179   C CE2 . TYR A 44   ? 2.5153 3.7555 2.0992 0.9486  -0.2608 -0.2597 44   TYR A CE2 
180   C CZ  . TYR A 44   ? 2.5162 3.7286 2.1067 0.9124  -0.2616 -0.2627 44   TYR A CZ  
181   O OH  . TYR A 44   ? 2.5109 3.7206 2.1141 0.8959  -0.2433 -0.2553 44   TYR A OH  
182   N N   . GLY A 45   ? 2.4191 3.7397 1.9840 0.9702  -0.3588 -0.3191 45   GLY A N   
183   C CA  . GLY A 45   ? 2.4315 3.8080 2.0053 0.9863  -0.3633 -0.3258 45   GLY A CA  
184   C C   . GLY A 45   ? 2.4203 3.8153 2.0119 0.9637  -0.3632 -0.3343 45   GLY A C   
185   O O   . GLY A 45   ? 2.3901 3.7630 1.9873 0.9317  -0.3692 -0.3448 45   GLY A O   
186   N N   . TYR A 46   ? 2.4571 3.8918 2.0574 0.9817  -0.3554 -0.3290 46   TYR A N   
187   C CA  . TYR A 46   ? 2.4903 3.9466 2.1080 0.9638  -0.3553 -0.3365 46   TYR A CA  
188   C C   . TYR A 46   ? 2.4852 3.9615 2.1103 0.9404  -0.3764 -0.3635 46   TYR A C   
189   O O   . TYR A 46   ? 2.5474 4.0114 2.1642 0.9309  -0.3889 -0.3757 46   TYR A O   
190   C CB  . TYR A 46   ? 2.5345 4.0376 2.1582 0.9927  -0.3441 -0.3255 46   TYR A CB  
191   C CG  . TYR A 46   ? 2.5836 4.1252 2.1972 1.0285  -0.3497 -0.3246 46   TYR A CG  
192   C CD1 . TYR A 46   ? 2.6060 4.1942 2.2218 1.0301  -0.3703 -0.3444 46   TYR A CD1 
193   C CD2 . TYR A 46   ? 2.6065 4.1370 2.2078 1.0606  -0.3333 -0.3051 46   TYR A CD2 
194   C CE1 . TYR A 46   ? 2.6267 4.2514 2.2332 1.0622  -0.3757 -0.3436 46   TYR A CE1 
195   C CE2 . TYR A 46   ? 2.6269 4.1901 2.2184 1.0946  -0.3383 -0.3042 46   TYR A CE2 
196   C CZ  . TYR A 46   ? 2.6406 4.2516 2.2349 1.0950  -0.3603 -0.3229 46   TYR A CZ  
197   O OH  . TYR A 46   ? 2.6604 4.3055 2.2452 1.1283  -0.3654 -0.3221 46   TYR A OH  
198   N N   . THR A 47   ? 2.4133 3.9197 2.0536 0.9314  -0.3780 -0.3727 47   THR A N   
199   C CA  . THR A 47   ? 2.3545 3.8756 2.0042 0.9056  -0.3935 -0.4003 47   THR A CA  
200   C C   . THR A 47   ? 2.3302 3.8889 1.9736 0.9131  -0.4096 -0.4196 47   THR A C   
201   O O   . THR A 47   ? 2.3204 3.8711 1.9639 0.8898  -0.4195 -0.4414 47   THR A O   
202   C CB  . THR A 47   ? 2.9938 4.5476 2.6609 0.9011  -0.3914 -0.4057 47   THR A CB  
203   O OG1 . THR A 47   ? 2.9797 4.5018 2.6533 0.8952  -0.3738 -0.3855 47   THR A OG1 
204   C CG2 . THR A 47   ? 2.9951 4.5530 2.6722 0.8711  -0.4042 -0.4361 47   THR A CG2 
205   N N   . GLU A 48   ? 2.2947 3.8955 1.9328 0.9457  -0.4102 -0.4115 48   GLU A N   
206   C CA  . GLU A 48   ? 2.2812 3.9258 1.9146 0.9540  -0.4247 -0.4293 48   GLU A CA  
207   C C   . GLU A 48   ? 2.2377 3.8452 1.8586 0.9399  -0.4311 -0.4366 48   GLU A C   
208   O O   . GLU A 48   ? 2.2363 3.8162 1.8438 0.9558  -0.4272 -0.4197 48   GLU A O   
209   C CB  . GLU A 48   ? 2.2956 3.9811 1.9223 0.9949  -0.4218 -0.4138 48   GLU A CB  
210   C CG  . GLU A 48   ? 2.2991 4.0419 1.9230 1.0054  -0.4365 -0.4321 48   GLU A CG  
211   C CD  . GLU A 48   ? 2.2861 4.0910 1.9249 1.0003  -0.4430 -0.4508 48   GLU A CD  
212   O OE1 . GLU A 48   ? 2.2692 4.0731 1.9202 0.9946  -0.4351 -0.4451 48   GLU A OE1 
213   O OE2 . GLU A 48   ? 2.2855 4.1403 1.9240 1.0012  -0.4552 -0.4713 48   GLU A OE2 
214   N N   . ALA A 49   ? 2.2032 3.8092 1.8279 0.9108  -0.4391 -0.4618 49   ALA A N   
215   C CA  . ALA A 49   ? 2.1655 3.7453 1.7781 0.8986  -0.4437 -0.4697 49   ALA A CA  
216   C C   . ALA A 49   ? 2.1473 3.7503 1.7473 0.9277  -0.4484 -0.4610 49   ALA A C   
217   O O   . ALA A 49   ? 2.1588 3.8067 1.7611 0.9553  -0.4492 -0.4544 49   ALA A O   
218   C CB  . ALA A 49   ? 2.1623 3.7604 1.7813 0.8707  -0.4493 -0.5016 49   ALA A CB  
219   N N   . PHE A 50   ? 2.1221 3.6941 1.7087 0.9227  -0.4506 -0.4599 50   PHE A N   
220   C CA  . PHE A 50   ? 2.1356 3.7274 1.7102 0.9484  -0.4560 -0.4540 50   PHE A CA  
221   C C   . PHE A 50   ? 2.0838 3.6381 1.6440 0.9378  -0.4584 -0.4545 50   PHE A C   
222   O O   . PHE A 50   ? 2.0625 3.5579 1.6154 0.9282  -0.4526 -0.4416 50   PHE A O   
223   C CB  . PHE A 50   ? 2.2306 3.8213 1.8005 0.9855  -0.4495 -0.4279 50   PHE A CB  
224   C CG  . PHE A 50   ? 2.3413 3.8651 1.9008 0.9882  -0.4400 -0.4060 50   PHE A CG  
225   C CD1 . PHE A 50   ? 2.4004 3.8994 1.9442 1.0087  -0.4399 -0.3930 50   PHE A CD1 
226   C CD2 . PHE A 50   ? 2.3946 3.8806 1.9602 0.9702  -0.4307 -0.3989 50   PHE A CD2 
227   C CE1 . PHE A 50   ? 2.4321 3.8709 1.9663 1.0112  -0.4305 -0.3743 50   PHE A CE1 
228   C CE2 . PHE A 50   ? 2.4183 3.8473 1.9744 0.9719  -0.4211 -0.3799 50   PHE A CE2 
229   C CZ  . PHE A 50   ? 2.4376 3.8435 1.9780 0.9924  -0.4209 -0.3681 50   PHE A CZ  
230   N N   . ASP A 51   ? 2.0680 3.6585 1.6242 0.9395  -0.4661 -0.4689 51   ASP A N   
231   C CA  . ASP A 51   ? 2.0597 3.6193 1.6033 0.9268  -0.4671 -0.4709 51   ASP A CA  
232   C C   . ASP A 51   ? 2.0622 3.5662 1.5906 0.9448  -0.4644 -0.4444 51   ASP A C   
233   O O   . ASP A 51   ? 2.0680 3.5711 1.5940 0.9752  -0.4626 -0.4266 51   ASP A O   
234   C CB  . ASP A 51   ? 2.0413 3.6551 1.5832 0.9301  -0.4747 -0.4886 51   ASP A CB  
235   C CG  . ASP A 51   ? 2.0143 3.6529 1.5638 0.8953  -0.4730 -0.5188 51   ASP A CG  
236   O OD1 . ASP A 51   ? 1.9871 3.6022 1.5438 0.8709  -0.4662 -0.5268 51   ASP A OD1 
237   O OD2 . ASP A 51   ? 2.0159 3.6979 1.5640 0.8925  -0.4769 -0.5356 51   ASP A OD2 
238   N N   . ALA A 52   ? 2.0409 3.4991 1.5589 0.9257  -0.4622 -0.4429 52   ALA A N   
239   C CA  . ALA A 52   ? 2.0030 3.4009 1.5059 0.9366  -0.4594 -0.4198 52   ALA A CA  
240   C C   . ALA A 52   ? 1.9981 3.3712 1.4895 0.9205  -0.4602 -0.4230 52   ALA A C   
241   O O   . ALA A 52   ? 2.0032 3.3552 1.4951 0.8891  -0.4542 -0.4310 52   ALA A O   
242   C CB  . ALA A 52   ? 1.9658 3.3134 1.4696 0.9251  -0.4508 -0.4067 52   ALA A CB  
243   N N   . THR A 53   ? 2.0012 3.3758 1.4821 0.9422  -0.4657 -0.4160 53   THR A N   
244   C CA  . THR A 53   ? 1.9869 3.3340 1.4557 0.9290  -0.4657 -0.4157 53   THR A CA  
245   C C   . THR A 53   ? 1.9668 3.2514 1.4201 0.9478  -0.4650 -0.3908 53   THR A C   
246   O O   . THR A 53   ? 1.9593 3.2429 1.4093 0.9813  -0.4674 -0.3786 53   THR A O   
247   C CB  . THR A 53   ? 2.0597 3.4622 1.5289 0.9351  -0.4731 -0.4315 53   THR A CB  
248   O OG1 . THR A 53   ? 2.0602 3.5034 1.5394 0.9040  -0.4699 -0.4575 53   THR A OG1 
249   C CG2 . THR A 53   ? 2.0695 3.4346 1.5231 0.9378  -0.4744 -0.4214 53   THR A CG2 
250   N N   . ILE A 54   ? 1.9294 3.1617 1.3728 0.9269  -0.4600 -0.3834 54   ILE A N   
251   C CA  . ILE A 54   ? 1.9191 3.0887 1.3477 0.9425  -0.4590 -0.3604 54   ILE A CA  
252   C C   . ILE A 54   ? 1.9008 3.0500 1.3184 0.9319  -0.4601 -0.3600 54   ILE A C   
253   O O   . ILE A 54   ? 1.8582 3.0395 1.2803 0.9088  -0.4586 -0.3770 54   ILE A O   
254   C CB  . ILE A 54   ? 1.9515 3.0676 1.3776 0.9265  -0.4502 -0.3469 54   ILE A CB  
255   C CG1 . ILE A 54   ? 1.9395 3.0764 1.3781 0.9298  -0.4473 -0.3491 54   ILE A CG1 
256   C CG2 . ILE A 54   ? 1.9537 3.0069 1.3646 0.9436  -0.4489 -0.3244 54   ILE A CG2 
257   C CD1 . ILE A 54   ? 1.9289 3.0209 1.3664 0.9105  -0.4385 -0.3383 54   ILE A CD1 
258   N N   . SER A 55   ? 1.9604 3.0550 1.3635 0.9479  -0.4610 -0.3411 55   SER A N   
259   C CA  . SER A 55   ? 2.0096 3.0753 1.4012 0.9380  -0.4613 -0.3373 55   SER A CA  
260   C C   . SER A 55   ? 2.0560 3.0561 1.4319 0.9606  -0.4630 -0.3154 55   SER A C   
261   O O   . SER A 55   ? 2.0361 3.0196 1.4099 0.9881  -0.4636 -0.3053 55   SER A O   
262   C CB  . SER A 55   ? 2.0360 3.1602 1.4315 0.9437  -0.4685 -0.3545 55   SER A CB  
263   O OG  . SER A 55   ? 2.0406 3.2185 1.4452 0.9726  -0.4754 -0.3616 55   SER A OG  
264   N N   . ILE A 56   ? 2.1359 3.0980 1.5007 0.9483  -0.4619 -0.3088 56   ILE A N   
265   C CA  . ILE A 56   ? 2.2452 3.1356 1.5942 0.9640  -0.4623 -0.2879 56   ILE A CA  
266   C C   . ILE A 56   ? 2.3202 3.2077 1.6609 0.9854  -0.4705 -0.2879 56   ILE A C   
267   O O   . ILE A 56   ? 2.3100 3.2087 1.6494 0.9653  -0.4704 -0.2948 56   ILE A O   
268   C CB  . ILE A 56   ? 2.3091 3.1453 1.6503 0.9306  -0.4527 -0.2759 56   ILE A CB  
269   C CG1 . ILE A 56   ? 2.3483 3.2184 1.6948 0.8961  -0.4467 -0.2905 56   ILE A CG1 
270   C CG2 . ILE A 56   ? 2.3986 3.2144 1.7428 0.9193  -0.4447 -0.2676 56   ILE A CG2 
271   C CD1 . ILE A 56   ? 2.3807 3.2141 1.7239 0.8592  -0.4315 -0.2819 56   ILE A CD1 
272   N N   . LYS A 57   ? 2.3927 3.2623 1.7271 1.0255  -0.4753 -0.2801 57   LYS A N   
273   C CA  . LYS A 57   ? 2.4546 3.3293 1.7823 1.0536  -0.4833 -0.2816 57   LYS A CA  
274   C C   . LYS A 57   ? 2.4918 3.2928 1.8038 1.0834  -0.4834 -0.2644 57   LYS A C   
275   O O   . LYS A 57   ? 2.5057 3.2731 1.8145 1.0990  -0.4779 -0.2550 57   LYS A O   
276   C CB  . LYS A 57   ? 2.4338 3.3871 1.7724 1.0804  -0.4887 -0.2962 57   LYS A CB  
277   C CG  . LYS A 57   ? 2.4097 3.4386 1.7630 1.0525  -0.4902 -0.3163 57   LYS A CG  
278   C CD  . LYS A 57   ? 2.3858 3.4928 1.7504 1.0788  -0.4949 -0.3291 57   LYS A CD  
279   C CE  . LYS A 57   ? 2.3715 3.5501 1.7508 1.0488  -0.4957 -0.3505 57   LYS A CE  
280   N NZ  . LYS A 57   ? 2.3644 3.6248 1.7538 1.0735  -0.5018 -0.3636 57   LYS A NZ  
281   N N   . SER A 58   ? 2.5191 3.2978 1.8215 1.0917  -0.4889 -0.2620 58   SER A N   
282   C CA  . SER A 58   ? 2.5539 3.2457 1.8397 1.1026  -0.4882 -0.2451 58   SER A CA  
283   C C   . SER A 58   ? 2.5440 3.2058 1.8207 1.1527  -0.4890 -0.2398 58   SER A C   
284   O O   . SER A 58   ? 2.5619 3.2508 1.8375 1.1801  -0.4947 -0.2463 58   SER A O   
285   C CB  . SER A 58   ? 2.5901 3.2659 1.8698 1.0817  -0.4922 -0.2446 58   SER A CB  
286   O OG  . SER A 58   ? 2.6087 3.3537 1.8950 1.0926  -0.4996 -0.2605 58   SER A OG  
287   N N   . TYR A 59   ? 2.5477 3.1506 1.8169 1.1641  -0.4818 -0.2281 59   TYR A N   
288   C CA  . TYR A 59   ? 2.5471 3.1196 1.8078 1.2118  -0.4773 -0.2247 59   TYR A CA  
289   C C   . TYR A 59   ? 2.9127 3.5499 2.1794 1.2506  -0.4786 -0.2362 59   TYR A C   
290   O O   . TYR A 59   ? 2.9165 3.6270 2.1973 1.2450  -0.4783 -0.2460 59   TYR A O   
291   C CB  . TYR A 59   ? 2.5445 3.0246 1.7876 1.2221  -0.4773 -0.2119 59   TYR A CB  
292   C CG  . TYR A 59   ? 2.5257 2.9593 1.7607 1.2561  -0.4661 -0.2070 59   TYR A CG  
293   C CD1 . TYR A 59   ? 2.4993 2.9685 1.7430 1.2639  -0.4558 -0.2112 59   TYR A CD1 
294   C CD2 . TYR A 59   ? 2.5305 2.8840 1.7494 1.2792  -0.4640 -0.1991 59   TYR A CD2 
295   C CE1 . TYR A 59   ? 2.4898 2.9198 1.7264 1.2930  -0.4420 -0.2083 59   TYR A CE1 
296   C CE2 . TYR A 59   ? 2.5226 2.8348 1.7341 1.3099  -0.4508 -0.1973 59   TYR A CE2 
297   C CZ  . TYR A 59   ? 2.5020 2.8543 1.7224 1.3162  -0.4389 -0.2022 59   TYR A CZ  
298   O OH  . TYR A 59   ? 2.4968 2.8099 1.7098 1.3448  -0.4225 -0.2017 59   TYR A OH  
299   N N   . PRO A 60   ? 2.8992 3.5108 2.1554 1.2908  -0.4790 -0.2349 60   PRO A N   
300   C CA  . PRO A 60   ? 2.8532 3.5302 2.1159 1.3304  -0.4756 -0.2437 60   PRO A CA  
301   C C   . PRO A 60   ? 2.7891 3.5519 2.0624 1.3242  -0.4868 -0.2558 60   PRO A C   
302   O O   . PRO A 60   ? 2.7682 3.5952 2.0490 1.3524  -0.4836 -0.2625 60   PRO A O   
303   C CB  . PRO A 60   ? 2.8875 3.5080 2.1351 1.3783  -0.4695 -0.2386 60   PRO A CB  
304   C CG  . PRO A 60   ? 2.9018 3.4233 2.1359 1.3622  -0.4689 -0.2273 60   PRO A CG  
305   C CD  . PRO A 60   ? 2.9047 3.4327 2.1439 1.3079  -0.4799 -0.2257 60   PRO A CD  
306   N N   . ASP A 61   ? 2.7473 3.5124 2.0212 1.2880  -0.4978 -0.2585 61   ASP A N   
307   C CA  . ASP A 61   ? 2.7105 3.5590 1.9949 1.2758  -0.5072 -0.2723 61   ASP A CA  
308   C C   . ASP A 61   ? 2.6706 3.5666 1.9692 1.2308  -0.5073 -0.2808 61   ASP A C   
309   O O   . ASP A 61   ? 2.6651 3.5256 1.9621 1.1900  -0.5070 -0.2775 61   ASP A O   
310   C CB  . ASP A 61   ? 2.7369 3.5608 2.0131 1.2618  -0.5162 -0.2721 61   ASP A CB  
311   C CG  . ASP A 61   ? 2.7602 3.5293 2.0329 1.2116  -0.5154 -0.2653 61   ASP A CG  
312   O OD1 . ASP A 61   ? 2.7698 3.5759 2.0487 1.1743  -0.5187 -0.2740 61   ASP A OD1 
313   O OD2 . ASP A 61   ? 2.7556 3.4466 2.0192 1.2091  -0.5096 -0.2515 61   ASP A OD2 
314   N N   . LYS A 62   ? 2.6355 3.6102 1.9478 1.2381  -0.5064 -0.2915 62   LYS A N   
315   C CA  . LYS A 62   ? 2.6114 3.6314 1.9375 1.1968  -0.5062 -0.3018 62   LYS A CA  
316   C C   . LYS A 62   ? 2.6170 3.6845 1.9485 1.1641  -0.5137 -0.3163 62   LYS A C   
317   O O   . LYS A 62   ? 2.6326 3.7737 1.9778 1.1477  -0.5151 -0.3319 62   LYS A O   
318   C CB  . LYS A 62   ? 2.5539 3.6358 1.8931 1.2135  -0.5016 -0.3078 62   LYS A CB  
319   C CG  . LYS A 62   ? 2.4849 3.5211 1.8235 1.2159  -0.4904 -0.2967 62   LYS A CG  
320   C CD  . LYS A 62   ? 2.4123 3.4892 1.7582 1.2502  -0.4818 -0.2964 62   LYS A CD  
321   C CE  . LYS A 62   ? 2.3536 3.3702 1.6943 1.2578  -0.4684 -0.2837 62   LYS A CE  
322   N NZ  . LYS A 62   ? 2.3193 3.3649 1.6652 1.2916  -0.4551 -0.2812 62   LYS A NZ  
323   N N   . LYS A 63   ? 2.6122 3.6354 1.9327 1.1539  -0.5169 -0.3115 63   LYS A N   
324   C CA  . LYS A 63   ? 2.6045 3.6667 1.9284 1.1217  -0.5209 -0.3247 63   LYS A CA  
325   C C   . LYS A 63   ? 2.5746 3.6215 1.9022 1.0676  -0.5130 -0.3280 63   LYS A C   
326   O O   . LYS A 63   ? 2.5676 3.6797 1.9078 1.0421  -0.5110 -0.3455 63   LYS A O   
327   C CB  . LYS A 63   ? 2.6350 3.6596 1.9458 1.1335  -0.5262 -0.3184 63   LYS A CB  
328   C CG  . LYS A 63   ? 2.6731 3.7273 1.9810 1.1864  -0.5330 -0.3189 63   LYS A CG  
329   C CD  . LYS A 63   ? 2.6967 3.8626 2.0189 1.1953  -0.5376 -0.3376 63   LYS A CD  
330   C CE  . LYS A 63   ? 2.7144 3.9341 2.0409 1.1635  -0.5424 -0.3540 63   LYS A CE  
331   N NZ  . LYS A 63   ? 2.7125 4.0424 2.0544 1.1641  -0.5456 -0.3740 63   LYS A NZ  
332   N N   . PHE A 64   ? 2.5585 3.5201 1.8752 1.0507  -0.5071 -0.3113 64   PHE A N   
333   C CA  . PHE A 64   ? 2.5134 3.4576 1.8327 1.0020  -0.4964 -0.3118 64   PHE A CA  
334   C C   . PHE A 64   ? 2.5004 3.4655 1.8303 0.9951  -0.4913 -0.3152 64   PHE A C   
335   O O   . PHE A 64   ? 2.4985 3.4364 1.8263 1.0210  -0.4923 -0.3044 64   PHE A O   
336   C CB  . PHE A 64   ? 2.4911 3.3381 1.7956 0.9884  -0.4905 -0.2902 64   PHE A CB  
337   C CG  . PHE A 64   ? 2.4656 3.2977 1.7648 0.9555  -0.4851 -0.2909 64   PHE A CG  
338   C CD1 . PHE A 64   ? 2.4586 3.2479 1.7458 0.9703  -0.4909 -0.2816 64   PHE A CD1 
339   C CD2 . PHE A 64   ? 2.4392 3.2974 1.7452 0.9093  -0.4719 -0.3009 64   PHE A CD2 
340   C CE1 . PHE A 64   ? 2.4514 3.2248 1.7339 0.9376  -0.4842 -0.2813 64   PHE A CE1 
341   C CE2 . PHE A 64   ? 2.4325 3.2764 1.7334 0.8769  -0.4627 -0.3013 64   PHE A CE2 
342   C CZ  . PHE A 64   ? 2.4400 3.2417 1.7293 0.8901  -0.4691 -0.2909 64   PHE A CZ  
343   N N   . SER A 65   ? 2.4820 3.4950 1.8231 0.9600  -0.4845 -0.3312 65   SER A N   
344   C CA  . SER A 65   ? 2.4844 3.5092 1.8351 0.9469  -0.4780 -0.3342 65   SER A CA  
345   C C   . SER A 65   ? 2.4811 3.4923 1.8333 0.8987  -0.4632 -0.3378 65   SER A C   
346   O O   . SER A 65   ? 2.4929 3.5587 1.8540 0.8733  -0.4575 -0.3584 65   SER A O   
347   C CB  . SER A 65   ? 2.5035 3.6127 1.8695 0.9610  -0.4838 -0.3533 65   SER A CB  
348   O OG  . SER A 65   ? 2.5196 3.6747 1.8974 0.9256  -0.4760 -0.3725 65   SER A OG  
349   N N   . TYR A 66   ? 2.4391 3.3776 1.7823 0.8873  -0.4551 -0.3177 66   TYR A N   
350   C CA  . TYR A 66   ? 2.3778 3.2880 1.7182 0.8450  -0.4379 -0.3146 66   TYR A CA  
351   C C   . TYR A 66   ? 2.3716 3.3346 1.7262 0.8197  -0.4279 -0.3342 66   TYR A C   
352   O O   . TYR A 66   ? 2.3622 3.3526 1.7206 0.7881  -0.4149 -0.3492 66   TYR A O   
353   C CB  . TYR A 66   ? 2.2906 3.1158 1.6187 0.8436  -0.4322 -0.2872 66   TYR A CB  
354   C CG  . TYR A 66   ? 2.2101 2.9848 1.5260 0.8785  -0.4446 -0.2701 66   TYR A CG  
355   C CD1 . TYR A 66   ? 2.1892 2.9117 1.4922 0.8739  -0.4434 -0.2573 66   TYR A CD1 
356   C CD2 . TYR A 66   ? 2.1626 2.9404 1.4798 0.9162  -0.4555 -0.2676 66   TYR A CD2 
357   C CE1 . TYR A 66   ? 2.1567 2.8291 1.4482 0.9072  -0.4541 -0.2432 66   TYR A CE1 
358   C CE2 . TYR A 66   ? 2.1352 2.8652 1.4407 0.9497  -0.4637 -0.2541 66   TYR A CE2 
359   C CZ  . TYR A 66   ? 2.1202 2.7967 1.4128 0.9457  -0.4637 -0.2425 66   TYR A CZ  
360   O OH  . TYR A 66   ? 2.0754 2.7007 1.3563 0.9799  -0.4712 -0.2305 66   TYR A OH  
361   N N   . SER A 67   ? 2.3618 3.3402 1.7243 0.8344  -0.4327 -0.3354 67   SER A N   
362   C CA  . SER A 67   ? 2.3296 3.3576 1.7062 0.8152  -0.4254 -0.3550 67   SER A CA  
363   C C   . SER A 67   ? 2.2837 3.3425 1.6702 0.8412  -0.4363 -0.3588 67   SER A C   
364   O O   . SER A 67   ? 2.2673 3.3079 1.6493 0.8743  -0.4472 -0.3456 67   SER A O   
365   C CB  . SER A 67   ? 2.3242 3.3134 1.6987 0.7818  -0.4059 -0.3477 67   SER A CB  
366   O OG  . SER A 67   ? 2.3150 3.2384 1.6797 0.7916  -0.4062 -0.3212 67   SER A OG  
367   N N   . SER A 68   ? 2.2668 3.3698 1.6667 0.8251  -0.4310 -0.3772 68   SER A N   
368   C CA  . SER A 68   ? 2.2809 3.4269 1.6928 0.8452  -0.4400 -0.3857 68   SER A CA  
369   C C   . SER A 68   ? 2.2931 3.4614 1.7173 0.8196  -0.4300 -0.4009 68   SER A C   
370   O O   . SER A 68   ? 2.2641 3.4064 1.6860 0.7898  -0.4149 -0.4013 68   SER A O   
371   C CB  . SER A 68   ? 2.3028 3.5152 1.7207 0.8645  -0.4517 -0.4022 68   SER A CB  
372   O OG  . SER A 68   ? 2.3269 3.5758 1.7471 0.8396  -0.4459 -0.4222 68   SER A OG  
373   N N   . GLY A 69   ? 2.3570 3.5717 1.7941 0.8320  -0.4368 -0.4128 69   GLY A N   
374   C CA  . GLY A 69   ? 2.4016 3.6372 1.8512 0.8098  -0.4283 -0.4288 69   GLY A CA  
375   C C   . GLY A 69   ? 2.4199 3.7120 1.8839 0.8249  -0.4373 -0.4429 69   GLY A C   
376   O O   . GLY A 69   ? 2.4125 3.7026 1.8773 0.8528  -0.4459 -0.4298 69   GLY A O   
377   N N   . HIS A 70   ? 2.4296 3.7714 1.9051 0.8058  -0.4330 -0.4700 70   HIS A N   
378   C CA  . HIS A 70   ? 2.4505 3.8498 1.9407 0.8168  -0.4406 -0.4858 70   HIS A CA  
379   C C   . HIS A 70   ? 2.3976 3.7817 1.8974 0.8025  -0.4337 -0.4889 70   HIS A C   
380   O O   . HIS A 70   ? 2.3713 3.7752 1.8798 0.7777  -0.4247 -0.5117 70   HIS A O   
381   C CB  . HIS A 70   ? 2.5334 3.9982 2.0308 0.8039  -0.4399 -0.5160 70   HIS A CB  
382   C CG  . HIS A 70   ? 2.6174 4.1491 2.1248 0.8279  -0.4531 -0.5260 70   HIS A CG  
383   N ND1 . HIS A 70   ? 2.6618 4.2151 2.1637 0.8594  -0.4650 -0.5150 70   HIS A ND1 
384   C CD2 . HIS A 70   ? 2.6564 4.2386 2.1788 0.8256  -0.4550 -0.5457 70   HIS A CD2 
385   C CE1 . HIS A 70   ? 2.6780 4.2948 2.1909 0.8762  -0.4731 -0.5261 70   HIS A CE1 
386   N NE2 . HIS A 70   ? 2.6759 4.3111 2.2015 0.8555  -0.4677 -0.5447 70   HIS A NE2 
387   N N   . VAL A 71   ? 2.3874 3.7362 1.8857 0.8182  -0.4366 -0.4669 71   VAL A N   
388   C CA  . VAL A 71   ? 2.3682 3.6940 1.8741 0.8045  -0.4297 -0.4657 71   VAL A CA  
389   C C   . VAL A 71   ? 2.3637 3.7189 1.8820 0.8215  -0.4365 -0.4663 71   VAL A C   
390   O O   . VAL A 71   ? 2.3497 3.6886 1.8651 0.8446  -0.4403 -0.4458 71   VAL A O   
391   C CB  . VAL A 71   ? 2.3352 3.5934 1.8295 0.8019  -0.4237 -0.4403 71   VAL A CB  
392   C CG1 . VAL A 71   ? 2.3323 3.5621 1.8137 0.7874  -0.4164 -0.4369 71   VAL A CG1 
393   C CG2 . VAL A 71   ? 2.3239 3.5643 1.8121 0.8331  -0.4317 -0.4169 71   VAL A CG2 
394   N N   . HIS A 72   ? 2.3946 3.7920 1.9268 0.8091  -0.4359 -0.4903 72   HIS A N   
395   C CA  . HIS A 72   ? 2.4344 3.8699 1.9791 0.8253  -0.4425 -0.4931 72   HIS A CA  
396   C C   . HIS A 72   ? 2.4219 3.8306 1.9752 0.8168  -0.4373 -0.4870 72   HIS A C   
397   O O   . HIS A 72   ? 2.4106 3.8218 1.9733 0.7935  -0.4318 -0.5053 72   HIS A O   
398   C CB  . HIS A 72   ? 2.5119 4.0123 2.0679 0.8181  -0.4457 -0.5230 72   HIS A CB  
399   C CG  . HIS A 72   ? 2.5747 4.1094 2.1456 0.8268  -0.4496 -0.5284 72   HIS A CG  
400   N ND1 . HIS A 72   ? 2.6060 4.1784 2.1793 0.8573  -0.4576 -0.5184 72   HIS A ND1 
401   C CD2 . HIS A 72   ? 2.5990 4.1336 2.1828 0.8093  -0.4452 -0.5416 72   HIS A CD2 
402   C CE1 . HIS A 72   ? 2.6149 4.2099 2.2022 0.8572  -0.4576 -0.5242 72   HIS A CE1 
403   N NE2 . HIS A 72   ? 2.6103 4.1817 2.2043 0.8279  -0.4511 -0.5388 72   HIS A NE2 
404   N N   . LEU A 73   ? 2.4261 3.8100 1.9765 0.8357  -0.4377 -0.4627 73   LEU A N   
405   C CA  . LEU A 73   ? 2.4442 3.8051 2.0030 0.8280  -0.4321 -0.4556 73   LEU A CA  
406   C C   . LEU A 73   ? 2.4925 3.8984 2.0676 0.8310  -0.4348 -0.4685 73   LEU A C   
407   O O   . LEU A 73   ? 2.4876 3.9454 2.0672 0.8394  -0.4413 -0.4836 73   LEU A O   
408   C CB  . LEU A 73   ? 2.3966 3.7208 1.9474 0.8465  -0.4288 -0.4270 73   LEU A CB  
409   C CG  . LEU A 73   ? 2.3757 3.7133 1.9166 0.8787  -0.4336 -0.4146 73   LEU A CG  
410   C CD1 . LEU A 73   ? 2.3516 3.6703 1.8904 0.9008  -0.4270 -0.3918 73   LEU A CD1 
411   C CD2 . LEU A 73   ? 2.3775 3.6876 1.9031 0.8764  -0.4355 -0.4107 73   LEU A CD2 
412   N N   . SER A 74   ? 2.5497 3.9356 2.1335 0.8234  -0.4293 -0.4621 74   SER A N   
413   C CA  . SER A 74   ? 2.5947 4.0137 2.1946 0.8233  -0.4300 -0.4717 74   SER A CA  
414   C C   . SER A 74   ? 2.6368 4.0157 2.2426 0.8112  -0.4217 -0.4595 74   SER A C   
415   O O   . SER A 74   ? 2.6707 4.0035 2.2683 0.8033  -0.4162 -0.4464 74   SER A O   
416   C CB  . SER A 74   ? 2.5849 4.0344 2.1941 0.8029  -0.4328 -0.5037 74   SER A CB  
417   O OG  . SER A 74   ? 2.5663 3.9766 2.1764 0.7744  -0.4257 -0.5135 74   SER A OG  
418   N N   . SER A 75   ? 2.6712 4.0679 2.2914 0.8092  -0.4201 -0.4634 75   SER A N   
419   C CA  . SER A 75   ? 2.7106 4.0699 2.3383 0.7938  -0.4115 -0.4541 75   SER A CA  
420   C C   . SER A 75   ? 2.7214 4.0472 2.3507 0.7633  -0.4091 -0.4692 75   SER A C   
421   O O   . SER A 75   ? 2.7002 3.9893 2.3335 0.7483  -0.4021 -0.4616 75   SER A O   
422   C CB  . SER A 75   ? 2.7613 4.1467 2.4049 0.7962  -0.4099 -0.4563 75   SER A CB  
423   O OG  . SER A 75   ? 2.7879 4.1813 2.4301 0.8203  -0.4032 -0.4321 75   SER A OG  
424   N N   . GLU A 76   ? 2.7240 4.0638 2.3501 0.7546  -0.4130 -0.4907 76   GLU A N   
425   C CA  . GLU A 76   ? 2.6972 4.0093 2.3239 0.7280  -0.4073 -0.5074 76   GLU A CA  
426   C C   . GLU A 76   ? 2.6226 3.8926 2.2344 0.7238  -0.4019 -0.4915 76   GLU A C   
427   O O   . GLU A 76   ? 2.6316 3.8649 2.2432 0.7053  -0.3940 -0.4913 76   GLU A O   
428   C CB  . GLU A 76   ? 2.7328 4.0809 2.3622 0.7205  -0.4095 -0.5382 76   GLU A CB  
429   C CG  . GLU A 76   ? 2.7415 4.0639 2.3688 0.6959  -0.3994 -0.5567 76   GLU A CG  
430   C CD  . GLU A 76   ? 2.7494 4.1096 2.3767 0.6898  -0.3984 -0.5862 76   GLU A CD  
431   O OE1 . GLU A 76   ? 2.7503 4.1535 2.3754 0.7061  -0.4073 -0.5874 76   GLU A OE1 
432   O OE2 . GLU A 76   ? 2.7498 4.0976 2.3793 0.6690  -0.3870 -0.6086 76   GLU A OE2 
433   N N   . ASN A 77   ? 2.5100 3.7866 2.1092 0.7420  -0.4060 -0.4783 77   ASN A N   
434   C CA  . ASN A 77   ? 2.4112 3.6502 1.9952 0.7423  -0.4022 -0.4603 77   ASN A CA  
435   C C   . ASN A 77   ? 2.2395 3.4576 1.8191 0.7581  -0.4012 -0.4325 77   ASN A C   
436   O O   . ASN A 77   ? 2.1818 3.3793 1.7480 0.7689  -0.4008 -0.4153 77   ASN A O   
437   C CB  . ASN A 77   ? 2.4797 3.7366 2.0524 0.7527  -0.4068 -0.4637 77   ASN A CB  
438   C CG  . ASN A 77   ? 2.5772 3.7955 2.1356 0.7432  -0.4004 -0.4544 77   ASN A CG  
439   O OD1 . ASN A 77   ? 2.6112 3.7902 2.1662 0.7336  -0.3935 -0.4410 77   ASN A OD1 
440   N ND2 . ASN A 77   ? 2.6109 3.8415 2.1607 0.7455  -0.4018 -0.4607 77   ASN A ND2 
441   N N   . LYS A 78   ? 2.1602 3.3835 1.7514 0.7590  -0.3992 -0.4288 78   LYS A N   
442   C CA  . LYS A 78   ? 2.0464 3.2560 1.6351 0.7740  -0.3944 -0.4047 78   LYS A CA  
443   C C   . LYS A 78   ? 1.9684 3.1862 1.5446 0.8017  -0.3972 -0.3912 78   LYS A C   
444   O O   . LYS A 78   ? 1.9487 3.1437 1.5172 0.8134  -0.3908 -0.3712 78   LYS A O   
445   C CB  . LYS A 78   ? 1.9408 3.1056 1.5258 0.7583  -0.3860 -0.3915 78   LYS A CB  
446   C CG  . LYS A 78   ? 1.8299 2.9839 1.4274 0.7326  -0.3824 -0.4036 78   LYS A CG  
447   C CD  . LYS A 78   ? 1.6860 2.8630 1.2990 0.7341  -0.3820 -0.4087 78   LYS A CD  
448   C CE  . LYS A 78   ? 1.6113 2.7717 1.2366 0.7084  -0.3784 -0.4208 78   LYS A CE  
449   N NZ  . LYS A 78   ? 1.5818 2.7682 1.2228 0.7076  -0.3805 -0.4330 78   LYS A NZ  
450   N N   . PHE A 79   ? 1.9518 3.2029 1.5261 0.8121  -0.4057 -0.4038 79   PHE A N   
451   C CA  . PHE A 79   ? 1.9415 3.2032 1.5043 0.8395  -0.4094 -0.3936 79   PHE A CA  
452   C C   . PHE A 79   ? 1.9698 3.1859 1.5173 0.8381  -0.4064 -0.3789 79   PHE A C   
453   O O   . PHE A 79   ? 1.9843 3.1782 1.5249 0.8527  -0.4002 -0.3600 79   PHE A O   
454   C CB  . PHE A 79   ? 1.9193 3.1976 1.4853 0.8653  -0.4042 -0.3793 79   PHE A CB  
455   C CG  . PHE A 79   ? 1.9461 3.2753 1.5260 0.8716  -0.4075 -0.3916 79   PHE A CG  
456   C CD1 . PHE A 79   ? 1.9280 3.2614 1.5209 0.8661  -0.3998 -0.3882 79   PHE A CD1 
457   C CD2 . PHE A 79   ? 1.9571 3.3306 1.5372 0.8817  -0.4178 -0.4064 79   PHE A CD2 
458   C CE1 . PHE A 79   ? 1.9205 3.2994 1.5260 0.8718  -0.4025 -0.3981 79   PHE A CE1 
459   C CE2 . PHE A 79   ? 1.9522 3.3752 1.5448 0.8875  -0.4209 -0.4175 79   PHE A CE2 
460   C CZ  . PHE A 79   ? 1.9316 3.3565 1.5369 0.8830  -0.4135 -0.4129 79   PHE A CZ  
461   N N   . GLN A 80   ? 2.0078 3.2103 1.5501 0.8196  -0.4086 -0.3883 80   GLN A N   
462   C CA  . GLN A 80   ? 2.0413 3.2007 1.5689 0.8150  -0.4056 -0.3750 80   GLN A CA  
463   C C   . GLN A 80   ? 2.0380 3.1991 1.5605 0.8004  -0.4077 -0.3885 80   GLN A C   
464   O O   . GLN A 80   ? 2.0421 3.2244 1.5739 0.7830  -0.4069 -0.4090 80   GLN A O   
465   C CB  . GLN A 80   ? 2.0656 3.1890 1.5945 0.7966  -0.3969 -0.3656 80   GLN A CB  
466   C CG  . GLN A 80   ? 2.0727 3.1956 1.6094 0.8030  -0.3913 -0.3555 80   GLN A CG  
467   C CD  . GLN A 80   ? 2.0723 3.1564 1.6054 0.7893  -0.3826 -0.3415 80   GLN A CD  
468   O OE1 . GLN A 80   ? 2.0748 3.1398 1.6063 0.7684  -0.3805 -0.3444 80   GLN A OE1 
469   N NE2 . GLN A 80   ? 2.0638 3.1381 1.5956 0.8012  -0.3754 -0.3263 80   GLN A NE2 
470   N N   . ASN A 81   ? 2.0461 3.1830 1.5538 0.8063  -0.4083 -0.3775 81   ASN A N   
471   C CA  . ASN A 81   ? 2.0712 3.2104 1.5737 0.7923  -0.4074 -0.3891 81   ASN A CA  
472   C C   . ASN A 81   ? 2.0376 3.1371 1.5229 0.7956  -0.4056 -0.3717 81   ASN A C   
473   O O   . ASN A 81   ? 2.0117 3.0826 1.4886 0.8110  -0.4065 -0.3519 81   ASN A O   
474   C CB  . ASN A 81   ? 2.1266 3.3173 1.6350 0.8007  -0.4151 -0.4084 81   ASN A CB  
475   C CG  . ASN A 81   ? 2.1707 3.3836 1.6860 0.7756  -0.4099 -0.4338 81   ASN A CG  
476   O OD1 . ASN A 81   ? 2.1780 3.3640 1.6875 0.7552  -0.3997 -0.4349 81   ASN A OD1 
477   N ND2 . ASN A 81   ? 2.1875 3.4505 1.7149 0.7776  -0.4149 -0.4547 81   ASN A ND2 
478   N N   . SER A 82   ? 2.0462 3.1429 1.5261 0.7807  -0.4015 -0.3796 82   SER A N   
479   C CA  . SER A 82   ? 2.0657 3.1203 1.5297 0.7801  -0.3979 -0.3620 82   SER A CA  
480   C C   . SER A 82   ? 2.1097 3.1749 1.5675 0.7754  -0.3976 -0.3708 82   SER A C   
481   O O   . SER A 82   ? 2.1313 3.2333 1.5971 0.7627  -0.3950 -0.3935 82   SER A O   
482   C CB  . SER A 82   ? 2.0758 3.0935 1.5365 0.7588  -0.3852 -0.3525 82   SER A CB  
483   O OG  . SER A 82   ? 2.0803 3.0596 1.5319 0.7696  -0.3859 -0.3285 82   SER A OG  
484   N N   . ALA A 83   ? 2.1205 3.1527 1.5639 0.7848  -0.3993 -0.3537 83   ALA A N   
485   C CA  . ALA A 83   ? 2.1250 3.1644 1.5619 0.7806  -0.3988 -0.3601 83   ALA A CA  
486   C C   . ALA A 83   ? 2.1620 3.1459 1.5828 0.7743  -0.3917 -0.3388 83   ALA A C   
487   O O   . ALA A 83   ? 2.1880 3.1322 1.6002 0.7878  -0.3948 -0.3174 83   ALA A O   
488   C CB  . ALA A 83   ? 2.1205 3.1920 1.5583 0.8076  -0.4133 -0.3648 83   ALA A CB  
489   N N   . ILE A 84   ? 2.1367 3.1177 1.5533 0.7528  -0.3804 -0.3450 84   ILE A N   
490   C CA  . ILE A 84   ? 2.1242 3.0536 1.5252 0.7465  -0.3729 -0.3242 84   ILE A CA  
491   C C   . ILE A 84   ? 2.1186 3.0489 1.5119 0.7589  -0.3817 -0.3235 84   ILE A C   
492   O O   . ILE A 84   ? 2.1154 3.0576 1.5071 0.7415  -0.3731 -0.3338 84   ILE A O   
493   C CB  . ILE A 84   ? 2.8787 3.7916 2.2773 0.7138  -0.3495 -0.3249 84   ILE A CB  
494   C CG1 . ILE A 84   ? 2.8809 3.8410 2.2884 0.6948  -0.3398 -0.3540 84   ILE A CG1 
495   C CG2 . ILE A 84   ? 2.8639 3.7621 2.2664 0.7056  -0.3409 -0.3179 84   ILE A CG2 
496   C CD1 . ILE A 84   ? 2.8806 3.8222 2.2832 0.6640  -0.3124 -0.3545 84   ILE A CD1 
497   N N   . LEU A 85   ? 2.0924 3.0099 1.4809 0.7890  -0.3971 -0.3120 85   LEU A N   
498   C CA  . LEU A 85   ? 2.0661 2.9697 1.4446 0.8045  -0.4053 -0.3058 85   LEU A CA  
499   C C   . LEU A 85   ? 2.0106 2.8563 1.3754 0.7870  -0.3936 -0.2869 85   LEU A C   
500   O O   . LEU A 85   ? 2.0122 2.8375 1.3763 0.7650  -0.3791 -0.2801 85   LEU A O   
501   C CB  . LEU A 85   ? 2.0601 2.9490 1.4345 0.8411  -0.4194 -0.2942 85   LEU A CB  
502   C CG  . LEU A 85   ? 2.0515 2.9964 1.4396 0.8593  -0.4280 -0.3098 85   LEU A CG  
503   C CD1 . LEU A 85   ? 2.0633 3.0689 1.4616 0.8465  -0.4285 -0.3346 85   LEU A CD1 
504   C CD2 . LEU A 85   ? 2.0298 2.9759 1.4262 0.8525  -0.4229 -0.3085 85   LEU A CD2 
505   N N   . THR A 86   ? 1.9743 2.7918 1.3280 0.7970  -0.3987 -0.2772 86   THR A N   
506   C CA  . THR A 86   ? 1.9429 2.7003 1.2830 0.7801  -0.3868 -0.2565 86   THR A CA  
507   C C   . THR A 86   ? 1.9507 2.6813 1.2798 0.7878  -0.3922 -0.2495 86   THR A C   
508   O O   . THR A 86   ? 1.9322 2.6902 1.2633 0.7746  -0.3888 -0.2631 86   THR A O   
509   C CB  . THR A 86   ? 1.7610 2.5248 1.1044 0.7423  -0.3643 -0.2615 86   THR A CB  
510   O OG1 . THR A 86   ? 1.7725 2.4759 1.1044 0.7302  -0.3513 -0.2356 86   THR A OG1 
511   C CG2 . THR A 86   ? 1.7682 2.5610 1.1134 0.7221  -0.3551 -0.2784 86   THR A CG2 
512   N N   . ILE A 87   ? 1.9385 2.6147 1.2560 0.8093  -0.4001 -0.2291 87   ILE A N   
513   C CA  . ILE A 87   ? 1.9675 2.6064 1.2733 0.8200  -0.4060 -0.2197 87   ILE A CA  
514   C C   . ILE A 87   ? 2.1840 2.7754 1.4798 0.7892  -0.3894 -0.2041 87   ILE A C   
515   O O   . ILE A 87   ? 2.2441 2.7814 1.5310 0.7840  -0.3822 -0.1822 87   ILE A O   
516   C CB  . ILE A 87   ? 1.8086 2.3975 1.1045 0.8526  -0.4170 -0.2031 87   ILE A CB  
517   C CG1 . ILE A 87   ? 1.7369 2.3656 1.0420 0.8815  -0.4276 -0.2144 87   ILE A CG1 
518   C CG2 . ILE A 87   ? 1.7523 2.3038 1.0367 0.8678  -0.4246 -0.1962 87   ILE A CG2 
519   C CD1 . ILE A 87   ? 1.7141 2.3004 1.0097 0.9170  -0.4359 -0.2028 87   ILE A CD1 
520   N N   . GLN A 88   ? 2.3071 2.9197 1.6042 0.7682  -0.3816 -0.2149 88   GLN A N   
521   C CA  . GLN A 88   ? 2.4166 2.9821 1.7036 0.7385  -0.3628 -0.1990 88   GLN A CA  
522   C C   . GLN A 88   ? 2.5595 3.0670 1.8329 0.7543  -0.3726 -0.1823 88   GLN A C   
523   O O   . GLN A 88   ? 2.5630 3.0649 1.8345 0.7895  -0.3924 -0.1828 88   GLN A O   
524   C CB  . GLN A 88   ? 2.4332 3.0457 1.7272 0.7072  -0.3467 -0.2189 88   GLN A CB  
525   C CG  . GLN A 88   ? 2.4281 3.1036 1.7367 0.6952  -0.3390 -0.2414 88   GLN A CG  
526   C CD  . GLN A 88   ? 2.4416 3.1231 1.7513 0.6543  -0.3083 -0.2462 88   GLN A CD  
527   O OE1 . GLN A 88   ? 2.4440 3.1812 1.7654 0.6397  -0.2984 -0.2705 88   GLN A OE1 
528   N NE2 . GLN A 88   ? 2.4381 3.0599 1.7352 0.6354  -0.2908 -0.2228 88   GLN A NE2 
529   N N   . PRO A 89   ? 2.6441 3.1050 1.9076 0.7287  -0.3569 -0.1668 89   PRO A N   
530   C CA  . PRO A 89   ? 2.7065 3.1126 1.9575 0.7361  -0.3631 -0.1530 89   PRO A CA  
531   C C   . PRO A 89   ? 2.6570 3.0995 1.9109 0.7513  -0.3781 -0.1721 89   PRO A C   
532   O O   . PRO A 89   ? 2.5763 3.0713 1.8376 0.7303  -0.3701 -0.1912 89   PRO A O   
533   C CB  . PRO A 89   ? 2.7246 3.0899 1.9681 0.6955  -0.3359 -0.1360 89   PRO A CB  
534   C CG  . PRO A 89   ? 2.7091 3.0749 1.9555 0.6813  -0.3201 -0.1275 89   PRO A CG  
535   C CD  . PRO A 89   ? 2.6761 3.1165 1.9375 0.6941  -0.3301 -0.1537 89   PRO A CD  
536   N N   . LYS A 90   ? 2.7460 3.1589 1.9933 0.7884  -0.3984 -0.1668 90   LYS A N   
537   C CA  . LYS A 90   ? 2.8028 3.2428 2.0510 0.8090  -0.4134 -0.1811 90   LYS A CA  
538   C C   . LYS A 90   ? 2.9714 3.3315 2.2043 0.8246  -0.4204 -0.1618 90   LYS A C   
539   O O   . LYS A 90   ? 2.9784 3.3094 2.2049 0.8018  -0.4119 -0.1549 90   LYS A O   
540   C CB  . LYS A 90   ? 2.6446 3.1404 1.9018 0.8478  -0.4316 -0.1983 90   LYS A CB  
541   C CG  . LYS A 90   ? 2.5017 3.0745 1.7743 0.8353  -0.4268 -0.2181 90   LYS A CG  
542   C CD  . LYS A 90   ? 2.4007 3.0320 1.6812 0.8052  -0.4175 -0.2379 90   LYS A CD  
543   C CE  . LYS A 90   ? 2.3456 3.0405 1.6403 0.7866  -0.4083 -0.2560 90   LYS A CE  
544   N NZ  . LYS A 90   ? 2.3416 3.1235 1.6485 0.7844  -0.4123 -0.2853 90   LYS A NZ  
545   N N   . GLN A 91   ? 3.1632 3.4861 2.3901 0.8629  -0.4341 -0.1536 91   GLN A N   
546   C CA  . GLN A 91   ? 3.3928 3.6319 2.6045 0.8802  -0.4402 -0.1356 91   GLN A CA  
547   C C   . GLN A 91   ? 3.6064 3.7659 2.8070 0.8518  -0.4254 -0.1086 91   GLN A C   
548   O O   . GLN A 91   ? 3.6190 3.7515 2.8173 0.8532  -0.4213 -0.0962 91   GLN A O   
549   C CB  . GLN A 91   ? 3.4230 3.6431 2.6309 0.9291  -0.4550 -0.1359 91   GLN A CB  
550   C CG  . GLN A 91   ? 3.4718 3.7432 2.6846 0.9642  -0.4692 -0.1556 91   GLN A CG  
551   C CD  . GLN A 91   ? 3.5197 3.8077 2.7322 0.9496  -0.4705 -0.1624 91   GLN A CD  
552   O OE1 . GLN A 91   ? 3.5284 3.8870 2.7517 0.9250  -0.4660 -0.1779 91   GLN A OE1 
553   N NE2 . GLN A 91   ? 3.5464 3.7691 2.7463 0.9643  -0.4760 -0.1519 91   GLN A NE2 
554   N N   . LEU A 92   ? 3.8219 3.9453 3.0158 0.8259  -0.4165 -0.0989 92   LEU A N   
555   C CA  . LEU A 92   ? 4.0207 4.0642 3.2032 0.7983  -0.4005 -0.0706 92   LEU A CA  
556   C C   . LEU A 92   ? 4.1760 4.1246 3.3427 0.8158  -0.4085 -0.0513 92   LEU A C   
557   O O   . LEU A 92   ? 4.1876 4.0644 3.3441 0.7956  -0.3961 -0.0258 92   LEU A O   
558   C CB  . LEU A 92   ? 4.0767 4.1376 3.2620 0.7490  -0.3773 -0.0692 92   LEU A CB  
559   C CG  . LEU A 92   ? 4.1045 4.2351 3.3022 0.7208  -0.3598 -0.0812 92   LEU A CG  
560   C CD1 . LEU A 92   ? 4.1246 4.2698 3.3239 0.6751  -0.3349 -0.0831 92   LEU A CD1 
561   C CD2 . LEU A 92   ? 4.1073 4.2100 3.3026 0.7159  -0.3499 -0.0629 92   LEU A CD2 
562   N N   . PRO A 93   ? 4.2941 4.2401 3.4586 0.8541  -0.4279 -0.0629 93   PRO A N   
563   C CA  . PRO A 93   ? 4.3875 4.2394 3.5368 0.8673  -0.4334 -0.0457 93   PRO A CA  
564   C C   . PRO A 93   ? 4.4589 4.2342 3.5975 0.8806  -0.4330 -0.0251 93   PRO A C   
565   O O   . PRO A 93   ? 4.4708 4.2551 3.6104 0.9158  -0.4430 -0.0330 93   PRO A O   
566   C CB  . PRO A 93   ? 4.3770 4.2520 3.5273 0.9120  -0.4532 -0.0652 93   PRO A CB  
567   C CG  . PRO A 93   ? 4.3549 4.3411 3.5213 0.9118  -0.4558 -0.0911 93   PRO A CG  
568   C CD  . PRO A 93   ? 4.3232 4.3422 3.4973 0.8892  -0.4440 -0.0891 93   PRO A CD  
569   N N   . GLY A 94   ? 4.5129 4.2149 3.6415 0.8520  -0.4197 0.0012  94   GLY A N   
570   C CA  . GLY A 94   ? 4.5529 4.1775 3.6701 0.8634  -0.4193 0.0221  94   GLY A CA  
571   C C   . GLY A 94   ? 4.5943 4.1620 3.7018 0.9079  -0.4365 0.0181  94   GLY A C   
572   O O   . GLY A 94   ? 4.6204 4.1620 3.7236 0.9143  -0.4429 0.0151  94   GLY A O   
573   N N   . GLY A 95   ? 4.6083 4.1566 3.7122 0.9387  -0.4425 0.0172  95   GLY A N   
574   C CA  . GLY A 95   ? 4.6192 4.1159 3.7140 0.9844  -0.4555 0.0104  95   GLY A CA  
575   C C   . GLY A 95   ? 4.6177 4.1853 3.7214 1.0236  -0.4656 -0.0172 95   GLY A C   
576   O O   . GLY A 95   ? 4.6125 4.1686 3.7135 1.0563  -0.4681 -0.0232 95   GLY A O   
577   N N   . GLN A 96   ? 4.6013 4.2434 3.7158 1.0205  -0.4697 -0.0340 96   GLN A N   
578   C CA  . GLN A 96   ? 4.5695 4.2881 3.6940 1.0544  -0.4770 -0.0583 96   GLN A CA  
579   C C   . GLN A 96   ? 4.5825 4.3307 3.7128 1.0504  -0.4706 -0.0579 96   GLN A C   
580   O O   . GLN A 96   ? 4.6027 4.3613 3.7365 1.0121  -0.4612 -0.0465 96   GLN A O   
581   C CB  . GLN A 96   ? 4.5123 4.3222 3.6501 1.0403  -0.4796 -0.0748 96   GLN A CB  
582   C CG  . GLN A 96   ? 4.4642 4.3620 3.6142 1.0690  -0.4846 -0.0973 96   GLN A CG  
583   C CD  . GLN A 96   ? 4.4482 4.4333 3.6100 1.0619  -0.4891 -0.1152 96   GLN A CD  
584   O OE1 . GLN A 96   ? 4.4496 4.4354 3.6114 1.0318  -0.4871 -0.1124 96   GLN A OE1 
585   N NE2 . GLN A 96   ? 4.4383 4.4988 3.6104 1.0888  -0.4936 -0.1338 96   GLN A NE2 
586   N N   . ASN A 97   ? 4.5656 4.3233 3.6961 1.0897  -0.4735 -0.0695 97   ASN A N   
587   C CA  . ASN A 97   ? 4.5233 4.3215 3.6612 1.0869  -0.4674 -0.0724 97   ASN A CA  
588   C C   . ASN A 97   ? 4.4284 4.3305 3.5833 1.0777  -0.4687 -0.0895 97   ASN A C   
589   O O   . ASN A 97   ? 4.4285 4.3803 3.5901 1.1087  -0.4718 -0.1066 97   ASN A O   
590   C CB  . ASN A 97   ? 4.5778 4.3498 3.7099 1.1308  -0.4667 -0.0798 97   ASN A CB  
591   C CG  . ASN A 97   ? 4.6253 4.2921 3.7401 1.1431  -0.4656 -0.0661 97   ASN A CG  
592   O OD1 . ASN A 97   ? 4.6456 4.2588 3.7533 1.1133  -0.4638 -0.0466 97   ASN A OD1 
593   N ND2 . ASN A 97   ? 4.6402 4.2756 3.7480 1.1874  -0.4646 -0.0763 97   ASN A ND2 
594   N N   . PRO A 98   ? 4.3144 4.2490 3.4762 1.0350  -0.4643 -0.0850 98   PRO A N   
595   C CA  . PRO A 98   ? 4.1951 4.2242 3.3722 1.0256  -0.4661 -0.1033 98   PRO A CA  
596   C C   . PRO A 98   ? 3.9938 4.0760 3.1815 1.0248  -0.4619 -0.1104 98   PRO A C   
597   O O   . PRO A 98   ? 4.0029 4.0475 3.1856 1.0259  -0.4567 -0.0994 98   PRO A O   
598   C CB  . PRO A 98   ? 4.2535 4.2852 3.4323 0.9771  -0.4578 -0.0945 98   PRO A CB  
599   C CG  . PRO A 98   ? 4.2931 4.2324 3.4580 0.9602  -0.4499 -0.0681 98   PRO A CG  
600   C CD  . PRO A 98   ? 4.3099 4.2059 3.4675 0.9938  -0.4537 -0.0640 98   PRO A CD  
601   N N   . VAL A 99   ? 3.7786 3.9465 2.9807 1.0230  -0.4639 -0.1286 99   VAL A N   
602   C CA  . VAL A 99   ? 3.5640 3.7811 2.7774 1.0076  -0.4578 -0.1330 99   VAL A CA  
603   C C   . VAL A 99   ? 3.3214 3.5319 2.5342 1.0372  -0.4571 -0.1342 99   VAL A C   
604   O O   . VAL A 99   ? 3.3062 3.5725 2.5306 1.0358  -0.4546 -0.1438 99   VAL A O   
605   C CB  . VAL A 99   ? 3.6096 3.7977 2.8203 0.9644  -0.4463 -0.1161 99   VAL A CB  
606   C CG1 . VAL A 99   ? 3.6190 3.8496 2.8399 0.9487  -0.4390 -0.1187 99   VAL A CG1 
607   C CG2 . VAL A 99   ? 3.6276 3.8279 2.8398 0.9323  -0.4419 -0.1166 99   VAL A CG2 
608   N N   . SER A 100  ? 3.0858 3.2281 2.2855 1.0634  -0.4579 -0.1255 100  SER A N   
609   C CA  . SER A 100  ? 2.8472 2.9798 2.0453 1.0899  -0.4535 -0.1275 100  SER A CA  
610   C C   . SER A 100  ? 2.6472 2.8512 1.8569 1.1160  -0.4550 -0.1467 100  SER A C   
611   O O   . SER A 100  ? 2.6837 2.8926 1.8912 1.1472  -0.4595 -0.1552 100  SER A O   
612   C CB  . SER A 100  ? 2.8063 2.8579 1.9883 1.1198  -0.4534 -0.1203 100  SER A CB  
613   O OG  . SER A 100  ? 2.7915 2.7885 1.9637 1.1063  -0.4578 -0.1084 100  SER A OG  
614   N N   . TYR A 101  ? 2.4125 2.6714 1.6345 1.1035  -0.4503 -0.1527 101  TYR A N   
615   C CA  . TYR A 101  ? 2.2243 2.5523 1.4582 1.1254  -0.4500 -0.1692 101  TYR A CA  
616   C C   . TYR A 101  ? 2.1185 2.5179 1.3650 1.1109  -0.4571 -0.1813 101  TYR A C   
617   O O   . TYR A 101  ? 2.1234 2.5183 1.3666 1.1060  -0.4639 -0.1819 101  TYR A O   
618   C CB  . TYR A 101  ? 2.1742 2.4816 1.4006 1.1735  -0.4484 -0.1744 101  TYR A CB  
619   C CG  . TYR A 101  ? 2.1435 2.4048 1.3619 1.1933  -0.4369 -0.1701 101  TYR A CG  
620   C CD1 . TYR A 101  ? 2.1467 2.4440 1.3716 1.2163  -0.4263 -0.1794 101  TYR A CD1 
621   C CD2 . TYR A 101  ? 2.1369 2.3196 1.3414 1.1877  -0.4349 -0.1570 101  TYR A CD2 
622   C CE1 . TYR A 101  ? 2.1510 2.4095 1.3689 1.2327  -0.4127 -0.1774 101  TYR A CE1 
623   C CE2 . TYR A 101  ? 2.1437 2.2873 1.3409 1.2053  -0.4231 -0.1554 101  TYR A CE2 
624   C CZ  . TYR A 101  ? 2.1560 2.3393 1.3601 1.2276  -0.4113 -0.1666 101  TYR A CZ  
625   O OH  . TYR A 101  ? 2.1603 2.3101 1.3578 1.2440  -0.3961 -0.1674 101  TYR A OH  
626   N N   . VAL A 102  ? 2.0523 2.5176 1.3132 1.1036  -0.4547 -0.1917 102  VAL A N   
627   C CA  . VAL A 102  ? 1.9985 2.5380 1.2723 1.0950  -0.4606 -0.2063 102  VAL A CA  
628   C C   . VAL A 102  ? 2.0072 2.6065 1.2933 1.1123  -0.4573 -0.2175 102  VAL A C   
629   O O   . VAL A 102  ? 1.9976 2.5789 1.2818 1.1304  -0.4490 -0.2136 102  VAL A O   
630   C CB  . VAL A 102  ? 1.9416 2.5042 1.2228 1.0487  -0.4599 -0.2077 102  VAL A CB  
631   C CG1 . VAL A 102  ? 1.9201 2.4177 1.1892 1.0252  -0.4577 -0.1923 102  VAL A CG1 
632   C CG2 . VAL A 102  ? 1.9140 2.5029 1.2054 1.0324  -0.4529 -0.2094 102  VAL A CG2 
633   N N   . TYR A 103  ? 2.0429 2.7136 1.3417 1.1046  -0.4622 -0.2316 103  TYR A N   
634   C CA  . TYR A 103  ? 2.0466 2.7804 1.3582 1.1216  -0.4597 -0.2424 103  TYR A CA  
635   C C   . TYR A 103  ? 2.0109 2.7984 1.3378 1.0872  -0.4596 -0.2522 103  TYR A C   
636   O O   . TYR A 103  ? 1.9409 2.7574 1.2727 1.0618  -0.4648 -0.2608 103  TYR A O   
637   C CB  . TYR A 103  ? 2.1928 2.9677 1.5054 1.1565  -0.4650 -0.2511 103  TYR A CB  
638   C CG  . TYR A 103  ? 2.2937 3.0319 1.5955 1.2028  -0.4585 -0.2443 103  TYR A CG  
639   C CD1 . TYR A 103  ? 2.3771 3.0411 1.6627 1.2138  -0.4589 -0.2342 103  TYR A CD1 
640   C CD2 . TYR A 103  ? 2.3506 3.1263 1.6580 1.2358  -0.4496 -0.2483 103  TYR A CD2 
641   C CE1 . TYR A 103  ? 2.4273 3.0546 1.7025 1.2571  -0.4507 -0.2301 103  TYR A CE1 
642   C CE2 . TYR A 103  ? 2.3993 3.1404 1.6963 1.2793  -0.4392 -0.2431 103  TYR A CE2 
643   C CZ  . TYR A 103  ? 2.4430 3.1092 1.7238 1.2900  -0.4399 -0.2351 103  TYR A CZ  
644   O OH  . TYR A 103  ? 2.4749 3.1020 1.7447 1.3333  -0.4278 -0.2318 103  TYR A OH  
645   N N   . LEU A 104  ? 2.0122 2.8084 1.3461 1.0857  -0.4519 -0.2512 104  LEU A N   
646   C CA  . LEU A 104  ? 2.0130 2.8581 1.3620 1.0582  -0.4506 -0.2610 104  LEU A CA  
647   C C   . LEU A 104  ? 2.0142 2.9261 1.3743 1.0801  -0.4529 -0.2734 104  LEU A C   
648   O O   . LEU A 104  ? 1.9789 2.8906 1.3360 1.1160  -0.4488 -0.2699 104  LEU A O   
649   C CB  . LEU A 104  ? 1.9980 2.8201 1.3492 1.0470  -0.4409 -0.2532 104  LEU A CB  
650   C CG  . LEU A 104  ? 1.9500 2.8056 1.3151 1.0143  -0.4382 -0.2606 104  LEU A CG  
651   C CD1 . LEU A 104  ? 1.9434 2.8000 1.3093 0.9784  -0.4408 -0.2650 104  LEU A CD1 
652   C CD2 . LEU A 104  ? 1.9228 2.7489 1.2875 1.0074  -0.4285 -0.2506 104  LEU A CD2 
653   N N   . GLU A 105  ? 2.0353 3.0040 1.4080 1.0593  -0.4576 -0.2881 105  GLU A N   
654   C CA  . GLU A 105  ? 2.0788 3.1161 1.4629 1.0781  -0.4601 -0.3000 105  GLU A CA  
655   C C   . GLU A 105  ? 2.0764 3.1607 1.4766 1.0510  -0.4592 -0.3128 105  GLU A C   
656   O O   . GLU A 105  ? 2.0745 3.1543 1.4776 1.0156  -0.4594 -0.3188 105  GLU A O   
657   C CB  . GLU A 105  ? 2.1194 3.1898 1.5012 1.0895  -0.4698 -0.3087 105  GLU A CB  
658   C CG  . GLU A 105  ? 2.1408 3.2766 1.5305 1.1215  -0.4717 -0.3163 105  GLU A CG  
659   C CD  . GLU A 105  ? 2.1738 3.3330 1.5578 1.1403  -0.4806 -0.3212 105  GLU A CD  
660   O OE1 . GLU A 105  ? 2.1849 3.3748 1.5724 1.1154  -0.4879 -0.3341 105  GLU A OE1 
661   O OE2 . GLU A 105  ? 2.1866 3.3338 1.5624 1.1801  -0.4785 -0.3127 105  GLU A OE2 
662   N N   . VAL A 106  ? 2.0655 3.1939 1.4762 1.0688  -0.4563 -0.3168 106  VAL A N   
663   C CA  . VAL A 106  ? 2.0618 3.2378 1.4886 1.0471  -0.4561 -0.3301 106  VAL A CA  
664   C C   . VAL A 106  ? 2.0674 3.3127 1.5033 1.0704  -0.4600 -0.3400 106  VAL A C   
665   O O   . VAL A 106  ? 2.0749 3.3256 1.5050 1.1071  -0.4586 -0.3323 106  VAL A O   
666   C CB  . VAL A 106  ? 2.0539 3.2077 1.4856 1.0408  -0.4459 -0.3219 106  VAL A CB  
667   C CG1 . VAL A 106  ? 2.0534 3.2556 1.5023 1.0214  -0.4458 -0.3358 106  VAL A CG1 
668   C CG2 . VAL A 106  ? 2.0612 3.1524 1.4841 1.0173  -0.4422 -0.3122 106  VAL A CG2 
669   N N   . VAL A 107  ? 2.0669 3.3654 1.5166 1.0502  -0.4639 -0.3573 107  VAL A N   
670   C CA  . VAL A 107  ? 2.0631 3.4344 1.5217 1.0686  -0.4691 -0.3686 107  VAL A CA  
671   C C   . VAL A 107  ? 2.0345 3.4465 1.5101 1.0523  -0.4667 -0.3798 107  VAL A C   
672   O O   . VAL A 107  ? 2.0261 3.4198 1.5069 1.0189  -0.4646 -0.3865 107  VAL A O   
673   C CB  . VAL A 107  ? 2.1488 3.5537 1.6053 1.0590  -0.4794 -0.3840 107  VAL A CB  
674   C CG1 . VAL A 107  ? 2.1481 3.6288 1.6113 1.0848  -0.4852 -0.3930 107  VAL A CG1 
675   C CG2 . VAL A 107  ? 2.1576 3.5091 1.5972 1.0648  -0.4814 -0.3731 107  VAL A CG2 
676   N N   . SER A 108  ? 2.0523 3.5175 1.5364 1.0769  -0.4658 -0.3808 108  SER A N   
677   C CA  . SER A 108  ? 2.0748 3.5798 1.5754 1.0636  -0.4637 -0.3908 108  SER A CA  
678   C C   . SER A 108  ? 2.1508 3.7294 1.6589 1.0914  -0.4664 -0.3954 108  SER A C   
679   O O   . SER A 108  ? 2.1685 3.7740 1.6698 1.1136  -0.4724 -0.3962 108  SER A O   
680   C CB  . SER A 108  ? 2.0679 3.5324 1.5713 1.0625  -0.4510 -0.3757 108  SER A CB  
681   O OG  . SER A 108  ? 2.0658 3.5116 1.5608 1.0990  -0.4411 -0.3559 108  SER A OG  
682   N N   . LYS A 109  ? 2.1985 3.8106 1.7206 1.0902  -0.4618 -0.3980 109  LYS A N   
683   C CA  . LYS A 109  ? 2.2579 3.9378 1.7867 1.1208  -0.4612 -0.3972 109  LYS A CA  
684   C C   . LYS A 109  ? 2.3144 3.9772 1.8385 1.1583  -0.4454 -0.3721 109  LYS A C   
685   O O   . LYS A 109  ? 2.3196 4.0273 1.8429 1.1943  -0.4421 -0.3654 109  LYS A O   
686   C CB  . LYS A 109  ? 2.2509 3.9831 1.7976 1.1023  -0.4637 -0.4134 109  LYS A CB  
687   C CG  . LYS A 109  ? 2.2718 3.9678 1.8282 1.0772  -0.4550 -0.4106 109  LYS A CG  
688   C CD  . LYS A 109  ? 2.2520 3.9000 1.8039 1.0952  -0.4382 -0.3842 109  LYS A CD  
689   C CE  . LYS A 109  ? 2.2224 3.8460 1.7857 1.0715  -0.4292 -0.3819 109  LYS A CE  
690   N NZ  . LYS A 109  ? 2.2160 3.8819 1.7910 1.0885  -0.4197 -0.3746 109  LYS A NZ  
691   N N   . HIS A 110  ? 2.3551 3.9548 1.8762 1.1496  -0.4336 -0.3588 110  HIS A N   
692   C CA  . HIS A 110  ? 2.3913 3.9735 1.9106 1.1776  -0.4132 -0.3373 110  HIS A CA  
693   C C   . HIS A 110  ? 2.3583 3.8897 1.8605 1.2046  -0.4034 -0.3211 110  HIS A C   
694   O O   . HIS A 110  ? 2.3623 3.8964 1.8609 1.2400  -0.3855 -0.3057 110  HIS A O   
695   C CB  . HIS A 110  ? 2.4636 4.0160 1.9923 1.1520  -0.4023 -0.3329 110  HIS A CB  
696   C CG  . HIS A 110  ? 2.5613 4.0946 2.0883 1.1769  -0.3778 -0.3117 110  HIS A CG  
697   N ND1 . HIS A 110  ? 2.6060 4.0813 2.1305 1.1627  -0.3639 -0.3014 110  HIS A ND1 
698   C CD2 . HIS A 110  ? 2.6000 4.1656 2.1266 1.2158  -0.3622 -0.2987 110  HIS A CD2 
699   C CE1 . HIS A 110  ? 2.6271 4.0994 2.1502 1.1899  -0.3396 -0.2843 110  HIS A CE1 
700   N NE2 . HIS A 110  ? 2.6234 4.1486 2.1475 1.2232  -0.3372 -0.2816 110  HIS A NE2 
701   N N   . PHE A 111  ? 2.3134 3.7966 1.8050 1.1882  -0.4126 -0.3245 111  PHE A N   
702   C CA  . PHE A 111  ? 2.2580 3.6924 1.7327 1.2137  -0.4058 -0.3117 111  PHE A CA  
703   C C   . PHE A 111  ? 2.1498 3.5585 1.6143 1.1989  -0.4228 -0.3199 111  PHE A C   
704   O O   . PHE A 111  ? 2.1016 3.5247 1.5718 1.1658  -0.4368 -0.3349 111  PHE A O   
705   C CB  . PHE A 111  ? 2.2889 3.6619 1.7592 1.2108  -0.3871 -0.2975 111  PHE A CB  
706   C CG  . PHE A 111  ? 2.3212 3.6595 1.7770 1.2503  -0.3707 -0.2829 111  PHE A CG  
707   C CD1 . PHE A 111  ? 2.3385 3.6958 1.7958 1.2843  -0.3479 -0.2716 111  PHE A CD1 
708   C CD2 . PHE A 111  ? 2.3333 3.6181 1.7736 1.2538  -0.3758 -0.2806 111  PHE A CD2 
709   C CE1 . PHE A 111  ? 2.3538 3.6778 1.7973 1.3216  -0.3295 -0.2602 111  PHE A CE1 
710   C CE2 . PHE A 111  ? 2.3433 3.5932 1.7701 1.2907  -0.3599 -0.2694 111  PHE A CE2 
711   C CZ  . PHE A 111  ? 2.3539 3.6233 1.7821 1.3248  -0.3363 -0.2601 111  PHE A CZ  
712   N N   . SER A 112  ? 2.0848 3.4543 1.5340 1.2240  -0.4195 -0.3102 112  SER A N   
713   C CA  . SER A 112  ? 2.0317 3.3578 1.4700 1.2070  -0.4314 -0.3133 112  SER A CA  
714   C C   . SER A 112  ? 2.0346 3.2896 1.4576 1.2254  -0.4198 -0.2980 112  SER A C   
715   O O   . SER A 112  ? 2.0432 3.2955 1.4608 1.2644  -0.4057 -0.2882 112  SER A O   
716   C CB  . SER A 112  ? 1.9854 3.3502 1.4206 1.2169  -0.4459 -0.3230 112  SER A CB  
717   O OG  . SER A 112  ? 1.9595 3.3025 1.3916 1.1817  -0.4585 -0.3321 112  SER A OG  
718   N N   . LYS A 113  ? 2.0188 3.2172 1.4353 1.1971  -0.4239 -0.2962 113  LYS A N   
719   C CA  . LYS A 113  ? 1.9831 3.1100 1.3853 1.2079  -0.4140 -0.2833 113  LYS A CA  
720   C C   . LYS A 113  ? 1.9331 3.0084 1.3259 1.1803  -0.4248 -0.2827 113  LYS A C   
721   O O   . LYS A 113  ? 1.9079 2.9948 1.3069 1.1445  -0.4349 -0.2909 113  LYS A O   
722   C CB  . LYS A 113  ? 1.9946 3.1014 1.4008 1.2044  -0.3959 -0.2754 113  LYS A CB  
723   C CG  . LYS A 113  ? 2.0398 3.0794 1.4314 1.2206  -0.3823 -0.2637 113  LYS A CG  
724   C CD  . LYS A 113  ? 2.0815 3.1241 1.4676 1.2678  -0.3631 -0.2573 113  LYS A CD  
725   C CE  . LYS A 113  ? 2.1025 3.0769 1.4746 1.2812  -0.3463 -0.2485 113  LYS A CE  
726   N NZ  . LYS A 113  ? 2.1022 3.0782 1.4719 1.3192  -0.3180 -0.2428 113  LYS A NZ  
727   N N   . SER A 114  ? 1.9586 2.9750 1.3362 1.1981  -0.4200 -0.2725 114  SER A N   
728   C CA  . SER A 114  ? 2.0250 2.9889 1.3915 1.1785  -0.4291 -0.2692 114  SER A CA  
729   C C   . SER A 114  ? 2.0535 2.9451 1.4064 1.1898  -0.4178 -0.2563 114  SER A C   
730   O O   . SER A 114  ? 2.0362 2.9229 1.3897 1.2088  -0.4018 -0.2521 114  SER A O   
731   C CB  . SER A 114  ? 2.0707 3.0469 1.4312 1.1907  -0.4416 -0.2739 114  SER A CB  
732   O OG  . SER A 114  ? 2.0876 3.1107 1.4509 1.2283  -0.4392 -0.2774 114  SER A OG  
733   N N   . LYS A 115  ? 2.0759 2.9122 1.4168 1.1775  -0.4242 -0.2503 115  LYS A N   
734   C CA  . LYS A 115  ? 2.0814 2.8488 1.4097 1.1842  -0.4142 -0.2390 115  LYS A CA  
735   C C   . LYS A 115  ? 2.0965 2.8039 1.4095 1.1835  -0.4219 -0.2321 115  LYS A C   
736   O O   . LYS A 115  ? 2.0789 2.7888 1.3921 1.1585  -0.4341 -0.2333 115  LYS A O   
737   C CB  . LYS A 115  ? 2.0683 2.8252 1.4019 1.1512  -0.4087 -0.2354 115  LYS A CB  
738   C CG  . LYS A 115  ? 2.0423 2.7348 1.3640 1.1546  -0.3977 -0.2247 115  LYS A CG  
739   C CD  . LYS A 115  ? 2.0041 2.7008 1.3277 1.1774  -0.3779 -0.2248 115  LYS A CD  
740   C CE  . LYS A 115  ? 1.9729 2.6161 1.2877 1.1690  -0.3667 -0.2167 115  LYS A CE  
741   N NZ  . LYS A 115  ? 1.9525 2.5940 1.2670 1.1923  -0.3436 -0.2178 115  LYS A NZ  
742   N N   . ARG A 116  ? 2.1318 2.7839 1.4314 1.2106  -0.4128 -0.2251 116  ARG A N   
743   C CA  . ARG A 116  ? 2.2012 2.7835 1.4852 1.2089  -0.4180 -0.2164 116  ARG A CA  
744   C C   . ARG A 116  ? 2.2114 2.7491 1.4912 1.1825  -0.4128 -0.2070 116  ARG A C   
745   O O   . ARG A 116  ? 2.2347 2.7591 1.5135 1.1922  -0.3988 -0.2055 116  ARG A O   
746   C CB  . ARG A 116  ? 2.2619 2.8046 1.5331 1.2543  -0.4100 -0.2153 116  ARG A CB  
747   C CG  . ARG A 116  ? 2.3326 2.7926 1.5867 1.2560  -0.4126 -0.2060 116  ARG A CG  
748   C CD  . ARG A 116  ? 2.4002 2.8083 1.6455 1.2684  -0.3959 -0.2016 116  ARG A CD  
749   N NE  . ARG A 116  ? 2.4716 2.8146 1.7006 1.3024  -0.3910 -0.1998 116  ARG A NE  
750   C CZ  . ARG A 116  ? 2.5179 2.7972 1.7351 1.3101  -0.3796 -0.1957 116  ARG A CZ  
751   N NH1 . ARG A 116  ? 2.5209 2.7956 1.7407 1.2852  -0.3725 -0.1919 116  ARG A NH1 
752   N NH2 . ARG A 116  ? 2.5442 2.7639 1.7468 1.3426  -0.3751 -0.1959 116  ARG A NH2 
753   N N   . MET A 117  ? 2.1993 2.7148 1.4765 1.1491  -0.4221 -0.2003 117  MET A N   
754   C CA  . MET A 117  ? 2.1734 2.6574 1.4483 1.1219  -0.4170 -0.1905 117  MET A CA  
755   C C   . MET A 117  ? 2.1422 2.5802 1.4079 1.0958  -0.4242 -0.1788 117  MET A C   
756   O O   . MET A 117  ? 2.1133 2.5750 1.3840 1.0724  -0.4318 -0.1806 117  MET A O   
757   C CB  . MET A 117  ? 2.1664 2.7057 1.4570 1.0964  -0.4144 -0.1959 117  MET A CB  
758   C CG  . MET A 117  ? 2.1683 2.7606 1.4702 1.0762  -0.4244 -0.2047 117  MET A CG  
759   S SD  . MET A 117  ? 2.1719 2.8145 1.4905 1.0426  -0.4208 -0.2102 117  MET A SD  
760   C CE  . MET A 117  ? 1.6813 2.3286 1.0028 1.0664  -0.4072 -0.2108 117  MET A CE  
761   N N   . PRO A 118  ? 2.1405 2.5124 1.3927 1.0991  -0.4196 -0.1667 118  PRO A N   
762   C CA  . PRO A 118  ? 2.1269 2.4434 1.3679 1.0796  -0.4241 -0.1523 118  PRO A CA  
763   C C   . PRO A 118  ? 2.0996 2.4369 1.3472 1.0369  -0.4256 -0.1465 118  PRO A C   
764   O O   . PRO A 118  ? 2.0641 2.4467 1.3233 1.0199  -0.4217 -0.1512 118  PRO A O   
765   C CB  . PRO A 118  ? 2.1254 2.3836 1.3547 1.0883  -0.4157 -0.1423 118  PRO A CB  
766   C CG  . PRO A 118  ? 2.1347 2.4016 1.3641 1.1261  -0.4078 -0.1540 118  PRO A CG  
767   C CD  . PRO A 118  ? 2.1392 2.4842 1.3854 1.1250  -0.4078 -0.1669 118  PRO A CD  
768   N N   . ILE A 119  ? 2.1166 2.4183 1.3563 1.0202  -0.4292 -0.1362 119  ILE A N   
769   C CA  . ILE A 119  ? 2.0902 2.4051 1.3341 0.9802  -0.4263 -0.1297 119  ILE A CA  
770   C C   . ILE A 119  ? 2.0907 2.3376 1.3208 0.9633  -0.4226 -0.1085 119  ILE A C   
771   O O   . ILE A 119  ? 2.0770 2.2657 1.2943 0.9826  -0.4254 -0.1006 119  ILE A O   
772   C CB  . ILE A 119  ? 2.0642 2.4271 1.3170 0.9693  -0.4311 -0.1426 119  ILE A CB  
773   C CG1 . ILE A 119  ? 2.0459 2.3675 1.2881 0.9720  -0.4358 -0.1367 119  ILE A CG1 
774   C CG2 . ILE A 119  ? 2.0507 2.4770 1.3155 0.9920  -0.4364 -0.1627 119  ILE A CG2 
775   C CD1 . ILE A 119  ? 2.0433 2.4133 1.2937 0.9555  -0.4381 -0.1492 119  ILE A CD1 
776   N N   . THR A 120  ? 2.0985 2.3517 1.3310 0.9279  -0.4147 -0.0992 120  THR A N   
777   C CA  . THR A 120  ? 2.1303 2.3216 1.3501 0.9096  -0.4075 -0.0758 120  THR A CA  
778   C C   . THR A 120  ? 2.1314 2.3293 1.3529 0.8730  -0.3974 -0.0682 120  THR A C   
779   O O   . THR A 120  ? 2.1222 2.3779 1.3559 0.8574  -0.3942 -0.0823 120  THR A O   
780   C CB  . THR A 120  ? 2.1545 2.3258 1.3705 0.9069  -0.4008 -0.0627 120  THR A CB  
781   O OG1 . THR A 120  ? 2.1660 2.3477 1.3838 0.9369  -0.4058 -0.0744 120  THR A OG1 
782   C CG2 . THR A 120  ? 1.6960 1.7903 0.8955 0.9002  -0.3961 -0.0375 120  THR A CG2 
783   N N   . TYR A 121  ? 2.1442 3.0117 1.4897 0.8580  -0.5973 -0.3587 121  TYR A N   
784   C CA  . TYR A 121  ? 2.1511 3.0156 1.4702 0.8361  -0.6032 -0.3870 121  TYR A CA  
785   C C   . TYR A 121  ? 2.0487 2.8818 1.3867 0.8112  -0.5836 -0.4025 121  TYR A C   
786   O O   . TYR A 121  ? 2.0685 2.8928 1.3885 0.7918  -0.5832 -0.4254 121  TYR A O   
787   C CB  . TYR A 121  ? 2.2497 3.0890 1.5070 0.8452  -0.5994 -0.3809 121  TYR A CB  
788   C CG  . TYR A 121  ? 2.3195 3.1841 1.5463 0.8708  -0.6170 -0.3632 121  TYR A CG  
789   C CD1 . TYR A 121  ? 2.3541 3.2690 1.5777 0.8704  -0.6462 -0.3756 121  TYR A CD1 
790   C CD2 . TYR A 121  ? 2.3435 3.1815 1.5439 0.8951  -0.6042 -0.3339 121  TYR A CD2 
791   C CE1 . TYR A 121  ? 2.3985 3.3374 1.5930 0.8936  -0.6631 -0.3578 121  TYR A CE1 
792   C CE2 . TYR A 121  ? 2.3813 3.2410 1.5525 0.9188  -0.6193 -0.3162 121  TYR A CE2 
793   C CZ  . TYR A 121  ? 2.4270 3.3377 1.5946 0.9180  -0.6493 -0.3275 121  TYR A CZ  
794   O OH  . TYR A 121  ? 2.4991 3.4332 1.6360 0.9420  -0.6656 -0.3079 121  TYR A OH  
795   N N   . ASP A 122  ? 1.9492 2.7641 1.3219 0.8119  -0.5662 -0.3893 122  ASP A N   
796   C CA  . ASP A 122  ? 1.8527 2.6430 1.2496 0.7879  -0.5493 -0.4023 122  ASP A CA  
797   C C   . ASP A 122  ? 1.7651 2.5872 1.2018 0.7673  -0.5612 -0.4269 122  ASP A C   
798   O O   . ASP A 122  ? 1.7655 2.6080 1.2439 0.7696  -0.5638 -0.4220 122  ASP A O   
799   C CB  . ASP A 122  ? 1.8473 2.6146 1.2709 0.7950  -0.5290 -0.3803 122  ASP A CB  
800   C CG  . ASP A 122  ? 1.8729 2.5906 1.2743 0.7919  -0.5056 -0.3717 122  ASP A CG  
801   O OD1 . ASP A 122  ? 1.8754 2.5722 1.2741 0.8090  -0.4915 -0.3476 122  ASP A OD1 
802   O OD2 . ASP A 122  ? 1.8849 2.5848 1.2739 0.7724  -0.5007 -0.3889 122  ASP A OD2 
803   N N   . ASN A 123  ? 1.7105 2.5358 1.1374 0.7467  -0.5664 -0.4537 123  ASN A N   
804   C CA  . ASN A 123  ? 1.6597 2.5108 1.1274 0.7260  -0.5742 -0.4776 123  ASN A CA  
805   C C   . ASN A 123  ? 1.6620 2.4832 1.1360 0.7006  -0.5568 -0.4936 123  ASN A C   
806   O O   . ASN A 123  ? 1.6893 2.4967 1.1337 0.6904  -0.5542 -0.5077 123  ASN A O   
807   C CB  . ASN A 123  ? 1.6738 2.5690 1.1361 0.7234  -0.6003 -0.4989 123  ASN A CB  
808   C CG  . ASN A 123  ? 1.6393 2.5595 1.1446 0.7009  -0.6070 -0.5261 123  ASN A CG  
809   O OD1 . ASN A 123  ? 1.6483 2.6107 1.1648 0.7000  -0.6289 -0.5414 123  ASN A OD1 
810   N ND2 . ASN A 123  ? 1.6216 2.5163 1.1509 0.6826  -0.5882 -0.5321 123  ASN A ND2 
811   N N   . GLY A 124  ? 1.6605 2.4726 1.1738 0.6902  -0.5443 -0.4908 124  GLY A N   
812   C CA  . GLY A 124  ? 1.6789 2.4665 1.2057 0.6656  -0.5283 -0.5041 124  GLY A CA  
813   C C   . GLY A 124  ? 1.4559 2.1968 0.9678 0.6658  -0.5051 -0.4859 124  GLY A C   
814   O O   . GLY A 124  ? 1.4529 2.1802 0.9569 0.6837  -0.4983 -0.4614 124  GLY A O   
815   N N   . PHE A 125  ? 1.4510 2.1681 0.9602 0.6458  -0.4926 -0.4980 125  PHE A N   
816   C CA  . PHE A 125  ? 1.4345 2.1098 0.9400 0.6409  -0.4703 -0.4830 125  PHE A CA  
817   C C   . PHE A 125  ? 1.4495 2.0997 0.9342 0.6263  -0.4603 -0.4953 125  PHE A C   
818   O O   . PHE A 125  ? 1.4497 2.1112 0.9474 0.6074  -0.4630 -0.5188 125  PHE A O   
819   C CB  . PHE A 125  ? 1.3964 2.0707 0.9432 0.6248  -0.4615 -0.4836 125  PHE A CB  
820   C CG  . PHE A 125  ? 1.3782 2.0757 0.9525 0.6345  -0.4678 -0.4742 125  PHE A CG  
821   C CD1 . PHE A 125  ? 1.3755 2.1081 0.9805 0.6266  -0.4810 -0.4916 125  PHE A CD1 
822   C CD2 . PHE A 125  ? 1.3687 2.0523 0.9410 0.6510  -0.4589 -0.4485 125  PHE A CD2 
823   C CE1 . PHE A 125  ? 1.3623 2.1156 0.9962 0.6350  -0.4851 -0.4829 125  PHE A CE1 
824   C CE2 . PHE A 125  ? 1.3709 2.0754 0.9713 0.6594  -0.4623 -0.4401 125  PHE A CE2 
825   C CZ  . PHE A 125  ? 1.3637 2.1030 0.9956 0.6512  -0.4753 -0.4571 125  PHE A CZ  
826   N N   . LEU A 126  ? 1.4615 2.0768 0.9172 0.6340  -0.4470 -0.4800 126  LEU A N   
827   C CA  . LEU A 126  ? 1.4723 2.0598 0.9144 0.6190  -0.4335 -0.4895 126  LEU A CA  
828   C C   . LEU A 126  ? 1.5309 2.0854 0.9918 0.6079  -0.4129 -0.4760 126  LEU A C   
829   O O   . LEU A 126  ? 1.5303 2.0646 0.9885 0.6196  -0.4038 -0.4523 126  LEU A O   
830   C CB  . LEU A 126  ? 1.5096 2.0796 0.9067 0.6317  -0.4316 -0.4854 126  LEU A CB  
831   C CG  . LEU A 126  ? 1.5483 2.1426 0.9176 0.6343  -0.4476 -0.5050 126  LEU A CG  
832   C CD1 . LEU A 126  ? 1.5457 2.1711 0.9380 0.6145  -0.4581 -0.5348 126  LEU A CD1 
833   C CD2 . LEU A 126  ? 1.5657 2.1828 0.9160 0.6591  -0.4645 -0.4926 126  LEU A CD2 
834   N N   . PHE A 127  ? 1.4860 2.0361 0.9670 0.5852  -0.4056 -0.4908 127  PHE A N   
835   C CA  . PHE A 127  ? 1.4290 1.9531 0.9311 0.5727  -0.3882 -0.4785 127  PHE A CA  
836   C C   . PHE A 127  ? 1.4249 1.9176 0.9171 0.5612  -0.3718 -0.4811 127  PHE A C   
837   O O   . PHE A 127  ? 1.4451 1.9436 0.9477 0.5439  -0.3700 -0.5017 127  PHE A O   
838   C CB  . PHE A 127  ? 1.4383 1.9824 0.9778 0.5545  -0.3911 -0.4909 127  PHE A CB  
839   C CG  . PHE A 127  ? 1.4356 2.0005 0.9950 0.5618  -0.3993 -0.4819 127  PHE A CG  
840   C CD1 . PHE A 127  ? 1.4286 1.9806 0.9829 0.5768  -0.3943 -0.4571 127  PHE A CD1 
841   C CD2 . PHE A 127  ? 1.4036 2.0001 0.9895 0.5526  -0.4103 -0.4992 127  PHE A CD2 
842   C CE1 . PHE A 127  ? 1.3725 1.9431 0.9472 0.5823  -0.3994 -0.4501 127  PHE A CE1 
843   C CE2 . PHE A 127  ? 1.3429 1.9572 0.9493 0.5582  -0.4159 -0.4917 127  PHE A CE2 
844   C CZ  . PHE A 127  ? 1.3520 1.9533 0.9526 0.5729  -0.4100 -0.4671 127  PHE A CZ  
845   N N   . ILE A 128  ? 1.4337 1.8927 0.9097 0.5698  -0.3584 -0.4605 128  ILE A N   
846   C CA  . ILE A 128  ? 1.4588 1.8867 0.9236 0.5611  -0.3421 -0.4624 128  ILE A CA  
847   C C   . ILE A 128  ? 1.4582 1.8629 0.9496 0.5442  -0.3250 -0.4532 128  ILE A C   
848   O O   . ILE A 128  ? 1.4009 1.7821 0.8958 0.5490  -0.3146 -0.4298 128  ILE A O   
849   C CB  . ILE A 128  ? 1.4604 1.8617 0.8909 0.5790  -0.3354 -0.4477 128  ILE A CB  
850   C CG1 . ILE A 128  ? 1.4789 1.9007 0.8873 0.6009  -0.3515 -0.4437 128  ILE A CG1 
851   C CG2 . ILE A 128  ? 1.4917 1.8770 0.9023 0.5715  -0.3265 -0.4627 128  ILE A CG2 
852   C CD1 . ILE A 128  ? 1.4965 1.8917 0.8705 0.6194  -0.3442 -0.4284 128  ILE A CD1 
853   N N   . HIS A 129  ? 1.4770 1.8886 0.9868 0.5246  -0.3216 -0.4719 129  HIS A N   
854   C CA  . HIS A 129  ? 1.4884 1.8839 1.0268 0.5073  -0.3071 -0.4643 129  HIS A CA  
855   C C   . HIS A 129  ? 1.5362 1.8974 1.0705 0.5008  -0.2873 -0.4599 129  HIS A C   
856   O O   . HIS A 129  ? 1.5779 1.9380 1.1193 0.4865  -0.2798 -0.4784 129  HIS A O   
857   C CB  . HIS A 129  ? 1.4473 1.8686 1.0122 0.4894  -0.3125 -0.4857 129  HIS A CB  
858   C CG  . HIS A 129  ? 1.4017 1.8102 0.9965 0.4715  -0.2990 -0.4776 129  HIS A CG  
859   N ND1 . HIS A 129  ? 1.3844 1.8108 1.0051 0.4542  -0.3001 -0.4942 129  HIS A ND1 
860   C CD2 . HIS A 129  ? 1.3857 1.7658 0.9889 0.4683  -0.2842 -0.4541 129  HIS A CD2 
861   C CE1 . HIS A 129  ? 1.3896 1.7989 1.0317 0.4413  -0.2865 -0.4803 129  HIS A CE1 
862   N NE2 . HIS A 129  ? 1.3955 1.7777 1.0280 0.4495  -0.2773 -0.4557 129  HIS A NE2 
863   N N   . THR A 130  ? 1.5447 1.8776 1.0696 0.5112  -0.2777 -0.4358 130  THR A N   
864   C CA  . THR A 130  ? 1.5623 1.8609 1.0894 0.5048  -0.2574 -0.4280 130  THR A CA  
865   C C   . THR A 130  ? 1.5520 1.8471 1.1155 0.4870  -0.2485 -0.4198 130  THR A C   
866   O O   . THR A 130  ? 1.5526 1.8625 1.1315 0.4853  -0.2565 -0.4106 130  THR A O   
867   C CB  . THR A 130  ? 1.5521 1.8225 1.0624 0.5211  -0.2502 -0.4038 130  THR A CB  
868   O OG1 . THR A 130  ? 1.5428 1.7811 1.0688 0.5125  -0.2302 -0.3898 130  THR A OG1 
869   C CG2 . THR A 130  ? 1.5311 1.8117 1.0474 0.5313  -0.2596 -0.3850 130  THR A CG2 
870   N N   . ASP A 131  ? 1.5509 1.8275 1.1289 0.4732  -0.2315 -0.4231 131  ASP A N   
871   C CA  . ASP A 131  ? 1.5344 1.8112 1.1472 0.4558  -0.2239 -0.4166 131  ASP A CA  
872   C C   . ASP A 131  ? 1.5535 1.8165 1.1787 0.4589  -0.2206 -0.3848 131  ASP A C   
873   O O   . ASP A 131  ? 1.5549 1.8336 1.1971 0.4521  -0.2274 -0.3781 131  ASP A O   
874   C CB  . ASP A 131  ? 1.5292 1.7895 1.1583 0.4405  -0.2047 -0.4260 131  ASP A CB  
875   C CG  . ASP A 131  ? 1.5319 1.7553 1.1624 0.4436  -0.1860 -0.4054 131  ASP A CG  
876   O OD1 . ASP A 131  ? 1.5363 1.7466 1.1434 0.4598  -0.1884 -0.3939 131  ASP A OD1 
877   O OD2 . ASP A 131  ? 1.5343 1.7410 1.1903 0.4304  -0.1681 -0.4004 131  ASP A OD2 
878   N N   . LYS A 132  ? 1.5733 1.8076 1.1896 0.4686  -0.2103 -0.3658 132  LYS A N   
879   C CA  . LYS A 132  ? 1.5756 1.7987 1.2024 0.4726  -0.2085 -0.3362 132  LYS A CA  
880   C C   . LYS A 132  ? 1.6222 1.8300 1.2236 0.4933  -0.2096 -0.3241 132  LYS A C   
881   O O   . LYS A 132  ? 1.7102 1.9137 1.2859 0.5034  -0.2105 -0.3373 132  LYS A O   
882   C CB  . LYS A 132  ? 1.5065 1.7090 1.1627 0.4591  -0.1917 -0.3189 132  LYS A CB  
883   C CG  . LYS A 132  ? 1.4509 1.6184 1.1065 0.4632  -0.1736 -0.3078 132  LYS A CG  
884   C CD  . LYS A 132  ? 1.3789 1.5348 1.0672 0.4456  -0.1571 -0.3029 132  LYS A CD  
885   C CE  . LYS A 132  ? 1.3688 1.4885 1.0630 0.4481  -0.1366 -0.2905 132  LYS A CE  
886   N NZ  . LYS A 132  ? 1.4123 1.5253 1.1238 0.4335  -0.1206 -0.3060 132  LYS A NZ  
887   N N   . PRO A 133  ? 1.5741 1.7752 1.1815 0.4995  -0.2100 -0.2997 133  PRO A N   
888   C CA  . PRO A 133  ? 1.4844 1.6779 1.0656 0.5202  -0.2136 -0.2940 133  PRO A CA  
889   C C   . PRO A 133  ? 1.4886 1.6461 1.0708 0.5266  -0.1975 -0.2737 133  PRO A C   
890   O O   . PRO A 133  ? 1.4871 1.6347 1.0540 0.5430  -0.1979 -0.2624 133  PRO A O   
891   C CB  . PRO A 133  ? 1.4521 1.6647 1.0409 0.5229  -0.2243 -0.2824 133  PRO A CB  
892   C CG  . PRO A 133  ? 1.5349 1.7469 1.1562 0.5038  -0.2188 -0.2684 133  PRO A CG  
893   C CD  . PRO A 133  ? 1.5451 1.7451 1.1783 0.4906  -0.2076 -0.2770 133  PRO A CD  
894   N N   . VAL A 134  ? 1.4149 1.5528 1.0170 0.5144  -0.1828 -0.2680 134  VAL A N   
895   C CA  . VAL A 134  ? 1.3890 1.4910 0.9926 0.5212  -0.1665 -0.2503 134  VAL A CA  
896   C C   . VAL A 134  ? 1.4519 1.5322 1.0677 0.5102  -0.1490 -0.2557 134  VAL A C   
897   O O   . VAL A 134  ? 1.4952 1.5825 1.1374 0.4934  -0.1450 -0.2569 134  VAL A O   
898   C CB  . VAL A 134  ? 1.3370 1.4315 0.9631 0.5210  -0.1639 -0.2215 134  VAL A CB  
899   C CG1 . VAL A 134  ? 1.3459 1.4057 0.9881 0.5197  -0.1448 -0.2048 134  VAL A CG1 
900   C CG2 . VAL A 134  ? 1.3301 1.4276 0.9377 0.5387  -0.1718 -0.2135 134  VAL A CG2 
901   N N   . TYR A 135  ? 1.5353 1.5881 1.1321 0.5199  -0.1370 -0.2586 135  TYR A N   
902   C CA  . TYR A 135  ? 1.5275 1.5564 1.1328 0.5102  -0.1174 -0.2662 135  TYR A CA  
903   C C   . TYR A 135  ? 1.4897 1.4786 1.1025 0.5161  -0.0977 -0.2471 135  TYR A C   
904   O O   . TYR A 135  ? 1.4354 1.4108 1.0354 0.5315  -0.0985 -0.2326 135  TYR A O   
905   C CB  . TYR A 135  ? 1.4563 1.4905 1.0299 0.5118  -0.1191 -0.2959 135  TYR A CB  
906   C CG  . TYR A 135  ? 1.4483 1.5216 1.0174 0.5055  -0.1376 -0.3164 135  TYR A CG  
907   C CD1 . TYR A 135  ? 1.4498 1.5349 1.0383 0.4872  -0.1334 -0.3329 135  TYR A CD1 
908   C CD2 . TYR A 135  ? 1.4386 1.5370 0.9874 0.5177  -0.1583 -0.3187 135  TYR A CD2 
909   C CE1 . TYR A 135  ? 1.4423 1.5631 1.0288 0.4813  -0.1500 -0.3525 135  TYR A CE1 
910   C CE2 . TYR A 135  ? 1.4310 1.5652 0.9787 0.5119  -0.1750 -0.3372 135  TYR A CE2 
911   C CZ  . TYR A 135  ? 1.4328 1.5781 0.9991 0.4937  -0.1712 -0.3545 135  TYR A CZ  
912   O OH  . TYR A 135  ? 1.4254 1.6060 0.9922 0.4879  -0.1873 -0.3737 135  TYR A OH  
913   N N   . THR A 136  ? 1.4832 1.4525 1.1186 0.5032  -0.0784 -0.2480 136  THR A N   
914   C CA  . THR A 136  ? 1.5037 1.4337 1.1533 0.5058  -0.0567 -0.2307 136  THR A CA  
915   C C   . THR A 136  ? 1.5566 1.4657 1.1927 0.5010  -0.0389 -0.2520 136  THR A C   
916   O O   . THR A 136  ? 1.5328 1.4580 1.1677 0.4888  -0.0393 -0.2750 136  THR A O   
917   C CB  . THR A 136  ? 1.5216 1.4461 1.2196 0.4926  -0.0465 -0.2087 136  THR A CB  
918   O OG1 . THR A 136  ? 1.5226 1.4776 1.2355 0.4778  -0.0554 -0.2191 136  THR A OG1 
919   C CG2 . THR A 136  ? 1.4951 1.4189 1.2072 0.5009  -0.0537 -0.1789 136  THR A CG2 
920   N N   . PRO A 137  ? 1.5617 1.4341 1.1880 0.5097  -0.0221 -0.2454 137  PRO A N   
921   C CA  . PRO A 137  ? 1.5515 1.4000 1.1620 0.5049  -0.0027 -0.2656 137  PRO A CA  
922   C C   . PRO A 137  ? 1.5576 1.4172 1.1887 0.4844  0.0060  -0.2844 137  PRO A C   
923   O O   . PRO A 137  ? 1.5415 1.3980 1.2168 0.4725  0.0164  -0.2702 137  PRO A O   
924   C CB  . PRO A 137  ? 1.5904 1.3956 1.2232 0.5077  0.0213  -0.2436 137  PRO A CB  
925   C CG  . PRO A 137  ? 1.5441 1.3501 1.1773 0.5234  0.0089  -0.2184 137  PRO A CG  
926   C CD  . PRO A 137  ? 1.5412 1.3907 1.1759 0.5227  -0.0177 -0.2176 137  PRO A CD  
927   N N   . ASP A 138  ? 1.5811 1.4551 1.1804 0.4807  0.0013  -0.3157 138  ASP A N   
928   C CA  . ASP A 138  ? 1.5966 1.4761 1.2087 0.4614  0.0140  -0.3400 138  ASP A CA  
929   C C   . ASP A 138  ? 1.6272 1.5471 1.2537 0.4508  -0.0024 -0.3517 138  ASP A C   
930   O O   . ASP A 138  ? 1.6306 1.5575 1.2674 0.4349  0.0076  -0.3741 138  ASP A O   
931   C CB  . ASP A 138  ? 1.7378 1.5822 1.3906 0.4494  0.0460  -0.3289 138  ASP A CB  
932   C CG  . ASP A 138  ? 1.8214 1.6255 1.4542 0.4537  0.0678  -0.3328 138  ASP A CG  
933   O OD1 . ASP A 138  ? 1.8614 1.6692 1.4490 0.4569  0.0631  -0.3577 138  ASP A OD1 
934   O OD2 . ASP A 138  ? 1.8196 1.5891 1.4811 0.4539  0.0893  -0.3111 138  ASP A OD2 
935   N N   . GLN A 139  ? 1.6391 1.5848 1.2670 0.4587  -0.0260 -0.3379 139  GLN A N   
936   C CA  . GLN A 139  ? 1.6322 1.6166 1.2707 0.4493  -0.0426 -0.3502 139  GLN A CA  
937   C C   . GLN A 139  ? 1.6761 1.6827 1.2753 0.4511  -0.0559 -0.3831 139  GLN A C   
938   O O   . GLN A 139  ? 1.6968 1.6919 1.2590 0.4626  -0.0568 -0.3898 139  GLN A O   
939   C CB  . GLN A 139  ? 1.6316 1.6379 1.2778 0.4570  -0.0643 -0.3290 139  GLN A CB  
940   C CG  . GLN A 139  ? 1.6202 1.6075 1.2965 0.4599  -0.0573 -0.2927 139  GLN A CG  
941   C CD  . GLN A 139  ? 1.5978 1.6132 1.2946 0.4558  -0.0741 -0.2785 139  GLN A CD  
942   O OE1 . GLN A 139  ? 1.5565 1.5772 1.2490 0.4662  -0.0868 -0.2593 139  GLN A OE1 
943   N NE2 . GLN A 139  ? 1.6054 1.6386 1.3241 0.4397  -0.0731 -0.2891 139  GLN A NE2 
944   N N   . SER A 140  ? 1.6692 1.7076 1.2761 0.4397  -0.0658 -0.4037 140  SER A N   
945   C CA  . SER A 140  ? 1.6919 1.7567 1.2633 0.4419  -0.0818 -0.4342 140  SER A CA  
946   C C   . SER A 140  ? 1.6405 1.7424 1.2062 0.4490  -0.1103 -0.4333 140  SER A C   
947   O O   . SER A 140  ? 1.6141 1.7355 1.2081 0.4388  -0.1152 -0.4332 140  SER A O   
948   C CB  . SER A 140  ? 1.7139 1.7864 1.2936 0.4229  -0.0696 -0.4659 140  SER A CB  
949   O OG  . SER A 140  ? 1.7403 1.7895 1.2958 0.4216  -0.0532 -0.4807 140  SER A OG  
950   N N   . VAL A 141  ? 1.6555 1.7657 1.1854 0.4667  -0.1276 -0.4319 141  VAL A N   
951   C CA  . VAL A 141  ? 1.5668 1.7108 1.0900 0.4755  -0.1537 -0.4303 141  VAL A CA  
952   C C   . VAL A 141  ? 1.6197 1.7998 1.1441 0.4648  -0.1664 -0.4600 141  VAL A C   
953   O O   . VAL A 141  ? 1.6336 1.8231 1.1322 0.4645  -0.1699 -0.4843 141  VAL A O   
954   C CB  . VAL A 141  ? 1.5414 1.6865 1.0240 0.4970  -0.1672 -0.4261 141  VAL A CB  
955   C CG1 . VAL A 141  ? 1.5092 1.6888 0.9898 0.5055  -0.1918 -0.4239 141  VAL A CG1 
956   C CG2 . VAL A 141  ? 1.5324 1.6405 1.0109 0.5091  -0.1541 -0.3989 141  VAL A CG2 
957   N N   . LYS A 142  ? 1.5701 1.7708 1.1242 0.4551  -0.1730 -0.4589 142  LYS A N   
958   C CA  . LYS A 142  ? 1.6170 1.8542 1.1729 0.4469  -0.1874 -0.4864 142  LYS A CA  
959   C C   . LYS A 142  ? 1.6483 1.9122 1.1793 0.4635  -0.2131 -0.4869 142  LYS A C   
960   O O   . LYS A 142  ? 1.6624 1.9208 1.1902 0.4765  -0.2191 -0.4628 142  LYS A O   
961   C CB  . LYS A 142  ? 1.5840 1.8328 1.1801 0.4307  -0.1844 -0.4857 142  LYS A CB  
962   C CG  . LYS A 142  ? 1.6091 1.8403 1.2313 0.4124  -0.1599 -0.4940 142  LYS A CG  
963   C CD  . LYS A 142  ? 1.6077 1.8624 1.2599 0.3958  -0.1612 -0.5097 142  LYS A CD  
964   C CE  . LYS A 142  ? 1.6334 1.8740 1.3097 0.3777  -0.1361 -0.5243 142  LYS A CE  
965   N NZ  . LYS A 142  ? 1.6269 1.8318 1.3264 0.3742  -0.1125 -0.4972 142  LYS A NZ  
966   N N   . VAL A 143  ? 1.6729 1.9660 1.1875 0.4632  -0.2277 -0.5138 143  VAL A N   
967   C CA  . VAL A 143  ? 1.6486 1.9697 1.1432 0.4790  -0.2523 -0.5141 143  VAL A CA  
968   C C   . VAL A 143  ? 1.6235 1.9849 1.1190 0.4727  -0.2696 -0.5435 143  VAL A C   
969   O O   . VAL A 143  ? 1.6536 2.0216 1.1478 0.4603  -0.2648 -0.5694 143  VAL A O   
970   C CB  . VAL A 143  ? 1.5261 1.8333 0.9799 0.4993  -0.2556 -0.5042 143  VAL A CB  
971   C CG1 . VAL A 143  ? 1.5534 1.8247 0.9936 0.4955  -0.2337 -0.5049 143  VAL A CG1 
972   C CG2 . VAL A 143  ? 1.5452 1.8857 0.9715 0.5090  -0.2777 -0.5224 143  VAL A CG2 
973   N N   . ARG A 144  ? 1.5822 1.9707 1.0823 0.4810  -0.2890 -0.5395 144  ARG A N   
974   C CA  . ARG A 144  ? 1.5846 2.0132 1.0821 0.4801  -0.3090 -0.5642 144  ARG A CA  
975   C C   . ARG A 144  ? 1.5579 2.0070 1.0448 0.4994  -0.3294 -0.5513 144  ARG A C   
976   O O   . ARG A 144  ? 1.5146 1.9461 0.9979 0.5116  -0.3263 -0.5246 144  ARG A O   
977   C CB  . ARG A 144  ? 1.5999 2.0467 1.1339 0.4602  -0.3077 -0.5824 144  ARG A CB  
978   C CG  . ARG A 144  ? 1.5970 2.0343 1.1625 0.4538  -0.3007 -0.5627 144  ARG A CG  
979   C CD  . ARG A 144  ? 1.6074 2.0712 1.2044 0.4387  -0.3062 -0.5810 144  ARG A CD  
980   N NE  . ARG A 144  ? 1.6002 2.0485 1.2254 0.4284  -0.2940 -0.5634 144  ARG A NE  
981   C CZ  . ARG A 144  ? 1.6273 2.0526 1.2693 0.4143  -0.2735 -0.5607 144  ARG A CZ  
982   N NH1 . ARG A 144  ? 1.6519 2.0662 1.2868 0.4083  -0.2614 -0.5765 144  ARG A NH1 
983   N NH2 . ARG A 144  ? 1.6189 2.0325 1.2850 0.4059  -0.2645 -0.5422 144  ARG A NH2 
984   N N   . VAL A 145  ? 1.5797 2.0661 1.0632 0.5020  -0.3493 -0.5704 145  VAL A N   
985   C CA  . VAL A 145  ? 1.4867 1.9953 0.9617 0.5206  -0.3686 -0.5597 145  VAL A CA  
986   C C   . VAL A 145  ? 1.5285 2.0745 1.0317 0.5129  -0.3833 -0.5762 145  VAL A C   
987   O O   . VAL A 145  ? 1.4841 2.0516 0.9918 0.5016  -0.3893 -0.6036 145  VAL A O   
988   C CB  . VAL A 145  ? 1.5218 2.0421 0.9578 0.5361  -0.3813 -0.5655 145  VAL A CB  
989   C CG1 . VAL A 145  ? 1.5150 2.0681 0.9517 0.5519  -0.4031 -0.5604 145  VAL A CG1 
990   C CG2 . VAL A 145  ? 1.5379 2.0218 0.9433 0.5488  -0.3687 -0.5452 145  VAL A CG2 
991   N N   . TYR A 146  ? 1.5213 2.0741 1.0450 0.5176  -0.3877 -0.5605 146  TYR A N   
992   C CA  . TYR A 146  ? 1.5113 2.1003 1.0604 0.5143  -0.4032 -0.5730 146  TYR A CA  
993   C C   . TYR A 146  ? 1.5550 2.1660 1.0867 0.5361  -0.4215 -0.5658 146  TYR A C   
994   O O   . TYR A 146  ? 1.5680 2.1646 1.0880 0.5520  -0.4190 -0.5409 146  TYR A O   
995   C CB  . TYR A 146  ? 1.4031 1.9860 0.9843 0.5058  -0.3957 -0.5602 146  TYR A CB  
996   C CG  . TYR A 146  ? 1.5094 2.0646 1.1044 0.4875  -0.3757 -0.5585 146  TYR A CG  
997   C CD1 . TYR A 146  ? 1.5490 2.1084 1.1573 0.4691  -0.3701 -0.5826 146  TYR A CD1 
998   C CD2 . TYR A 146  ? 1.5230 2.0482 1.1190 0.4886  -0.3617 -0.5323 146  TYR A CD2 
999   C CE1 . TYR A 146  ? 1.5471 2.0806 1.1701 0.4530  -0.3503 -0.5789 146  TYR A CE1 
1000  C CE2 . TYR A 146  ? 1.5088 2.0097 1.1190 0.4724  -0.3438 -0.5281 146  TYR A CE2 
1001  C CZ  . TYR A 146  ? 1.5145 2.0192 1.1384 0.4551  -0.3379 -0.5505 146  TYR A CZ  
1002  O OH  . TYR A 146  ? 1.4867 1.9673 1.1264 0.4401  -0.3192 -0.5441 146  TYR A OH  
1003  N N   . SER A 147  ? 1.6160 2.2624 1.1467 0.5371  -0.4395 -0.5871 147  SER A N   
1004  C CA  . SER A 147  ? 1.6558 2.3270 1.1702 0.5584  -0.4586 -0.5803 147  SER A CA  
1005  C C   . SER A 147  ? 1.6608 2.3738 1.2053 0.5567  -0.4765 -0.5940 147  SER A C   
1006  O O   . SER A 147  ? 1.6712 2.4039 1.2334 0.5407  -0.4812 -0.6203 147  SER A O   
1007  C CB  . SER A 147  ? 1.7146 2.3890 1.1881 0.5665  -0.4657 -0.5889 147  SER A CB  
1008  O OG  . SER A 147  ? 1.7471 2.4547 1.2241 0.5562  -0.4797 -0.6191 147  SER A OG  
1009  N N   . LEU A 148  ? 1.6601 2.3859 1.2125 0.5732  -0.4851 -0.5760 148  LEU A N   
1010  C CA  . LEU A 148  ? 1.6446 2.4085 1.2285 0.5738  -0.5008 -0.5851 148  LEU A CA  
1011  C C   . LEU A 148  ? 1.7275 2.5166 1.2956 0.5979  -0.5193 -0.5743 148  LEU A C   
1012  O O   . LEU A 148  ? 1.7871 2.5590 1.3240 0.6151  -0.5163 -0.5542 148  LEU A O   
1013  C CB  . LEU A 148  ? 1.5915 2.3465 1.2093 0.5687  -0.4902 -0.5721 148  LEU A CB  
1014  C CG  . LEU A 148  ? 1.5665 2.3119 1.2122 0.5430  -0.4779 -0.5873 148  LEU A CG  
1015  C CD1 . LEU A 148  ? 1.5746 2.3028 1.2037 0.5290  -0.4691 -0.6029 148  LEU A CD1 
1016  C CD2 . LEU A 148  ? 1.5519 2.2714 1.2122 0.5387  -0.4610 -0.5666 148  LEU A CD2 
1017  N N   . ASN A 149  ? 1.6896 2.5195 1.2807 0.5992  -0.5379 -0.5872 149  ASN A N   
1018  C CA  . ASN A 149  ? 1.6793 2.5384 1.2640 0.6222  -0.5567 -0.5753 149  ASN A CA  
1019  C C   . ASN A 149  ? 1.6254 2.4962 1.2482 0.6299  -0.5567 -0.5600 149  ASN A C   
1020  O O   . ASN A 149  ? 1.5757 2.4416 1.2332 0.6139  -0.5468 -0.5665 149  ASN A O   
1021  C CB  . ASN A 149  ? 1.7372 2.6387 1.3250 0.6185  -0.5793 -0.6005 149  ASN A CB  
1022  C CG  . ASN A 149  ? 1.7632 2.6870 1.3991 0.6006  -0.5825 -0.6220 149  ASN A CG  
1023  O OD1 . ASN A 149  ? 1.7519 2.6531 1.4083 0.5830  -0.5651 -0.6273 149  ASN A OD1 
1024  N ND2 . ASN A 149  ? 1.7914 2.7595 1.4463 0.6051  -0.6045 -0.6335 149  ASN A ND2 
1025  N N   . ASP A 150  ? 1.5928 2.4801 1.2099 0.6537  -0.5673 -0.5406 150  ASP A N   
1026  C CA  . ASP A 150  ? 1.6007 2.5016 1.2549 0.6629  -0.5670 -0.5257 150  ASP A CA  
1027  C C   . ASP A 150  ? 1.5409 2.4511 1.2433 0.6422  -0.5625 -0.5419 150  ASP A C   
1028  O O   . ASP A 150  ? 1.5170 2.4221 1.2486 0.6429  -0.5520 -0.5294 150  ASP A O   
1029  C CB  . ASP A 150  ? 1.6324 2.5732 1.2886 0.6848  -0.5894 -0.5181 150  ASP A CB  
1030  C CG  . ASP A 150  ? 1.8275 2.8099 1.4917 0.6767  -0.6130 -0.5455 150  ASP A CG  
1031  O OD1 . ASP A 150  ? 1.8037 2.8220 1.5068 0.6784  -0.6262 -0.5506 150  ASP A OD1 
1032  O OD2 . ASP A 150  ? 1.8618 2.8417 1.4945 0.6684  -0.6179 -0.5622 150  ASP A OD2 
1033  N N   . ASP A 151  ? 1.5892 2.5126 1.3000 0.6233  -0.5693 -0.5705 151  ASP A N   
1034  C CA  . ASP A 151  ? 1.6168 2.5524 1.3733 0.6038  -0.5668 -0.5888 151  ASP A CA  
1035  C C   . ASP A 151  ? 1.6020 2.5048 1.3590 0.5802  -0.5471 -0.5992 151  ASP A C   
1036  O O   . ASP A 151  ? 1.6115 2.5224 1.3977 0.5607  -0.5453 -0.6205 151  ASP A O   
1037  C CB  . ASP A 151  ? 1.6739 2.6517 1.4462 0.5991  -0.5887 -0.6150 151  ASP A CB  
1038  C CG  . ASP A 151  ? 1.6870 2.6923 1.5129 0.5940  -0.5939 -0.6228 151  ASP A CG  
1039  O OD1 . ASP A 151  ? 1.7066 2.7466 1.5515 0.5884  -0.6108 -0.6455 151  ASP A OD1 
1040  O OD2 . ASP A 151  ? 1.6673 2.6605 1.5173 0.5951  -0.5808 -0.6072 151  ASP A OD2 
1041  N N   . LEU A 152  ? 1.6232 2.4891 1.3488 0.5822  -0.5322 -0.5838 152  LEU A N   
1042  C CA  . LEU A 152  ? 1.6527 2.4856 1.3781 0.5614  -0.5127 -0.5888 152  LEU A CA  
1043  C C   . LEU A 152  ? 1.6929 2.5351 1.4301 0.5398  -0.5146 -0.6198 152  LEU A C   
1044  O O   . LEU A 152  ? 1.6727 2.5012 1.4320 0.5202  -0.5010 -0.6277 152  LEU A O   
1045  C CB  . LEU A 152  ? 1.6337 2.4517 1.3879 0.5531  -0.4971 -0.5768 152  LEU A CB  
1046  C CG  . LEU A 152  ? 1.6400 2.4441 1.3877 0.5703  -0.4896 -0.5470 152  LEU A CG  
1047  C CD1 . LEU A 152  ? 1.6523 2.4364 1.3559 0.5865  -0.4884 -0.5315 152  LEU A CD1 
1048  C CD2 . LEU A 152  ? 1.6538 2.4902 1.4256 0.5852  -0.5020 -0.5422 152  LEU A CD2 
1049  N N   . LYS A 153  ? 1.7419 2.6083 1.4653 0.5431  -0.5309 -0.6375 153  LYS A N   
1050  C CA  . LYS A 153  ? 1.7565 2.6301 1.4862 0.5233  -0.5311 -0.6681 153  LYS A CA  
1051  C C   . LYS A 153  ? 1.7969 2.6558 1.4847 0.5243  -0.5290 -0.6727 153  LYS A C   
1052  O O   . LYS A 153  ? 1.7727 2.6244 1.4268 0.5424  -0.5330 -0.6547 153  LYS A O   
1053  C CB  . LYS A 153  ? 1.7918 2.7108 1.5487 0.5217  -0.5514 -0.6910 153  LYS A CB  
1054  C CG  . LYS A 153  ? 1.7774 2.7050 1.5826 0.5067  -0.5466 -0.7021 153  LYS A CG  
1055  C CD  . LYS A 153  ? 1.8072 2.7815 1.6416 0.5093  -0.5682 -0.7205 153  LYS A CD  
1056  C CE  . LYS A 153  ? 1.8045 2.7858 1.6891 0.4962  -0.5623 -0.7290 153  LYS A CE  
1057  N NZ  . LYS A 153  ? 1.7870 2.7443 1.6820 0.4993  -0.5471 -0.7030 153  LYS A NZ  
1058  N N   . PRO A 154  ? 1.8481 2.7016 1.5388 0.5044  -0.5213 -0.6972 154  PRO A N   
1059  C CA  . PRO A 154  ? 1.9264 2.7592 1.5825 0.5002  -0.5127 -0.7031 154  PRO A CA  
1060  C C   . PRO A 154  ? 1.9751 2.8065 1.5878 0.5212  -0.5219 -0.6873 154  PRO A C   
1061  O O   . PRO A 154  ? 2.0077 2.8044 1.5929 0.5247  -0.5075 -0.6719 154  PRO A O   
1062  C CB  . PRO A 154  ? 1.9296 2.7890 1.5977 0.4842  -0.5200 -0.7397 154  PRO A CB  
1063  C CG  . PRO A 154  ? 1.9089 2.7812 1.6246 0.4711  -0.5184 -0.7510 154  PRO A CG  
1064  C CD  . PRO A 154  ? 1.8690 2.7396 1.5988 0.4845  -0.5207 -0.7238 154  PRO A CD  
1065  N N   . ALA A 155  ? 2.0328 2.9014 1.6403 0.5350  -0.5452 -0.6907 155  ALA A N   
1066  C CA  . ALA A 155  ? 2.0753 2.9457 1.6418 0.5568  -0.5555 -0.6736 155  ALA A CA  
1067  C C   . ALA A 155  ? 2.1599 3.0230 1.6855 0.5523  -0.5543 -0.6880 155  ALA A C   
1068  O O   . ALA A 155  ? 2.1794 3.0220 1.6661 0.5658  -0.5507 -0.6704 155  ALA A O   
1069  C CB  . ALA A 155  ? 2.0460 2.8823 1.6016 0.5715  -0.5421 -0.6390 155  ALA A CB  
1070  N N   . LYS A 156  ? 2.1859 3.0650 1.7208 0.5329  -0.5559 -0.7205 156  LYS A N   
1071  C CA  . LYS A 156  ? 2.2166 3.0845 1.7172 0.5237  -0.5493 -0.7372 156  LYS A CA  
1072  C C   . LYS A 156  ? 2.2048 3.0791 1.6580 0.5433  -0.5625 -0.7244 156  LYS A C   
1073  O O   . LYS A 156  ? 2.2031 3.1129 1.6545 0.5583  -0.5859 -0.7195 156  LYS A O   
1074  C CB  . LYS A 156  ? 2.2642 3.1625 1.7819 0.5036  -0.5560 -0.7761 156  LYS A CB  
1075  C CG  . LYS A 156  ? 2.2631 3.1502 1.8239 0.4823  -0.5390 -0.7908 156  LYS A CG  
1076  C CD  . LYS A 156  ? 2.2953 3.2255 1.8891 0.4700  -0.5538 -0.8225 156  LYS A CD  
1077  C CE  . LYS A 156  ? 2.2937 3.2183 1.9367 0.4587  -0.5434 -0.8243 156  LYS A CE  
1078  N NZ  . LYS A 156  ? 2.3176 3.2861 1.9969 0.4516  -0.5605 -0.8498 156  LYS A NZ  
1079  N N   . ARG A 157  ? 2.1747 3.0138 1.5908 0.5433  -0.5467 -0.7182 157  ARG A N   
1080  C CA  . ARG A 157  ? 2.1723 3.0096 1.5394 0.5613  -0.5550 -0.7044 157  ARG A CA  
1081  C C   . ARG A 157  ? 2.2198 3.0147 1.5562 0.5521  -0.5316 -0.7069 157  ARG A C   
1082  O O   . ARG A 157  ? 2.2209 2.9883 1.5783 0.5356  -0.5099 -0.7128 157  ARG A O   
1083  C CB  . ARG A 157  ? 2.0829 2.9094 1.4474 0.5862  -0.5574 -0.6674 157  ARG A CB  
1084  C CG  . ARG A 157  ? 1.9984 2.8645 1.3947 0.5972  -0.5786 -0.6614 157  ARG A CG  
1085  C CD  . ARG A 157  ? 1.9222 2.7726 1.3246 0.6181  -0.5746 -0.6263 157  ARG A CD  
1086  N NE  . ARG A 157  ? 1.8818 2.7706 1.3182 0.6274  -0.5931 -0.6219 157  ARG A NE  
1087  C CZ  . ARG A 157  ? 1.8563 2.7432 1.3037 0.6467  -0.5937 -0.5937 157  ARG A CZ  
1088  N NH1 . ARG A 157  ? 1.8453 2.6940 1.2711 0.6589  -0.5774 -0.5680 157  ARG A NH1 
1089  N NH2 . ARG A 157  ? 1.8373 2.7603 1.3194 0.6536  -0.6095 -0.5917 157  ARG A NH2 
1090  N N   . GLU A 158  ? 2.2803 3.0688 1.5680 0.5624  -0.5347 -0.7016 158  GLU A N   
1091  C CA  . GLU A 158  ? 2.3187 3.0600 1.5788 0.5562  -0.5092 -0.6983 158  GLU A CA  
1092  C C   . GLU A 158  ? 2.2828 2.9871 1.5242 0.5773  -0.4988 -0.6613 158  GLU A C   
1093  O O   . GLU A 158  ? 2.3080 3.0235 1.5237 0.5991  -0.5134 -0.6434 158  GLU A O   
1094  C CB  . GLU A 158  ? 2.4279 3.1774 1.6464 0.5475  -0.5119 -0.7218 158  GLU A CB  
1095  C CG  . GLU A 158  ? 2.4998 3.2722 1.7392 0.5213  -0.5115 -0.7607 158  GLU A CG  
1096  C CD  . GLU A 158  ? 2.5982 3.3669 1.7973 0.5083  -0.5050 -0.7845 158  GLU A CD  
1097  O OE1 . GLU A 158  ? 2.6240 3.3478 1.8019 0.5051  -0.4805 -0.7771 158  GLU A OE1 
1098  O OE2 . GLU A 158  ? 2.6459 3.4568 1.8354 0.5005  -0.5240 -0.8110 158  GLU A OE2 
1099  N N   . THR A 159  ? 2.2014 2.8623 1.4575 0.5705  -0.4731 -0.6501 159  THR A N   
1100  C CA  . THR A 159  ? 2.1088 2.7339 1.3582 0.5878  -0.4609 -0.6159 159  THR A CA  
1101  C C   . THR A 159  ? 2.0167 2.5952 1.2347 0.5857  -0.4376 -0.6100 159  THR A C   
1102  O O   . THR A 159  ? 2.0127 2.5794 1.2274 0.5663  -0.4243 -0.6316 159  THR A O   
1103  C CB  . THR A 159  ? 2.1109 2.7240 1.4072 0.5825  -0.4506 -0.6037 159  THR A CB  
1104  O OG1 . THR A 159  ? 2.1048 2.7594 1.4334 0.5818  -0.4699 -0.6117 159  THR A OG1 
1105  C CG2 . THR A 159  ? 2.1078 2.6896 1.3991 0.6010  -0.4404 -0.5689 159  THR A CG2 
1106  N N   . VAL A 160  ? 1.9359 2.4868 1.1336 0.6054  -0.4308 -0.5812 160  VAL A N   
1107  C CA  . VAL A 160  ? 1.9034 2.4093 1.0706 0.6049  -0.4088 -0.5749 160  VAL A CA  
1108  C C   . VAL A 160  ? 1.8824 2.3469 1.0541 0.6177  -0.3911 -0.5435 160  VAL A C   
1109  O O   . VAL A 160  ? 1.8706 2.3347 1.0296 0.6402  -0.3981 -0.5205 160  VAL A O   
1110  C CB  . VAL A 160  ? 1.9344 2.4457 1.0488 0.6159  -0.4177 -0.5782 160  VAL A CB  
1111  C CG1 . VAL A 160  ? 1.9391 2.4069 1.0252 0.6330  -0.4016 -0.5514 160  VAL A CG1 
1112  C CG2 . VAL A 160  ? 1.9691 2.4819 1.0660 0.5943  -0.4116 -0.6096 160  VAL A CG2 
1113  N N   . LEU A 161  ? 1.8883 2.3174 1.0783 0.6033  -0.3673 -0.5426 161  LEU A N   
1114  C CA  . LEU A 161  ? 1.8724 2.2618 1.0694 0.6132  -0.3497 -0.5140 161  LEU A CA  
1115  C C   . LEU A 161  ? 1.9097 2.2563 1.0733 0.6158  -0.3296 -0.5086 161  LEU A C   
1116  O O   . LEU A 161  ? 1.9473 2.2924 1.0831 0.6067  -0.3266 -0.5288 161  LEU A O   
1117  C CB  . LEU A 161  ? 1.8282 2.2075 1.0733 0.5989  -0.3381 -0.5091 161  LEU A CB  
1118  C CG  . LEU A 161  ? 1.8100 2.2026 1.0804 0.5735  -0.3350 -0.5359 161  LEU A CG  
1119  C CD1 . LEU A 161  ? 1.8317 2.1946 1.0849 0.5607  -0.3147 -0.5484 161  LEU A CD1 
1120  C CD2 . LEU A 161  ? 1.7589 2.1476 1.0761 0.5632  -0.3279 -0.5267 161  LEU A CD2 
1121  N N   . THR A 162  ? 1.8666 2.1783 1.0345 0.6272  -0.3149 -0.4820 162  THR A N   
1122  C CA  . THR A 162  ? 1.8726 2.1435 1.0067 0.6364  -0.2977 -0.4710 162  THR A CA  
1123  C C   . THR A 162  ? 1.8484 2.0812 1.0058 0.6417  -0.2786 -0.4445 162  THR A C   
1124  O O   . THR A 162  ? 1.8424 2.0717 0.9982 0.6612  -0.2820 -0.4220 162  THR A O   
1125  C CB  . THR A 162  ? 2.1821 2.4652 1.2714 0.6596  -0.3125 -0.4637 162  THR A CB  
1126  O OG1 . THR A 162  ? 2.1880 2.4307 1.2583 0.6766  -0.2967 -0.4397 162  THR A OG1 
1127  C CG2 . THR A 162  ? 2.1440 2.4708 1.2474 0.6727  -0.3379 -0.4572 162  THR A CG2 
1128  N N   . PHE A 163  ? 1.8324 2.0380 1.0131 0.6240  -0.2581 -0.4472 163  PHE A N   
1129  C CA  . PHE A 163  ? 1.8045 1.9737 1.0093 0.6266  -0.2392 -0.4228 163  PHE A CA  
1130  C C   . PHE A 163  ? 1.8284 1.9633 1.0050 0.6468  -0.2282 -0.4025 163  PHE A C   
1131  O O   . PHE A 163  ? 1.8743 1.9926 1.0124 0.6508  -0.2219 -0.4096 163  PHE A O   
1132  C CB  . PHE A 163  ? 1.8031 1.9458 1.0298 0.6052  -0.2173 -0.4305 163  PHE A CB  
1133  C CG  . PHE A 163  ? 1.7814 1.9516 1.0359 0.5841  -0.2231 -0.4513 163  PHE A CG  
1134  C CD1 . PHE A 163  ? 1.8041 2.0055 1.0401 0.5772  -0.2368 -0.4787 163  PHE A CD1 
1135  C CD2 . PHE A 163  ? 1.7327 1.8979 1.0321 0.5710  -0.2145 -0.4435 163  PHE A CD2 
1136  C CE1 . PHE A 163  ? 1.8111 2.0369 1.0744 0.5577  -0.2407 -0.4990 163  PHE A CE1 
1137  C CE2 . PHE A 163  ? 1.7273 1.9162 1.0530 0.5519  -0.2182 -0.4623 163  PHE A CE2 
1138  C CZ  . PHE A 163  ? 1.7740 1.9925 1.0827 0.5451  -0.2306 -0.4907 163  PHE A CZ  
1139  N N   . ILE A 164  ? 1.8011 1.9229 0.9971 0.6582  -0.2238 -0.3776 164  ILE A N   
1140  C CA  . ILE A 164  ? 1.8583 1.9496 1.0294 0.6786  -0.2138 -0.3586 164  ILE A CA  
1141  C C   . ILE A 164  ? 1.8752 1.9282 1.0725 0.6779  -0.1927 -0.3381 164  ILE A C   
1142  O O   . ILE A 164  ? 1.8375 1.8980 1.0680 0.6785  -0.1952 -0.3237 164  ILE A O   
1143  C CB  . ILE A 164  ? 1.9000 2.0150 1.0630 0.7001  -0.2304 -0.3457 164  ILE A CB  
1144  C CG1 . ILE A 164  ? 1.9369 2.0962 1.0798 0.7016  -0.2546 -0.3639 164  ILE A CG1 
1145  C CG2 . ILE A 164  ? 1.9332 2.0152 1.0680 0.7219  -0.2183 -0.3272 164  ILE A CG2 
1146  C CD1 . ILE A 164  ? 1.9360 2.1205 1.0715 0.7244  -0.2710 -0.3505 164  ILE A CD1 
1147  N N   . ASP A 165  ? 1.9459 1.9579 1.1282 0.6766  -0.1715 -0.3367 165  ASP A N   
1148  C CA  . ASP A 165  ? 1.9830 1.9578 1.1943 0.6732  -0.1503 -0.3188 165  ASP A CA  
1149  C C   . ASP A 165  ? 1.8981 1.8689 1.1209 0.6915  -0.1517 -0.2938 165  ASP A C   
1150  O O   . ASP A 165  ? 1.8626 1.8502 1.0642 0.7094  -0.1643 -0.2896 165  ASP A O   
1151  C CB  . ASP A 165  ? 2.1293 2.0585 1.3211 0.6705  -0.1260 -0.3214 165  ASP A CB  
1152  C CG  . ASP A 165  ? 2.2736 2.1754 1.4297 0.6933  -0.1183 -0.3086 165  ASP A CG  
1153  O OD1 . ASP A 165  ? 2.3114 2.2312 1.4555 0.7122  -0.1322 -0.2984 165  ASP A OD1 
1154  O OD2 . ASP A 165  ? 2.3325 2.1934 1.4733 0.6920  -0.0966 -0.3090 165  ASP A OD2 
1155  N N   . PRO A 166  ? 1.8958 1.8449 1.1537 0.6866  -0.1381 -0.2771 166  PRO A N   
1156  C CA  . PRO A 166  ? 1.8699 1.8163 1.1458 0.7000  -0.1380 -0.2544 166  PRO A CA  
1157  C C   . PRO A 166  ? 1.8693 1.7912 1.1145 0.7236  -0.1298 -0.2431 166  PRO A C   
1158  O O   . PRO A 166  ? 1.8396 1.7518 1.0998 0.7349  -0.1247 -0.2243 166  PRO A O   
1159  C CB  . PRO A 166  ? 1.8836 1.8046 1.1986 0.6873  -0.1214 -0.2413 166  PRO A CB  
1160  C CG  . PRO A 166  ? 1.9025 1.8273 1.2293 0.6650  -0.1188 -0.2577 166  PRO A CG  
1161  C CD  . PRO A 166  ? 1.9198 1.8476 1.2052 0.6665  -0.1219 -0.2793 166  PRO A CD  
1162  N N   . GLU A 167  ? 1.9040 1.8154 1.1068 0.7307  -0.1277 -0.2543 167  GLU A N   
1163  C CA  . GLU A 167  ? 1.9490 1.8364 1.1212 0.7538  -0.1193 -0.2428 167  GLU A CA  
1164  C C   . GLU A 167  ? 1.9689 1.8860 1.1038 0.7671  -0.1378 -0.2512 167  GLU A C   
1165  O O   . GLU A 167  ? 2.0106 1.9180 1.1196 0.7888  -0.1356 -0.2408 167  GLU A O   
1166  C CB  . GLU A 167  ? 2.0228 1.8625 1.1751 0.7526  -0.0959 -0.2441 167  GLU A CB  
1167  C CG  . GLU A 167  ? 2.0516 1.8538 1.2377 0.7500  -0.0744 -0.2270 167  GLU A CG  
1168  C CD  . GLU A 167  ? 2.1404 1.8927 1.3060 0.7503  -0.0495 -0.2284 167  GLU A CD  
1169  O OE1 . GLU A 167  ? 2.1782 1.9081 1.3097 0.7693  -0.0415 -0.2228 167  GLU A OE1 
1170  O OE2 . GLU A 167  ? 2.1603 1.8947 1.3444 0.7316  -0.0364 -0.2349 167  GLU A OE2 
1171  N N   . GLY A 168  ? 1.9632 1.9174 1.0972 0.7544  -0.1561 -0.2696 168  GLY A N   
1172  C CA  . GLY A 168  ? 1.9835 1.9739 1.0903 0.7662  -0.1773 -0.2764 168  GLY A CA  
1173  C C   . GLY A 168  ? 2.0670 2.0535 1.1253 0.7672  -0.1789 -0.2922 168  GLY A C   
1174  O O   . GLY A 168  ? 2.0915 2.0964 1.1173 0.7836  -0.1919 -0.2917 168  GLY A O   
1175  N N   . SER A 169  ? 2.0987 2.0609 1.1519 0.7498  -0.1648 -0.3054 169  SER A N   
1176  C CA  . SER A 169  ? 2.1849 2.1539 1.1966 0.7436  -0.1696 -0.3268 169  SER A CA  
1177  C C   . SER A 169  ? 2.1430 2.1443 1.1748 0.7198  -0.1814 -0.3497 169  SER A C   
1178  O O   . SER A 169  ? 2.0978 2.0963 1.1720 0.7040  -0.1748 -0.3498 169  SER A O   
1179  C CB  . SER A 169  ? 2.2703 2.1901 1.2550 0.7406  -0.1444 -0.3294 169  SER A CB  
1180  O OG  . SER A 169  ? 2.3365 2.2655 1.2716 0.7392  -0.1511 -0.3478 169  SER A OG  
1181  N N   . GLU A 170  ? 2.1653 2.1990 1.1672 0.7176  -0.1993 -0.3687 170  GLU A N   
1182  C CA  . GLU A 170  ? 2.1578 2.2231 1.1761 0.6951  -0.2102 -0.3932 170  GLU A CA  
1183  C C   . GLU A 170  ? 2.1051 2.1359 1.1343 0.6737  -0.1856 -0.4043 170  GLU A C   
1184  O O   . GLU A 170  ? 2.0901 2.0760 1.1078 0.6777  -0.1631 -0.3943 170  GLU A O   
1185  C CB  . GLU A 170  ? 2.2695 2.3701 1.2474 0.6963  -0.2308 -0.4128 170  GLU A CB  
1186  C CG  . GLU A 170  ? 2.3363 2.4719 1.3013 0.7190  -0.2551 -0.4009 170  GLU A CG  
1187  C CD  . GLU A 170  ? 2.4450 2.6185 1.3725 0.7187  -0.2769 -0.4202 170  GLU A CD  
1188  O OE1 . GLU A 170  ? 2.5182 2.6759 1.4027 0.7148  -0.2697 -0.4320 170  GLU A OE1 
1189  O OE2 . GLU A 170  ? 2.4518 2.6716 1.3938 0.7216  -0.3011 -0.4238 170  GLU A OE2 
1190  N N   . VAL A 171  ? 2.0779 2.1284 1.1315 0.6511  -0.1882 -0.4247 171  VAL A N   
1191  C CA  . VAL A 171  ? 2.0896 2.1088 1.1552 0.6301  -0.1635 -0.4364 171  VAL A CA  
1192  C C   . VAL A 171  ? 2.0521 2.1002 1.1215 0.6075  -0.1699 -0.4675 171  VAL A C   
1193  O O   . VAL A 171  ? 2.0674 2.0940 1.1377 0.5892  -0.1498 -0.4833 171  VAL A O   
1194  C CB  . VAL A 171  ? 2.1147 2.1079 1.2310 0.6242  -0.1461 -0.4178 171  VAL A CB  
1195  C CG1 . VAL A 171  ? 2.1329 2.1008 1.2687 0.6006  -0.1219 -0.4313 171  VAL A CG1 
1196  C CG2 . VAL A 171  ? 2.1178 2.0748 1.2302 0.6440  -0.1340 -0.3894 171  VAL A CG2 
1197  N N   . ASP A 172  ? 2.0030 2.0997 1.0760 0.6084  -0.1966 -0.4772 172  ASP A N   
1198  C CA  . ASP A 172  ? 2.0246 2.1523 1.1040 0.5872  -0.2040 -0.5079 172  ASP A CA  
1199  C C   . ASP A 172  ? 2.0265 2.2070 1.0934 0.5960  -0.2367 -0.5161 172  ASP A C   
1200  O O   . ASP A 172  ? 2.0162 2.2061 1.0645 0.6183  -0.2513 -0.4985 172  ASP A O   
1201  C CB  . ASP A 172  ? 2.0147 2.1403 1.1496 0.5682  -0.1930 -0.5100 172  ASP A CB  
1202  C CG  . ASP A 172  ? 2.0699 2.2101 1.2132 0.5425  -0.1876 -0.5429 172  ASP A CG  
1203  O OD1 . ASP A 172  ? 2.0609 2.1803 1.2399 0.5255  -0.1662 -0.5451 172  ASP A OD1 
1204  O OD2 . ASP A 172  ? 2.1057 2.2788 1.2219 0.5393  -0.2043 -0.5662 172  ASP A OD2 
1205  N N   . MET A 173  ? 2.0269 2.2420 1.1065 0.5785  -0.2473 -0.5425 173  MET A N   
1206  C CA  . MET A 173  ? 2.0148 2.2815 1.0883 0.5847  -0.2779 -0.5519 173  MET A CA  
1207  C C   . MET A 173  ? 1.9838 2.2771 1.0775 0.5601  -0.2806 -0.5836 173  MET A C   
1208  O O   . MET A 173  ? 2.0130 2.2854 1.1078 0.5412  -0.2598 -0.6004 173  MET A O   
1209  C CB  . MET A 173  ? 2.0822 2.3587 1.0995 0.5995  -0.2910 -0.5539 173  MET A CB  
1210  C CG  . MET A 173  ? 2.0962 2.4152 1.1078 0.6189  -0.3214 -0.5445 173  MET A CG  
1211  S SD  . MET A 173  ? 2.3312 2.6513 1.2806 0.6451  -0.3335 -0.5307 173  MET A SD  
1212  C CE  . MET A 173  ? 2.2510 2.5026 1.1858 0.6525  -0.3000 -0.5087 173  MET A CE  
1213  N N   . VAL A 174  ? 1.9456 2.2843 1.0586 0.5599  -0.3043 -0.5918 174  VAL A N   
1214  C CA  . VAL A 174  ? 1.9673 2.3379 1.0951 0.5382  -0.3105 -0.6250 174  VAL A CA  
1215  C C   . VAL A 174  ? 1.9414 2.3635 1.0895 0.5422  -0.3396 -0.6308 174  VAL A C   
1216  O O   . VAL A 174  ? 1.9323 2.3591 1.1073 0.5531  -0.3465 -0.6100 174  VAL A O   
1217  C CB  . VAL A 174  ? 1.9873 2.3339 1.1542 0.5150  -0.2846 -0.6346 174  VAL A CB  
1218  C CG1 . VAL A 174  ? 1.9605 2.2763 1.1602 0.5216  -0.2711 -0.6040 174  VAL A CG1 
1219  C CG2 . VAL A 174  ? 1.9861 2.3711 1.1838 0.4965  -0.2943 -0.6624 174  VAL A CG2 
1220  N N   . GLU A 175  ? 1.9273 2.3881 1.0623 0.5333  -0.3562 -0.6593 175  GLU A N   
1221  C CA  . GLU A 175  ? 1.9106 2.4214 1.0675 0.5345  -0.3828 -0.6689 175  GLU A CA  
1222  C C   . GLU A 175  ? 1.8778 2.4012 1.0755 0.5092  -0.3756 -0.6954 175  GLU A C   
1223  O O   . GLU A 175  ? 1.8642 2.3598 1.0678 0.4917  -0.3510 -0.7070 175  GLU A O   
1224  C CB  . GLU A 175  ? 1.9972 2.5457 1.1140 0.5423  -0.4077 -0.6819 175  GLU A CB  
1225  C CG  . GLU A 175  ? 2.0841 2.6121 1.1502 0.5380  -0.3966 -0.6924 175  GLU A CG  
1226  C CD  . GLU A 175  ? 2.1274 2.6775 1.1431 0.5574  -0.4192 -0.6854 175  GLU A CD  
1227  O OE1 . GLU A 175  ? 2.1215 2.7217 1.1355 0.5607  -0.4475 -0.6966 175  GLU A OE1 
1228  O OE2 . GLU A 175  ? 2.1502 2.6667 1.1284 0.5695  -0.4081 -0.6681 175  GLU A OE2 
1229  N N   . GLU A 176  ? 1.8960 2.4595 1.1238 0.5075  -0.3951 -0.7042 176  GLU A N   
1230  C CA  . GLU A 176  ? 1.9103 2.4890 1.1789 0.4842  -0.3896 -0.7302 176  GLU A CA  
1231  C C   . GLU A 176  ? 1.9610 2.5909 1.2508 0.4872  -0.4178 -0.7406 176  GLU A C   
1232  O O   . GLU A 176  ? 1.9498 2.5964 1.2332 0.5075  -0.4374 -0.7211 176  GLU A O   
1233  C CB  . GLU A 176  ? 1.8597 2.4027 1.1673 0.4758  -0.3651 -0.7157 176  GLU A CB  
1234  C CG  . GLU A 176  ? 2.0734 2.6136 1.4149 0.4489  -0.3465 -0.7420 176  GLU A CG  
1235  C CD  . GLU A 176  ? 2.2602 2.7581 1.5927 0.4357  -0.3151 -0.7464 176  GLU A CD  
1236  O OE1 . GLU A 176  ? 2.2936 2.7839 1.5856 0.4369  -0.3123 -0.7548 176  GLU A OE1 
1237  O OE2 . GLU A 176  ? 2.2315 2.7038 1.5986 0.4235  -0.2923 -0.7414 176  GLU A OE2 
1238  N N   . ILE A 177  ? 2.0117 2.6661 1.3285 0.4671  -0.4188 -0.7715 177  ILE A N   
1239  C CA  . ILE A 177  ? 2.0532 2.7585 1.3903 0.4677  -0.4454 -0.7864 177  ILE A CA  
1240  C C   . ILE A 177  ? 2.0520 2.7604 1.4386 0.4663  -0.4450 -0.7767 177  ILE A C   
1241  O O   . ILE A 177  ? 2.0118 2.6901 1.4241 0.4546  -0.4221 -0.7725 177  ILE A O   
1242  C CB  . ILE A 177  ? 2.0956 2.8313 1.4345 0.4466  -0.4491 -0.8287 177  ILE A CB  
1243  C CG1 . ILE A 177  ? 2.0777 2.7998 1.4592 0.4226  -0.4258 -0.8476 177  ILE A CG1 
1244  C CG2 . ILE A 177  ? 2.1410 2.8680 1.4306 0.4437  -0.4442 -0.8402 177  ILE A CG2 
1245  C CD1 . ILE A 177  ? 2.0341 2.7832 1.4645 0.4180  -0.4359 -0.8543 177  ILE A CD1 
1246  N N   . ASP A 178  ? 2.0848 2.8299 1.4852 0.4776  -0.4698 -0.7729 178  ASP A N   
1247  C CA  . ASP A 178  ? 2.0954 2.8436 1.5402 0.4774  -0.4701 -0.7622 178  ASP A CA  
1248  C C   . ASP A 178  ? 2.1324 2.9143 1.6160 0.4604  -0.4774 -0.7921 178  ASP A C   
1249  O O   . ASP A 178  ? 2.1487 2.9705 1.6441 0.4670  -0.5010 -0.7985 178  ASP A O   
1250  C CB  . ASP A 178  ? 2.0499 2.8100 1.4917 0.5015  -0.4880 -0.7339 178  ASP A CB  
1251  C CG  . ASP A 178  ? 1.9521 2.6988 1.4314 0.5018  -0.4799 -0.7151 178  ASP A CG  
1252  O OD1 . ASP A 178  ? 1.9216 2.6683 1.3990 0.5205  -0.4876 -0.6889 178  ASP A OD1 
1253  O OD2 . ASP A 178  ? 1.9144 2.6502 1.4243 0.4829  -0.4648 -0.7266 178  ASP A OD2 
1254  N N   . HIS A 179  ? 2.1577 2.9224 1.6638 0.4389  -0.4559 -0.8093 179  HIS A N   
1255  C CA  . HIS A 179  ? 2.1779 2.9709 1.7209 0.4212  -0.4590 -0.8402 179  HIS A CA  
1256  C C   . HIS A 179  ? 2.1126 2.9137 1.6965 0.4227  -0.4635 -0.8297 179  HIS A C   
1257  O O   . HIS A 179  ? 2.0973 2.9339 1.7082 0.4169  -0.4776 -0.8502 179  HIS A O   
1258  C CB  . HIS A 179  ? 2.2625 3.0332 1.8178 0.3979  -0.4320 -0.8616 179  HIS A CB  
1259  C CG  . HIS A 179  ? 2.3658 3.1707 1.9392 0.3800  -0.4370 -0.9027 179  HIS A CG  
1260  N ND1 . HIS A 179  ? 2.4332 3.2466 1.9828 0.3698  -0.4343 -0.9293 179  HIS A ND1 
1261  C CD2 . HIS A 179  ? 2.3861 3.2188 1.9996 0.3700  -0.4439 -0.9228 179  HIS A CD2 
1262  C CE1 . HIS A 179  ? 2.4670 3.3133 2.0420 0.3542  -0.4395 -0.9645 179  HIS A CE1 
1263  N NE2 . HIS A 179  ? 2.4378 3.2959 2.0524 0.3544  -0.4454 -0.9610 179  HIS A NE2 
1264  N N   . ILE A 180  ? 2.0561 2.8253 1.6455 0.4298  -0.4516 -0.7987 180  ILE A N   
1265  C CA  . ILE A 180  ? 1.9933 2.7686 1.6203 0.4292  -0.4541 -0.7894 180  ILE A CA  
1266  C C   . ILE A 180  ? 1.9082 2.6710 1.5296 0.4482  -0.4583 -0.7531 180  ILE A C   
1267  O O   . ILE A 180  ? 1.8327 2.6121 1.4797 0.4518  -0.4677 -0.7474 180  ILE A O   
1268  C CB  . ILE A 180  ? 1.7704 2.5262 1.4322 0.4074  -0.4311 -0.7991 180  ILE A CB  
1269  C CG1 . ILE A 180  ? 1.7489 2.4584 1.3989 0.4035  -0.4056 -0.7808 180  ILE A CG1 
1270  C CG2 . ILE A 180  ? 1.7989 2.5757 1.4759 0.3890  -0.4293 -0.8381 180  ILE A CG2 
1271  C CD1 . ILE A 180  ? 1.7150 2.4075 1.3991 0.3824  -0.3833 -0.7898 180  ILE A CD1 
1272  N N   . GLY A 181  ? 1.8859 2.6196 1.4751 0.4599  -0.4505 -0.7298 181  GLY A N   
1273  C CA  . GLY A 181  ? 1.8338 2.5545 1.4166 0.4779  -0.4528 -0.6964 181  GLY A CA  
1274  C C   . GLY A 181  ? 1.7815 2.4562 1.3555 0.4756  -0.4293 -0.6751 181  GLY A C   
1275  O O   . GLY A 181  ? 1.7811 2.4374 1.3440 0.4899  -0.4267 -0.6467 181  GLY A O   
1276  N N   . ILE A 182  ? 1.7561 2.4130 1.3378 0.4571  -0.4114 -0.6894 182  ILE A N   
1277  C CA  . ILE A 182  ? 1.7375 2.3514 1.3142 0.4527  -0.3878 -0.6715 182  ILE A CA  
1278  C C   . ILE A 182  ? 1.7428 2.3401 1.2877 0.4525  -0.3790 -0.6793 182  ILE A C   
1279  O O   . ILE A 182  ? 1.7574 2.3373 1.3104 0.4362  -0.3604 -0.6915 182  ILE A O   
1280  C CB  . ILE A 182  ? 1.7080 2.3100 1.3207 0.4316  -0.3703 -0.6782 182  ILE A CB  
1281  C CG1 . ILE A 182  ? 1.6920 2.3169 1.3362 0.4284  -0.3805 -0.6795 182  ILE A CG1 
1282  C CG2 . ILE A 182  ? 1.6907 2.2502 1.3028 0.4297  -0.3483 -0.6522 182  ILE A CG2 
1283  C CD1 . ILE A 182  ? 1.6870 2.3163 1.3666 0.4064  -0.3700 -0.6997 182  ILE A CD1 
1284  N N   . ILE A 183  ? 1.7492 2.3521 1.2585 0.4702  -0.3915 -0.6723 183  ILE A N   
1285  C CA  . ILE A 183  ? 1.7524 2.3364 1.2262 0.4720  -0.3830 -0.6760 183  ILE A CA  
1286  C C   . ILE A 183  ? 1.7412 2.2796 1.2189 0.4637  -0.3550 -0.6626 183  ILE A C   
1287  O O   . ILE A 183  ? 1.7439 2.2581 1.2264 0.4719  -0.3475 -0.6340 183  ILE A O   
1288  C CB  . ILE A 183  ? 1.7531 2.3370 1.1901 0.4959  -0.3958 -0.6565 183  ILE A CB  
1289  C CG1 . ILE A 183  ? 1.7456 2.3758 1.1765 0.5055  -0.4240 -0.6684 183  ILE A CG1 
1290  C CG2 . ILE A 183  ? 1.7949 2.3537 1.1941 0.4974  -0.3842 -0.6579 183  ILE A CG2 
1291  C CD1 . ILE A 183  ? 1.7638 2.3961 1.1586 0.5302  -0.4369 -0.6482 183  ILE A CD1 
1292  N N   . SER A 184  ? 1.7750 2.3026 1.2521 0.4474  -0.3391 -0.6834 184  SER A N   
1293  C CA  . SER A 184  ? 1.7507 2.2362 1.2377 0.4375  -0.3107 -0.6723 184  SER A CA  
1294  C C   . SER A 184  ? 1.8700 2.3278 1.3218 0.4405  -0.2973 -0.6718 184  SER A C   
1295  O O   . SER A 184  ? 1.9018 2.3635 1.3429 0.4283  -0.2905 -0.6985 184  SER A O   
1296  C CB  . SER A 184  ? 1.7531 2.2415 1.2771 0.4140  -0.2961 -0.6939 184  SER A CB  
1297  O OG  . SER A 184  ? 1.7209 2.2447 1.2696 0.4097  -0.3125 -0.7072 184  SER A OG  
1298  N N   . PHE A 185  ? 1.8344 2.2636 1.2692 0.4560  -0.2923 -0.6420 185  PHE A N   
1299  C CA  . PHE A 185  ? 1.8622 2.2629 1.2619 0.4615  -0.2802 -0.6380 185  PHE A CA  
1300  C C   . PHE A 185  ? 1.8385 2.1998 1.2544 0.4472  -0.2493 -0.6352 185  PHE A C   
1301  O O   . PHE A 185  ? 1.7871 2.1418 1.2418 0.4350  -0.2376 -0.6312 185  PHE A O   
1302  C CB  . PHE A 185  ? 1.8566 2.2421 1.2337 0.4849  -0.2867 -0.6068 185  PHE A CB  
1303  C CG  . PHE A 185  ? 1.8584 2.2774 1.2126 0.5020  -0.3142 -0.6071 185  PHE A CG  
1304  C CD1 . PHE A 185  ? 1.8976 2.3224 1.2083 0.5116  -0.3226 -0.6151 185  PHE A CD1 
1305  C CD2 . PHE A 185  ? 1.8371 2.2813 1.2137 0.5086  -0.3309 -0.5982 185  PHE A CD2 
1306  C CE1 . PHE A 185  ? 1.9136 2.3701 1.2049 0.5285  -0.3481 -0.6125 185  PHE A CE1 
1307  C CE2 . PHE A 185  ? 1.8516 2.3265 1.2110 0.5251  -0.3551 -0.5965 185  PHE A CE2 
1308  C CZ  . PHE A 185  ? 1.8984 2.3802 1.2158 0.5356  -0.3642 -0.6029 185  PHE A CZ  
1309  N N   . PRO A 186  ? 1.8963 2.2300 1.2830 0.4491  -0.2351 -0.6352 186  PRO A N   
1310  C CA  . PRO A 186  ? 1.9419 2.2387 1.3454 0.4343  -0.2039 -0.6352 186  PRO A CA  
1311  C C   . PRO A 186  ? 1.9318 2.1906 1.3422 0.4454  -0.1911 -0.5990 186  PRO A C   
1312  O O   . PRO A 186  ? 1.9547 2.2060 1.3367 0.4648  -0.2006 -0.5809 186  PRO A O   
1313  C CB  . PRO A 186  ? 1.9951 2.2836 1.3594 0.4313  -0.1966 -0.6554 186  PRO A CB  
1314  C CG  . PRO A 186  ? 2.0167 2.3290 1.3377 0.4513  -0.2245 -0.6531 186  PRO A CG  
1315  C CD  . PRO A 186  ? 1.9538 2.2848 1.2919 0.4657  -0.2447 -0.6316 186  PRO A CD  
1316  N N   . ASP A 187  ? 1.9318 2.1675 1.3804 0.4332  -0.1694 -0.5889 187  ASP A N   
1317  C CA  . ASP A 187  ? 1.9059 2.1056 1.3683 0.4407  -0.1554 -0.5546 187  ASP A CA  
1318  C C   . ASP A 187  ? 1.9036 2.0712 1.3305 0.4535  -0.1460 -0.5440 187  ASP A C   
1319  O O   . ASP A 187  ? 1.9013 2.0615 1.3023 0.4483  -0.1374 -0.5644 187  ASP A O   
1320  C CB  . ASP A 187  ? 1.9270 2.1057 1.4342 0.4227  -0.1298 -0.5498 187  ASP A CB  
1321  C CG  . ASP A 187  ? 1.9388 2.1442 1.4826 0.4123  -0.1378 -0.5529 187  ASP A CG  
1322  O OD1 . ASP A 187  ? 1.9406 2.1828 1.4766 0.4135  -0.1600 -0.5699 187  ASP A OD1 
1323  O OD2 . ASP A 187  ? 1.9367 2.1259 1.5178 0.4027  -0.1214 -0.5380 187  ASP A OD2 
1324  N N   . PHE A 188  ? 1.8489 1.9979 1.2748 0.4694  -0.1474 -0.5126 188  PHE A N   
1325  C CA  . PHE A 188  ? 1.8216 1.9404 1.2154 0.4845  -0.1403 -0.4989 188  PHE A CA  
1326  C C   . PHE A 188  ? 1.8166 1.8946 1.2379 0.4822  -0.1161 -0.4741 188  PHE A C   
1327  O O   . PHE A 188  ? 1.7910 1.8659 1.2343 0.4888  -0.1197 -0.4487 188  PHE A O   
1328  C CB  . PHE A 188  ? 1.7819 1.9165 1.1535 0.5067  -0.1637 -0.4831 188  PHE A CB  
1329  C CG  . PHE A 188  ? 1.7621 1.8647 1.1054 0.5245  -0.1564 -0.4639 188  PHE A CG  
1330  C CD1 . PHE A 188  ? 1.7538 1.8320 1.1152 0.5336  -0.1485 -0.4336 188  PHE A CD1 
1331  C CD2 . PHE A 188  ? 1.8118 1.9107 1.1096 0.5326  -0.1586 -0.4760 188  PHE A CD2 
1332  C CE1 . PHE A 188  ? 1.7624 1.8111 1.0993 0.5507  -0.1413 -0.4164 188  PHE A CE1 
1333  C CE2 . PHE A 188  ? 1.8294 1.8978 1.1005 0.5497  -0.1512 -0.4581 188  PHE A CE2 
1334  C CZ  . PHE A 188  ? 1.8046 1.8473 1.0965 0.5590  -0.1421 -0.4285 188  PHE A CZ  
1335  N N   . LYS A 189  ? 1.8646 1.9122 1.2860 0.4718  -0.0908 -0.4822 189  LYS A N   
1336  C CA  . LYS A 189  ? 1.8285 1.8369 1.2822 0.4666  -0.0645 -0.4610 189  LYS A CA  
1337  C C   . LYS A 189  ? 1.8339 1.8128 1.2728 0.4857  -0.0614 -0.4334 189  LYS A C   
1338  O O   . LYS A 189  ? 1.8530 1.8162 1.2528 0.4955  -0.0588 -0.4384 189  LYS A O   
1339  C CB  . LYS A 189  ? 1.8920 1.8777 1.3503 0.4489  -0.0368 -0.4814 189  LYS A CB  
1340  C CG  . LYS A 189  ? 1.9358 1.8727 1.4060 0.4491  -0.0080 -0.4632 189  LYS A CG  
1341  C CD  . LYS A 189  ? 1.9481 1.8717 1.4754 0.4380  0.0091  -0.4441 189  LYS A CD  
1342  C CE  . LYS A 189  ? 1.9854 1.8620 1.5293 0.4314  0.0436  -0.4365 189  LYS A CE  
1343  N NZ  . LYS A 189  ? 2.0103 1.8590 1.5145 0.4464  0.0474  -0.4311 189  LYS A NZ  
1344  N N   . ILE A 190  ? 1.7446 1.7164 1.2141 0.4907  -0.0617 -0.4046 190  ILE A N   
1345  C CA  . ILE A 190  ? 1.7573 1.7003 1.2196 0.5074  -0.0566 -0.3781 190  ILE A CA  
1346  C C   . ILE A 190  ? 1.8301 1.7273 1.2947 0.5026  -0.0261 -0.3762 190  ILE A C   
1347  O O   . ILE A 190  ? 1.9122 1.7955 1.4115 0.4861  -0.0061 -0.3772 190  ILE A O   
1348  C CB  . ILE A 190  ? 1.6830 1.6301 1.1836 0.5093  -0.0617 -0.3495 190  ILE A CB  
1349  C CG1 . ILE A 190  ? 1.5600 1.5522 1.0682 0.5055  -0.0860 -0.3571 190  ILE A CG1 
1350  C CG2 . ILE A 190  ? 1.5951 1.5225 1.0854 0.5289  -0.0630 -0.3237 190  ILE A CG2 
1351  C CD1 . ILE A 190  ? 1.5472 1.5622 1.0304 0.5237  -0.1105 -0.3509 190  ILE A CD1 
1352  N N   . PRO A 191  ? 1.8636 1.7364 1.2919 0.5168  -0.0212 -0.3735 191  PRO A N   
1353  C CA  . PRO A 191  ? 1.8749 1.7011 1.3001 0.5142  0.0080  -0.3717 191  PRO A CA  
1354  C C   . PRO A 191  ? 1.9212 1.7178 1.3985 0.5064  0.0309  -0.3486 191  PRO A C   
1355  O O   . PRO A 191  ? 1.8671 1.6733 1.3761 0.5099  0.0222  -0.3253 191  PRO A O   
1356  C CB  . PRO A 191  ? 1.8738 1.6836 1.2605 0.5367  0.0027  -0.3599 191  PRO A CB  
1357  C CG  . PRO A 191  ? 1.8619 1.7121 1.2142 0.5460  -0.0264 -0.3725 191  PRO A CG  
1358  C CD  . PRO A 191  ? 1.8329 1.7227 1.2179 0.5363  -0.0435 -0.3743 191  PRO A CD  
1359  N N   . SER A 192  ? 1.9532 1.7143 1.4391 0.4955  0.0603  -0.3551 192  SER A N   
1360  C CA  . SER A 192  ? 1.9305 1.6604 1.4672 0.4879  0.0852  -0.3335 192  SER A CA  
1361  C C   . SER A 192  ? 1.8344 1.5487 1.3812 0.5054  0.0809  -0.3007 192  SER A C   
1362  O O   . SER A 192  ? 1.7667 1.4790 1.3583 0.5032  0.0835  -0.2762 192  SER A O   
1363  C CB  . SER A 192  ? 1.9918 1.6806 1.5266 0.4773  0.1188  -0.3462 192  SER A CB  
1364  O OG  . SER A 192  ? 2.0346 1.7370 1.5418 0.4644  0.1208  -0.3815 192  SER A OG  
1365  N N   . ASN A 193  ? 1.8597 1.5638 1.3632 0.5229  0.0744  -0.3009 193  ASN A N   
1366  C CA  . ASN A 193  ? 1.8762 1.5656 1.3822 0.5413  0.0703  -0.2735 193  ASN A CA  
1367  C C   . ASN A 193  ? 1.8928 1.6023 1.3484 0.5597  0.0467  -0.2799 193  ASN A C   
1368  O O   . ASN A 193  ? 1.9425 1.6290 1.3590 0.5706  0.0539  -0.2858 193  ASN A O   
1369  C CB  . ASN A 193  ? 1.9155 1.5522 1.4275 0.5437  0.1003  -0.2639 193  ASN A CB  
1370  C CG  . ASN A 193  ? 1.9360 1.5543 1.4290 0.5657  0.0971  -0.2458 193  ASN A CG  
1371  O OD1 . ASN A 193  ? 1.9108 1.5548 1.3989 0.5783  0.0742  -0.2345 193  ASN A OD1 
1372  N ND2 . ASN A 193  ? 1.9738 1.5462 1.4570 0.5701  0.1218  -0.2437 193  ASN A ND2 
1373  N N   . PRO A 194  ? 1.8833 1.6357 1.3405 0.5629  0.0194  -0.2785 194  PRO A N   
1374  C CA  . PRO A 194  ? 1.8626 1.6427 1.2767 0.5776  -0.0048 -0.2878 194  PRO A CA  
1375  C C   . PRO A 194  ? 1.8313 1.5982 1.2314 0.5998  -0.0086 -0.2673 194  PRO A C   
1376  O O   . PRO A 194  ? 1.8071 1.5439 1.2313 0.6039  0.0065  -0.2460 194  PRO A O   
1377  C CB  . PRO A 194  ? 1.8500 1.6764 1.2845 0.5706  -0.0279 -0.2897 194  PRO A CB  
1378  C CG  . PRO A 194  ? 1.8597 1.6826 1.3402 0.5505  -0.0149 -0.2872 194  PRO A CG  
1379  C CD  . PRO A 194  ? 1.8615 1.6391 1.3636 0.5511  0.0111  -0.2688 194  PRO A CD  
1380  N N   . ARG A 195  ? 1.8845 1.6753 1.2467 0.6139  -0.0285 -0.2746 195  ARG A N   
1381  C CA  . ARG A 195  ? 1.9103 1.6976 1.2571 0.6360  -0.0357 -0.2577 195  ARG A CA  
1382  C C   . ARG A 195  ? 1.8757 1.6964 1.2544 0.6355  -0.0539 -0.2445 195  ARG A C   
1383  O O   . ARG A 195  ? 1.8675 1.7278 1.2392 0.6334  -0.0748 -0.2559 195  ARG A O   
1384  C CB  . ARG A 195  ? 1.9745 1.7776 1.2686 0.6496  -0.0497 -0.2729 195  ARG A CB  
1385  C CG  . ARG A 195  ? 2.0382 1.8106 1.2992 0.6710  -0.0403 -0.2628 195  ARG A CG  
1386  C CD  . ARG A 195  ? 2.1347 1.8754 1.3615 0.6676  -0.0224 -0.2779 195  ARG A CD  
1387  N NE  . ARG A 195  ? 2.2127 1.9515 1.3867 0.6865  -0.0283 -0.2818 195  ARG A NE  
1388  C CZ  . ARG A 195  ? 2.2601 1.9596 1.4119 0.7014  -0.0116 -0.2714 195  ARG A CZ  
1389  N NH1 . ARG A 195  ? 2.2474 1.9057 1.4267 0.6995  0.0122  -0.2573 195  ARG A NH1 
1390  N NH2 . ARG A 195  ? 2.3096 2.0115 1.4123 0.7186  -0.0186 -0.2747 195  ARG A NH2 
1391  N N   . TYR A 196  ? 1.8400 1.6453 1.2540 0.6364  -0.0456 -0.2212 196  TYR A N   
1392  C CA  . TYR A 196  ? 1.7580 1.5924 1.2079 0.6291  -0.0591 -0.2096 196  TYR A CA  
1393  C C   . TYR A 196  ? 1.7032 1.5631 1.1403 0.6443  -0.0775 -0.2037 196  TYR A C   
1394  O O   . TYR A 196  ? 1.6966 1.5385 1.1192 0.6620  -0.0724 -0.1928 196  TYR A O   
1395  C CB  . TYR A 196  ? 1.7802 1.5901 1.2723 0.6240  -0.0440 -0.1861 196  TYR A CB  
1396  C CG  . TYR A 196  ? 1.7963 1.5884 1.3160 0.6055  -0.0270 -0.1882 196  TYR A CG  
1397  C CD1 . TYR A 196  ? 1.7692 1.5877 1.3085 0.5873  -0.0343 -0.1978 196  TYR A CD1 
1398  C CD2 . TYR A 196  ? 1.8141 1.5619 1.3427 0.6062  -0.0020 -0.1802 196  TYR A CD2 
1399  C CE1 . TYR A 196  ? 1.7790 1.5812 1.3463 0.5707  -0.0169 -0.1991 196  TYR A CE1 
1400  C CE2 . TYR A 196  ? 1.8122 1.5431 1.3700 0.5891  0.0157  -0.1814 196  TYR A CE2 
1401  C CZ  . TYR A 196  ? 1.7901 1.5488 1.3673 0.5717  0.0083  -0.1906 196  TYR A CZ  
1402  O OH  . TYR A 196  ? 1.7824 1.5247 1.3911 0.5551  0.0274  -0.1911 196  TYR A OH  
1403  N N   . GLY A 197  ? 1.6351 1.5359 1.0797 0.6372  -0.0972 -0.2108 197  GLY A N   
1404  C CA  . GLY A 197  ? 1.6369 1.5634 1.0745 0.6498  -0.1134 -0.2052 197  GLY A CA  
1405  C C   . GLY A 197  ? 1.6218 1.5909 1.0463 0.6475  -0.1350 -0.2228 197  GLY A C   
1406  O O   . GLY A 197  ? 1.6341 1.6218 1.0680 0.6312  -0.1410 -0.2371 197  GLY A O   
1407  N N   . MET A 198  ? 1.6206 1.6051 1.0255 0.6644  -0.1459 -0.2214 198  MET A N   
1408  C CA  . MET A 198  ? 1.6131 1.6398 1.0125 0.6633  -0.1667 -0.2345 198  MET A CA  
1409  C C   . MET A 198  ? 1.5852 1.6237 0.9516 0.6644  -0.1748 -0.2573 198  MET A C   
1410  O O   . MET A 198  ? 1.5535 1.5871 0.8858 0.6818  -0.1763 -0.2595 198  MET A O   
1411  C CB  . MET A 198  ? 1.6561 1.6957 1.0533 0.6803  -0.1736 -0.2223 198  MET A CB  
1412  C CG  . MET A 198  ? 1.9506 2.0344 1.3529 0.6789  -0.1937 -0.2310 198  MET A CG  
1413  S SD  . MET A 198  ? 2.0912 2.2043 1.5244 0.6517  -0.2041 -0.2431 198  MET A SD  
1414  C CE  . MET A 198  ? 1.3920 1.4764 0.8576 0.6375  -0.1873 -0.2253 198  MET A CE  
1415  N N   . TRP A 199  ? 1.5785 1.6338 0.9550 0.6458  -0.1800 -0.2743 199  TRP A N   
1416  C CA  . TRP A 199  ? 1.6098 1.6819 0.9577 0.6448  -0.1895 -0.2980 199  TRP A CA  
1417  C C   . TRP A 199  ? 1.6136 1.7276 0.9544 0.6519  -0.2121 -0.3057 199  TRP A C   
1418  O O   . TRP A 199  ? 1.6177 1.7495 0.9817 0.6521  -0.2194 -0.2961 199  TRP A O   
1419  C CB  . TRP A 199  ? 1.6409 1.7134 1.0031 0.6221  -0.1840 -0.3150 199  TRP A CB  
1420  C CG  . TRP A 199  ? 1.7080 1.7383 1.0672 0.6185  -0.1610 -0.3110 199  TRP A CG  
1421  C CD1 . TRP A 199  ? 1.7231 1.7217 1.1032 0.6196  -0.1445 -0.2894 199  TRP A CD1 
1422  C CD2 . TRP A 199  ? 1.7558 1.7697 1.0895 0.6136  -0.1509 -0.3289 199  TRP A CD2 
1423  N NE1 . TRP A 199  ? 1.7769 1.7392 1.1487 0.6160  -0.1240 -0.2921 199  TRP A NE1 
1424  C CE2 . TRP A 199  ? 1.7840 1.7543 1.1265 0.6118  -0.1268 -0.3166 199  TRP A CE2 
1425  C CE3 . TRP A 199  ? 1.7782 1.8107 1.0835 0.6096  -0.1595 -0.3547 199  TRP A CE3 
1426  C CZ2 . TRP A 199  ? 1.7925 1.7359 1.1166 0.6055  -0.1096 -0.3296 199  TRP A CZ2 
1427  C CZ3 . TRP A 199  ? 1.7993 1.8068 1.0844 0.6029  -0.1434 -0.3680 199  TRP A CZ3 
1428  C CH2 . TRP A 199  ? 1.8158 1.7783 1.1103 0.6007  -0.1180 -0.3557 199  TRP A CH2 
1429  N N   . THR A 200  ? 1.6008 1.7313 0.9108 0.6574  -0.2230 -0.3229 200  THR A N   
1430  C CA  . THR A 200  ? 1.5393 1.7107 0.8456 0.6642  -0.2447 -0.3299 200  THR A CA  
1431  C C   . THR A 200  ? 1.5680 1.7620 0.8592 0.6541  -0.2555 -0.3563 200  THR A C   
1432  O O   . THR A 200  ? 1.6241 1.8030 0.8850 0.6556  -0.2498 -0.3657 200  THR A O   
1433  C CB  . THR A 200  ? 1.5550 1.7253 0.8318 0.6901  -0.2490 -0.3185 200  THR A CB  
1434  O OG1 . THR A 200  ? 1.5434 1.6825 0.8269 0.7008  -0.2335 -0.2953 200  THR A OG1 
1435  C CG2 . THR A 200  ? 1.5401 1.7515 0.8235 0.6978  -0.2691 -0.3203 200  THR A CG2 
1436  N N   . ILE A 201  ? 1.5451 1.7749 0.8571 0.6426  -0.2702 -0.3698 201  ILE A N   
1437  C CA  . ILE A 201  ? 1.5745 1.8307 0.8711 0.6352  -0.2830 -0.3959 201  ILE A CA  
1438  C C   . ILE A 201  ? 1.6053 1.9007 0.8935 0.6488  -0.3058 -0.3988 201  ILE A C   
1439  O O   . ILE A 201  ? 1.6495 1.9692 0.9662 0.6459  -0.3153 -0.3967 201  ILE A O   
1440  C CB  . ILE A 201  ? 1.5541 1.8242 0.8811 0.6102  -0.2826 -0.4141 201  ILE A CB  
1441  C CG1 . ILE A 201  ? 1.5573 1.7919 0.8957 0.5953  -0.2599 -0.4131 201  ILE A CG1 
1442  C CG2 . ILE A 201  ? 1.6100 1.9093 0.9214 0.6034  -0.2962 -0.4421 201  ILE A CG2 
1443  C CD1 . ILE A 201  ? 1.5592 1.8078 0.9157 0.5722  -0.2587 -0.4376 201  ILE A CD1 
1444  N N   . LYS A 202  ? 1.7018 2.0041 0.9521 0.6633  -0.3143 -0.4031 202  LYS A N   
1445  C CA  . LYS A 202  ? 1.6891 2.0324 0.9340 0.6752  -0.3372 -0.4068 202  LYS A CA  
1446  C C   . LYS A 202  ? 1.6896 2.0672 0.9311 0.6616  -0.3529 -0.4356 202  LYS A C   
1447  O O   . LYS A 202  ? 1.6997 2.0662 0.9307 0.6467  -0.3452 -0.4530 202  LYS A O   
1448  C CB  . LYS A 202  ? 1.7883 2.1254 0.9956 0.7008  -0.3403 -0.3925 202  LYS A CB  
1449  C CG  . LYS A 202  ? 1.8283 2.1387 1.0406 0.7179  -0.3274 -0.3642 202  LYS A CG  
1450  C CD  . LYS A 202  ? 1.9151 2.2201 1.0881 0.7435  -0.3299 -0.3516 202  LYS A CD  
1451  C CE  . LYS A 202  ? 1.9488 2.2120 1.1172 0.7573  -0.3093 -0.3277 202  LYS A CE  
1452  N NZ  . LYS A 202  ? 2.0116 2.2489 1.1327 0.7712  -0.3017 -0.3239 202  LYS A NZ  
1453  N N   . ALA A 203  ? 1.6493 2.0685 0.9012 0.6663  -0.3740 -0.4415 203  ALA A N   
1454  C CA  . ALA A 203  ? 1.6769 2.1314 0.9262 0.6544  -0.3903 -0.4692 203  ALA A CA  
1455  C C   . ALA A 203  ? 1.7149 2.2109 0.9562 0.6704  -0.4149 -0.4693 203  ALA A C   
1456  O O   . ALA A 203  ? 1.6813 2.1913 0.9453 0.6810  -0.4211 -0.4545 203  ALA A O   
1457  C CB  . ALA A 203  ? 1.6045 2.0698 0.8945 0.6308  -0.3883 -0.4852 203  ALA A CB  
1458  N N   . LYS A 204  ? 1.7904 2.3070 1.0008 0.6711  -0.4283 -0.4862 204  LYS A N   
1459  C CA  . LYS A 204  ? 1.8438 2.4019 1.0426 0.6868  -0.4532 -0.4861 204  LYS A CA  
1460  C C   . LYS A 204  ? 1.8316 2.4286 1.0303 0.6720  -0.4710 -0.5167 204  LYS A C   
1461  O O   . LYS A 204  ? 1.8166 2.4041 1.0095 0.6521  -0.4627 -0.5386 204  LYS A O   
1462  C CB  . LYS A 204  ? 1.9287 2.4745 1.0800 0.7089  -0.4541 -0.4703 204  LYS A CB  
1463  C CG  . LYS A 204  ? 2.0405 2.5548 1.1535 0.7000  -0.4398 -0.4807 204  LYS A CG  
1464  C CD  . LYS A 204  ? 2.1285 2.6195 1.1966 0.7222  -0.4347 -0.4606 204  LYS A CD  
1465  C CE  . LYS A 204  ? 2.1883 2.6308 1.2308 0.7135  -0.4100 -0.4631 204  LYS A CE  
1466  N NZ  . LYS A 204  ? 2.2552 2.6819 1.2454 0.7324  -0.4086 -0.4509 204  LYS A NZ  
1467  N N   . TYR A 205  ? 1.8680 2.5093 1.0760 0.6813  -0.4949 -0.5185 205  TYR A N   
1468  C CA  . TYR A 205  ? 1.9564 2.6382 1.1701 0.6668  -0.5130 -0.5482 205  TYR A CA  
1469  C C   . TYR A 205  ? 2.0962 2.7832 1.2581 0.6697  -0.5205 -0.5584 205  TYR A C   
1470  O O   . TYR A 205  ? 2.1607 2.8490 1.2907 0.6915  -0.5280 -0.5396 205  TYR A O   
1471  C CB  . TYR A 205  ? 1.9333 2.6614 1.1791 0.6748  -0.5357 -0.5468 205  TYR A CB  
1472  C CG  . TYR A 205  ? 1.9020 2.6348 1.2008 0.6582  -0.5304 -0.5556 205  TYR A CG  
1473  C CD1 . TYR A 205  ? 1.8686 2.5987 1.2005 0.6671  -0.5267 -0.5349 205  TYR A CD1 
1474  C CD2 . TYR A 205  ? 1.9123 2.6500 1.2275 0.6325  -0.5267 -0.5849 205  TYR A CD2 
1475  C CE1 . TYR A 205  ? 1.8333 2.5661 1.2109 0.6505  -0.5208 -0.5433 205  TYR A CE1 
1476  C CE2 . TYR A 205  ? 1.8741 2.6141 1.2361 0.6171  -0.5205 -0.5924 205  TYR A CE2 
1477  C CZ  . TYR A 205  ? 1.8359 2.5734 1.2275 0.6260  -0.5181 -0.5714 205  TYR A CZ  
1478  O OH  . TYR A 205  ? 1.7920 2.5312 1.2271 0.6096  -0.5116 -0.5794 205  TYR A OH  
1479  N N   . LYS A 206  ? 2.1671 2.8553 1.3191 0.6477  -0.5170 -0.5877 206  LYS A N   
1480  C CA  . LYS A 206  ? 2.2316 2.9204 1.3308 0.6478  -0.5208 -0.5987 206  LYS A CA  
1481  C C   . LYS A 206  ? 2.2677 2.9997 1.3467 0.6672  -0.5498 -0.5915 206  LYS A C   
1482  O O   . LYS A 206  ? 2.2840 3.0054 1.3258 0.6879  -0.5516 -0.5699 206  LYS A O   
1483  C CB  . LYS A 206  ? 2.2662 2.9642 1.3635 0.6200  -0.5176 -0.6361 206  LYS A CB  
1484  C CG  . LYS A 206  ? 2.3320 3.0276 1.3722 0.6178  -0.5188 -0.6485 206  LYS A CG  
1485  C CD  . LYS A 206  ? 2.3669 3.0627 1.4059 0.5884  -0.5085 -0.6855 206  LYS A CD  
1486  C CE  . LYS A 206  ? 2.3855 3.1369 1.4482 0.5756  -0.5318 -0.7142 206  LYS A CE  
1487  N NZ  . LYS A 206  ? 2.4236 3.1830 1.4710 0.5496  -0.5260 -0.7522 206  LYS A NZ  
1488  N N   . GLU A 207  ? 2.2657 3.0462 1.3724 0.6607  -0.5718 -0.6086 207  GLU A N   
1489  C CA  . GLU A 207  ? 2.2906 3.1188 1.3880 0.6779  -0.6016 -0.6022 207  GLU A CA  
1490  C C   . GLU A 207  ? 2.2390 3.0645 1.3484 0.7058  -0.6048 -0.5654 207  GLU A C   
1491  O O   . GLU A 207  ? 2.2083 2.9908 1.3172 0.7141  -0.5833 -0.5436 207  GLU A O   
1492  C CB  . GLU A 207  ? 2.3261 3.2041 1.4599 0.6628  -0.6218 -0.6295 207  GLU A CB  
1493  C CG  . GLU A 207  ? 2.3831 3.2762 1.4936 0.6400  -0.6256 -0.6659 207  GLU A CG  
1494  C CD  . GLU A 207  ? 2.4444 3.3716 1.5075 0.6503  -0.6497 -0.6678 207  GLU A CD  
1495  O OE1 . GLU A 207  ? 2.4626 3.3798 1.4936 0.6741  -0.6530 -0.6389 207  GLU A OE1 
1496  O OE2 . GLU A 207  ? 2.4763 3.4408 1.5344 0.6345  -0.6654 -0.6982 207  GLU A OE2 
1497  N N   . ASP A 208  ? 2.1875 3.0595 1.3082 0.7204  -0.6308 -0.5583 208  ASP A N   
1498  C CA  . ASP A 208  ? 2.1085 2.9817 1.2427 0.7472  -0.6337 -0.5240 208  ASP A CA  
1499  C C   . ASP A 208  ? 2.0193 2.8775 1.2077 0.7417  -0.6192 -0.5182 208  ASP A C   
1500  O O   . ASP A 208  ? 2.0092 2.8706 1.2282 0.7187  -0.6151 -0.5418 208  ASP A O   
1501  C CB  . ASP A 208  ? 2.0750 3.0056 1.2179 0.7600  -0.6650 -0.5217 208  ASP A CB  
1502  C CG  . ASP A 208  ? 2.0333 3.0045 1.1939 0.7382  -0.6826 -0.5565 208  ASP A CG  
1503  O OD1 . ASP A 208  ? 1.9562 2.9328 1.1666 0.7234  -0.6785 -0.5699 208  ASP A OD1 
1504  O OD2 . ASP A 208  ? 2.0785 3.0749 1.2016 0.7351  -0.6995 -0.5710 208  ASP A OD2 
1505  N N   . PHE A 209  ? 1.9605 2.8052 1.1611 0.7628  -0.6120 -0.4871 209  PHE A N   
1506  C CA  . PHE A 209  ? 1.8815 2.7039 1.1266 0.7595  -0.5940 -0.4767 209  PHE A CA  
1507  C C   . PHE A 209  ? 1.8803 2.6473 1.1046 0.7663  -0.5669 -0.4565 209  PHE A C   
1508  O O   . PHE A 209  ? 1.9087 2.6444 1.1055 0.7542  -0.5532 -0.4666 209  PHE A O   
1509  C CB  . PHE A 209  ? 1.8095 2.6349 1.0902 0.7309  -0.5896 -0.5044 209  PHE A CB  
1510  C CG  . PHE A 209  ? 1.7595 2.6359 1.0767 0.7243  -0.6120 -0.5215 209  PHE A CG  
1511  C CD1 . PHE A 209  ? 1.7402 2.6292 1.0764 0.6984  -0.6143 -0.5537 209  PHE A CD1 
1512  C CD2 . PHE A 209  ? 1.7106 2.6217 1.0459 0.7440  -0.6295 -0.5054 209  PHE A CD2 
1513  C CE1 . PHE A 209  ? 1.6971 2.6321 1.0694 0.6919  -0.6341 -0.5705 209  PHE A CE1 
1514  C CE2 . PHE A 209  ? 1.6974 2.6553 1.0703 0.7377  -0.6497 -0.5211 209  PHE A CE2 
1515  C CZ  . PHE A 209  ? 1.6824 2.6520 1.0735 0.7114  -0.6522 -0.5543 209  PHE A CZ  
1516  N N   . SER A 210  ? 1.8578 2.6129 1.0979 0.7849  -0.5582 -0.4286 210  SER A N   
1517  C CA  . SER A 210  ? 1.8512 2.5563 1.0736 0.7938  -0.5333 -0.4079 210  SER A CA  
1518  C C   . SER A 210  ? 1.8027 2.4756 1.0559 0.7757  -0.5114 -0.4108 210  SER A C   
1519  O O   . SER A 210  ? 1.7746 2.4052 1.0170 0.7796  -0.4900 -0.3960 210  SER A O   
1520  C CB  . SER A 210  ? 1.8513 2.5567 1.0752 0.8225  -0.5317 -0.3764 210  SER A CB  
1521  O OG  . SER A 210  ? 1.8567 2.5137 1.0634 0.8307  -0.5073 -0.3581 210  SER A OG  
1522  N N   . THR A 211  ? 1.7897 2.4837 1.0815 0.7562  -0.5171 -0.4296 211  THR A N   
1523  C CA  . THR A 211  ? 1.7553 2.4269 1.0819 0.7393  -0.4995 -0.4311 211  THR A CA  
1524  C C   . THR A 211  ? 1.7507 2.3760 1.0572 0.7280  -0.4780 -0.4322 211  THR A C   
1525  O O   . THR A 211  ? 1.7629 2.3814 1.0417 0.7187  -0.4784 -0.4481 211  THR A O   
1526  C CB  . THR A 211  ? 1.7445 2.4474 1.1104 0.7185  -0.5103 -0.4550 211  THR A CB  
1527  O OG1 . THR A 211  ? 1.7853 2.5127 1.1329 0.7095  -0.5263 -0.4796 211  THR A OG1 
1528  C CG2 . THR A 211  ? 1.7090 2.4453 1.1098 0.7291  -0.5222 -0.4463 211  THR A CG2 
1529  N N   . THR A 212  ? 1.7304 2.3250 1.0537 0.7281  -0.4588 -0.4154 212  THR A N   
1530  C CA  . THR A 212  ? 1.7423 2.2908 1.0488 0.7225  -0.4372 -0.4093 212  THR A CA  
1531  C C   . THR A 212  ? 1.7373 2.2696 1.0781 0.7011  -0.4233 -0.4133 212  THR A C   
1532  O O   . THR A 212  ? 1.7456 2.2850 1.1201 0.6994  -0.4211 -0.4051 212  THR A O   
1533  C CB  . THR A 212  ? 1.7360 2.2577 1.0306 0.7443  -0.4242 -0.3807 212  THR A CB  
1534  O OG1 . THR A 212  ? 1.7664 2.3076 1.0379 0.7676  -0.4373 -0.3712 212  THR A OG1 
1535  C CG2 . THR A 212  ? 1.7474 2.2218 1.0173 0.7419  -0.4036 -0.3744 212  THR A CG2 
1536  N N   . GLY A 213  ? 1.7261 2.2357 1.0582 0.6845  -0.4127 -0.4251 213  GLY A N   
1537  C CA  . GLY A 213  ? 1.6985 2.1853 1.0581 0.6673  -0.3964 -0.4225 213  GLY A CA  
1538  C C   . GLY A 213  ? 1.6972 2.1392 1.0394 0.6736  -0.3762 -0.4040 213  GLY A C   
1539  O O   . GLY A 213  ? 1.7390 2.1638 1.0455 0.6836  -0.3727 -0.4019 213  GLY A O   
1540  N N   . THR A 214  ? 1.6677 2.0907 1.0352 0.6671  -0.3627 -0.3905 214  THR A N   
1541  C CA  . THR A 214  ? 1.6465 2.0269 1.0038 0.6690  -0.3428 -0.3751 214  THR A CA  
1542  C C   . THR A 214  ? 1.5598 1.9278 0.9503 0.6492  -0.3314 -0.3725 214  THR A C   
1543  O O   . THR A 214  ? 1.5260 1.9155 0.9461 0.6396  -0.3373 -0.3752 214  THR A O   
1544  C CB  . THR A 214  ? 1.6771 2.0426 1.0227 0.6925  -0.3369 -0.3507 214  THR A CB  
1545  O OG1 . THR A 214  ? 1.7194 2.0831 1.0255 0.7106  -0.3419 -0.3506 214  THR A OG1 
1546  C CG2 . THR A 214  ? 1.6491 1.9742 1.0011 0.6902  -0.3157 -0.3333 214  THR A CG2 
1547  N N   . ALA A 215  ? 1.5272 1.8605 0.9126 0.6426  -0.3148 -0.3672 215  ALA A N   
1548  C CA  . ALA A 215  ? 1.4708 1.7903 0.8858 0.6239  -0.3032 -0.3630 215  ALA A CA  
1549  C C   . ALA A 215  ? 1.4752 1.7530 0.8812 0.6291  -0.2845 -0.3450 215  ALA A C   
1550  O O   . ALA A 215  ? 1.4821 1.7434 0.8587 0.6457  -0.2808 -0.3393 215  ALA A O   
1551  C CB  . ALA A 215  ? 1.4514 1.7795 0.8756 0.6030  -0.3043 -0.3853 215  ALA A CB  
1552  N N   . TYR A 216  ? 1.4466 1.7071 0.8779 0.6157  -0.2723 -0.3348 216  TYR A N   
1553  C CA  . TYR A 216  ? 1.5458 1.7664 0.9711 0.6187  -0.2541 -0.3200 216  TYR A CA  
1554  C C   . TYR A 216  ? 1.4150 1.6215 0.8660 0.5978  -0.2425 -0.3197 216  TYR A C   
1555  O O   . TYR A 216  ? 1.4469 1.6739 0.9213 0.5814  -0.2482 -0.3283 216  TYR A O   
1556  C CB  . TYR A 216  ? 1.5869 1.7931 1.0157 0.6330  -0.2479 -0.2958 216  TYR A CB  
1557  C CG  . TYR A 216  ? 1.6554 1.8765 1.0655 0.6541  -0.2574 -0.2927 216  TYR A CG  
1558  C CD1 . TYR A 216  ? 1.7161 1.9132 1.1031 0.6744  -0.2489 -0.2795 216  TYR A CD1 
1559  C CD2 . TYR A 216  ? 1.7101 1.9685 1.1279 0.6541  -0.2738 -0.3020 216  TYR A CD2 
1560  C CE1 . TYR A 216  ? 1.7577 1.9685 1.1292 0.6946  -0.2565 -0.2751 216  TYR A CE1 
1561  C CE2 . TYR A 216  ? 1.7535 2.0262 1.1577 0.6738  -0.2817 -0.2977 216  TYR A CE2 
1562  C CZ  . TYR A 216  ? 1.7794 2.0287 1.1604 0.6942  -0.2730 -0.2838 216  TYR A CZ  
1563  O OH  . TYR A 216  ? 1.8115 2.0761 1.1811 0.7143  -0.2801 -0.2783 216  TYR A OH  
1564  N N   . PHE A 217  ? 1.4279 1.5983 0.8744 0.5989  -0.2254 -0.3096 217  PHE A N   
1565  C CA  . PHE A 217  ? 1.4401 1.5906 0.9144 0.5829  -0.2110 -0.3006 217  PHE A CA  
1566  C C   . PHE A 217  ? 1.4795 1.5908 0.9493 0.5927  -0.1940 -0.2809 217  PHE A C   
1567  O O   . PHE A 217  ? 1.5174 1.6138 0.9584 0.6095  -0.1911 -0.2798 217  PHE A O   
1568  C CB  . PHE A 217  ? 1.4297 1.5826 0.9114 0.5646  -0.2067 -0.3205 217  PHE A CB  
1569  C CG  . PHE A 217  ? 1.4669 1.6019 0.9208 0.5681  -0.1984 -0.3346 217  PHE A CG  
1570  C CD1 . PHE A 217  ? 1.5472 1.6501 1.0093 0.5593  -0.1780 -0.3321 217  PHE A CD1 
1571  C CD2 . PHE A 217  ? 1.5018 1.6525 0.9222 0.5791  -0.2104 -0.3505 217  PHE A CD2 
1572  C CE1 . PHE A 217  ? 1.5559 1.6411 0.9917 0.5605  -0.1683 -0.3468 217  PHE A CE1 
1573  C CE2 . PHE A 217  ? 1.5712 1.7058 0.9634 0.5805  -0.2025 -0.3643 217  PHE A CE2 
1574  C CZ  . PHE A 217  ? 1.5766 1.6779 0.9762 0.5706  -0.1808 -0.3633 217  PHE A CZ  
1575  N N   . GLU A 218  ? 1.5327 1.6281 1.0319 0.5829  -0.1830 -0.2640 218  GLU A N   
1576  C CA  . GLU A 218  ? 1.5911 1.6500 1.0914 0.5916  -0.1668 -0.2443 218  GLU A CA  
1577  C C   . GLU A 218  ? 1.5802 1.6125 1.0960 0.5786  -0.1492 -0.2438 218  GLU A C   
1578  O O   . GLU A 218  ? 1.5542 1.5945 1.0981 0.5610  -0.1475 -0.2439 218  GLU A O   
1579  C CB  . GLU A 218  ? 1.6644 1.7247 1.1870 0.5939  -0.1677 -0.2211 218  GLU A CB  
1580  C CG  . GLU A 218  ? 1.7667 1.7931 1.2855 0.6083  -0.1537 -0.2020 218  GLU A CG  
1581  C CD  . GLU A 218  ? 1.8206 1.8525 1.3592 0.6114  -0.1558 -0.1816 218  GLU A CD  
1582  O OE1 . GLU A 218  ? 1.8520 1.8563 1.4006 0.6168  -0.1427 -0.1638 218  GLU A OE1 
1583  O OE2 . GLU A 218  ? 1.8300 1.8934 1.3749 0.6076  -0.1697 -0.1840 218  GLU A OE2 
1584  N N   . VAL A 219  ? 1.6103 1.6105 1.1074 0.5874  -0.1348 -0.2437 219  VAL A N   
1585  C CA  . VAL A 219  ? 1.6076 1.5784 1.1202 0.5763  -0.1148 -0.2425 219  VAL A CA  
1586  C C   . VAL A 219  ? 1.5987 1.5429 1.1330 0.5812  -0.1027 -0.2155 219  VAL A C   
1587  O O   . VAL A 219  ? 1.6059 1.5309 1.1222 0.5982  -0.0983 -0.2065 219  VAL A O   
1588  C CB  . VAL A 219  ? 1.6116 1.5605 1.0912 0.5815  -0.1041 -0.2590 219  VAL A CB  
1589  C CG1 . VAL A 219  ? 1.5851 1.4895 1.0776 0.5798  -0.0787 -0.2468 219  VAL A CG1 
1590  C CG2 . VAL A 219  ? 1.5206 1.4904 0.9927 0.5675  -0.1090 -0.2867 219  VAL A CG2 
1591  N N   . LYS A 220  ? 1.5892 1.5340 1.1629 0.5667  -0.0980 -0.2020 220  LYS A N   
1592  C CA  . LYS A 220  ? 1.5704 1.4904 1.1709 0.5685  -0.0857 -0.1754 220  LYS A CA  
1593  C C   . LYS A 220  ? 1.5503 1.4424 1.1769 0.5562  -0.0645 -0.1711 220  LYS A C   
1594  O O   . LYS A 220  ? 1.4695 1.3688 1.1037 0.5419  -0.0611 -0.1857 220  LYS A O   
1595  C CB  . LYS A 220  ? 1.5286 1.4728 1.1548 0.5637  -0.0983 -0.1578 220  LYS A CB  
1596  C CG  . LYS A 220  ? 1.5338 1.5007 1.1389 0.5767  -0.1151 -0.1590 220  LYS A CG  
1597  C CD  . LYS A 220  ? 1.5747 1.5773 1.1999 0.5648  -0.1308 -0.1540 220  LYS A CD  
1598  C CE  . LYS A 220  ? 1.5579 1.5790 1.1727 0.5762  -0.1430 -0.1489 220  LYS A CE  
1599  N NZ  . LYS A 220  ? 1.5417 1.5536 1.1781 0.5781  -0.1385 -0.1241 220  LYS A NZ  
1600  N N   . GLU A 221  ? 1.6597 1.5195 1.3017 0.5623  -0.0491 -0.1510 221  GLU A N   
1601  C CA  . GLU A 221  ? 1.7886 1.6161 1.4580 0.5534  -0.0258 -0.1433 221  GLU A CA  
1602  C C   . GLU A 221  ? 1.7400 1.5735 1.4590 0.5397  -0.0235 -0.1208 221  GLU A C   
1603  O O   . GLU A 221  ? 1.7051 1.5350 1.4448 0.5441  -0.0251 -0.0966 221  GLU A O   
1604  C CB  . GLU A 221  ? 1.9378 1.7251 1.6005 0.5676  -0.0092 -0.1325 221  GLU A CB  
1605  C CG  . GLU A 221  ? 2.0716 1.8248 1.7716 0.5590  0.0154  -0.1185 221  GLU A CG  
1606  C CD  . GLU A 221  ? 2.1686 1.8918 1.8811 0.5715  0.0263  -0.0962 221  GLU A CD  
1607  O OE1 . GLU A 221  ? 2.1867 1.9164 1.8772 0.5867  0.0148  -0.0928 221  GLU A OE1 
1608  O OE2 . GLU A 221  ? 2.2088 1.9022 1.9551 0.5660  0.0471  -0.0823 221  GLU A OE2 
1609  N N   . TYR A 222  ? 1.7271 1.5694 1.4656 0.5229  -0.0189 -0.1285 222  TYR A N   
1610  C CA  . TYR A 222  ? 1.6963 1.5471 1.4807 0.5094  -0.0174 -0.1069 222  TYR A CA  
1611  C C   . TYR A 222  ? 1.7085 1.5248 1.5289 0.5098  0.0033  -0.0817 222  TYR A C   
1612  O O   . TYR A 222  ? 1.7341 1.5168 1.5535 0.5117  0.0245  -0.0877 222  TYR A O   
1613  C CB  . TYR A 222  ? 1.6712 1.5374 1.4690 0.4920  -0.0146 -0.1216 222  TYR A CB  
1614  C CG  . TYR A 222  ? 1.6376 1.5091 1.4831 0.4791  -0.0107 -0.0970 222  TYR A CG  
1615  C CD1 . TYR A 222  ? 1.6034 1.5098 1.4582 0.4701  -0.0283 -0.0922 222  TYR A CD1 
1616  C CD2 . TYR A 222  ? 1.6586 1.4999 1.5404 0.4763  0.0109  -0.0768 222  TYR A CD2 
1617  C CE1 . TYR A 222  ? 1.5993 1.5110 1.4962 0.4585  -0.0252 -0.0675 222  TYR A CE1 
1618  C CE2 . TYR A 222  ? 1.6507 1.4978 1.5775 0.4654  0.0140  -0.0513 222  TYR A CE2 
1619  C CZ  . TYR A 222  ? 1.6202 1.5029 1.5536 0.4565  -0.0044 -0.0462 222  TYR A CZ  
1620  O OH  . TYR A 222  ? 1.6026 1.4910 1.5799 0.4457  -0.0011 -0.0190 222  TYR A OH  
1621  N N   . VAL A 223  ? 1.6828 1.5085 1.5354 0.5072  -0.0030 -0.0537 223  VAL A N   
1622  C CA  . VAL A 223  ? 1.6466 1.4455 1.5403 0.5066  0.0136  -0.0261 223  VAL A CA  
1623  C C   . VAL A 223  ? 1.6402 1.4592 1.5762 0.4917  0.0095  -0.0048 223  VAL A C   
1624  O O   . VAL A 223  ? 1.6117 1.4648 1.5442 0.4872  -0.0112 -0.0011 223  VAL A O   
1625  C CB  . VAL A 223  ? 1.6124 1.4048 1.5067 0.5201  0.0077  -0.0065 223  VAL A CB  
1626  C CG1 . VAL A 223  ? 1.5920 1.3533 1.5301 0.5197  0.0273  0.0198  223  VAL A CG1 
1627  C CG2 . VAL A 223  ? 1.6240 1.4051 1.4720 0.5372  0.0055  -0.0245 223  VAL A CG2 
1628  N N   . LEU A 224  ? 1.6832 1.4797 1.6603 0.4843  0.0302  0.0107  224  LEU A N   
1629  C CA  . LEU A 224  ? 1.6972 1.5094 1.7194 0.4707  0.0291  0.0352  224  LEU A CA  
1630  C C   . LEU A 224  ? 1.6961 1.5205 1.7363 0.4748  0.0150  0.0657  224  LEU A C   
1631  O O   . LEU A 224  ? 1.7082 1.5102 1.7542 0.4859  0.0213  0.0780  224  LEU A O   
1632  C CB  . LEU A 224  ? 1.6828 1.4651 1.7473 0.4632  0.0577  0.0449  224  LEU A CB  
1633  C CG  . LEU A 224  ? 1.6868 1.4860 1.7834 0.4464  0.0617  0.0507  224  LEU A CG  
1634  C CD1 . LEU A 224  ? 1.6750 1.4891 1.8134 0.4414  0.0538  0.0888  224  LEU A CD1 
1635  C CD2 . LEU A 224  ? 1.6758 1.5076 1.7383 0.4404  0.0443  0.0243  224  LEU A CD2 
1636  N N   . PRO A 225  ? 2.5057 1.4743 1.5178 0.5862  -0.6767 -0.3051 225  PRO A N   
1637  C CA  . PRO A 225  ? 2.3908 1.4223 1.4584 0.5913  -0.6381 -0.2920 225  PRO A CA  
1638  C C   . PRO A 225  ? 2.3945 1.4143 1.4986 0.5979  -0.6307 -0.2987 225  PRO A C   
1639  O O   . PRO A 225  ? 2.3849 1.3799 1.5053 0.5842  -0.6641 -0.2939 225  PRO A O   
1640  C CB  . PRO A 225  ? 2.3520 1.4528 1.4733 0.5638  -0.6587 -0.2581 225  PRO A CB  
1641  C CG  . PRO A 225  ? 2.4049 1.4767 1.5031 0.5433  -0.7085 -0.2537 225  PRO A CG  
1642  C CD  . PRO A 225  ? 2.4906 1.4785 1.5387 0.5544  -0.7242 -0.2834 225  PRO A CD  
1643  N N   . HIS A 226  ? 2.3807 1.4185 1.5013 0.6193  -0.5868 -0.3098 226  HIS A N   
1644  C CA  . HIS A 226  ? 2.4298 1.4624 1.5885 0.6291  -0.5783 -0.3173 226  HIS A CA  
1645  C C   . HIS A 226  ? 2.3198 1.4257 1.5518 0.6171  -0.5831 -0.2918 226  HIS A C   
1646  O O   . HIS A 226  ? 2.2857 1.3874 1.5494 0.6161  -0.5979 -0.2860 226  HIS A O   
1647  C CB  . HIS A 226  ? 2.5107 1.5270 1.6587 0.6593  -0.5296 -0.3445 226  HIS A CB  
1648  C CG  . HIS A 226  ? 2.6768 1.6083 1.7543 0.6767  -0.5242 -0.3716 226  HIS A CG  
1649  N ND1 . HIS A 226  ? 2.7456 1.6534 1.7703 0.6956  -0.4907 -0.3865 226  HIS A ND1 
1650  C CD2 . HIS A 226  ? 2.7625 1.6254 1.8111 0.6797  -0.5466 -0.3865 226  HIS A CD2 
1651  C CE1 . HIS A 226  ? 2.8444 1.6730 1.8066 0.7107  -0.4931 -0.4096 226  HIS A CE1 
1652  N NE2 . HIS A 226  ? 2.8558 1.6560 1.8325 0.7007  -0.5275 -0.4115 226  HIS A NE2 
1653  N N   . PHE A 227  ? 2.2586 1.4306 1.5146 0.6102  -0.5695 -0.2763 227  PHE A N   
1654  C CA  . PHE A 227  ? 2.1684 1.4134 1.4870 0.6015  -0.5713 -0.2535 227  PHE A CA  
1655  C C   . PHE A 227  ? 2.1375 1.4402 1.4663 0.5897  -0.5632 -0.2366 227  PHE A C   
1656  O O   . PHE A 227  ? 2.1836 1.4863 1.4885 0.5990  -0.5359 -0.2490 227  PHE A O   
1657  C CB  . PHE A 227  ? 2.0757 1.3488 1.4336 0.6241  -0.5397 -0.2700 227  PHE A CB  
1658  C CG  . PHE A 227  ? 1.9957 1.2698 1.3435 0.6434  -0.4950 -0.2954 227  PHE A CG  
1659  C CD1 . PHE A 227  ? 1.9119 1.2448 1.2818 0.6416  -0.4706 -0.2903 227  PHE A CD1 
1660  C CD2 . PHE A 227  ? 2.0268 1.2405 1.3452 0.6643  -0.4746 -0.3239 227  PHE A CD2 
1661  C CE1 . PHE A 227  ? 1.9046 1.2353 1.2702 0.6596  -0.4259 -0.3122 227  PHE A CE1 
1662  C CE2 . PHE A 227  ? 2.0105 1.2220 1.3226 0.6831  -0.4289 -0.3452 227  PHE A CE2 
1663  C CZ  . PHE A 227  ? 1.9559 1.2255 1.2930 0.6806  -0.4040 -0.3389 227  PHE A CZ  
1664  N N   . SER A 228  ? 2.0912 1.4428 1.4567 0.5707  -0.5839 -0.2070 228  SER A N   
1665  C CA  . SER A 228  ? 2.0794 1.4861 1.4572 0.5571  -0.5796 -0.1880 228  SER A CA  
1666  C C   . SER A 228  ? 1.9758 1.4371 1.3785 0.5720  -0.5365 -0.1992 228  SER A C   
1667  O O   . SER A 228  ? 1.9197 1.4258 1.3666 0.5801  -0.5245 -0.2004 228  SER A O   
1668  C CB  . SER A 228  ? 2.1076 1.5539 1.5234 0.5355  -0.6077 -0.1531 228  SER A CB  
1669  O OG  . SER A 228  ? 2.0938 1.6007 1.5295 0.5235  -0.6007 -0.1337 228  SER A OG  
1670  N N   . VAL A 229  ? 1.9535 1.4095 1.3285 0.5770  -0.5136 -0.2084 229  VAL A N   
1671  C CA  . VAL A 229  ? 1.7586 1.2682 1.1635 0.5870  -0.4731 -0.2153 229  VAL A CA  
1672  C C   . VAL A 229  ? 1.7842 1.3436 1.2008 0.5688  -0.4791 -0.1892 229  VAL A C   
1673  O O   . VAL A 229  ? 1.7852 1.3197 1.1640 0.5589  -0.4956 -0.1786 229  VAL A O   
1674  C CB  . VAL A 229  ? 1.5803 1.0527 0.9547 0.6091  -0.4330 -0.2427 229  VAL A CB  
1675  C CG1 . VAL A 229  ? 1.4947 1.0165 0.8919 0.6125  -0.3961 -0.2413 229  VAL A CG1 
1676  C CG2 . VAL A 229  ? 1.5505 1.0054 0.9449 0.6294  -0.4128 -0.2695 229  VAL A CG2 
1677  N N   . SER A 230  ? 1.7078 1.3379 1.1778 0.5651  -0.4692 -0.1793 230  SER A N   
1678  C CA  . SER A 230  ? 1.6476 1.3343 1.1383 0.5500  -0.4682 -0.1558 230  SER A CA  
1679  C C   . SER A 230  ? 1.5963 1.3249 1.1136 0.5626  -0.4229 -0.1707 230  SER A C   
1680  O O   . SER A 230  ? 1.5852 1.3216 1.1275 0.5802  -0.3957 -0.1963 230  SER A O   
1681  C CB  . SER A 230  ? 1.5972 1.3353 1.1285 0.5365  -0.4899 -0.1313 230  SER A CB  
1682  O OG  . SER A 230  ? 1.5478 1.3304 1.1205 0.5506  -0.4708 -0.1450 230  SER A OG  
1683  N N   . ILE A 231  ? 1.5609 1.3192 1.0798 0.5535  -0.4142 -0.1549 231  ILE A N   
1684  C CA  . ILE A 231  ? 1.5296 1.3274 1.0785 0.5643  -0.3695 -0.1677 231  ILE A CA  
1685  C C   . ILE A 231  ? 1.5627 1.4205 1.1385 0.5491  -0.3695 -0.1431 231  ILE A C   
1686  O O   . ILE A 231  ? 1.6052 1.4535 1.1547 0.5365  -0.3870 -0.1206 231  ILE A O   
1687  C CB  . ILE A 231  ? 1.5155 1.2634 1.0253 0.5807  -0.3382 -0.1844 231  ILE A CB  
1688  C CG1 . ILE A 231  ? 1.4794 1.2651 1.0120 0.5848  -0.2985 -0.1830 231  ILE A CG1 
1689  C CG2 . ILE A 231  ? 1.5687 1.2574 1.0120 0.5755  -0.3672 -0.1720 231  ILE A CG2 
1690  C CD1 . ILE A 231  ? 1.5266 1.2616 1.0162 0.6024  -0.2665 -0.1932 231  ILE A CD1 
1691  N N   . GLU A 232  ? 1.5660 1.4867 1.1960 0.5513  -0.3518 -0.1490 232  GLU A N   
1692  C CA  . GLU A 232  ? 1.5834 1.5668 1.2447 0.5379  -0.3520 -0.1270 232  GLU A CA  
1693  C C   . GLU A 232  ? 1.5303 1.5586 1.2339 0.5481  -0.3065 -0.1454 232  GLU A C   
1694  O O   . GLU A 232  ? 1.4908 1.5338 1.2277 0.5628  -0.2835 -0.1752 232  GLU A O   
1695  C CB  . GLU A 232  ? 1.6450 1.6662 1.3307 0.5296  -0.3800 -0.1126 232  GLU A CB  
1696  C CG  . GLU A 232  ? 1.7877 1.7612 1.4429 0.5238  -0.4193 -0.1015 232  GLU A CG  
1697  C CD  . GLU A 232  ? 1.8521 1.8490 1.5304 0.5298  -0.4343 -0.1023 232  GLU A CD  
1698  O OE1 . GLU A 232  ? 1.8405 1.8996 1.5543 0.5323  -0.4261 -0.0994 232  GLU A OE1 
1699  O OE2 . GLU A 232  ? 1.9060 1.8574 1.5640 0.5335  -0.4550 -0.1056 232  GLU A OE2 
1700  N N   . PRO A 233  ? 1.5401 1.5918 1.2476 0.5403  -0.2935 -0.1282 233  PRO A N   
1701  C CA  . PRO A 233  ? 1.5367 1.6175 1.2783 0.5498  -0.2465 -0.1436 233  PRO A CA  
1702  C C   . PRO A 233  ? 1.4776 1.6338 1.2728 0.5433  -0.2410 -0.1405 233  PRO A C   
1703  O O   . PRO A 233  ? 1.4980 1.6777 1.2897 0.5286  -0.2723 -0.1140 233  PRO A O   
1704  C CB  . PRO A 233  ? 1.5692 1.6251 1.2739 0.5452  -0.2425 -0.1207 233  PRO A CB  
1705  C CG  . PRO A 233  ? 1.5632 1.5951 1.2272 0.5281  -0.2951 -0.0917 233  PRO A CG  
1706  C CD  . PRO A 233  ? 1.5499 1.6007 1.2335 0.5218  -0.3222 -0.0926 233  PRO A CD  
1707  N N   . GLU A 234  ? 1.4188 1.6116 1.2637 0.5539  -0.2013 -0.1667 234  GLU A N   
1708  C CA  . GLU A 234  ? 1.3311 1.5958 1.2250 0.5497  -0.1982 -0.1686 234  GLU A CA  
1709  C C   . GLU A 234  ? 1.2838 1.5747 1.1674 0.5321  -0.2152 -0.1296 234  GLU A C   
1710  O O   . GLU A 234  ? 1.2914 1.6126 1.1777 0.5238  -0.2430 -0.1132 234  GLU A O   
1711  C CB  . GLU A 234  ? 1.3096 1.6108 1.2634 0.5615  -0.1514 -0.2026 234  GLU A CB  
1712  C CG  . GLU A 234  ? 1.4624 1.8340 1.4637 0.5627  -0.1585 -0.2174 234  GLU A CG  
1713  C CD  . GLU A 234  ? 1.4441 1.8605 1.5143 0.5729  -0.1170 -0.2555 234  GLU A CD  
1714  O OE1 . GLU A 234  ? 1.4644 1.8546 1.5556 0.5820  -0.0799 -0.2782 234  GLU A OE1 
1715  O OE2 . GLU A 234  ? 1.4055 1.8830 1.5099 0.5725  -0.1213 -0.2635 234  GLU A OE2 
1716  N N   . TYR A 235  ? 1.2187 1.4971 1.0906 0.5278  -0.1979 -0.1134 235  TYR A N   
1717  C CA  . TYR A 235  ? 1.1718 1.4679 1.0322 0.5109  -0.2179 -0.0748 235  TYR A CA  
1718  C C   . TYR A 235  ? 1.1744 1.4173 0.9871 0.5085  -0.2246 -0.0557 235  TYR A C   
1719  O O   . TYR A 235  ? 1.1994 1.3925 0.9842 0.5211  -0.2120 -0.0716 235  TYR A O   
1720  C CB  . TYR A 235  ? 1.1485 1.5053 1.0553 0.5083  -0.1897 -0.0715 235  TYR A CB  
1721  C CG  . TYR A 235  ? 1.1486 1.5608 1.1079 0.5162  -0.1704 -0.1004 235  TYR A CG  
1722  C CD1 . TYR A 235  ? 1.1617 1.6341 1.1548 0.5099  -0.1629 -0.0905 235  TYR A CD1 
1723  C CD2 . TYR A 235  ? 1.1638 1.5702 1.1416 0.5310  -0.1589 -0.1394 235  TYR A CD2 
1724  C CE1 . TYR A 235  ? 1.1699 1.6952 1.2092 0.5188  -0.1471 -0.1203 235  TYR A CE1 
1725  C CE2 . TYR A 235  ? 1.1660 1.6274 1.1954 0.5394  -0.1447 -0.1699 235  TYR A CE2 
1726  C CZ  . TYR A 235  ? 1.1761 1.6964 1.2337 0.5336  -0.1398 -0.1609 235  TYR A CZ  
1727  O OH  . TYR A 235  ? 1.1666 1.7415 1.2716 0.5434  -0.1283 -0.1937 235  TYR A OH  
1728  N N   . ASN A 236  ? 1.1394 1.3950 0.9441 0.4940  -0.2435 -0.0223 236  ASN A N   
1729  C CA  . ASN A 236  ? 1.1662 1.3760 0.9243 0.4912  -0.2611 -0.0029 236  ASN A CA  
1730  C C   . ASN A 236  ? 1.1244 1.3283 0.8772 0.5020  -0.2270 0.0002  236  ASN A C   
1731  O O   . ASN A 236  ? 1.2164 1.3790 0.9236 0.5053  -0.2398 0.0131  236  ASN A O   
1732  C CB  . ASN A 236  ? 1.2205 1.4456 0.9771 0.4702  -0.3025 0.0314  236  ASN A CB  
1733  C CG  . ASN A 236  ? 1.3236 1.5218 1.0614 0.4615  -0.3427 0.0337  236  ASN A CG  
1734  O OD1 . ASN A 236  ? 1.3438 1.5172 1.0711 0.4715  -0.3407 0.0094  236  ASN A OD1 
1735  N ND2 . ASN A 236  ? 1.3789 1.5812 1.1166 0.4427  -0.3790 0.0631  236  ASN A ND2 
1736  N N   . PHE A 237  ? 0.9912 1.2370 0.7905 0.5083  -0.1848 -0.0107 237  PHE A N   
1737  C CA  . PHE A 237  ? 0.9827 1.2175 0.7803 0.5222  -0.1443 -0.0107 237  PHE A CA  
1738  C C   . PHE A 237  ? 0.9250 1.1797 0.7700 0.5344  -0.0969 -0.0436 237  PHE A C   
1739  O O   . PHE A 237  ? 0.8559 1.1476 0.7390 0.5294  -0.1003 -0.0605 237  PHE A O   
1740  C CB  . PHE A 237  ? 0.8849 1.1610 0.7055 0.5141  -0.1389 0.0173  237  PHE A CB  
1741  C CG  . PHE A 237  ? 0.8981 1.1785 0.6992 0.4967  -0.1872 0.0492  237  PHE A CG  
1742  C CD1 . PHE A 237  ? 0.9126 1.1934 0.7015 0.4960  -0.1917 0.0756  237  PHE A CD1 
1743  C CD2 . PHE A 237  ? 0.8958 1.1829 0.6970 0.4813  -0.2268 0.0537  237  PHE A CD2 
1744  C CE1 . PHE A 237  ? 0.9466 1.2361 0.7285 0.4788  -0.2368 0.1037  237  PHE A CE1 
1745  C CE2 . PHE A 237  ? 0.9866 1.2792 0.7803 0.4639  -0.2683 0.0834  237  PHE A CE2 
1746  C CZ  . PHE A 237  ? 0.9385 1.2333 0.7251 0.4620  -0.2738 0.1072  237  PHE A CZ  
1747  N N   . ILE A 238  ? 0.9846 1.2149 0.8287 0.5516  -0.0521 -0.0526 238  ILE A N   
1748  C CA  . ILE A 238  ? 0.9739 1.2282 0.8770 0.5616  -0.0020 -0.0831 238  ILE A CA  
1749  C C   . ILE A 238  ? 1.0217 1.3168 0.9688 0.5615  0.0338  -0.0728 238  ILE A C   
1750  O O   . ILE A 238  ? 1.0516 1.3302 0.9713 0.5654  0.0406  -0.0453 238  ILE A O   
1751  C CB  . ILE A 238  ? 0.8965 1.0970 0.7822 0.5809  0.0291  -0.1050 238  ILE A CB  
1752  C CG1 . ILE A 238  ? 0.9416 1.0922 0.7660 0.5807  -0.0131 -0.1049 238  ILE A CG1 
1753  C CG2 . ILE A 238  ? 0.9647 1.1946 0.9205 0.5864  0.0645  -0.1439 238  ILE A CG2 
1754  C CD1 . ILE A 238  ? 0.9689 1.0755 0.7892 0.5978  0.0124  -0.1361 238  ILE A CD1 
1755  N N   . GLY A 239  ? 1.0320 1.3818 1.0475 0.5577  0.0539  -0.0960 239  GLY A N   
1756  C CA  . GLY A 239  ? 1.0248 1.4260 1.0902 0.5532  0.0795  -0.0883 239  GLY A CA  
1757  C C   . GLY A 239  ? 1.0340 1.4630 1.1726 0.5616  0.1273  -0.1292 239  GLY A C   
1758  O O   . GLY A 239  ? 1.0313 1.4533 1.1857 0.5669  0.1279  -0.1626 239  GLY A O   
1759  N N   . TYR A 240  ? 1.0207 1.4803 1.2084 0.5633  0.1672  -0.1289 240  TYR A N   
1760  C CA  . TYR A 240  ? 1.0478 1.5160 1.3041 0.5743  0.2211  -0.1685 240  TYR A CA  
1761  C C   . TYR A 240  ? 1.0614 1.5603 1.3550 0.5721  0.2050  -0.2103 240  TYR A C   
1762  O O   . TYR A 240  ? 1.0339 1.5204 1.3670 0.5825  0.2347  -0.2465 240  TYR A O   
1763  C CB  . TYR A 240  ? 1.0183 1.5285 1.3361 0.5734  0.2613  -0.1691 240  TYR A CB  
1764  C CG  . TYR A 240  ? 0.9306 1.5096 1.2847 0.5602  0.2382  -0.1795 240  TYR A CG  
1765  C CD1 . TYR A 240  ? 0.8470 1.4679 1.2674 0.5615  0.2506  -0.2269 240  TYR A CD1 
1766  C CD2 . TYR A 240  ? 0.9268 1.5280 1.2473 0.5479  0.2027  -0.1423 240  TYR A CD2 
1767  C CE1 . TYR A 240  ? 0.8001 1.4812 1.2432 0.5529  0.2281  -0.2359 240  TYR A CE1 
1768  C CE2 . TYR A 240  ? 0.8866 1.5467 1.2339 0.5382  0.1845  -0.1489 240  TYR A CE2 
1769  C CZ  . TYR A 240  ? 0.8402 1.5395 1.2440 0.5417  0.1966  -0.1951 240  TYR A CZ  
1770  O OH  . TYR A 240  ? 0.8548 1.6121 1.2747 0.5346  0.1763  -0.1987 240  TYR A OH  
1771  N N   . LYS A 241  ? 1.1039 1.6421 1.3849 0.5598  0.1582  -0.2037 241  LYS A N   
1772  C CA  . LYS A 241  ? 1.1376 1.7131 1.4501 0.5598  0.1378  -0.2407 241  LYS A CA  
1773  C C   . LYS A 241  ? 1.2041 1.7391 1.5107 0.5704  0.1374  -0.2682 241  LYS A C   
1774  O O   . LYS A 241  ? 1.1997 1.7493 1.5685 0.5794  0.1651  -0.3124 241  LYS A O   
1775  C CB  . LYS A 241  ? 0.9232 1.5319 1.2017 0.5479  0.0844  -0.2187 241  LYS A CB  
1776  C CG  . LYS A 241  ? 0.6589 1.3339 0.9758 0.5415  0.0891  -0.2178 241  LYS A CG  
1777  C CD  . LYS A 241  ? 0.8409 1.5412 1.1176 0.5308  0.0406  -0.1876 241  LYS A CD  
1778  C CE  . LYS A 241  ? 1.2120 1.9776 1.5224 0.5266  0.0469  -0.1861 241  LYS A CE  
1779  N NZ  . LYS A 241  ? 1.1946 1.9685 1.4979 0.5158  0.0554  -0.1435 241  LYS A NZ  
1780  N N   . ASN A 242  ? 1.2509 1.7352 1.4872 0.5696  0.1068  -0.2437 242  ASN A N   
1781  C CA  . ASN A 242  ? 1.2774 1.7137 1.5015 0.5809  0.1114  -0.2650 242  ASN A CA  
1782  C C   . ASN A 242  ? 1.3539 1.7266 1.5435 0.5902  0.1440  -0.2478 242  ASN A C   
1783  O O   . ASN A 242  ? 1.3555 1.7037 1.4894 0.5860  0.1313  -0.2086 242  ASN A O   
1784  C CB  . ASN A 242  ? 1.2222 1.6428 1.3956 0.5772  0.0565  -0.2585 242  ASN A CB  
1785  C CG  . ASN A 242  ? 1.1496 1.5935 1.2840 0.5619  0.0106  -0.2219 242  ASN A CG  
1786  O OD1 . ASN A 242  ? 1.1283 1.5803 1.2427 0.5584  -0.0303 -0.2207 242  ASN A OD1 
1787  N ND2 . ASN A 242  ? 1.1006 1.5551 1.2269 0.5536  0.0188  -0.1909 242  ASN A ND2 
1788  N N   . PHE A 243  ? 1.4234 1.7707 1.6482 0.6044  0.1865  -0.2779 243  PHE A N   
1789  C CA  . PHE A 243  ? 1.5477 1.8381 1.7506 0.6178  0.2313  -0.2650 243  PHE A CA  
1790  C C   . PHE A 243  ? 1.6007 1.8860 1.8737 0.6306  0.2798  -0.3081 243  PHE A C   
1791  O O   . PHE A 243  ? 1.6269 1.8642 1.8978 0.6454  0.3275  -0.3072 243  PHE A O   
1792  C CB  . PHE A 243  ? 1.5577 1.8621 1.7716 0.6165  0.2616  -0.2399 243  PHE A CB  
1793  C CG  . PHE A 243  ? 1.6253 1.8700 1.8114 0.6341  0.3100  -0.2225 243  PHE A CG  
1794  C CD1 . PHE A 243  ? 1.6732 1.8646 1.7660 0.6399  0.2883  -0.1855 243  PHE A CD1 
1795  C CD2 . PHE A 243  ? 1.6350 1.8770 1.8884 0.6461  0.3772  -0.2428 243  PHE A CD2 
1796  C CE1 . PHE A 243  ? 1.7162 1.8531 1.7753 0.6597  0.3312  -0.1683 243  PHE A CE1 
1797  C CE2 . PHE A 243  ? 1.6796 1.8648 1.9029 0.6650  0.4242  -0.2227 243  PHE A CE2 
1798  C CZ  . PHE A 243  ? 1.7223 1.8551 1.8446 0.6730  0.4006  -0.1849 243  PHE A CZ  
1799  N N   . LYS A 244  ? 1.6530 1.9913 1.9926 0.6258  0.2688  -0.3463 244  LYS A N   
1800  C CA  . LYS A 244  ? 1.7394 2.0724 2.1396 0.6367  0.2953  -0.3911 244  LYS A CA  
1801  C C   . LYS A 244  ? 1.7585 2.0888 2.1249 0.6353  0.2409  -0.4005 244  LYS A C   
1802  O O   . LYS A 244  ? 1.8256 2.1482 2.2301 0.6448  0.2501  -0.4353 244  LYS A O   
1803  C CB  . LYS A 244  ? 1.7482 2.1404 2.2560 0.6316  0.3248  -0.4315 244  LYS A CB  
1804  C CG  . LYS A 244  ? 1.7958 2.1706 2.3383 0.6218  0.3819  -0.4198 244  LYS A CG  
1805  C CD  . LYS A 244  ? 1.7988 2.2012 2.4459 0.6045  0.4098  -0.4627 244  LYS A CD  
1806  C CE  . LYS A 244  ? 1.8092 2.1982 2.4998 0.5939  0.4662  -0.4511 244  LYS A CE  
1807  N NZ  . LYS A 244  ? 1.7670 2.2057 2.4733 0.5827  0.4576  -0.4431 244  LYS A NZ  
1808  N N   . ASN A 245  ? 1.7205 2.0551 2.0176 0.6242  0.1860  -0.3681 245  ASN A N   
1809  C CA  . ASN A 245  ? 1.7081 2.0301 1.9626 0.6233  0.1345  -0.3691 245  ASN A CA  
1810  C C   . ASN A 245  ? 1.6547 1.9645 1.8252 0.6105  0.0808  -0.3244 245  ASN A C   
1811  O O   . ASN A 245  ? 1.6503 1.9847 1.8093 0.5996  0.0746  -0.2970 245  ASN A O   
1812  C CB  . ASN A 245  ? 1.6885 2.0701 2.0076 0.6246  0.1163  -0.4095 245  ASN A CB  
1813  C CG  . ASN A 245  ? 1.6896 2.1352 2.0204 0.6134  0.0909  -0.4014 245  ASN A CG  
1814  O OD1 . ASN A 245  ? 1.7010 2.1546 2.0166 0.6044  0.1004  -0.3728 245  ASN A OD1 
1815  N ND2 . ASN A 245  ? 1.7038 2.1951 2.0589 0.6157  0.0583  -0.4253 245  ASN A ND2 
1816  N N   . PHE A 246  ? 1.5699 1.8426 1.6890 0.6119  0.0436  -0.3189 246  PHE A N   
1817  C CA  . PHE A 246  ? 1.4030 1.6514 1.4445 0.6006  -0.0064 -0.2796 246  PHE A CA  
1818  C C   . PHE A 246  ? 1.3386 1.5639 1.3538 0.6036  -0.0449 -0.2884 246  PHE A C   
1819  O O   . PHE A 246  ? 1.3532 1.5188 1.3315 0.6120  -0.0405 -0.2904 246  PHE A O   
1820  C CB  . PHE A 246  ? 1.3162 1.5012 1.2963 0.6036  0.0070  -0.2533 246  PHE A CB  
1821  C CG  . PHE A 246  ? 1.1959 1.3704 1.1145 0.5894  -0.0345 -0.2115 246  PHE A CG  
1822  C CD1 . PHE A 246  ? 1.0901 1.3105 1.0237 0.5769  -0.0395 -0.1894 246  PHE A CD1 
1823  C CD2 . PHE A 246  ? 1.2018 1.3194 1.0508 0.5888  -0.0672 -0.1956 246  PHE A CD2 
1824  C CE1 . PHE A 246  ? 1.0616 1.2738 0.9471 0.5635  -0.0767 -0.1519 246  PHE A CE1 
1825  C CE2 . PHE A 246  ? 1.1722 1.2816 0.9734 0.5750  -0.1059 -0.1600 246  PHE A CE2 
1826  C CZ  . PHE A 246  ? 1.1085 1.2662 0.9305 0.5621  -0.1104 -0.1379 246  PHE A CZ  
1827  N N   . GLU A 247  ? 1.2882 1.5573 1.3183 0.5985  -0.0812 -0.2919 247  GLU A N   
1828  C CA  . GLU A 247  ? 1.3024 1.5564 1.3198 0.6049  -0.1143 -0.3045 247  GLU A CA  
1829  C C   . GLU A 247  ? 1.4063 1.5990 1.3446 0.5975  -0.1502 -0.2714 247  GLU A C   
1830  O O   . GLU A 247  ? 1.4203 1.6234 1.3289 0.5840  -0.1874 -0.2408 247  GLU A O   
1831  C CB  . GLU A 247  ? 1.8298 2.1512 1.8831 0.6052  -0.1418 -0.3156 247  GLU A CB  
1832  C CG  . GLU A 247  ? 1.5717 1.9122 1.6683 0.6227  -0.1485 -0.3577 247  GLU A CG  
1833  C CD  . GLU A 247  ? 0.8763 1.2961 1.0227 0.6285  -0.1610 -0.3790 247  GLU A CD  
1834  O OE1 . GLU A 247  ? 0.8091 1.2689 0.9574 0.6187  -0.1614 -0.3619 247  GLU A OE1 
1835  O OE2 . GLU A 247  ? 0.7755 1.2188 0.9595 0.6443  -0.1700 -0.4143 247  GLU A OE2 
1836  N N   . ILE A 248  ? 1.4038 1.5321 1.3104 0.6065  -0.1368 -0.2781 248  ILE A N   
1837  C CA  . ILE A 248  ? 1.3810 1.4474 1.2152 0.6016  -0.1694 -0.2545 248  ILE A CA  
1838  C C   . ILE A 248  ? 1.3570 1.4086 1.1880 0.6077  -0.1981 -0.2680 248  ILE A C   
1839  O O   . ILE A 248  ? 1.3738 1.4082 1.2273 0.6235  -0.1772 -0.2989 248  ILE A O   
1840  C CB  . ILE A 248  ? 1.4065 1.4051 1.2003 0.6127  -0.1404 -0.2580 248  ILE A CB  
1841  C CG1 . ILE A 248  ? 1.3853 1.3923 1.1864 0.6138  -0.1005 -0.2494 248  ILE A CG1 
1842  C CG2 . ILE A 248  ? 1.4580 1.3967 1.1750 0.6067  -0.1780 -0.2344 248  ILE A CG2 
1843  C CD1 . ILE A 248  ? 1.4336 1.3708 1.1759 0.6254  -0.0798 -0.2424 248  ILE A CD1 
1844  N N   . THR A 249  ? 1.3358 1.3929 1.1424 0.5962  -0.2438 -0.2442 249  THR A N   
1845  C CA  . THR A 249  ? 1.3542 1.3988 1.1582 0.6029  -0.2726 -0.2532 249  THR A CA  
1846  C C   . THR A 249  ? 1.4399 1.4113 1.1817 0.5991  -0.2997 -0.2379 249  THR A C   
1847  O O   . THR A 249  ? 1.4484 1.4059 1.1537 0.5826  -0.3284 -0.2061 249  THR A O   
1848  C CB  . THR A 249  ? 1.4136 1.5116 1.2336 0.5958  -0.3055 -0.2362 249  THR A CB  
1849  O OG1 . THR A 249  ? 1.3718 1.5316 1.2247 0.5894  -0.2902 -0.2310 249  THR A OG1 
1850  C CG2 . THR A 249  ? 1.3937 1.5086 1.2422 0.6128  -0.3169 -0.2609 249  THR A CG2 
1851  N N   . ILE A 250  ? 1.4972 1.4226 1.2303 0.6140  -0.2917 -0.2616 250  ILE A N   
1852  C CA  . ILE A 250  ? 1.5741 1.4288 1.2489 0.6117  -0.3178 -0.2511 250  ILE A CA  
1853  C C   . ILE A 250  ? 1.6271 1.4752 1.3077 0.6163  -0.3492 -0.2539 250  ILE A C   
1854  O O   . ILE A 250  ? 1.5964 1.4737 1.3209 0.6310  -0.3391 -0.2779 250  ILE A O   
1855  C CB  . ILE A 250  ? 1.5963 1.3920 1.2432 0.6256  -0.2865 -0.2706 250  ILE A CB  
1856  C CG1 . ILE A 250  ? 1.6160 1.4082 1.3009 0.6458  -0.2636 -0.3058 250  ILE A CG1 
1857  C CG2 . ILE A 250  ? 1.5533 1.3667 1.2109 0.6273  -0.2459 -0.2722 250  ILE A CG2 
1858  C CD1 . ILE A 250  ? 1.6629 1.4053 1.3309 0.6616  -0.2212 -0.3255 250  ILE A CD1 
1859  N N   . LYS A 251  ? 1.7255 1.5353 1.3649 0.6046  -0.3872 -0.2301 251  LYS A N   
1860  C CA  . LYS A 251  ? 1.8221 1.6289 1.4680 0.6077  -0.4182 -0.2251 251  LYS A CA  
1861  C C   . LYS A 251  ? 1.9716 1.7007 1.5708 0.6061  -0.4425 -0.2212 251  LYS A C   
1862  O O   . LYS A 251  ? 2.0065 1.7053 1.5703 0.5886  -0.4675 -0.1973 251  LYS A O   
1863  C CB  . LYS A 251  ? 1.8137 1.6710 1.4741 0.5936  -0.4440 -0.1931 251  LYS A CB  
1864  C CG  . LYS A 251  ? 1.7754 1.7091 1.4771 0.5936  -0.4232 -0.1949 251  LYS A CG  
1865  C CD  . LYS A 251  ? 1.7691 1.7534 1.4852 0.5862  -0.4469 -0.1664 251  LYS A CD  
1866  C CE  . LYS A 251  ? 1.7894 1.7609 1.4792 0.5619  -0.4682 -0.1265 251  LYS A CE  
1867  N NZ  . LYS A 251  ? 1.7535 1.7806 1.4615 0.5549  -0.4800 -0.0977 251  LYS A NZ  
1868  N N   . ALA A 252  ? 2.0388 1.7378 1.6430 0.6247  -0.4356 -0.2466 252  ALA A N   
1869  C CA  . ALA A 252  ? 2.1288 1.7496 1.6901 0.6274  -0.4507 -0.2511 252  ALA A CA  
1870  C C   . ALA A 252  ? 2.1482 1.7559 1.7155 0.6293  -0.4833 -0.2406 252  ALA A C   
1871  O O   . ALA A 252  ? 2.1272 1.7760 1.7343 0.6422  -0.4831 -0.2465 252  ALA A O   
1872  C CB  . ALA A 252  ? 2.1548 1.7398 1.7123 0.6483  -0.4151 -0.2865 252  ALA A CB  
1873  N N   . ARG A 253  ? 2.2039 1.7517 1.7317 0.6184  -0.5110 -0.2269 253  ARG A N   
1874  C CA  . ARG A 253  ? 2.2399 1.7724 1.7735 0.6171  -0.5422 -0.2102 253  ARG A CA  
1875  C C   . ARG A 253  ? 2.2348 1.6870 1.7255 0.6074  -0.5666 -0.2061 253  ARG A C   
1876  O O   . ARG A 253  ? 2.2682 1.6946 1.7265 0.5906  -0.5760 -0.1987 253  ARG A O   
1877  C CB  . ARG A 253  ? 2.2900 1.8761 1.8443 0.6012  -0.5608 -0.1746 253  ARG A CB  
1878  C CG  . ARG A 253  ? 2.3991 1.9768 1.9304 0.5752  -0.5734 -0.1524 253  ARG A CG  
1879  C CD  . ARG A 253  ? 2.4939 2.0941 2.0410 0.5583  -0.6002 -0.1132 253  ARG A CD  
1880  N NE  . ARG A 253  ? 2.6079 2.1790 2.1606 0.5660  -0.6191 -0.1047 253  ARG A NE  
1881  C CZ  . ARG A 253  ? 2.6403 2.2479 2.2193 0.5842  -0.6164 -0.1010 253  ARG A CZ  
1882  N NH1 . ARG A 253  ? 2.6042 2.2803 2.2079 0.5959  -0.5972 -0.1086 253  ARG A NH1 
1883  N NH2 . ARG A 253  ? 2.6875 2.2631 2.2682 0.5924  -0.6337 -0.0906 253  ARG A NH2 
1884  N N   . TYR A 254  ? 2.1903 1.6038 1.6825 0.6186  -0.5787 -0.2117 254  TYR A N   
1885  C CA  . TYR A 254  ? 2.1630 1.4988 1.6195 0.6100  -0.6027 -0.2104 254  TYR A CA  
1886  C C   . TYR A 254  ? 2.1078 1.4431 1.5703 0.5859  -0.6369 -0.1737 254  TYR A C   
1887  O O   . TYR A 254  ? 2.0397 1.4315 1.5336 0.5803  -0.6411 -0.1474 254  TYR A O   
1888  C CB  . TYR A 254  ? 2.1884 1.4797 1.6470 0.6312  -0.6009 -0.2300 254  TYR A CB  
1889  C CG  . TYR A 254  ? 2.1764 1.4757 1.6446 0.6569  -0.5647 -0.2650 254  TYR A CG  
1890  C CD1 . TYR A 254  ? 2.1647 1.4986 1.6762 0.6782  -0.5552 -0.2739 254  TYR A CD1 
1891  C CD2 . TYR A 254  ? 2.1947 1.4673 1.6308 0.6610  -0.5394 -0.2886 254  TYR A CD2 
1892  C CE1 . TYR A 254  ? 2.1509 1.4938 1.6815 0.7005  -0.5217 -0.3074 254  TYR A CE1 
1893  C CE2 . TYR A 254  ? 2.1849 1.4633 1.6362 0.6841  -0.5019 -0.3190 254  TYR A CE2 
1894  C CZ  . TYR A 254  ? 2.1587 1.4729 1.6613 0.7025  -0.4933 -0.3292 254  TYR A CZ  
1895  O OH  . TYR A 254  ? 2.1504 1.4724 1.6783 0.7244  -0.4557 -0.3611 254  TYR A OH  
1896  N N   . PHE A 255  ? 2.1705 1.4410 1.6041 0.5721  -0.6604 -0.1729 255  PHE A N   
1897  C CA  . PHE A 255  ? 2.2072 1.4740 1.6517 0.5459  -0.6912 -0.1404 255  PHE A CA  
1898  C C   . PHE A 255  ? 2.2953 1.5630 1.7722 0.5494  -0.7034 -0.1169 255  PHE A C   
1899  O O   . PHE A 255  ? 2.2761 1.5497 1.7737 0.5302  -0.7232 -0.0841 255  PHE A O   
1900  C CB  . PHE A 255  ? 2.2547 1.4485 1.6631 0.5318  -0.7147 -0.1526 255  PHE A CB  
1901  C CG  . PHE A 255  ? 2.2355 1.4280 1.6075 0.5259  -0.7101 -0.1676 255  PHE A CG  
1902  C CD1 . PHE A 255  ? 2.2354 1.4249 1.6035 0.5006  -0.7364 -0.1531 255  PHE A CD1 
1903  C CD2 . PHE A 255  ? 2.2176 1.4121 1.5618 0.5469  -0.6784 -0.1955 255  PHE A CD2 
1904  C CE1 . PHE A 255  ? 2.2376 1.4268 1.5696 0.4983  -0.7339 -0.1659 255  PHE A CE1 
1905  C CE2 . PHE A 255  ? 2.2147 1.4064 1.5219 0.5447  -0.6717 -0.2061 255  PHE A CE2 
1906  C CZ  . PHE A 255  ? 2.2310 1.4204 1.5295 0.5213  -0.7008 -0.1912 255  PHE A CZ  
1907  N N   . TYR A 256  ? 2.4143 1.6732 1.8965 0.5752  -0.6906 -0.1334 256  TYR A N   
1908  C CA  . TYR A 256  ? 2.5414 1.7976 2.0502 0.5850  -0.7007 -0.1124 256  TYR A CA  
1909  C C   . TYR A 256  ? 2.6662 2.0022 2.2070 0.5975  -0.6904 -0.0917 256  TYR A C   
1910  O O   . TYR A 256  ? 2.7269 2.0725 2.2842 0.6205  -0.6883 -0.0898 256  TYR A O   
1911  C CB  . TYR A 256  ? 2.5353 1.7341 2.0348 0.6072  -0.6978 -0.1384 256  TYR A CB  
1912  C CG  . TYR A 256  ? 2.4689 1.6652 1.9540 0.6296  -0.6707 -0.1806 256  TYR A CG  
1913  C CD1 . TYR A 256  ? 2.4230 1.6577 1.9352 0.6573  -0.6530 -0.1925 256  TYR A CD1 
1914  C CD2 . TYR A 256  ? 2.4753 1.6277 1.9211 0.6250  -0.6626 -0.2088 256  TYR A CD2 
1915  C CE1 . TYR A 256  ? 2.3906 1.6219 1.8993 0.6771  -0.6256 -0.2310 256  TYR A CE1 
1916  C CE2 . TYR A 256  ? 2.4476 1.5935 1.8819 0.6468  -0.6330 -0.2445 256  TYR A CE2 
1917  C CZ  . TYR A 256  ? 2.3986 1.5841 1.8686 0.6715  -0.6135 -0.2553 256  TYR A CZ  
1918  O OH  . TYR A 256  ? 2.3724 1.5519 1.8403 0.6921  -0.5815 -0.2907 256  TYR A OH  
1919  N N   . ASN A 257  ? 2.6994 2.0921 2.2476 0.5836  -0.6851 -0.0770 257  ASN A N   
1920  C CA  . ASN A 257  ? 2.7257 2.1976 2.3000 0.5937  -0.6755 -0.0588 257  ASN A CA  
1921  C C   . ASN A 257  ? 2.6493 2.1593 2.2377 0.6256  -0.6574 -0.0852 257  ASN A C   
1922  O O   . ASN A 257  ? 2.6109 2.1641 2.2186 0.6427  -0.6592 -0.0704 257  ASN A O   
1923  C CB  . ASN A 257  ? 2.8739 2.3551 2.4651 0.5873  -0.6920 -0.0124 257  ASN A CB  
1924  C CG  . ASN A 257  ? 3.0573 2.4844 2.6500 0.6000  -0.7050 -0.0045 257  ASN A CG  
1925  O OD1 . ASN A 257  ? 3.1492 2.5068 2.7309 0.5874  -0.7178 -0.0098 257  ASN A OD1 
1926  N ND2 . ASN A 257  ? 3.0820 2.5406 2.6880 0.6263  -0.7029 0.0081  257  ASN A ND2 
1927  N N   . LYS A 258  ? 2.6074 2.1023 2.1870 0.6345  -0.6394 -0.1248 258  LYS A N   
1928  C CA  . LYS A 258  ? 2.5818 2.1055 2.1827 0.6637  -0.6218 -0.1550 258  LYS A CA  
1929  C C   . LYS A 258  ? 2.4655 2.0037 2.0664 0.6655  -0.5931 -0.1897 258  LYS A C   
1930  O O   . LYS A 258  ? 2.5073 1.9907 2.0839 0.6637  -0.5837 -0.2112 258  LYS A O   
1931  C CB  . LYS A 258  ? 2.6755 2.1410 2.2730 0.6816  -0.6285 -0.1686 258  LYS A CB  
1932  C CG  . LYS A 258  ? 2.7238 2.2149 2.3451 0.7047  -0.6410 -0.1533 258  LYS A CG  
1933  C CD  . LYS A 258  ? 2.7019 2.2723 2.3558 0.7262  -0.6264 -0.1725 258  LYS A CD  
1934  C CE  . LYS A 258  ? 2.7279 2.3324 2.4015 0.7532  -0.6412 -0.1583 258  LYS A CE  
1935  N NZ  . LYS A 258  ? 2.6878 2.3779 2.3918 0.7703  -0.6317 -0.1756 258  LYS A NZ  
1936  N N   . VAL A 259  ? 2.3667 1.9778 1.9952 0.6710  -0.5776 -0.1955 259  VAL A N   
1937  C CA  . VAL A 259  ? 2.2634 1.8944 1.8971 0.6694  -0.5473 -0.2224 259  VAL A CA  
1938  C C   . VAL A 259  ? 2.2363 1.8313 1.8734 0.6876  -0.5234 -0.2623 259  VAL A C   
1939  O O   . VAL A 259  ? 2.2353 1.8163 1.8884 0.7077  -0.5269 -0.2763 259  VAL A O   
1940  C CB  . VAL A 259  ? 2.1297 1.8483 1.8021 0.6750  -0.5336 -0.2260 259  VAL A CB  
1941  C CG1 . VAL A 259  ? 2.1126 1.8709 1.7846 0.6636  -0.5560 -0.1860 259  VAL A CG1 
1942  C CG2 . VAL A 259  ? 2.1119 1.8652 1.8267 0.7039  -0.5229 -0.2575 259  VAL A CG2 
1943  N N   . VAL A 260  ? 2.2068 1.7855 1.8282 0.6817  -0.4975 -0.2790 260  VAL A N   
1944  C CA  . VAL A 260  ? 2.2244 1.7771 1.8538 0.7000  -0.4656 -0.3164 260  VAL A CA  
1945  C C   . VAL A 260  ? 2.2204 1.8354 1.9126 0.7211  -0.4510 -0.3393 260  VAL A C   
1946  O O   . VAL A 260  ? 2.1715 1.8540 1.8928 0.7187  -0.4584 -0.3292 260  VAL A O   
1947  C CB  . VAL A 260  ? 2.1948 1.7401 1.8047 0.6923  -0.4350 -0.3256 260  VAL A CB  
1948  C CG1 . VAL A 260  ? 2.1994 1.7265 1.8276 0.7136  -0.3940 -0.3633 260  VAL A CG1 
1949  C CG2 . VAL A 260  ? 2.2311 1.7149 1.7770 0.6743  -0.4527 -0.3071 260  VAL A CG2 
1950  N N   . THR A 261  ? 2.2758 1.8698 1.9910 0.7425  -0.4317 -0.3713 261  THR A N   
1951  C CA  . THR A 261  ? 2.2816 1.9376 2.0653 0.7630  -0.4170 -0.3990 261  THR A CA  
1952  C C   . THR A 261  ? 2.2848 1.9535 2.0987 0.7676  -0.3700 -0.4299 261  THR A C   
1953  O O   . THR A 261  ? 2.2700 1.9792 2.0932 0.7560  -0.3559 -0.4258 261  THR A O   
1954  C CB  . THR A 261  ? 2.3249 1.9639 2.1324 0.7866  -0.4282 -0.4147 261  THR A CB  
1955  O OG1 . THR A 261  ? 2.3509 1.9919 2.1404 0.7852  -0.4698 -0.3838 261  THR A OG1 
1956  C CG2 . THR A 261  ? 2.2970 2.0012 2.1808 0.8082  -0.4117 -0.4494 261  THR A CG2 
1957  N N   . GLU A 262  ? 2.3371 1.9706 2.1695 0.7851  -0.3429 -0.4599 262  GLU A N   
1958  C CA  . GLU A 262  ? 2.3847 2.0161 2.2392 0.7889  -0.2929 -0.4847 262  GLU A CA  
1959  C C   . GLU A 262  ? 2.4120 1.9766 2.1890 0.7748  -0.2830 -0.4664 262  GLU A C   
1960  O O   . GLU A 262  ? 2.4352 1.9420 2.1527 0.7689  -0.3096 -0.4486 262  GLU A O   
1961  C CB  . GLU A 262  ? 2.4940 2.1082 2.3967 0.8133  -0.2635 -0.5219 262  GLU A CB  
1962  C CG  . GLU A 262  ? 2.5849 2.1948 2.5179 0.8191  -0.2050 -0.5472 262  GLU A CG  
1963  C CD  . GLU A 262  ? 2.6992 2.2829 2.6783 0.8429  -0.1730 -0.5817 262  GLU A CD  
1964  O OE1 . GLU A 262  ? 2.7712 2.2950 2.7232 0.8489  -0.1321 -0.5893 262  GLU A OE1 
1965  O OE2 . GLU A 262  ? 2.7119 2.3350 2.7538 0.8572  -0.1886 -0.6008 262  GLU A OE2 
1966  N N   . ALA A 263  ? 2.4190 1.9922 2.1977 0.7704  -0.2458 -0.4712 263  ALA A N   
1967  C CA  . ALA A 263  ? 2.4675 1.9811 2.1722 0.7614  -0.2340 -0.4559 263  ALA A CA  
1968  C C   . ALA A 263  ? 2.4231 1.9473 2.1516 0.7678  -0.1790 -0.4714 263  ALA A C   
1969  O O   . ALA A 263  ? 2.3893 1.9777 2.1910 0.7707  -0.1587 -0.4871 263  ALA A O   
1970  C CB  . ALA A 263  ? 2.4848 2.0099 2.1450 0.7374  -0.2721 -0.4202 263  ALA A CB  
1971  N N   . ASP A 264  ? 2.4286 1.8879 2.0954 0.7718  -0.1538 -0.4681 264  ASP A N   
1972  C CA  . ASP A 264  ? 2.4190 1.8804 2.0989 0.7791  -0.0982 -0.4768 264  ASP A CA  
1973  C C   . ASP A 264  ? 2.4069 1.8720 2.0338 0.7621  -0.1072 -0.4470 264  ASP A C   
1974  O O   . ASP A 264  ? 2.4179 1.8301 1.9629 0.7563  -0.1320 -0.4282 264  ASP A O   
1975  C CB  . ASP A 264  ? 2.5442 1.9308 2.1933 0.8014  -0.0551 -0.4943 264  ASP A CB  
1976  C CG  . ASP A 264  ? 2.6170 2.0257 2.3442 0.8181  0.0086  -0.5219 264  ASP A CG  
1977  O OD1 . ASP A 264  ? 2.5841 2.0568 2.3714 0.8107  0.0250  -0.5238 264  ASP A OD1 
1978  O OD2 . ASP A 264  ? 2.7055 2.0674 2.4384 0.8387  0.0435  -0.5427 264  ASP A OD2 
1979  N N   . VAL A 265  ? 2.3553 1.8841 2.0319 0.7544  -0.0892 -0.4442 265  VAL A N   
1980  C CA  . VAL A 265  ? 2.3090 1.8500 1.9462 0.7388  -0.0963 -0.4159 265  VAL A CA  
1981  C C   . VAL A 265  ? 2.3459 1.8673 1.9722 0.7497  -0.0402 -0.4169 265  VAL A C   
1982  O O   . VAL A 265  ? 2.3489 1.8969 2.0435 0.7604  0.0074  -0.4383 265  VAL A O   
1983  C CB  . VAL A 265  ? 2.1311 1.7568 1.8250 0.7221  -0.1137 -0.4071 265  VAL A CB  
1984  C CG1 . VAL A 265  ? 2.0939 1.7227 1.7408 0.7069  -0.1233 -0.3761 265  VAL A CG1 
1985  C CG2 . VAL A 265  ? 2.0855 1.7417 1.7971 0.7133  -0.1656 -0.4031 265  VAL A CG2 
1986  N N   . TYR A 266  ? 2.4028 1.8816 1.9475 0.7471  -0.0465 -0.3933 266  TYR A N   
1987  C CA  . TYR A 266  ? 2.4544 1.9100 1.9764 0.7602  0.0058  -0.3886 266  TYR A CA  
1988  C C   . TYR A 266  ? 2.3884 1.8628 1.8734 0.7464  -0.0095 -0.3578 266  TYR A C   
1989  O O   . TYR A 266  ? 2.4260 1.8560 1.8264 0.7445  -0.0386 -0.3388 266  TYR A O   
1990  C CB  . TYR A 266  ? 2.6349 2.0018 2.0799 0.7827  0.0278  -0.3938 266  TYR A CB  
1991  C CG  . TYR A 266  ? 2.7710 2.1147 2.2584 0.8028  0.0684  -0.4245 266  TYR A CG  
1992  C CD1 . TYR A 266  ? 2.8240 2.1783 2.3499 0.7996  0.0394  -0.4424 266  TYR A CD1 
1993  C CD2 . TYR A 266  ? 2.8776 2.1865 2.3670 0.8266  0.1371  -0.4342 266  TYR A CD2 
1994  C CE1 . TYR A 266  ? 2.8853 2.2194 2.4542 0.8188  0.0756  -0.4710 266  TYR A CE1 
1995  C CE2 . TYR A 266  ? 2.9423 2.2296 2.4765 0.8450  0.1766  -0.4623 266  TYR A CE2 
1996  C CZ  . TYR A 266  ? 2.9462 2.2474 2.5213 0.8407  0.1443  -0.4816 266  TYR A CZ  
1997  O OH  . TYR A 266  ? 2.9771 2.2591 2.6019 0.8595  0.1824  -0.5101 266  TYR A OH  
1998  N N   . ILE A 267  ? 2.2725 1.8121 1.8232 0.7383  0.0115  -0.3553 267  ILE A N   
1999  C CA  . ILE A 267  ? 2.1843 1.7500 1.7131 0.7253  0.0002  -0.3267 267  ILE A CA  
2000  C C   . ILE A 267  ? 2.1924 1.7442 1.7133 0.7405  0.0581  -0.3199 267  ILE A C   
2001  O O   . ILE A 267  ? 2.2001 1.7753 1.7905 0.7496  0.1108  -0.3376 267  ILE A O   
2002  C CB  . ILE A 267  ? 2.0199 1.6689 1.6217 0.7051  -0.0190 -0.3243 267  ILE A CB  
2003  C CG1 . ILE A 267  ? 1.9688 1.6344 1.5825 0.6930  -0.0717 -0.3291 267  ILE A CG1 
2004  C CG2 . ILE A 267  ? 2.0127 1.6848 1.5873 0.6906  -0.0368 -0.2928 267  ILE A CG2 
2005  C CD1 . ILE A 267  ? 1.8693 1.6171 1.5572 0.6788  -0.0863 -0.3317 267  ILE A CD1 
2006  N N   . THR A 268  ? 2.2107 1.7257 1.6498 0.7438  0.0473  -0.2943 268  THR A N   
2007  C CA  . THR A 268  ? 2.2238 1.7173 1.6397 0.7620  0.0999  -0.2825 268  THR A CA  
2008  C C   . THR A 268  ? 2.2125 1.7399 1.6101 0.7475  0.0743  -0.2521 268  THR A C   
2009  O O   . THR A 268  ? 2.2275 1.7506 1.5763 0.7333  0.0156  -0.2363 268  THR A O   
2010  C CB  . THR A 268  ? 2.3479 1.7535 1.6630 0.7878  0.1122  -0.2789 268  THR A CB  
2011  O OG1 . THR A 268  ? 2.3879 1.7667 1.6295 0.7774  0.0449  -0.2688 268  THR A OG1 
2012  C CG2 . THR A 268  ? 2.3826 1.7477 1.7152 0.8077  0.1537  -0.3074 268  THR A CG2 
2013  N N   . PHE A 269  ? 2.1586 1.7184 1.5987 0.7512  0.1194  -0.2441 269  PHE A N   
2014  C CA  . PHE A 269  ? 2.0827 1.6805 1.5165 0.7383  0.1008  -0.2153 269  PHE A CA  
2015  C C   . PHE A 269  ? 2.0462 1.5999 1.4084 0.7598  0.1264  -0.1919 269  PHE A C   
2016  O O   . PHE A 269  ? 2.1204 1.6114 1.4340 0.7871  0.1643  -0.1970 269  PHE A O   
2017  C CB  . PHE A 269  ? 2.0266 1.6978 1.5612 0.7264  0.1294  -0.2214 269  PHE A CB  
2018  C CG  . PHE A 269  ? 1.9761 1.6942 1.5843 0.7107  0.1108  -0.2469 269  PHE A CG  
2019  C CD1 . PHE A 269  ? 1.9556 1.6862 1.6380 0.7198  0.1567  -0.2783 269  PHE A CD1 
2020  C CD2 . PHE A 269  ? 1.9411 1.6893 1.5444 0.6883  0.0471  -0.2394 269  PHE A CD2 
2021  C CE1 . PHE A 269  ? 1.9138 1.6894 1.6613 0.7082  0.1357  -0.3028 269  PHE A CE1 
2022  C CE2 . PHE A 269  ? 1.8986 1.6885 1.5626 0.6776  0.0293  -0.2605 269  PHE A CE2 
2023  C CZ  . PHE A 269  ? 1.8880 1.6928 1.6223 0.6882  0.0716  -0.2931 269  PHE A CZ  
2024  N N   . GLY A 270  ? 1.9369 1.5243 1.2934 0.7494  0.1077  -0.1654 270  GLY A N   
2025  C CA  . GLY A 270  ? 1.9611 1.5123 1.2494 0.7712  0.1278  -0.1403 270  GLY A CA  
2026  C C   . GLY A 270  ? 1.8745 1.4726 1.1686 0.7567  0.1011  -0.1115 270  GLY A C   
2027  O O   . GLY A 270  ? 1.8627 1.5077 1.1858 0.7284  0.0491  -0.1076 270  GLY A O   
2028  N N   . ILE A 271  ? 1.8135 1.3979 1.0808 0.7774  0.1387  -0.0900 271  ILE A N   
2029  C CA  . ILE A 271  ? 1.6892 1.3165 0.9637 0.7673  0.1196  -0.0613 271  ILE A CA  
2030  C C   . ILE A 271  ? 1.7598 1.3588 0.9445 0.7691  0.0576  -0.0432 271  ILE A C   
2031  O O   . ILE A 271  ? 1.8203 1.3714 0.9448 0.7744  0.0276  -0.0555 271  ILE A O   
2032  C CB  . ILE A 271  ? 1.6230 1.2453 0.9060 0.7907  0.1845  -0.0452 271  ILE A CB  
2033  C CG1 . ILE A 271  ? 1.5647 1.1920 0.9251 0.7964  0.2535  -0.0700 271  ILE A CG1 
2034  C CG2 . ILE A 271  ? 1.5738 1.2584 0.8993 0.7742  0.1714  -0.0214 271  ILE A CG2 
2035  C CD1 . ILE A 271  ? 1.4426 1.1419 0.9087 0.7646  0.2423  -0.0917 271  ILE A CD1 
2036  N N   . ARG A 272  ? 1.8049 1.4337 0.9831 0.7647  0.0369  -0.0157 272  ARG A N   
2037  C CA  . ARG A 272  ? 1.9392 1.5499 1.0443 0.7628  -0.0300 -0.0012 272  ARG A CA  
2038  C C   . ARG A 272  ? 2.0219 1.6724 1.1343 0.7596  -0.0446 0.0296  272  ARG A C   
2039  O O   . ARG A 272  ? 1.9559 1.6717 1.1486 0.7358  -0.0434 0.0373  272  ARG A O   
2040  C CB  . ARG A 272  ? 1.8834 1.5133 1.0100 0.7302  -0.0932 -0.0150 272  ARG A CB  
2041  C CG  . ARG A 272  ? 1.9170 1.5197 0.9736 0.7267  -0.1636 -0.0087 272  ARG A CG  
2042  C CD  . ARG A 272  ? 1.8967 1.4814 0.9540 0.7089  -0.2019 -0.0320 272  ARG A CD  
2043  N NE  . ARG A 272  ? 1.9243 1.5040 0.9506 0.6924  -0.2759 -0.0270 272  ARG A NE  
2044  C CZ  . ARG A 272  ? 1.9659 1.5086 0.9640 0.6848  -0.3150 -0.0460 272  ARG A CZ  
2045  N NH1 . ARG A 272  ? 1.9788 1.4869 0.9722 0.6940  -0.2865 -0.0697 272  ARG A NH1 
2046  N NH2 . ARG A 272  ? 1.9869 1.5267 0.9657 0.6685  -0.3816 -0.0421 272  ARG A NH2 
2047  N N   . GLU A 273  ? 2.1908 1.8026 1.2183 0.7851  -0.0598 0.0467  273  GLU A N   
2048  C CA  . GLU A 273  ? 2.2643 1.9128 1.2958 0.7847  -0.0782 0.0766  273  GLU A CA  
2049  C C   . GLU A 273  ? 2.2250 1.9253 1.2982 0.7464  -0.1489 0.0806  273  GLU A C   
2050  O O   . GLU A 273  ? 2.1651 1.9281 1.3080 0.7267  -0.1492 0.0968  273  GLU A O   
2051  C CB  . GLU A 273  ? 2.4522 2.0462 1.3761 0.8232  -0.0872 0.0921  273  GLU A CB  
2052  C CG  . GLU A 273  ? 2.5437 2.1158 1.4481 0.8607  -0.0127 0.1101  273  GLU A CG  
2053  C CD  . GLU A 273  ? 2.4993 2.1354 1.5070 0.8452  0.0323  0.1233  273  GLU A CD  
2054  O OE1 . GLU A 273  ? 2.4534 2.1476 1.5065 0.8233  -0.0020 0.1400  273  GLU A OE1 
2055  O OE2 . GLU A 273  ? 2.5026 2.1302 1.5493 0.8550  0.1034  0.1155  273  GLU A OE2 
2056  N N   . ASP A 274  ? 2.2648 1.9373 1.2980 0.7361  -0.2062 0.0657  274  ASP A N   
2057  C CA  . ASP A 274  ? 2.2301 1.9418 1.2949 0.7027  -0.2756 0.0713  274  ASP A CA  
2058  C C   . ASP A 274  ? 2.2703 1.9514 1.3166 0.6868  -0.3208 0.0473  274  ASP A C   
2059  O O   . ASP A 274  ? 2.2714 1.9103 1.2943 0.6974  -0.2959 0.0249  274  ASP A O   
2060  C CB  . ASP A 274  ? 2.2863 2.0016 1.3094 0.7123  -0.3186 0.0933  274  ASP A CB  
2061  C CG  . ASP A 274  ? 2.7880 2.4292 1.6944 0.7507  -0.3319 0.0866  274  ASP A CG  
2062  O OD1 . ASP A 274  ? 2.8328 2.4611 1.6973 0.7484  -0.3978 0.0849  274  ASP A OD1 
2063  O OD2 . ASP A 274  ? 2.8339 2.4298 1.6907 0.7844  -0.2764 0.0831  274  ASP A OD2 
2064  N N   . LEU A 275  ? 2.2832 1.9858 1.3450 0.6611  -0.3860 0.0523  275  LEU A N   
2065  C CA  . LEU A 275  ? 2.3524 2.0219 1.3950 0.6465  -0.4325 0.0311  275  LEU A CA  
2066  C C   . LEU A 275  ? 2.5343 2.1564 1.4969 0.6587  -0.4902 0.0250  275  LEU A C   
2067  O O   . LEU A 275  ? 2.5547 2.1595 1.5145 0.6403  -0.5410 0.0109  275  LEU A O   
2068  C CB  . LEU A 275  ? 2.2234 1.9462 1.3528 0.6056  -0.4592 0.0350  275  LEU A CB  
2069  C CG  . LEU A 275  ? 2.1038 1.8631 1.3002 0.5970  -0.4073 0.0315  275  LEU A CG  
2070  C CD1 . LEU A 275  ? 2.0271 1.8426 1.3013 0.5610  -0.4344 0.0414  275  LEU A CD1 
2071  C CD2 . LEU A 275  ? 2.1090 1.8199 1.2780 0.6109  -0.3796 0.0036  275  LEU A CD2 
2072  N N   . LYS A 276  ? 2.6554 2.2571 1.5543 0.6904  -0.4830 0.0352  276  LYS A N   
2073  C CA  . LYS A 276  ? 2.8148 2.3610 1.6194 0.7126  -0.5297 0.0236  276  LYS A CA  
2074  C C   . LYS A 276  ? 3.0040 2.4822 1.7160 0.7570  -0.4816 0.0123  276  LYS A C   
2075  O O   . LYS A 276  ? 3.1377 2.5640 1.7548 0.7867  -0.5057 0.0040  276  LYS A O   
2076  C CB  . LYS A 276  ? 2.7574 2.3333 1.5545 0.7171  -0.5701 0.0444  276  LYS A CB  
2077  C CG  . LYS A 276  ? 2.7857 2.3102 1.4883 0.7397  -0.6281 0.0291  276  LYS A CG  
2078  C CD  . LYS A 276  ? 2.7181 2.2807 1.4270 0.7410  -0.6760 0.0478  276  LYS A CD  
2079  C CE  . LYS A 276  ? 2.6585 2.2298 1.3338 0.7774  -0.6310 0.0743  276  LYS A CE  
2080  N NZ  . LYS A 276  ? 2.7401 2.2430 1.2882 0.8281  -0.6293 0.0652  276  LYS A NZ  
2081  N N   . ASP A 277  ? 3.0493 2.5296 1.7924 0.7621  -0.4124 0.0118  277  ASP A N   
2082  C CA  . ASP A 277  ? 3.2166 2.6381 1.8910 0.8025  -0.3524 0.0043  277  ASP A CA  
2083  C C   . ASP A 277  ? 3.2737 2.6474 1.9305 0.8003  -0.3479 -0.0265 277  ASP A C   
2084  O O   . ASP A 277  ? 3.2225 2.6205 1.9523 0.7788  -0.3219 -0.0352 277  ASP A O   
2085  C CB  . ASP A 277  ? 3.2417 2.6976 1.9739 0.8091  -0.2756 0.0218  277  ASP A CB  
2086  C CG  . ASP A 277  ? 3.3976 2.7954 2.0734 0.8500  -0.2042 0.0168  277  ASP A CG  
2087  O OD1 . ASP A 277  ? 3.5318 2.8607 2.1109 0.8785  -0.2120 0.0035  277  ASP A OD1 
2088  O OD2 . ASP A 277  ? 3.3760 2.7973 2.1076 0.8538  -0.1379 0.0258  277  ASP A OD2 
2089  N N   . ASP A 278  ? 3.3852 2.6912 1.9440 0.8240  -0.3750 -0.0439 278  ASP A N   
2090  C CA  . ASP A 278  ? 3.4020 2.6543 1.9330 0.8268  -0.3706 -0.0737 278  ASP A CA  
2091  C C   . ASP A 278  ? 3.3485 2.5806 1.8905 0.8467  -0.2868 -0.0779 278  ASP A C   
2092  O O   . ASP A 278  ? 3.3473 2.5501 1.8960 0.8438  -0.2729 -0.1010 278  ASP A O   
2093  C CB  . ASP A 278  ? 3.9208 3.1007 2.3354 0.8532  -0.4139 -0.0925 278  ASP A CB  
2094  C CG  . ASP A 278  ? 3.9801 3.1292 2.2977 0.8987  -0.4011 -0.0773 278  ASP A CG  
2095  O OD1 . ASP A 278  ? 3.9418 3.1080 2.2713 0.9170  -0.3416 -0.0538 278  ASP A OD1 
2096  O OD2 . ASP A 278  ? 4.0600 3.1658 2.2873 0.9178  -0.4515 -0.0898 278  ASP A OD2 
2097  N N   . GLN A 279  ? 3.3005 2.5503 1.8520 0.8662  -0.2309 -0.0556 279  GLN A N   
2098  C CA  . GLN A 279  ? 3.2406 2.4666 1.8003 0.8898  -0.1465 -0.0583 279  GLN A CA  
2099  C C   . GLN A 279  ? 3.0308 2.3225 1.6979 0.8727  -0.0976 -0.0442 279  GLN A C   
2100  O O   . GLN A 279  ? 2.9398 2.2852 1.6467 0.8595  -0.1104 -0.0220 279  GLN A O   
2101  C CB  . GLN A 279  ? 3.4067 2.5708 1.8610 0.9412  -0.1074 -0.0472 279  GLN A CB  
2102  C CG  . GLN A 279  ? 3.4608 2.5927 1.9251 0.9667  -0.0160 -0.0507 279  GLN A CG  
2103  C CD  . GLN A 279  ? 3.5042 2.5986 1.9733 0.9622  -0.0071 -0.0830 279  GLN A CD  
2104  O OE1 . GLN A 279  ? 3.4391 2.5634 2.0012 0.9428  0.0279  -0.0945 279  GLN A OE1 
2105  N NE2 . GLN A 279  ? 3.6128 2.6418 1.9819 0.9814  -0.0403 -0.0991 279  GLN A NE2 
2106  N N   . LYS A 280  ? 2.9355 2.2206 1.6497 0.8750  -0.0393 -0.0592 280  LYS A N   
2107  C CA  . LYS A 280  ? 2.7769 2.1244 1.6013 0.8563  0.0038  -0.0548 280  LYS A CA  
2108  C C   . LYS A 280  ? 2.7794 2.0974 1.6275 0.8766  0.0824  -0.0700 280  LYS A C   
2109  O O   . LYS A 280  ? 2.8331 2.1124 1.6666 0.8807  0.0861  -0.0943 280  LYS A O   
2110  C CB  . LYS A 280  ? 2.6313 2.0390 1.5387 0.8114  -0.0447 -0.0653 280  LYS A CB  
2111  C CG  . LYS A 280  ? 2.5793 1.9589 1.4825 0.8005  -0.0716 -0.0939 280  LYS A CG  
2112  C CD  . LYS A 280  ? 2.5820 1.9427 1.4310 0.7870  -0.1521 -0.0961 280  LYS A CD  
2113  C CE  . LYS A 280  ? 2.5724 1.8992 1.4180 0.7794  -0.1709 -0.1247 280  LYS A CE  
2114  N NZ  . LYS A 280  ? 2.5953 1.9015 1.3996 0.7639  -0.2472 -0.1308 280  LYS A NZ  
2115  N N   . GLU A 281  ? 2.7246 2.0606 1.6138 0.8897  0.1469  -0.0555 281  GLU A N   
2116  C CA  . GLU A 281  ? 2.7463 2.0548 1.6658 0.9106  0.2282  -0.0676 281  GLU A CA  
2117  C C   . GLU A 281  ? 2.5894 1.9369 1.6134 0.8834  0.2374  -0.0971 281  GLU A C   
2118  O O   . GLU A 281  ? 2.4733 1.8854 1.5955 0.8621  0.2530  -0.0981 281  GLU A O   
2119  C CB  . GLU A 281  ? 2.8436 2.1682 1.7941 0.9275  0.2924  -0.0437 281  GLU A CB  
2120  C CG  . GLU A 281  ? 3.0479 2.3499 1.9062 0.9521  0.2766  -0.0100 281  GLU A CG  
2121  C CD  . GLU A 281  ? 3.3025 2.5214 2.0249 0.9877  0.2608  -0.0094 281  GLU A CD  
2122  O OE1 . GLU A 281  ? 3.3842 2.5562 2.0825 0.9966  0.2739  -0.0334 281  GLU A OE1 
2123  O OE2 . GLU A 281  ? 3.4085 2.6092 2.0468 1.0083  0.2341  0.0143  281  GLU A OE2 
2124  N N   . MET A 282  ? 2.6150 1.9235 1.6178 0.8860  0.2283  -0.1223 282  MET A N   
2125  C CA  . MET A 282  ? 2.5532 1.8960 1.6523 0.8648  0.2376  -0.1513 282  MET A CA  
2126  C C   . MET A 282  ? 2.5355 1.9018 1.7245 0.8723  0.3170  -0.1575 282  MET A C   
2127  O O   . MET A 282  ? 2.5596 1.9206 1.7420 0.8900  0.3626  -0.1366 282  MET A O   
2128  C CB  . MET A 282  ? 2.6053 1.8916 1.6638 0.8752  0.2308  -0.1759 282  MET A CB  
2129  C CG  . MET A 282  ? 2.6354 1.9026 1.6261 0.8622  0.1498  -0.1781 282  MET A CG  
2130  S SD  . MET A 282  ? 2.6183 1.9697 1.6867 0.8144  0.0794  -0.1777 282  MET A SD  
2131  C CE  . MET A 282  ? 2.0589 1.4352 1.0890 0.8112  0.0521  -0.1413 282  MET A CE  
2132  N N   . MET A 283  ? 2.5314 1.9241 1.8083 0.8595  0.3336  -0.1873 283  MET A N   
2133  C CA  . MET A 283  ? 2.5689 1.9929 1.9483 0.8622  0.4037  -0.1987 283  MET A CA  
2134  C C   . MET A 283  ? 2.6981 2.1126 2.1363 0.8642  0.4295  -0.2350 283  MET A C   
2135  O O   . MET A 283  ? 2.6770 2.1151 2.1382 0.8444  0.3802  -0.2548 283  MET A O   
2136  C CB  . MET A 283  ? 2.4584 1.9700 1.9282 0.8319  0.3849  -0.1972 283  MET A CB  
2137  C CG  . MET A 283  ? 2.6220 2.1551 2.0519 0.8264  0.3587  -0.1616 283  MET A CG  
2138  S SD  . MET A 283  ? 1.7361 1.3725 1.2627 0.7876  0.3222  -0.1612 283  MET A SD  
2139  C CE  . MET A 283  ? 1.6616 1.3159 1.1794 0.7614  0.2403  -0.1780 283  MET A CE  
2140  N N   . GLN A 284  ? 2.8382 2.2180 2.3034 0.8891  0.5083  -0.2425 284  GLN A N   
2141  C CA  . GLN A 284  ? 2.9244 2.2977 2.4606 0.8932  0.5435  -0.2777 284  GLN A CA  
2142  C C   . GLN A 284  ? 2.8872 2.3433 2.5452 0.8630  0.5212  -0.3064 284  GLN A C   
2143  O O   . GLN A 284  ? 2.8420 2.3598 2.5311 0.8399  0.4860  -0.2981 284  GLN A O   
2144  C CB  . GLN A 284  ? 2.9740 2.3135 2.5476 0.9207  0.6401  -0.2779 284  GLN A CB  
2145  C CG  . GLN A 284  ? 2.9097 2.3037 2.5755 0.9120  0.6811  -0.2722 284  GLN A CG  
2146  C CD  . GLN A 284  ? 2.9241 2.3120 2.5155 0.9179  0.6719  -0.2308 284  GLN A CD  
2147  O OE1 . GLN A 284  ? 2.8993 2.3123 2.4407 0.9002  0.6008  -0.2163 284  GLN A OE1 
2148  N NE2 . GLN A 284  ? 2.9684 2.3228 2.5559 0.9437  0.7457  -0.2109 284  GLN A NE2 
2149  N N   . THR A 285  ? 2.9032 2.3610 2.6309 0.8652  0.5432  -0.3408 285  THR A N   
2150  C CA  . THR A 285  ? 2.8433 2.3791 2.6898 0.8419  0.5267  -0.3720 285  THR A CA  
2151  C C   . THR A 285  ? 2.7791 2.3641 2.6000 0.8144  0.4420  -0.3617 285  THR A C   
2152  O O   . THR A 285  ? 2.6985 2.3516 2.5797 0.7952  0.4279  -0.3622 285  THR A O   
2153  C CB  . THR A 285  ? 2.8364 2.4177 2.7887 0.8344  0.5843  -0.3765 285  THR A CB  
2154  O OG1 . THR A 285  ? 2.9133 2.4360 2.8494 0.8530  0.6580  -0.3592 285  THR A OG1 
2155  C CG2 . THR A 285  ? 2.7940 2.4403 2.8726 0.8075  0.5790  -0.4112 285  THR A CG2 
2156  N N   . ALA A 286  ? 2.8057 2.3512 2.5329 0.8141  0.3885  -0.3508 286  ALA A N   
2157  C CA  . ALA A 286  ? 2.7356 2.3191 2.4436 0.7893  0.3086  -0.3449 286  ALA A CA  
2158  C C   . ALA A 286  ? 2.6799 2.2783 2.4350 0.7838  0.2832  -0.3766 286  ALA A C   
2159  O O   . ALA A 286  ? 2.6961 2.2391 2.4034 0.7961  0.2766  -0.3841 286  ALA A O   
2160  C CB  . ALA A 286  ? 2.7924 2.3249 2.3779 0.7912  0.2640  -0.3153 286  ALA A CB  
2161  N N   . MET A 287  ? 2.6064 2.2801 2.4536 0.7671  0.2686  -0.3954 287  MET A N   
2162  C CA  . MET A 287  ? 2.5503 2.2502 2.4605 0.7648  0.2507  -0.4287 287  MET A CA  
2163  C C   . MET A 287  ? 2.6062 2.2522 2.4516 0.7712  0.2162  -0.4302 287  MET A C   
2164  O O   . MET A 287  ? 2.6278 2.2433 2.3849 0.7645  0.1702  -0.4052 287  MET A O   
2165  C CB  . MET A 287  ? 2.4422 2.2240 2.4069 0.7430  0.2041  -0.4341 287  MET A CB  
2166  C CG  . MET A 287  ? 2.3592 2.2067 2.4309 0.7398  0.2407  -0.4566 287  MET A CG  
2167  S SD  . MET A 287  ? 2.7985 2.7369 2.9122 0.7172  0.1814  -0.4592 287  MET A SD  
2168  C CE  . MET A 287  ? 2.3365 2.2652 2.3609 0.7025  0.1546  -0.4083 287  MET A CE  
2169  N N   . GLN A 288  ? 2.6498 2.2857 2.5470 0.7841  0.2394  -0.4618 288  GLN A N   
2170  C CA  . GLN A 288  ? 2.7493 2.3390 2.6026 0.7914  0.2103  -0.4692 288  GLN A CA  
2171  C C   . GLN A 288  ? 2.7130 2.3573 2.6367 0.7831  0.1718  -0.4938 288  GLN A C   
2172  O O   . GLN A 288  ? 2.6473 2.3561 2.6690 0.7801  0.1861  -0.5174 288  GLN A O   
2173  C CB  . GLN A 288  ? 2.8787 2.4001 2.7213 0.8176  0.2692  -0.4831 288  GLN A CB  
2174  C CG  . GLN A 288  ? 2.9259 2.4737 2.8783 0.8286  0.3386  -0.5113 288  GLN A CG  
2175  C CD  . GLN A 288  ? 3.0664 2.5409 3.0021 0.8558  0.4056  -0.5183 288  GLN A CD  
2176  O OE1 . GLN A 288  ? 3.1525 2.5627 3.0147 0.8685  0.3957  -0.5153 288  GLN A OE1 
2177  N NE2 . GLN A 288  ? 3.0916 2.5815 3.0949 0.8534  0.4692  -0.5186 288  GLN A NE2 
2178  N N   . ASN A 289  ? 2.7714 2.3889 2.6427 0.7806  0.1213  -0.4881 289  ASN A N   
2179  C CA  . ASN A 289  ? 2.7734 2.4286 2.6986 0.7788  0.0857  -0.5094 289  ASN A CA  
2180  C C   . ASN A 289  ? 2.6339 2.3808 2.6426 0.7669  0.0698  -0.5208 289  ASN A C   
2181  O O   . ASN A 289  ? 2.5580 2.3457 2.6536 0.7722  0.1099  -0.5467 289  ASN A O   
2182  C CB  . ASN A 289  ? 2.8907 2.5204 2.8665 0.8001  0.1235  -0.5433 289  ASN A CB  
2183  C CG  . ASN A 289  ? 3.0353 2.5735 2.9365 0.8168  0.1568  -0.5364 289  ASN A CG  
2184  O OD1 . ASN A 289  ? 3.1045 2.5953 2.9071 0.8130  0.1403  -0.5078 289  ASN A OD1 
2185  N ND2 . ASN A 289  ? 3.0732 2.5868 3.0220 0.8367  0.2041  -0.5639 289  ASN A ND2 
2186  N N   . THR A 290  ? 2.5834 2.3608 2.5653 0.7515  0.0116  -0.5018 290  THR A N   
2187  C CA  . THR A 290  ? 2.5005 2.3555 2.5527 0.7473  -0.0167 -0.5181 290  THR A CA  
2188  C C   . THR A 290  ? 2.4762 2.3080 2.4817 0.7469  -0.0704 -0.5066 290  THR A C   
2189  O O   . THR A 290  ? 2.4849 2.3441 2.4654 0.7340  -0.1173 -0.4844 290  THR A O   
2190  C CB  . THR A 290  ? 2.0608 1.9797 2.1273 0.7302  -0.0293 -0.5023 290  THR A CB  
2191  O OG1 . THR A 290  ? 2.0270 1.9835 2.1711 0.7341  0.0209  -0.5268 290  THR A OG1 
2192  C CG2 . THR A 290  ? 2.0128 1.9935 2.1044 0.7252  -0.0802 -0.5042 290  THR A CG2 
2193  N N   . MET A 291  ? 2.4392 2.2149 2.4320 0.7619  -0.0590 -0.5204 291  MET A N   
2194  C CA  . MET A 291  ? 2.4227 2.1613 2.3690 0.7641  -0.1027 -0.5110 291  MET A CA  
2195  C C   . MET A 291  ? 2.3219 2.1032 2.2536 0.7495  -0.1597 -0.4876 291  MET A C   
2196  O O   . MET A 291  ? 2.2724 2.1234 2.2646 0.7512  -0.1731 -0.5002 291  MET A O   
2197  C CB  . MET A 291  ? 2.4540 2.1934 2.4598 0.7843  -0.0945 -0.5457 291  MET A CB  
2198  C CG  . MET A 291  ? 2.4981 2.2029 2.5386 0.8014  -0.0336 -0.5733 291  MET A CG  
2199  S SD  . MET A 291  ? 2.7997 2.5153 2.9180 0.8238  -0.0347 -0.6127 291  MET A SD  
2200  C CE  . MET A 291  ? 2.6843 2.5070 2.8818 0.8197  -0.0736 -0.6262 291  MET A CE  
2201  N N   . LEU A 292  ? 2.2947 2.0336 2.1466 0.7364  -0.1924 -0.4542 292  LEU A N   
2202  C CA  . LEU A 292  ? 2.2085 1.9763 2.0430 0.7234  -0.2446 -0.4282 292  LEU A CA  
2203  C C   . LEU A 292  ? 2.1268 1.9228 2.0082 0.7384  -0.2651 -0.4469 292  LEU A C   
2204  O O   . LEU A 292  ? 2.1511 1.9154 2.0489 0.7554  -0.2520 -0.4706 292  LEU A O   
2205  C CB  . LEU A 292  ? 2.2590 1.9610 2.0101 0.7115  -0.2755 -0.3980 292  LEU A CB  
2206  C CG  . LEU A 292  ? 2.2402 1.9620 1.9621 0.6912  -0.3210 -0.3611 292  LEU A CG  
2207  C CD1 . LEU A 292  ? 2.2175 1.9751 1.9688 0.6964  -0.3545 -0.3580 292  LEU A CD1 
2208  C CD2 . LEU A 292  ? 2.1830 1.9554 1.9159 0.6769  -0.3106 -0.3467 292  LEU A CD2 
2209  N N   . ILE A 293  ? 2.0219 1.8773 1.9234 0.7343  -0.2970 -0.4355 293  ILE A N   
2210  C CA  . ILE A 293  ? 1.9395 1.8298 1.8863 0.7522  -0.3173 -0.4536 293  ILE A CA  
2211  C C   . ILE A 293  ? 1.8948 1.8154 1.8187 0.7456  -0.3632 -0.4221 293  ILE A C   
2212  O O   . ILE A 293  ? 1.8560 1.8323 1.7908 0.7369  -0.3690 -0.4109 293  ILE A O   
2213  C CB  . ILE A 293  ? 1.8715 1.8275 1.9038 0.7655  -0.2897 -0.4935 293  ILE A CB  
2214  C CG1 . ILE A 293  ? 1.8569 1.7773 1.9254 0.7808  -0.2495 -0.5288 293  ILE A CG1 
2215  C CG2 . ILE A 293  ? 1.8484 1.8696 1.9210 0.7794  -0.3233 -0.5029 293  ILE A CG2 
2216  C CD1 . ILE A 293  ? 1.7988 1.7787 1.9623 0.7924  -0.2166 -0.5716 293  ILE A CD1 
2217  N N   . ASN A 294  ? 1.9119 1.7916 1.8027 0.7501  -0.3936 -0.4061 294  ASN A N   
2218  C CA  . ASN A 294  ? 1.9127 1.8094 1.7775 0.7451  -0.4346 -0.3712 294  ASN A CA  
2219  C C   . ASN A 294  ? 1.8356 1.7266 1.6545 0.7181  -0.4452 -0.3313 294  ASN A C   
2220  O O   . ASN A 294  ? 1.8006 1.7307 1.6145 0.7129  -0.4681 -0.3049 294  ASN A O   
2221  C CB  . ASN A 294  ? 1.9535 1.9298 1.8667 0.7624  -0.4472 -0.3837 294  ASN A CB  
2222  C CG  . ASN A 294  ? 2.0389 2.0240 1.9240 0.7659  -0.4875 -0.3489 294  ASN A CG  
2223  O OD1 . ASN A 294  ? 2.0441 2.0664 1.9151 0.7554  -0.4992 -0.3222 294  ASN A OD1 
2224  N ND2 . ASN A 294  ? 2.0953 2.0429 1.9714 0.7813  -0.5066 -0.3467 294  ASN A ND2 
2225  N N   . GLY A 295  ? 1.8140 1.6552 1.5989 0.7028  -0.4283 -0.3270 295  GLY A N   
2226  C CA  . GLY A 295  ? 1.7909 1.6144 1.5304 0.6778  -0.4427 -0.2903 295  GLY A CA  
2227  C C   . GLY A 295  ? 1.7258 1.5915 1.4772 0.6659  -0.4198 -0.2888 295  GLY A C   
2228  O O   . GLY A 295  ? 1.7066 1.5686 1.4285 0.6454  -0.4302 -0.2592 295  GLY A O   
2229  N N   . ILE A 296  ? 1.6744 1.5809 1.4747 0.6789  -0.3883 -0.3218 296  ILE A N   
2230  C CA  . ILE A 296  ? 1.5908 1.5390 1.4118 0.6703  -0.3607 -0.3251 296  ILE A CA  
2231  C C   . ILE A 296  ? 1.6208 1.5711 1.4828 0.6832  -0.3149 -0.3641 296  ILE A C   
2232  O O   . ILE A 296  ? 1.6351 1.5825 1.5324 0.7018  -0.3049 -0.3950 296  ILE A O   
2233  C CB  . ILE A 296  ? 1.4219 1.4510 1.2777 0.6693  -0.3716 -0.3186 296  ILE A CB  
2234  C CG1 . ILE A 296  ? 1.4023 1.4338 1.2271 0.6626  -0.4136 -0.2817 296  ILE A CG1 
2235  C CG2 . ILE A 296  ? 1.3245 1.3847 1.1879 0.6549  -0.3483 -0.3112 296  ILE A CG2 
2236  C CD1 . ILE A 296  ? 1.3795 1.4211 1.1778 0.6396  -0.4220 -0.2443 296  ILE A CD1 
2237  N N   . ALA A 297  ? 1.6113 1.5639 1.4694 0.6732  -0.2859 -0.3602 297  ALA A N   
2238  C CA  . ALA A 297  ? 1.5768 1.5477 1.4848 0.6826  -0.2375 -0.3917 297  ALA A CA  
2239  C C   . ALA A 297  ? 1.5775 1.5800 1.4847 0.6676  -0.2227 -0.3742 297  ALA A C   
2240  O O   . ALA A 297  ? 1.6006 1.5980 1.4624 0.6511  -0.2481 -0.3389 297  ALA A O   
2241  C CB  . ALA A 297  ? 1.5967 1.4988 1.4834 0.6925  -0.2065 -0.4057 297  ALA A CB  
2242  N N   . GLN A 298  ? 1.5523 1.5883 1.5156 0.6735  -0.1808 -0.3993 298  GLN A N   
2243  C CA  . GLN A 298  ? 1.5251 1.6008 1.5017 0.6617  -0.1638 -0.3871 298  GLN A CA  
2244  C C   . GLN A 298  ? 1.4834 1.5550 1.5044 0.6707  -0.1059 -0.4133 298  GLN A C   
2245  O O   . GLN A 298  ? 1.4867 1.5526 1.5533 0.6860  -0.0824 -0.4474 298  GLN A O   
2246  C CB  . GLN A 298  ? 1.5222 1.6775 1.5438 0.6593  -0.1838 -0.3924 298  GLN A CB  
2247  C CG  . GLN A 298  ? 1.5959 1.7652 1.5714 0.6441  -0.2274 -0.3519 298  GLN A CG  
2248  C CD  . GLN A 298  ? 1.6318 1.8723 1.6393 0.6366  -0.2249 -0.3467 298  GLN A CD  
2249  O OE1 . GLN A 298  ? 1.6394 1.9167 1.7019 0.6412  -0.1907 -0.3735 298  GLN A OE1 
2250  N NE2 . GLN A 298  ? 1.6486 1.9067 1.6236 0.6250  -0.2589 -0.3122 298  GLN A NE2 
2251  N N   . VAL A 299  ? 1.4603 1.5326 1.4702 0.6621  -0.0811 -0.3962 299  VAL A N   
2252  C CA  . VAL A 299  ? 1.4662 1.5493 1.5320 0.6699  -0.0238 -0.4194 299  VAL A CA  
2253  C C   . VAL A 299  ? 1.4897 1.6020 1.5499 0.6565  -0.0161 -0.3952 299  VAL A C   
2254  O O   . VAL A 299  ? 1.5726 1.6675 1.5685 0.6443  -0.0453 -0.3583 299  VAL A O   
2255  C CB  . VAL A 299  ? 1.5095 1.5197 1.5430 0.6814  0.0148  -0.4199 299  VAL A CB  
2256  C CG1 . VAL A 299  ? 1.5228 1.5115 1.5899 0.6980  0.0272  -0.4538 299  VAL A CG1 
2257  C CG2 . VAL A 299  ? 1.5632 1.5147 1.4960 0.6745  -0.0128 -0.3811 299  VAL A CG2 
2258  N N   . THR A 300  ? 1.4378 1.5962 1.5704 0.6585  0.0221  -0.4170 300  THR A N   
2259  C CA  . THR A 300  ? 1.4086 1.5916 1.5422 0.6479  0.0387  -0.3957 300  THR A CA  
2260  C C   . THR A 300  ? 1.4891 1.6238 1.6150 0.6566  0.0940  -0.3914 300  THR A C   
2261  O O   . THR A 300  ? 1.4817 1.5855 1.6348 0.6714  0.1306  -0.4163 300  THR A O   
2262  C CB  . THR A 300  ? 1.8331 2.0991 2.0457 0.6435  0.0432  -0.4182 300  THR A CB  
2263  O OG1 . THR A 300  ? 1.8262 2.1168 2.1208 0.6563  0.0667  -0.4671 300  THR A OG1 
2264  C CG2 . THR A 300  ? 1.8097 2.1179 2.0004 0.6338  -0.0131 -0.4035 300  THR A CG2 
2265  N N   . PHE A 301  ? 1.5668 1.6935 1.6544 0.6493  0.1009  -0.3581 301  PHE A N   
2266  C CA  . PHE A 301  ? 1.7074 1.7774 1.7625 0.6605  0.1456  -0.3446 301  PHE A CA  
2267  C C   . PHE A 301  ? 1.7889 1.8922 1.8939 0.6592  0.1906  -0.3418 301  PHE A C   
2268  O O   . PHE A 301  ? 1.8232 1.9532 1.9104 0.6472  0.1737  -0.3149 301  PHE A O   
2269  C CB  . PHE A 301  ? 1.7147 1.7325 1.6651 0.6568  0.1087  -0.3053 301  PHE A CB  
2270  C CG  . PHE A 301  ? 1.7015 1.6658 1.6011 0.6689  0.1445  -0.2833 301  PHE A CG  
2271  C CD1 . PHE A 301  ? 1.7128 1.6267 1.6121 0.6898  0.1951  -0.2979 301  PHE A CD1 
2272  C CD2 . PHE A 301  ? 1.6909 1.6540 1.5395 0.6610  0.1259  -0.2461 301  PHE A CD2 
2273  C CE1 . PHE A 301  ? 1.7499 1.6124 1.5935 0.7047  0.2280  -0.2747 301  PHE A CE1 
2274  C CE2 . PHE A 301  ? 1.7114 1.6262 1.5076 0.6754  0.1552  -0.2247 301  PHE A CE2 
2275  C CZ  . PHE A 301  ? 1.7543 1.6178 1.5444 0.6982  0.2065  -0.2383 301  PHE A CZ  
2276  N N   . ASP A 302  ? 1.8235 1.9272 1.9991 0.6715  0.2492  -0.3712 302  ASP A N   
2277  C CA  . ASP A 302  ? 1.8251 1.9537 2.0557 0.6723  0.3001  -0.3713 302  ASP A CA  
2278  C C   . ASP A 302  ? 1.8452 1.9147 2.0032 0.6820  0.3264  -0.3322 302  ASP A C   
2279  O O   . ASP A 302  ? 1.8612 1.8730 2.0022 0.7005  0.3693  -0.3334 302  ASP A O   
2280  C CB  . ASP A 302  ? 1.8779 2.0226 2.2142 0.6823  0.3559  -0.4168 302  ASP A CB  
2281  C CG  . ASP A 302  ? 1.9409 2.1200 2.3458 0.6710  0.3997  -0.4172 302  ASP A CG  
2282  O OD1 . ASP A 302  ? 1.9583 2.1710 2.4547 0.6556  0.4182  -0.4498 302  ASP A OD1 
2283  O OD2 . ASP A 302  ? 1.9708 2.1422 2.3402 0.6740  0.4133  -0.3846 302  ASP A OD2 
2284  N N   . SER A 303  ? 1.8406 1.9247 1.9539 0.6712  0.2992  -0.2970 303  SER A N   
2285  C CA  . SER A 303  ? 1.8720 1.9064 1.9099 0.6809  0.3124  -0.2578 303  SER A CA  
2286  C C   . SER A 303  ? 1.8904 1.9115 1.9704 0.6966  0.3881  -0.2574 303  SER A C   
2287  O O   . SER A 303  ? 1.9546 1.9161 1.9760 0.7154  0.4177  -0.2344 303  SER A O   
2288  C CB  . SER A 303  ? 1.8236 1.8872 1.8198 0.6641  0.2631  -0.2234 303  SER A CB  
2289  O OG  . SER A 303  ? 1.7689 1.8477 1.7384 0.6490  0.1985  -0.2239 303  SER A OG  
2290  N N   . GLU A 304  ? 1.8063 1.8818 1.9877 0.6903  0.4200  -0.2833 304  GLU A N   
2291  C CA  . GLU A 304  ? 1.7619 1.8297 1.9967 0.7029  0.4937  -0.2836 304  GLU A CA  
2292  C C   . GLU A 304  ? 1.7623 1.7644 1.9917 0.7217  0.5453  -0.2910 304  GLU A C   
2293  O O   . GLU A 304  ? 1.7639 1.7111 1.9423 0.7425  0.5848  -0.2631 304  GLU A O   
2294  C CB  . GLU A 304  ? 1.7273 1.8622 2.0737 0.6799  0.5064  -0.3132 304  GLU A CB  
2295  C CG  . GLU A 304  ? 1.7559 1.8938 2.1455 0.6730  0.5581  -0.2966 304  GLU A CG  
2296  C CD  . GLU A 304  ? 1.7442 1.9342 2.2453 0.6456  0.5705  -0.3316 304  GLU A CD  
2297  O OE1 . GLU A 304  ? 1.7436 1.9566 2.2863 0.6364  0.5476  -0.3696 304  GLU A OE1 
2298  O OE2 . GLU A 304  ? 1.7339 1.9409 2.2806 0.6352  0.6017  -0.3232 304  GLU A OE2 
2299  N N   . THR A 305  ? 1.7512 1.7604 2.0321 0.7111  0.5418  -0.3256 305  THR A N   
2300  C CA  . THR A 305  ? 1.8303 1.7794 2.1039 0.7233  0.5786  -0.3331 305  THR A CA  
2301  C C   . THR A 305  ? 1.9032 1.7814 2.0562 0.7545  0.5732  -0.3064 305  THR A C   
2302  O O   . THR A 305  ? 1.9199 1.7414 2.0292 0.7749  0.6212  -0.2813 305  THR A O   
2303  C CB  . THR A 305  ? 1.7862 1.7584 2.1028 0.7130  0.5458  -0.3728 305  THR A CB  
2304  O OG1 . THR A 305  ? 1.7373 1.7791 2.1643 0.6867  0.5437  -0.4042 305  THR A OG1 
2305  C CG2 . THR A 305  ? 1.8428 1.7542 2.1544 0.7257  0.5823  -0.3817 305  THR A CG2 
2306  N N   . ALA A 306  ? 1.9788 1.8600 2.0724 0.7495  0.5057  -0.3062 306  ALA A N   
2307  C CA  . ALA A 306  ? 2.1573 1.9714 2.1358 0.7614  0.4780  -0.2840 306  ALA A CA  
2308  C C   . ALA A 306  ? 2.3003 2.0720 2.1805 0.7736  0.4780  -0.2388 306  ALA A C   
2309  O O   . ALA A 306  ? 2.3597 2.0914 2.1410 0.7771  0.4333  -0.2199 306  ALA A O   
2310  C CB  . ALA A 306  ? 2.1116 1.9473 2.0603 0.7428  0.3995  -0.2903 306  ALA A CB  
2311  N N   . VAL A 307  ? 2.4659 2.2454 2.3735 0.7812  0.5266  -0.2223 307  VAL A N   
2312  C CA  . VAL A 307  ? 2.6868 2.4284 2.5030 0.7961  0.5274  -0.1788 307  VAL A CA  
2313  C C   . VAL A 307  ? 2.9498 2.6617 2.7932 0.8209  0.6137  -0.1689 307  VAL A C   
2314  O O   . VAL A 307  ? 2.9981 2.6437 2.7586 0.8493  0.6412  -0.1432 307  VAL A O   
2315  C CB  . VAL A 307  ? 1.8794 1.6765 1.6891 0.7742  0.4759  -0.1553 307  VAL A CB  
2316  C CG1 . VAL A 307  ? 1.9234 1.6904 1.6649 0.7921  0.4904  -0.1135 307  VAL A CG1 
2317  C CG2 . VAL A 307  ? 1.8676 1.6777 1.6273 0.7543  0.3917  -0.1541 307  VAL A CG2 
2318  N N   . LYS A 308  ? 3.1095 2.8696 3.0704 0.8115  0.6571  -0.1907 308  LYS A N   
2319  C CA  . LYS A 308  ? 3.3673 3.1086 3.3704 0.8289  0.7385  -0.1787 308  LYS A CA  
2320  C C   . LYS A 308  ? 3.6814 3.3348 3.6139 0.8639  0.7891  -0.1631 308  LYS A C   
2321  O O   . LYS A 308  ? 3.7697 3.3758 3.5931 0.8866  0.7822  -0.1269 308  LYS A O   
2322  C CB  . LYS A 308  ? 3.3125 3.1014 3.4507 0.7931  0.7665  -0.2036 308  LYS A CB  
2323  C CG  . LYS A 308  ? 3.2026 3.0732 3.4075 0.7638  0.7335  -0.2113 308  LYS A CG  
2324  C CD  . LYS A 308  ? 3.1518 3.0566 3.4848 0.7347  0.7740  -0.2333 308  LYS A CD  
2325  C CE  . LYS A 308  ? 3.1242 3.0345 3.5245 0.7191  0.7746  -0.2753 308  LYS A CE  
2326  N NZ  . LYS A 308  ? 3.0891 3.0323 3.6200 0.6920  0.8126  -0.3027 308  LYS A NZ  
2327  N N   . GLU A 309  ? 3.8642 3.4945 3.8497 0.8568  0.8284  -0.1817 309  GLU A N   
2328  C CA  . GLU A 309  ? 4.0892 3.6351 4.0151 0.8904  0.8860  -0.1656 309  GLU A CA  
2329  C C   . GLU A 309  ? 4.0273 3.5218 3.8225 0.9215  0.8456  -0.1635 309  GLU A C   
2330  O O   . GLU A 309  ? 4.2645 3.6836 3.9778 0.9561  0.8830  -0.1459 309  GLU A O   
2331  C CB  . GLU A 309  ? 4.3599 3.8963 4.3791 0.8743  0.9323  -0.1901 309  GLU A CB  
2332  C CG  . GLU A 309  ? 4.7507 4.1984 4.7124 0.9091  0.9949  -0.1752 309  GLU A CG  
2333  C CD  . GLU A 309  ? 5.0053 4.4069 4.9517 0.9347  1.0731  -0.1358 309  GLU A CD  
2334  O OE1 . GLU A 309  ? 5.0458 4.4872 5.0620 0.9175  1.0909  -0.1261 309  GLU A OE1 
2335  O OE2 . GLU A 309  ? 5.1710 4.4940 5.0335 0.9742  1.1187  -0.1145 309  GLU A OE2 
2336  N N   . LEU A 310  ? 3.7931 3.3261 3.5620 0.8971  0.7599  -0.1720 310  LEU A N   
2337  C CA  . LEU A 310  ? 3.7006 3.1877 3.3509 0.9041  0.7032  -0.1638 310  LEU A CA  
2338  C C   . LEU A 310  ? 3.5298 2.9994 3.0666 0.9117  0.6592  -0.1227 310  LEU A C   
2339  O O   . LEU A 310  ? 3.5346 2.9736 2.9746 0.9139  0.6017  -0.1163 310  LEU A O   
2340  C CB  . LEU A 310  ? 3.6867 3.2157 3.3700 0.8743  0.6360  -0.1958 310  LEU A CB  
2341  C CG  . LEU A 310  ? 3.6317 3.2017 3.4455 0.8611  0.6649  -0.2399 310  LEU A CG  
2342  C CD1 . LEU A 310  ? 3.5987 3.1831 3.4117 0.8441  0.6025  -0.2673 310  LEU A CD1 
2343  C CD2 . LEU A 310  ? 3.6823 3.2065 3.5365 0.8818  0.7517  -0.2467 310  LEU A CD2 
2344  N N   . SER A 311  ? 3.3463 2.8356 2.8991 0.9163  0.6863  -0.0964 311  SER A N   
2345  C CA  . SER A 311  ? 3.2250 2.6983 2.6767 0.9279  0.6516  -0.0562 311  SER A CA  
2346  C C   . SER A 311  ? 3.1286 2.6296 2.6272 0.9332  0.6969  -0.0313 311  SER A C   
2347  O O   . SER A 311  ? 3.0578 2.5895 2.6672 0.9259  0.7527  -0.0475 311  SER A O   
2348  C CB  . SER A 311  ? 3.1129 2.6262 2.5320 0.8982  0.5534  -0.0564 311  SER A CB  
2349  O OG  . SER A 311  ? 3.1100 2.5780 2.4458 0.9028  0.5080  -0.0661 311  SER A OG  
2350  N N   . TYR A 312  ? 3.1228 2.6132 2.5407 0.9465  0.6727  0.0066  312  TYR A N   
2351  C CA  . TYR A 312  ? 3.0945 2.6137 2.5528 0.9511  0.7083  0.0334  312  TYR A CA  
2352  C C   . TYR A 312  ? 2.4491 2.0588 2.0223 0.9104  0.6851  0.0174  312  TYR A C   
2353  O O   . TYR A 312  ? 2.4054 2.0468 2.0233 0.9099  0.7112  0.0363  312  TYR A O   
2354  C CB  . TYR A 312  ? 3.1703 2.6649 2.5152 0.9731  0.6743  0.0764  312  TYR A CB  
2355  C CG  . TYR A 312  ? 3.2996 2.7171 2.5592 1.0236  0.7348  0.1072  312  TYR A CG  
2356  C CD1 . TYR A 312  ? 3.4029 2.7661 2.5223 1.0521  0.6959  0.1288  312  TYR A CD1 
2357  C CD2 . TYR A 312  ? 3.3228 2.7212 2.6416 1.0444  0.8310  0.1148  312  TYR A CD2 
2358  C CE1 . TYR A 312  ? 3.5136 2.8051 2.5458 1.1025  0.7507  0.1584  312  TYR A CE1 
2359  C CE2 . TYR A 312  ? 3.4284 2.7533 2.6651 1.0937  0.8900  0.1469  312  TYR A CE2 
2360  C CZ  . TYR A 312  ? 3.5202 2.7918 2.6096 1.1237  0.8491  0.1692  312  TYR A CZ  
2361  O OH  . TYR A 312  ? 3.6274 2.8247 2.6263 1.1765  0.9068  0.2019  312  TYR A OH  
2362  N N   . TYR A 313  ? 2.3779 2.0273 1.9952 0.8788  0.6372  -0.0163 313  TYR A N   
2363  C CA  . TYR A 313  ? 2.2330 1.9663 1.9381 0.8418  0.6023  -0.0303 313  TYR A CA  
2364  C C   . TYR A 313  ? 2.2144 1.9927 2.0535 0.8261  0.6481  -0.0684 313  TYR A C   
2365  O O   . TYR A 313  ? 2.2062 1.9963 2.0854 0.8128  0.6347  -0.1045 313  TYR A O   
2366  C CB  . TYR A 313  ? 2.0945 1.8513 1.7615 0.8165  0.5128  -0.0385 313  TYR A CB  
2367  C CG  . TYR A 313  ? 2.0596 1.7719 1.6024 0.8293  0.4610  -0.0109 313  TYR A CG  
2368  C CD1 . TYR A 313  ? 2.0791 1.7447 1.5542 0.8348  0.4297  -0.0237 313  TYR A CD1 
2369  C CD2 . TYR A 313  ? 2.0433 1.7619 1.5396 0.8358  0.4409  0.0258  313  TYR A CD2 
2370  C CE1 . TYR A 313  ? 2.1355 1.7597 1.4977 0.8467  0.3791  -0.0030 313  TYR A CE1 
2371  C CE2 . TYR A 313  ? 2.0942 1.7747 1.4793 0.8480  0.3880  0.0472  313  TYR A CE2 
2372  C CZ  . TYR A 313  ? 2.1342 1.7668 1.4517 0.8532  0.3567  0.0315  313  TYR A CZ  
2373  O OH  . TYR A 313  ? 2.1848 1.7786 1.3935 0.8657  0.3025  0.0481  313  TYR A OH  
2374  N N   . SER A 314  ? 2.1946 2.0006 2.1039 0.8276  0.6982  -0.0607 314  SER A N   
2375  C CA  . SER A 314  ? 2.1264 1.9724 2.1677 0.8165  0.7503  -0.0963 314  SER A CA  
2376  C C   . SER A 314  ? 1.9582 1.8887 2.0772 0.7861  0.7206  -0.1075 314  SER A C   
2377  O O   . SER A 314  ? 1.8770 1.8512 2.0856 0.7572  0.7167  -0.1416 314  SER A O   
2378  C CB  . SER A 314  ? 2.2410 2.0444 2.3066 0.8378  0.8367  -0.0768 314  SER A CB  
2379  O OG  . SER A 314  ? 2.3131 2.1033 2.3158 0.8601  0.8424  -0.0336 314  SER A OG  
2380  N N   . LEU A 315  ? 1.9115 1.8600 1.9886 0.7830  0.6918  -0.0718 315  LEU A N   
2381  C CA  . LEU A 315  ? 1.8158 1.8410 1.9460 0.7543  0.6519  -0.0784 315  LEU A CA  
2382  C C   . LEU A 315  ? 1.7087 1.7463 1.7648 0.7375  0.5634  -0.0692 315  LEU A C   
2383  O O   . LEU A 315  ? 1.7393 1.7311 1.6955 0.7504  0.5351  -0.0399 315  LEU A O   
2384  C CB  . LEU A 315  ? 1.8963 1.9387 2.0403 0.7602  0.6787  -0.0453 315  LEU A CB  
2385  C CG  . LEU A 315  ? 1.9547 2.0078 2.1946 0.7635  0.7559  -0.0509 315  LEU A CG  
2386  C CD1 . LEU A 315  ? 1.9958 2.0173 2.1954 0.7930  0.7964  -0.0051 315  LEU A CD1 
2387  C CD2 . LEU A 315  ? 1.8693 1.9950 2.2030 0.7244  0.7383  -0.0729 315  LEU A CD2 
2388  N N   . GLU A 316  ? 1.5510 1.6481 1.6553 0.7103  0.5208  -0.0947 316  GLU A N   
2389  C CA  . GLU A 316  ? 1.4768 1.5904 1.5227 0.6925  0.4404  -0.0837 316  GLU A CA  
2390  C C   . GLU A 316  ? 1.4207 1.5447 1.4214 0.6910  0.4150  -0.0399 316  GLU A C   
2391  O O   . GLU A 316  ? 1.4173 1.5193 1.3373 0.6902  0.3630  -0.0162 316  GLU A O   
2392  C CB  . GLU A 316  ? 1.4445 1.6242 1.5572 0.6669  0.4087  -0.1155 316  GLU A CB  
2393  C CG  . GLU A 316  ? 1.5043 1.6978 1.5626 0.6489  0.3303  -0.1052 316  GLU A CG  
2394  C CD  . GLU A 316  ? 1.5467 1.7940 1.6110 0.6306  0.2945  -0.0802 316  GLU A CD  
2395  O OE1 . GLU A 316  ? 1.5362 1.8310 1.6683 0.6254  0.3232  -0.0852 316  GLU A OE1 
2396  O OE2 . GLU A 316  ? 1.5774 1.8200 1.5818 0.6208  0.2376  -0.0563 316  GLU A OE2 
2397  N N   . ASP A 317  ? 1.3705 1.5297 1.4303 0.6906  0.4523  -0.0318 317  ASP A N   
2398  C CA  . ASP A 317  ? 1.4078 1.5692 1.4363 0.6975  0.4508  0.0105  317  ASP A CA  
2399  C C   . ASP A 317  ? 1.5066 1.6066 1.4236 0.7157  0.4218  0.0405  317  ASP A C   
2400  O O   . ASP A 317  ? 1.4913 1.5989 1.3556 0.7042  0.3569  0.0579  317  ASP A O   
2401  C CB  . ASP A 317  ? 1.4290 1.5847 1.5159 0.7153  0.5311  0.0125  317  ASP A CB  
2402  C CG  . ASP A 317  ? 1.6010 1.7868 1.7001 0.7160  0.5377  0.0471  317  ASP A CG  
2403  O OD1 . ASP A 317  ? 1.6394 1.8291 1.6773 0.7134  0.4872  0.0800  317  ASP A OD1 
2404  O OD2 . ASP A 317  ? 1.5727 1.7777 1.7482 0.7201  0.5962  0.0404  317  ASP A OD2 
2405  N N   . LEU A 318  ? 1.6326 1.6712 1.5185 0.7452  0.4734  0.0442  318  LEU A N   
2406  C CA  . LEU A 318  ? 1.7404 1.7068 1.5178 0.7709  0.4618  0.0635  318  LEU A CA  
2407  C C   . LEU A 318  ? 1.7245 1.6746 1.4489 0.7586  0.3992  0.0475  318  LEU A C   
2408  O O   . LEU A 318  ? 1.7302 1.6373 1.4363 0.7691  0.4165  0.0261  318  LEU A O   
2409  C CB  . LEU A 318  ? 1.8213 1.7304 1.6010 0.8001  0.5379  0.0540  318  LEU A CB  
2410  C CG  . LEU A 318  ? 1.9131 1.7991 1.7113 0.8278  0.6147  0.0758  318  LEU A CG  
2411  C CD1 . LEU A 318  ? 1.9609 1.8051 1.7961 0.8448  0.6876  0.0518  318  LEU A CD1 
2412  C CD2 . LEU A 318  ? 2.0233 1.8620 1.7124 0.8573  0.6019  0.1195  318  LEU A CD2 
2413  N N   . ASN A 319  ? 1.6700 1.6524 1.3723 0.7369  0.3286  0.0584  319  ASN A N   
2414  C CA  . ASN A 319  ? 1.5824 1.5543 1.2477 0.7222  0.2705  0.0424  319  ASN A CA  
2415  C C   . ASN A 319  ? 1.4627 1.4890 1.1417 0.6922  0.2049  0.0524  319  ASN A C   
2416  O O   . ASN A 319  ? 1.3961 1.4754 1.1452 0.6696  0.1997  0.0349  319  ASN A O   
2417  C CB  . ASN A 319  ? 1.5426 1.5198 1.2661 0.7149  0.2959  0.0016  319  ASN A CB  
2418  C CG  . ASN A 319  ? 1.6400 1.5730 1.3058 0.7165  0.2616  -0.0139 319  ASN A CG  
2419  O OD1 . ASN A 319  ? 1.7122 1.6125 1.2954 0.7205  0.2150  0.0042  319  ASN A OD1 
2420  N ND2 . ASN A 319  ? 1.6467 1.5777 1.3568 0.7140  0.2829  -0.0493 319  ASN A ND2 
2421  N N   . ASN A 320  ? 1.4624 1.4770 1.0775 0.6933  0.1563  0.0806  320  ASN A N   
2422  C CA  . ASN A 320  ? 1.4212 1.4805 1.0475 0.6643  0.0912  0.0900  320  ASN A CA  
2423  C C   . ASN A 320  ? 1.4884 1.5052 1.0336 0.6648  0.0313  0.0949  320  ASN A C   
2424  O O   . ASN A 320  ? 1.4890 1.5248 1.0189 0.6506  -0.0232 0.1145  320  ASN A O   
2425  C CB  . ASN A 320  ? 1.4063 1.5147 1.0656 0.6574  0.0881  0.1192  320  ASN A CB  
2426  C CG  . ASN A 320  ? 1.3842 1.5471 1.1367 0.6480  0.1357  0.1084  320  ASN A CG  
2427  O OD1 . ASN A 320  ? 1.3360 1.5569 1.1422 0.6231  0.1145  0.1072  320  ASN A OD1 
2428  N ND2 . ASN A 320  ? 1.4107 1.5534 1.1841 0.6689  0.2024  0.0987  320  ASN A ND2 
2429  N N   . LYS A 321  ? 1.5426 1.5012 1.0417 0.6818  0.0459  0.0750  321  LYS A N   
2430  C CA  . LYS A 321  ? 1.6157 1.5214 1.0367 0.6861  -0.0003 0.0685  321  LYS A CA  
2431  C C   . LYS A 321  ? 1.5479 1.4564 0.9950 0.6675  -0.0177 0.0391  321  LYS A C   
2432  O O   . LYS A 321  ? 1.4738 1.4330 0.9962 0.6487  -0.0068 0.0275  321  LYS A O   
2433  C CB  . LYS A 321  ? 1.7775 1.6115 1.1257 0.7235  0.0376  0.0670  321  LYS A CB  
2434  C CG  . LYS A 321  ? 1.8347 1.6613 1.2264 0.7409  0.1194  0.0547  321  LYS A CG  
2435  C CD  . LYS A 321  ? 1.9942 1.7532 1.3096 0.7824  0.1618  0.0673  321  LYS A CD  
2436  C CE  . LYS A 321  ? 2.0211 1.7950 1.3675 0.8001  0.2210  0.0901  321  LYS A CE  
2437  N NZ  . LYS A 321  ? 2.1244 1.8290 1.3867 0.8436  0.2600  0.1070  321  LYS A NZ  
2438  N N   . TYR A 322  ? 1.5706 1.4232 0.9538 0.6753  -0.0430 0.0261  322  TYR A N   
2439  C CA  . TYR A 322  ? 1.5363 1.3912 0.9369 0.6559  -0.0743 0.0035  322  TYR A CA  
2440  C C   . TYR A 322  ? 1.5673 1.3977 0.9860 0.6668  -0.0321 -0.0278 322  TYR A C   
2441  O O   . TYR A 322  ? 1.6304 1.4222 1.0275 0.6931  0.0188  -0.0331 322  TYR A O   
2442  C CB  . TYR A 322  ? 1.5621 1.3797 0.8947 0.6505  -0.1397 0.0077  322  TYR A CB  
2443  C CG  . TYR A 322  ? 1.5375 1.3975 0.8853 0.6290  -0.1884 0.0326  322  TYR A CG  
2444  C CD1 . TYR A 322  ? 1.4969 1.3788 0.8674 0.6007  -0.2412 0.0325  322  TYR A CD1 
2445  C CD2 . TYR A 322  ? 1.5900 1.4705 0.9368 0.6374  -0.1774 0.0579  322  TYR A CD2 
2446  C CE1 . TYR A 322  ? 1.5251 1.4474 0.9182 0.5804  -0.2816 0.0564  322  TYR A CE1 
2447  C CE2 . TYR A 322  ? 1.6044 1.5269 0.9728 0.6179  -0.2198 0.0811  322  TYR A CE2 
2448  C CZ  . TYR A 322  ? 1.5890 1.5329 0.9826 0.5888  -0.2712 0.0801  322  TYR A CZ  
2449  O OH  . TYR A 322  ? 1.6009 1.5874 1.0232 0.5692  -0.3098 0.1042  322  TYR A OH  
2450  N N   . LEU A 323  ? 1.5278 1.3818 0.9889 0.6477  -0.0520 -0.0473 323  LEU A N   
2451  C CA  . LEU A 323  ? 1.5650 1.3936 1.0403 0.6572  -0.0242 -0.0787 323  LEU A CA  
2452  C C   . LEU A 323  ? 1.6462 1.4338 1.0719 0.6520  -0.0740 -0.0884 323  LEU A C   
2453  O O   . LEU A 323  ? 1.6317 1.4468 1.0707 0.6287  -0.1241 -0.0824 323  LEU A O   
2454  C CB  . LEU A 323  ? 1.4873 1.3782 1.0571 0.6434  -0.0031 -0.0972 323  LEU A CB  
2455  C CG  . LEU A 323  ? 1.4882 1.3620 1.0883 0.6539  0.0288  -0.1323 323  LEU A CG  
2456  C CD1 . LEU A 323  ? 1.4935 1.3451 1.0685 0.6459  -0.0178 -0.1453 323  LEU A CD1 
2457  C CD2 . LEU A 323  ? 1.5515 1.3667 1.1160 0.6828  0.0815  -0.1365 323  LEU A CD2 
2458  N N   . TYR A 324  ? 1.7618 1.4826 1.1316 0.6742  -0.0581 -0.1026 324  TYR A N   
2459  C CA  . TYR A 324  ? 1.8591 1.5319 1.1756 0.6725  -0.1022 -0.1136 324  TYR A CA  
2460  C C   . TYR A 324  ? 1.8526 1.5174 1.2044 0.6738  -0.0875 -0.1442 324  TYR A C   
2461  O O   . TYR A 324  ? 1.8495 1.4954 1.2174 0.6936  -0.0324 -0.1619 324  TYR A O   
2462  C CB  . TYR A 324  ? 2.0094 1.6076 1.2276 0.6984  -0.1017 -0.1093 324  TYR A CB  
2463  C CG  . TYR A 324  ? 2.1264 1.6636 1.2866 0.7037  -0.1327 -0.1274 324  TYR A CG  
2464  C CD1 . TYR A 324  ? 2.2054 1.7191 1.3100 0.6940  -0.1962 -0.1194 324  TYR A CD1 
2465  C CD2 . TYR A 324  ? 2.1651 1.6667 1.3287 0.7191  -0.0974 -0.1536 324  TYR A CD2 
2466  C CE1 . TYR A 324  ? 2.2740 1.7294 1.3261 0.6990  -0.2244 -0.1377 324  TYR A CE1 
2467  C CE2 . TYR A 324  ? 2.2339 1.6774 1.3433 0.7250  -0.1246 -0.1702 324  TYR A CE2 
2468  C CZ  . TYR A 324  ? 2.2786 1.6986 1.3311 0.7148  -0.1881 -0.1623 324  TYR A CZ  
2469  O OH  . TYR A 324  ? 2.3238 1.6853 1.3243 0.7203  -0.2156 -0.1801 324  TYR A OH  
2470  N N   . ILE A 325  ? 1.8186 1.4954 1.1830 0.6541  -0.1360 -0.1494 325  ILE A N   
2471  C CA  . ILE A 325  ? 1.7709 1.4445 1.1702 0.6548  -0.1303 -0.1767 325  ILE A CA  
2472  C C   . ILE A 325  ? 1.8029 1.4216 1.1449 0.6539  -0.1741 -0.1826 325  ILE A C   
2473  O O   . ILE A 325  ? 1.8170 1.4304 1.1266 0.6387  -0.2256 -0.1656 325  ILE A O   
2474  C CB  . ILE A 325  ? 1.6624 1.4076 1.1408 0.6336  -0.1458 -0.1795 325  ILE A CB  
2475  C CG1 . ILE A 325  ? 1.6260 1.4346 1.1491 0.6228  -0.1330 -0.1615 325  ILE A CG1 
2476  C CG2 . ILE A 325  ? 1.6263 1.3817 1.1595 0.6433  -0.1140 -0.2114 325  ILE A CG2 
2477  C CD1 . ILE A 325  ? 1.5461 1.4241 1.1417 0.6060  -0.1446 -0.1662 325  ILE A CD1 
2478  N N   . ALA A 326  ? 1.8134 1.3921 1.1495 0.6701  -0.1522 -0.2080 326  ALA A N   
2479  C CA  . ALA A 326  ? 1.8637 1.3826 1.1448 0.6734  -0.1857 -0.2178 326  ALA A CA  
2480  C C   . ALA A 326  ? 1.8567 1.3605 1.1702 0.6857  -0.1590 -0.2471 326  ALA A C   
2481  O O   . ALA A 326  ? 1.8497 1.3326 1.1694 0.7076  -0.1047 -0.2629 326  ALA A O   
2482  C CB  . ALA A 326  ? 1.9301 1.3808 1.1182 0.6920  -0.1853 -0.2129 326  ALA A CB  
2483  N N   . VAL A 327  ? 1.8728 1.3882 1.2103 0.6717  -0.1973 -0.2529 327  VAL A N   
2484  C CA  . VAL A 327  ? 1.8814 1.3929 1.2590 0.6807  -0.1823 -0.2793 327  VAL A CA  
2485  C C   . VAL A 327  ? 1.9720 1.4061 1.2855 0.6921  -0.1985 -0.2908 327  VAL A C   
2486  O O   . VAL A 327  ? 2.0414 1.4406 1.2937 0.6842  -0.2395 -0.2773 327  VAL A O   
2487  C CB  . VAL A 327  ? 1.7694 1.3384 1.2060 0.6613  -0.2174 -0.2760 327  VAL A CB  
2488  C CG1 . VAL A 327  ? 1.7522 1.3315 1.2434 0.6731  -0.1987 -0.3048 327  VAL A CG1 
2489  C CG2 . VAL A 327  ? 1.6820 1.3237 1.1648 0.6465  -0.2144 -0.2589 327  VAL A CG2 
2490  N N   . THR A 328  ? 2.0097 1.4180 1.3408 0.7107  -0.1666 -0.3171 328  THR A N   
2491  C CA  . THR A 328  ? 2.0870 1.4308 1.3754 0.7196  -0.1853 -0.3317 328  THR A CA  
2492  C C   . THR A 328  ? 2.0614 1.4281 1.4174 0.7216  -0.1842 -0.3522 328  THR A C   
2493  O O   . THR A 328  ? 1.9920 1.3752 1.4009 0.7363  -0.1386 -0.3727 328  THR A O   
2494  C CB  . THR A 328  ? 2.1934 1.4624 1.4150 0.7468  -0.1476 -0.3440 328  THR A CB  
2495  O OG1 . THR A 328  ? 2.2563 1.5072 1.4134 0.7487  -0.1491 -0.3246 328  THR A OG1 
2496  C CG2 . THR A 328  ? 2.2470 1.4490 1.4173 0.7534  -0.1749 -0.3571 328  THR A CG2 
2497  N N   . VAL A 329  ? 2.0992 1.4675 1.4561 0.7072  -0.2350 -0.3460 329  VAL A N   
2498  C CA  . VAL A 329  ? 2.1051 1.5015 1.5232 0.7081  -0.2441 -0.3597 329  VAL A CA  
2499  C C   . VAL A 329  ? 2.2703 1.5986 1.6540 0.7206  -0.2537 -0.3754 329  VAL A C   
2500  O O   . VAL A 329  ? 2.3623 1.6575 1.7049 0.7094  -0.2983 -0.3637 329  VAL A O   
2501  C CB  . VAL A 329  ? 1.9959 1.4368 1.4352 0.6850  -0.2949 -0.3373 329  VAL A CB  
2502  C CG1 . VAL A 329  ? 1.9282 1.4025 1.4291 0.6903  -0.3031 -0.3502 329  VAL A CG1 
2503  C CG2 . VAL A 329  ? 1.9299 1.4323 1.3902 0.6694  -0.2941 -0.3164 329  VAL A CG2 
2504  N N   . ILE A 330  ? 2.3422 1.6485 1.7463 0.7433  -0.2116 -0.4023 330  ILE A N   
2505  C CA  . ILE A 330  ? 2.4678 1.7070 1.8410 0.7575  -0.2166 -0.4190 330  ILE A CA  
2506  C C   . ILE A 330  ? 2.5295 1.7973 1.9675 0.7597  -0.2330 -0.4306 330  ILE A C   
2507  O O   . ILE A 330  ? 2.4540 1.7701 1.9659 0.7691  -0.2055 -0.4473 330  ILE A O   
2508  C CB  . ILE A 330  ? 2.6627 1.8423 2.0019 0.7840  -0.1621 -0.4396 330  ILE A CB  
2509  C CG1 . ILE A 330  ? 2.6187 1.8422 2.0333 0.7971  -0.1043 -0.4563 330  ILE A CG1 
2510  C CG2 . ILE A 330  ? 2.7053 1.8388 1.9555 0.7851  -0.1594 -0.4257 330  ILE A CG2 
2511  C CD1 . ILE A 330  ? 2.6753 1.8426 2.0554 0.8223  -0.0440 -0.4694 330  ILE A CD1 
2512  N N   . GLU A 331  ? 2.6802 1.9187 2.0920 0.7515  -0.2790 -0.4219 331  GLU A N   
2513  C CA  . GLU A 331  ? 2.7735 2.0410 2.2403 0.7531  -0.3012 -0.4257 331  GLU A CA  
2514  C C   . GLU A 331  ? 2.8975 2.1463 2.4001 0.7787  -0.2670 -0.4572 331  GLU A C   
2515  O O   . GLU A 331  ? 2.9735 2.1529 2.4320 0.7928  -0.2470 -0.4714 331  GLU A O   
2516  C CB  . GLU A 331  ? 2.8183 2.0467 2.2461 0.7407  -0.3522 -0.4088 331  GLU A CB  
2517  C CG  . GLU A 331  ? 2.8218 2.0578 2.2935 0.7501  -0.3689 -0.4153 331  GLU A CG  
2518  C CD  . GLU A 331  ? 2.8908 2.0590 2.3168 0.7457  -0.4038 -0.4084 331  GLU A CD  
2519  O OE1 . GLU A 331  ? 2.9255 2.0552 2.2929 0.7305  -0.4227 -0.3958 331  GLU A OE1 
2520  O OE2 . GLU A 331  ? 2.9102 2.0634 2.3603 0.7579  -0.4129 -0.4166 331  GLU A OE2 
2521  N N   . SER A 332  ? 2.9338 2.2451 2.5170 0.7859  -0.2613 -0.4688 332  SER A N   
2522  C CA  . SER A 332  ? 3.0387 2.3460 2.6743 0.8103  -0.2264 -0.5010 332  SER A CA  
2523  C C   . SER A 332  ? 3.1704 2.4233 2.7917 0.8226  -0.2448 -0.5092 332  SER A C   
2524  O O   . SER A 332  ? 3.2110 2.4185 2.8335 0.8424  -0.2116 -0.5327 332  SER A O   
2525  C CB  . SER A 332  ? 2.9915 2.3873 2.7219 0.8147  -0.2205 -0.5140 332  SER A CB  
2526  O OG  . SER A 332  ? 3.0162 2.4116 2.8064 0.8379  -0.1840 -0.5477 332  SER A OG  
2527  N N   . THR A 333  ? 3.2454 2.5020 2.8557 0.8119  -0.2950 -0.4891 333  THR A N   
2528  C CA  . THR A 333  ? 3.3499 2.5557 2.9494 0.8228  -0.3150 -0.4940 333  THR A CA  
2529  C C   . THR A 333  ? 3.4501 2.5605 2.9693 0.8241  -0.3106 -0.4972 333  THR A C   
2530  O O   . THR A 333  ? 3.5054 2.5692 3.0214 0.8445  -0.2793 -0.5216 333  THR A O   
2531  C CB  . THR A 333  ? 3.3507 2.5820 2.9583 0.8116  -0.3675 -0.4678 333  THR A CB  
2532  O OG1 . THR A 333  ? 3.4179 2.5755 2.9644 0.8036  -0.3957 -0.4547 333  THR A OG1 
2533  C CG2 . THR A 333  ? 3.2922 2.5870 2.9047 0.7901  -0.3849 -0.4424 333  THR A CG2 
2534  N N   . GLY A 334  ? 3.4697 2.5518 2.9258 0.8033  -0.3417 -0.4742 334  GLY A N   
2535  C CA  . GLY A 334  ? 3.5328 2.5261 2.9095 0.8041  -0.3457 -0.4789 334  GLY A CA  
2536  C C   . GLY A 334  ? 3.5326 2.4892 2.8634 0.8158  -0.3010 -0.4950 334  GLY A C   
2537  O O   . GLY A 334  ? 3.6453 2.5250 2.9175 0.8282  -0.2911 -0.5095 334  GLY A O   
2538  N N   . GLY A 335  ? 3.3757 2.3854 2.7311 0.8137  -0.2726 -0.4921 335  GLY A N   
2539  C CA  . GLY A 335  ? 3.2978 2.2765 2.6089 0.8252  -0.2281 -0.5014 335  GLY A CA  
2540  C C   . GLY A 335  ? 3.2113 2.1618 2.4409 0.8101  -0.2513 -0.4827 335  GLY A C   
2541  O O   . GLY A 335  ? 3.2452 2.1569 2.4178 0.8219  -0.2210 -0.4878 335  GLY A O   
2542  N N   . PHE A 336  ? 3.1158 2.0859 2.3411 0.7854  -0.3049 -0.4605 336  PHE A N   
2543  C CA  . PHE A 336  ? 3.0118 1.9625 2.1716 0.7683  -0.3348 -0.4428 336  PHE A CA  
2544  C C   . PHE A 336  ? 2.8897 1.8767 2.0447 0.7687  -0.3036 -0.4348 336  PHE A C   
2545  O O   . PHE A 336  ? 2.8646 1.8660 2.0475 0.7865  -0.2523 -0.4479 336  PHE A O   
2546  C CB  . PHE A 336  ? 2.9120 1.9008 2.0973 0.7400  -0.3890 -0.4172 336  PHE A CB  
2547  C CG  . PHE A 336  ? 2.8796 1.8164 2.0459 0.7341  -0.4299 -0.4181 336  PHE A CG  
2548  C CD1 . PHE A 336  ? 2.7989 1.7649 2.0225 0.7270  -0.4533 -0.4079 336  PHE A CD1 
2549  C CD2 . PHE A 336  ? 2.9329 1.7917 2.0240 0.7365  -0.4456 -0.4290 336  PHE A CD2 
2550  C CE1 . PHE A 336  ? 2.8268 1.7439 2.0373 0.7214  -0.4884 -0.4064 336  PHE A CE1 
2551  C CE2 . PHE A 336  ? 2.9682 1.7791 2.0480 0.7296  -0.4828 -0.4313 336  PHE A CE2 
2552  C CZ  . PHE A 336  ? 2.9203 1.7598 2.0621 0.7215  -0.5028 -0.4189 336  PHE A CZ  
2553  N N   . SER A 337  ? 2.8032 1.8049 1.9274 0.7489  -0.3342 -0.4129 337  SER A N   
2554  C CA  . SER A 337  ? 2.6829 1.7313 1.8135 0.7454  -0.3111 -0.3996 337  SER A CA  
2555  C C   . SER A 337  ? 2.6655 1.7369 1.7755 0.7197  -0.3557 -0.3732 337  SER A C   
2556  O O   . SER A 337  ? 2.7172 1.7437 1.7751 0.7107  -0.3968 -0.3698 337  SER A O   
2557  C CB  . SER A 337  ? 2.6855 1.6888 1.7602 0.7705  -0.2628 -0.4121 337  SER A CB  
2558  O OG  . SER A 337  ? 2.5923 1.6378 1.6701 0.7664  -0.2439 -0.3958 337  SER A OG  
2559  N N   . GLU A 338  ? 2.5804 1.7226 1.7355 0.7085  -0.3459 -0.3562 338  GLU A N   
2560  C CA  . GLU A 338  ? 2.5599 1.7359 1.7114 0.6834  -0.3845 -0.3293 338  GLU A CA  
2561  C C   . GLU A 338  ? 2.4819 1.7056 1.6460 0.6839  -0.3538 -0.3177 338  GLU A C   
2562  O O   . GLU A 338  ? 2.4119 1.6796 1.6306 0.6918  -0.3140 -0.3241 338  GLU A O   
2563  C CB  . GLU A 338  ? 2.5510 1.7760 1.7641 0.6623  -0.4186 -0.3141 338  GLU A CB  
2564  C CG  . GLU A 338  ? 2.6136 1.8413 1.8110 0.6362  -0.4701 -0.2898 338  GLU A CG  
2565  C CD  . GLU A 338  ? 2.7536 1.9042 1.8764 0.6379  -0.4965 -0.2988 338  GLU A CD  
2566  O OE1 . GLU A 338  ? 2.8116 1.9039 1.9104 0.6500  -0.4990 -0.3190 338  GLU A OE1 
2567  O OE2 . GLU A 338  ? 2.8035 1.9529 1.8923 0.6279  -0.5157 -0.2869 338  GLU A OE2 
2568  N N   . GLU A 339  ? 2.4980 1.7116 1.6131 0.6761  -0.3732 -0.3023 339  GLU A N   
2569  C CA  . GLU A 339  ? 2.4746 1.7279 1.5939 0.6768  -0.3479 -0.2881 339  GLU A CA  
2570  C C   . GLU A 339  ? 2.3395 1.6476 1.4872 0.6482  -0.3874 -0.2602 339  GLU A C   
2571  O O   . GLU A 339  ? 2.3019 1.5990 1.4434 0.6299  -0.4370 -0.2516 339  GLU A O   
2572  C CB  . GLU A 339  ? 2.6515 1.8472 1.6854 0.6969  -0.3334 -0.2920 339  GLU A CB  
2573  C CG  . GLU A 339  ? 2.8011 1.9555 1.8139 0.7289  -0.2745 -0.3138 339  GLU A CG  
2574  C CD  . GLU A 339  ? 3.0224 2.0904 1.9333 0.7515  -0.2768 -0.3258 339  GLU A CD  
2575  O OE1 . GLU A 339  ? 3.1062 2.1553 1.9554 0.7491  -0.3084 -0.3147 339  GLU A OE1 
2576  O OE2 . GLU A 339  ? 3.1008 2.1196 1.9928 0.7732  -0.2473 -0.3479 339  GLU A OE2 
2577  N N   . ALA A 340  ? 2.2869 1.6528 1.4699 0.6451  -0.3621 -0.2467 340  ALA A N   
2578  C CA  . ALA A 340  ? 2.2306 1.6544 1.4440 0.6207  -0.3892 -0.2190 340  ALA A CA  
2579  C C   . ALA A 340  ? 2.1754 1.6336 1.3953 0.6276  -0.3521 -0.2092 340  ALA A C   
2580  O O   . ALA A 340  ? 2.1540 1.6157 1.3901 0.6463  -0.3009 -0.2233 340  ALA A O   
2581  C CB  . ALA A 340  ? 2.1931 1.6756 1.4806 0.6043  -0.4004 -0.2121 340  ALA A CB  
2582  N N   . GLU A 341  ? 2.1421 1.6272 1.3564 0.6124  -0.3765 -0.1849 341  GLU A N   
2583  C CA  . GLU A 341  ? 2.1395 1.6592 1.3622 0.6185  -0.3428 -0.1724 341  GLU A CA  
2584  C C   . GLU A 341  ? 1.7644 1.3520 1.0323 0.5943  -0.3639 -0.1445 341  GLU A C   
2585  O O   . GLU A 341  ? 1.7508 1.3470 1.0245 0.5727  -0.4120 -0.1303 341  GLU A O   
2586  C CB  . GLU A 341  ? 2.2368 1.7000 1.3775 0.6391  -0.3360 -0.1727 341  GLU A CB  
2587  C CG  . GLU A 341  ? 2.3170 1.7444 1.4017 0.6293  -0.3956 -0.1652 341  GLU A CG  
2588  C CD  . GLU A 341  ? 2.3895 1.7908 1.4066 0.6461  -0.3949 -0.1563 341  GLU A CD  
2589  O OE1 . GLU A 341  ? 2.3937 1.7979 1.4017 0.6673  -0.3442 -0.1540 341  GLU A OE1 
2590  O OE2 . GLU A 341  ? 2.4440 1.8216 1.4186 0.6391  -0.4455 -0.1520 341  GLU A OE2 
2591  N N   . ILE A 342  ? 1.7207 1.3552 1.0243 0.5981  -0.3253 -0.1369 342  ILE A N   
2592  C CA  . ILE A 342  ? 1.6516 1.3414 0.9845 0.5803  -0.3393 -0.1098 342  ILE A CA  
2593  C C   . ILE A 342  ? 1.7042 1.3768 0.9932 0.5954  -0.3213 -0.0997 342  ILE A C   
2594  O O   . ILE A 342  ? 1.7191 1.3828 1.0047 0.6167  -0.2699 -0.1090 342  ILE A O   
2595  C CB  . ILE A 342  ? 1.5109 1.2716 0.9206 0.5738  -0.3085 -0.1081 342  ILE A CB  
2596  C CG1 . ILE A 342  ? 1.4916 1.2780 0.9446 0.5603  -0.3297 -0.1141 342  ILE A CG1 
2597  C CG2 . ILE A 342  ? 1.4203 1.2322 0.8537 0.5600  -0.3144 -0.0806 342  ILE A CG2 
2598  C CD1 . ILE A 342  ? 1.4291 1.2737 0.9500 0.5628  -0.2945 -0.1256 342  ILE A CD1 
2599  N N   . PRO A 343  ? 1.7229 1.3934 0.9833 0.5850  -0.3624 -0.0796 343  PRO A N   
2600  C CA  . PRO A 343  ? 1.7676 1.4097 0.9690 0.6037  -0.3555 -0.0710 343  PRO A CA  
2601  C C   . PRO A 343  ? 1.7026 1.3825 0.9353 0.6152  -0.3011 -0.0616 343  PRO A C   
2602  O O   . PRO A 343  ? 1.7769 1.4244 0.9753 0.6423  -0.2568 -0.0684 343  PRO A O   
2603  C CB  . PRO A 343  ? 1.7632 1.4238 0.9619 0.5830  -0.4127 -0.0491 343  PRO A CB  
2604  C CG  . PRO A 343  ? 1.7340 1.4223 0.9852 0.5541  -0.4468 -0.0467 343  PRO A CG  
2605  C CD  . PRO A 343  ? 1.6862 1.4012 0.9877 0.5552  -0.4072 -0.0589 343  PRO A CD  
2606  N N   . GLY A 344  ? 1.6130 1.3613 0.9138 0.5946  -0.3024 -0.0455 344  GLY A N   
2607  C CA  . GLY A 344  ? 1.5486 1.3397 0.8908 0.6015  -0.2531 -0.0369 344  GLY A CA  
2608  C C   . GLY A 344  ? 1.4239 1.2903 0.8481 0.5773  -0.2550 -0.0278 344  GLY A C   
2609  O O   . GLY A 344  ? 1.4218 1.3076 0.8650 0.5549  -0.2983 -0.0210 344  GLY A O   
2610  N N   . ILE A 345  ? 1.3780 1.2842 0.8498 0.5830  -0.2065 -0.0276 345  ILE A N   
2611  C CA  . ILE A 345  ? 1.3117 1.2885 0.8599 0.5651  -0.1995 -0.0246 345  ILE A CA  
2612  C C   . ILE A 345  ? 1.2922 1.2940 0.8597 0.5746  -0.1590 -0.0118 345  ILE A C   
2613  O O   . ILE A 345  ? 1.3225 1.3042 0.8895 0.5952  -0.1092 -0.0255 345  ILE A O   
2614  C CB  . ILE A 345  ? 1.2659 1.2531 0.8568 0.5704  -0.1684 -0.0558 345  ILE A CB  
2615  C CG1 . ILE A 345  ? 1.1336 1.1023 0.7138 0.5615  -0.2070 -0.0677 345  ILE A CG1 
2616  C CG2 . ILE A 345  ? 1.2047 1.2632 0.8712 0.5605  -0.1472 -0.0579 345  ILE A CG2 
2617  C CD1 . ILE A 345  ? 1.0975 1.0872 0.7265 0.5662  -0.1825 -0.0967 345  ILE A CD1 
2618  N N   . LYS A 346  ? 1.2472 1.2896 0.8328 0.5608  -0.1775 0.0152  346  LYS A N   
2619  C CA  . LYS A 346  ? 1.1070 1.1668 0.7034 0.5720  -0.1418 0.0311  346  LYS A CA  
2620  C C   . LYS A 346  ? 1.0524 1.1505 0.7154 0.5768  -0.0844 0.0143  346  LYS A C   
2621  O O   . LYS A 346  ? 1.0767 1.2185 0.7918 0.5621  -0.0877 0.0028  346  LYS A O   
2622  C CB  . LYS A 346  ? 1.0905 1.1903 0.7006 0.5547  -0.1764 0.0627  346  LYS A CB  
2623  C CG  . LYS A 346  ? 1.1423 1.2477 0.7457 0.5691  -0.1511 0.0838  346  LYS A CG  
2624  C CD  . LYS A 346  ? 1.1488 1.3032 0.7807 0.5510  -0.1819 0.1144  346  LYS A CD  
2625  C CE  . LYS A 346  ? 1.2106 1.3422 0.7983 0.5416  -0.2467 0.1295  346  LYS A CE  
2626  N NZ  . LYS A 346  ? 1.2077 1.3770 0.8160 0.5333  -0.2680 0.1605  346  LYS A NZ  
2627  N N   . TYR A 347  ? 1.0669 1.1475 0.7294 0.5985  -0.0313 0.0114  347  TYR A N   
2628  C CA  . TYR A 347  ? 1.0821 1.2051 0.8195 0.6006  0.0228  -0.0036 347  TYR A CA  
2629  C C   . TYR A 347  ? 1.0450 1.2213 0.8187 0.5901  0.0237  0.0221  347  TYR A C   
2630  O O   . TYR A 347  ? 1.0264 1.1927 0.7614 0.5920  0.0020  0.0516  347  TYR A O   
2631  C CB  . TYR A 347  ? 1.0895 1.1731 0.8234 0.6276  0.0863  -0.0157 347  TYR A CB  
2632  C CG  . TYR A 347  ? 1.1043 1.1595 0.8495 0.6366  0.1102  -0.0513 347  TYR A CG  
2633  C CD1 . TYR A 347  ? 1.0657 1.1615 0.8927 0.6318  0.1425  -0.0814 347  TYR A CD1 
2634  C CD2 . TYR A 347  ? 1.1840 1.1718 0.8594 0.6514  0.1007  -0.0565 347  TYR A CD2 
2635  C CE1 . TYR A 347  ? 1.0939 1.1669 0.9387 0.6405  0.1632  -0.1154 347  TYR A CE1 
2636  C CE2 . TYR A 347  ? 1.2110 1.1729 0.9002 0.6604  0.1240  -0.0886 347  TYR A CE2 
2637  C CZ  . TYR A 347  ? 1.1770 1.1828 0.9540 0.6545  0.1549  -0.1178 347  TYR A CZ  
2638  O OH  . TYR A 347  ? 1.2013 1.1858 1.0007 0.6632  0.1762  -0.1515 347  TYR A OH  
2639  N N   . VAL A 348  ? 1.0350 1.2685 0.8829 0.5804  0.0476  0.0100  348  VAL A N   
2640  C CA  . VAL A 348  ? 1.0558 1.3400 0.9400 0.5711  0.0512  0.0337  348  VAL A CA  
2641  C C   . VAL A 348  ? 1.0372 1.3581 0.9934 0.5767  0.1099  0.0177  348  VAL A C   
2642  O O   . VAL A 348  ? 1.0262 1.3716 1.0317 0.5731  0.1268  -0.0149 348  VAL A O   
2643  C CB  . VAL A 348  ? 1.0779 1.4093 0.9794 0.5458  0.0021  0.0454  348  VAL A CB  
2644  C CG1 . VAL A 348  ? 1.0443 1.4333 0.9961 0.5376  0.0169  0.0641  348  VAL A CG1 
2645  C CG2 . VAL A 348  ? 1.1361 1.4365 0.9767 0.5387  -0.0541 0.0687  348  VAL A CG2 
2646  N N   . LEU A 349  ? 1.0152 1.3404 0.9798 0.5861  0.1400  0.0393  349  LEU A N   
2647  C CA  . LEU A 349  ? 0.9859 1.3480 1.0245 0.5894  0.1948  0.0253  349  LEU A CA  
2648  C C   . LEU A 349  ? 0.8891 1.3214 0.9803 0.5676  0.1749  0.0230  349  LEU A C   
2649  O O   . LEU A 349  ? 0.8245 1.2919 0.9722 0.5625  0.1922  -0.0098 349  LEU A O   
2650  C CB  . LEU A 349  ? 1.0647 1.4118 1.0958 0.6061  0.2302  0.0537  349  LEU A CB  
2651  C CG  . LEU A 349  ? 1.0672 1.4266 1.1656 0.6182  0.3020  0.0398  349  LEU A CG  
2652  C CD1 . LEU A 349  ? 1.0327 1.4490 1.1829 0.6087  0.3114  0.0567  349  LEU A CD1 
2653  C CD2 . LEU A 349  ? 1.0441 1.4115 1.1986 0.6165  0.3311  -0.0083 349  LEU A CD2 
2654  N N   . SER A 350  ? 1.2317 0.9680 0.7979 0.3488  0.1510  -0.0380 350  SER A N   
2655  C CA  . SER A 350  ? 1.2047 0.9311 0.7705 0.3425  0.1469  -0.0221 350  SER A CA  
2656  C C   . SER A 350  ? 1.2175 0.9269 0.7585 0.3362  0.1141  -0.0123 350  SER A C   
2657  O O   . SER A 350  ? 1.2528 0.9656 0.7772 0.3326  0.1044  0.0006  350  SER A O   
2658  C CB  . SER A 350  ? 1.1991 0.9401 0.7709 0.3388  0.1745  0.0068  350  SER A CB  
2659  O OG  . SER A 350  ? 1.2000 0.9345 0.7669 0.3318  0.1680  0.0255  350  SER A OG  
2660  N N   . PRO A 351  ? 1.1993 0.8896 0.7369 0.3340  0.0965  -0.0182 351  PRO A N   
2661  C CA  . PRO A 351  ? 1.2240 0.8930 0.7367 0.3279  0.0632  -0.0134 351  PRO A CA  
2662  C C   . PRO A 351  ? 1.2522 0.9248 0.7520 0.3153  0.0623  0.0192  351  PRO A C   
2663  O O   . PRO A 351  ? 1.3020 0.9564 0.7816 0.3075  0.0359  0.0251  351  PRO A O   
2664  C CB  . PRO A 351  ? 1.2076 0.8543 0.7195 0.3305  0.0465  -0.0294 351  PRO A CB  
2665  C CG  . PRO A 351  ? 1.1763 0.8365 0.7159 0.3404  0.0688  -0.0513 351  PRO A CG  
2666  C CD  . PRO A 351  ? 1.1650 0.8496 0.7186 0.3377  0.1022  -0.0338 351  PRO A CD  
2667  N N   . TYR A 352  ? 1.2326 0.9273 0.7445 0.3133  0.0896  0.0394  352  TYR A N   
2668  C CA  . TYR A 352  ? 1.2458 0.9510 0.7481 0.3029  0.0893  0.0693  352  TYR A CA  
2669  C C   . TYR A 352  ? 1.2342 0.9627 0.7376 0.3060  0.1025  0.0804  352  TYR A C   
2670  O O   . TYR A 352  ? 1.1991 0.9359 0.7120 0.3155  0.1180  0.0680  352  TYR A O   
2671  C CB  . TYR A 352  ? 1.2640 0.9771 0.7765 0.2986  0.1070  0.0868  352  TYR A CB  
2672  C CG  . TYR A 352  ? 1.2922 0.9859 0.8036 0.2970  0.0990  0.0762  352  TYR A CG  
2673  C CD1 . TYR A 352  ? 1.3274 1.0037 0.8192 0.2861  0.0761  0.0848  352  TYR A CD1 
2674  C CD2 . TYR A 352  ? 1.2997 0.9928 0.8289 0.3058  0.1148  0.0581  352  TYR A CD2 
2675  C CE1 . TYR A 352  ? 1.3446 1.0022 0.8312 0.2852  0.0681  0.0763  352  TYR A CE1 
2676  C CE2 . TYR A 352  ? 1.3313 1.0084 0.8580 0.3052  0.1063  0.0478  352  TYR A CE2 
2677  C CZ  . TYR A 352  ? 1.3527 1.0118 0.8565 0.2956  0.0827  0.0575  352  TYR A CZ  
2678  O OH  . TYR A 352  ? 1.3712 1.0138 0.8691 0.2960  0.0741  0.0477  352  TYR A OH  
2679  N N   . LYS A 353  ? 1.2696 1.0098 0.7634 0.2977  0.0966  0.1039  353  LYS A N   
2680  C CA  . LYS A 353  ? 1.2910 1.0561 0.7846 0.3011  0.1090  0.1185  353  LYS A CA  
2681  C C   . LYS A 353  ? 1.2120 0.9971 0.7077 0.2939  0.1148  0.1487  353  LYS A C   
2682  O O   . LYS A 353  ? 1.1586 0.9420 0.6437 0.2817  0.0944  0.1586  353  LYS A O   
2683  C CB  . LYS A 353  ? 1.3858 1.1477 0.8617 0.3009  0.0874  0.1076  353  LYS A CB  
2684  C CG  . LYS A 353  ? 1.4893 1.2238 0.9504 0.2922  0.0542  0.0952  353  LYS A CG  
2685  C CD  . LYS A 353  ? 1.5787 1.3005 1.0273 0.2974  0.0352  0.0705  353  LYS A CD  
2686  C CE  . LYS A 353  ? 1.6323 1.3603 1.0633 0.2900  0.0155  0.0780  353  LYS A CE  
2687  N NZ  . LYS A 353  ? 1.6651 1.3831 1.0844 0.2969  -0.0004 0.0523  353  LYS A NZ  
2688  N N   . LEU A 354  ? 1.1881 0.9918 0.6988 0.3014  0.1433  0.1625  354  LEU A N   
2689  C CA  . LEU A 354  ? 1.1859 1.0121 0.7025 0.2982  0.1519  0.1900  354  LEU A CA  
2690  C C   . LEU A 354  ? 1.1738 1.0219 0.6807 0.2994  0.1456  0.2040  354  LEU A C   
2691  O O   . LEU A 354  ? 1.1907 1.0412 0.6906 0.3076  0.1491  0.1968  354  LEU A O   
2692  C CB  . LEU A 354  ? 1.1975 1.0334 0.7340 0.3083  0.1849  0.1992  354  LEU A CB  
2693  C CG  . LEU A 354  ? 1.1784 0.9985 0.7298 0.3140  0.2039  0.1832  354  LEU A CG  
2694  C CD1 . LEU A 354  ? 1.2006 1.0084 0.7525 0.3049  0.1927  0.1786  354  LEU A CD1 
2695  C CD2 . LEU A 354  ? 1.1685 0.9743 0.7170 0.3191  0.2026  0.1580  354  LEU A CD2 
2696  N N   . ASN A 355  ? 1.1570 1.0238 0.6645 0.2915  0.1381  0.2241  355  ASN A N   
2697  C CA  . ASN A 355  ? 1.1827 1.0760 0.6845 0.2937  0.1340  0.2397  355  ASN A CA  
2698  C C   . ASN A 355  ? 1.1610 1.0792 0.6744 0.2880  0.1360  0.2627  355  ASN A C   
2699  O O   . ASN A 355  ? 1.1099 1.0240 0.6234 0.2734  0.1220  0.2637  355  ASN A O   
2700  C CB  . ASN A 355  ? 1.3118 1.1998 0.7940 0.2850  0.1043  0.2289  355  ASN A CB  
2701  C CG  . ASN A 355  ? 1.3877 1.2598 0.8650 0.2673  0.0805  0.2244  355  ASN A CG  
2702  O OD1 . ASN A 355  ? 1.4232 1.2648 0.8951 0.2641  0.0720  0.2061  355  ASN A OD1 
2703  N ND2 . ASN A 355  ? 1.4161 1.3085 0.8946 0.2554  0.0690  0.2408  355  ASN A ND2 
2704  N N   . LEU A 356  ? 1.1407 1.0845 0.6635 0.2998  0.1538  0.2813  356  LEU A N   
2705  C CA  . LEU A 356  ? 1.1078 1.0806 0.6451 0.2977  0.1579  0.3031  356  LEU A CA  
2706  C C   . LEU A 356  ? 1.1339 1.1200 0.6640 0.2804  0.1296  0.3058  356  LEU A C   
2707  O O   . LEU A 356  ? 1.1844 1.1606 0.6969 0.2745  0.1088  0.2938  356  LEU A O   
2708  C CB  . LEU A 356  ? 1.1394 1.1369 0.6819 0.3151  0.1744  0.3210  356  LEU A CB  
2709  C CG  . LEU A 356  ? 1.1204 1.1030 0.6711 0.3312  0.2047  0.3207  356  LEU A CG  
2710  C CD1 . LEU A 356  ? 1.1184 1.1233 0.6742 0.3487  0.2214  0.3428  356  LEU A CD1 
2711  C CD2 . LEU A 356  ? 1.1267 1.0983 0.6948 0.3267  0.2168  0.3174  356  LEU A CD2 
2712  N N   . VAL A 357  ? 1.1387 1.1471 0.6829 0.2715  0.1290  0.3201  357  VAL A N   
2713  C CA  . VAL A 357  ? 1.1682 1.1892 0.7080 0.2519  0.1036  0.3227  357  VAL A CA  
2714  C C   . VAL A 357  ? 1.2325 1.2989 0.7901 0.2516  0.1062  0.3435  357  VAL A C   
2715  O O   . VAL A 357  ? 1.1495 1.2303 0.7255 0.2528  0.1222  0.3541  357  VAL A O   
2716  C CB  . VAL A 357  ? 1.1145 1.1139 0.6527 0.2334  0.0960  0.3163  357  VAL A CB  
2717  C CG1 . VAL A 357  ? 1.1242 1.1465 0.6656 0.2128  0.0776  0.3261  357  VAL A CG1 
2718  C CG2 . VAL A 357  ? 1.1243 1.0801 0.6422 0.2296  0.0823  0.2942  357  VAL A CG2 
2719  N N   . ALA A 358  ? 1.2552 1.3463 0.8081 0.2503  0.0897  0.3481  358  ALA A N   
2720  C CA  . ALA A 358  ? 1.2834 1.4229 0.8551 0.2527  0.0910  0.3672  358  ALA A CA  
2721  C C   . ALA A 358  ? 1.2661 1.4197 0.8588 0.2710  0.1205  0.3812  358  ALA A C   
2722  O O   . ALA A 358  ? 1.2038 1.3802 0.8172 0.2661  0.1284  0.3912  358  ALA A O   
2723  C CB  . ALA A 358  ? 1.3234 1.4806 0.9029 0.2271  0.0725  0.3694  358  ALA A CB  
2724  N N   . THR A 359  ? 1.2568 1.3944 0.8433 0.2918  0.1375  0.3807  359  THR A N   
2725  C CA  . THR A 359  ? 1.2589 1.4068 0.8629 0.3121  0.1648  0.3943  359  THR A CA  
2726  C C   . THR A 359  ? 1.2226 1.3786 0.8188 0.3348  0.1725  0.4043  359  THR A C   
2727  O O   . THR A 359  ? 1.1820 1.3081 0.7654 0.3453  0.1854  0.3975  359  THR A O   
2728  C CB  . THR A 359  ? 1.2946 1.4073 0.9021 0.3144  0.1856  0.3845  359  THR A CB  
2729  O OG1 . THR A 359  ? 1.3199 1.3963 0.9074 0.3167  0.1851  0.3684  359  THR A OG1 
2730  C CG2 . THR A 359  ? 1.2806 1.3885 0.8944 0.2936  0.1793  0.3780  359  THR A CG2 
2731  N N   . PRO A 360  ? 1.2186 1.4167 0.8232 0.3423  0.1651  0.4208  360  PRO A N   
2732  C CA  . PRO A 360  ? 1.2077 1.4246 0.8041 0.3631  0.1662  0.4347  360  PRO A CA  
2733  C C   . PRO A 360  ? 1.2143 1.4074 0.8095 0.3848  0.1948  0.4415  360  PRO A C   
2734  O O   . PRO A 360  ? 1.1228 1.3048 0.7362 0.3878  0.2149  0.4428  360  PRO A O   
2735  C CB  . PRO A 360  ? 1.2047 1.4713 0.8249 0.3672  0.1613  0.4516  360  PRO A CB  
2736  C CG  . PRO A 360  ? 1.2055 1.4841 0.8371 0.3408  0.1454  0.4427  360  PRO A CG  
2737  C CD  . PRO A 360  ? 1.2067 1.4407 0.8323 0.3283  0.1542  0.4268  360  PRO A CD  
2738  N N   . LEU A 361  ? 1.2493 1.4344 0.8228 0.3990  0.1971  0.4458  361  LEU A N   
2739  C CA  . LEU A 361  ? 1.2880 1.4424 0.8565 0.4159  0.2251  0.4500  361  LEU A CA  
2740  C C   . LEU A 361  ? 1.4004 1.5699 0.9752 0.4413  0.2408  0.4748  361  LEU A C   
2741  O O   . LEU A 361  ? 1.4040 1.5513 0.9650 0.4568  0.2589  0.4822  361  LEU A O   
2742  C CB  . LEU A 361  ? 1.2742 1.4011 0.8138 0.4141  0.2236  0.4368  361  LEU A CB  
2743  C CG  . LEU A 361  ? 1.2491 1.3410 0.7923 0.3989  0.2292  0.4137  361  LEU A CG  
2744  C CD1 . LEU A 361  ? 1.2067 1.3029 0.7491 0.3757  0.2021  0.3969  361  LEU A CD1 
2745  C CD2 . LEU A 361  ? 1.2840 1.3453 0.8068 0.4039  0.2415  0.4031  361  LEU A CD2 
2746  N N   . PHE A 362  ? 1.4758 1.6828 1.0725 0.4451  0.2341  0.4874  362  PHE A N   
2747  C CA  . PHE A 362  ? 1.5566 1.7836 1.1629 0.4703  0.2447  0.5111  362  PHE A CA  
2748  C C   . PHE A 362  ? 1.4400 1.6821 1.0811 0.4717  0.2556  0.5151  362  PHE A C   
2749  O O   . PHE A 362  ? 1.3804 1.6472 1.0381 0.4543  0.2419  0.5072  362  PHE A O   
2750  C CB  . PHE A 362  ? 1.7234 1.9945 1.3218 0.4763  0.2197  0.5226  362  PHE A CB  
2751  C CG  . PHE A 362  ? 1.8823 2.1440 1.4448 0.4747  0.2065  0.5178  362  PHE A CG  
2752  C CD1 . PHE A 362  ? 1.9240 2.2105 1.4767 0.4588  0.1768  0.5074  362  PHE A CD1 
2753  C CD2 . PHE A 362  ? 1.9603 2.1872 1.4985 0.4883  0.2251  0.5226  362  PHE A CD2 
2754  C CE1 . PHE A 362  ? 1.9936 2.2719 1.5126 0.4583  0.1651  0.5012  362  PHE A CE1 
2755  C CE2 . PHE A 362  ? 2.0209 2.2408 1.5250 0.4871  0.2147  0.5174  362  PHE A CE2 
2756  C CZ  . PHE A 362  ? 2.0335 2.2794 1.5276 0.4729  0.1844  0.5061  362  PHE A CZ  
2757  N N   . LEU A 363  ? 1.3679 1.5944 1.0197 0.4922  0.2810  0.5270  363  LEU A N   
2758  C CA  . LEU A 363  ? 1.3063 1.5494 0.9916 0.4972  0.2926  0.5311  363  LEU A CA  
2759  C C   . LEU A 363  ? 1.2523 1.5398 0.9532 0.5186  0.2866  0.5522  363  LEU A C   
2760  O O   . LEU A 363  ? 1.2471 1.5313 0.9356 0.5415  0.2908  0.5694  363  LEU A O   
2761  C CB  . LEU A 363  ? 1.2754 1.4758 0.9685 0.5055  0.3237  0.5279  363  LEU A CB  
2762  C CG  . LEU A 363  ? 1.1877 1.3435 0.8551 0.5134  0.3384  0.5290  363  LEU A CG  
2763  C CD1 . LEU A 363  ? 1.2195 1.3769 0.8832 0.5423  0.3488  0.5539  363  LEU A CD1 
2764  C CD2 . LEU A 363  ? 1.1773 1.2913 0.8526 0.5071  0.3622  0.5140  363  LEU A CD2 
2765  N N   . LYS A 364  ? 1.2593 1.5898 0.9862 0.5098  0.2752  0.5503  364  LYS A N   
2766  C CA  . LYS A 364  ? 1.3254 1.6989 1.0791 0.5303  0.2757  0.5665  364  LYS A CA  
2767  C C   . LYS A 364  ? 1.3738 1.7227 1.1479 0.5427  0.3055  0.5669  364  LYS A C   
2768  O O   . LYS A 364  ? 1.3469 1.6687 1.1236 0.5251  0.3166  0.5502  364  LYS A O   
2769  C CB  . LYS A 364  ? 1.3335 1.7600 1.1106 0.5115  0.2561  0.5601  364  LYS A CB  
2770  C CG  . LYS A 364  ? 1.3846 1.8301 1.1430 0.4914  0.2261  0.5536  364  LYS A CG  
2771  C CD  . LYS A 364  ? 1.4091 1.8121 1.1429 0.4645  0.2224  0.5341  364  LYS A CD  
2772  C CE  . LYS A 364  ? 1.4342 1.8576 1.1527 0.4435  0.1912  0.5259  364  LYS A CE  
2773  N NZ  . LYS A 364  ? 1.4687 1.9317 1.1825 0.4603  0.1735  0.5400  364  LYS A NZ  
2774  N N   . PRO A 365  ? 1.4377 1.7936 1.2250 0.5737  0.3181  0.5850  365  PRO A N   
2775  C CA  . PRO A 365  ? 1.4631 1.7927 1.2700 0.5864  0.3469  0.5840  365  PRO A CA  
2776  C C   . PRO A 365  ? 1.4907 1.8625 1.3363 0.5852  0.3495  0.5794  365  PRO A C   
2777  O O   . PRO A 365  ? 1.5079 1.9350 1.3697 0.5825  0.3307  0.5830  365  PRO A O   
2778  C CB  . PRO A 365  ? 1.4762 1.7895 1.2758 0.6209  0.3579  0.6065  365  PRO A CB  
2779  C CG  . PRO A 365  ? 1.4712 1.8025 1.2448 0.6252  0.3348  0.6187  365  PRO A CG  
2780  C CD  . PRO A 365  ? 1.4492 1.8273 1.2293 0.6002  0.3081  0.6068  365  PRO A CD  
2781  N N   . GLY A 366  ? 1.5346 1.8812 1.3956 0.5864  0.3735  0.5702  366  GLY A N   
2782  C CA  . GLY A 366  ? 1.6222 2.0053 1.5169 0.5815  0.3784  0.5622  366  GLY A CA  
2783  C C   . GLY A 366  ? 1.5297 1.9268 1.4212 0.5454  0.3653  0.5446  366  GLY A C   
2784  O O   . GLY A 366  ? 1.5257 1.9357 1.4365 0.5339  0.3742  0.5331  366  GLY A O   
2785  N N   . ILE A 367  ? 1.4451 1.8389 1.3110 0.5272  0.3439  0.5425  367  ILE A N   
2786  C CA  . ILE A 367  ? 1.3870 1.7852 1.2468 0.4933  0.3316  0.5263  367  ILE A CA  
2787  C C   . ILE A 367  ? 1.3692 1.7081 1.2068 0.4808  0.3429  0.5111  367  ILE A C   
2788  O O   . ILE A 367  ? 1.3865 1.6860 1.2062 0.4930  0.3514  0.5137  367  ILE A O   
2789  C CB  . ILE A 367  ? 1.3894 1.8182 1.2374 0.4784  0.3015  0.5291  367  ILE A CB  
2790  C CG1 . ILE A 367  ? 1.3681 1.8643 1.2472 0.4819  0.2912  0.5376  367  ILE A CG1 
2791  C CG2 . ILE A 367  ? 1.3742 1.7869 1.2056 0.4443  0.2893  0.5124  367  ILE A CG2 
2792  C CD1 . ILE A 367  ? 1.3666 1.8977 1.2381 0.4749  0.2625  0.5431  367  ILE A CD1 
2793  N N   . PRO A 368  ? 1.2987 1.6318 1.1379 0.4570  0.3441  0.4950  368  PRO A N   
2794  C CA  . PRO A 368  ? 1.2874 1.5660 1.1071 0.4475  0.3540  0.4796  368  PRO A CA  
2795  C C   . PRO A 368  ? 1.2408 1.5014 1.0307 0.4289  0.3321  0.4730  368  PRO A C   
2796  O O   . PRO A 368  ? 1.2586 1.5452 1.0450 0.4097  0.3103  0.4717  368  PRO A O   
2797  C CB  . PRO A 368  ? 1.2384 1.5222 1.0700 0.4305  0.3613  0.4662  368  PRO A CB  
2798  C CG  . PRO A 368  ? 1.2392 1.5832 1.0950 0.4273  0.3533  0.4750  368  PRO A CG  
2799  C CD  . PRO A 368  ? 1.2672 1.6391 1.1214 0.4356  0.3350  0.4897  368  PRO A CD  
2800  N N   . TYR A 369  ? 1.2186 1.4358 0.9883 0.4342  0.3383  0.4682  369  TYR A N   
2801  C CA  . TYR A 369  ? 1.2861 1.4857 1.0279 0.4203  0.3191  0.4611  369  TYR A CA  
2802  C C   . TYR A 369  ? 1.2528 1.4280 0.9848 0.3960  0.3138  0.4406  369  TYR A C   
2803  O O   . TYR A 369  ? 1.2499 1.3964 0.9853 0.3972  0.3316  0.4298  369  TYR A O   
2804  C CB  . TYR A 369  ? 1.2770 1.4426 1.0025 0.4369  0.3306  0.4644  369  TYR A CB  
2805  C CG  . TYR A 369  ? 1.3337 1.4836 1.0304 0.4268  0.3130  0.4575  369  TYR A CG  
2806  C CD1 . TYR A 369  ? 1.3901 1.5689 1.0770 0.4164  0.2858  0.4605  369  TYR A CD1 
2807  C CD2 . TYR A 369  ? 1.3821 1.4900 1.0626 0.4278  0.3238  0.4468  369  TYR A CD2 
2808  C CE1 . TYR A 369  ? 1.4004 1.5646 1.0608 0.4079  0.2697  0.4522  369  TYR A CE1 
2809  C CE2 . TYR A 369  ? 1.4124 1.5078 1.0676 0.4196  0.3087  0.4389  369  TYR A CE2 
2810  C CZ  . TYR A 369  ? 1.4394 1.5622 1.0838 0.4102  0.2815  0.4415  369  TYR A CZ  
2811  O OH  . TYR A 369  ? 1.4856 1.5955 1.1045 0.4029  0.2665  0.4317  369  TYR A OH  
2812  N N   . PRO A 370  ? 1.0571 1.2441 0.7775 0.3743  0.2888  0.4353  370  PRO A N   
2813  C CA  . PRO A 370  ? 1.0503 1.2148 0.7549 0.3496  0.2749  0.4179  370  PRO A CA  
2814  C C   . PRO A 370  ? 1.1760 1.3034 0.8548 0.3465  0.2660  0.4054  370  PRO A C   
2815  O O   . PRO A 370  ? 1.1834 1.3164 0.8522 0.3553  0.2588  0.4122  370  PRO A O   
2816  C CB  . PRO A 370  ? 1.0515 1.2512 0.7568 0.3320  0.2507  0.4233  370  PRO A CB  
2817  C CG  . PRO A 370  ? 1.0884 1.3347 0.8167 0.3474  0.2555  0.4418  370  PRO A CG  
2818  C CD  . PRO A 370  ? 1.0618 1.2954 0.7901 0.3743  0.2720  0.4495  370  PRO A CD  
2819  N N   . ILE A 371  ? 1.0505 1.1433 0.7178 0.3347  0.2650  0.3872  371  ILE A N   
2820  C CA  . ILE A 371  ? 1.0556 1.1158 0.7010 0.3334  0.2571  0.3735  371  ILE A CA  
2821  C C   . ILE A 371  ? 1.0926 1.1284 0.7224 0.3130  0.2391  0.3551  371  ILE A C   
2822  O O   . ILE A 371  ? 1.0839 1.0875 0.7076 0.3140  0.2458  0.3390  371  ILE A O   
2823  C CB  . ILE A 371  ? 1.0811 1.1108 0.7284 0.3496  0.2822  0.3663  371  ILE A CB  
2824  C CG1 . ILE A 371  ? 1.0653 1.1061 0.7212 0.3718  0.3006  0.3839  371  ILE A CG1 
2825  C CG2 . ILE A 371  ? 1.0604 1.0595 0.6875 0.3459  0.2743  0.3489  371  ILE A CG2 
2826  C CD1 . ILE A 371  ? 1.0687 1.0770 0.7272 0.3837  0.3259  0.3764  371  ILE A CD1 
2827  N N   . LYS A 372  ? 1.0773 1.1266 0.7007 0.2947  0.2163  0.3567  372  LYS A N   
2828  C CA  . LYS A 372  ? 1.0614 1.0823 0.6672 0.2757  0.1978  0.3404  372  LYS A CA  
2829  C C   . LYS A 372  ? 1.0680 1.0561 0.6536 0.2771  0.1865  0.3228  372  LYS A C   
2830  O O   . LYS A 372  ? 1.1489 1.1408 0.7218 0.2719  0.1668  0.3220  372  LYS A O   
2831  C CB  . LYS A 372  ? 1.0699 1.1088 0.6706 0.2548  0.1742  0.3466  372  LYS A CB  
2832  C CG  . LYS A 372  ? 1.1395 1.2259 0.7600 0.2557  0.1777  0.3662  372  LYS A CG  
2833  C CD  . LYS A 372  ? 1.1782 1.2837 0.7931 0.2350  0.1514  0.3704  372  LYS A CD  
2834  C CE  . LYS A 372  ? 1.5613 1.7193 1.1964 0.2405  0.1517  0.3881  372  LYS A CE  
2835  N NZ  . LYS A 372  ? 1.5482 1.7403 1.1998 0.2227  0.1487  0.3977  372  LYS A NZ  
2836  N N   . VAL A 373  ? 1.0637 1.0217 0.6472 0.2833  0.1978  0.3071  373  VAL A N   
2837  C CA  . VAL A 373  ? 1.2259 1.1556 0.7925 0.2839  0.1863  0.2881  373  VAL A CA  
2838  C C   . VAL A 373  ? 1.1820 1.0897 0.7322 0.2663  0.1608  0.2755  373  VAL A C   
2839  O O   . VAL A 373  ? 1.1867 1.0983 0.7383 0.2539  0.1564  0.2819  373  VAL A O   
2840  C CB  . VAL A 373  ? 1.0639 0.9722 0.6364 0.2972  0.2074  0.2743  373  VAL A CB  
2841  C CG1 . VAL A 373  ? 1.0579 0.9829 0.6482 0.3125  0.2351  0.2888  373  VAL A CG1 
2842  C CG2 . VAL A 373  ? 1.0595 0.9454 0.6336 0.2913  0.2088  0.2596  373  VAL A CG2 
2843  N N   . GLN A 374  ? 1.1220 1.0060 0.6560 0.2651  0.1444  0.2581  374  GLN A N   
2844  C CA  . GLN A 374  ? 1.1570 1.0181 0.6740 0.2491  0.1180  0.2482  374  GLN A CA  
2845  C C   . GLN A 374  ? 1.2585 1.0858 0.7637 0.2538  0.1085  0.2230  374  GLN A C   
2846  O O   . GLN A 374  ? 1.3373 1.1626 0.8362 0.2607  0.1032  0.2137  374  GLN A O   
2847  C CB  . GLN A 374  ? 1.1475 1.0231 0.6553 0.2372  0.0963  0.2575  374  GLN A CB  
2848  C CG  . GLN A 374  ? 1.2187 1.0644 0.7055 0.2248  0.0670  0.2430  374  GLN A CG  
2849  C CD  . GLN A 374  ? 1.3028 1.1640 0.7827 0.2104  0.0459  0.2524  374  GLN A CD  
2850  O OE1 . GLN A 374  ? 1.3237 1.1902 0.7963 0.2144  0.0352  0.2468  374  GLN A OE1 
2851  N NE2 . GLN A 374  ? 1.3275 1.1979 0.8100 0.1928  0.0404  0.2663  374  GLN A NE2 
2852  N N   . VAL A 375  ? 1.2617 1.0642 0.7638 0.2511  0.1064  0.2110  375  VAL A N   
2853  C CA  . VAL A 375  ? 1.2380 1.0119 0.7333 0.2584  0.0991  0.1854  375  VAL A CA  
2854  C C   . VAL A 375  ? 1.2992 1.0476 0.7730 0.2491  0.0667  0.1743  375  VAL A C   
2855  O O   . VAL A 375  ? 1.3157 1.0567 0.7778 0.2338  0.0500  0.1842  375  VAL A O   
2856  C CB  . VAL A 375  ? 1.1495 0.9071 0.6508 0.2619  0.1088  0.1741  375  VAL A CB  
2857  C CG1 . VAL A 375  ? 1.1359 0.8675 0.6314 0.2694  0.0975  0.1466  375  VAL A CG1 
2858  C CG2 . VAL A 375  ? 1.1014 0.8783 0.6250 0.2722  0.1412  0.1802  375  VAL A CG2 
2859  N N   . LYS A 376  ? 1.3121 1.0465 0.7810 0.2584  0.0589  0.1531  376  LYS A N   
2860  C CA  . LYS A 376  ? 1.3114 1.0194 0.7607 0.2531  0.0282  0.1388  376  LYS A CA  
2861  C C   . LYS A 376  ? 1.2555 0.9416 0.7053 0.2659  0.0247  0.1104  376  LYS A C   
2862  O O   . LYS A 376  ? 1.1892 0.8871 0.6551 0.2783  0.0469  0.1016  376  LYS A O   
2863  C CB  . LYS A 376  ? 1.3410 1.0633 0.7834 0.2512  0.0184  0.1424  376  LYS A CB  
2864  C CG  . LYS A 376  ? 1.3859 1.1148 0.8193 0.2332  0.0024  0.1615  376  LYS A CG  
2865  C CD  . LYS A 376  ? 1.4001 1.1569 0.8333 0.2334  0.0012  0.1696  376  LYS A CD  
2866  C CE  . LYS A 376  ? 1.4177 1.1837 0.8450 0.2142  -0.0156 0.1864  376  LYS A CE  
2867  N NZ  . LYS A 376  ? 1.4318 1.2397 0.8687 0.2176  -0.0043 0.2022  376  LYS A NZ  
2868  N N   . ASP A 377  ? 1.3041 0.9582 0.7374 0.2627  -0.0029 0.0957  377  ASP A N   
2869  C CA  . ASP A 377  ? 1.3563 0.9910 0.7912 0.2760  -0.0093 0.0669  377  ASP A CA  
2870  C C   . ASP A 377  ? 1.4306 1.0638 0.8602 0.2828  -0.0208 0.0497  377  ASP A C   
2871  O O   . ASP A 377  ? 1.4608 1.0986 0.8793 0.2754  -0.0324 0.0582  377  ASP A O   
2872  C CB  . ASP A 377  ? 1.3830 0.9805 0.8019 0.2723  -0.0346 0.0582  377  ASP A CB  
2873  C CG  . ASP A 377  ? 1.4477 1.0245 0.8440 0.2575  -0.0616 0.0685  377  ASP A CG  
2874  O OD1 . ASP A 377  ? 1.4628 1.0596 0.8588 0.2477  -0.0580 0.0860  377  ASP A OD1 
2875  O OD2 . ASP A 377  ? 1.5055 1.0459 0.8846 0.2556  -0.0866 0.0594  377  ASP A OD2 
2876  N N   . SER A 378  ? 1.4866 1.1144 0.9250 0.2972  -0.0183 0.0234  378  SER A N   
2877  C CA  . SER A 378  ? 1.5211 1.1475 0.9559 0.3062  -0.0282 0.0014  378  SER A CA  
2878  C C   . SER A 378  ? 1.2512 0.8521 0.6622 0.2981  -0.0624 -0.0005 378  SER A C   
2879  O O   . SER A 378  ? 1.2663 0.8620 0.6714 0.3052  -0.0751 -0.0202 378  SER A O   
2880  C CB  . SER A 378  ? 1.5489 1.1694 0.9978 0.3217  -0.0246 -0.0292 378  SER A CB  
2881  O OG  . SER A 378  ? 1.5408 1.1464 0.9954 0.3225  -0.0257 -0.0319 378  SER A OG  
2882  N N   . LEU A 379  ? 1.2925 0.8782 0.6905 0.2826  -0.0759 0.0199  379  LEU A N   
2883  C CA  . LEU A 379  ? 1.3741 0.9348 0.7505 0.2714  -0.1064 0.0215  379  LEU A CA  
2884  C C   . LEU A 379  ? 1.4702 1.0491 0.8424 0.2537  -0.1036 0.0500  379  LEU A C   
2885  O O   . LEU A 379  ? 1.5336 1.0916 0.8896 0.2390  -0.1266 0.0572  379  LEU A O   
2886  C CB  . LEU A 379  ? 1.3826 0.8987 0.7434 0.2675  -0.1320 0.0163  379  LEU A CB  
2887  C CG  . LEU A 379  ? 1.4097 0.8963 0.7632 0.2814  -0.1554 -0.0152 379  LEU A CG  
2888  C CD1 . LEU A 379  ? 1.4288 0.8741 0.7713 0.2853  -0.1756 -0.0240 379  LEU A CD1 
2889  C CD2 . LEU A 379  ? 1.4538 0.9285 0.7922 0.2750  -0.1774 -0.0198 379  LEU A CD2 
2890  N N   . ASP A 380  ? 1.4902 1.1075 0.8779 0.2551  -0.0757 0.0658  380  ASP A N   
2891  C CA  . ASP A 380  ? 1.5485 1.1898 0.9363 0.2407  -0.0712 0.0925  380  ASP A CA  
2892  C C   . ASP A 380  ? 1.5915 1.2173 0.9701 0.2207  -0.0844 0.1113  380  ASP A C   
2893  O O   . ASP A 380  ? 1.6041 1.2424 0.9788 0.2061  -0.0921 0.1264  380  ASP A O   
2894  C CB  . ASP A 380  ? 1.6384 1.2923 1.0182 0.2393  -0.0826 0.0887  380  ASP A CB  
2895  C CG  . ASP A 380  ? 1.7073 1.3893 1.0961 0.2560  -0.0620 0.0804  380  ASP A CG  
2896  O OD1 . ASP A 380  ? 1.6917 1.4073 1.0917 0.2582  -0.0387 0.0989  380  ASP A OD1 
2897  O OD2 . ASP A 380  ? 1.7843 1.4540 1.1681 0.2672  -0.0695 0.0552  380  ASP A OD2 
2898  N N   . GLN A 381  ? 1.6213 1.2214 0.9958 0.2190  -0.0874 0.1102  381  GLN A N   
2899  C CA  . GLN A 381  ? 1.6458 1.2428 1.0151 0.2003  -0.0887 0.1334  381  GLN A CA  
2900  C C   . GLN A 381  ? 1.5774 1.2073 0.9661 0.2040  -0.0573 0.1487  381  GLN A C   
2901  O O   . GLN A 381  ? 1.5357 1.1795 0.9393 0.2209  -0.0371 0.1392  381  GLN A O   
2902  C CB  . GLN A 381  ? 1.7269 1.2781 1.0765 0.1936  -0.1091 0.1292  381  GLN A CB  
2903  C CG  . GLN A 381  ? 1.8281 1.3383 1.1575 0.1916  -0.1413 0.1131  381  GLN A CG  
2904  C CD  . GLN A 381  ? 1.9049 1.3908 1.2327 0.2127  -0.1484 0.0853  381  GLN A CD  
2905  O OE1 . GLN A 381  ? 1.9684 1.4110 1.2780 0.2130  -0.1715 0.0759  381  GLN A OE1 
2906  N NE2 . GLN A 381  ? 1.8895 1.4035 1.2370 0.2305  -0.1282 0.0722  381  GLN A NE2 
2907  N N   . LEU A 382  ? 1.5162 1.1587 0.9055 0.1877  -0.0525 0.1718  382  LEU A N   
2908  C CA  . LEU A 382  ? 1.4454 1.1189 0.8530 0.1911  -0.0238 0.1862  382  LEU A CA  
2909  C C   . LEU A 382  ? 1.4626 1.1134 0.8666 0.1973  -0.0192 0.1772  382  LEU A C   
2910  O O   . LEU A 382  ? 1.5365 1.1508 0.9204 0.1911  -0.0402 0.1708  382  LEU A O   
2911  C CB  . LEU A 382  ? 1.4338 1.1289 0.8435 0.1717  -0.0220 0.2111  382  LEU A CB  
2912  C CG  . LEU A 382  ? 1.4246 1.1572 0.8474 0.1731  -0.0168 0.2193  382  LEU A CG  
2913  C CD1 . LEU A 382  ? 1.4385 1.2004 0.8684 0.1548  -0.0148 0.2427  382  LEU A CD1 
2914  C CD2 . LEU A 382  ? 1.3758 1.1344 0.8179 0.1946  0.0103  0.2168  382  LEU A CD2 
2915  N N   . VAL A 383  ? 1.4055 1.0755 0.8278 0.2103  0.0071  0.1757  383  VAL A N   
2916  C CA  . VAL A 383  ? 1.3700 1.0217 0.7895 0.2153  0.0117  0.1668  383  VAL A CA  
2917  C C   . VAL A 383  ? 1.3626 1.0415 0.7980 0.2153  0.0393  0.1812  383  VAL A C   
2918  O O   . VAL A 383  ? 1.3455 1.0533 0.8025 0.2248  0.0628  0.1848  383  VAL A O   
2919  C CB  . VAL A 383  ? 1.3056 0.9416 0.7296 0.2336  0.0104  0.1393  383  VAL A CB  
2920  C CG1 . VAL A 383  ? 1.3199 0.9627 0.7480 0.2405  0.0056  0.1298  383  VAL A CG1 
2921  C CG2 . VAL A 383  ? 1.2123 0.8654 0.6574 0.2459  0.0385  0.1337  383  VAL A CG2 
2922  N N   . GLY A 384  ? 1.3940 1.0625 0.8169 0.2040  0.0361  0.1902  384  GLY A N   
2923  C CA  . GLY A 384  ? 1.3893 1.0839 0.8251 0.2022  0.0608  0.2040  384  GLY A CA  
2924  C C   . GLY A 384  ? 1.4143 1.1004 0.8546 0.2145  0.0733  0.1890  384  GLY A C   
2925  O O   . GLY A 384  ? 1.4492 1.1075 0.8799 0.2222  0.0596  0.1689  384  GLY A O   
2926  N N   . GLY A 385  ? 1.4035 1.1147 0.8598 0.2169  0.0990  0.1973  385  GLY A N   
2927  C CA  . GLY A 385  ? 1.3972 1.1031 0.8586 0.2268  0.1122  0.1833  385  GLY A CA  
2928  C C   . GLY A 385  ? 1.3681 1.0750 0.8501 0.2449  0.1242  0.1627  385  GLY A C   
2929  O O   . GLY A 385  ? 1.3789 1.0730 0.8625 0.2533  0.1263  0.1435  385  GLY A O   
2930  N N   . VAL A 386  ? 1.3262 1.0487 0.8234 0.2504  0.1318  0.1659  386  VAL A N   
2931  C CA  . VAL A 386  ? 1.2843 1.0111 0.8026 0.2659  0.1487  0.1495  386  VAL A CA  
2932  C C   . VAL A 386  ? 1.1945 0.9483 0.7361 0.2712  0.1801  0.1615  386  VAL A C   
2933  O O   . VAL A 386  ? 1.1856 0.9604 0.7304 0.2662  0.1864  0.1832  386  VAL A O   
2934  C CB  . VAL A 386  ? 1.1563 0.8807 0.6752 0.2711  0.1395  0.1424  386  VAL A CB  
2935  C CG1 . VAL A 386  ? 1.1344 0.8487 0.6650 0.2840  0.1450  0.1157  386  VAL A CG1 
2936  C CG2 . VAL A 386  ? 1.1813 0.8863 0.6756 0.2614  0.1075  0.1428  386  VAL A CG2 
2937  N N   . PRO A 387  ? 1.1390 0.8920 0.6978 0.2816  0.1994  0.1465  387  PRO A N   
2938  C CA  . PRO A 387  ? 1.1680 0.9434 0.7490 0.2876  0.2290  0.1585  387  PRO A CA  
2939  C C   . PRO A 387  ? 1.1950 0.9797 0.7877 0.2956  0.2387  0.1632  387  PRO A C   
2940  O O   . PRO A 387  ? 1.2215 0.9939 0.8116 0.2993  0.2305  0.1476  387  PRO A O   
2941  C CB  . PRO A 387  ? 1.1713 0.9387 0.7659 0.2948  0.2449  0.1383  387  PRO A CB  
2942  C CG  . PRO A 387  ? 1.0873 0.8301 0.6665 0.2934  0.2209  0.1145  387  PRO A CG  
2943  C CD  . PRO A 387  ? 1.1011 0.8359 0.6636 0.2890  0.1969  0.1185  387  PRO A CD  
2944  N N   . VAL A 388  ? 1.1894 0.9960 0.7941 0.2991  0.2562  0.1838  388  VAL A N   
2945  C CA  . VAL A 388  ? 1.1763 0.9924 0.7879 0.3070  0.2652  0.1922  388  VAL A CA  
2946  C C   . VAL A 388  ? 1.2005 1.0306 0.8344 0.3180  0.2966  0.2041  388  VAL A C   
2947  O O   . VAL A 388  ? 1.2063 1.0558 0.8454 0.3179  0.3030  0.2235  388  VAL A O   
2948  C CB  . VAL A 388  ? 1.1771 1.0074 0.7742 0.2997  0.2458  0.2108  388  VAL A CB  
2949  C CG1 . VAL A 388  ? 1.1866 1.0392 0.7935 0.3084  0.2605  0.2306  388  VAL A CG1 
2950  C CG2 . VAL A 388  ? 1.1710 0.9849 0.7494 0.2946  0.2200  0.1976  388  VAL A CG2 
2951  N N   . THR A 389  ? 1.1847 1.0050 0.8325 0.3274  0.3166  0.1927  389  THR A N   
2952  C CA  . THR A 389  ? 1.1944 1.0229 0.8619 0.3383  0.3463  0.2054  389  THR A CA  
2953  C C   . THR A 389  ? 1.2156 1.0590 0.8806 0.3453  0.3504  0.2284  389  THR A C   
2954  O O   . THR A 389  ? 1.2723 1.1163 0.9227 0.3432  0.3353  0.2289  389  THR A O   
2955  C CB  . THR A 389  ? 1.3515 1.1625 1.0372 0.3446  0.3702  0.1863  389  THR A CB  
2956  O OG1 . THR A 389  ? 1.3544 1.1503 1.0348 0.3403  0.3585  0.1614  389  THR A OG1 
2957  C CG2 . THR A 389  ? 1.3441 1.1530 1.0443 0.3453  0.3840  0.1796  389  THR A CG2 
2958  N N   . LEU A 390  ? 1.1601 1.0158 0.8386 0.3546  0.3697  0.2469  390  LEU A N   
2959  C CA  . LEU A 390  ? 1.1338 1.0048 0.8087 0.3630  0.3722  0.2699  390  LEU A CA  
2960  C C   . LEU A 390  ? 1.1966 1.0620 0.8877 0.3777  0.4025  0.2798  390  LEU A C   
2961  O O   . LEU A 390  ? 1.2572 1.1341 0.9619 0.3852  0.4145  0.2935  390  LEU A O   
2962  C CB  . LEU A 390  ? 1.0845 0.9834 0.7569 0.3600  0.3586  0.2893  390  LEU A CB  
2963  C CG  . LEU A 390  ? 1.1029 1.0209 0.7779 0.3728  0.3658  0.3141  390  LEU A CG  
2964  C CD1 . LEU A 390  ? 1.1639 1.0863 0.8187 0.3699  0.3469  0.3171  390  LEU A CD1 
2965  C CD2 . LEU A 390  ? 1.0561 1.0042 0.7411 0.3750  0.3639  0.3327  390  LEU A CD2 
2966  N N   . ASN A 391  ? 1.1812 1.0284 0.8716 0.3820  0.4157  0.2728  391  ASN A N   
2967  C CA  . ASN A 391  ? 1.2322 1.0692 0.9356 0.3951  0.4449  0.2838  391  ASN A CA  
2968  C C   . ASN A 391  ? 1.2832 1.1350 0.9754 0.4055  0.4435  0.3110  391  ASN A C   
2969  O O   . ASN A 391  ? 1.3191 1.1787 0.9920 0.4018  0.4260  0.3128  391  ASN A O   
2970  C CB  . ASN A 391  ? 1.2801 1.0920 0.9869 0.3933  0.4609  0.2658  391  ASN A CB  
2971  C CG  . ASN A 391  ? 1.3112 1.1075 1.0361 0.3874  0.4707  0.2407  391  ASN A CG  
2972  O OD1 . ASN A 391  ? 1.2966 1.0946 1.0184 0.3774  0.4525  0.2218  391  ASN A OD1 
2973  N ND2 . ASN A 391  ? 1.3413 1.1207 1.0844 0.3938  0.4992  0.2399  391  ASN A ND2 
2974  N N   . ALA A 392  ? 1.2919 1.1474 0.9953 0.4195  0.4608  0.3312  392  ALA A N   
2975  C CA  . ALA A 392  ? 1.2957 1.1679 0.9879 0.4318  0.4574  0.3586  392  ALA A CA  
2976  C C   . ALA A 392  ? 1.2858 1.1419 0.9866 0.4487  0.4853  0.3752  392  ALA A C   
2977  O O   . ALA A 392  ? 1.2907 1.1280 1.0106 0.4514  0.5061  0.3675  392  ALA A O   
2978  C CB  . ALA A 392  ? 1.2922 1.1985 0.9869 0.4325  0.4387  0.3721  392  ALA A CB  
2979  N N   . GLN A 393  ? 1.3123 1.1746 0.9981 0.4607  0.4854  0.3981  393  GLN A N   
2980  C CA  . GLN A 393  ? 1.3944 1.2328 1.0826 0.4762  0.5129  0.4139  393  GLN A CA  
2981  C C   . GLN A 393  ? 1.4206 1.2759 1.0956 0.4944  0.5083  0.4455  393  GLN A C   
2982  O O   . GLN A 393  ? 1.3923 1.2723 1.0479 0.4930  0.4856  0.4529  393  GLN A O   
2983  C CB  . GLN A 393  ? 1.4237 1.2308 1.1031 0.4686  0.5293  0.4006  393  GLN A CB  
2984  C CG  . GLN A 393  ? 1.4500 1.2254 1.1328 0.4802  0.5608  0.4138  393  GLN A CG  
2985  C CD  . GLN A 393  ? 1.4758 1.2551 1.1351 0.4959  0.5612  0.4447  393  GLN A CD  
2986  O OE1 . GLN A 393  ? 1.5004 1.2618 1.1627 0.5119  0.5807  0.4656  393  GLN A OE1 
2987  N NE2 . GLN A 393  ? 1.4682 1.2702 1.1030 0.4923  0.5387  0.4479  393  GLN A NE2 
2988  N N   . THR A 394  ? 1.4705 1.3114 1.1563 0.5121  0.5294  0.4631  394  THR A N   
2989  C CA  . THR A 394  ? 1.5177 1.3816 1.2021 0.5320  0.5226  0.4908  394  THR A CA  
2990  C C   . THR A 394  ? 1.6650 1.5017 1.3457 0.5536  0.5464  0.5150  394  THR A C   
2991  O O   . THR A 394  ? 1.7200 1.5203 1.4136 0.5550  0.5727  0.5095  394  THR A O   
2992  C CB  . THR A 394  ? 1.4246 1.3152 1.1355 0.5334  0.5149  0.4868  394  THR A CB  
2993  O OG1 . THR A 394  ? 1.3821 1.3113 1.0864 0.5215  0.4850  0.4822  394  THR A OG1 
2994  C CG2 . THR A 394  ? 1.4360 1.3357 1.1591 0.5586  0.5229  0.5115  394  THR A CG2 
2995  N N   . ILE A 395  ? 1.7204 1.5733 1.3826 0.5703  0.5366  0.5417  395  ILE A N   
2996  C CA  . ILE A 395  ? 1.7899 1.6193 1.4497 0.5945  0.5563  0.5681  395  ILE A CA  
2997  C C   . ILE A 395  ? 1.8551 1.7187 1.5222 0.6170  0.5421  0.5907  395  ILE A C   
2998  O O   . ILE A 395  ? 1.8531 1.7612 1.5160 0.6145  0.5147  0.5920  395  ILE A O   
2999  C CB  . ILE A 395  ? 1.8137 1.6183 1.4394 0.5986  0.5654  0.5840  395  ILE A CB  
3000  C CG1 . ILE A 395  ? 1.8034 1.6455 1.4021 0.6051  0.5379  0.5998  395  ILE A CG1 
3001  C CG2 . ILE A 395  ? 1.8145 1.5913 1.4337 0.5759  0.5785  0.5605  395  ILE A CG2 
3002  C CD1 . ILE A 395  ? 1.8496 1.6771 1.4221 0.6287  0.5458  0.6330  395  ILE A CD1 
3003  N N   . ASP A 396  ? 1.9059 1.7472 1.5852 0.6390  0.5615  0.6075  396  ASP A N   
3004  C CA  . ASP A 396  ? 1.9269 1.7964 1.6204 0.6641  0.5529  0.6272  396  ASP A CA  
3005  C C   . ASP A 396  ? 1.9516 1.8333 1.6147 0.6816  0.5398  0.6556  396  ASP A C   
3006  O O   . ASP A 396  ? 1.9817 1.8388 1.6131 0.6771  0.5450  0.6623  396  ASP A O   
3007  C CB  . ASP A 396  ? 1.9920 1.8251 1.7069 0.6825  0.5802  0.6340  396  ASP A CB  
3008  C CG  . ASP A 396  ? 2.0523 1.9190 1.8023 0.6948  0.5744  0.6309  396  ASP A CG  
3009  O OD1 . ASP A 396  ? 2.1079 1.9540 1.8748 0.7173  0.5914  0.6417  396  ASP A OD1 
3010  O OD2 . ASP A 396  ? 2.0374 1.9509 1.7982 0.6814  0.5532  0.6172  396  ASP A OD2 
3011  N N   . VAL A 397  ? 1.9663 1.8877 1.6384 0.7020  0.5226  0.6720  397  VAL A N   
3012  C CA  . VAL A 397  ? 2.0267 1.9535 1.6701 0.7247  0.5132  0.7021  397  VAL A CA  
3013  C C   . VAL A 397  ? 2.0929 1.9628 1.7281 0.7453  0.5422  0.7225  397  VAL A C   
3014  O O   . VAL A 397  ? 2.1250 1.9755 1.7264 0.7593  0.5445  0.7468  397  VAL A O   
3015  C CB  . VAL A 397  ? 2.0286 2.0132 1.6868 0.7442  0.4879  0.7149  397  VAL A CB  
3016  C CG1 . VAL A 397  ? 2.0385 2.0164 1.7272 0.7709  0.5019  0.7257  397  VAL A CG1 
3017  C CG2 . VAL A 397  ? 2.0637 2.0650 1.6852 0.7591  0.4692  0.7393  397  VAL A CG2 
3018  N N   . ASN A 398  ? 2.1085 1.9501 1.7736 0.7458  0.5648  0.7114  398  ASN A N   
3019  C CA  . ASN A 398  ? 2.1626 1.9447 1.8261 0.7619  0.5948  0.7259  398  ASN A CA  
3020  C C   . ASN A 398  ? 2.1646 1.8966 1.8040 0.7414  0.6161  0.7194  398  ASN A C   
3021  O O   . ASN A 398  ? 2.1651 1.8423 1.8033 0.7474  0.6442  0.7272  398  ASN A O   
3022  C CB  . ASN A 398  ? 2.1814 1.9536 1.8875 0.7651  0.6105  0.7097  398  ASN A CB  
3023  C CG  . ASN A 398  ? 2.2583 1.9926 1.9718 0.7965  0.6296  0.7322  398  ASN A CG  
3024  O OD1 . ASN A 398  ? 2.3233 2.0450 2.0110 0.8193  0.6273  0.7629  398  ASN A OD1 
3025  N ND2 . ASN A 398  ? 2.2474 1.9623 1.9951 0.7989  0.6478  0.7169  398  ASN A ND2 
3026  N N   . GLN A 399  ? 2.1526 1.9041 1.7751 0.7164  0.6029  0.7035  399  GLN A N   
3027  C CA  . GLN A 399  ? 2.1868 1.8998 1.7874 0.6956  0.6208  0.6945  399  GLN A CA  
3028  C C   . GLN A 399  ? 2.1817 1.8594 1.8093 0.6766  0.6458  0.6674  399  GLN A C   
3029  O O   . GLN A 399  ? 2.1946 1.8291 1.8104 0.6652  0.6692  0.6642  399  GLN A O   
3030  C CB  . GLN A 399  ? 2.2565 1.9324 1.8201 0.7119  0.6350  0.7265  399  GLN A CB  
3031  C CG  . GLN A 399  ? 2.2838 1.9953 1.8113 0.7205  0.6090  0.7451  399  GLN A CG  
3032  C CD  . GLN A 399  ? 2.2614 2.0023 1.7771 0.6929  0.5921  0.7207  399  GLN A CD  
3033  O OE1 . GLN A 399  ? 2.2766 1.9931 1.7689 0.6769  0.6051  0.7148  399  GLN A OE1 
3034  N NE2 . GLN A 399  ? 2.2192 2.0126 1.7517 0.6870  0.5634  0.7060  399  GLN A NE2 
3035  N N   . GLU A 400  ? 2.1553 1.8543 1.8187 0.6727  0.6402  0.6472  400  GLU A N   
3036  C CA  . GLU A 400  ? 2.1373 1.8129 1.8281 0.6541  0.6584  0.6173  400  GLU A CA  
3037  C C   . GLU A 400  ? 2.0383 1.7458 1.7329 0.6265  0.6401  0.5869  400  GLU A C   
3038  O O   . GLU A 400  ? 2.0014 1.7551 1.6915 0.6255  0.6124  0.5875  400  GLU A O   
3039  C CB  . GLU A 400  ? 2.1617 1.8403 1.8878 0.6694  0.6642  0.6145  400  GLU A CB  
3040  C CG  . GLU A 400  ? 2.2326 1.8599 1.9793 0.6665  0.6958  0.6019  400  GLU A CG  
3041  C CD  . GLU A 400  ? 2.3047 1.9270 2.0786 0.6911  0.7042  0.6096  400  GLU A CD  
3042  O OE1 . GLU A 400  ? 2.3542 1.9283 2.1280 0.7066  0.7275  0.6250  400  GLU A OE1 
3043  O OE2 . GLU A 400  ? 2.3066 1.9728 2.1013 0.6948  0.6877  0.6003  400  GLU A OE2 
3044  N N   . THR A 401  ? 1.9990 1.6821 1.7020 0.6043  0.6544  0.5602  401  THR A N   
3045  C CA  . THR A 401  ? 1.9019 1.6124 1.6085 0.5800  0.6362  0.5313  401  THR A CA  
3046  C C   . THR A 401  ? 1.8222 1.5426 1.5612 0.5729  0.6356  0.5073  401  THR A C   
3047  O O   . THR A 401  ? 1.8566 1.5640 1.6177 0.5858  0.6503  0.5102  401  THR A O   
3048  C CB  . THR A 401  ? 1.9000 1.5855 1.5977 0.5579  0.6477  0.5106  401  THR A CB  
3049  O OG1 . THR A 401  ? 1.9021 1.5515 1.6245 0.5522  0.6741  0.4939  401  THR A OG1 
3050  C CG2 . THR A 401  ? 1.9482 1.6172 1.6127 0.5609  0.6546  0.5301  401  THR A CG2 
3051  N N   . SER A 402  ? 1.7323 1.4736 1.4724 0.5517  0.6191  0.4825  402  SER A N   
3052  C CA  . SER A 402  ? 1.6368 1.3892 1.4020 0.5414  0.6159  0.4576  402  SER A CA  
3053  C C   . SER A 402  ? 1.5445 1.3027 1.3032 0.5164  0.6030  0.4299  402  SER A C   
3054  O O   . SER A 402  ? 1.4868 1.2700 1.2269 0.5088  0.5795  0.4310  402  SER A O   
3055  C CB  . SER A 402  ? 1.6321 1.4272 1.4066 0.5513  0.5967  0.4674  402  SER A CB  
3056  O OG  . SER A 402  ? 1.6263 1.4548 1.3795 0.5490  0.5703  0.4788  402  SER A OG  
3057  N N   . ASP A 403  ? 1.5087 1.2433 1.2832 0.5044  0.6177  0.4043  403  ASP A N   
3058  C CA  . ASP A 403  ? 1.4756 1.2164 1.2470 0.4829  0.6044  0.3763  403  ASP A CA  
3059  C C   . ASP A 403  ? 1.4175 1.1805 1.2032 0.4762  0.5906  0.3597  403  ASP A C   
3060  O O   . ASP A 403  ? 1.4281 1.1772 1.2330 0.4714  0.6028  0.3394  403  ASP A O   
3061  C CB  . ASP A 403  ? 1.5322 1.2384 1.3112 0.4723  0.6259  0.3558  403  ASP A CB  
3062  C CG  . ASP A 403  ? 1.5901 1.2885 1.3476 0.4661  0.6260  0.3587  403  ASP A CG  
3063  O OD1 . ASP A 403  ? 1.5586 1.2793 1.3000 0.4564  0.6019  0.3512  403  ASP A OD1 
3064  O OD2 . ASP A 403  ? 1.6521 1.3206 1.4087 0.4707  0.6511  0.3683  403  ASP A OD2 
3065  N N   . LEU A 404  ? 1.3680 1.1659 1.1429 0.4749  0.5648  0.3684  404  LEU A N   
3066  C CA  . LEU A 404  ? 1.3084 1.1309 1.0912 0.4664  0.5486  0.3561  404  LEU A CA  
3067  C C   . LEU A 404  ? 1.3099 1.1183 1.1010 0.4509  0.5506  0.3245  404  LEU A C   
3068  O O   . LEU A 404  ? 1.3358 1.1211 1.1241 0.4422  0.5570  0.3077  404  LEU A O   
3069  C CB  . LEU A 404  ? 1.2240 1.0782 0.9876 0.4590  0.5184  0.3637  404  LEU A CB  
3070  C CG  . LEU A 404  ? 1.1890 1.0683 0.9509 0.4752  0.5134  0.3930  404  LEU A CG  
3071  C CD1 . LEU A 404  ? 1.1226 1.0367 0.8698 0.4665  0.4832  0.3989  404  LEU A CD1 
3072  C CD2 . LEU A 404  ? 1.1395 1.0278 0.9253 0.4869  0.5261  0.3976  404  LEU A CD2 
3073  N N   . ASP A 405  ? 1.2769 1.1017 1.0783 0.4479  0.5450  0.3163  405  ASP A N   
3074  C CA  . ASP A 405  ? 1.2414 1.0603 1.0456 0.4330  0.5398  0.2879  405  ASP A CA  
3075  C C   . ASP A 405  ? 1.1703 1.0075 0.9536 0.4186  0.5095  0.2844  405  ASP A C   
3076  O O   . ASP A 405  ? 1.1523 1.0155 0.9260 0.4197  0.4931  0.3028  405  ASP A O   
3077  C CB  . ASP A 405  ? 1.2952 1.1217 1.1171 0.4366  0.5493  0.2807  405  ASP A CB  
3078  C CG  . ASP A 405  ? 1.5095 1.3061 1.3526 0.4446  0.5789  0.2691  405  ASP A CG  
3079  O OD1 . ASP A 405  ? 1.5391 1.3110 1.3832 0.4362  0.5854  0.2496  405  ASP A OD1 
3080  O OD2 . ASP A 405  ? 1.4904 1.2886 1.3501 0.4588  0.5952  0.2778  405  ASP A OD2 
3081  N N   . PRO A 406  ? 1.1546 0.9778 0.9315 0.4055  0.5015  0.2603  406  PRO A N   
3082  C CA  . PRO A 406  ? 1.1343 0.9654 0.8905 0.3927  0.4737  0.2542  406  PRO A CA  
3083  C C   . PRO A 406  ? 1.1850 1.0335 0.9365 0.3840  0.4568  0.2507  406  PRO A C   
3084  O O   . PRO A 406  ? 1.2410 1.0861 1.0035 0.3831  0.4660  0.2381  406  PRO A O   
3085  C CB  . PRO A 406  ? 1.1290 0.9363 0.8865 0.3850  0.4764  0.2266  406  PRO A CB  
3086  C CG  . PRO A 406  ? 1.1528 0.9402 0.9315 0.3928  0.5068  0.2208  406  PRO A CG  
3087  C CD  . PRO A 406  ? 1.1505 0.9480 0.9416 0.4031  0.5191  0.2359  406  PRO A CD  
3088  N N   . SER A 407  ? 1.1897 1.0564 0.9244 0.3769  0.4327  0.2612  407  SER A N   
3089  C CA  . SER A 407  ? 1.2340 1.1172 0.9625 0.3667  0.4171  0.2605  407  SER A CA  
3090  C C   . SER A 407  ? 1.2437 1.1151 0.9524 0.3526  0.3930  0.2444  407  SER A C   
3091  O O   . SER A 407  ? 1.2596 1.1179 0.9606 0.3524  0.3872  0.2381  407  SER A O   
3092  C CB  . SER A 407  ? 1.2645 1.1780 0.9909 0.3685  0.4082  0.2856  407  SER A CB  
3093  O OG  . SER A 407  ? 1.3102 1.2239 1.0429 0.3829  0.4206  0.3007  407  SER A OG  
3094  N N   . LYS A 408  ? 1.2220 1.0968 0.9217 0.3414  0.3796  0.2373  408  LYS A N   
3095  C CA  . LYS A 408  ? 1.1733 1.0347 0.8521 0.3288  0.3541  0.2234  408  LYS A CA  
3096  C C   . LYS A 408  ? 1.1192 0.9954 0.7845 0.3166  0.3370  0.2331  408  LYS A C   
3097  O O   . LYS A 408  ? 1.1316 1.0211 0.8042 0.3162  0.3474  0.2378  408  LYS A O   
3098  C CB  . LYS A 408  ? 1.1801 1.0186 0.8605 0.3278  0.3574  0.1964  408  LYS A CB  
3099  C CG  . LYS A 408  ? 1.2302 1.0542 0.8888 0.3170  0.3299  0.1822  408  LYS A CG  
3100  C CD  . LYS A 408  ? 1.2878 1.0912 0.9517 0.3191  0.3336  0.1535  408  LYS A CD  
3101  C CE  . LYS A 408  ? 1.2999 1.0989 0.9893 0.3302  0.3622  0.1459  408  LYS A CE  
3102  N NZ  . LYS A 408  ? 1.3079 1.0888 1.0042 0.3309  0.3629  0.1162  408  LYS A NZ  
3103  N N   . SER A 409  ? 1.0775 0.9520 0.7234 0.3061  0.3116  0.2364  409  SER A N   
3104  C CA  . SER A 409  ? 1.1138 0.9972 0.7445 0.2912  0.2942  0.2443  409  SER A CA  
3105  C C   . SER A 409  ? 1.0895 0.9468 0.6974 0.2817  0.2690  0.2296  409  SER A C   
3106  O O   . SER A 409  ? 1.0422 0.8787 0.6502 0.2881  0.2684  0.2113  409  SER A O   
3107  C CB  . SER A 409  ? 1.1623 1.0748 0.7941 0.2865  0.2873  0.2682  409  SER A CB  
3108  O OG  . SER A 409  ? 1.0451 0.9644 0.6615 0.2686  0.2697  0.2751  409  SER A OG  
3109  N N   . VAL A 410  ? 1.0752 0.9331 0.6642 0.2665  0.2487  0.2369  410  VAL A N   
3110  C CA  . VAL A 410  ? 1.1326 0.9629 0.6985 0.2584  0.2227  0.2244  410  VAL A CA  
3111  C C   . VAL A 410  ? 1.2009 1.0353 0.7510 0.2442  0.1997  0.2384  410  VAL A C   
3112  O O   . VAL A 410  ? 1.2189 1.0785 0.7730 0.2360  0.2022  0.2574  410  VAL A O   
3113  C CB  . VAL A 410  ? 1.1475 0.9593 0.7000 0.2535  0.2179  0.2120  410  VAL A CB  
3114  C CG1 . VAL A 410  ? 1.1952 0.9759 0.7233 0.2474  0.1889  0.1993  410  VAL A CG1 
3115  C CG2 . VAL A 410  ? 1.1224 0.9310 0.6927 0.2673  0.2403  0.1954  410  VAL A CG2 
3116  N N   . THR A 411  ? 1.2330 1.0433 0.7670 0.2416  0.1773  0.2273  411  THR A N   
3117  C CA  . THR A 411  ? 1.2223 1.0350 0.7450 0.2313  0.1566  0.2371  411  THR A CA  
3118  C C   . THR A 411  ? 1.2225 1.0275 0.7261 0.2124  0.1408  0.2458  411  THR A C   
3119  O O   . THR A 411  ? 1.1893 0.9680 0.6768 0.2093  0.1323  0.2351  411  THR A O   
3120  C CB  . THR A 411  ? 1.2476 1.0358 0.7604 0.2370  0.1397  0.2194  411  THR A CB  
3121  O OG1 . THR A 411  ? 1.2989 1.0920 0.8029 0.2289  0.1213  0.2277  411  THR A OG1 
3122  C CG2 . THR A 411  ? 1.2289 0.9826 0.7233 0.2341  0.1225  0.2021  411  THR A CG2 
3123  N N   . ARG A 412  ? 1.2818 1.1110 0.7874 0.1996  0.1380  0.2654  412  ARG A N   
3124  C CA  . ARG A 412  ? 1.4206 1.2447 0.9088 0.1787  0.1257  0.2759  412  ARG A CA  
3125  C C   . ARG A 412  ? 1.4604 1.2418 0.9194 0.1690  0.0965  0.2659  412  ARG A C   
3126  O O   . ARG A 412  ? 1.4742 1.2375 0.9298 0.1778  0.0844  0.2521  412  ARG A O   
3127  C CB  . ARG A 412  ? 1.5399 1.3990 1.0380 0.1654  0.1255  0.2966  412  ARG A CB  
3128  C CG  . ARG A 412  ? 1.6890 1.5463 1.1715 0.1418  0.1176  0.3085  412  ARG A CG  
3129  C CD  . ARG A 412  ? 1.7975 1.6953 1.2948 0.1278  0.1193  0.3275  412  ARG A CD  
3130  N NE  . ARG A 412  ? 1.8728 1.8108 1.3918 0.1305  0.1450  0.3385  412  ARG A NE  
3131  C CZ  . ARG A 412  ? 1.9346 1.9139 1.4700 0.1188  0.1497  0.3546  412  ARG A CZ  
3132  N NH1 . ARG A 412  ? 1.9601 1.9452 1.4925 0.1024  0.1301  0.3614  412  ARG A NH1 
3133  N NH2 . ARG A 412  ? 1.9489 1.9649 1.5051 0.1235  0.1737  0.3624  412  ARG A NH2 
3134  N N   . VAL A 413  ? 1.4915 1.2563 0.9290 0.1516  0.0857  0.2726  413  VAL A N   
3135  C CA  . VAL A 413  ? 1.5351 1.2534 0.9422 0.1440  0.0578  0.2635  413  VAL A CA  
3136  C C   . VAL A 413  ? 1.5618 1.2705 0.9576 0.1272  0.0343  0.2712  413  VAL A C   
3137  O O   . VAL A 413  ? 1.5733 1.2486 0.9540 0.1291  0.0115  0.2587  413  VAL A O   
3138  C CB  . VAL A 413  ? 1.5942 1.2934 0.9783 0.1332  0.0562  0.2681  413  VAL A CB  
3139  C CG1 . VAL A 413  ? 1.6281 1.2743 0.9800 0.1315  0.0277  0.2562  413  VAL A CG1 
3140  C CG2 . VAL A 413  ? 1.5774 1.2943 0.9749 0.1470  0.0822  0.2626  413  VAL A CG2 
3141  N N   . ASP A 414  ? 1.6013 1.3409 1.0060 0.1106  0.0400  0.2906  414  ASP A N   
3142  C CA  . ASP A 414  ? 1.6316 1.3684 1.0289 0.0907  0.0198  0.2996  414  ASP A CA  
3143  C C   . ASP A 414  ? 1.5666 1.3317 0.9855 0.1004  0.0211  0.2973  414  ASP A C   
3144  O O   . ASP A 414  ? 1.5778 1.3406 0.9927 0.0887  0.0027  0.2991  414  ASP A O   
3145  C CB  . ASP A 414  ? 1.6933 1.4599 1.0959 0.0682  0.0289  0.3213  414  ASP A CB  
3146  C CG  . ASP A 414  ? 1.7097 1.5310 1.1448 0.0787  0.0583  0.3296  414  ASP A CG  
3147  O OD1 . ASP A 414  ? 1.7161 1.5419 1.1551 0.0905  0.0778  0.3268  414  ASP A OD1 
3148  O OD2 . ASP A 414  ? 1.7053 1.5647 1.1621 0.0762  0.0612  0.3380  414  ASP A OD2 
3149  N N   . ASP A 415  ? 1.5180 1.3108 0.9596 0.1211  0.0438  0.2942  415  ASP A N   
3150  C CA  . ASP A 415  ? 1.4822 1.3123 0.9465 0.1305  0.0516  0.2984  415  ASP A CA  
3151  C C   . ASP A 415  ? 1.3730 1.1865 0.8358 0.1498  0.0468  0.2804  415  ASP A C   
3152  O O   . ASP A 415  ? 1.3320 1.1564 0.7979 0.1518  0.0374  0.2792  415  ASP A O   
3153  C CB  . ASP A 415  ? 1.5536 1.4244 1.0435 0.1409  0.0817  0.3090  415  ASP A CB  
3154  C CG  . ASP A 415  ? 1.6171 1.5323 1.1299 0.1462  0.0889  0.3200  415  ASP A CG  
3155  O OD1 . ASP A 415  ? 1.6650 1.5789 1.1724 0.1424  0.0704  0.3177  415  ASP A OD1 
3156  O OD2 . ASP A 415  ? 1.6100 1.5609 1.1454 0.1552  0.1120  0.3303  415  ASP A OD2 
3157  N N   . GLY A 416  ? 1.3060 1.0941 0.7637 0.1632  0.0528  0.2655  416  GLY A N   
3158  C CA  . GLY A 416  ? 1.2839 1.0633 0.7464 0.1836  0.0568  0.2480  416  GLY A CA  
3159  C C   . GLY A 416  ? 1.2958 1.1117 0.7838 0.1994  0.0843  0.2549  416  GLY A C   
3160  O O   . GLY A 416  ? 1.3199 1.1337 0.8142 0.2160  0.0926  0.2434  416  GLY A O   
3161  N N   . VAL A 417  ? 1.2556 1.1049 0.7584 0.1947  0.0990  0.2738  417  VAL A N   
3162  C CA  . VAL A 417  ? 1.2305 1.1136 0.7563 0.2102  0.1221  0.2825  417  VAL A CA  
3163  C C   . VAL A 417  ? 1.1977 1.0856 0.7386 0.2219  0.1490  0.2819  417  VAL A C   
3164  O O   . VAL A 417  ? 1.1959 1.0829 0.7358 0.2138  0.1539  0.2851  417  VAL A O   
3165  C CB  . VAL A 417  ? 1.2764 1.1991 0.8139 0.2013  0.1223  0.3032  417  VAL A CB  
3166  C CG1 . VAL A 417  ? 1.2604 1.2166 0.8229 0.2182  0.1495  0.3144  417  VAL A CG1 
3167  C CG2 . VAL A 417  ? 1.3100 1.2371 0.8385 0.1944  0.0994  0.3038  417  VAL A CG2 
3168  N N   . ALA A 418  ? 1.1963 1.0892 0.7506 0.2406  0.1673  0.2778  418  ALA A N   
3169  C CA  . ALA A 418  ? 1.2172 1.1171 0.7891 0.2520  0.1945  0.2783  418  ALA A CA  
3170  C C   . ALA A 418  ? 1.2097 1.1457 0.8024 0.2622  0.2125  0.2968  418  ALA A C   
3171  O O   . ALA A 418  ? 1.2038 1.1435 0.8021 0.2759  0.2203  0.2979  418  ALA A O   
3172  C CB  . ALA A 418  ? 1.2217 1.0965 0.7950 0.2654  0.2041  0.2586  418  ALA A CB  
3173  N N   . SER A 419  ? 1.2171 1.1798 0.8207 0.2563  0.2191  0.3112  419  SER A N   
3174  C CA  . SER A 419  ? 1.2303 1.2314 0.8540 0.2658  0.2315  0.3298  419  SER A CA  
3175  C C   . SER A 419  ? 1.1798 1.1875 0.8245 0.2849  0.2613  0.3320  419  SER A C   
3176  O O   . SER A 419  ? 1.1878 1.1899 0.8379 0.2840  0.2740  0.3262  419  SER A O   
3177  C CB  . SER A 419  ? 1.2796 1.3129 0.9087 0.2502  0.2240  0.3444  419  SER A CB  
3178  O OG  . SER A 419  ? 1.3081 1.3253 0.9166 0.2276  0.2009  0.3396  419  SER A OG  
3179  N N   . PHE A 420  ? 1.1417 1.1602 0.7971 0.3022  0.2726  0.3405  420  PHE A N   
3180  C CA  . PHE A 420  ? 1.2081 1.2339 0.8850 0.3201  0.3008  0.3457  420  PHE A CA  
3181  C C   . PHE A 420  ? 1.2657 1.3315 0.9617 0.3305  0.3083  0.3668  420  PHE A C   
3182  O O   . PHE A 420  ? 1.3433 1.4367 1.0377 0.3231  0.2914  0.3781  420  PHE A O   
3183  C CB  . PHE A 420  ? 1.1971 1.1981 0.8737 0.3355  0.3145  0.3390  420  PHE A CB  
3184  C CG  . PHE A 420  ? 1.0316 0.9976 0.6961 0.3294  0.3114  0.3171  420  PHE A CG  
3185  C CD1 . PHE A 420  ? 1.0294 0.9743 0.7039 0.3382  0.3328  0.3049  420  PHE A CD1 
3186  C CD2 . PHE A 420  ? 1.0345 0.9883 0.6788 0.3151  0.2866  0.3076  420  PHE A CD2 
3187  C CE1 . PHE A 420  ? 1.0676 0.9833 0.7332 0.3331  0.3291  0.2829  420  PHE A CE1 
3188  C CE2 . PHE A 420  ? 1.1062 1.0290 0.7405 0.3115  0.2825  0.2863  420  PHE A CE2 
3189  C CZ  . PHE A 420  ? 1.0938 0.9990 0.7394 0.3205  0.3037  0.2736  420  PHE A CZ  
3190  N N   . VAL A 421  ? 1.2229 1.2916 0.9382 0.3482  0.3335  0.3710  421  VAL A N   
3191  C CA  . VAL A 421  ? 1.1578 1.2592 0.8920 0.3648  0.3429  0.3904  421  VAL A CA  
3192  C C   . VAL A 421  ? 1.1603 1.2467 0.9102 0.3856  0.3710  0.3904  421  VAL A C   
3193  O O   . VAL A 421  ? 1.1788 1.2503 0.9358 0.3844  0.3856  0.3780  421  VAL A O   
3194  C CB  . VAL A 421  ? 1.1039 1.2467 0.8542 0.3581  0.3404  0.3995  421  VAL A CB  
3195  C CG1 . VAL A 421  ? 1.0883 1.2540 0.8654 0.3809  0.3621  0.4117  421  VAL A CG1 
3196  C CG2 . VAL A 421  ? 1.0758 1.2473 0.8193 0.3448  0.3150  0.4087  421  VAL A CG2 
3197  N N   . LEU A 422  ? 1.1522 1.2410 0.9058 0.4044  0.3782  0.4043  422  LEU A N   
3198  C CA  . LEU A 422  ? 1.1639 1.2375 0.9327 0.4257  0.4050  0.4080  422  LEU A CA  
3199  C C   . LEU A 422  ? 1.2227 1.3317 1.0081 0.4435  0.4079  0.4297  422  LEU A C   
3200  O O   . LEU A 422  ? 1.2204 1.3562 0.9996 0.4430  0.3896  0.4425  422  LEU A O   
3201  C CB  . LEU A 422  ? 1.1627 1.1979 0.9185 0.4333  0.4144  0.4045  422  LEU A CB  
3202  C CG  . LEU A 422  ? 1.0677 1.0895 0.7981 0.4207  0.3955  0.3973  422  LEU A CG  
3203  C CD1 . LEU A 422  ? 1.0770 1.1246 0.7981 0.4268  0.3801  0.4163  422  LEU A CD1 
3204  C CD2 . LEU A 422  ? 1.0753 1.0568 0.7992 0.4248  0.4116  0.3861  422  LEU A CD2 
3205  N N   . ASN A 423  ? 1.2647 1.3753 1.0724 0.4591  0.4298  0.4321  423  ASN A N   
3206  C CA  . ASN A 423  ? 1.2727 1.4185 1.1005 0.4787  0.4337  0.4511  423  ASN A CA  
3207  C C   . ASN A 423  ? 1.2752 1.3995 1.1026 0.5038  0.4479  0.4653  423  ASN A C   
3208  O O   . ASN A 423  ? 1.2573 1.3457 1.0895 0.5134  0.4701  0.4596  423  ASN A O   
3209  C CB  . ASN A 423  ? 1.2596 1.4262 1.1126 0.4806  0.4468  0.4453  423  ASN A CB  
3210  C CG  . ASN A 423  ? 1.2360 1.4174 1.0837 0.4538  0.4341  0.4318  423  ASN A CG  
3211  O OD1 . ASN A 423  ? 1.2442 1.4691 1.1028 0.4469  0.4243  0.4376  423  ASN A OD1 
3212  N ND2 . ASN A 423  ? 1.2142 1.3596 1.0436 0.4378  0.4327  0.4142  423  ASN A ND2 
3213  N N   . LEU A 424  ? 1.2828 1.4282 1.1027 0.5136  0.4341  0.4839  424  LEU A N   
3214  C CA  . LEU A 424  ? 1.3182 1.4376 1.1265 0.5332  0.4433  0.4982  424  LEU A CA  
3215  C C   . LEU A 424  ? 1.3552 1.4870 1.1815 0.5636  0.4552  0.5186  424  LEU A C   
3216  O O   . LEU A 424  ? 1.3464 1.5245 1.1858 0.5726  0.4424  0.5311  424  LEU A O   
3217  C CB  . LEU A 424  ? 1.3088 1.4306 1.0887 0.5251  0.4220  0.5036  424  LEU A CB  
3218  C CG  . LEU A 424  ? 1.3021 1.3850 1.0631 0.5055  0.4236  0.4834  424  LEU A CG  
3219  C CD1 . LEU A 424  ? 1.3288 1.4015 1.0604 0.5028  0.4111  0.4879  424  LEU A CD1 
3220  C CD2 . LEU A 424  ? 1.3050 1.3449 1.0741 0.5126  0.4524  0.4752  424  LEU A CD2 
3221  N N   . PRO A 425  ? 1.3842 1.4737 1.2121 0.5795  0.4797  0.5214  425  PRO A N   
3222  C CA  . PRO A 425  ? 1.4471 1.5390 1.2918 0.6100  0.4933  0.5398  425  PRO A CA  
3223  C C   . PRO A 425  ? 1.5259 1.6452 1.3589 0.6254  0.4756  0.5639  425  PRO A C   
3224  O O   . PRO A 425  ? 1.6018 1.6960 1.4078 0.6279  0.4742  0.5734  425  PRO A O   
3225  C CB  . PRO A 425  ? 1.4511 1.4830 1.2879 0.6179  0.5189  0.5390  425  PRO A CB  
3226  C CG  . PRO A 425  ? 1.4084 1.4149 1.2376 0.5902  0.5224  0.5124  425  PRO A CG  
3227  C CD  . PRO A 425  ? 1.3656 1.4023 1.1791 0.5696  0.4952  0.5076  425  PRO A CD  
3228  N N   . SER A 426  ? 1.5516 1.7233 1.4042 0.6354  0.4624  0.5728  426  SER A N   
3229  C CA  . SER A 426  ? 1.6038 1.8071 1.4482 0.6529  0.4440  0.5955  426  SER A CA  
3230  C C   . SER A 426  ? 1.7301 1.8953 1.5414 0.6660  0.4469  0.6128  426  SER A C   
3231  O O   . SER A 426  ? 1.7073 1.8857 1.4935 0.6591  0.4268  0.6188  426  SER A O   
3232  C CB  . SER A 426  ? 1.6481 1.8884 1.5249 0.6801  0.4467  0.6077  426  SER A CB  
3233  O OG  . SER A 426  ? 1.6643 1.8850 1.5660 0.6864  0.4714  0.5969  426  SER A OG  
3234  N N   . GLY A 427  ? 1.7730 1.8903 1.5832 0.6837  0.4722  0.6202  427  GLY A N   
3235  C CA  . GLY A 427  ? 1.8173 1.8935 1.5951 0.6942  0.4793  0.6368  427  GLY A CA  
3236  C C   . GLY A 427  ? 1.7888 1.8335 1.5371 0.6687  0.4798  0.6238  427  GLY A C   
3237  O O   . GLY A 427  ? 1.8106 1.8092 1.5373 0.6731  0.4961  0.6313  427  GLY A O   
3238  N N   . VAL A 428  ? 1.7165 1.7857 1.4640 0.6418  0.4624  0.6042  428  VAL A N   
3239  C CA  . VAL A 428  ? 1.6685 1.7117 1.3900 0.6189  0.4606  0.5901  428  VAL A CA  
3240  C C   . VAL A 428  ? 1.6457 1.7119 1.3379 0.6183  0.4366  0.6012  428  VAL A C   
3241  O O   . VAL A 428  ? 1.6479 1.7590 1.3450 0.6282  0.4166  0.6134  428  VAL A O   
3242  C CB  . VAL A 428  ? 1.6276 1.6790 1.3605 0.5908  0.4538  0.5624  428  VAL A CB  
3243  C CG1 . VAL A 428  ? 1.6150 1.7202 1.3508 0.5805  0.4237  0.5612  428  VAL A CG1 
3244  C CG2 . VAL A 428  ? 1.6193 1.6338 1.3303 0.5710  0.4586  0.5454  428  VAL A CG2 
3245  N N   . THR A 429  ? 1.6196 1.6584 1.2833 0.6051  0.4378  0.5940  429  THR A N   
3246  C CA  . THR A 429  ? 1.6202 1.6638 1.2490 0.6111  0.4251  0.6085  429  THR A CA  
3247  C C   . THR A 429  ? 1.5240 1.5668 1.1303 0.5859  0.4106  0.5887  429  THR A C   
3248  O O   . THR A 429  ? 1.4729 1.5520 1.0713 0.5767  0.3829  0.5846  429  THR A O   
3249  C CB  . THR A 429  ? 1.7348 1.7305 1.3447 0.6274  0.4517  0.6251  429  THR A CB  
3250  O OG1 . THR A 429  ? 1.7527 1.7054 1.3634 0.6101  0.4733  0.6054  429  THR A OG1 
3251  C CG2 . THR A 429  ? 1.7745 1.7624 1.4051 0.6538  0.4676  0.6443  429  THR A CG2 
3252  N N   . VAL A 430  ? 1.4968 1.4965 1.0927 0.5761  0.4303  0.5769  430  VAL A N   
3253  C CA  . VAL A 430  ? 1.4391 1.4300 1.0222 0.5519  0.4228  0.5525  430  VAL A CA  
3254  C C   . VAL A 430  ? 1.4467 1.4177 1.0568 0.5381  0.4367  0.5303  430  VAL A C   
3255  O O   . VAL A 430  ? 1.4580 1.3985 1.0817 0.5461  0.4634  0.5329  430  VAL A O   
3256  C CB  . VAL A 430  ? 1.4005 1.3569 0.9546 0.5525  0.4388  0.5544  430  VAL A CB  
3257  C CG1 . VAL A 430  ? 1.3592 1.3130 0.8991 0.5297  0.4273  0.5285  430  VAL A CG1 
3258  C CG2 . VAL A 430  ? 1.4279 1.3943 0.9545 0.5716  0.4337  0.5811  430  VAL A CG2 
3259  N N   . LEU A 431  ? 1.4133 1.4015 1.0299 0.5176  0.4175  0.5091  431  LEU A N   
3260  C CA  . LEU A 431  ? 1.3358 1.3056 0.9682 0.4998  0.4241  0.4832  431  LEU A CA  
3261  C C   . LEU A 431  ? 1.3348 1.2894 0.9464 0.4827  0.4164  0.4628  431  LEU A C   
3262  O O   . LEU A 431  ? 1.2020 1.1764 0.7946 0.4763  0.3928  0.4613  431  LEU A O   
3263  C CB  . LEU A 431  ? 1.2435 1.2455 0.8952 0.4903  0.4058  0.4767  431  LEU A CB  
3264  C CG  . LEU A 431  ? 1.1970 1.1916 0.8676 0.4740  0.4079  0.4543  431  LEU A CG  
3265  C CD1 . LEU A 431  ? 1.1409 1.1649 0.8072 0.4569  0.3782  0.4464  431  LEU A CD1 
3266  C CD2 . LEU A 431  ? 1.1951 1.1508 0.8611 0.4638  0.4216  0.4328  431  LEU A CD2 
3267  N N   . GLU A 432  ? 1.3194 1.2400 0.9356 0.4758  0.4361  0.4460  432  GLU A N   
3268  C CA  . GLU A 432  ? 1.3231 1.2311 0.9249 0.4600  0.4293  0.4231  432  GLU A CA  
3269  C C   . GLU A 432  ? 1.3195 1.2197 0.9379 0.4428  0.4241  0.3952  432  GLU A C   
3270  O O   . GLU A 432  ? 1.3594 1.2386 0.9967 0.4423  0.4443  0.3860  432  GLU A O   
3271  C CB  . GLU A 432  ? 1.3508 1.2275 0.9428 0.4644  0.4552  0.4232  432  GLU A CB  
3272  C CG  . GLU A 432  ? 1.4389 1.3185 1.0064 0.4799  0.4601  0.4494  432  GLU A CG  
3273  C CD  . GLU A 432  ? 1.4838 1.3765 1.0210 0.4741  0.4412  0.4445  432  GLU A CD  
3274  O OE1 . GLU A 432  ? 1.4213 1.3187 0.9572 0.4581  0.4244  0.4196  432  GLU A OE1 
3275  O OE2 . GLU A 432  ? 1.5511 1.4486 1.0646 0.4868  0.4432  0.4658  432  GLU A OE2 
3276  N N   . PHE A 433  ? 1.2656 1.1801 0.8763 0.4287  0.3972  0.3811  433  PHE A N   
3277  C CA  . PHE A 433  ? 1.2232 1.1260 0.8463 0.4140  0.3929  0.3557  433  PHE A CA  
3278  C C   . PHE A 433  ? 1.2763 1.1647 0.8877 0.4011  0.3820  0.3295  433  PHE A C   
3279  O O   . PHE A 433  ? 1.3039 1.2000 0.8948 0.3982  0.3651  0.3276  433  PHE A O   
3280  C CB  . PHE A 433  ? 1.1670 1.0907 0.8017 0.4075  0.3769  0.3578  433  PHE A CB  
3281  C CG  . PHE A 433  ? 1.1596 1.1112 0.7805 0.4015  0.3478  0.3654  433  PHE A CG  
3282  C CD1 . PHE A 433  ? 1.1561 1.1344 0.7748 0.4129  0.3439  0.3896  433  PHE A CD1 
3283  C CD2 . PHE A 433  ? 1.0912 1.0425 0.7028 0.3846  0.3235  0.3480  433  PHE A CD2 
3284  C CE1 . PHE A 433  ? 1.1411 1.1478 0.7496 0.4060  0.3164  0.3950  433  PHE A CE1 
3285  C CE2 . PHE A 433  ? 1.0924 1.0676 0.6925 0.3773  0.2968  0.3541  433  PHE A CE2 
3286  C CZ  . PHE A 433  ? 1.1029 1.1073 0.7023 0.3874  0.2934  0.3772  433  PHE A CZ  
3287  N N   . ASN A 434  ? 1.2890 1.1569 0.9146 0.3948  0.3928  0.3083  434  ASN A N   
3288  C CA  . ASN A 434  ? 1.2595 1.1152 0.8801 0.3828  0.3803  0.2801  434  ASN A CA  
3289  C C   . ASN A 434  ? 1.2925 1.1501 0.9209 0.3724  0.3636  0.2686  434  ASN A C   
3290  O O   . ASN A 434  ? 1.3180 1.1781 0.9621 0.3743  0.3732  0.2751  434  ASN A O   
3291  C CB  . ASN A 434  ? 1.2305 1.0628 0.8635 0.3834  0.4049  0.2630  434  ASN A CB  
3292  C CG  . ASN A 434  ? 1.2066 1.0330 0.8332 0.3926  0.4268  0.2756  434  ASN A CG  
3293  O OD1 . ASN A 434  ? 1.1853 1.0179 0.7916 0.3932  0.4186  0.2775  434  ASN A OD1 
3294  N ND2 . ASN A 434  ? 1.2228 1.0352 0.8654 0.3995  0.4556  0.2838  434  ASN A ND2 
3295  N N   . VAL A 435  ? 1.3236 1.1777 0.9404 0.3620  0.3398  0.2505  435  VAL A N   
3296  C CA  . VAL A 435  ? 1.3199 1.1759 0.9371 0.3514  0.3200  0.2440  435  VAL A CA  
3297  C C   . VAL A 435  ? 1.3150 1.1520 0.9278 0.3443  0.3082  0.2155  435  VAL A C   
3298  O O   . VAL A 435  ? 1.3172 1.1508 0.9169 0.3436  0.2973  0.2056  435  VAL A O   
3299  C CB  . VAL A 435  ? 1.0628 0.9384 0.6644 0.3459  0.2946  0.2583  435  VAL A CB  
3300  C CG1 . VAL A 435  ? 1.0595 0.9271 0.6505 0.3324  0.2677  0.2434  435  VAL A CG1 
3301  C CG2 . VAL A 435  ? 1.0603 0.9575 0.6718 0.3489  0.3001  0.2815  435  VAL A CG2 
3302  N N   . LYS A 436  ? 1.1798 1.0051 0.8030 0.3399  0.3096  0.2008  436  LYS A N   
3303  C CA  . LYS A 436  ? 1.1517 0.9602 0.7697 0.3346  0.2946  0.1735  436  LYS A CA  
3304  C C   . LYS A 436  ? 1.1973 0.9974 0.8125 0.3261  0.2776  0.1638  436  LYS A C   
3305  O O   . LYS A 436  ? 1.1907 0.9977 0.8111 0.3238  0.2825  0.1761  436  LYS A O   
3306  C CB  . LYS A 436  ? 1.0997 0.8969 0.7328 0.3401  0.3159  0.1543  436  LYS A CB  
3307  C CG  . LYS A 436  ? 1.0444 0.8342 0.6989 0.3417  0.3366  0.1464  436  LYS A CG  
3308  C CD  . LYS A 436  ? 1.2748 1.0512 0.9413 0.3414  0.3417  0.1148  436  LYS A CD  
3309  C CE  . LYS A 436  ? 1.3279 1.0978 1.0204 0.3447  0.3730  0.1070  436  LYS A CE  
3310  N NZ  . LYS A 436  ? 1.3113 1.0788 1.0152 0.3491  0.4004  0.1074  436  LYS A NZ  
3311  N N   . THR A 437  ? 1.2427 1.0280 0.8482 0.3221  0.2570  0.1418  437  THR A N   
3312  C CA  . THR A 437  ? 1.3298 1.1013 0.9306 0.3159  0.2411  0.1283  437  THR A CA  
3313  C C   . THR A 437  ? 1.2664 1.0300 0.8861 0.3206  0.2589  0.1090  437  THR A C   
3314  O O   . THR A 437  ? 1.1861 0.9475 0.8195 0.3267  0.2735  0.0938  437  THR A O   
3315  C CB  . THR A 437  ? 1.0569 0.8126 0.6406 0.3124  0.2115  0.1104  437  THR A CB  
3316  O OG1 . THR A 437  ? 1.0570 0.8098 0.6481 0.3198  0.2174  0.0910  437  THR A OG1 
3317  C CG2 . THR A 437  ? 1.0664 0.8254 0.6299 0.3050  0.1893  0.1261  437  THR A CG2 
3318  N N   . ASP A 438  ? 1.3174 1.0778 0.9378 0.3168  0.2579  0.1089  438  ASP A N   
3319  C CA  . ASP A 438  ? 1.4115 1.1636 1.0475 0.3202  0.2695  0.0867  438  ASP A CA  
3320  C C   . ASP A 438  ? 1.4135 1.1499 1.0369 0.3169  0.2447  0.0664  438  ASP A C   
3321  O O   . ASP A 438  ? 1.3920 1.1245 1.0216 0.3173  0.2496  0.0550  438  ASP A O   
3322  C CB  . ASP A 438  ? 1.4962 1.2570 1.1488 0.3225  0.2958  0.0967  438  ASP A CB  
3323  C CG  . ASP A 438  ? 1.5778 1.3366 1.2560 0.3294  0.3231  0.0824  438  ASP A CG  
3324  O OD1 . ASP A 438  ? 1.5944 1.3492 1.2772 0.3318  0.3234  0.0685  438  ASP A OD1 
3325  O OD2 . ASP A 438  ? 1.6104 1.3717 1.3040 0.3318  0.3445  0.0847  438  ASP A OD2 
3326  N N   . ALA A 439  ? 1.4395 1.1659 1.0445 0.3146  0.2177  0.0612  439  ALA A N   
3327  C CA  . ALA A 439  ? 1.4890 1.1977 1.0849 0.3155  0.1946  0.0372  439  ALA A CA  
3328  C C   . ALA A 439  ? 1.5133 1.2226 1.1309 0.3214  0.2103  0.0140  439  ALA A C   
3329  O O   . ALA A 439  ? 1.5307 1.2478 1.1716 0.3267  0.2312  0.0024  439  ALA A O   
3330  C CB  . ALA A 439  ? 1.5144 1.2159 1.1045 0.3190  0.1771  0.0235  439  ALA A CB  
3331  N N   . PRO A 440  ? 1.4992 1.1998 1.1081 0.3197  0.2001  0.0068  440  PRO A N   
3332  C CA  . PRO A 440  ? 1.4473 1.1505 1.0762 0.3243  0.2149  -0.0145 440  PRO A CA  
3333  C C   . PRO A 440  ? 1.4026 1.0990 1.0395 0.3311  0.2009  -0.0467 440  PRO A C   
3334  O O   . PRO A 440  ? 1.3947 1.0976 1.0568 0.3356  0.2161  -0.0693 440  PRO A O   
3335  C CB  . PRO A 440  ? 1.4598 1.1560 1.0684 0.3197  0.2033  -0.0084 440  PRO A CB  
3336  C CG  . PRO A 440  ? 1.5576 1.2446 1.1343 0.3114  0.1795  0.0158  440  PRO A CG  
3337  C CD  . PRO A 440  ? 1.5426 1.2277 1.1205 0.3136  0.1708  0.0145  440  PRO A CD  
3338  N N   . ASP A 441  ? 1.3860 1.0696 1.0023 0.3318  0.1718  -0.0489 441  ASP A N   
3339  C CA  . ASP A 441  ? 1.4117 1.0884 1.0324 0.3398  0.1531  -0.0783 441  ASP A CA  
3340  C C   . ASP A 441  ? 1.3602 1.0436 0.9901 0.3426  0.1569  -0.0817 441  ASP A C   
3341  O O   . ASP A 441  ? 1.3499 1.0319 0.9872 0.3499  0.1445  -0.1069 441  ASP A O   
3342  C CB  . ASP A 441  ? 1.5512 1.2053 1.1392 0.3394  0.1166  -0.0766 441  ASP A CB  
3343  C CG  . ASP A 441  ? 1.6597 1.3059 1.2232 0.3310  0.1059  -0.0477 441  ASP A CG  
3344  O OD1 . ASP A 441  ? 1.7438 1.3705 1.2854 0.3318  0.0764  -0.0499 441  ASP A OD1 
3345  O OD2 . ASP A 441  ? 1.6410 1.3007 1.2085 0.3242  0.1268  -0.0240 441  ASP A OD2 
3346  N N   . LEU A 442  ? 1.3275 1.0194 0.9556 0.3375  0.1725  -0.0566 442  LEU A N   
3347  C CA  . LEU A 442  ? 1.2726 0.9748 0.9122 0.3407  0.1831  -0.0611 442  LEU A CA  
3348  C C   . LEU A 442  ? 1.2823 1.0002 0.9541 0.3428  0.2180  -0.0713 442  LEU A C   
3349  O O   . LEU A 442  ? 1.2843 1.0077 0.9661 0.3396  0.2416  -0.0571 442  LEU A O   
3350  C CB  . LEU A 442  ? 1.1990 0.9039 0.8212 0.3356  0.1826  -0.0321 442  LEU A CB  
3351  C CG  . LEU A 442  ? 1.1515 0.8432 0.7517 0.3366  0.1501  -0.0379 442  LEU A CG  
3352  C CD1 . LEU A 442  ? 1.1399 0.8385 0.7276 0.3328  0.1508  -0.0163 442  LEU A CD1 
3353  C CD2 . LEU A 442  ? 1.1129 0.8034 0.7265 0.3460  0.1424  -0.0730 442  LEU A CD2 
3354  N N   . PRO A 443  ? 1.2329 0.9579 0.9219 0.3480  0.2221  -0.0961 443  PRO A N   
3355  C CA  . PRO A 443  ? 1.2500 0.9884 0.9701 0.3480  0.2556  -0.1070 443  PRO A CA  
3356  C C   . PRO A 443  ? 1.3487 1.0936 1.0657 0.3449  0.2793  -0.0789 443  PRO A C   
3357  O O   . PRO A 443  ? 1.3819 1.1248 1.0753 0.3445  0.2654  -0.0602 443  PRO A O   
3358  C CB  . PRO A 443  ? 1.1876 0.9332 0.9222 0.3535  0.2489  -0.1396 443  PRO A CB  
3359  C CG  . PRO A 443  ? 1.1878 0.9216 0.8984 0.3581  0.2111  -0.1454 443  PRO A CG  
3360  C CD  . PRO A 443  ? 1.2017 0.9238 0.8821 0.3532  0.1992  -0.1125 443  PRO A CD  
3361  N N   . GLU A 444  ? 1.3821 1.1334 1.1214 0.3431  0.3133  -0.0758 444  GLU A N   
3362  C CA  . GLU A 444  ? 1.4244 1.1784 1.1577 0.3415  0.3347  -0.0443 444  GLU A CA  
3363  C C   . GLU A 444  ? 1.3259 1.0854 1.0429 0.3433  0.3294  -0.0357 444  GLU A C   
3364  O O   . GLU A 444  ? 1.2652 1.0249 0.9602 0.3430  0.3201  -0.0101 444  GLU A O   
3365  C CB  . GLU A 444  ? 1.5880 1.3438 1.3476 0.3400  0.3721  -0.0444 444  GLU A CB  
3366  C CG  . GLU A 444  ? 1.7571 1.5099 1.5112 0.3399  0.3889  -0.0109 444  GLU A CG  
3367  C CD  . GLU A 444  ? 1.8872 1.6447 1.6210 0.3422  0.3909  0.0185  444  GLU A CD  
3368  O OE1 . GLU A 444  ? 1.9276 1.6899 1.6509 0.3430  0.3813  0.0123  444  GLU A OE1 
3369  O OE2 . GLU A 444  ? 1.9229 1.6804 1.6516 0.3440  0.4018  0.0467  444  GLU A OE2 
3370  N N   . GLU A 445  ? 1.3310 1.0970 1.0599 0.3449  0.3350  -0.0590 445  GLU A N   
3371  C CA  . GLU A 445  ? 1.3426 1.1157 1.0565 0.3472  0.3296  -0.0573 445  GLU A CA  
3372  C C   . GLU A 445  ? 1.2765 1.0446 0.9596 0.3481  0.2977  -0.0429 445  GLU A C   
3373  O O   . GLU A 445  ? 1.2830 1.0539 0.9482 0.3475  0.2997  -0.0157 445  GLU A O   
3374  C CB  . GLU A 445  ? 1.4139 1.1946 1.1428 0.3498  0.3255  -0.0937 445  GLU A CB  
3375  C CG  . GLU A 445  ? 1.5034 1.2936 1.2628 0.3469  0.3598  -0.1091 445  GLU A CG  
3376  C CD  . GLU A 445  ? 1.5943 1.3973 1.3701 0.3496  0.3545  -0.1463 445  GLU A CD  
3377  O OE1 . GLU A 445  ? 1.6186 1.4198 1.3910 0.3550  0.3230  -0.1674 445  GLU A OE1 
3378  O OE2 . GLU A 445  ? 1.6284 1.4432 1.4202 0.3465  0.3824  -0.1544 445  GLU A OE2 
3379  N N   . ASN A 446  ? 1.2348 0.9948 0.9121 0.3497  0.2676  -0.0615 446  ASN A N   
3380  C CA  . ASN A 446  ? 1.2436 0.9953 0.8928 0.3495  0.2353  -0.0528 446  ASN A CA  
3381  C C   . ASN A 446  ? 1.1957 0.9408 0.8281 0.3439  0.2270  -0.0226 446  ASN A C   
3382  O O   . ASN A 446  ? 1.1908 0.9274 0.8011 0.3414  0.2002  -0.0150 446  ASN A O   
3383  C CB  . ASN A 446  ? 1.3029 1.0445 0.9521 0.3538  0.2071  -0.0826 446  ASN A CB  
3384  C CG  . ASN A 446  ? 1.3550 1.1078 1.0296 0.3592  0.2195  -0.1151 446  ASN A CG  
3385  O OD1 . ASN A 446  ? 1.3531 1.1069 1.0495 0.3606  0.2244  -0.1350 446  ASN A OD1 
3386  N ND2 . ASN A 446  ? 1.4005 1.1644 1.0732 0.3619  0.2258  -0.1213 446  ASN A ND2 
3387  N N   . GLN A 447  ? 1.1816 0.9308 0.8253 0.3416  0.2506  -0.0059 447  GLN A N   
3388  C CA  . GLN A 447  ? 1.2334 0.9833 0.8635 0.3370  0.2479  0.0251  447  GLN A CA  
3389  C C   . GLN A 447  ? 1.2232 0.9829 0.8365 0.3367  0.2469  0.0478  447  GLN A C   
3390  O O   . GLN A 447  ? 1.1918 0.9607 0.8091 0.3408  0.2651  0.0491  447  GLN A O   
3391  C CB  . GLN A 447  ? 1.2544 1.0088 0.9033 0.3370  0.2775  0.0365  447  GLN A CB  
3392  C CG  . GLN A 447  ? 1.2958 1.0422 0.9557 0.3355  0.2760  0.0227  447  GLN A CG  
3393  C CD  . GLN A 447  ? 1.3300 1.0702 0.9701 0.3303  0.2524  0.0352  447  GLN A CD  
3394  O OE1 . GLN A 447  ? 1.3312 1.0750 0.9534 0.3268  0.2410  0.0567  447  GLN A OE1 
3395  N NE2 . GLN A 447  ? 1.3538 1.0852 0.9961 0.3291  0.2443  0.0215  447  GLN A NE2 
3396  N N   . ALA A 448  ? 1.0646 0.8239 0.6592 0.3315  0.2272  0.0666  448  ALA A N   
3397  C CA  . ALA A 448  ? 1.0722 0.8427 0.6511 0.3312  0.2226  0.0850  448  ALA A CA  
3398  C C   . ALA A 448  ? 1.1964 0.9829 0.7795 0.3331  0.2452  0.1146  448  ALA A C   
3399  O O   . ALA A 448  ? 1.1620 0.9512 0.7502 0.3301  0.2493  0.1299  448  ALA A O   
3400  C CB  . ALA A 448  ? 1.0812 0.8447 0.6389 0.3241  0.1897  0.0888  448  ALA A CB  
3401  N N   . ARG A 449  ? 1.2167 1.0143 0.7955 0.3386  0.2583  0.1234  449  ARG A N   
3402  C CA  . ARG A 449  ? 1.2272 1.0385 0.8094 0.3431  0.2798  0.1516  449  ARG A CA  
3403  C C   . ARG A 449  ? 1.2500 1.0767 0.8133 0.3461  0.2739  0.1698  449  ARG A C   
3404  O O   . ARG A 449  ? 1.2534 1.0808 0.8016 0.3459  0.2600  0.1585  449  ARG A O   
3405  C CB  . ARG A 449  ? 1.2328 1.0401 0.8331 0.3492  0.3131  0.1477  449  ARG A CB  
3406  C CG  . ARG A 449  ? 1.2710 1.0728 0.8719 0.3502  0.3154  0.1222  449  ARG A CG  
3407  C CD  . ARG A 449  ? 1.3305 1.1263 0.9536 0.3527  0.3471  0.1140  449  ARG A CD  
3408  N NE  . ARG A 449  ? 1.3624 1.1479 1.0032 0.3491  0.3433  0.0871  449  ARG A NE  
3409  C CZ  . ARG A 449  ? 1.3983 1.1774 1.0620 0.3489  0.3654  0.0824  449  ARG A CZ  
3410  N NH1 . ARG A 449  ? 1.4118 1.1907 1.0832 0.3522  0.3928  0.1038  449  ARG A NH1 
3411  N NH2 . ARG A 449  ? 1.3895 1.1615 1.0678 0.3460  0.3591  0.0560  449  ARG A NH2 
3412  N N   . GLU A 450  ? 1.2782 1.1185 0.8430 0.3498  0.2846  0.1974  450  GLU A N   
3413  C CA  . GLU A 450  ? 1.2993 1.1578 0.8473 0.3538  0.2786  0.2178  450  GLU A CA  
3414  C C   . GLU A 450  ? 1.2855 1.1530 0.8435 0.3628  0.3030  0.2433  450  GLU A C   
3415  O O   . GLU A 450  ? 1.2856 1.1479 0.8624 0.3631  0.3163  0.2465  450  GLU A O   
3416  C CB  . GLU A 450  ? 1.3716 1.2408 0.9091 0.3452  0.2485  0.2248  450  GLU A CB  
3417  C CG  . GLU A 450  ? 1.4637 1.3250 0.9846 0.3381  0.2210  0.2043  450  GLU A CG  
3418  C CD  . GLU A 450  ? 1.5572 1.4249 1.0614 0.3446  0.2219  0.2003  450  GLU A CD  
3419  O OE1 . GLU A 450  ? 1.6031 1.4875 1.1017 0.3524  0.2343  0.2213  450  GLU A OE1 
3420  O OE2 . GLU A 450  ? 1.5763 1.4328 1.0722 0.3428  0.2102  0.1762  450  GLU A OE2 
3421  N N   . GLY A 451  ? 1.2711 1.1517 0.8157 0.3712  0.3084  0.2612  451  GLY A N   
3422  C CA  . GLY A 451  ? 1.2487 1.1365 0.8002 0.3826  0.3306  0.2874  451  GLY A CA  
3423  C C   . GLY A 451  ? 1.2323 1.1453 0.7681 0.3878  0.3161  0.3103  451  GLY A C   
3424  O O   . GLY A 451  ? 1.2725 1.1951 0.7884 0.3841  0.2948  0.3049  451  GLY A O   
3425  N N   . TYR A 452  ? 1.1773 1.1022 0.7230 0.3971  0.3266  0.3345  452  TYR A N   
3426  C CA  . TYR A 452  ? 1.1816 1.1351 0.7170 0.4028  0.3116  0.3563  452  TYR A CA  
3427  C C   . TYR A 452  ? 1.2325 1.1911 0.7748 0.4205  0.3342  0.3834  452  TYR A C   
3428  O O   . TYR A 452  ? 1.2327 1.1711 0.7901 0.4258  0.3601  0.3841  452  TYR A O   
3429  C CB  . TYR A 452  ? 1.1562 1.1274 0.7012 0.3912  0.2877  0.3548  452  TYR A CB  
3430  C CG  . TYR A 452  ? 1.1633 1.1258 0.7001 0.3741  0.2635  0.3307  452  TYR A CG  
3431  C CD1 . TYR A 452  ? 1.2126 1.1928 0.7355 0.3661  0.2349  0.3303  452  TYR A CD1 
3432  C CD2 . TYR A 452  ? 1.1630 1.0993 0.7069 0.3664  0.2681  0.3079  452  TYR A CD2 
3433  C CE1 . TYR A 452  ? 1.2376 1.2060 0.7524 0.3508  0.2119  0.3090  452  TYR A CE1 
3434  C CE2 . TYR A 452  ? 1.1800 1.1062 0.7152 0.3526  0.2440  0.2866  452  TYR A CE2 
3435  C CZ  . TYR A 452  ? 1.2051 1.1458 0.7254 0.3450  0.2163  0.2880  452  TYR A CZ  
3436  O OH  . TYR A 452  ? 1.1837 1.1114 0.6942 0.3320  0.1917  0.2683  452  TYR A OH  
3437  N N   . ARG A 453  ? 1.2138 1.1984 0.7451 0.4304  0.3241  0.4049  453  ARG A N   
3438  C CA  . ARG A 453  ? 1.2026 1.1925 0.7389 0.4496  0.3423  0.4320  453  ARG A CA  
3439  C C   . ARG A 453  ? 1.2034 1.2316 0.7445 0.4561  0.3237  0.4510  453  ARG A C   
3440  O O   . ARG A 453  ? 1.2062 1.2578 0.7327 0.4506  0.2982  0.4498  453  ARG A O   
3441  C CB  . ARG A 453  ? 1.2350 1.2124 0.7461 0.4616  0.3567  0.4425  453  ARG A CB  
3442  C CG  . ARG A 453  ? 1.2655 1.2496 0.7759 0.4831  0.3698  0.4734  453  ARG A CG  
3443  C CD  . ARG A 453  ? 1.3223 1.3085 0.7994 0.4952  0.3709  0.4891  453  ARG A CD  
3444  N NE  . ARG A 453  ? 1.3834 1.3339 0.8508 0.4994  0.4014  0.4908  453  ARG A NE  
3445  C CZ  . ARG A 453  ? 1.4437 1.3827 0.8862 0.4934  0.4053  0.4799  453  ARG A CZ  
3446  N NH1 . ARG A 453  ? 1.4495 1.4089 0.8738 0.4844  0.3793  0.4660  453  ARG A NH1 
3447  N NH2 . ARG A 453  ? 1.4752 1.3827 0.9112 0.4960  0.4356  0.4824  453  ARG A NH2 
3448  N N   . ALA A 454  ? 1.2026 1.2384 0.7653 0.4679  0.3362  0.4673  454  ALA A N   
3449  C CA  . ALA A 454  ? 1.2714 1.3479 0.8443 0.4733  0.3187  0.4827  454  ALA A CA  
3450  C C   . ALA A 454  ? 1.3353 1.4194 0.9100 0.4986  0.3322  0.5098  454  ALA A C   
3451  O O   . ALA A 454  ? 1.3709 1.4265 0.9521 0.5098  0.3592  0.5160  454  ALA A O   
3452  C CB  . ALA A 454  ? 1.2080 1.2953 0.8093 0.4623  0.3158  0.4744  454  ALA A CB  
3453  N N   . ILE A 455  ? 1.3556 1.4780 0.9261 0.5079  0.3131  0.5258  455  ILE A N   
3454  C CA  . ILE A 455  ? 1.4003 1.5307 0.9656 0.5350  0.3218  0.5534  455  ILE A CA  
3455  C C   . ILE A 455  ? 1.3666 1.5454 0.9526 0.5451  0.3055  0.5675  455  ILE A C   
3456  O O   . ILE A 455  ? 1.3429 1.5568 0.9343 0.5309  0.2800  0.5591  455  ILE A O   
3457  C CB  . ILE A 455  ? 1.2994 1.4289 0.8274 0.5416  0.3136  0.5613  455  ILE A CB  
3458  C CG1 . ILE A 455  ? 1.3120 1.3945 0.8208 0.5388  0.3368  0.5540  455  ILE A CG1 
3459  C CG2 . ILE A 455  ? 1.3311 1.4813 0.8529 0.5679  0.3117  0.5895  455  ILE A CG2 
3460  C CD1 . ILE A 455  ? 1.3608 1.4425 0.8399 0.5243  0.3212  0.5376  455  ILE A CD1 
3461  N N   . ALA A 456  ? 1.3580 1.5393 0.9565 0.5696  0.3198  0.5886  456  ALA A N   
3462  C CA  . ALA A 456  ? 1.3308 1.5583 0.9574 0.5791  0.3082  0.5985  456  ALA A CA  
3463  C C   . ALA A 456  ? 1.3671 1.6406 0.9821 0.5899  0.2812  0.6126  456  ALA A C   
3464  O O   . ALA A 456  ? 1.3918 1.6574 0.9778 0.6071  0.2806  0.6286  456  ALA A O   
3465  C CB  . ALA A 456  ? 1.3415 1.5546 0.9900 0.6017  0.3332  0.6126  456  ALA A CB  
3466  N N   . TYR A 457  ? 1.3515 1.6734 0.9885 0.5783  0.2590  0.6059  457  TYR A N   
3467  C CA  . TYR A 457  ? 1.3903 1.7649 1.0274 0.5891  0.2334  0.6180  457  TYR A CA  
3468  C C   . TYR A 457  ? 1.4348 1.8141 1.0797 0.6240  0.2457  0.6432  457  TYR A C   
3469  O O   . TYR A 457  ? 1.4021 1.8038 1.0818 0.6346  0.2520  0.6483  457  TYR A O   
3470  C CB  . TYR A 457  ? 1.4163 1.8411 1.0870 0.5719  0.2152  0.6074  457  TYR A CB  
3471  C CG  . TYR A 457  ? 1.4927 1.9782 1.1680 0.5771  0.1854  0.6146  457  TYR A CG  
3472  C CD1 . TYR A 457  ? 1.5064 2.0334 1.2012 0.5519  0.1635  0.6002  457  TYR A CD1 
3473  C CD2 . TYR A 457  ? 1.5491 2.0504 1.2090 0.6063  0.1787  0.6356  457  TYR A CD2 
3474  C CE1 . TYR A 457  ? 1.5192 2.1041 1.2212 0.5546  0.1358  0.6045  457  TYR A CE1 
3475  C CE2 . TYR A 457  ? 1.5665 2.1272 1.2318 0.6112  0.1494  0.6404  457  TYR A CE2 
3476  C CZ  . TYR A 457  ? 1.5378 2.1410 1.2258 0.5845  0.1282  0.6237  457  TYR A CZ  
3477  O OH  . TYR A 457  ? 1.5325 2.1960 1.2288 0.5872  0.0993  0.6262  457  TYR A OH  
3478  N N   . SER A 458  ? 1.5196 1.8762 1.1300 0.6425  0.2495  0.6591  458  SER A N   
3479  C CA  . SER A 458  ? 1.6067 1.9608 1.2161 0.6778  0.2598  0.6859  458  SER A CA  
3480  C C   . SER A 458  ? 1.6150 2.0345 1.2372 0.6935  0.2318  0.6975  458  SER A C   
3481  O O   . SER A 458  ? 1.5760 2.0257 1.1790 0.6861  0.2055  0.6942  458  SER A O   
3482  C CB  . SER A 458  ? 1.6736 1.9818 1.2363 0.6883  0.2713  0.6985  458  SER A CB  
3483  O OG  . SER A 458  ? 1.6657 1.9348 1.2119 0.6614  0.2815  0.6777  458  SER A OG  
3484  N N   . SER A 459  ? 1.6643 2.1083 1.3215 0.7144  0.2368  0.7085  459  SER A N   
3485  C CA  . SER A 459  ? 1.6904 2.1988 1.3644 0.7329  0.2118  0.7198  459  SER A CA  
3486  C C   . SER A 459  ? 1.7426 2.2525 1.4391 0.7692  0.2259  0.7404  459  SER A C   
3487  O O   . SER A 459  ? 1.7121 2.2143 1.4423 0.7693  0.2449  0.7345  459  SER A O   
3488  C CB  . SER A 459  ? 1.6316 2.1967 1.3408 0.7071  0.1920  0.6995  459  SER A CB  
3489  O OG  . SER A 459  ? 1.6252 2.2509 1.3361 0.7143  0.1606  0.7046  459  SER A OG  
3490  N N   . LEU A 460  ? 1.8747 2.3938 1.5507 0.8011  0.2159  0.7645  460  LEU A N   
3491  C CA  . LEU A 460  ? 2.0103 2.5176 1.6983 0.8399  0.2302  0.7875  460  LEU A CA  
3492  C C   . LEU A 460  ? 2.0580 2.6248 1.8007 0.8511  0.2224  0.7839  460  LEU A C   
3493  O O   . LEU A 460  ? 2.0899 2.6443 1.8553 0.8770  0.2398  0.7946  460  LEU A O   
3494  C CB  . LEU A 460  ? 2.1312 2.6324 1.7786 0.8721  0.2193  0.8157  460  LEU A CB  
3495  C CG  . LEU A 460  ? 2.2404 2.6914 1.8782 0.9088  0.2431  0.8426  460  LEU A CG  
3496  C CD1 . LEU A 460  ? 2.2676 2.6383 1.8647 0.8988  0.2709  0.8466  460  LEU A CD1 
3497  C CD2 . LEU A 460  ? 2.3244 2.8005 1.9446 0.9497  0.2236  0.8716  460  LEU A CD2 
3498  N N   . SER A 461  ? 2.2849 2.4730 1.7238 1.2448  -0.1296 0.1940  461  SER A N   
3499  C CA  . SER A 461  ? 2.2944 2.5504 1.7625 1.2439  -0.1414 0.1627  461  SER A CA  
3500  C C   . SER A 461  ? 2.2543 2.4821 1.7509 1.2157  -0.1315 0.1607  461  SER A C   
3501  O O   . SER A 461  ? 2.2289 2.5036 1.7506 1.2092  -0.1371 0.1358  461  SER A O   
3502  C CB  . SER A 461  ? 2.2878 2.6235 1.7715 1.2198  -0.1501 0.1329  461  SER A CB  
3503  O OG  . SER A 461  ? 2.3418 2.7127 1.8008 1.2507  -0.1632 0.1299  461  SER A OG  
3504  N N   . GLN A 462  ? 2.2382 2.3885 1.7308 1.1987  -0.1167 0.1862  462  GLN A N   
3505  C CA  . GLN A 462  ? 2.1739 2.2897 1.6912 1.1686  -0.1081 0.1860  462  GLN A CA  
3506  C C   . GLN A 462  ? 2.0531 2.2167 1.5945 1.1222  -0.1097 0.1606  462  GLN A C   
3507  O O   . GLN A 462  ? 2.0322 2.1809 1.5932 1.0930  -0.1053 0.1540  462  GLN A O   
3508  C CB  . GLN A 462  ? 2.1880 2.3055 1.7144 1.1953  -0.1121 0.1801  462  GLN A CB  
3509  C CG  . GLN A 462  ? 2.2211 2.2618 1.7332 1.2242  -0.1045 0.2096  462  GLN A CG  
3510  C CD  . GLN A 462  ? 2.2011 2.1672 1.7228 1.1922  -0.0900 0.2281  462  GLN A CD  
3511  O OE1 . GLN A 462  ? 2.1354 2.1057 1.6730 1.1483  -0.0870 0.2192  462  GLN A OE1 
3512  N NE2 . GLN A 462  ? 2.2478 2.1438 1.7609 1.2145  -0.0816 0.2535  462  GLN A NE2 
3513  N N   . SER A 463  ? 1.9867 2.2065 1.5246 1.1159  -0.1163 0.1465  463  SER A N   
3514  C CA  . SER A 463  ? 1.8978 2.1734 1.4578 1.0755  -0.1189 0.1198  463  SER A CA  
3515  C C   . SER A 463  ? 1.8160 2.0544 1.3796 1.0325  -0.1102 0.1305  463  SER A C   
3516  O O   . SER A 463  ? 1.8594 2.0625 1.4058 1.0394  -0.1057 0.1505  463  SER A O   
3517  C CB  . SER A 463  ? 1.9070 2.2639 1.4645 1.0921  -0.1314 0.0975  463  SER A CB  
3518  O OG  . SER A 463  ? 1.8813 2.2862 1.4576 1.0513  -0.1320 0.0755  463  SER A OG  
3519  N N   . TYR A 464  ? 1.7129 1.9568 1.2979 0.9885  -0.1077 0.1172  464  TYR A N   
3520  C CA  . TYR A 464  ? 1.6432 1.8603 1.2348 0.9467  -0.1024 0.1236  464  TYR A CA  
3521  C C   . TYR A 464  ? 1.5848 1.8554 1.1959 0.9062  -0.1059 0.0966  464  TYR A C   
3522  O O   . TYR A 464  ? 1.5601 1.8898 1.1795 0.9111  -0.1108 0.0724  464  TYR A O   
3523  C CB  . TYR A 464  ? 1.6466 1.7775 1.2420 0.9300  -0.0937 0.1465  464  TYR A CB  
3524  C CG  . TYR A 464  ? 1.7096 1.7871 1.2914 0.9689  -0.0891 0.1690  464  TYR A CG  
3525  C CD1 . TYR A 464  ? 1.7607 1.8115 1.3217 0.9987  -0.0848 0.1897  464  TYR A CD1 
3526  C CD2 . TYR A 464  ? 1.7238 1.7748 1.3122 0.9750  -0.0883 0.1699  464  TYR A CD2 
3527  C CE1 . TYR A 464  ? 1.8231 1.8212 1.3707 1.0341  -0.0794 0.2114  464  TYR A CE1 
3528  C CE2 . TYR A 464  ? 1.7918 1.7928 1.3700 1.0102  -0.0839 0.1903  464  TYR A CE2 
3529  C CZ  . TYR A 464  ? 1.8432 1.8171 1.4013 1.0399  -0.0792 0.2115  464  TYR A CZ  
3530  O OH  . TYR A 464  ? 1.8925 1.8137 1.4397 1.0746  -0.0738 0.2324  464  TYR A OH  
3531  N N   . LEU A 465  ? 1.5577 1.8068 1.1771 0.8661  -0.1028 0.1002  465  LEU A N   
3532  C CA  . LEU A 465  ? 1.5488 1.8384 1.1857 0.8228  -0.1051 0.0770  465  LEU A CA  
3533  C C   . LEU A 465  ? 1.5523 1.7842 1.1984 0.7782  -0.1016 0.0883  465  LEU A C   
3534  O O   . LEU A 465  ? 1.5788 1.7600 1.2222 0.7780  -0.0979 0.1094  465  LEU A O   
3535  C CB  . LEU A 465  ? 1.5471 1.9135 1.1878 0.8224  -0.1105 0.0565  465  LEU A CB  
3536  C CG  . LEU A 465  ? 1.5415 1.9518 1.2011 0.7773  -0.1117 0.0320  465  LEU A CG  
3537  C CD1 . LEU A 465  ? 1.5635 2.0042 1.2306 0.7727  -0.1112 0.0116  465  LEU A CD1 
3538  C CD2 . LEU A 465  ? 1.5358 2.0153 1.2018 0.7751  -0.1166 0.0136  465  LEU A CD2 
3539  N N   . TYR A 466  ? 1.5055 1.7458 1.1625 0.7409  -0.1028 0.0733  466  TYR A N   
3540  C CA  . TYR A 466  ? 1.4461 1.6322 1.1115 0.6968  -0.1026 0.0813  466  TYR A CA  
3541  C C   . TYR A 466  ? 1.4224 1.6488 1.0976 0.6533  -0.1054 0.0589  466  TYR A C   
3542  O O   . TYR A 466  ? 1.4549 1.7074 1.1290 0.6432  -0.1050 0.0418  466  TYR A O   
3543  C CB  . TYR A 466  ? 1.4294 1.5550 1.0912 0.6943  -0.1016 0.0916  466  TYR A CB  
3544  C CG  . TYR A 466  ? 1.3768 1.4434 1.0463 0.6512  -0.1044 0.0998  466  TYR A CG  
3545  C CD1 . TYR A 466  ? 1.3661 1.4340 1.0462 0.6223  -0.1067 0.0998  466  TYR A CD1 
3546  C CD2 . TYR A 466  ? 1.3552 1.3628 1.0222 0.6407  -0.1059 0.1077  466  TYR A CD2 
3547  C CE1 . TYR A 466  ? 1.3503 1.3635 1.0395 0.5838  -0.1114 0.1071  466  TYR A CE1 
3548  C CE2 . TYR A 466  ? 1.3479 1.2985 1.0220 0.6024  -0.1113 0.1155  466  TYR A CE2 
3549  C CZ  . TYR A 466  ? 1.3302 1.2844 1.0161 0.5743  -0.1144 0.1152  466  TYR A CZ  
3550  O OH  . TYR A 466  ? 1.3103 1.2108 1.0061 0.5365  -0.1216 0.1219  466  TYR A OH  
3551  N N   . ILE A 467  ? 1.3674 1.5950 1.0524 0.6252  -0.1073 0.0590  467  ILE A N   
3552  C CA  . ILE A 467  ? 1.3340 1.5899 1.0280 0.5805  -0.1097 0.0399  467  ILE A CA  
3553  C C   . ILE A 467  ? 1.3380 1.5308 1.0387 0.5379  -0.1135 0.0512  467  ILE A C   
3554  O O   . ILE A 467  ? 1.3362 1.4814 1.0435 0.5372  -0.1145 0.0697  467  ILE A O   
3555  C CB  . ILE A 467  ? 1.2908 1.6223 0.9942 0.5777  -0.1105 0.0208  467  ILE A CB  
3556  C CG1 . ILE A 467  ? 1.2548 1.5641 0.9657 0.5717  -0.1119 0.0343  467  ILE A CG1 
3557  C CG2 . ILE A 467  ? 1.3116 1.7054 1.0097 0.6217  -0.1097 0.0086  467  ILE A CG2 
3558  C CD1 . ILE A 467  ? 1.2261 1.6036 0.9486 0.5595  -0.1137 0.0147  467  ILE A CD1 
3559  N N   . ASP A 468  ? 1.3538 1.5461 1.0531 0.5017  -0.1156 0.0393  468  ASP A N   
3560  C CA  . ASP A 468  ? 1.4256 1.5552 1.1292 0.4625  -0.1219 0.0498  468  ASP A CA  
3561  C C   . ASP A 468  ? 1.4138 1.5809 1.1168 0.4235  -0.1229 0.0288  468  ASP A C   
3562  O O   . ASP A 468  ? 1.3867 1.6268 1.0906 0.4299  -0.1177 0.0079  468  ASP A O   
3563  C CB  . ASP A 468  ? 1.5377 1.5948 1.2304 0.4651  -0.1244 0.0649  468  ASP A CB  
3564  C CG  . ASP A 468  ? 1.6125 1.5915 1.3135 0.4344  -0.1335 0.0811  468  ASP A CG  
3565  O OD1 . ASP A 468  ? 1.6223 1.6006 1.3394 0.4156  -0.1369 0.0831  468  ASP A OD1 
3566  O OD2 . ASP A 468  ? 1.6519 1.5697 1.3447 0.4294  -0.1382 0.0910  468  ASP A OD2 
3567  N N   . TRP A 469  ? 1.4873 1.6034 1.1891 0.3833  -0.1300 0.0338  469  TRP A N   
3568  C CA  . TRP A 469  ? 1.5879 1.7287 1.2857 0.3417  -0.1308 0.0161  469  TRP A CA  
3569  C C   . TRP A 469  ? 1.7634 1.8234 1.4548 0.3066  -0.1416 0.0297  469  TRP A C   
3570  O O   . TRP A 469  ? 1.7691 1.7710 1.4708 0.3125  -0.1486 0.0495  469  TRP A O   
3571  C CB  . TRP A 469  ? 1.5402 1.7325 1.2577 0.3287  -0.1306 0.0054  469  TRP A CB  
3572  C CG  . TRP A 469  ? 1.5100 1.6523 1.2438 0.3078  -0.1398 0.0206  469  TRP A CG  
3573  C CD1 . TRP A 469  ? 1.4986 1.6285 1.2404 0.2643  -0.1467 0.0166  469  TRP A CD1 
3574  C CD2 . TRP A 469  ? 1.5117 1.6101 1.2575 0.3292  -0.1423 0.0412  469  TRP A CD2 
3575  N NE1 . TRP A 469  ? 1.4765 1.5588 1.2370 0.2576  -0.1544 0.0324  469  TRP A NE1 
3576  C CE2 . TRP A 469  ? 1.4924 1.5551 1.2560 0.2966  -0.1509 0.0473  469  TRP A CE2 
3577  C CE3 . TRP A 469  ? 1.5342 1.6185 1.2778 0.3723  -0.1375 0.0549  469  TRP A CE3 
3578  C CZ2 . TRP A 469  ? 1.4986 1.5149 1.2800 0.3054  -0.1535 0.0648  469  TRP A CZ2 
3579  C CZ3 . TRP A 469  ? 1.5263 1.5620 1.2846 0.3804  -0.1391 0.0737  469  TRP A CZ3 
3580  C CH2 . TRP A 469  ? 1.5066 1.5103 1.2847 0.3470  -0.1465 0.0776  469  TRP A CH2 
3581  N N   . THR A 470  ? 1.9190 1.9710 1.5937 0.2698  -0.1435 0.0196  470  THR A N   
3582  C CA  . THR A 470  ? 2.0699 2.0454 1.7409 0.2332  -0.1576 0.0325  470  THR A CA  
3583  C C   . THR A 470  ? 2.2556 2.2409 1.9253 0.1862  -0.1618 0.0216  470  THR A C   
3584  O O   . THR A 470  ? 2.2766 2.3235 1.9406 0.1743  -0.1520 0.0012  470  THR A O   
3585  C CB  . THR A 470  ? 2.0545 1.9580 1.7018 0.2307  -0.1643 0.0438  470  THR A CB  
3586  O OG1 . THR A 470  ? 2.0539 1.9414 1.7059 0.2736  -0.1611 0.0558  470  THR A OG1 
3587  C CG2 . THR A 470  ? 2.0161 1.8398 1.6664 0.1989  -0.1823 0.0586  470  THR A CG2 
3588  N N   . ASP A 471  ? 2.4377 2.3590 2.1152 0.1604  -0.1769 0.0354  471  ASP A N   
3589  C CA  . ASP A 471  ? 2.6485 2.5613 2.3276 0.1150  -0.1851 0.0300  471  ASP A CA  
3590  C C   . ASP A 471  ? 2.8203 2.6391 2.5032 0.0983  -0.2050 0.0502  471  ASP A C   
3591  O O   . ASP A 471  ? 2.8132 2.6034 2.5204 0.1196  -0.2097 0.0641  471  ASP A O   
3592  C CB  . ASP A 471  ? 2.7073 2.6821 2.4173 0.1149  -0.1802 0.0205  471  ASP A CB  
3593  C CG  . ASP A 471  ? 2.8093 2.7883 2.5227 0.0680  -0.1862 0.0113  471  ASP A CG  
3594  O OD1 . ASP A 471  ? 2.8442 2.8880 2.5543 0.0558  -0.1752 -0.0086 471  ASP A OD1 
3595  O OD2 . ASP A 471  ? 2.8560 2.7740 2.5779 0.0428  -0.2022 0.0233  471  ASP A OD2 
3596  N N   . ASN A 472  ? 2.9761 2.7453 2.6346 0.0611  -0.2167 0.0513  472  ASN A N   
3597  C CA  . ASN A 472  ? 3.1115 2.7874 2.7703 0.0464  -0.2384 0.0691  472  ASN A CA  
3598  C C   . ASN A 472  ? 3.1856 2.8308 2.8806 0.0286  -0.2535 0.0772  472  ASN A C   
3599  O O   . ASN A 472  ? 3.1895 2.7596 2.8936 0.0228  -0.2716 0.0914  472  ASN A O   
3600  C CB  . ASN A 472  ? 3.1396 2.7643 2.7545 0.0152  -0.2482 0.0688  472  ASN A CB  
3601  C CG  . ASN A 472  ? 3.1140 2.7870 2.7034 -0.0146 -0.2374 0.0508  472  ASN A CG  
3602  O OD1 . ASN A 472  ? 3.0755 2.8240 2.6824 -0.0113 -0.2228 0.0370  472  ASN A OD1 
3603  N ND2 . ASN A 472  ? 3.1353 2.7628 2.6822 -0.0443 -0.2443 0.0503  472  ASN A ND2 
3604  N N   . HIS A 473  ? 3.2746 2.9773 2.9926 0.0206  -0.2465 0.0669  473  HIS A N   
3605  C CA  . HIS A 473  ? 3.3646 3.0433 3.1196 0.0033  -0.2594 0.0723  473  HIS A CA  
3606  C C   . HIS A 473  ? 3.1616 2.8768 2.9561 0.0327  -0.2497 0.0737  473  HIS A C   
3607  O O   . HIS A 473  ? 3.1413 2.9246 2.9356 0.0606  -0.2316 0.0653  473  HIS A O   
3608  C CB  . HIS A 473  ? 3.6470 3.3423 3.3993 -0.0396 -0.2647 0.0613  473  HIS A CB  
3609  C CG  . HIS A 473  ? 3.9189 3.6829 3.6439 -0.0467 -0.2474 0.0433  473  HIS A CG  
3610  N ND1 . HIS A 473  ? 4.0073 3.8587 3.7496 -0.0332 -0.2299 0.0278  473  HIS A ND1 
3611  C CD2 . HIS A 473  ? 4.0631 3.8190 3.7460 -0.0663 -0.2451 0.0374  473  HIS A CD2 
3612  C CE1 . HIS A 473  ? 4.2079 4.1042 3.9236 -0.0445 -0.2174 0.0121  473  HIS A CE1 
3613  N NE2 . HIS A 473  ? 4.1253 3.9662 3.8043 -0.0648 -0.2247 0.0175  473  HIS A NE2 
3614  N N   . LYS A 474  ? 3.0043 2.6719 2.8323 0.0248  -0.2627 0.0836  474  LYS A N   
3615  C CA  . LYS A 474  ? 2.8418 2.5225 2.7056 0.0526  -0.2545 0.0884  474  LYS A CA  
3616  C C   . LYS A 474  ? 2.6597 2.4223 2.5392 0.0579  -0.2400 0.0746  474  LYS A C   
3617  O O   . LYS A 474  ? 2.6669 2.4470 2.5704 0.0822  -0.2309 0.0772  474  LYS A O   
3618  C CB  . LYS A 474  ? 2.8727 2.4806 2.7723 0.0389  -0.2716 0.1000  474  LYS A CB  
3619  C CG  . LYS A 474  ? 2.9001 2.4815 2.8106 -0.0063 -0.2907 0.0958  474  LYS A CG  
3620  C CD  . LYS A 474  ? 2.9081 2.4324 2.8648 -0.0146 -0.3049 0.1039  474  LYS A CD  
3621  C CE  . LYS A 474  ? 2.8905 2.4587 2.8834 0.0058  -0.2884 0.1004  474  LYS A CE  
3622  N NZ  . LYS A 474  ? 2.8820 2.4001 2.9241 -0.0063 -0.3002 0.1049  474  LYS A NZ  
3623  N N   . ALA A 475  ? 2.4448 2.2571 2.3102 0.0356  -0.2373 0.0592  475  ALA A N   
3624  C CA  . ALA A 475  ? 2.2076 2.0968 2.0909 0.0388  -0.2257 0.0444  475  ALA A CA  
3625  C C   . ALA A 475  ? 2.0197 1.9745 1.8776 0.0320  -0.2156 0.0268  475  ALA A C   
3626  O O   . ALA A 475  ? 2.0034 1.9390 1.8391 0.0024  -0.2218 0.0235  475  ALA A O   
3627  C CB  . ALA A 475  ? 2.1934 2.0677 2.1098 0.0065  -0.2370 0.0419  475  ALA A CB  
3628  N N   . LEU A 476  ? 1.8368 1.8676 1.6972 0.0597  -0.2000 0.0149  476  LEU A N   
3629  C CA  . LEU A 476  ? 1.6831 1.7826 1.5259 0.0552  -0.1895 -0.0048 476  LEU A CA  
3630  C C   . LEU A 476  ? 1.6077 1.7446 1.4702 0.0218  -0.1912 -0.0200 476  LEU A C   
3631  O O   . LEU A 476  ? 1.6143 1.7849 1.5048 0.0288  -0.1893 -0.0252 476  LEU A O   
3632  C CB  . LEU A 476  ? 1.5725 1.7390 1.4122 0.0993  -0.1746 -0.0129 476  LEU A CB  
3633  C CG  . LEU A 476  ? 1.4910 1.6227 1.3225 0.1394  -0.1725 0.0045  476  LEU A CG  
3634  C CD1 . LEU A 476  ? 1.4599 1.6583 1.2819 0.1799  -0.1593 -0.0053 476  LEU A CD1 
3635  C CD2 . LEU A 476  ? 1.5030 1.5667 1.3111 0.1309  -0.1793 0.0171  476  LEU A CD2 
3636  N N   . LEU A 477  ? 1.5351 1.6639 1.3820 -0.0155 -0.1945 -0.0274 477  LEU A N   
3637  C CA  . LEU A 477  ? 1.4604 1.6239 1.3251 -0.0492 -0.1953 -0.0424 477  LEU A CA  
3638  C C   . LEU A 477  ? 1.3505 1.6116 1.2225 -0.0320 -0.1790 -0.0652 477  LEU A C   
3639  O O   . LEU A 477  ? 1.3446 1.6397 1.1963 -0.0120 -0.1679 -0.0729 477  LEU A O   
3640  C CB  . LEU A 477  ? 1.5353 1.6607 1.3764 -0.0933 -0.2019 -0.0434 477  LEU A CB  
3641  C CG  . LEU A 477  ? 1.6274 1.6523 1.4520 -0.1051 -0.2196 -0.0208 477  LEU A CG  
3642  C CD1 . LEU A 477  ? 1.7007 1.6893 1.4865 -0.1409 -0.2233 -0.0217 477  LEU A CD1 
3643  C CD2 . LEU A 477  ? 1.6336 1.6078 1.4919 -0.1185 -0.2372 -0.0089 477  LEU A CD2 
3644  N N   . VAL A 478  ? 1.2919 1.5974 1.1952 -0.0385 -0.1785 -0.0768 478  VAL A N   
3645  C CA  . VAL A 478  ? 1.2910 1.6906 1.2056 -0.0258 -0.1656 -0.1010 478  VAL A CA  
3646  C C   . VAL A 478  ? 1.3099 1.7331 1.2091 -0.0568 -0.1587 -0.1171 478  VAL A C   
3647  O O   . VAL A 478  ? 1.3040 1.6795 1.1956 -0.0966 -0.1660 -0.1120 478  VAL A O   
3648  C CB  . VAL A 478  ? 1.2822 1.7159 1.2329 -0.0357 -0.1684 -0.1108 478  VAL A CB  
3649  C CG1 . VAL A 478  ? 1.2982 1.7467 1.2575 -0.0828 -0.1693 -0.1257 478  VAL A CG1 
3650  C CG2 . VAL A 478  ? 1.2734 1.7888 1.2363 0.0017  -0.1587 -0.1265 478  VAL A CG2 
3651  N N   . GLY A 479  ? 1.3477 1.8434 1.2428 -0.0392 -0.1447 -0.1371 479  GLY A N   
3652  C CA  . GLY A 479  ? 1.4086 1.9244 1.2858 -0.0649 -0.1345 -0.1525 479  GLY A CA  
3653  C C   . GLY A 479  ? 1.4402 1.9308 1.2824 -0.0478 -0.1287 -0.1456 479  GLY A C   
3654  O O   . GLY A 479  ? 1.4897 2.0208 1.3199 -0.0522 -0.1151 -0.1635 479  GLY A O   
3655  N N   . GLU A 480  ? 1.4545 1.8788 1.2823 -0.0286 -0.1382 -0.1210 480  GLU A N   
3656  C CA  . GLU A 480  ? 1.4609 1.8565 1.2563 -0.0110 -0.1340 -0.1134 480  GLU A CA  
3657  C C   . GLU A 480  ? 1.4429 1.9070 1.2427 0.0340  -0.1222 -0.1265 480  GLU A C   
3658  O O   . GLU A 480  ? 1.4154 1.9479 1.2412 0.0511  -0.1184 -0.1414 480  GLU A O   
3659  C CB  . GLU A 480  ? 1.5075 1.8120 1.2897 -0.0039 -0.1482 -0.0844 480  GLU A CB  
3660  C CG  . GLU A 480  ? 1.6352 1.8608 1.3926 -0.0470 -0.1586 -0.0728 480  GLU A CG  
3661  C CD  . GLU A 480  ? 1.7590 1.8953 1.5016 -0.0365 -0.1728 -0.0465 480  GLU A CD  
3662  O OE1 . GLU A 480  ? 1.8055 1.8737 1.5211 -0.0645 -0.1824 -0.0366 480  GLU A OE1 
3663  O OE2 . GLU A 480  ? 1.7966 1.9287 1.5540 0.0003  -0.1745 -0.0358 480  GLU A OE2 
3664  N N   . HIS A 481  ? 1.4807 1.9265 1.2550 0.0531  -0.1173 -0.1219 481  HIS A N   
3665  C CA  . HIS A 481  ? 1.5039 2.0126 1.2815 0.0950  -0.1069 -0.1353 481  HIS A CA  
3666  C C   . HIS A 481  ? 1.4670 1.9259 1.2260 0.1288  -0.1107 -0.1148 481  HIS A C   
3667  O O   . HIS A 481  ? 1.4629 1.8687 1.1947 0.1177  -0.1108 -0.1059 481  HIS A O   
3668  C CB  . HIS A 481  ? 1.6034 2.1625 1.3724 0.0810  -0.0913 -0.1612 481  HIS A CB  
3669  C CG  . HIS A 481  ? 1.6613 2.3004 1.4578 0.0659  -0.0834 -0.1887 481  HIS A CG  
3670  N ND1 . HIS A 481  ? 1.6830 2.4082 1.5021 0.0973  -0.0760 -0.2116 481  HIS A ND1 
3671  C CD2 . HIS A 481  ? 1.6878 2.3337 1.4941 0.0227  -0.0824 -0.1981 481  HIS A CD2 
3672  C CE1 . HIS A 481  ? 1.6903 2.4730 1.5335 0.0742  -0.0706 -0.2346 481  HIS A CE1 
3673  N NE2 . HIS A 481  ? 1.6947 2.4309 1.5307 0.0284  -0.0734 -0.2267 481  HIS A NE2 
3674  N N   . LEU A 482  ? 1.4420 1.9187 1.2148 0.1703  -0.1136 -0.1079 482  LEU A N   
3675  C CA  . LEU A 482  ? 1.4506 1.8764 1.2103 0.2041  -0.1178 -0.0858 482  LEU A CA  
3676  C C   . LEU A 482  ? 1.4734 1.9296 1.2200 0.2378  -0.1088 -0.0944 482  LEU A C   
3677  O O   . LEU A 482  ? 1.4889 2.0091 1.2475 0.2717  -0.1044 -0.1069 482  LEU A O   
3678  C CB  . LEU A 482  ? 1.4199 1.8449 1.1978 0.2319  -0.1237 -0.0731 482  LEU A CB  
3679  C CG  . LEU A 482  ? 1.4027 1.7508 1.1727 0.2516  -0.1302 -0.0445 482  LEU A CG  
3680  C CD1 . LEU A 482  ? 1.3583 1.6947 1.1484 0.2608  -0.1353 -0.0328 482  LEU A CD1 
3681  C CD2 . LEU A 482  ? 1.4227 1.7749 1.1772 0.2949  -0.1248 -0.0405 482  LEU A CD2 
3682  N N   . ASN A 483  ? 1.4761 1.8859 1.1981 0.2294  -0.1070 -0.0882 483  ASN A N   
3683  C CA  . ASN A 483  ? 1.4728 1.9035 1.1838 0.2630  -0.0992 -0.0944 483  ASN A CA  
3684  C C   . ASN A 483  ? 1.4545 1.8389 1.1616 0.3022  -0.1056 -0.0702 483  ASN A C   
3685  O O   . ASN A 483  ? 1.4734 1.7792 1.1684 0.2927  -0.1130 -0.0486 483  ASN A O   
3686  C CB  . ASN A 483  ? 1.5276 1.9323 1.2125 0.2381  -0.0926 -0.1009 483  ASN A CB  
3687  C CG  . ASN A 483  ? 1.5639 2.0174 1.2452 0.2667  -0.0808 -0.1186 483  ASN A CG  
3688  O OD1 . ASN A 483  ? 1.5561 2.0898 1.2562 0.2779  -0.0727 -0.1427 483  ASN A OD1 
3689  N ND2 . ASN A 483  ? 1.5945 2.0001 1.2541 0.2789  -0.0803 -0.1081 483  ASN A ND2 
3690  N N   . ILE A 484  ? 1.3971 1.8294 1.1145 0.3461  -0.1029 -0.0746 484  ILE A N   
3691  C CA  . ILE A 484  ? 1.3453 1.7407 1.0616 0.3849  -0.1078 -0.0518 484  ILE A CA  
3692  C C   . ILE A 484  ? 1.3080 1.7265 1.0169 0.4291  -0.1029 -0.0554 484  ILE A C   
3693  O O   . ILE A 484  ? 1.3021 1.7941 1.0199 0.4488  -0.0984 -0.0764 484  ILE A O   
3694  C CB  . ILE A 484  ? 1.3179 1.7366 1.0521 0.3968  -0.1119 -0.0477 484  ILE A CB  
3695  C CG1 . ILE A 484  ? 1.3067 1.7218 1.0381 0.4478  -0.1123 -0.0338 484  ILE A CG1 
3696  C CG2 . ILE A 484  ? 1.3025 1.8065 1.0527 0.3882  -0.1086 -0.0752 484  ILE A CG2 
3697  C CD1 . ILE A 484  ? 1.2673 1.7038 1.0113 0.4595  -0.1152 -0.0304 484  ILE A CD1 
3698  N N   . ILE A 485  ? 1.2767 1.6309 0.9717 0.4449  -0.1047 -0.0352 485  ILE A N   
3699  C CA  . ILE A 485  ? 1.2853 1.6484 0.9707 0.4782  -0.0999 -0.0389 485  ILE A CA  
3700  C C   . ILE A 485  ? 1.3271 1.7023 1.0154 0.5312  -0.1009 -0.0292 485  ILE A C   
3701  O O   . ILE A 485  ? 1.3555 1.6723 1.0395 0.5481  -0.1043 -0.0041 485  ILE A O   
3702  C CB  . ILE A 485  ? 1.2809 1.5689 0.9487 0.4676  -0.1010 -0.0244 485  ILE A CB  
3703  C CG1 . ILE A 485  ? 1.2747 1.5629 0.9315 0.4229  -0.0976 -0.0400 485  ILE A CG1 
3704  C CG2 . ILE A 485  ? 1.3130 1.6038 0.9740 0.5085  -0.0970 -0.0240 485  ILE A CG2 
3705  C CD1 . ILE A 485  ? 1.2608 1.6146 0.9305 0.3972  -0.0941 -0.0618 485  ILE A CD1 
3706  N N   . VAL A 486  ? 1.3025 1.7516 0.9979 0.5574  -0.0977 -0.0499 486  VAL A N   
3707  C CA  . VAL A 486  ? 1.2894 1.7596 0.9860 0.6075  -0.1005 -0.0437 486  VAL A CA  
3708  C C   . VAL A 486  ? 1.3075 1.7587 0.9947 0.6394  -0.0982 -0.0392 486  VAL A C   
3709  O O   . VAL A 486  ? 1.3368 1.8366 1.0285 0.6485  -0.0945 -0.0614 486  VAL A O   
3710  C CB  . VAL A 486  ? 1.2755 1.8377 0.9869 0.6209  -0.1013 -0.0702 486  VAL A CB  
3711  C CG1 . VAL A 486  ? 1.2995 1.8738 1.0088 0.6639  -0.1074 -0.0593 486  VAL A CG1 
3712  C CG2 . VAL A 486  ? 1.2248 1.8191 0.9491 0.5771  -0.1004 -0.0860 486  VAL A CG2 
3713  N N   . THR A 487  ? 1.3433 1.7233 1.0198 0.6557  -0.0999 -0.0116 487  THR A N   
3714  C CA  . THR A 487  ? 1.3647 1.7197 1.0329 0.6886  -0.0981 -0.0045 487  THR A CA  
3715  C C   . THR A 487  ? 1.3896 1.7446 1.0542 0.7391  -0.1011 0.0103  487  THR A C   
3716  O O   . THR A 487  ? 1.3822 1.6808 1.0407 0.7462  -0.1019 0.0360  487  THR A O   
3717  C CB  . THR A 487  ? 1.4104 1.6783 1.0687 0.6696  -0.0974 0.0150  487  THR A CB  
3718  O OG1 . THR A 487  ? 1.4170 1.6284 1.0760 0.6561  -0.1009 0.0382  487  THR A OG1 
3719  C CG2 . THR A 487  ? 1.3843 1.6520 1.0387 0.6259  -0.0946 -0.0014 487  THR A CG2 
3720  N N   . PRO A 488  ? 1.4247 1.8415 1.0930 0.7741  -0.1026 -0.0064 488  PRO A N   
3721  C CA  . PRO A 488  ? 1.4721 1.8975 1.1336 0.8246  -0.1072 0.0042  488  PRO A CA  
3722  C C   . PRO A 488  ? 1.5825 1.9509 1.2334 0.8562  -0.1056 0.0246  488  PRO A C   
3723  O O   . PRO A 488  ? 1.5302 1.8921 1.1715 0.8968  -0.1088 0.0379  488  PRO A O   
3724  C CB  . PRO A 488  ? 1.4417 1.9559 1.1152 0.8439  -0.1112 -0.0264 488  PRO A CB  
3725  C CG  . PRO A 488  ? 1.4112 1.9658 1.0994 0.8000  -0.1067 -0.0524 488  PRO A CG  
3726  C CD  . PRO A 488  ? 1.4139 1.9004 1.0944 0.7652  -0.1003 -0.0394 488  PRO A CD  
3727  N N   . LYS A 489  ? 1.7681 2.0944 1.4192 0.8370  -0.1010 0.0268  489  LYS A N   
3728  C CA  . LYS A 489  ? 1.9614 2.2267 1.6049 0.8615  -0.0989 0.0460  489  LYS A CA  
3729  C C   . LYS A 489  ? 2.0975 2.3430 1.7310 0.9091  -0.1011 0.0670  489  LYS A C   
3730  O O   . LYS A 489  ? 2.1129 2.3475 1.7396 0.9130  -0.1020 0.0813  489  LYS A O   
3731  C CB  . LYS A 489  ? 1.9944 2.1796 1.6349 0.8284  -0.0959 0.0644  489  LYS A CB  
3732  C CG  . LYS A 489  ? 2.0509 2.1666 1.6861 0.8515  -0.0937 0.0854  489  LYS A CG  
3733  C CD  . LYS A 489  ? 2.0859 2.1520 1.7212 0.8167  -0.0925 0.0852  489  LYS A CD  
3734  C CE  . LYS A 489  ? 2.1325 2.1571 1.7656 0.8413  -0.0905 0.0925  489  LYS A CE  
3735  N NZ  . LYS A 489  ? 2.1624 2.2440 1.7976 0.8702  -0.0893 0.0721  489  LYS A NZ  
3736  N N   . SER A 490  ? 2.2065 2.4468 1.8382 0.9447  -0.1014 0.0681  490  SER A N   
3737  C CA  . SER A 490  ? 2.3028 2.5107 1.9222 0.9912  -0.1026 0.0904  490  SER A CA  
3738  C C   . SER A 490  ? 2.3458 2.6168 1.9619 1.0338  -0.1107 0.0786  490  SER A C   
3739  O O   . SER A 490  ? 2.3904 2.6685 2.0080 1.0678  -0.1134 0.0749  490  SER A O   
3740  C CB  . SER A 490  ? 2.3477 2.4920 1.9563 0.9853  -0.0984 0.1199  490  SER A CB  
3741  O OG  . SER A 490  ? 2.3632 2.4509 1.9791 0.9464  -0.0935 0.1282  490  SER A OG  
3742  N N   . PRO A 491  ? 2.3227 2.6409 1.9359 1.0320  -0.1159 0.0708  491  PRO A N   
3743  C CA  . PRO A 491  ? 2.2818 2.6577 1.8904 1.0732  -0.1264 0.0597  491  PRO A CA  
3744  C C   . PRO A 491  ? 2.1608 2.5587 1.7788 1.1042  -0.1304 0.0466  491  PRO A C   
3745  O O   . PRO A 491  ? 2.0965 2.5294 1.7347 1.0866  -0.1283 0.0219  491  PRO A O   
3746  C CB  . PRO A 491  ? 2.3121 2.7630 1.9348 1.0470  -0.1306 0.0316  491  PRO A CB  
3747  C CG  . PRO A 491  ? 2.3242 2.7350 1.9444 1.0025  -0.1229 0.0446  491  PRO A CG  
3748  C CD  . PRO A 491  ? 2.3251 2.6513 1.9413 0.9911  -0.1139 0.0682  491  PRO A CD  
3749  N N   . TYR A 492  ? 2.1179 2.4902 1.7198 1.1504  -0.1352 0.0643  492  TYR A N   
3750  C CA  . TYR A 492  ? 2.0953 2.4785 1.7054 1.1841  -0.1396 0.0561  492  TYR A CA  
3751  C C   . TYR A 492  ? 2.0739 2.5423 1.7102 1.1747  -0.1448 0.0169  492  TYR A C   
3752  O O   . TYR A 492  ? 2.1011 2.5837 1.7546 1.1810  -0.1435 0.0011  492  TYR A O   
3753  C CB  . TYR A 492  ? 2.1231 2.4975 1.7124 1.2384  -0.1498 0.0718  492  TYR A CB  
3754  C CG  . TYR A 492  ? 2.0966 2.5418 1.6820 1.2617  -0.1653 0.0547  492  TYR A CG  
3755  C CD1 . TYR A 492  ? 2.1153 2.5660 1.6850 1.3152  -0.1789 0.0609  492  TYR A CD1 
3756  C CD2 . TYR A 492  ? 2.0375 2.5415 1.6344 1.2314  -0.1676 0.0326  492  TYR A CD2 
3757  C CE1 . TYR A 492  ? 2.1059 2.6179 1.6708 1.3382  -0.1956 0.0452  492  TYR A CE1 
3758  C CE2 . TYR A 492  ? 2.0283 2.5962 1.6231 1.2540  -0.1830 0.0160  492  TYR A CE2 
3759  C CZ  . TYR A 492  ? 2.0721 2.6433 1.6504 1.3076  -0.1976 0.0223  492  TYR A CZ  
3760  O OH  . TYR A 492  ? 2.0952 2.7277 1.6703 1.3311  -0.2153 0.0055  492  TYR A OH  
3761  N N   . ILE A 493  ? 2.0658 2.5916 1.7075 1.1581  -0.1496 -0.0007 493  ILE A N   
3762  C CA  . ILE A 493  ? 2.0973 2.7034 1.7685 1.1434  -0.1515 -0.0403 493  ILE A CA  
3763  C C   . ILE A 493  ? 2.1135 2.7626 1.7972 1.0957  -0.1471 -0.0598 493  ILE A C   
3764  O O   . ILE A 493  ? 2.1237 2.7475 1.7938 1.0734  -0.1447 -0.0441 493  ILE A O   
3765  C CB  . ILE A 493  ? 2.9794 3.6475 2.6639 1.1914  -0.1664 -0.0616 493  ILE A CB  
3766  C CG1 . ILE A 493  ? 2.9915 3.6496 2.6906 1.2093  -0.1633 -0.0690 493  ILE A CG1 
3767  C CG2 . ILE A 493  ? 2.9591 3.7198 2.6702 1.1787  -0.1722 -0.1001 493  ILE A CG2 
3768  C CD1 . ILE A 493  ? 3.0152 3.7311 2.7320 1.2570  -0.1786 -0.0911 493  ILE A CD1 
3769  N N   . ASP A 494  ? 2.1164 2.8282 1.8278 1.0803  -0.1447 -0.0949 494  ASP A N   
3770  C CA  . ASP A 494  ? 2.0835 2.8387 1.8118 1.0323  -0.1373 -0.1192 494  ASP A CA  
3771  C C   . ASP A 494  ? 2.0842 2.9300 1.8339 1.0403  -0.1470 -0.1505 494  ASP A C   
3772  O O   . ASP A 494  ? 2.0630 2.9578 1.8339 1.0051  -0.1402 -0.1780 494  ASP A O   
3773  C CB  . ASP A 494  ? 2.0834 2.8454 1.8283 1.0082  -0.1249 -0.1395 494  ASP A CB  
3774  C CG  . ASP A 494  ? 2.0149 2.8327 1.7841 1.0439  -0.1295 -0.1673 494  ASP A CG  
3775  O OD1 . ASP A 494  ? 2.0224 2.8319 1.7867 1.0927  -0.1410 -0.1564 494  ASP A OD1 
3776  O OD2 . ASP A 494  ? 1.9999 2.8679 1.7935 1.0224  -0.1210 -0.2002 494  ASP A OD2 
3777  N N   . LYS A 495  ? 2.1049 2.9729 1.8492 1.0861  -0.1630 -0.1476 495  LYS A N   
3778  C CA  . LYS A 495  ? 2.0806 3.0364 1.8475 1.0984  -0.1751 -0.1796 495  LYS A CA  
3779  C C   . LYS A 495  ? 2.0002 2.9759 1.7640 1.0685  -0.1756 -0.1813 495  LYS A C   
3780  O O   . LYS A 495  ? 1.9840 3.0037 1.7487 1.0897  -0.1901 -0.1902 495  LYS A O   
3781  C CB  . LYS A 495  ? 2.1471 3.1208 1.9083 1.1590  -0.1948 -0.1780 495  LYS A CB  
3782  C CG  . LYS A 495  ? 2.1793 3.1743 1.9624 1.1890  -0.1978 -0.1956 495  LYS A CG  
3783  C CD  . LYS A 495  ? 2.1456 3.1894 1.9663 1.1533  -0.1837 -0.2317 495  LYS A CD  
3784  C CE  . LYS A 495  ? 2.1140 3.0933 1.9239 1.1185  -0.1636 -0.2158 495  LYS A CE  
3785  N NZ  . LYS A 495  ? 2.0619 3.0602 1.8839 1.0607  -0.1474 -0.2331 495  LYS A NZ  
3786  N N   . ILE A 496  ? 1.9354 2.8775 1.6957 1.0189  -0.1607 -0.1733 496  ILE A N   
3787  C CA  . ILE A 496  ? 1.8883 2.8408 1.6466 0.9859  -0.1595 -0.1731 496  ILE A CA  
3788  C C   . ILE A 496  ? 1.8954 2.9379 1.6882 0.9666  -0.1605 -0.2144 496  ILE A C   
3789  O O   . ILE A 496  ? 1.8821 2.9546 1.6984 0.9435  -0.1500 -0.2391 496  ILE A O   
3790  C CB  . ILE A 496  ? 1.8213 2.7054 1.5660 0.9390  -0.1449 -0.1513 496  ILE A CB  
3791  C CG1 . ILE A 496  ? 1.7741 2.5702 1.4924 0.9563  -0.1419 -0.1150 496  ILE A CG1 
3792  C CG2 . ILE A 496  ? 1.8433 2.7260 1.5822 0.9129  -0.1460 -0.1441 496  ILE A CG2 
3793  C CD1 . ILE A 496  ? 1.7379 2.5081 1.4616 0.9509  -0.1325 -0.1179 496  ILE A CD1 
3794  N N   . THR A 497  ? 1.9446 3.0293 1.7399 0.9765  -0.1724 -0.2223 497  THR A N   
3795  C CA  . THR A 497  ? 1.9804 3.1497 1.8098 0.9576  -0.1740 -0.2608 497  THR A CA  
3796  C C   . THR A 497  ? 1.9651 3.1246 1.7988 0.8989  -0.1601 -0.2616 497  THR A C   
3797  O O   . THR A 497  ? 1.9644 3.1428 1.8181 0.8631  -0.1465 -0.2815 497  THR A O   
3798  C CB  . THR A 497  ? 2.0566 3.2737 1.8861 0.9920  -0.1941 -0.2693 497  THR A CB  
3799  O OG1 . THR A 497  ? 2.0493 3.3414 1.9117 0.9662  -0.1944 -0.3039 497  THR A OG1 
3800  C CG2 . THR A 497  ? 2.0838 3.2398 1.8734 0.9990  -0.1987 -0.2321 497  THR A CG2 
3801  N N   . HIS A 498  ? 1.9517 3.0787 1.7650 0.8894  -0.1634 -0.2396 498  HIS A N   
3802  C CA  . HIS A 498  ? 1.9011 3.0188 1.7189 0.8367  -0.1534 -0.2394 498  HIS A CA  
3803  C C   . HIS A 498  ? 1.8497 2.8779 1.6357 0.8244  -0.1493 -0.1991 498  HIS A C   
3804  O O   . HIS A 498  ? 1.8719 2.8633 1.6331 0.8587  -0.1571 -0.1744 498  HIS A O   
3805  C CB  . HIS A 498  ? 1.9348 3.1166 1.7688 0.8337  -0.1628 -0.2599 498  HIS A CB  
3806  C CG  . HIS A 498  ? 1.9788 3.2532 1.8520 0.8351  -0.1654 -0.3037 498  HIS A CG  
3807  N ND1 . HIS A 498  ? 2.0140 3.3468 1.8988 0.8803  -0.1825 -0.3226 498  HIS A ND1 
3808  C CD2 . HIS A 498  ? 1.9691 3.2868 1.8732 0.7962  -0.1530 -0.3331 498  HIS A CD2 
3809  C CE1 . HIS A 498  ? 2.0167 3.4274 1.9425 0.8696  -0.1806 -0.3632 498  HIS A CE1 
3810  N NE2 . HIS A 498  ? 1.9893 3.3923 1.9269 0.8183  -0.1615 -0.3702 498  HIS A NE2 
3811  N N   . TYR A 499  ? 1.7254 2.7178 1.5125 0.7753  -0.1372 -0.1930 499  TYR A N   
3812  C CA  . TYR A 499  ? 1.6275 2.5468 1.3939 0.7560  -0.1345 -0.1610 499  TYR A CA  
3813  C C   . TYR A 499  ? 1.5415 2.4942 1.3176 0.7367  -0.1386 -0.1697 499  TYR A C   
3814  O O   . TYR A 499  ? 1.4992 2.5118 1.3003 0.7113  -0.1367 -0.1986 499  TYR A O   
3815  C CB  . TYR A 499  ? 1.5943 2.4597 1.3582 0.7122  -0.1225 -0.1519 499  TYR A CB  
3816  C CG  . TYR A 499  ? 1.6027 2.4292 1.3561 0.7271  -0.1178 -0.1429 499  TYR A CG  
3817  C CD1 . TYR A 499  ? 1.6159 2.3720 1.3468 0.7522  -0.1194 -0.1110 499  TYR A CD1 
3818  C CD2 . TYR A 499  ? 1.6211 2.4811 1.3882 0.7155  -0.1105 -0.1672 499  TYR A CD2 
3819  C CE1 . TYR A 499  ? 1.6346 2.3552 1.3576 0.7660  -0.1152 -0.1036 499  TYR A CE1 
3820  C CE2 . TYR A 499  ? 1.6394 2.4644 1.3973 0.7285  -0.1058 -0.1605 499  TYR A CE2 
3821  C CZ  . TYR A 499  ? 1.6463 2.4022 1.3827 0.7542  -0.1089 -0.1288 499  TYR A CZ  
3822  O OH  . TYR A 499  ? 1.6508 2.3742 1.3802 0.7669  -0.1043 -0.1239 499  TYR A OH  
3823  N N   . ASN A 500  ? 1.5183 2.4317 1.2755 0.7478  -0.1429 -0.1455 500  ASN A N   
3824  C CA  . ASN A 500  ? 1.4786 2.4156 1.2431 0.7292  -0.1463 -0.1510 500  ASN A CA  
3825  C C   . ASN A 500  ? 1.4123 2.2747 1.1651 0.7009  -0.1405 -0.1228 500  ASN A C   
3826  O O   . ASN A 500  ? 1.4347 2.2316 1.1649 0.7192  -0.1389 -0.0936 500  ASN A O   
3827  C CB  . ASN A 500  ? 1.5065 2.4830 1.2614 0.7729  -0.1591 -0.1553 500  ASN A CB  
3828  C CG  . ASN A 500  ? 1.5430 2.5626 1.2988 0.8174  -0.1676 -0.1699 500  ASN A CG  
3829  O OD1 . ASN A 500  ? 1.5434 2.6210 1.3256 0.8109  -0.1674 -0.1994 500  ASN A OD1 
3830  N ND2 . ASN A 500  ? 1.5699 2.5606 1.2973 0.8632  -0.1749 -0.1497 500  ASN A ND2 
3831  N N   . TYR A 501  ? 1.3565 2.2287 1.1271 0.6559  -0.1371 -0.1325 501  TYR A N   
3832  C CA  . TYR A 501  ? 1.3235 2.1304 1.0887 0.6280  -0.1332 -0.1092 501  TYR A CA  
3833  C C   . TYR A 501  ? 1.3104 2.1427 1.0807 0.6250  -0.1377 -0.1135 501  TYR A C   
3834  O O   . TYR A 501  ? 1.3032 2.2034 1.0793 0.6450  -0.1448 -0.1343 501  TYR A O   
3835  C CB  . TYR A 501  ? 1.3397 2.1247 1.1190 0.5763  -0.1269 -0.1132 501  TYR A CB  
3836  C CG  . TYR A 501  ? 1.3629 2.2168 1.1676 0.5458  -0.1270 -0.1441 501  TYR A CG  
3837  C CD1 . TYR A 501  ? 1.3653 2.2190 1.1836 0.5121  -0.1277 -0.1461 501  TYR A CD1 
3838  C CD2 . TYR A 501  ? 1.3871 2.3065 1.2049 0.5506  -0.1257 -0.1723 501  TYR A CD2 
3839  C CE1 . TYR A 501  ? 1.3723 2.2891 1.2154 0.4836  -0.1271 -0.1749 501  TYR A CE1 
3840  C CE2 . TYR A 501  ? 1.3952 2.3780 1.2387 0.5223  -0.1241 -0.2017 501  TYR A CE2 
3841  C CZ  . TYR A 501  ? 1.3904 2.3717 1.2459 0.4889  -0.1249 -0.2026 501  TYR A CZ  
3842  O OH  . TYR A 501  ? 1.3907 2.4359 1.2732 0.4609  -0.1227 -0.2326 501  TYR A OH  
3843  N N   . LEU A 502  ? 1.2935 2.0711 1.0639 0.5981  -0.1340 -0.0954 502  LEU A N   
3844  C CA  . LEU A 502  ? 1.2641 2.0491 1.0353 0.5979  -0.1365 -0.0936 502  LEU A CA  
3845  C C   . LEU A 502  ? 1.2680 1.9879 1.0478 0.5582  -0.1312 -0.0762 502  LEU A C   
3846  O O   . LEU A 502  ? 1.2584 1.9050 1.0259 0.5618  -0.1266 -0.0500 502  LEU A O   
3847  C CB  . LEU A 502  ? 1.2374 2.0072 0.9793 0.6482  -0.1388 -0.0773 502  LEU A CB  
3848  C CG  . LEU A 502  ? 1.2063 2.0024 0.9396 0.6644  -0.1431 -0.0807 502  LEU A CG  
3849  C CD1 . LEU A 502  ? 1.1633 2.0492 0.9188 0.6554  -0.1514 -0.1155 502  LEU A CD1 
3850  C CD2 . LEU A 502  ? 1.2252 2.0045 0.9233 0.7174  -0.1455 -0.0647 502  LEU A CD2 
3851  N N   . ILE A 503  ? 1.2384 1.9850 1.0419 0.5205  -0.1323 -0.0917 503  ILE A N   
3852  C CA  . ILE A 503  ? 1.2381 1.9272 1.0549 0.4789  -0.1294 -0.0789 503  ILE A CA  
3853  C C   . ILE A 503  ? 1.2327 1.9280 1.0601 0.4695  -0.1301 -0.0803 503  ILE A C   
3854  O O   . ILE A 503  ? 1.2219 1.9818 1.0647 0.4605  -0.1338 -0.1038 503  ILE A O   
3855  C CB  . ILE A 503  ? 1.2199 1.9210 1.0568 0.4332  -0.1297 -0.0940 503  ILE A CB  
3856  C CG1 . ILE A 503  ? 1.2362 1.9387 1.0625 0.4403  -0.1276 -0.0971 503  ILE A CG1 
3857  C CG2 . ILE A 503  ? 1.2053 1.8379 1.0533 0.3932  -0.1294 -0.0783 503  ILE A CG2 
3858  C CD1 . ILE A 503  ? 1.2067 1.9229 1.0468 0.3965  -0.1259 -0.1134 503  ILE A CD1 
3859  N N   . LEU A 504  ? 1.2727 1.9003 1.0937 0.4712  -0.1258 -0.0560 504  LEU A N   
3860  C CA  . LEU A 504  ? 1.2782 1.8991 1.1090 0.4616  -0.1242 -0.0544 504  LEU A CA  
3861  C C   . LEU A 504  ? 1.3170 1.8944 1.1755 0.4130  -0.1243 -0.0504 504  LEU A C   
3862  O O   . LEU A 504  ? 1.3409 1.8787 1.2041 0.3920  -0.1255 -0.0429 504  LEU A O   
3863  C CB  . LEU A 504  ? 1.2378 1.8095 1.0449 0.4946  -0.1172 -0.0308 504  LEU A CB  
3864  C CG  . LEU A 504  ? 1.2279 1.8221 1.0010 0.5467  -0.1168 -0.0273 504  LEU A CG  
3865  C CD1 . LEU A 504  ? 1.2243 1.8753 0.9926 0.5630  -0.1242 -0.0440 504  LEU A CD1 
3866  C CD2 . LEU A 504  ? 1.1536 1.6712 0.9048 0.5699  -0.1082 0.0028  504  LEU A CD2 
3867  N N   . SER A 505  ? 1.3615 1.9437 1.2375 0.3961  -0.1237 -0.0554 505  SER A N   
3868  C CA  . SER A 505  ? 1.3656 1.9030 1.2704 0.3519  -0.1250 -0.0511 505  SER A CA  
3869  C C   . SER A 505  ? 1.3956 1.9436 1.3187 0.3405  -0.1231 -0.0578 505  SER A C   
3870  O O   . SER A 505  ? 1.3716 1.9869 1.3020 0.3392  -0.1259 -0.0798 505  SER A O   
3871  C CB  . SER A 505  ? 1.3426 1.9017 1.2653 0.3138  -0.1319 -0.0663 505  SER A CB  
3872  O OG  . SER A 505  ? 1.3248 1.8367 1.2736 0.2727  -0.1352 -0.0610 505  SER A OG  
3873  N N   . LYS A 506  ? 1.4369 1.9185 1.3705 0.3309  -0.1184 -0.0404 506  LYS A N   
3874  C CA  . LYS A 506  ? 1.4510 1.9371 1.3986 0.3259  -0.1138 -0.0450 506  LYS A CA  
3875  C C   . LYS A 506  ? 1.5023 2.0324 1.4188 0.3686  -0.1087 -0.0493 506  LYS A C   
3876  O O   . LYS A 506  ? 1.5158 2.1106 1.4356 0.3695  -0.1121 -0.0703 506  LYS A O   
3877  C CB  . LYS A 506  ? 1.4162 1.9447 1.3969 0.2877  -0.1211 -0.0676 506  LYS A CB  
3878  C CG  . LYS A 506  ? 1.3718 1.8462 1.3847 0.2442  -0.1264 -0.0617 506  LYS A CG  
3879  C CD  . LYS A 506  ? 1.3313 1.8519 1.3689 0.2078  -0.1355 -0.0836 506  LYS A CD  
3880  C CE  . LYS A 506  ? 1.3259 1.9063 1.3447 0.2187  -0.1384 -0.0972 506  LYS A CE  
3881  N NZ  . LYS A 506  ? 1.3224 1.8639 1.3290 0.2115  -0.1415 -0.0853 506  LYS A NZ  
3882  N N   . GLY A 507  ? 1.5233 2.0177 1.4085 0.4043  -0.1018 -0.0296 507  GLY A N   
3883  C CA  . GLY A 507  ? 1.5700 2.0874 1.4194 0.4478  -0.0962 -0.0276 507  GLY A CA  
3884  C C   . GLY A 507  ? 1.6131 2.2115 1.4438 0.4727  -0.1051 -0.0472 507  GLY A C   
3885  O O   . GLY A 507  ? 1.6296 2.2495 1.4284 0.5098  -0.1034 -0.0470 507  GLY A O   
3886  N N   . LYS A 508  ? 1.5915 2.2326 1.4412 0.4526  -0.1146 -0.0644 508  LYS A N   
3887  C CA  . LYS A 508  ? 1.5924 2.3172 1.4357 0.4695  -0.1236 -0.0886 508  LYS A CA  
3888  C C   . LYS A 508  ? 1.5210 2.2635 1.3635 0.4719  -0.1286 -0.0931 508  LYS A C   
3889  O O   . LYS A 508  ? 1.4911 2.2097 1.3532 0.4392  -0.1288 -0.0915 508  LYS A O   
3890  C CB  . LYS A 508  ? 1.5890 2.3723 1.4632 0.4396  -0.1291 -0.1157 508  LYS A CB  
3891  C CG  . LYS A 508  ? 1.6218 2.4381 1.4841 0.4593  -0.1290 -0.1252 508  LYS A CG  
3892  C CD  . LYS A 508  ? 1.6006 2.4531 1.4984 0.4234  -0.1318 -0.1469 508  LYS A CD  
3893  C CE  . LYS A 508  ? 1.6214 2.4637 1.5079 0.4340  -0.1260 -0.1445 508  LYS A CE  
3894  N NZ  . LYS A 508  ? 1.5936 2.4516 1.5181 0.3951  -0.1263 -0.1607 508  LYS A NZ  
3895  N N   . ILE A 509  ? 1.4868 2.2706 1.3057 0.5114  -0.1330 -0.0994 509  ILE A N   
3896  C CA  . ILE A 509  ? 1.4221 2.2429 1.2443 0.5153  -0.1380 -0.1120 509  ILE A CA  
3897  C C   . ILE A 509  ? 1.3620 2.2467 1.2177 0.4813  -0.1430 -0.1419 509  ILE A C   
3898  O O   . ILE A 509  ? 1.3624 2.2983 1.2284 0.4804  -0.1473 -0.1606 509  ILE A O   
3899  C CB  . ILE A 509  ? 1.4146 2.2779 1.2101 0.5654  -0.1439 -0.1180 509  ILE A CB  
3900  C CG1 . ILE A 509  ? 1.4271 2.2291 1.1861 0.6008  -0.1384 -0.0888 509  ILE A CG1 
3901  C CG2 . ILE A 509  ? 1.4215 2.3204 1.2226 0.5716  -0.1479 -0.1312 509  ILE A CG2 
3902  C CD1 . ILE A 509  ? 1.4469 2.2830 1.1741 0.6527  -0.1456 -0.0917 509  ILE A CD1 
3903  N N   . ILE A 510  ? 1.3278 2.2097 1.1993 0.4534  -0.1419 -0.1469 510  ILE A N   
3904  C CA  . ILE A 510  ? 1.2951 2.2307 1.1981 0.4168  -0.1443 -0.1740 510  ILE A CA  
3905  C C   . ILE A 510  ? 1.3013 2.2784 1.2086 0.4172  -0.1444 -0.1910 510  ILE A C   
3906  O O   . ILE A 510  ? 1.2642 2.3022 1.1957 0.3969  -0.1455 -0.2184 510  ILE A O   
3907  C CB  . ILE A 510  ? 1.3870 2.2745 1.3116 0.3661  -0.1414 -0.1663 510  ILE A CB  
3908  C CG1 . ILE A 510  ? 1.3893 2.1850 1.2988 0.3632  -0.1374 -0.1346 510  ILE A CG1 
3909  C CG2 . ILE A 510  ? 1.3764 2.2739 1.3178 0.3527  -0.1429 -0.1720 510  ILE A CG2 
3910  C CD1 . ILE A 510  ? 1.3632 2.1074 1.2940 0.3150  -0.1375 -0.1268 510  ILE A CD1 
3911  N N   . HIS A 511  ? 1.3580 2.3018 1.2432 0.4401  -0.1421 -0.1757 511  HIS A N   
3912  C CA  . HIS A 511  ? 1.4197 2.4028 1.3073 0.4458  -0.1411 -0.1921 511  HIS A CA  
3913  C C   . HIS A 511  ? 1.4723 2.4496 1.3334 0.4966  -0.1433 -0.1815 511  HIS A C   
3914  O O   . HIS A 511  ? 1.4954 2.4190 1.3334 0.5195  -0.1430 -0.1557 511  HIS A O   
3915  C CB  . HIS A 511  ? 1.4546 2.3929 1.3459 0.4074  -0.1347 -0.1851 511  HIS A CB  
3916  C CG  . HIS A 511  ? 1.4630 2.3847 1.3749 0.3568  -0.1335 -0.1876 511  HIS A CG  
3917  N ND1 . HIS A 511  ? 1.4584 2.4419 1.3970 0.3297  -0.1333 -0.2157 511  HIS A ND1 
3918  C CD2 . HIS A 511  ? 1.4641 2.3135 1.3758 0.3285  -0.1332 -0.1662 511  HIS A CD2 
3919  C CE1 . HIS A 511  ? 1.4400 2.3890 1.3920 0.2869  -0.1330 -0.2104 511  HIS A CE1 
3920  N NE2 . HIS A 511  ? 1.4430 2.3108 1.3795 0.2856  -0.1337 -0.1808 511  HIS A NE2 
3921  N N   . PHE A 512  ? 1.5150 2.5476 1.3810 0.5137  -0.1449 -0.2023 512  PHE A N   
3922  C CA  . PHE A 512  ? 1.5753 2.6087 1.4196 0.5621  -0.1482 -0.1957 512  PHE A CA  
3923  C C   . PHE A 512  ? 1.5468 2.6467 1.4091 0.5657  -0.1483 -0.2254 512  PHE A C   
3924  O O   . PHE A 512  ? 1.4975 2.6581 1.3879 0.5424  -0.1482 -0.2539 512  PHE A O   
3925  C CB  . PHE A 512  ? 1.6693 2.7230 1.4976 0.6036  -0.1575 -0.1933 512  PHE A CB  
3926  C CG  . PHE A 512  ? 1.7223 2.8638 1.5720 0.6079  -0.1661 -0.2267 512  PHE A CG  
3927  C CD1 . PHE A 512  ? 1.7583 2.9520 1.6008 0.6536  -0.1774 -0.2408 512  PHE A CD1 
3928  C CD2 . PHE A 512  ? 1.7070 2.8789 1.5859 0.5660  -0.1640 -0.2448 512  PHE A CD2 
3929  C CE1 . PHE A 512  ? 1.7651 3.0400 1.6300 0.6575  -0.1869 -0.2732 512  PHE A CE1 
3930  C CE2 . PHE A 512  ? 1.7069 2.9603 1.6087 0.5690  -0.1719 -0.2770 512  PHE A CE2 
3931  C CZ  . PHE A 512  ? 1.7333 3.0389 1.6287 0.6148  -0.1836 -0.2917 512  PHE A CZ  
3932  N N   . GLY A 513  ? 1.5640 2.6528 1.4128 0.5941  -0.1476 -0.2199 513  GLY A N   
3933  C CA  . GLY A 513  ? 1.5764 2.7225 1.4446 0.5943  -0.1453 -0.2482 513  GLY A CA  
3934  C C   . GLY A 513  ? 1.6028 2.7322 1.4558 0.6283  -0.1448 -0.2408 513  GLY A C   
3935  O O   . GLY A 513  ? 1.6040 2.6820 1.4296 0.6596  -0.1482 -0.2138 513  GLY A O   
3936  N N   . THR A 514  ? 1.6111 2.7841 1.4833 0.6216  -0.1395 -0.2659 514  THR A N   
3937  C CA  . THR A 514  ? 1.6482 2.8160 1.5116 0.6546  -0.1393 -0.2645 514  THR A CA  
3938  C C   . THR A 514  ? 1.6205 2.8009 1.4989 0.6271  -0.1261 -0.2827 514  THR A C   
3939  O O   . THR A 514  ? 1.6049 2.8452 1.5116 0.6022  -0.1208 -0.3137 514  THR A O   
3940  C CB  . THR A 514  ? 1.6865 2.9161 1.5561 0.7064  -0.1536 -0.2814 514  THR A CB  
3941  O OG1 . THR A 514  ? 1.7135 2.9006 1.5522 0.7419  -0.1635 -0.2529 514  THR A OG1 
3942  C CG2 . THR A 514  ? 1.7148 2.9677 1.5925 0.7313  -0.1523 -0.2956 514  THR A CG2 
3943  N N   . ARG A 515  ? 1.6433 2.7643 1.5017 0.6301  -0.1198 -0.2632 515  ARG A N   
3944  C CA  . ARG A 515  ? 1.6852 2.8156 1.5522 0.6122  -0.1074 -0.2798 515  ARG A CA  
3945  C C   . ARG A 515  ? 1.6863 2.8370 1.5540 0.6596  -0.1115 -0.2864 515  ARG A C   
3946  O O   . ARG A 515  ? 1.7025 2.8125 1.5485 0.6967  -0.1200 -0.2614 515  ARG A O   
3947  C CB  . ARG A 515  ? 1.7509 2.7977 1.5948 0.5784  -0.0977 -0.2549 515  ARG A CB  
3948  C CG  . ARG A 515  ? 1.7922 2.8045 1.6323 0.5359  -0.0968 -0.2423 515  ARG A CG  
3949  C CD  . ARG A 515  ? 1.8332 2.9167 1.7020 0.5093  -0.0943 -0.2731 515  ARG A CD  
3950  N NE  . ARG A 515  ? 1.8682 2.9181 1.7351 0.4683  -0.0941 -0.2613 515  ARG A NE  
3951  C CZ  . ARG A 515  ? 1.9230 2.9131 1.7760 0.4274  -0.0869 -0.2479 515  ARG A CZ  
3952  N NH1 . ARG A 515  ? 1.9542 2.9118 1.7917 0.4218  -0.0787 -0.2448 515  ARG A NH1 
3953  N NH2 . ARG A 515  ? 1.9285 2.8899 1.7826 0.3924  -0.0889 -0.2380 515  ARG A NH2 
3954  N N   . GLU A 516  ? 1.6634 2.8757 1.5569 0.6584  -0.1050 -0.3201 516  GLU A N   
3955  C CA  . GLU A 516  ? 1.6510 2.8826 1.5488 0.7018  -0.1087 -0.3285 516  GLU A CA  
3956  C C   . GLU A 516  ? 1.6319 2.7870 1.5031 0.6988  -0.1003 -0.3037 516  GLU A C   
3957  O O   . GLU A 516  ? 1.5969 2.7122 1.4582 0.6556  -0.0875 -0.2976 516  GLU A O   
3958  C CB  . GLU A 516  ? 1.6675 2.9852 1.6045 0.6995  -0.1025 -0.3735 516  GLU A CB  
3959  C CG  . GLU A 516  ? 1.7054 3.0435 1.6511 0.7438  -0.1064 -0.3843 516  GLU A CG  
3960  C CD  . GLU A 516  ? 1.7195 3.1525 1.7054 0.7735  -0.1166 -0.4230 516  GLU A CD  
3961  O OE1 . GLU A 516  ? 1.7284 3.1938 1.7347 0.7928  -0.1134 -0.4449 516  GLU A OE1 
3962  O OE2 . GLU A 516  ? 1.7256 3.2004 1.7237 0.7789  -0.1285 -0.4322 516  GLU A OE2 
3963  N N   . LYS A 517  ? 1.6509 2.7825 1.5093 0.7447  -0.1086 -0.2886 517  LYS A N   
3964  C CA  . LYS A 517  ? 1.6805 2.7396 1.5153 0.7461  -0.1018 -0.2653 517  LYS A CA  
3965  C C   . LYS A 517  ? 1.7645 2.8481 1.6140 0.7381  -0.0891 -0.2905 517  LYS A C   
3966  O O   . LYS A 517  ? 1.8013 2.9511 1.6771 0.7636  -0.0915 -0.3191 517  LYS A O   
3967  C CB  . LYS A 517  ? 1.6545 2.6755 1.4699 0.7978  -0.1142 -0.2388 517  LYS A CB  
3968  C CG  . LYS A 517  ? 1.6337 2.5672 1.4229 0.7960  -0.1081 -0.2086 517  LYS A CG  
3969  C CD  . LYS A 517  ? 1.6264 2.5610 1.4193 0.8264  -0.1061 -0.2156 517  LYS A CD  
3970  C CE  . LYS A 517  ? 1.6187 2.4616 1.3845 0.8290  -0.1026 -0.1820 517  LYS A CE  
3971  N NZ  . LYS A 517  ? 1.6349 2.4640 1.3963 0.8808  -0.1094 -0.1726 517  LYS A NZ  
3972  N N   . PHE A 518  ? 1.8049 2.8334 1.6372 0.7034  -0.0760 -0.2802 518  PHE A N   
3973  C CA  . PHE A 518  ? 1.8716 2.9160 1.7126 0.6919  -0.0616 -0.3030 518  PHE A CA  
3974  C C   . PHE A 518  ? 1.9290 2.9693 1.7715 0.7393  -0.0660 -0.3016 518  PHE A C   
3975  O O   . PHE A 518  ? 1.9136 2.8832 1.7311 0.7500  -0.0672 -0.2737 518  PHE A O   
3976  C CB  . PHE A 518  ? 1.9122 2.8928 1.7285 0.6428  -0.0483 -0.2906 518  PHE A CB  
3977  C CG  . PHE A 518  ? 1.9543 2.9571 1.7766 0.5922  -0.0397 -0.3049 518  PHE A CG  
3978  C CD1 . PHE A 518  ? 1.9611 3.0494 1.8167 0.5906  -0.0386 -0.3372 518  PHE A CD1 
3979  C CD2 . PHE A 518  ? 1.9840 2.9224 1.7801 0.5466  -0.0334 -0.2874 518  PHE A CD2 
3980  C CE1 . PHE A 518  ? 1.9651 3.0745 1.8281 0.5438  -0.0298 -0.3511 518  PHE A CE1 
3981  C CE2 . PHE A 518  ? 1.9899 2.9471 1.7909 0.4998  -0.0257 -0.3004 518  PHE A CE2 
3982  C CZ  . PHE A 518  ? 1.9772 3.0202 1.8120 0.4982  -0.0230 -0.3321 518  PHE A CZ  
3983  N N   . SER A 519  ? 1.9974 3.1151 1.8722 0.7665  -0.0686 -0.3338 519  SER A N   
3984  C CA  . SER A 519  ? 2.0735 3.2024 1.9568 0.8190  -0.0774 -0.3362 519  SER A CA  
3985  C C   . SER A 519  ? 2.1325 3.1930 1.9937 0.8221  -0.0701 -0.3173 519  SER A C   
3986  O O   . SER A 519  ? 2.1870 3.2043 2.0329 0.8596  -0.0805 -0.2921 519  SER A O   
3987  C CB  . SER A 519  ? 2.0639 3.2840 1.9902 0.8302  -0.0741 -0.3821 519  SER A CB  
3988  O OG  . SER A 519  ? 2.0338 3.3171 1.9834 0.8106  -0.0749 -0.4052 519  SER A OG  
3989  N N   . ASP A 520  ? 2.1386 3.1883 1.9969 0.7821  -0.0516 -0.3302 520  ASP A N   
3990  C CA  . ASP A 520  ? 2.1923 3.1757 2.0279 0.7793  -0.0439 -0.3143 520  ASP A CA  
3991  C C   . ASP A 520  ? 2.1658 3.0583 1.9653 0.7749  -0.0512 -0.2697 520  ASP A C   
3992  O O   . ASP A 520  ? 2.1776 3.0440 1.9701 0.8144  -0.0649 -0.2460 520  ASP A O   
3993  C CB  . ASP A 520  ? 2.2982 3.2850 2.1320 0.7319  -0.0222 -0.3368 520  ASP A CB  
3994  C CG  . ASP A 520  ? 2.4104 3.4007 2.2369 0.6793  -0.0146 -0.3402 520  ASP A CG  
3995  O OD1 . ASP A 520  ? 2.4392 3.4333 2.2659 0.6797  -0.0263 -0.3268 520  ASP A OD1 
3996  O OD2 . ASP A 520  ? 2.4608 3.4484 2.2802 0.6372  0.0034  -0.3563 520  ASP A OD2 
3997  N N   . ALA A 521  ? 2.1227 2.9674 1.9002 0.7265  -0.0423 -0.2591 521  ALA A N   
3998  C CA  . ALA A 521  ? 2.0481 2.7993 1.7938 0.7179  -0.0468 -0.2207 521  ALA A CA  
3999  C C   . ALA A 521  ? 1.8880 2.6109 1.6264 0.7364  -0.0614 -0.1908 521  ALA A C   
4000  O O   . ALA A 521  ? 1.8511 2.6256 1.6048 0.7502  -0.0688 -0.1986 521  ALA A O   
4001  C CB  . ALA A 521  ? 2.0778 2.7865 1.8022 0.6607  -0.0359 -0.2188 521  ALA A CB  
4002  N N   . SER A 522  ? 1.7783 2.4177 1.4935 0.7360  -0.0649 -0.1578 522  SER A N   
4003  C CA  . SER A 522  ? 1.6826 2.2802 1.3881 0.7501  -0.0757 -0.1267 522  SER A CA  
4004  C C   . SER A 522  ? 1.5914 2.1999 1.2981 0.7159  -0.0778 -0.1253 522  SER A C   
4005  O O   . SER A 522  ? 1.5839 2.2512 1.3051 0.7267  -0.0826 -0.1374 522  SER A O   
4006  C CB  . SER A 522  ? 1.6794 2.1828 1.3638 0.7492  -0.0765 -0.0954 522  SER A CB  
4007  O OG  . SER A 522  ? 1.6722 2.1327 1.3492 0.7659  -0.0848 -0.0655 522  SER A OG  
4008  N N   . TYR A 523  ? 1.5065 2.0568 1.1983 0.6749  -0.0752 -0.1113 523  TYR A N   
4009  C CA  . TYR A 523  ? 1.4056 1.9508 1.0977 0.6422  -0.0782 -0.1051 523  TYR A CA  
4010  C C   . TYR A 523  ? 1.3410 1.9376 1.0423 0.6020  -0.0708 -0.1330 523  TYR A C   
4011  O O   . TYR A 523  ? 1.3235 1.9273 1.0209 0.5818  -0.0611 -0.1501 523  TYR A O   
4012  C CB  . TYR A 523  ? 1.4059 1.8605 1.0796 0.6159  -0.0806 -0.0772 523  TYR A CB  
4013  C CG  . TYR A 523  ? 1.4048 1.8192 1.0631 0.5874  -0.0742 -0.0810 523  TYR A CG  
4014  C CD1 . TYR A 523  ? 1.3945 1.8151 1.0467 0.5388  -0.0687 -0.0956 523  TYR A CD1 
4015  C CD2 . TYR A 523  ? 1.4014 1.7687 1.0489 0.6089  -0.0738 -0.0695 523  TYR A CD2 
4016  C CE1 . TYR A 523  ? 1.3959 1.7762 1.0283 0.5131  -0.0633 -0.0983 523  TYR A CE1 
4017  C CE2 . TYR A 523  ? 1.3931 1.7226 1.0240 0.5837  -0.0688 -0.0733 523  TYR A CE2 
4018  C CZ  . TYR A 523  ? 1.4025 1.7382 1.0241 0.5361  -0.0637 -0.0875 523  TYR A CZ  
4019  O OH  . TYR A 523  ? 1.4394 1.7337 1.0390 0.5111  -0.0589 -0.0908 523  TYR A OH  
4020  N N   . GLN A 524  ? 1.3327 1.9601 1.0447 0.5873  -0.0745 -0.1368 524  GLN A N   
4021  C CA  . GLN A 524  ? 1.3665 2.0205 1.0834 0.5394  -0.0674 -0.1562 524  GLN A CA  
4022  C C   . GLN A 524  ? 1.3922 2.0104 1.1055 0.5073  -0.0734 -0.1395 524  GLN A C   
4023  O O   . GLN A 524  ? 1.4010 1.9638 1.1065 0.5183  -0.0817 -0.1116 524  GLN A O   
4024  C CB  . GLN A 524  ? 1.3601 2.1107 1.1030 0.5468  -0.0631 -0.1907 524  GLN A CB  
4025  C CG  . GLN A 524  ? 1.3454 2.1375 1.1041 0.5732  -0.0735 -0.1902 524  GLN A CG  
4026  C CD  . GLN A 524  ? 1.3675 2.2405 1.1488 0.6086  -0.0742 -0.2175 524  GLN A CD  
4027  O OE1 . GLN A 524  ? 1.3850 2.2597 1.1654 0.6385  -0.0729 -0.2210 524  GLN A OE1 
4028  N NE2 . GLN A 524  ? 1.3626 2.3045 1.1666 0.6059  -0.0772 -0.2389 524  GLN A NE2 
4029  N N   . SER A 525  ? 1.3969 2.0447 1.1171 0.4660  -0.0681 -0.1573 525  SER A N   
4030  C CA  . SER A 525  ? 1.3925 2.0103 1.1122 0.4325  -0.0737 -0.1447 525  SER A CA  
4031  C C   . SER A 525  ? 1.3796 2.0707 1.1245 0.4378  -0.0759 -0.1617 525  SER A C   
4032  O O   . SER A 525  ? 1.3457 2.1118 1.1077 0.4477  -0.0701 -0.1901 525  SER A O   
4033  C CB  . SER A 525  ? 1.4418 2.0311 1.1478 0.3786  -0.0671 -0.1505 525  SER A CB  
4034  O OG  . SER A 525  ? 1.4778 2.0202 1.1602 0.3742  -0.0622 -0.1457 525  SER A OG  
4035  N N   . ILE A 526  ? 1.3872 2.0568 1.1361 0.4329  -0.0845 -0.1453 526  ILE A N   
4036  C CA  . ILE A 526  ? 1.3227 2.0541 1.0939 0.4292  -0.0873 -0.1607 526  ILE A CA  
4037  C C   . ILE A 526  ? 1.2906 1.9953 1.0638 0.3781  -0.0876 -0.1577 526  ILE A C   
4038  O O   . ILE A 526  ? 1.2175 1.8516 0.9800 0.3646  -0.0937 -0.1326 526  ILE A O   
4039  C CB  . ILE A 526  ? 1.2399 1.9727 1.0145 0.4681  -0.0970 -0.1456 526  ILE A CB  
4040  C CG1 . ILE A 526  ? 1.1832 1.9213 0.9495 0.5207  -0.0989 -0.1405 526  ILE A CG1 
4041  C CG2 . ILE A 526  ? 1.2222 2.0282 1.0193 0.4679  -0.0999 -0.1665 526  ILE A CG2 
4042  C CD1 . ILE A 526  ? 1.1822 1.9366 0.9495 0.5609  -0.1074 -0.1316 526  ILE A CD1 
4043  N N   . ASN A 527  ? 1.2912 2.0504 1.0796 0.3489  -0.0813 -0.1837 527  ASN A N   
4044  C CA  . ASN A 527  ? 1.3581 2.0864 1.1464 0.2997  -0.0820 -0.1797 527  ASN A CA  
4045  C C   . ASN A 527  ? 1.3986 2.1629 1.2105 0.2906  -0.0876 -0.1859 527  ASN A C   
4046  O O   . ASN A 527  ? 1.4066 2.2420 1.2397 0.2809  -0.0827 -0.2130 527  ASN A O   
4047  C CB  . ASN A 527  ? 1.3921 2.1318 1.1744 0.2607  -0.0700 -0.1989 527  ASN A CB  
4048  C CG  . ASN A 527  ? 1.4202 2.0957 1.1883 0.2119  -0.0728 -0.1852 527  ASN A CG  
4049  O OD1 . ASN A 527  ? 1.3973 2.0776 1.1801 0.1886  -0.0777 -0.1852 527  ASN A OD1 
4050  N ND2 . ASN A 527  ? 1.4762 2.0889 1.2153 0.1965  -0.0708 -0.1733 527  ASN A ND2 
4051  N N   . ILE A 528  ? 1.4353 2.1491 1.2452 0.2925  -0.0973 -0.1616 528  ILE A N   
4052  C CA  . ILE A 528  ? 1.4488 2.1885 1.2800 0.2830  -0.1028 -0.1655 528  ILE A CA  
4053  C C   . ILE A 528  ? 1.4657 2.1688 1.3005 0.2304  -0.1044 -0.1621 528  ILE A C   
4054  O O   . ILE A 528  ? 1.4741 2.0989 1.2942 0.2130  -0.1094 -0.1393 528  ILE A O   
4055  C CB  . ILE A 528  ? 1.4967 2.2028 1.3257 0.3141  -0.1112 -0.1421 528  ILE A CB  
4056  C CG1 . ILE A 528  ? 1.5193 2.2389 1.3366 0.3664  -0.1107 -0.1380 528  ILE A CG1 
4057  C CG2 . ILE A 528  ? 1.4900 2.2354 1.3410 0.3105  -0.1156 -0.1505 528  ILE A CG2 
4058  C CD1 . ILE A 528  ? 1.5474 2.1975 1.3419 0.3746  -0.1097 -0.1167 528  ILE A CD1 
4059  N N   . PRO A 529  ? 1.4457 2.2046 1.3014 0.2048  -0.1010 -0.1854 529  PRO A N   
4060  C CA  . PRO A 529  ? 1.4625 2.1893 1.3264 0.1593  -0.1052 -0.1807 529  PRO A CA  
4061  C C   . PRO A 529  ? 1.4597 2.1385 1.3292 0.1679  -0.1166 -0.1571 529  PRO A C   
4062  O O   . PRO A 529  ? 1.4770 2.1804 1.3530 0.2056  -0.1190 -0.1547 529  PRO A O   
4063  C CB  . PRO A 529  ? 1.4320 2.2429 1.3240 0.1458  -0.1002 -0.2114 529  PRO A CB  
4064  C CG  . PRO A 529  ? 1.4438 2.3171 1.3360 0.1669  -0.0899 -0.2343 529  PRO A CG  
4065  C CD  . PRO A 529  ? 1.4500 2.3009 1.3239 0.2133  -0.0929 -0.2182 529  PRO A CD  
4066  N N   . VAL A 530  ? 1.4534 2.0629 1.3199 0.1343  -0.1235 -0.1400 530  VAL A N   
4067  C CA  . VAL A 530  ? 1.4236 1.9986 1.3048 0.1356  -0.1327 -0.1240 530  VAL A CA  
4068  C C   . VAL A 530  ? 1.3831 2.0080 1.2926 0.1100  -0.1333 -0.1430 530  VAL A C   
4069  O O   . VAL A 530  ? 1.3757 2.0005 1.2893 0.0691  -0.1326 -0.1526 530  VAL A O   
4070  C CB  . VAL A 530  ? 1.1367 1.6124 1.0073 0.1134  -0.1420 -0.0975 530  VAL A CB  
4071  C CG1 . VAL A 530  ? 1.1250 1.5789 1.0050 0.0626  -0.1477 -0.1013 530  VAL A CG1 
4072  C CG2 . VAL A 530  ? 1.1308 1.5658 1.0113 0.1355  -0.1481 -0.0774 530  VAL A CG2 
4073  N N   . THR A 531  ? 1.3618 2.0307 1.2893 0.1343  -0.1342 -0.1493 531  THR A N   
4074  C CA  . THR A 531  ? 1.3564 2.0748 1.3128 0.1125  -0.1352 -0.1684 531  THR A CA  
4075  C C   . THR A 531  ? 1.3509 2.0278 1.3248 0.0987  -0.1433 -0.1551 531  THR A C   
4076  O O   . THR A 531  ? 1.3442 1.9727 1.3118 0.1197  -0.1466 -0.1340 531  THR A O   
4077  C CB  . THR A 531  ? 1.3583 2.1659 1.3273 0.1443  -0.1316 -0.1912 531  THR A CB  
4078  O OG1 . THR A 531  ? 1.3410 2.1982 1.3391 0.1169  -0.1320 -0.2130 531  THR A OG1 
4079  C CG2 . THR A 531  ? 1.3661 2.1639 1.3308 0.1845  -0.1353 -0.1772 531  THR A CG2 
4080  N N   . GLN A 532  ? 1.3631 2.0634 1.3617 0.0639  -0.1453 -0.1696 532  GLN A N   
4081  C CA  . GLN A 532  ? 1.3801 2.0493 1.4015 0.0461  -0.1528 -0.1620 532  GLN A CA  
4082  C C   . GLN A 532  ? 1.3881 2.0707 1.4149 0.0841  -0.1525 -0.1571 532  GLN A C   
4083  O O   . GLN A 532  ? 1.3933 2.0341 1.4339 0.0777  -0.1571 -0.1449 532  GLN A O   
4084  C CB  . GLN A 532  ? 1.3778 2.0900 1.4267 0.0085  -0.1534 -0.1841 532  GLN A CB  
4085  C CG  . GLN A 532  ? 1.3757 2.0663 1.4535 -0.0101 -0.1609 -0.1806 532  GLN A CG  
4086  C CD  . GLN A 532  ? 1.3760 1.9767 1.4545 -0.0421 -0.1706 -0.1593 532  GLN A CD  
4087  O OE1 . GLN A 532  ? 1.3957 1.9538 1.4528 -0.0590 -0.1726 -0.1500 532  GLN A OE1 
4088  N NE2 . GLN A 532  ? 1.3455 1.9168 1.4494 -0.0506 -0.1774 -0.1527 532  GLN A NE2 
4089  N N   . ASN A 533  ? 1.4078 2.1466 1.4230 0.1236  -0.1472 -0.1670 533  ASN A N   
4090  C CA  . ASN A 533  ? 1.4112 2.1578 1.4233 0.1617  -0.1466 -0.1607 533  ASN A CA  
4091  C C   . ASN A 533  ? 1.4108 2.0835 1.4014 0.1844  -0.1460 -0.1314 533  ASN A C   
4092  O O   . ASN A 533  ? 1.4218 2.0801 1.4099 0.2087  -0.1444 -0.1212 533  ASN A O   
4093  C CB  . ASN A 533  ? 1.4465 2.2736 1.4510 0.1986  -0.1435 -0.1801 533  ASN A CB  
4094  C CG  . ASN A 533  ? 1.4706 2.3746 1.5008 0.1793  -0.1440 -0.2111 533  ASN A CG  
4095  O OD1 . ASN A 533  ? 1.4965 2.4510 1.5274 0.1791  -0.1411 -0.2299 533  ASN A OD1 
4096  N ND2 . ASN A 533  ? 1.4583 2.3717 1.5124 0.1618  -0.1470 -0.2179 533  ASN A ND2 
4097  N N   . MET A 534  ? 1.3797 2.0059 1.3540 0.1766  -0.1464 -0.1187 534  MET A N   
4098  C CA  . MET A 534  ? 1.3508 1.9067 1.3062 0.1975  -0.1459 -0.0920 534  MET A CA  
4099  C C   . MET A 534  ? 1.3213 1.7993 1.2925 0.1683  -0.1519 -0.0745 534  MET A C   
4100  O O   . MET A 534  ? 1.3144 1.7273 1.2770 0.1804  -0.1523 -0.0527 534  MET A O   
4101  C CB  . MET A 534  ? 1.3551 1.8999 1.2864 0.2044  -0.1442 -0.0885 534  MET A CB  
4102  C CG  . MET A 534  ? 1.3513 1.9776 1.2766 0.2194  -0.1394 -0.1121 534  MET A CG  
4103  S SD  . MET A 534  ? 1.3206 1.9400 1.2223 0.2181  -0.1356 -0.1138 534  MET A SD  
4104  C CE  . MET A 534  ? 1.0296 1.6011 0.9062 0.2656  -0.1342 -0.0888 534  MET A CE  
4105  N N   . VAL A 535  ? 1.2854 1.7724 1.2828 0.1309  -0.1570 -0.0856 535  VAL A N   
4106  C CA  . VAL A 535  ? 1.2768 1.6948 1.2911 0.0926  -0.1662 -0.0741 535  VAL A CA  
4107  C C   . VAL A 535  ? 1.2805 1.6180 1.3017 0.0977  -0.1695 -0.0506 535  VAL A C   
4108  O O   . VAL A 535  ? 1.3058 1.5784 1.3296 0.0737  -0.1786 -0.0384 535  VAL A O   
4109  C CB  . VAL A 535  ? 1.2637 1.7091 1.3095 0.0573  -0.1707 -0.0905 535  VAL A CB  
4110  C CG1 . VAL A 535  ? 1.2722 1.7358 1.3152 0.0219  -0.1741 -0.1035 535  VAL A CG1 
4111  C CG2 . VAL A 535  ? 1.3008 1.8181 1.3586 0.0789  -0.1639 -0.1073 535  VAL A CG2 
4112  N N   . PRO A 536  ? 1.2646 1.6037 1.2909 0.1260  -0.1626 -0.0451 536  PRO A N   
4113  C CA  . PRO A 536  ? 1.2407 1.4954 1.2772 0.1235  -0.1657 -0.0235 536  PRO A CA  
4114  C C   . PRO A 536  ? 1.2088 1.4233 1.2170 0.1518  -0.1626 -0.0055 536  PRO A C   
4115  O O   . PRO A 536  ? 1.2214 1.3647 1.2324 0.1416  -0.1692 0.0103  536  PRO A O   
4116  C CB  . PRO A 536  ? 1.2700 1.5324 1.3238 0.1393  -0.1576 -0.0237 536  PRO A CB  
4117  C CG  . PRO A 536  ? 1.2847 1.6288 1.3467 0.1332  -0.1558 -0.0477 536  PRO A CG  
4118  C CD  . PRO A 536  ? 1.2781 1.6751 1.3153 0.1405  -0.1560 -0.0589 536  PRO A CD  
4119  N N   . SER A 537  ? 1.1701 1.4328 1.1523 0.1882  -0.1533 -0.0092 537  SER A N   
4120  C CA  . SER A 537  ? 1.1554 1.3946 1.1090 0.2198  -0.1490 0.0046  537  SER A CA  
4121  C C   . SER A 537  ? 1.1754 1.4909 1.1089 0.2549  -0.1408 -0.0078 537  SER A C   
4122  O O   . SER A 537  ? 1.1864 1.5645 1.1296 0.2491  -0.1404 -0.0267 537  SER A O   
4123  C CB  . SER A 537  ? 1.1204 1.2896 1.0778 0.2379  -0.1447 0.0271  537  SER A CB  
4124  O OG  . SER A 537  ? 1.1087 1.3015 1.0588 0.2727  -0.1327 0.0291  537  SER A OG  
4125  N N   . SER A 538  ? 1.1546 1.4645 1.0615 0.2913  -0.1355 0.0020  538  SER A N   
4126  C CA  . SER A 538  ? 1.0946 1.4705 0.9810 0.3287  -0.1300 -0.0083 538  SER A CA  
4127  C C   . SER A 538  ? 1.1120 1.4508 0.9734 0.3661  -0.1249 0.0104  538  SER A C   
4128  O O   . SER A 538  ? 1.1217 1.3920 0.9838 0.3585  -0.1261 0.0277  538  SER A O   
4129  C CB  . SER A 538  ? 1.0706 1.5094 0.9539 0.3172  -0.1334 -0.0304 538  SER A CB  
4130  O OG  . SER A 538  ? 1.0105 1.4835 0.9174 0.2805  -0.1376 -0.0484 538  SER A OG  
4131  N N   . ARG A 539  ? 1.0745 1.4564 0.9145 0.4068  -0.1204 0.0070  539  ARG A N   
4132  C CA  . ARG A 539  ? 1.0974 1.4559 0.9131 0.4403  -0.1173 0.0203  539  ARG A CA  
4133  C C   . ARG A 539  ? 1.1037 1.5343 0.9054 0.4622  -0.1191 0.0020  539  ARG A C   
4134  O O   . ARG A 539  ? 1.0961 1.5941 0.9023 0.4655  -0.1211 -0.0176 539  ARG A O   
4135  C CB  . ARG A 539  ? 1.1181 1.4400 0.9183 0.4764  -0.1093 0.0401  539  ARG A CB  
4136  C CG  . ARG A 539  ? 1.1116 1.3875 0.9287 0.4606  -0.1048 0.0511  539  ARG A CG  
4137  C CD  . ARG A 539  ? 1.2028 1.4443 0.9993 0.4990  -0.0943 0.0702  539  ARG A CD  
4138  N NE  . ARG A 539  ? 1.2617 1.4215 1.0640 0.4957  -0.0903 0.0918  539  ARG A NE  
4139  C CZ  . ARG A 539  ? 1.2958 1.4015 1.1221 0.4733  -0.0866 0.1011  539  ARG A CZ  
4140  N NH1 . ARG A 539  ? 1.2987 1.4253 1.1431 0.4531  -0.0860 0.0907  539  ARG A NH1 
4141  N NH2 . ARG A 539  ? 1.3447 1.3766 1.1794 0.4714  -0.0837 0.1193  539  ARG A NH2 
4142  N N   . LEU A 540  ? 1.1312 1.5481 0.9183 0.4773  -0.1187 0.0069  540  LEU A N   
4143  C CA  . LEU A 540  ? 1.1644 1.6449 0.9385 0.5068  -0.1196 -0.0086 540  LEU A CA  
4144  C C   . LEU A 540  ? 1.1935 1.6448 0.9438 0.5508  -0.1163 0.0085  540  LEU A C   
4145  O O   . LEU A 540  ? 1.1654 1.5446 0.9103 0.5526  -0.1130 0.0310  540  LEU A O   
4146  C CB  . LEU A 540  ? 1.2012 1.7220 0.9843 0.4809  -0.1220 -0.0302 540  LEU A CB  
4147  C CG  . LEU A 540  ? 1.2582 1.7415 1.0355 0.4650  -0.1212 -0.0260 540  LEU A CG  
4148  C CD1 . LEU A 540  ? 1.3073 1.7466 1.0650 0.5010  -0.1186 -0.0068 540  LEU A CD1 
4149  C CD2 . LEU A 540  ? 1.2580 1.8075 1.0403 0.4523  -0.1206 -0.0538 540  LEU A CD2 
4150  N N   . LEU A 541  ? 1.2062 1.7151 0.9443 0.5866  -0.1182 -0.0032 541  LEU A N   
4151  C CA  . LEU A 541  ? 1.2396 1.7312 0.9544 0.6325  -0.1166 0.0105  541  LEU A CA  
4152  C C   . LEU A 541  ? 1.2984 1.8613 1.0124 0.6514  -0.1216 -0.0130 541  LEU A C   
4153  O O   . LEU A 541  ? 1.2840 1.9164 1.0115 0.6415  -0.1260 -0.0383 541  LEU A O   
4154  C CB  . LEU A 541  ? 1.2249 1.7054 0.9228 0.6623  -0.1144 0.0239  541  LEU A CB  
4155  C CG  . LEU A 541  ? 1.2919 1.7866 0.9622 0.7155  -0.1159 0.0297  541  LEU A CG  
4156  C CD1 . LEU A 541  ? 1.2724 1.7057 0.9220 0.7354  -0.1079 0.0567  541  LEU A CD1 
4157  C CD2 . LEU A 541  ? 1.2871 1.8701 0.9571 0.7311  -0.1252 0.0033  541  LEU A CD2 
4158  N N   . VAL A 542  ? 1.3626 1.9077 1.0642 0.6775  -0.1206 -0.0057 542  VAL A N   
4159  C CA  . VAL A 542  ? 1.4084 2.0122 1.1142 0.6902  -0.1240 -0.0283 542  VAL A CA  
4160  C C   . VAL A 542  ? 1.5064 2.1049 1.1916 0.7426  -0.1262 -0.0181 542  VAL A C   
4161  O O   . VAL A 542  ? 1.5244 2.0557 1.1948 0.7570  -0.1218 0.0075  542  VAL A O   
4162  C CB  . VAL A 542  ? 1.3824 1.9622 1.0967 0.6592  -0.1198 -0.0317 542  VAL A CB  
4163  C CG1 . VAL A 542  ? 1.3889 1.9988 1.1002 0.6850  -0.1200 -0.0440 542  VAL A CG1 
4164  C CG2 . VAL A 542  ? 1.3525 1.9628 1.0870 0.6110  -0.1193 -0.0511 542  VAL A CG2 
4165  N N   . TYR A 543  ? 1.5725 2.2415 1.2584 0.7712  -0.1337 -0.0387 543  TYR A N   
4166  C CA  . TYR A 543  ? 1.6495 2.3195 1.3160 0.8233  -0.1385 -0.0314 543  TYR A CA  
4167  C C   . TYR A 543  ? 1.6719 2.4124 1.3508 0.8435  -0.1455 -0.0594 543  TYR A C   
4168  O O   . TYR A 543  ? 1.6571 2.4684 1.3566 0.8303  -0.1499 -0.0884 543  TYR A O   
4169  C CB  . TYR A 543  ? 1.6903 2.3620 1.3354 0.8532  -0.1437 -0.0211 543  TYR A CB  
4170  C CG  . TYR A 543  ? 1.7040 2.4525 1.3596 0.8507  -0.1527 -0.0470 543  TYR A CG  
4171  C CD1 . TYR A 543  ? 1.7006 2.4544 1.3687 0.8131  -0.1497 -0.0517 543  TYR A CD1 
4172  C CD2 . TYR A 543  ? 1.7215 2.5358 1.3756 0.8874  -0.1654 -0.0672 543  TYR A CD2 
4173  C CE1 . TYR A 543  ? 1.6948 2.5182 1.3735 0.8111  -0.1581 -0.0759 543  TYR A CE1 
4174  C CE2 . TYR A 543  ? 1.7131 2.5975 1.3781 0.8860  -0.1750 -0.0921 543  TYR A CE2 
4175  C CZ  . TYR A 543  ? 1.6870 2.5758 1.3641 0.8474  -0.1707 -0.0962 543  TYR A CZ  
4176  O OH  . TYR A 543  ? 1.6518 2.6089 1.3414 0.8446  -0.1799 -0.1213 543  TYR A OH  
4177  N N   . TYR A 544  ? 1.7058 2.4256 1.3748 0.8751  -0.1459 -0.0513 544  TYR A N   
4178  C CA  . TYR A 544  ? 1.7300 2.5124 1.4079 0.9076  -0.1546 -0.0746 544  TYR A CA  
4179  C C   . TYR A 544  ? 1.7636 2.5400 1.4155 0.9616  -0.1649 -0.0608 544  TYR A C   
4180  O O   . TYR A 544  ? 1.7871 2.4947 1.4124 0.9750  -0.1608 -0.0291 544  TYR A O   
4181  C CB  . TYR A 544  ? 1.7389 2.5068 1.4260 0.9054  -0.1483 -0.0786 544  TYR A CB  
4182  C CG  . TYR A 544  ? 1.7632 2.4485 1.4283 0.9238  -0.1434 -0.0460 544  TYR A CG  
4183  C CD1 . TYR A 544  ? 1.7561 2.3682 1.4070 0.9051  -0.1361 -0.0173 544  TYR A CD1 
4184  C CD2 . TYR A 544  ? 1.7738 2.4549 1.4359 0.9593  -0.1457 -0.0455 544  TYR A CD2 
4185  C CE1 . TYR A 544  ? 1.7768 2.3145 1.4114 0.9208  -0.1309 0.0108  544  TYR A CE1 
4186  C CE2 . TYR A 544  ? 1.7897 2.3951 1.4337 0.9755  -0.1408 -0.0163 544  TYR A CE2 
4187  C CZ  . TYR A 544  ? 1.7958 2.3301 1.4264 0.9559  -0.1331 0.0116  544  TYR A CZ  
4188  O OH  . TYR A 544  ? 1.8200 2.2782 1.4359 0.9702  -0.1273 0.0398  544  TYR A OH  
4189  N N   . ILE A 545  ? 1.7396 2.5865 1.3992 0.9918  -0.1784 -0.0849 545  ILE A N   
4190  C CA  . ILE A 545  ? 1.7583 2.6030 1.3911 1.0451  -0.1912 -0.0741 545  ILE A CA  
4191  C C   . ILE A 545  ? 1.7897 2.6322 1.4240 1.0806  -0.1954 -0.0754 545  ILE A C   
4192  O O   . ILE A 545  ? 1.7577 2.6624 1.4205 1.0842  -0.2009 -0.1057 545  ILE A O   
4193  C CB  . ILE A 545  ? 1.7030 2.6234 1.3404 1.0612  -0.2074 -0.0988 545  ILE A CB  
4194  C CG1 . ILE A 545  ? 1.6402 2.5871 1.2936 1.0161  -0.2026 -0.1114 545  ILE A CG1 
4195  C CG2 . ILE A 545  ? 1.7707 2.6655 1.3669 1.1065  -0.2184 -0.0779 545  ILE A CG2 
4196  C CD1 . ILE A 545  ? 1.5037 2.5277 1.1644 1.0299  -0.2189 -0.1380 545  ILE A CD1 
4197  N N   . VAL A 546  ? 1.8857 2.6560 1.4914 1.1058  -0.1919 -0.0432 546  VAL A N   
4198  C CA  . VAL A 546  ? 1.9766 2.7290 1.5828 1.1364  -0.1933 -0.0391 546  VAL A CA  
4199  C C   . VAL A 546  ? 2.1546 2.9149 1.7386 1.1952  -0.2099 -0.0339 546  VAL A C   
4200  O O   . VAL A 546  ? 2.1964 2.9073 1.7434 1.2180  -0.2112 -0.0059 546  VAL A O   
4201  C CB  . VAL A 546  ? 1.9101 2.5712 1.5021 1.1254  -0.1778 -0.0063 546  VAL A CB  
4202  C CG1 . VAL A 546  ? 1.9325 2.5513 1.5021 1.1744  -0.1822 0.0145  546  VAL A CG1 
4203  C CG2 . VAL A 546  ? 1.8626 2.5223 1.4823 1.0862  -0.1664 -0.0187 546  VAL A CG2 
4204  N N   . THR A 547  ? 2.3053 3.1245 1.9114 1.2200  -0.2223 -0.0607 547  THR A N   
4205  C CA  . THR A 547  ? 2.5102 3.3403 2.0973 1.2770  -0.2414 -0.0583 547  THR A CA  
4206  C C   . THR A 547  ? 2.7277 3.4942 2.2976 1.3088  -0.2388 -0.0330 547  THR A C   
4207  O O   . THR A 547  ? 2.7515 3.5438 2.3422 1.3315  -0.2457 -0.0489 547  THR A O   
4208  C CB  . THR A 547  ? 2.4966 3.4213 2.1185 1.2939  -0.2590 -0.1004 547  THR A CB  
4209  O OG1 . THR A 547  ? 2.4501 3.4341 2.0919 1.2617  -0.2600 -0.1251 547  THR A OG1 
4210  C CG2 . THR A 547  ? 2.5468 3.4845 2.1467 1.3536  -0.2833 -0.0986 547  THR A CG2 
4211  N N   . GLY A 548  ? 2.9187 3.6023 2.4527 1.3105  -0.2281 0.0052  548  GLY A N   
4212  C CA  . GLY A 548  ? 3.1354 3.7575 2.6471 1.3476  -0.2278 0.0314  548  GLY A CA  
4213  C C   . GLY A 548  ? 3.3690 4.0252 2.8655 1.4023  -0.2517 0.0240  548  GLY A C   
4214  O O   . GLY A 548  ? 3.4067 4.1015 2.8897 1.4119  -0.2653 0.0148  548  GLY A O   
4215  N N   . GLU A 549  ? 3.5382 4.1810 3.0373 1.4385  -0.2585 0.0269  549  GLU A N   
4216  C CA  . GLU A 549  ? 3.7086 4.3836 3.1959 1.4925  -0.2840 0.0184  549  GLU A CA  
4217  C C   . GLU A 549  ? 3.7656 4.4014 3.1963 1.5214  -0.2928 0.0458  549  GLU A C   
4218  O O   . GLU A 549  ? 3.7950 4.4753 3.2135 1.5520  -0.3161 0.0323  549  GLU A O   
4219  C CB  . GLU A 549  ? 3.8432 4.4990 3.3417 1.5261  -0.2883 0.0209  549  GLU A CB  
4220  C CG  . GLU A 549  ? 3.9661 4.5228 3.4318 1.5371  -0.2738 0.0630  549  GLU A CG  
4221  C CD  . GLU A 549  ? 3.9994 4.5133 3.4816 1.4891  -0.2470 0.0731  549  GLU A CD  
4222  O OE1 . GLU A 549  ? 3.9771 4.5380 3.4959 1.4494  -0.2404 0.0467  549  GLU A OE1 
4223  O OE2 . GLU A 549  ? 4.0449 4.4766 3.5030 1.4911  -0.2329 0.1071  549  GLU A OE2 
4224  N N   . GLN A 550  ? 3.7587 4.3107 3.1550 1.5109  -0.2740 0.0832  550  GLN A N   
4225  C CA  . GLN A 550  ? 3.7705 4.2732 3.1085 1.5358  -0.2770 0.1127  550  GLN A CA  
4226  C C   . GLN A 550  ? 3.6520 4.1864 2.9760 1.5144  -0.2792 0.1045  550  GLN A C   
4227  O O   . GLN A 550  ? 3.7074 4.2525 2.9947 1.5450  -0.2964 0.1067  550  GLN A O   
4228  C CB  . GLN A 550  ? 3.8370 4.2383 3.1471 1.5303  -0.2533 0.1540  550  GLN A CB  
4229  C CG  . GLN A 550  ? 3.8176 4.1894 3.1441 1.4745  -0.2273 0.1616  550  GLN A CG  
4230  C CD  . GLN A 550  ? 3.7848 4.1694 3.1623 1.4428  -0.2171 0.1459  550  GLN A CD  
4231  O OE1 . GLN A 550  ? 3.7964 4.2084 3.1977 1.4621  -0.2266 0.1304  550  GLN A OE1 
4232  N NE2 . GLN A 550  ? 3.7378 4.1009 3.1312 1.3939  -0.1981 0.1496  550  GLN A NE2 
4233  N N   . THR A 551  ? 3.4712 4.0197 2.8239 1.4621  -0.2627 0.0948  551  THR A N   
4234  C CA  . THR A 551  ? 3.3385 3.9074 2.6801 1.4361  -0.2606 0.0900  551  THR A CA  
4235  C C   . THR A 551  ? 3.1217 3.7286 2.5102 1.3796  -0.2481 0.0680  551  THR A C   
4236  O O   . THR A 551  ? 3.0863 3.6630 2.4990 1.3515  -0.2312 0.0735  551  THR A O   
4237  C CB  . THR A 551  ? 3.3901 3.8744 2.6829 1.4334  -0.2435 0.1287  551  THR A CB  
4238  O OG1 . THR A 551  ? 3.4803 3.9271 2.7224 1.4849  -0.2546 0.1501  551  THR A OG1 
4239  C CG2 . THR A 551  ? 3.3745 3.8801 2.6594 1.4039  -0.2399 0.1222  551  THR A CG2 
4240  N N   . ALA A 552  ? 2.9507 3.6212 2.3505 1.3631  -0.2569 0.0434  552  ALA A N   
4241  C CA  . ALA A 552  ? 2.7417 3.4515 2.1847 1.3100  -0.2465 0.0211  552  ALA A CA  
4242  C C   . ALA A 552  ? 2.5653 3.2083 2.0023 1.2685  -0.2221 0.0460  552  ALA A C   
4243  O O   . ALA A 552  ? 2.5703 3.1742 1.9732 1.2688  -0.2166 0.0666  552  ALA A O   
4244  C CB  . ALA A 552  ? 2.7267 3.5149 2.1805 1.3037  -0.2613 -0.0088 552  ALA A CB  
4245  N N   . GLU A 553  ? 2.4083 3.0378 1.8782 1.2331  -0.2080 0.0431  553  GLU A N   
4246  C CA  . GLU A 553  ? 2.2371 2.8077 1.7103 1.1895  -0.1869 0.0622  553  GLU A CA  
4247  C C   . GLU A 553  ? 2.0868 2.6970 1.5933 1.1371  -0.1817 0.0406  553  GLU A C   
4248  O O   . GLU A 553  ? 2.0314 2.6844 1.5725 1.1165  -0.1825 0.0165  553  GLU A O   
4249  C CB  . GLU A 553  ? 2.1758 2.6829 1.6557 1.1851  -0.1739 0.0809  553  GLU A CB  
4250  C CG  . GLU A 553  ? 2.1645 2.5797 1.6125 1.1935  -0.1601 0.1197  553  GLU A CG  
4251  C CD  . GLU A 553  ? 2.1187 2.4724 1.5831 1.1707  -0.1447 0.1347  553  GLU A CD  
4252  O OE1 . GLU A 553  ? 2.0781 2.4529 1.5752 1.1330  -0.1415 0.1177  553  GLU A OE1 
4253  O OE2 . GLU A 553  ? 2.1307 2.4136 1.5747 1.1902  -0.1359 0.1631  553  GLU A OE2 
4254  N N   . LEU A 554  ? 2.0411 2.6343 1.5363 1.1153  -0.1754 0.0495  554  LEU A N   
4255  C CA  . LEU A 554  ? 1.9561 2.5626 1.4801 1.0622  -0.1670 0.0376  554  LEU A CA  
4256  C C   . LEU A 554  ? 1.9211 2.4502 1.4496 1.0376  -0.1504 0.0612  554  LEU A C   
4257  O O   . LEU A 554  ? 1.9519 2.4118 1.4554 1.0559  -0.1425 0.0906  554  LEU A O   
4258  C CB  . LEU A 554  ? 1.9566 2.5699 1.4683 1.0489  -0.1665 0.0388  554  LEU A CB  
4259  C CG  . LEU A 554  ? 1.9695 2.6668 1.4861 1.0572  -0.1825 0.0097  554  LEU A CG  
4260  C CD1 . LEU A 554  ? 1.9427 2.6498 1.4674 1.0194  -0.1772 0.0042  554  LEU A CD1 
4261  C CD2 . LEU A 554  ? 1.9514 2.7204 1.5044 1.0519  -0.1916 -0.0233 554  LEU A CD2 
4262  N N   . VAL A 555  ? 1.8687 2.4078 1.4288 0.9957  -0.1453 0.0479  555  VAL A N   
4263  C CA  . VAL A 555  ? 1.8343 2.3016 1.4010 0.9698  -0.1321 0.0676  555  VAL A CA  
4264  C C   . VAL A 555  ? 1.7347 2.2164 1.3293 0.9156  -0.1282 0.0533  555  VAL A C   
4265  O O   . VAL A 555  ? 1.6958 2.2446 1.3103 0.9000  -0.1342 0.0249  555  VAL A O   
4266  C CB  . VAL A 555  ? 1.8687 2.3179 1.4390 0.9879  -0.1316 0.0701  555  VAL A CB  
4267  C CG1 . VAL A 555  ? 1.8672 2.2575 1.4514 0.9530  -0.1208 0.0815  555  VAL A CG1 
4268  C CG2 . VAL A 555  ? 1.9118 2.3229 1.4523 1.0375  -0.1327 0.0926  555  VAL A CG2 
4269  N N   . SER A 556  ? 1.6727 2.0912 1.2696 0.8869  -0.1183 0.0723  556  SER A N   
4270  C CA  . SER A 556  ? 1.6262 2.0524 1.2477 0.8358  -0.1161 0.0606  556  SER A CA  
4271  C C   . SER A 556  ? 1.6417 1.9851 1.2673 0.8094  -0.1066 0.0843  556  SER A C   
4272  O O   . SER A 556  ? 1.6997 1.9855 1.3094 0.8295  -0.1000 0.1091  556  SER A O   
4273  C CB  . SER A 556  ? 1.5910 2.0718 1.2175 0.8241  -0.1208 0.0445  556  SER A CB  
4274  O OG  . SER A 556  ? 1.6012 2.0369 1.2161 0.8219  -0.1146 0.0644  556  SER A OG  
4275  N N   . ASP A 557  ? 1.5528 1.8900 1.2001 0.7644  -0.1061 0.0758  557  ASP A N   
4276  C CA  . ASP A 557  ? 1.4701 1.7365 1.1276 0.7324  -0.1005 0.0930  557  ASP A CA  
4277  C C   . ASP A 557  ? 1.3844 1.6813 1.0608 0.6908  -0.1034 0.0777  557  ASP A C   
4278  O O   . ASP A 557  ? 1.3375 1.7063 1.0176 0.6897  -0.1084 0.0554  557  ASP A O   
4279  C CB  . ASP A 557  ? 1.4876 1.7105 1.1508 0.7193  -0.0999 0.0979  557  ASP A CB  
4280  C CG  . ASP A 557  ? 1.4960 1.6567 1.1754 0.6772  -0.0986 0.1083  557  ASP A CG  
4281  O OD1 . ASP A 557  ? 1.5282 1.6308 1.2095 0.6789  -0.0934 0.1288  557  ASP A OD1 
4282  O OD2 . ASP A 557  ? 1.4639 1.6316 1.1541 0.6425  -0.1030 0.0956  557  ASP A OD2 
4283  N N   . SER A 558  ? 1.3819 1.6245 1.0722 0.6573  -0.1008 0.0889  558  SER A N   
4284  C CA  . SER A 558  ? 1.3656 1.6284 1.0748 0.6184  -0.1035 0.0773  558  SER A CA  
4285  C C   . SER A 558  ? 1.3500 1.5446 1.0773 0.5790  -0.1037 0.0887  558  SER A C   
4286  O O   . SER A 558  ? 1.3474 1.4744 1.0727 0.5865  -0.1002 0.1086  558  SER A O   
4287  C CB  . SER A 558  ? 1.3783 1.6591 1.0824 0.6334  -0.1003 0.0796  558  SER A CB  
4288  O OG  . SER A 558  ? 1.4030 1.6155 1.0993 0.6488  -0.0916 0.1051  558  SER A OG  
4289  N N   . VAL A 559  ? 1.3367 1.5482 1.0827 0.5378  -0.1086 0.0755  559  VAL A N   
4290  C CA  . VAL A 559  ? 1.3064 1.4574 1.0700 0.4978  -0.1126 0.0832  559  VAL A CA  
4291  C C   . VAL A 559  ? 1.3171 1.4783 1.1029 0.4624  -0.1158 0.0753  559  VAL A C   
4292  O O   . VAL A 559  ? 1.3492 1.5766 1.1388 0.4540  -0.1176 0.0558  559  VAL A O   
4293  C CB  . VAL A 559  ? 1.2288 1.3791 0.9894 0.4751  -0.1186 0.0739  559  VAL A CB  
4294  C CG1 . VAL A 559  ? 1.1886 1.3323 0.9297 0.5082  -0.1156 0.0791  559  VAL A CG1 
4295  C CG2 . VAL A 559  ? 1.1520 1.3754 0.9167 0.4535  -0.1216 0.0481  559  VAL A CG2 
4296  N N   . TRP A 560  ? 1.2795 1.3761 1.0832 0.4415  -0.1169 0.0891  560  TRP A N   
4297  C CA  . TRP A 560  ? 1.2563 1.3585 1.0841 0.4090  -0.1201 0.0820  560  TRP A CA  
4298  C C   . TRP A 560  ? 1.1971 1.2983 1.0354 0.3659  -0.1310 0.0710  560  TRP A C   
4299  O O   . TRP A 560  ? 1.2144 1.2621 1.0514 0.3526  -0.1368 0.0799  560  TRP A O   
4300  C CB  . TRP A 560  ? 1.3403 1.3736 1.1866 0.4054  -0.1163 0.0999  560  TRP A CB  
4301  C CG  . TRP A 560  ? 1.3996 1.4333 1.2746 0.3705  -0.1204 0.0924  560  TRP A CG  
4302  C CD1 . TRP A 560  ? 1.4361 1.5184 1.3176 0.3704  -0.1162 0.0810  560  TRP A CD1 
4303  C CD2 . TRP A 560  ? 1.4241 1.4071 1.3257 0.3305  -0.1308 0.0947  560  TRP A CD2 
4304  N NE1 . TRP A 560  ? 1.4339 1.5000 1.3465 0.3322  -0.1223 0.0758  560  TRP A NE1 
4305  C CE2 . TRP A 560  ? 1.4200 1.4247 1.3455 0.3074  -0.1320 0.0842  560  TRP A CE2 
4306  C CE3 . TRP A 560  ? 1.4571 1.3776 1.3639 0.3123  -0.1407 0.1039  560  TRP A CE3 
4307  C CZ2 . TRP A 560  ? 1.4145 1.3807 1.3706 0.2674  -0.1428 0.0831  560  TRP A CZ2 
4308  C CZ3 . TRP A 560  ? 1.4607 1.3418 1.3956 0.2729  -0.1526 0.1030  560  TRP A CZ3 
4309  C CH2 . TRP A 560  ? 1.4291 1.3328 1.3892 0.2510  -0.1536 0.0929  560  TRP A CH2 
4310  N N   . LEU A 561  ? 1.1826 1.3400 1.0302 0.3435  -0.1340 0.0518  561  LEU A N   
4311  C CA  . LEU A 561  ? 1.2060 1.3647 1.0595 0.3017  -0.1432 0.0407  561  LEU A CA  
4312  C C   . LEU A 561  ? 1.2493 1.3832 1.1305 0.2611  -0.1511 0.0392  561  LEU A C   
4313  O O   . LEU A 561  ? 1.2806 1.4657 1.1749 0.2478  -0.1507 0.0237  561  LEU A O   
4314  C CB  . LEU A 561  ? 1.1784 1.4214 1.0237 0.3012  -0.1409 0.0170  561  LEU A CB  
4315  C CG  . LEU A 561  ? 1.1807 1.4578 1.0018 0.3373  -0.1350 0.0131  561  LEU A CG  
4316  C CD1 . LEU A 561  ? 1.1450 1.5032 0.9655 0.3299  -0.1334 -0.0131 561  LEU A CD1 
4317  C CD2 . LEU A 561  ? 1.1975 1.4169 1.0036 0.3343  -0.1374 0.0253  561  LEU A CD2 
4318  N N   . ASN A 562  ? 1.2394 1.2967 1.1314 0.2406  -0.1594 0.0535  562  ASN A N   
4319  C CA  . ASN A 562  ? 1.2331 1.2651 1.1542 0.2018  -0.1689 0.0514  562  ASN A CA  
4320  C C   . ASN A 562  ? 1.2614 1.3177 1.1797 0.1639  -0.1774 0.0364  562  ASN A C   
4321  O O   . ASN A 562  ? 1.2837 1.3192 1.1815 0.1528  -0.1825 0.0376  562  ASN A O   
4322  C CB  . ASN A 562  ? 1.1959 1.1374 1.1341 0.1904  -0.1776 0.0697  562  ASN A CB  
4323  C CG  . ASN A 562  ? 1.5396 1.4529 1.5109 0.1491  -0.1901 0.0663  562  ASN A CG  
4324  O OD1 . ASN A 562  ? 1.5088 1.4697 1.4939 0.1320  -0.1897 0.0518  562  ASN A OD1 
4325  N ND2 . ASN A 562  ? 1.5482 1.3830 1.5342 0.1338  -0.2021 0.0792  562  ASN A ND2 
4326  N N   . ILE A 563  ? 1.2363 1.3345 1.1742 0.1430  -0.1783 0.0220  563  ILE A N   
4327  C CA  . ILE A 563  ? 1.2331 1.3548 1.1672 0.1073  -0.1844 0.0077  563  ILE A CA  
4328  C C   . ILE A 563  ? 1.2669 1.3634 1.2309 0.0680  -0.1956 0.0056  563  ILE A C   
4329  O O   . ILE A 563  ? 1.2708 1.3393 1.2615 0.0702  -0.1974 0.0128  563  ILE A O   
4330  C CB  . ILE A 563  ? 1.2011 1.4142 1.1244 0.1194  -0.1738 -0.0133 563  ILE A CB  
4331  C CG1 . ILE A 563  ? 1.1859 1.4498 1.1348 0.0987  -0.1740 -0.0307 563  ILE A CG1 
4332  C CG2 . ILE A 563  ? 1.1768 1.4215 1.0869 0.1686  -0.1627 -0.0107 563  ILE A CG2 
4333  C CD1 . ILE A 563  ? 1.1927 1.5361 1.1339 0.0941  -0.1676 -0.0542 563  ILE A CD1 
4334  N N   . GLU A 564  ? 1.3067 1.4095 1.2657 0.0315  -0.2026 -0.0043 564  GLU A N   
4335  C CA  . GLU A 564  ? 1.3295 1.3968 1.3118 -0.0104 -0.2166 -0.0048 564  GLU A CA  
4336  C C   . GLU A 564  ? 1.3550 1.4603 1.3733 -0.0158 -0.2142 -0.0155 564  GLU A C   
4337  O O   . GLU A 564  ? 1.3623 1.5432 1.3821 -0.0038 -0.2032 -0.0317 564  GLU A O   
4338  C CB  . GLU A 564  ? 1.3533 1.4299 1.3166 -0.0461 -0.2212 -0.0150 564  GLU A CB  
4339  C CG  . GLU A 564  ? 1.3697 1.5380 1.3289 -0.0465 -0.2079 -0.0383 564  GLU A CG  
4340  C CD  . GLU A 564  ? 1.4156 1.5871 1.3710 -0.0926 -0.2132 -0.0493 564  GLU A CD  
4341  O OE1 . GLU A 564  ? 1.4318 1.6605 1.3721 -0.0978 -0.2022 -0.0662 564  GLU A OE1 
4342  O OE2 . GLU A 564  ? 1.4288 1.5429 1.3974 -0.1240 -0.2286 -0.0411 564  GLU A OE2 
4343  N N   . GLU A 565  ? 1.3813 1.4349 1.4303 -0.0342 -0.2254 -0.0080 565  GLU A N   
4344  C CA  . GLU A 565  ? 1.4289 1.5151 1.5143 -0.0446 -0.2241 -0.0195 565  GLU A CA  
4345  C C   . GLU A 565  ? 1.4074 1.5326 1.5005 -0.0814 -0.2287 -0.0372 565  GLU A C   
4346  O O   . GLU A 565  ? 1.3728 1.4780 1.4968 -0.1110 -0.2391 -0.0403 565  GLU A O   
4347  C CB  . GLU A 565  ? 1.5051 1.5241 1.6256 -0.0544 -0.2342 -0.0080 565  GLU A CB  
4348  C CG  . GLU A 565  ? 1.5789 1.5749 1.7023 -0.0170 -0.2243 0.0047  565  GLU A CG  
4349  C CD  . GLU A 565  ? 1.6304 1.5519 1.7899 -0.0291 -0.2346 0.0159  565  GLU A CD  
4350  O OE1 . GLU A 565  ? 1.6375 1.5206 1.8169 -0.0659 -0.2526 0.0149  565  GLU A OE1 
4351  O OE2 . GLU A 565  ? 1.6481 1.5487 1.8162 -0.0016 -0.2246 0.0252  565  GLU A OE2 
4352  N N   . LYS A 566  ? 1.4313 1.6114 1.4983 -0.0800 -0.2206 -0.0493 566  LYS A N   
4353  C CA  . LYS A 566  ? 1.4443 1.6756 1.5213 -0.1097 -0.2201 -0.0691 566  LYS A CA  
4354  C C   . LYS A 566  ? 1.4442 1.7335 1.5535 -0.1000 -0.2134 -0.0836 566  LYS A C   
4355  O O   . LYS A 566  ? 1.4294 1.7576 1.5346 -0.0625 -0.2023 -0.0859 566  LYS A O   
4356  C CB  . LYS A 566  ? 1.4490 1.7351 1.4950 -0.1046 -0.2091 -0.0818 566  LYS A CB  
4357  C CG  . LYS A 566  ? 1.4379 1.7821 1.4960 -0.1341 -0.2059 -0.1043 566  LYS A CG  
4358  C CD  . LYS A 566  ? 1.4734 1.8279 1.4989 -0.1499 -0.2006 -0.1106 566  LYS A CD  
4359  C CE  . LYS A 566  ? 1.4839 1.8996 1.5234 -0.1785 -0.1946 -0.1346 566  LYS A CE  
4360  N NZ  . LYS A 566  ? 1.4684 1.9754 1.5297 -0.1524 -0.1831 -0.1557 566  LYS A NZ  
4361  N N   . CYS A 567  ? 2.1161 1.8372 1.6243 0.2243  0.0194  -0.0340 567  CYS A N   
4362  C CA  . CYS A 567  ? 2.1007 1.8700 1.6382 0.2076  0.0279  -0.0371 567  CYS A CA  
4363  C C   . CYS A 567  ? 2.1026 1.8993 1.6528 0.2046  0.0457  -0.0381 567  CYS A C   
4364  O O   . CYS A 567  ? 2.1211 1.8985 1.6564 0.2154  0.0524  -0.0362 567  CYS A O   
4365  C CB  . CYS A 567  ? 2.1091 1.8712 1.6434 0.2024  0.0352  -0.0468 567  CYS A CB  
4366  S SG  . CYS A 567  ? 2.9218 2.6722 2.4533 0.2010  0.0149  -0.0485 567  CYS A SG  
4367  N N   . GLY A 568  ? 2.0596 1.9034 1.6378 0.1908  0.0528  -0.0423 568  GLY A N   
4368  C CA  . GLY A 568  ? 2.0611 1.9318 1.6534 0.1868  0.0711  -0.0468 568  GLY A CA  
4369  C C   . GLY A 568  ? 2.0635 1.9252 1.6549 0.1822  0.0892  -0.0578 568  GLY A C   
4370  O O   . GLY A 568  ? 2.0777 1.9305 1.6644 0.1851  0.1063  -0.0600 568  GLY A O   
4371  N N   . ASN A 569  ? 2.0782 1.9434 1.6760 0.1747  0.0853  -0.0644 569  ASN A N   
4372  C CA  . ASN A 569  ? 2.0785 1.9283 1.6753 0.1709  0.0994  -0.0744 569  ASN A CA  
4373  C C   . ASN A 569  ? 2.0752 1.8770 1.6449 0.1787  0.0920  -0.0736 569  ASN A C   
4374  O O   . ASN A 569  ? 2.0848 1.8923 1.6592 0.1753  0.0790  -0.0769 569  ASN A O   
4375  C CB  . ASN A 569  ? 2.0618 1.9580 1.6918 0.1564  0.1016  -0.0864 569  ASN A CB  
4376  C CG  . ASN A 569  ? 2.0656 1.9875 1.7175 0.1489  0.1205  -0.0945 569  ASN A CG  
4377  O OD1 . ASN A 569  ? 2.0863 1.9895 1.7282 0.1538  0.1339  -0.0905 569  ASN A OD1 
4378  N ND2 . ASN A 569  ? 2.0373 2.0042 1.7205 0.1373  0.1217  -0.1069 569  ASN A ND2 
4379  N N   . GLN A 570  ? 2.0746 1.8311 1.6152 0.1903  0.1000  -0.0692 570  GLN A N   
4380  C CA  . GLN A 570  ? 2.0810 1.7922 1.5937 0.1998  0.0923  -0.0683 570  GLN A CA  
4381  C C   . GLN A 570  ? 2.1171 1.8309 1.6424 0.1908  0.0980  -0.0782 570  GLN A C   
4382  O O   . GLN A 570  ? 2.1188 1.8226 1.6460 0.1879  0.1159  -0.0810 570  GLN A O   
4383  C CB  . GLN A 570  ? 2.0640 1.7283 1.5410 0.2154  0.1011  -0.0617 570  GLN A CB  
4384  C CG  . GLN A 570  ? 2.5300 2.1741 1.9840 0.2304  0.0866  -0.0544 570  GLN A CG  
4385  C CD  . GLN A 570  ? 2.5100 2.1702 1.9681 0.2338  0.0940  -0.0500 570  GLN A CD  
4386  O OE1 . GLN A 570  ? 2.4717 2.1735 1.9591 0.2222  0.0997  -0.0515 570  GLN A OE1 
4387  N NE2 . GLN A 570  ? 2.5287 2.1574 1.9573 0.2510  0.0932  -0.0455 570  GLN A NE2 
4388  N N   . LEU A 571  ? 2.1679 1.8976 1.7047 0.1858  0.0827  -0.0836 571  LEU A N   
4389  C CA  . LEU A 571  ? 2.1715 1.8973 1.7162 0.1808  0.0843  -0.0940 571  LEU A CA  
4390  C C   . LEU A 571  ? 2.2436 1.9200 1.7563 0.1937  0.0750  -0.0916 571  LEU A C   
4391  O O   . LEU A 571  ? 2.2724 1.9404 1.7722 0.2007  0.0577  -0.0874 571  LEU A O   
4392  C CB  . LEU A 571  ? 2.0475 1.8223 1.6227 0.1696  0.0729  -0.1029 571  LEU A CB  
4393  C CG  . LEU A 571  ? 1.9583 1.7220 1.5316 0.1707  0.0623  -0.1117 571  LEU A CG  
4394  C CD1 . LEU A 571  ? 1.8855 1.6161 1.4527 0.1723  0.0750  -0.1184 571  LEU A CD1 
4395  C CD2 . LEU A 571  ? 1.8568 1.6773 1.4628 0.1594  0.0535  -0.1214 571  LEU A CD2 
4396  N N   . GLN A 572  ? 2.2414 1.8851 1.7423 0.1969  0.0860  -0.0939 572  GLN A N   
4397  C CA  . GLN A 572  ? 2.2957 1.8929 1.7650 0.2105  0.0772  -0.0918 572  GLN A CA  
4398  C C   . GLN A 572  ? 2.2409 1.8262 1.7173 0.2072  0.0811  -0.1008 572  GLN A C   
4399  O O   . GLN A 572  ? 2.2113 1.7888 1.6953 0.2023  0.0990  -0.1015 572  GLN A O   
4400  C CB  . GLN A 572  ? 2.4628 2.0160 1.8947 0.2256  0.0857  -0.0801 572  GLN A CB  
4401  C CG  . GLN A 572  ? 2.6255 2.1322 2.0206 0.2429  0.0737  -0.0775 572  GLN A CG  
4402  C CD  . GLN A 572  ? 2.7317 2.2476 2.1286 0.2455  0.0484  -0.0821 572  GLN A CD  
4403  O OE1 . GLN A 572  ? 2.7478 2.2950 2.1620 0.2393  0.0389  -0.0816 572  GLN A OE1 
4404  N NE2 . GLN A 572  ? 2.7938 2.2821 2.1734 0.2547  0.0373  -0.0860 572  GLN A NE2 
4405  N N   . VAL A 573  ? 2.1943 1.7780 1.6697 0.2103  0.0638  -0.1078 573  VAL A N   
4406  C CA  . VAL A 573  ? 2.1467 1.7193 1.6292 0.2091  0.0635  -0.1180 573  VAL A CA  
4407  C C   . VAL A 573  ? 2.2069 1.7215 1.6513 0.2261  0.0605  -0.1126 573  VAL A C   
4408  O O   . VAL A 573  ? 2.2427 1.7362 1.6592 0.2389  0.0484  -0.1064 573  VAL A O   
4409  C CB  . VAL A 573  ? 2.0008 1.6157 1.5100 0.2016  0.0470  -0.1310 573  VAL A CB  
4410  C CG1 . VAL A 573  ? 1.9322 1.5985 1.4807 0.1854  0.0553  -0.1400 573  VAL A CG1 
4411  C CG2 . VAL A 573  ? 1.9520 1.5809 1.4539 0.2051  0.0300  -0.1250 573  VAL A CG2 
4412  N N   . HIS A 574  ? 2.2115 1.7003 1.6553 0.2265  0.0711  -0.1147 574  HIS A N   
4413  C CA  . HIS A 574  ? 2.2588 1.6933 1.6665 0.2431  0.0692  -0.1084 574  HIS A CA  
4414  C C   . HIS A 574  ? 2.3061 1.7262 1.7250 0.2423  0.0680  -0.1181 574  HIS A C   
4415  O O   . HIS A 574  ? 2.2687 1.7073 1.7198 0.2288  0.0781  -0.1260 574  HIS A O   
4416  C CB  . HIS A 574  ? 2.3172 1.7169 1.6976 0.2503  0.0884  -0.0919 574  HIS A CB  
4417  C CG  . HIS A 574  ? 2.3696 1.7744 1.7317 0.2565  0.0873  -0.0829 574  HIS A CG  
4418  N ND1 . HIS A 574  ? 2.3930 1.7913 1.7338 0.2688  0.0675  -0.0831 574  HIS A ND1 
4419  C CD2 . HIS A 574  ? 2.3854 1.8017 1.7493 0.2524  0.1025  -0.0748 574  HIS A CD2 
4420  C CE1 . HIS A 574  ? 2.4046 1.8083 1.7348 0.2723  0.0700  -0.0756 574  HIS A CE1 
4421  N NE2 . HIS A 574  ? 2.4032 1.8185 1.7463 0.2631  0.0912  -0.0705 574  HIS A NE2 
4422  N N   . LEU A 575  ? 2.4002 1.7872 1.7933 0.2575  0.0547  -0.1185 575  LEU A N   
4423  C CA  . LEU A 575  ? 2.5059 1.8717 1.9049 0.2602  0.0524  -0.1266 575  LEU A CA  
4424  C C   . LEU A 575  ? 2.6725 1.9857 2.0471 0.2682  0.0694  -0.1118 575  LEU A C   
4425  O O   . LEU A 575  ? 2.7543 2.0372 2.0913 0.2809  0.0745  -0.0960 575  LEU A O   
4426  C CB  . LEU A 575  ? 2.4526 1.8116 1.8384 0.2730  0.0287  -0.1354 575  LEU A CB  
4427  C CG  . LEU A 575  ? 2.3398 1.7526 1.7576 0.2634  0.0122  -0.1522 575  LEU A CG  
4428  C CD1 . LEU A 575  ? 2.3184 1.7229 1.7250 0.2761  -0.0100 -0.1615 575  LEU A CD1 
4429  C CD2 . LEU A 575  ? 2.3042 1.7519 1.7652 0.2469  0.0196  -0.1660 575  LEU A CD2 
4430  N N   . SER A 576  ? 2.7511 2.0541 2.1477 0.2612  0.0777  -0.1170 576  SER A N   
4431  C CA  . SER A 576  ? 2.8761 2.1317 2.2566 0.2652  0.0964  -0.1010 576  SER A CA  
4432  C C   . SER A 576  ? 2.9421 2.1453 2.2735 0.2883  0.0903  -0.0878 576  SER A C   
4433  O O   . SER A 576  ? 2.9673 2.1437 2.2645 0.2978  0.1023  -0.0687 576  SER A O   
4434  C CB  . SER A 576  ? 2.9250 2.1786 2.3434 0.2530  0.1033  -0.1109 576  SER A CB  
4435  O OG  . SER A 576  ? 2.9492 2.2273 2.3999 0.2342  0.1224  -0.1104 576  SER A OG  
4436  N N   . PRO A 577  ? 3.0223 2.2124 2.3497 0.2985  0.0717  -0.0986 577  PRO A N   
4437  C CA  . PRO A 577  ? 3.0725 2.2212 2.3510 0.3223  0.0620  -0.0881 577  PRO A CA  
4438  C C   . PRO A 577  ? 3.0562 2.2278 2.3176 0.3292  0.0469  -0.0915 577  PRO A C   
4439  O O   . PRO A 577  ? 3.0512 2.2524 2.3299 0.3270  0.0276  -0.1083 577  PRO A O   
4440  C CB  . PRO A 577  ? 3.1144 2.2497 2.4003 0.3297  0.0450  -0.1019 577  PRO A CB  
4441  C CG  . PRO A 577  ? 3.0910 2.2481 2.4267 0.3102  0.0519  -0.1150 577  PRO A CG  
4442  C CD  . PRO A 577  ? 3.0225 2.2291 2.3859 0.2915  0.0602  -0.1193 577  PRO A CD  
4443  N N   . ASP A 578  ? 3.0159 2.1755 2.2460 0.3373  0.0552  -0.0763 578  ASP A N   
4444  C CA  . ASP A 578  ? 2.9630 2.1441 2.1817 0.3426  0.0405  -0.0804 578  ASP A CA  
4445  C C   . ASP A 578  ? 2.9461 2.1078 2.1375 0.3627  0.0165  -0.0867 578  ASP A C   
4446  O O   . ASP A 578  ? 2.9087 2.0811 2.0879 0.3698  0.0020  -0.0901 578  ASP A O   
4447  C CB  . ASP A 578  ? 3.0029 2.1775 2.1967 0.3472  0.0546  -0.0648 578  ASP A CB  
4448  C CG  . ASP A 578  ? 3.0173 2.2273 2.2192 0.3433  0.0431  -0.0712 578  ASP A CG  
4449  O OD1 . ASP A 578  ? 3.0066 2.2373 2.2215 0.3424  0.0217  -0.0846 578  ASP A OD1 
4450  O OD2 . ASP A 578  ? 3.0320 2.2492 2.2280 0.3413  0.0557  -0.0622 578  ASP A OD2 
4451  N N   . ALA A 579  ? 2.9729 2.1061 2.1565 0.3720  0.0115  -0.0889 579  ALA A N   
4452  C CA  . ALA A 579  ? 2.9862 2.1014 2.1444 0.3923  -0.0117 -0.0960 579  ALA A CA  
4453  C C   . ALA A 579  ? 2.8956 2.0531 2.0785 0.3858  -0.0339 -0.1145 579  ALA A C   
4454  O O   . ALA A 579  ? 2.8717 2.0712 2.0962 0.3658  -0.0329 -0.1245 579  ALA A O   
4455  C CB  . ALA A 579  ? 3.0348 2.1177 2.1880 0.4014  -0.0142 -0.0973 579  ALA A CB  
4456  N N   . ASP A 580  ? 2.8621 2.0096 2.0195 0.4032  -0.0539 -0.1186 580  ASP A N   
4457  C CA  . ASP A 580  ? 2.8120 1.9974 1.9899 0.3978  -0.0747 -0.1328 580  ASP A CA  
4458  C C   . ASP A 580  ? 2.7737 1.9720 1.9702 0.3992  -0.0930 -0.1499 580  ASP A C   
4459  O O   . ASP A 580  ? 2.7577 1.9788 1.9634 0.4006  -0.1133 -0.1612 580  ASP A O   
4460  C CB  . ASP A 580  ? 2.8898 2.0599 2.0343 0.4150  -0.0878 -0.1298 580  ASP A CB  
4461  C CG  . ASP A 580  ? 3.0211 2.1489 2.1250 0.4417  -0.0994 -0.1298 580  ASP A CG  
4462  O OD1 . ASP A 580  ? 3.0638 2.1831 2.1729 0.4457  -0.1054 -0.1369 580  ASP A OD1 
4463  O OD2 . ASP A 580  ? 3.0804 2.1843 2.1471 0.4597  -0.1033 -0.1234 580  ASP A OD2 
4464  N N   . ALA A 581  ? 2.7710 1.9535 1.9735 0.3996  -0.0860 -0.1516 581  ALA A N   
4465  C CA  . ALA A 581  ? 2.7302 1.9275 1.9545 0.4003  -0.1016 -0.1694 581  ALA A CA  
4466  C C   . ALA A 581  ? 2.7093 1.8965 1.9518 0.3930  -0.0873 -0.1702 581  ALA A C   
4467  O O   . ALA A 581  ? 2.7359 1.8825 1.9569 0.3987  -0.0710 -0.1550 581  ALA A O   
4468  C CB  . ALA A 581  ? 2.7851 1.9517 1.9766 0.4251  -0.1210 -0.1733 581  ALA A CB  
4469  N N   . TYR A 582  ? 2.6100 1.8351 1.8932 0.3805  -0.0933 -0.1880 582  TYR A N   
4470  C CA  . TYR A 582  ? 2.5527 1.7736 1.8605 0.3719  -0.0814 -0.1925 582  TYR A CA  
4471  C C   . TYR A 582  ? 2.5021 1.7258 1.8245 0.3801  -0.0981 -0.2117 582  TYR A C   
4472  O O   . TYR A 582  ? 2.4977 1.7458 1.8240 0.3861  -0.1182 -0.2252 582  TYR A O   
4473  C CB  . TYR A 582  ? 2.4806 1.7509 1.8308 0.3469  -0.0695 -0.1983 582  TYR A CB  
4474  C CG  . TYR A 582  ? 2.4551 1.7252 1.7981 0.3367  -0.0502 -0.1807 582  TYR A CG  
4475  C CD1 . TYR A 582  ? 2.4708 1.7132 1.8119 0.3317  -0.0282 -0.1681 582  TYR A CD1 
4476  C CD2 . TYR A 582  ? 2.4171 1.7161 1.7579 0.3316  -0.0542 -0.1770 582  TYR A CD2 
4477  C CE1 . TYR A 582  ? 2.4632 1.7088 1.7989 0.3227  -0.0105 -0.1531 582  TYR A CE1 
4478  C CE2 . TYR A 582  ? 2.4083 1.7082 1.7432 0.3236  -0.0376 -0.1623 582  TYR A CE2 
4479  C CZ  . TYR A 582  ? 2.4329 1.7075 1.7648 0.3195  -0.0157 -0.1508 582  TYR A CZ  
4480  O OH  . TYR A 582  ? 2.4262 1.7050 1.7530 0.3121  0.0006  -0.1372 582  TYR A OH  
4481  N N   . SER A 583  ? 2.4993 1.6987 1.8322 0.3798  -0.0895 -0.2132 583  SER A N   
4482  C CA  . SER A 583  ? 2.4762 1.6755 1.8265 0.3875  -0.1037 -0.2324 583  SER A CA  
4483  C C   . SER A 583  ? 2.4110 1.6740 1.8117 0.3702  -0.1085 -0.2557 583  SER A C   
4484  O O   . SER A 583  ? 2.3284 1.6178 1.7554 0.3511  -0.0937 -0.2554 583  SER A O   
4485  C CB  . SER A 583  ? 2.5758 1.7227 1.9210 0.3928  -0.0920 -0.2239 583  SER A CB  
4486  O OG  . SER A 583  ? 2.5916 1.7405 1.9537 0.3742  -0.0688 -0.2135 583  SER A OG  
4487  N N   . PRO A 584  ? 2.3775 1.6672 1.7915 0.3778  -0.1293 -0.2766 584  PRO A N   
4488  C CA  . PRO A 584  ? 2.3397 1.6952 1.7993 0.3640  -0.1355 -0.2997 584  PRO A CA  
4489  C C   . PRO A 584  ? 2.2844 1.6414 1.7766 0.3551  -0.1258 -0.3112 584  PRO A C   
4490  O O   . PRO A 584  ? 2.2954 1.6609 1.8072 0.3621  -0.1379 -0.3321 584  PRO A O   
4491  C CB  . PRO A 584  ? 2.3369 1.7056 1.7967 0.3796  -0.1596 -0.3180 584  PRO A CB  
4492  C CG  . PRO A 584  ? 2.3988 1.7182 1.8123 0.3990  -0.1671 -0.3029 584  PRO A CG  
4493  C CD  . PRO A 584  ? 2.4485 1.7087 1.8348 0.4013  -0.1483 -0.2800 584  PRO A CD  
4494  N N   . GLY A 585  ? 2.2831 1.6320 1.7826 0.3407  -0.1051 -0.2991 585  GLY A N   
4495  C CA  . GLY A 585  ? 2.2870 1.6420 1.8229 0.3304  -0.0964 -0.3119 585  GLY A CA  
4496  C C   . GLY A 585  ? 2.3153 1.6342 1.8451 0.3207  -0.0731 -0.2913 585  GLY A C   
4497  O O   . GLY A 585  ? 2.3095 1.6323 1.8710 0.3091  -0.0628 -0.2991 585  GLY A O   
4498  N N   . GLN A 586  ? 2.3633 1.6489 1.8534 0.3257  -0.0649 -0.2657 586  GLN A N   
4499  C CA  . GLN A 586  ? 2.4203 1.6702 1.9002 0.3183  -0.0419 -0.2437 586  GLN A CA  
4500  C C   . GLN A 586  ? 2.4102 1.7032 1.9278 0.2953  -0.0272 -0.2490 586  GLN A C   
4501  O O   . GLN A 586  ? 2.3646 1.7127 1.8968 0.2854  -0.0305 -0.2566 586  GLN A O   
4502  C CB  . GLN A 586  ? 2.4360 1.6584 1.8689 0.3268  -0.0363 -0.2181 586  GLN A CB  
4503  C CG  . GLN A 586  ? 2.4874 1.6688 1.9050 0.3227  -0.0125 -0.1940 586  GLN A CG  
4504  C CD  . GLN A 586  ? 2.5490 1.7018 1.9170 0.3350  -0.0083 -0.1704 586  GLN A CD  
4505  O OE1 . GLN A 586  ? 2.5547 1.7155 1.9002 0.3469  -0.0245 -0.1729 586  GLN A OE1 
4506  N NE2 . GLN A 586  ? 2.5913 1.7120 1.9433 0.3324  0.0133  -0.1481 586  GLN A NE2 
4507  N N   . THR A 587  ? 2.4824 1.7498 2.0170 0.2871  -0.0113 -0.2448 587  THR A N   
4508  C CA  . THR A 587  ? 2.5204 1.8178 2.0846 0.2664  0.0061  -0.2447 587  THR A CA  
4509  C C   . THR A 587  ? 2.5571 1.8394 2.0867 0.2657  0.0205  -0.2174 587  THR A C   
4510  O O   . THR A 587  ? 2.5675 1.7972 2.0576 0.2791  0.0246  -0.1968 587  THR A O   
4511  C CB  . THR A 587  ? 2.5845 1.8507 2.1754 0.2590  0.0187  -0.2462 587  THR A CB  
4512  O OG1 . THR A 587  ? 2.6525 1.8486 2.2085 0.2717  0.0255  -0.2228 587  THR A OG1 
4513  C CG2 . THR A 587  ? 2.5917 1.8759 2.2211 0.2599  0.0031  -0.2769 587  THR A CG2 
4514  N N   . VAL A 588  ? 2.5746 1.9035 2.1179 0.2517  0.0276  -0.2175 588  VAL A N   
4515  C CA  . VAL A 588  ? 2.6021 1.9223 2.1146 0.2518  0.0396  -0.1942 588  VAL A CA  
4516  C C   . VAL A 588  ? 2.5646 1.9326 2.1025 0.2334  0.0516  -0.1953 588  VAL A C   
4517  O O   . VAL A 588  ? 2.5538 1.9772 2.1180 0.2251  0.0426  -0.2118 588  VAL A O   
4518  C CB  . VAL A 588  ? 2.6086 1.9296 2.0853 0.2661  0.0237  -0.1890 588  VAL A CB  
4519  C CG1 . VAL A 588  ? 2.5614 1.9371 2.0619 0.2631  0.0042  -0.2109 588  VAL A CG1 
4520  C CG2 . VAL A 588  ? 2.6004 1.9244 2.0546 0.2640  0.0344  -0.1703 588  VAL A CG2 
4521  N N   . SER A 589  ? 2.5500 1.8976 2.0783 0.2282  0.0722  -0.1766 589  SER A N   
4522  C CA  . SER A 589  ? 2.5264 1.9154 2.0793 0.2114  0.0854  -0.1769 589  SER A CA  
4523  C C   . SER A 589  ? 2.4794 1.8928 2.0106 0.2138  0.0819  -0.1675 589  SER A C   
4524  O O   . SER A 589  ? 2.4860 1.8658 1.9764 0.2265  0.0828  -0.1498 589  SER A O   
4525  C CB  . SER A 589  ? 2.6006 1.9578 2.1556 0.2044  0.1097  -0.1613 589  SER A CB  
4526  O OG  . SER A 589  ? 2.6730 1.9814 2.2266 0.2099  0.1120  -0.1589 589  SER A OG  
4527  N N   . LEU A 590  ? 2.4226 1.8945 1.9814 0.2024  0.0774  -0.1794 590  LEU A N   
4528  C CA  . LEU A 590  ? 2.3571 1.8533 1.9012 0.2026  0.0752  -0.1698 590  LEU A CA  
4529  C C   . LEU A 590  ? 2.3223 1.8388 1.8817 0.1899  0.0942  -0.1630 590  LEU A C   
4530  O O   . LEU A 590  ? 2.3388 1.8795 1.9348 0.1766  0.1030  -0.1744 590  LEU A O   
4531  C CB  . LEU A 590  ? 2.2622 1.8106 1.8236 0.1997  0.0563  -0.1841 590  LEU A CB  
4532  C CG  . LEU A 590  ? 2.1445 1.7360 1.7120 0.1922  0.0568  -0.1786 590  LEU A CG  
4533  C CD1 . LEU A 590  ? 2.1308 1.6920 1.6588 0.2035  0.0549  -0.1598 590  LEU A CD1 
4534  C CD2 . LEU A 590  ? 2.0700 1.7190 1.6620 0.1866  0.0406  -0.1928 590  LEU A CD2 
4535  N N   . ASN A 591  ? 2.2820 1.7892 1.8146 0.1949  0.0996  -0.1460 591  ASN A N   
4536  C CA  . ASN A 591  ? 2.2432 1.7682 1.7863 0.1852  0.1174  -0.1383 591  ASN A CA  
4537  C C   . ASN A 591  ? 2.1895 1.7617 1.7401 0.1808  0.1108  -0.1386 591  ASN A C   
4538  O O   . ASN A 591  ? 2.1856 1.7556 1.7139 0.1901  0.0965  -0.1334 591  ASN A O   
4539  C CB  . ASN A 591  ? 2.2857 1.7621 1.7932 0.1946  0.1331  -0.1174 591  ASN A CB  
4540  C CG  . ASN A 591  ? 2.3498 1.7882 1.8608 0.1928  0.1482  -0.1134 591  ASN A CG  
4541  O OD1 . ASN A 591  ? 2.3559 1.8102 1.9010 0.1782  0.1621  -0.1189 591  ASN A OD1 
4542  N ND2 . ASN A 591  ? 2.3992 1.7869 1.8754 0.2079  0.1453  -0.1033 591  ASN A ND2 
4543  N N   . MET A 592  ? 2.1503 1.7643 1.7331 0.1670  0.1206  -0.1443 592  MET A N   
4544  C CA  . MET A 592  ? 2.0930 1.7466 1.6805 0.1637  0.1175  -0.1406 592  MET A CA  
4545  C C   . MET A 592  ? 2.1225 1.7602 1.6951 0.1655  0.1348  -0.1255 592  MET A C   
4546  O O   . MET A 592  ? 2.1450 1.7531 1.7137 0.1648  0.1517  -0.1202 592  MET A O   
4547  C CB  . MET A 592  ? 2.0435 1.7590 1.6744 0.1494  0.1156  -0.1568 592  MET A CB  
4548  C CG  . MET A 592  ? 1.9998 1.7526 1.6404 0.1493  0.0950  -0.1662 592  MET A CG  
4549  S SD  . MET A 592  ? 2.2582 2.0095 1.9145 0.1493  0.0848  -0.1859 592  MET A SD  
4550  C CE  . MET A 592  ? 2.1090 1.8464 1.7896 0.1402  0.1053  -0.1939 592  MET A CE  
4551  N N   . ALA A 593  ? 2.1157 1.7737 1.6809 0.1678  0.1306  -0.1182 593  ALA A N   
4552  C CA  . ALA A 593  ? 2.1622 1.8079 1.7117 0.1719  0.1450  -0.1049 593  ALA A CA  
4553  C C   . ALA A 593  ? 2.1866 1.8744 1.7477 0.1687  0.1409  -0.1032 593  ALA A C   
4554  O O   . ALA A 593  ? 2.1536 1.8595 1.7140 0.1708  0.1230  -0.1038 593  ALA A O   
4555  C CB  . ALA A 593  ? 2.1737 1.7658 1.6768 0.1896  0.1432  -0.0911 593  ALA A CB  
4556  N N   . THR A 594  ? 2.2570 1.9602 1.8300 0.1636  0.1576  -0.1004 594  THR A N   
4557  C CA  . THR A 594  ? 2.2986 2.0390 1.8814 0.1621  0.1551  -0.0978 594  THR A CA  
4558  C C   . THR A 594  ? 2.3546 2.0955 1.9376 0.1623  0.1747  -0.0916 594  THR A C   
4559  O O   . THR A 594  ? 2.3950 2.1294 1.9897 0.1555  0.1929  -0.0938 594  THR A O   
4560  C CB  . THR A 594  ? 2.2782 2.0771 1.9012 0.1485  0.1499  -0.1106 594  THR A CB  
4561  O OG1 . THR A 594  ? 2.2708 2.0737 1.9065 0.1433  0.1416  -0.1224 594  THR A OG1 
4562  C CG2 . THR A 594  ? 2.2534 2.0824 1.8768 0.1512  0.1349  -0.1053 594  THR A CG2 
4563  N N   . GLY A 595  ? 2.4003 2.1509 1.9730 0.1695  0.1706  -0.0841 595  GLY A N   
4564  C CA  . GLY A 595  ? 2.4591 2.2167 2.0329 0.1710  0.1876  -0.0791 595  GLY A CA  
4565  C C   . GLY A 595  ? 2.5225 2.3347 2.1376 0.1570  0.1942  -0.0888 595  GLY A C   
4566  O O   . GLY A 595  ? 2.5143 2.3416 2.1381 0.1560  0.2084  -0.0873 595  GLY A O   
4567  N N   . MET A 596  ? 2.5444 2.3891 2.1853 0.1470  0.1834  -0.0996 596  MET A N   
4568  C CA  . MET A 596  ? 2.5683 2.4688 2.2486 0.1348  0.1872  -0.1108 596  MET A CA  
4569  C C   . MET A 596  ? 2.5523 2.4748 2.2559 0.1250  0.1785  -0.1248 596  MET A C   
4570  O O   . MET A 596  ? 2.5758 2.4871 2.2665 0.1288  0.1628  -0.1236 596  MET A O   
4571  C CB  . MET A 596  ? 2.5590 2.4931 2.2416 0.1392  0.1763  -0.1056 596  MET A CB  
4572  C CG  . MET A 596  ? 2.5720 2.4996 2.2430 0.1473  0.1866  -0.0968 596  MET A CG  
4573  S SD  . MET A 596  ? 2.8716 2.8345 2.5775 0.1362  0.2099  -0.1069 596  MET A SD  
4574  C CE  . MET A 596  ? 2.2121 2.2450 1.9530 0.1290  0.1979  -0.1164 596  MET A CE  
4575  N N   . ASP A 597  ? 2.5081 2.4632 2.2475 0.1127  0.1885  -0.1394 597  ASP A N   
4576  C CA  . ASP A 597  ? 2.4721 2.4550 2.2379 0.1039  0.1802  -0.1563 597  ASP A CA  
4577  C C   . ASP A 597  ? 2.3616 2.3689 2.1212 0.1079  0.1589  -0.1543 597  ASP A C   
4578  O O   . ASP A 597  ? 2.3202 2.3522 2.0766 0.1115  0.1526  -0.1458 597  ASP A O   
4579  C CB  . ASP A 597  ? 2.5293 2.5634 2.3380 0.0919  0.1892  -0.1729 597  ASP A CB  
4580  C CG  . ASP A 597  ? 2.6363 2.6514 2.4553 0.0865  0.2112  -0.1732 597  ASP A CG  
4581  O OD1 . ASP A 597  ? 2.6912 2.6600 2.5005 0.0859  0.2194  -0.1706 597  ASP A OD1 
4582  O OD2 . ASP A 597  ? 2.6534 2.7006 2.4908 0.0830  0.2205  -0.1754 597  ASP A OD2 
4583  N N   . SER A 598  ? 2.3032 2.3044 2.0625 0.1072  0.1480  -0.1616 598  SER A N   
4584  C CA  . SER A 598  ? 2.1984 2.2191 1.9502 0.1110  0.1284  -0.1577 598  SER A CA  
4585  C C   . SER A 598  ? 2.0761 2.1154 1.8427 0.1071  0.1178  -0.1728 598  SER A C   
4586  O O   . SER A 598  ? 2.0760 2.0957 1.8505 0.1043  0.1231  -0.1850 598  SER A O   
4587  C CB  . SER A 598  ? 2.2017 2.1740 1.9144 0.1226  0.1208  -0.1392 598  SER A CB  
4588  O OG  . SER A 598  ? 2.1668 2.1595 1.8756 0.1249  0.1024  -0.1335 598  SER A OG  
4589  N N   . TRP A 599  ? 1.9686 2.0470 1.7396 0.1073  0.1027  -0.1714 599  TRP A N   
4590  C CA  . TRP A 599  ? 1.8970 1.9927 1.6763 0.1062  0.0902  -0.1830 599  TRP A CA  
4591  C C   . TRP A 599  ? 1.8624 1.9113 1.6107 0.1146  0.0794  -0.1716 599  TRP A C   
4592  O O   . TRP A 599  ? 1.8831 1.9118 1.6090 0.1204  0.0744  -0.1536 599  TRP A O   
4593  C CB  . TRP A 599  ? 1.8874 2.0545 1.6888 0.1021  0.0804  -0.1873 599  TRP A CB  
4594  C CG  . TRP A 599  ? 1.9349 2.1505 1.7694 0.0949  0.0893  -0.2045 599  TRP A CG  
4595  C CD1 . TRP A 599  ? 1.9496 2.2074 1.7972 0.0925  0.0930  -0.2010 599  TRP A CD1 
4596  C CD2 . TRP A 599  ? 1.9577 2.1823 1.8173 0.0897  0.0950  -0.2290 599  TRP A CD2 
4597  N NE1 . TRP A 599  ? 1.9450 2.2400 1.8243 0.0862  0.1006  -0.2227 599  TRP A NE1 
4598  C CE2 . TRP A 599  ? 1.9427 2.2175 1.8311 0.0840  0.1018  -0.2404 599  TRP A CE2 
4599  C CE3 . TRP A 599  ? 1.9780 2.1729 1.8401 0.0898  0.0941  -0.2429 599  TRP A CE3 
4600  C CZ2 . TRP A 599  ? 1.9274 2.2231 1.8478 0.0779  0.1073  -0.2660 599  TRP A CZ2 
4601  C CZ3 . TRP A 599  ? 1.9656 2.1796 1.8593 0.0839  0.0996  -0.2672 599  TRP A CZ3 
4602  C CH2 . TRP A 599  ? 1.9400 2.2039 1.8633 0.0776  0.1060  -0.2791 599  TRP A CH2 
4603  N N   . VAL A 600  ? 1.7956 1.8268 1.5440 0.1159  0.0751  -0.1835 600  VAL A N   
4604  C CA  . VAL A 600  ? 1.7346 1.7233 1.4560 0.1243  0.0643  -0.1762 600  VAL A CA  
4605  C C   . VAL A 600  ? 1.6717 1.7042 1.4065 0.1226  0.0485  -0.1837 600  VAL A C   
4606  O O   . VAL A 600  ? 1.6567 1.7486 1.4169 0.1160  0.0473  -0.1911 600  VAL A O   
4607  C CB  . VAL A 600  ? 1.7477 1.6861 1.4605 0.1279  0.0709  -0.1845 600  VAL A CB  
4608  C CG1 . VAL A 600  ? 1.7675 1.6560 1.4477 0.1389  0.0608  -0.1754 600  VAL A CG1 
4609  C CG2 . VAL A 600  ? 1.7530 1.6628 1.4628 0.1263  0.0898  -0.1799 600  VAL A CG2 
4610  N N   . ALA A 601  ? 1.6372 1.6438 1.3550 0.1291  0.0365  -0.1817 601  ALA A N   
4611  C CA  . ALA A 601  ? 1.6025 1.6490 1.3351 0.1278  0.0228  -0.1926 601  ALA A CA  
4612  C C   . ALA A 601  ? 1.6244 1.6302 1.3356 0.1366  0.0111  -0.1913 601  ALA A C   
4613  O O   . ALA A 601  ? 1.6456 1.6485 1.3440 0.1395  -0.0004 -0.1782 601  ALA A O   
4614  C CB  . ALA A 601  ? 1.5541 1.6591 1.2996 0.1226  0.0152  -0.1835 601  ALA A CB  
4615  N N   . LEU A 602  ? 1.6293 1.6044 1.3385 0.1408  0.0133  -0.2052 602  LEU A N   
4616  C CA  . LEU A 602  ? 1.6409 1.5725 1.3282 0.1509  0.0029  -0.2052 602  LEU A CA  
4617  C C   . LEU A 602  ? 1.6521 1.6217 1.3492 0.1516  -0.0142 -0.2118 602  LEU A C   
4618  O O   . LEU A 602  ? 1.6264 1.6589 1.3482 0.1441  -0.0176 -0.2170 602  LEU A O   
4619  C CB  . LEU A 602  ? 1.6337 1.5228 1.3177 0.1557  0.0098  -0.2176 602  LEU A CB  
4620  C CG  . LEU A 602  ? 1.6248 1.4863 1.3074 0.1524  0.0289  -0.2132 602  LEU A CG  
4621  C CD1 . LEU A 602  ? 1.6193 1.4261 1.2929 0.1582  0.0355  -0.2192 602  LEU A CD1 
4622  C CD2 . LEU A 602  ? 1.6085 1.4477 1.2671 0.1545  0.0345  -0.1911 602  LEU A CD2 
4623  N N   . ALA A 603  ? 1.6713 1.6030 1.3482 0.1613  -0.0248 -0.2110 603  ALA A N   
4624  C CA  . ALA A 603  ? 1.5991 1.5589 1.2827 0.1633  -0.0414 -0.2167 603  ALA A CA  
4625  C C   . ALA A 603  ? 1.6102 1.5089 1.2648 0.1764  -0.0494 -0.2148 603  ALA A C   
4626  O O   . ALA A 603  ? 1.6161 1.4621 1.2438 0.1825  -0.0446 -0.2019 603  ALA A O   
4627  C CB  . ALA A 603  ? 1.5586 1.5586 1.2486 0.1567  -0.0486 -0.2014 603  ALA A CB  
4628  N N   . ALA A 604  ? 1.5839 1.4913 1.2439 0.1818  -0.0617 -0.2286 604  ALA A N   
4629  C CA  . ALA A 604  ? 1.6041 1.4573 1.2378 0.1956  -0.0708 -0.2290 604  ALA A CA  
4630  C C   . ALA A 604  ? 1.5865 1.4729 1.2299 0.1974  -0.0886 -0.2353 604  ALA A C   
4631  O O   . ALA A 604  ? 1.5891 1.5061 1.2511 0.1983  -0.0942 -0.2535 604  ALA A O   
4632  C CB  . ALA A 604  ? 1.5978 1.4148 1.2276 0.2031  -0.0651 -0.2430 604  ALA A CB  
4633  N N   . VAL A 605  ? 1.5911 1.4733 1.2238 0.1975  -0.0977 -0.2204 605  VAL A N   
4634  C CA  . VAL A 605  ? 1.5945 1.5103 1.2387 0.1971  -0.1142 -0.2231 605  VAL A CA  
4635  C C   . VAL A 605  ? 1.6490 1.5167 1.2701 0.2122  -0.1268 -0.2281 605  VAL A C   
4636  O O   . VAL A 605  ? 1.6950 1.5026 1.2861 0.2219  -0.1245 -0.2202 605  VAL A O   
4637  C CB  . VAL A 605  ? 1.5628 1.4965 1.2102 0.1885  -0.1183 -0.2033 605  VAL A CB  
4638  C CG1 . VAL A 605  ? 1.5579 1.5159 1.2151 0.1884  -0.1359 -0.2036 605  VAL A CG1 
4639  C CG2 . VAL A 605  ? 1.5383 1.5251 1.2090 0.1742  -0.1073 -0.1971 605  VAL A CG2 
4640  N N   . ASP A 606  ? 1.6715 1.5663 1.3056 0.2155  -0.1402 -0.2414 606  ASP A N   
4641  C CA  . ASP A 606  ? 1.7060 1.5603 1.3191 0.2296  -0.1548 -0.2441 606  ASP A CA  
4642  C C   . ASP A 606  ? 1.6920 1.5347 1.2957 0.2265  -0.1610 -0.2253 606  ASP A C   
4643  O O   . ASP A 606  ? 1.6841 1.5721 1.3095 0.2163  -0.1688 -0.2198 606  ASP A O   
4644  C CB  . ASP A 606  ? 1.7231 1.6168 1.3555 0.2324  -0.1695 -0.2606 606  ASP A CB  
4645  C CG  . ASP A 606  ? 1.7357 1.5972 1.3506 0.2447  -0.1868 -0.2609 606  ASP A CG  
4646  O OD1 . ASP A 606  ? 1.7709 1.5789 1.3576 0.2517  -0.1870 -0.2489 606  ASP A OD1 
4647  O OD2 . ASP A 606  ? 1.7164 1.6070 1.3457 0.2481  -0.2004 -0.2738 606  ASP A OD2 
4648  N N   . SER A 607  ? 1.4312 1.4382 1.3396 0.2959  -0.8422 -0.4035 607  SER A N   
4649  C CA  . SER A 607  ? 1.4205 1.4879 1.3588 0.3033  -0.8049 -0.4012 607  SER A CA  
4650  C C   . SER A 607  ? 1.3938 1.5051 1.3048 0.3293  -0.7976 -0.4593 607  SER A C   
4651  O O   . SER A 607  ? 1.3553 1.5192 1.2962 0.3300  -0.7682 -0.4636 607  SER A O   
4652  C CB  . SER A 607  ? 1.5120 1.5694 1.4427 0.3266  -0.7757 -0.3702 607  SER A CB  
4653  O OG  . SER A 607  ? 1.5776 1.6312 1.4451 0.3748  -0.7723 -0.4105 607  SER A OG  
4654  N N   . ALA A 608  ? 1.4021 1.4928 1.2574 0.3509  -0.8225 -0.5053 608  ALA A N   
4655  C CA  . ALA A 608  ? 1.3756 1.5086 1.2037 0.3792  -0.8132 -0.5646 608  ALA A CA  
4656  C C   . ALA A 608  ? 1.2952 1.4732 1.1532 0.3571  -0.8089 -0.5929 608  ALA A C   
4657  O O   . ALA A 608  ? 1.2702 1.4930 1.1235 0.3739  -0.7888 -0.6366 608  ALA A O   
4658  C CB  . ALA A 608  ? 1.4555 1.5559 1.2125 0.4120  -0.8407 -0.6073 608  ALA A CB  
4659  N N   . VAL A 609  ? 1.2542 1.4202 1.1420 0.3215  -0.8261 -0.5707 609  VAL A N   
4660  C CA  . VAL A 609  ? 1.1802 1.3817 1.0900 0.3039  -0.8197 -0.5941 609  VAL A CA  
4661  C C   . VAL A 609  ? 1.1527 1.4062 1.0969 0.3048  -0.7740 -0.5935 609  VAL A C   
4662  O O   . VAL A 609  ? 1.1438 1.4313 1.0745 0.3217  -0.7554 -0.6417 609  VAL A O   
4663  C CB  . VAL A 609  ? 1.1307 1.3134 1.0716 0.2697  -0.8415 -0.5615 609  VAL A CB  
4664  C CG1 . VAL A 609  ? 1.1900 1.3286 1.0944 0.2711  -0.8866 -0.5770 609  VAL A CG1 
4665  C CG2 . VAL A 609  ? 1.1097 1.2818 1.0923 0.2520  -0.8333 -0.5015 609  VAL A CG2 
4666  N N   . TYR A 610  ? 1.1115 1.3718 1.1005 0.2871  -0.7560 -0.5413 610  TYR A N   
4667  C CA  . TYR A 610  ? 1.0629 1.3674 1.0835 0.2902  -0.7137 -0.5324 610  TYR A CA  
4668  C C   . TYR A 610  ? 1.7929 2.1201 1.7882 0.3275  -0.6938 -0.5674 610  TYR A C   
4669  O O   . TYR A 610  ? 1.7091 2.0719 1.6988 0.3392  -0.6747 -0.6159 610  TYR A O   
4670  C CB  . TYR A 610  ? 1.0254 1.3254 1.0864 0.2745  -0.7046 -0.4684 610  TYR A CB  
4671  C CG  . TYR A 610  ? 1.0587 1.3241 1.1373 0.2466  -0.7346 -0.4313 610  TYR A CG  
4672  C CD1 . TYR A 610  ? 1.0603 1.3397 1.1755 0.2201  -0.7340 -0.4111 610  TYR A CD1 
4673  C CD2 . TYR A 610  ? 1.0593 1.2781 1.1185 0.2483  -0.7619 -0.4170 610  TYR A CD2 
4674  C CE1 . TYR A 610  ? 1.1038 1.3581 1.2407 0.1958  -0.7630 -0.3817 610  TYR A CE1 
4675  C CE2 . TYR A 610  ? 1.1081 1.2973 1.1908 0.2201  -0.7893 -0.3860 610  TYR A CE2 
4676  C CZ  . TYR A 610  ? 1.1142 1.3253 1.2386 0.1939  -0.7907 -0.3703 610  TYR A CZ  
4677  O OH  . TYR A 610  ? 1.0747 1.2661 1.2283 0.1677  -0.8179 -0.3452 610  TYR A OH  
4678  N N   . GLY A 611  ? 1.8935 2.1996 1.8746 0.3470  -0.6969 -0.5430 611  GLY A N   
4679  C CA  . GLY A 611  ? 1.9950 2.3137 1.9421 0.3897  -0.6859 -0.5748 611  GLY A CA  
4680  C C   . GLY A 611  ? 2.0654 2.4439 2.0290 0.4071  -0.6501 -0.6109 611  GLY A C   
4681  O O   . GLY A 611  ? 2.0688 2.4727 2.0657 0.4088  -0.6216 -0.5811 611  GLY A O   
4682  N N   . VAL A 612  ? 2.1516 2.5538 2.0937 0.4196  -0.6512 -0.6767 612  VAL A N   
4683  C CA  . VAL A 612  ? 2.2286 2.6883 2.1819 0.4419  -0.6186 -0.7252 612  VAL A CA  
4684  C C   . VAL A 612  ? 2.3277 2.8202 2.3361 0.4208  -0.5818 -0.6958 612  VAL A C   
4685  O O   . VAL A 612  ? 2.3278 2.8206 2.3612 0.3866  -0.5748 -0.6865 612  VAL A O   
4686  C CB  . VAL A 612  ? 3.2462 3.7296 3.1822 0.4439  -0.6217 -0.8000 612  VAL A CB  
4687  C CG1 . VAL A 612  ? 3.2879 3.7598 3.1657 0.4822  -0.6499 -0.8463 612  VAL A CG1 
4688  C CG2 . VAL A 612  ? 3.2419 3.7040 3.1881 0.4030  -0.6337 -0.7913 612  VAL A CG2 
4689  N N   . GLN A 613  ? 2.4639 2.9829 2.4872 0.4448  -0.5584 -0.6822 613  GLN A N   
4690  C CA  . GLN A 613  ? 2.5623 3.1053 2.6345 0.4276  -0.5274 -0.6408 613  GLN A CA  
4691  C C   . GLN A 613  ? 2.6738 3.1880 2.7692 0.3838  -0.5361 -0.5890 613  GLN A C   
4692  O O   . GLN A 613  ? 2.6438 3.1659 2.7544 0.3585  -0.5261 -0.6023 613  GLN A O   
4693  C CB  . GLN A 613  ? 2.5464 3.1441 2.6454 0.4315  -0.4904 -0.6875 613  GLN A CB  
4694  C CG  . GLN A 613  ? 2.4901 3.1074 2.6364 0.4100  -0.4588 -0.6442 613  GLN A CG  
4695  C CD  . GLN A 613  ? 2.4452 3.1175 2.6178 0.4280  -0.4199 -0.6807 613  GLN A CD  
4696  O OE1 . GLN A 613  ? 2.4426 3.1434 2.6069 0.4667  -0.4156 -0.7113 613  GLN A OE1 
4697  N NE2 . GLN A 613  ? 2.4096 3.0956 2.6129 0.4018  -0.3910 -0.6772 613  GLN A NE2 
4698  N N   . ARG A 614  ? 2.7922 3.2726 2.8892 0.3763  -0.5537 -0.5319 614  ARG A N   
4699  C CA  . ARG A 614  ? 2.8584 3.3203 2.9840 0.3380  -0.5609 -0.4826 614  ARG A CA  
4700  C C   . ARG A 614  ? 2.8856 3.3852 3.0530 0.3297  -0.5258 -0.4575 614  ARG A C   
4701  O O   . ARG A 614  ? 2.9040 3.4113 3.0918 0.3348  -0.5156 -0.4135 614  ARG A O   
4702  C CB  . ARG A 614  ? 2.8897 3.3106 3.0127 0.3319  -0.5848 -0.4317 614  ARG A CB  
4703  C CG  . ARG A 614  ? 2.8675 3.2656 3.0141 0.2935  -0.6039 -0.3954 614  ARG A CG  
4704  C CD  . ARG A 614  ? 2.8971 3.2437 3.0199 0.2895  -0.6399 -0.3841 614  ARG A CD  
4705  N NE  . ARG A 614  ? 2.8996 3.2279 3.0571 0.2600  -0.6511 -0.3308 614  ARG A NE  
4706  C CZ  . ARG A 614  ? 2.9437 3.2315 3.0959 0.2568  -0.6682 -0.3021 614  ARG A CZ  
4707  N NH1 . ARG A 614  ? 2.9824 3.2394 3.0890 0.2846  -0.6756 -0.3191 614  ARG A NH1 
4708  N NH2 . ARG A 614  ? 2.9553 3.2331 3.1469 0.2272  -0.6761 -0.2583 614  ARG A NH2 
4709  N N   . GLY A 615  ? 2.8737 3.3948 3.0514 0.3177  -0.5061 -0.4860 615  GLY A N   
4710  C CA  . GLY A 615  ? 2.8732 3.4288 3.0837 0.3133  -0.4696 -0.4716 615  GLY A CA  
4711  C C   . GLY A 615  ? 2.9186 3.4744 3.1574 0.3043  -0.4685 -0.4047 615  GLY A C   
4712  O O   . GLY A 615  ? 2.9469 3.4757 3.1914 0.2829  -0.4920 -0.3681 615  GLY A O   
4713  N N   . ALA A 616  ? 2.9311 3.5207 3.1899 0.3213  -0.4416 -0.3913 616  ALA A N   
4714  C CA  . ALA A 616  ? 2.9543 3.5502 3.2407 0.3160  -0.4381 -0.3293 616  ALA A CA  
4715  C C   . ALA A 616  ? 2.9537 3.5378 3.2592 0.2823  -0.4458 -0.2930 616  ALA A C   
4716  O O   . ALA A 616  ? 2.9845 3.5473 3.2988 0.2674  -0.4690 -0.2550 616  ALA A O   
4717  C CB  . ALA A 616  ? 2.9349 3.5748 3.2418 0.3369  -0.4040 -0.3253 616  ALA A CB  
4718  N N   . LYS A 617  ? 2.9104 3.5071 3.2206 0.2718  -0.4257 -0.3076 617  LYS A N   
4719  C CA  . LYS A 617  ? 2.8800 3.4691 3.2033 0.2471  -0.4297 -0.2762 617  LYS A CA  
4720  C C   . LYS A 617  ? 2.8354 3.4263 3.1850 0.2381  -0.4451 -0.2195 617  LYS A C   
4721  O O   . LYS A 617  ? 2.8378 3.4569 3.2094 0.2463  -0.4265 -0.1899 617  LYS A O   
4722  C CB  . LYS A 617  ? 2.9137 3.4697 3.2150 0.2311  -0.4532 -0.2995 617  LYS A CB  
4723  C CG  . LYS A 617  ? 2.9259 3.4767 3.2331 0.2131  -0.4520 -0.2785 617  LYS A CG  
4724  C CD  . LYS A 617  ? 2.9135 3.4841 3.2210 0.2185  -0.4102 -0.2855 617  LYS A CD  
4725  C CE  . LYS A 617  ? 2.9263 3.4842 3.2259 0.2071  -0.4067 -0.2722 617  LYS A CE  
4726  N NZ  . LYS A 617  ? 2.9140 3.4835 3.2080 0.2136  -0.3627 -0.2777 617  LYS A NZ  
4727  N N   . LYS A 618  ? 2.7866 3.3487 3.1356 0.2213  -0.4786 -0.2068 618  LYS A N   
4728  C CA  . LYS A 618  ? 2.7348 3.2934 3.1107 0.2098  -0.4956 -0.1594 618  LYS A CA  
4729  C C   . LYS A 618  ? 2.6094 3.1303 2.9797 0.1912  -0.5338 -0.1618 618  LYS A C   
4730  O O   . LYS A 618  ? 2.5742 3.0779 2.9234 0.1858  -0.5472 -0.1931 618  LYS A O   
4731  C CB  . LYS A 618  ? 2.7964 3.3849 3.2055 0.1985  -0.4833 -0.1194 618  LYS A CB  
4732  C CG  . LYS A 618  ? 2.8366 3.4635 3.2574 0.2156  -0.4482 -0.1058 618  LYS A CG  
4733  C CD  . LYS A 618  ? 2.8834 3.5215 3.3186 0.2294  -0.4420 -0.0792 618  LYS A CD  
4734  C CE  . LYS A 618  ? 2.8700 3.5511 3.3220 0.2454  -0.4101 -0.0600 618  LYS A CE  
4735  N NZ  . LYS A 618  ? 2.8442 3.5395 3.2775 0.2625  -0.3847 -0.0997 618  LYS A NZ  
4736  N N   . PRO A 619  ? 2.5433 3.0501 2.9327 0.1816  -0.5502 -0.1296 619  PRO A N   
4737  C CA  . PRO A 619  ? 2.5003 2.9728 2.8926 0.1611  -0.5861 -0.1280 619  PRO A CA  
4738  C C   . PRO A 619  ? 2.4255 2.9131 2.8553 0.1363  -0.5990 -0.1034 619  PRO A C   
4739  O O   . PRO A 619  ? 2.4153 2.8946 2.8356 0.1289  -0.6171 -0.1245 619  PRO A O   
4740  C CB  . PRO A 619  ? 2.5561 3.0047 2.9518 0.1637  -0.5903 -0.1048 619  PRO A CB  
4741  C CG  . PRO A 619  ? 2.5576 3.0286 2.9444 0.1917  -0.5576 -0.0998 619  PRO A CG  
4742  C CD  . PRO A 619  ? 2.5277 3.0438 2.9301 0.1938  -0.5341 -0.0993 619  PRO A CD  
4743  N N   . LEU A 620  ? 2.3647 2.8760 2.8352 0.1263  -0.5898 -0.0618 620  LEU A N   
4744  C CA  . LEU A 620  ? 2.2953 2.8313 2.8066 0.1056  -0.6002 -0.0387 620  LEU A CA  
4745  C C   . LEU A 620  ? 2.2619 2.8355 2.7724 0.1141  -0.5806 -0.0386 620  LEU A C   
4746  O O   . LEU A 620  ? 2.2701 2.8626 2.8015 0.1037  -0.5916 -0.0302 620  LEU A O   
4747  C CB  . LEU A 620  ? 2.2444 2.7938 2.8012 0.0911  -0.5958 0.0037  620  LEU A CB  
4748  C CG  . LEU A 620  ? 2.1938 2.7854 2.7991 0.0742  -0.5973 0.0303  620  LEU A CG  
4749  C CD1 . LEU A 620  ? 2.2054 2.7865 2.8317 0.0523  -0.6328 0.0187  620  LEU A CD1 
4750  C CD2 . LEU A 620  ? 2.1862 2.7981 2.8312 0.0661  -0.5802 0.0716  620  LEU A CD2 
4751  N N   . GLU A 621  ? 2.2385 2.8227 2.7244 0.1349  -0.5509 -0.0489 621  GLU A N   
4752  C CA  . GLU A 621  ? 2.2188 2.8280 2.6938 0.1455  -0.5278 -0.0539 621  GLU A CA  
4753  C C   . GLU A 621  ? 2.1598 2.7445 2.5994 0.1476  -0.5368 -0.0920 621  GLU A C   
4754  O O   . GLU A 621  ? 2.1533 2.7482 2.5825 0.1522  -0.5256 -0.0946 621  GLU A O   
4755  C CB  . GLU A 621  ? 2.2718 2.9001 2.7373 0.1660  -0.4919 -0.0538 621  GLU A CB  
4756  C CG  . GLU A 621  ? 2.3211 2.9663 2.7679 0.1790  -0.4620 -0.0662 621  GLU A CG  
4757  C CD  . GLU A 621  ? 2.3461 3.0110 2.7885 0.1993  -0.4288 -0.0706 621  GLU A CD  
4758  O OE1 . GLU A 621  ? 2.3567 3.0448 2.8237 0.2043  -0.4224 -0.0401 621  GLU A OE1 
4759  O OE2 . GLU A 621  ? 2.3433 3.0018 2.7593 0.2107  -0.4084 -0.1061 621  GLU A OE2 
4760  N N   . ARG A 622  ? 2.1111 2.6617 2.5293 0.1462  -0.5565 -0.1208 622  ARG A N   
4761  C CA  . ARG A 622  ? 2.0386 2.5648 2.4251 0.1469  -0.5694 -0.1558 622  ARG A CA  
4762  C C   . ARG A 622  ? 1.9642 2.4984 2.3654 0.1380  -0.5870 -0.1417 622  ARG A C   
4763  O O   . ARG A 622  ? 1.9613 2.4971 2.3408 0.1469  -0.5741 -0.1522 622  ARG A O   
4764  C CB  . ARG A 622  ? 2.0685 2.5592 2.4375 0.1436  -0.5982 -0.1817 622  ARG A CB  
4765  C CG  . ARG A 622  ? 2.0736 2.5401 2.4025 0.1494  -0.6054 -0.2252 622  ARG A CG  
4766  C CD  . ARG A 622  ? 1.8875 2.3206 2.1970 0.1481  -0.6363 -0.2505 622  ARG A CD  
4767  N NE  . ARG A 622  ? 1.9246 2.3418 2.2560 0.1318  -0.6753 -0.2333 622  ARG A NE  
4768  C CZ  . ARG A 622  ? 1.9441 2.3285 2.2616 0.1284  -0.7065 -0.2492 622  ARG A CZ  
4769  N NH1 . ARG A 622  ? 1.9503 2.3166 2.2291 0.1423  -0.7049 -0.2833 622  ARG A NH1 
4770  N NH2 . ARG A 622  ? 1.9531 2.3239 2.2958 0.1116  -0.7394 -0.2333 622  ARG A NH2 
4771  N N   . VAL A 623  ? 1.8914 2.4314 2.3295 0.1220  -0.6144 -0.1189 623  VAL A N   
4772  C CA  . VAL A 623  ? 1.8421 2.3981 2.3002 0.1158  -0.6334 -0.1085 623  VAL A CA  
4773  C C   . VAL A 623  ? 1.7660 2.3615 2.2370 0.1236  -0.6082 -0.0832 623  VAL A C   
4774  O O   . VAL A 623  ? 1.7607 2.3616 2.2122 0.1353  -0.6043 -0.0899 623  VAL A O   
4775  C CB  . VAL A 623  ? 1.3093 1.8635 1.8099 0.0943  -0.6703 -0.0967 623  VAL A CB  
4776  C CG1 . VAL A 623  ? 1.2936 1.8907 1.8403 0.0860  -0.6720 -0.0677 623  VAL A CG1 
4777  C CG2 . VAL A 623  ? 1.2978 1.8221 1.7822 0.0917  -0.7070 -0.1270 623  VAL A CG2 
4778  N N   . PHE A 624  ? 1.7016 2.3228 2.2005 0.1202  -0.5901 -0.0542 624  PHE A N   
4779  C CA  . PHE A 624  ? 1.6302 2.2907 2.1403 0.1286  -0.5680 -0.0299 624  PHE A CA  
4780  C C   . PHE A 624  ? 1.6759 2.3302 2.1400 0.1498  -0.5396 -0.0455 624  PHE A C   
4781  O O   . PHE A 624  ? 1.6851 2.3586 2.1431 0.1600  -0.5322 -0.0359 624  PHE A O   
4782  C CB  . PHE A 624  ? 1.4921 2.1788 2.0309 0.1263  -0.5476 0.0009  624  PHE A CB  
4783  C CG  . PHE A 624  ? 1.3625 2.0824 1.9544 0.1098  -0.5619 0.0318  624  PHE A CG  
4784  C CD1 . PHE A 624  ? 1.3174 2.0377 1.9424 0.0958  -0.5632 0.0525  624  PHE A CD1 
4785  C CD2 . PHE A 624  ? 1.3003 2.0507 1.9079 0.1097  -0.5728 0.0380  624  PHE A CD2 
4786  C CE1 . PHE A 624  ? 1.2907 2.0416 1.9683 0.0775  -0.5729 0.0792  624  PHE A CE1 
4787  C CE2 . PHE A 624  ? 1.2684 2.0549 1.9297 0.0932  -0.5856 0.0613  624  PHE A CE2 
4788  C CZ  . PHE A 624  ? 1.2715 2.0584 1.9703 0.0748  -0.5847 0.0821  624  PHE A CZ  
4789  N N   . GLN A 625  ? 1.7219 2.3490 2.1527 0.1573  -0.5219 -0.0710 625  GLN A N   
4790  C CA  . GLN A 625  ? 1.7868 2.4037 2.1761 0.1744  -0.4891 -0.0882 625  GLN A CA  
4791  C C   . GLN A 625  ? 1.7870 2.3879 2.1503 0.1809  -0.5012 -0.0998 625  GLN A C   
4792  O O   . GLN A 625  ? 1.7964 2.4094 2.1467 0.1938  -0.4866 -0.0872 625  GLN A O   
4793  C CB  . GLN A 625  ? 1.8892 2.4799 2.2516 0.1785  -0.4724 -0.1225 625  GLN A CB  
4794  C CG  . GLN A 625  ? 1.9798 2.5893 2.3567 0.1831  -0.4492 -0.1163 625  GLN A CG  
4795  C CD  . GLN A 625  ? 2.0730 2.6651 2.4214 0.1921  -0.4255 -0.1569 625  GLN A CD  
4796  O OE1 . GLN A 625  ? 2.1081 2.6945 2.4324 0.2006  -0.3942 -0.1733 625  GLN A OE1 
4797  N NE2 . GLN A 625  ? 2.1051 2.6885 2.4556 0.1913  -0.4389 -0.1751 625  GLN A NE2 
4798  N N   . PHE A 626  ? 1.7608 2.3341 2.1140 0.1748  -0.5291 -0.1239 626  PHE A N   
4799  C CA  . PHE A 626  ? 1.7548 2.3118 2.0841 0.1830  -0.5467 -0.1372 626  PHE A CA  
4800  C C   . PHE A 626  ? 1.6381 2.2275 1.9921 0.1865  -0.5640 -0.1119 626  PHE A C   
4801  O O   . PHE A 626  ? 1.6046 2.1981 1.9318 0.2059  -0.5474 -0.1071 626  PHE A O   
4802  C CB  . PHE A 626  ? 1.8385 2.3689 2.1666 0.1729  -0.5826 -0.1622 626  PHE A CB  
4803  C CG  . PHE A 626  ? 1.9396 2.4602 2.2555 0.1806  -0.6121 -0.1729 626  PHE A CG  
4804  C CD1 . PHE A 626  ? 1.9930 2.4801 2.2600 0.1949  -0.6058 -0.2012 626  PHE A CD1 
4805  C CD2 . PHE A 626  ? 1.9726 2.5196 2.3277 0.1746  -0.6456 -0.1569 626  PHE A CD2 
4806  C CE1 . PHE A 626  ? 2.0354 2.5142 2.2887 0.2069  -0.6338 -0.2111 626  PHE A CE1 
4807  C CE2 . PHE A 626  ? 2.0146 2.5573 2.3604 0.1857  -0.6748 -0.1702 626  PHE A CE2 
4808  C CZ  . PHE A 626  ? 2.0440 2.5518 2.3368 0.2037  -0.6696 -0.1964 626  PHE A CZ  
4809  N N   . LEU A 627  ? 1.5651 2.1776 1.9697 0.1685  -0.5951 -0.0971 627  LEU A N   
4810  C CA  . LEU A 627  ? 1.5020 2.1489 1.9388 0.1684  -0.6195 -0.0822 627  LEU A CA  
4811  C C   . LEU A 627  ? 1.4814 2.1647 1.9188 0.1829  -0.5955 -0.0578 627  LEU A C   
4812  O O   . LEU A 627  ? 1.5239 2.2442 1.9909 0.1842  -0.6139 -0.0463 627  LEU A O   
4813  C CB  . LEU A 627  ? 1.4267 2.0892 1.9229 0.1413  -0.6505 -0.0719 627  LEU A CB  
4814  C CG  . LEU A 627  ? 1.3595 2.0714 1.9126 0.1303  -0.6641 -0.0479 627  LEU A CG  
4815  C CD1 . LEU A 627  ? 1.3540 2.0638 1.9553 0.1043  -0.7008 -0.0525 627  LEU A CD1 
4816  C CD2 . LEU A 627  ? 1.3235 2.0611 1.8955 0.1258  -0.6335 -0.0173 627  LEU A CD2 
4817  N N   . GLU A 628  ? 1.4514 2.1261 1.8566 0.1948  -0.5548 -0.0526 628  GLU A N   
4818  C CA  . GLU A 628  ? 1.4369 2.1413 1.8347 0.2115  -0.5304 -0.0304 628  GLU A CA  
4819  C C   . GLU A 628  ? 1.4374 2.1078 1.7705 0.2352  -0.4933 -0.0430 628  GLU A C   
4820  O O   . GLU A 628  ? 1.4372 2.1136 1.7557 0.2444  -0.4578 -0.0300 628  GLU A O   
4821  C CB  . GLU A 628  ? 1.4609 2.2003 1.8985 0.1996  -0.5153 -0.0016 628  GLU A CB  
4822  C CG  . GLU A 628  ? 1.8281 2.5493 2.2476 0.2008  -0.4793 -0.0039 628  GLU A CG  
4823  C CD  . GLU A 628  ? 1.8464 2.6068 2.2882 0.2040  -0.4563 0.0270  628  GLU A CD  
4824  O OE1 . GLU A 628  ? 1.8748 2.6591 2.3061 0.2196  -0.4459 0.0426  628  GLU A OE1 
4825  O OE2 . GLU A 628  ? 1.8258 2.5928 2.2918 0.1943  -0.4490 0.0351  628  GLU A OE2 
4826  N N   . LYS A 629  ? 1.4252 2.0569 1.7194 0.2448  -0.5001 -0.0694 629  LYS A N   
4827  C CA  . LYS A 629  ? 1.4203 2.0174 1.6495 0.2708  -0.4661 -0.0799 629  LYS A CA  
4828  C C   . LYS A 629  ? 1.4049 2.0131 1.6139 0.2964  -0.4833 -0.0752 629  LYS A C   
4829  O O   . LYS A 629  ? 1.3778 1.9544 1.5267 0.3245  -0.4617 -0.0828 629  LYS A O   
4830  C CB  . LYS A 629  ? 1.4387 1.9852 1.6330 0.2681  -0.4555 -0.1121 629  LYS A CB  
4831  C CG  . LYS A 629  ? 1.4125 1.9566 1.6315 0.2452  -0.4456 -0.1214 629  LYS A CG  
4832  C CD  . LYS A 629  ? 1.7010 2.2759 1.9438 0.2419  -0.4185 -0.0977 629  LYS A CD  
4833  C CE  . LYS A 629  ? 1.4936 2.0656 1.7535 0.2269  -0.4049 -0.1116 629  LYS A CE  
4834  N NZ  . LYS A 629  ? 1.4573 2.0646 1.7464 0.2256  -0.3860 -0.0873 629  LYS A NZ  
4835  N N   . SER A 630  ? 1.3846 2.0387 1.6454 0.2874  -0.5216 -0.0638 630  SER A N   
4836  C CA  . SER A 630  ? 1.3986 2.0813 1.6537 0.3117  -0.5394 -0.0585 630  SER A CA  
4837  C C   . SER A 630  ? 1.4215 2.1361 1.6742 0.3234  -0.5133 -0.0318 630  SER A C   
4838  O O   . SER A 630  ? 1.4902 2.2384 1.7404 0.3450  -0.5246 -0.0244 630  SER A O   
4839  C CB  . SER A 630  ? 1.3450 2.0692 1.6659 0.2931  -0.5893 -0.0610 630  SER A CB  
4840  O OG  . SER A 630  ? 1.2794 2.0332 1.6609 0.2608  -0.5917 -0.0425 630  SER A OG  
4841  N N   . ASP A 631  ? 1.3934 2.1015 1.6490 0.3105  -0.4802 -0.0190 631  ASP A N   
4842  C CA  . ASP A 631  ? 1.4085 2.1371 1.6493 0.3256  -0.4491 0.0046  631  ASP A CA  
4843  C C   . ASP A 631  ? 1.4532 2.1339 1.6118 0.3602  -0.4158 -0.0047 631  ASP A C   
4844  O O   . ASP A 631  ? 1.4453 2.0757 1.5665 0.3594  -0.3827 -0.0179 631  ASP A O   
4845  C CB  . ASP A 631  ? 1.4519 2.1862 1.7189 0.3047  -0.4233 0.0179  631  ASP A CB  
4846  C CG  . ASP A 631  ? 1.6114 2.3788 1.8759 0.3182  -0.3985 0.0455  631  ASP A CG  
4847  O OD1 . ASP A 631  ? 1.6723 2.4091 1.8801 0.3406  -0.3612 0.0445  631  ASP A OD1 
4848  O OD2 . ASP A 631  ? 1.6401 2.4616 1.9584 0.3061  -0.4144 0.0677  631  ASP A OD2 
4849  N N   . LEU A 632  ? 1.4815 2.1781 1.6119 0.3916  -0.4244 0.0004  632  LEU A N   
4850  C CA  . LEU A 632  ? 1.5235 2.1719 1.5686 0.4310  -0.3950 -0.0066 632  LEU A CA  
4851  C C   . LEU A 632  ? 1.5125 2.1338 1.5183 0.4382  -0.3412 0.0068  632  LEU A C   
4852  O O   . LEU A 632  ? 1.5470 2.1056 1.4922 0.4507  -0.3029 -0.0053 632  LEU A O   
4853  C CB  . LEU A 632  ? 1.5697 2.2513 1.5969 0.4667  -0.4188 -0.0030 632  LEU A CB  
4854  C CG  . LEU A 632  ? 1.5414 2.2782 1.6341 0.4545  -0.4762 -0.0121 632  LEU A CG  
4855  C CD1 . LEU A 632  ? 1.5318 2.3245 1.6249 0.4859  -0.4979 -0.0067 632  LEU A CD1 
4856  C CD2 . LEU A 632  ? 1.5566 2.2568 1.6373 0.4550  -0.4985 -0.0401 632  LEU A CD2 
4857  N N   . GLY A 633  ? 1.4108 2.0799 1.4541 0.4293  -0.3380 0.0306  633  GLY A N   
4858  C CA  . GLY A 633  ? 1.3651 2.0193 1.3796 0.4369  -0.2916 0.0450  633  GLY A CA  
4859  C C   . GLY A 633  ? 1.2891 1.8926 1.2895 0.4201  -0.2516 0.0302  633  GLY A C   
4860  O O   . GLY A 633  ? 1.2968 1.8563 1.2796 0.4131  -0.2479 0.0058  633  GLY A O   
4861  N N   . CYS A 634  ? 1.2810 1.8940 1.2904 0.4148  -0.2215 0.0429  634  CYS A N   
4862  C CA  . CYS A 634  ? 1.2913 1.8633 1.2909 0.4010  -0.1811 0.0251  634  CYS A CA  
4863  C C   . CYS A 634  ? 1.3056 1.8990 1.3167 0.4019  -0.1512 0.0420  634  CYS A C   
4864  O O   . CYS A 634  ? 1.3712 1.9916 1.3701 0.4220  -0.1503 0.0674  634  CYS A O   
4865  C CB  . CYS A 634  ? 1.3439 1.8405 1.2665 0.4201  -0.1445 0.0048  634  CYS A CB  
4866  S SG  . CYS A 634  ? 1.8025 2.2485 1.7199 0.3981  -0.0973 -0.0283 634  CYS A SG  
4867  N N   . GLY A 635  ? 1.2608 1.8448 1.2951 0.3824  -0.1279 0.0256  635  GLY A N   
4868  C CA  . GLY A 635  ? 1.2289 1.8314 1.2749 0.3846  -0.0982 0.0362  635  GLY A CA  
4869  C C   . GLY A 635  ? 1.2018 1.8757 1.3140 0.3746  -0.1249 0.0610  635  GLY A C   
4870  O O   . GLY A 635  ? 1.1693 1.8801 1.3239 0.3622  -0.1673 0.0713  635  GLY A O   
4871  N N   . ALA A 636  ? 1.2173 1.9088 1.3385 0.3802  -0.0983 0.0698  636  ALA A N   
4872  C CA  . ALA A 636  ? 1.1875 1.9445 1.3663 0.3751  -0.1175 0.0948  636  ALA A CA  
4873  C C   . ALA A 636  ? 1.1774 1.9717 1.3488 0.3928  -0.1341 0.1299  636  ALA A C   
4874  O O   . ALA A 636  ? 1.1616 2.0145 1.3810 0.3880  -0.1593 0.1551  636  ALA A O   
4875  C CB  . ALA A 636  ? 1.2228 1.9849 1.4114 0.3784  -0.0831 0.0878  636  ALA A CB  
4876  N N   . GLY A 637  ? 1.1943 1.9523 1.3019 0.4152  -0.1177 0.1298  637  GLY A N   
4877  C CA  . GLY A 637  ? 1.2334 2.0218 1.3216 0.4377  -0.1339 0.1566  637  GLY A CA  
4878  C C   . GLY A 637  ? 1.3510 2.0940 1.3607 0.4693  -0.0948 0.1578  637  GLY A C   
4879  O O   . GLY A 637  ? 1.3381 2.0225 1.3120 0.4697  -0.0536 0.1371  637  GLY A O   
4880  N N   . GLY A 638  ? 1.4130 2.1822 1.3953 0.4959  -0.1071 0.1801  638  GLY A N   
4881  C CA  . GLY A 638  ? 1.4799 2.2179 1.3897 0.5302  -0.0727 0.1893  638  GLY A CA  
4882  C C   . GLY A 638  ? 1.5089 2.1577 1.3369 0.5473  -0.0361 0.1683  638  GLY A C   
4883  O O   . GLY A 638  ? 1.5590 2.1584 1.3858 0.5286  -0.0104 0.1437  638  GLY A O   
4884  N N   . GLY A 639  ? 1.5000 2.1283 1.2569 0.5852  -0.0326 0.1774  639  GLY A N   
4885  C CA  . GLY A 639  ? 1.5180 2.0563 1.1848 0.6091  0.0056  0.1621  639  GLY A CA  
4886  C C   . GLY A 639  ? 1.5716 2.0500 1.1739 0.6278  0.0641  0.1647  639  GLY A C   
4887  O O   . GLY A 639  ? 1.5060 1.9821 1.1418 0.6053  0.0903  0.1589  639  GLY A O   
4888  N N   . LEU A 640  ? 1.6801 2.1106 1.1883 0.6717  0.0840  0.1723  640  LEU A N   
4889  C CA  . LEU A 640  ? 1.7408 2.0850 1.1662 0.6927  0.1472  0.1697  640  LEU A CA  
4890  C C   . LEU A 640  ? 1.7873 2.1078 1.1158 0.7492  0.1520  0.1880  640  LEU A C   
4891  O O   . LEU A 640  ? 1.8222 2.0960 1.0844 0.7748  0.1940  0.1978  640  LEU A O   
4892  C CB  . LEU A 640  ? 1.7473 2.0083 1.1462 0.6772  0.1829  0.1405  640  LEU A CB  
4893  C CG  . LEU A 640  ? 1.4411 1.5960 0.7620 0.6871  0.2551  0.1274  640  LEU A CG  
4894  C CD1 . LEU A 640  ? 1.4627 1.6043 0.7466 0.7070  0.2903  0.1450  640  LEU A CD1 
4895  C CD2 . LEU A 640  ? 1.4096 1.5413 0.7836 0.6407  0.2770  0.0950  640  LEU A CD2 
4896  N N   . ASN A 641  ? 1.7801 2.1349 1.1026 0.7691  0.1070  0.1899  641  ASN A N   
4897  C CA  . ASN A 641  ? 1.8107 2.1787 1.0644 0.8230  0.0905  0.2049  641  ASN A CA  
4898  C C   . ASN A 641  ? 1.7726 2.2489 1.1135 0.8080  0.0224  0.2084  641  ASN A C   
4899  O O   . ASN A 641  ? 1.7373 2.2444 1.1610 0.7644  -0.0019 0.1967  641  ASN A O   
4900  C CB  . ASN A 641  ? 1.9036 2.1959 1.0634 0.8624  0.1042  0.1920  641  ASN A CB  
4901  C CG  . ASN A 641  ? 1.9888 2.1682 1.0931 0.8548  0.1679  0.1770  641  ASN A CG  
4902  O OD1 . ASN A 641  ? 2.0316 2.1560 1.0947 0.8576  0.2203  0.1828  641  ASN A OD1 
4903  N ND2 . ASN A 641  ? 2.0151 2.1583 1.1170 0.8458  0.1649  0.1563  641  ASN A ND2 
4904  N N   . ASN A 642  ? 1.8102 2.3437 1.1329 0.8438  -0.0082 0.2221  642  ASN A N   
4905  C CA  . ASN A 642  ? 1.7694 2.4034 1.1726 0.8311  -0.0713 0.2210  642  ASN A CA  
4906  C C   . ASN A 642  ? 1.7462 2.3577 1.1541 0.8259  -0.0915 0.1968  642  ASN A C   
4907  O O   . ASN A 642  ? 1.6478 2.3234 1.1406 0.7961  -0.1375 0.1885  642  ASN A O   
4908  C CB  . ASN A 642  ? 1.8600 2.5508 1.2267 0.8791  -0.0968 0.2324  642  ASN A CB  
4909  C CG  . ASN A 642  ? 1.8683 2.6630 1.3182 0.8668  -0.1596 0.2262  642  ASN A CG  
4910  O OD1 . ASN A 642  ? 1.9273 2.7528 1.3423 0.9083  -0.1865 0.2177  642  ASN A OD1 
4911  N ND2 . ASN A 642  ? 1.8126 2.6604 1.3725 0.8108  -0.1820 0.2282  642  ASN A ND2 
4912  N N   . ALA A 643  ? 1.8324 2.3483 1.1456 0.8562  -0.0547 0.1857  643  ALA A N   
4913  C CA  . ALA A 643  ? 1.8521 2.3341 1.1648 0.8500  -0.0657 0.1627  643  ALA A CA  
4914  C C   . ALA A 643  ? 1.7256 2.2097 1.1258 0.7863  -0.0647 0.1540  643  ALA A C   
4915  O O   . ALA A 643  ? 1.6222 2.1780 1.1157 0.7520  -0.1106 0.1501  643  ALA A O   
4916  C CB  . ALA A 643  ? 1.9990 2.3700 1.1906 0.8930  -0.0170 0.1552  643  ALA A CB  
4917  N N   . ASN A 644  ? 1.7189 2.1246 1.0877 0.7720  -0.0107 0.1495  644  ASN A N   
4918  C CA  . ASN A 644  ? 1.6647 2.0664 1.1068 0.7163  -0.0037 0.1366  644  ASN A CA  
4919  C C   . ASN A 644  ? 1.6143 2.1162 1.1698 0.6779  -0.0541 0.1438  644  ASN A C   
4920  O O   . ASN A 644  ? 1.6233 2.1503 1.2368 0.6506  -0.0884 0.1301  644  ASN A O   
4921  C CB  . ASN A 644  ? 1.6447 1.9883 1.0624 0.7044  0.0575  0.1375  644  ASN A CB  
4922  C CG  . ASN A 644  ? 1.6163 1.9165 1.0663 0.6629  0.0818  0.1119  644  ASN A CG  
4923  O OD1 . ASN A 644  ? 1.6079 1.8615 1.0466 0.6489  0.1319  0.1044  644  ASN A OD1 
4924  N ND2 . ASN A 644  ? 1.6044 1.9213 1.0950 0.6438  0.0462  0.0958  644  ASN A ND2 
4925  N N   . VAL A 645  ? 1.5896 2.1462 1.1730 0.6779  -0.0580 0.1659  645  VAL A N   
4926  C CA  . VAL A 645  ? 1.5203 2.1727 1.2058 0.6462  -0.1022 0.1774  645  VAL A CA  
4927  C C   . VAL A 645  ? 1.5066 2.2088 1.2400 0.6378  -0.1571 0.1680  645  VAL A C   
4928  O O   . VAL A 645  ? 1.4500 2.1835 1.2625 0.5972  -0.1820 0.1617  645  VAL A O   
4929  C CB  . VAL A 645  ? 1.5418 2.2545 1.2291 0.6669  -0.1096 0.2040  645  VAL A CB  
4930  C CG1 . VAL A 645  ? 1.4869 2.2954 1.2788 0.6342  -0.1533 0.2158  645  VAL A CG1 
4931  C CG2 . VAL A 645  ? 1.5503 2.2243 1.1996 0.6744  -0.0601 0.2146  645  VAL A CG2 
4932  N N   . PHE A 646  ? 1.5346 2.2445 1.2190 0.6785  -0.1754 0.1659  646  PHE A N   
4933  C CA  . PHE A 646  ? 1.4883 2.2416 1.2115 0.6763  -0.2256 0.1516  646  PHE A CA  
4934  C C   . PHE A 646  ? 1.5207 2.2189 1.2420 0.6593  -0.2257 0.1273  646  PHE A C   
4935  O O   . PHE A 646  ? 1.4819 2.2179 1.2701 0.6328  -0.2661 0.1157  646  PHE A O   
4936  C CB  . PHE A 646  ? 1.5032 2.2709 1.1625 0.7319  -0.2405 0.1493  646  PHE A CB  
4937  C CG  . PHE A 646  ? 1.4186 2.2869 1.1315 0.7352  -0.2789 0.1606  646  PHE A CG  
4938  C CD1 . PHE A 646  ? 1.3978 2.2866 1.0675 0.7685  -0.2651 0.1787  646  PHE A CD1 
4939  C CD2 . PHE A 646  ? 1.3371 2.2794 1.1451 0.7037  -0.3277 0.1520  646  PHE A CD2 
4940  C CE1 . PHE A 646  ? 1.3499 2.3358 1.0717 0.7706  -0.3000 0.1873  646  PHE A CE1 
4941  C CE2 . PHE A 646  ? 1.2844 2.3212 1.1471 0.7035  -0.3600 0.1604  646  PHE A CE2 
4942  C CZ  . PHE A 646  ? 1.2920 2.3529 1.1127 0.7368  -0.3466 0.1776  646  PHE A CZ  
4943  N N   . HIS A 647  ? 1.5663 2.1743 1.2104 0.6746  -0.1792 0.1192  647  HIS A N   
4944  C CA  . HIS A 647  ? 1.6053 2.1547 1.2376 0.6619  -0.1731 0.0954  647  HIS A CA  
4945  C C   . HIS A 647  ? 1.4283 1.9987 1.1501 0.6048  -0.1863 0.0878  647  HIS A C   
4946  O O   . HIS A 647  ? 1.3627 1.9713 1.1437 0.5837  -0.2300 0.0778  647  HIS A O   
4947  C CB  . HIS A 647  ? 1.7902 2.2381 1.3260 0.6850  -0.1115 0.0900  647  HIS A CB  
4948  C CG  . HIS A 647  ? 1.9663 2.3515 1.4610 0.6933  -0.1060 0.0666  647  HIS A CG  
4949  N ND1 . HIS A 647  ? 1.9822 2.3816 1.5388 0.6578  -0.1363 0.0480  647  HIS A ND1 
4950  C CD2 . HIS A 647  ? 2.1060 2.4112 1.5005 0.7351  -0.0723 0.0593  647  HIS A CD2 
4951  C CE1 . HIS A 647  ? 2.0512 2.3873 1.5507 0.6768  -0.1240 0.0299  647  HIS A CE1 
4952  N NE2 . HIS A 647  ? 2.1326 2.4099 1.5334 0.7237  -0.0839 0.0368  647  HIS A NE2 
4953  N N   . LEU A 648  ? 1.3696 1.9141 1.0991 0.5822  -0.1478 0.0910  648  LEU A N   
4954  C CA  . LEU A 648  ? 1.2888 1.8548 1.0973 0.5338  -0.1564 0.0839  648  LEU A CA  
4955  C C   . LEU A 648  ? 1.2064 1.8575 1.1044 0.5094  -0.2094 0.0944  648  LEU A C   
4956  O O   . LEU A 648  ? 1.1713 1.8380 1.1311 0.4734  -0.2277 0.0857  648  LEU A O   
4957  C CB  . LEU A 648  ? 1.2422 1.7923 1.0511 0.5224  -0.1116 0.0903  648  LEU A CB  
4958  C CG  . LEU A 648  ? 1.2498 1.7111 0.9897 0.5309  -0.0555 0.0718  648  LEU A CG  
4959  C CD1 . LEU A 648  ? 1.2454 1.6885 0.9568 0.5408  -0.0085 0.0834  648  LEU A CD1 
4960  C CD2 . LEU A 648  ? 1.2144 1.6558 0.9932 0.4944  -0.0522 0.0445  648  LEU A CD2 
4961  N N   . ALA A 649  ? 1.2050 1.9102 1.1085 0.5296  -0.2326 0.1123  649  ALA A N   
4962  C CA  . ALA A 649  ? 1.1349 1.9188 1.1218 0.5072  -0.2805 0.1205  649  ALA A CA  
4963  C C   . ALA A 649  ? 1.0993 1.8817 1.1096 0.4964  -0.3179 0.0987  649  ALA A C   
4964  O O   . ALA A 649  ? 1.0371 1.8678 1.1226 0.4669  -0.3538 0.0991  649  ALA A O   
4965  C CB  . ALA A 649  ? 1.1843 2.0252 1.1649 0.5357  -0.2967 0.1377  649  ALA A CB  
4966  N N   . GLY A 650  ? 1.1573 1.8818 1.1008 0.5219  -0.3080 0.0798  650  GLY A N   
4967  C CA  . GLY A 650  ? 1.1809 1.9046 1.1363 0.5214  -0.3454 0.0580  650  GLY A CA  
4968  C C   . GLY A 650  ? 1.2313 1.9817 1.1546 0.5640  -0.3706 0.0536  650  GLY A C   
4969  O O   . GLY A 650  ? 1.2123 1.9709 1.1457 0.5707  -0.4059 0.0336  650  GLY A O   
4970  N N   . LEU A 651  ? 1.2590 2.0244 1.1418 0.5960  -0.3530 0.0704  651  LEU A N   
4971  C CA  . LEU A 651  ? 1.3249 2.1286 1.1802 0.6397  -0.3776 0.0664  651  LEU A CA  
4972  C C   . LEU A 651  ? 1.4147 2.1530 1.1533 0.6973  -0.3445 0.0629  651  LEU A C   
4973  O O   . LEU A 651  ? 1.4389 2.1107 1.1180 0.7038  -0.2944 0.0724  651  LEU A O   
4974  C CB  . LEU A 651  ? 1.2884 2.1700 1.1857 0.6375  -0.3881 0.0877  651  LEU A CB  
4975  C CG  . LEU A 651  ? 1.2117 2.1707 1.2241 0.5888  -0.4253 0.0922  651  LEU A CG  
4976  C CD1 . LEU A 651  ? 1.1848 2.2099 1.2265 0.5890  -0.4243 0.1163  651  LEU A CD1 
4977  C CD2 . LEU A 651  ? 1.2109 2.2133 1.2671 0.5887  -0.4752 0.0680  651  LEU A CD2 
4978  N N   . THR A 652  ? 1.4564 2.2135 1.1621 0.7411  -0.3718 0.0477  652  THR A N   
4979  C CA  . THR A 652  ? 1.5022 2.2316 1.1057 0.8043  -0.3480 0.0525  652  THR A CA  
4980  C C   . THR A 652  ? 1.4514 2.2725 1.0793 0.8331  -0.3913 0.0474  652  THR A C   
4981  O O   . THR A 652  ? 1.3920 2.2807 1.0965 0.8164  -0.4406 0.0301  652  THR A O   
4982  C CB  . THR A 652  ? 1.5532 2.1857 1.0505 0.8470  -0.3172 0.0395  652  THR A CB  
4983  O OG1 . THR A 652  ? 1.6077 2.1852 1.0038 0.8903  -0.2684 0.0557  652  THR A OG1 
4984  C CG2 . THR A 652  ? 1.5857 2.2392 1.0658 0.8878  -0.3586 0.0135  652  THR A CG2 
4985  N N   . PHE A 653  ? 1.4978 2.3245 1.0659 0.8727  -0.3714 0.0622  653  PHE A N   
4986  C CA  . PHE A 653  ? 1.5231 2.4485 1.1300 0.8883  -0.4080 0.0612  653  PHE A CA  
4987  C C   . PHE A 653  ? 1.6331 2.5538 1.1432 0.9663  -0.4115 0.0477  653  PHE A C   
4988  O O   . PHE A 653  ? 1.6658 2.4981 1.0712 1.0091  -0.3792 0.0448  653  PHE A O   
4989  C CB  . PHE A 653  ? 1.5277 2.4861 1.1630 0.8654  -0.3893 0.0909  653  PHE A CB  
4990  C CG  . PHE A 653  ? 1.6306 2.5110 1.1624 0.8968  -0.3332 0.1113  653  PHE A CG  
4991  C CD1 . PHE A 653  ? 1.6807 2.5883 1.1618 0.9389  -0.3254 0.1245  653  PHE A CD1 
4992  C CD2 . PHE A 653  ? 1.6609 2.4419 1.1483 0.8832  -0.2873 0.1158  653  PHE A CD2 
4993  C CE1 . PHE A 653  ? 1.7343 2.5660 1.1200 0.9667  -0.2724 0.1434  653  PHE A CE1 
4994  C CE2 . PHE A 653  ? 1.7126 2.4198 1.1096 0.9086  -0.2326 0.1326  653  PHE A CE2 
4995  C CZ  . PHE A 653  ? 1.7476 2.4777 1.0929 0.9503  -0.2249 0.1473  653  PHE A CZ  
4996  N N   . LEU A 654  ? 1.7018 2.7182 1.2456 0.9858  -0.4486 0.0394  654  LEU A N   
4997  C CA  . LEU A 654  ? 1.8280 2.8647 1.3013 1.0599  -0.4682 0.0160  654  LEU A CA  
4998  C C   . LEU A 654  ? 1.9676 3.0653 1.4182 1.0931  -0.4701 0.0260  654  LEU A C   
4999  O O   . LEU A 654  ? 1.9930 3.1982 1.5178 1.0888  -0.5139 0.0103  654  LEU A O   
5000  C CB  . LEU A 654  ? 1.7369 2.8540 1.2967 1.0495  -0.5271 -0.0189 654  LEU A CB  
5001  C CG  . LEU A 654  ? 1.7757 2.8752 1.2524 1.1243  -0.5421 -0.0500 654  LEU A CG  
5002  C CD1 . LEU A 654  ? 1.8391 2.8118 1.1763 1.1689  -0.4860 -0.0337 654  LEU A CD1 
5003  C CD2 . LEU A 654  ? 1.7484 2.8668 1.2993 1.0964  -0.5810 -0.0787 654  LEU A CD2 
5004  N N   . THR A 655  ? 2.0686 3.0982 1.4158 1.1276  -0.4225 0.0500  655  THR A N   
5005  C CA  . THR A 655  ? 2.1263 3.2056 1.4556 1.1481  -0.4172 0.0676  655  THR A CA  
5006  C C   . THR A 655  ? 2.3150 3.3175 1.4910 1.2244  -0.3772 0.0767  655  THR A C   
5007  O O   . THR A 655  ? 2.3206 3.2241 1.4294 1.2218  -0.3236 0.1005  655  THR A O   
5008  C CB  . THR A 655  ? 2.3971 3.4803 1.7927 1.0825  -0.3935 0.1019  655  THR A CB  
5009  O OG1 . THR A 655  ? 2.2926 3.4585 1.8296 1.0157  -0.4309 0.0974  655  THR A OG1 
5010  C CG2 . THR A 655  ? 2.4130 3.5276 1.7683 1.1109  -0.3799 0.1231  655  THR A CG2 
5011  N N   . ASN A 656  ? 2.4864 3.5339 1.6055 1.2937  -0.4014 0.0564  656  ASN A N   
5012  C CA  . ASN A 656  ? 2.7110 3.6772 1.6751 1.3706  -0.3617 0.0653  656  ASN A CA  
5013  C C   . ASN A 656  ? 2.7248 3.6942 1.6612 1.3709  -0.3343 0.0967  656  ASN A C   
5014  O O   . ASN A 656  ? 2.7206 3.7888 1.6892 1.3829  -0.3642 0.0944  656  ASN A O   
5015  C CB  . ASN A 656  ? 2.8347 3.8260 1.7211 1.4575  -0.3905 0.0312  656  ASN A CB  
5016  C CG  . ASN A 656  ? 2.8705 3.7836 1.7045 1.4840  -0.3845 0.0111  656  ASN A CG  
5017  O OD1 . ASN A 656  ? 2.9121 3.8539 1.7066 1.5462  -0.4156 -0.0219 656  ASN A OD1 
5018  N ND2 . ASN A 656  ? 2.8426 3.6597 1.6769 1.4384  -0.3448 0.0293  656  ASN A ND2 
5019  N N   . ALA A 657  ? 2.7413 3.6008 1.6209 1.3557  -0.2760 0.1243  657  ALA A N   
5020  C CA  . ALA A 657  ? 2.7264 3.5647 1.5782 1.3481  -0.2400 0.1566  657  ALA A CA  
5021  C C   . ALA A 657  ? 2.7331 3.4477 1.5523 1.3154  -0.1803 0.1747  657  ALA A C   
5022  O O   . ALA A 657  ? 2.8146 3.4206 1.5080 1.3598  -0.1289 0.1844  657  ALA A O   
5023  C CB  . ALA A 657  ? 2.6068 3.5599 1.5946 1.2865  -0.2724 0.1677  657  ALA A CB  
5024  N N   . ASN A 658  ? 2.6429 3.3740 1.5760 1.2379  -0.1865 0.1771  658  ASN A N   
5025  C CA  . ASN A 658  ? 2.6318 3.2586 1.5523 1.2006  -0.1359 0.1863  658  ASN A CA  
5026  C C   . ASN A 658  ? 2.6267 3.1949 1.5293 1.2028  -0.1348 0.1642  658  ASN A C   
5027  O O   . ASN A 658  ? 2.5882 3.2205 1.5499 1.1983  -0.1845 0.1422  658  ASN A O   
5028  C CB  . ASN A 658  ? 2.5131 3.1839 1.5579 1.1199  -0.1394 0.2000  658  ASN A CB  
5029  C CG  . ASN A 658  ? 2.4702 3.1289 1.4954 1.1156  -0.1050 0.2269  658  ASN A CG  
5030  O OD1 . ASN A 658  ? 2.3960 3.0627 1.4958 1.0593  -0.0926 0.2390  658  ASN A OD1 
5031  N ND2 . ASN A 658  ? 2.5183 3.1564 1.4393 1.1787  -0.0894 0.2353  658  ASN A ND2 
5032  N N   . ALA A 659  ? 2.6640 3.1102 1.4864 1.2091  -0.0766 0.1691  659  ALA A N   
5033  C CA  . ALA A 659  ? 2.6839 3.0675 1.4892 1.2069  -0.0693 0.1502  659  ALA A CA  
5034  C C   . ALA A 659  ? 2.5779 3.0220 1.5229 1.1317  -0.1053 0.1401  659  ALA A C   
5035  O O   . ALA A 659  ? 2.5501 2.9780 1.5525 1.0734  -0.0821 0.1502  659  ALA A O   
5036  C CB  . ALA A 659  ? 2.7526 2.9994 1.4656 1.2123  0.0052  0.1591  659  ALA A CB  
5037  N N   . ASP A 660  ? 2.5430 3.0571 1.5421 1.1345  -0.1619 0.1184  660  ASP A N   
5038  C CA  . ASP A 660  ? 2.4438 3.0122 1.5715 1.0659  -0.1982 0.1078  660  ASP A CA  
5039  C C   . ASP A 660  ? 2.4305 2.9117 1.5491 1.0383  -0.1690 0.0987  660  ASP A C   
5040  O O   . ASP A 660  ? 2.3336 2.8456 1.5432 0.9880  -0.1973 0.0868  660  ASP A O   
5041  C CB  . ASP A 660  ? 2.4444 3.1159 1.6403 1.0733  -0.2673 0.0853  660  ASP A CB  
5042  C CG  . ASP A 660  ? 2.5732 3.2211 1.6800 1.1465  -0.2797 0.0623  660  ASP A CG  
5043  O OD1 . ASP A 660  ? 2.6394 3.1958 1.6797 1.1635  -0.2515 0.0551  660  ASP A OD1 
5044  O OD2 . ASP A 660  ? 2.5976 3.3218 1.7031 1.1879  -0.3185 0.0494  660  ASP A OD2 
5045  N N   . ASP A 661  ? 2.5092 2.8804 1.5159 1.0712  -0.1098 0.1048  661  ASP A N   
5046  C CA  . ASP A 661  ? 2.5180 2.7942 1.4889 1.0601  -0.0737 0.0942  661  ASP A CA  
5047  C C   . ASP A 661  ? 2.4760 2.7571 1.5470 0.9814  -0.0707 0.0908  661  ASP A C   
5048  O O   . ASP A 661  ? 2.4101 2.7632 1.5773 0.9340  -0.0931 0.0993  661  ASP A O   
5049  C CB  . ASP A 661  ? 2.5276 2.6868 1.3678 1.1017  -0.0011 0.1061  661  ASP A CB  
5050  C CG  . ASP A 661  ? 2.3901 2.5069 1.2509 1.0532  0.0500  0.1201  661  ASP A CG  
5051  O OD1 . ASP A 661  ? 2.3208 2.4554 1.1738 1.0571  0.0641  0.1390  661  ASP A OD1 
5052  O OD2 . ASP A 661  ? 2.3543 2.4236 1.2417 1.0116  0.0746  0.1095  661  ASP A OD2 
5053  N N   . SER A 662  ? 2.5176 2.7211 1.5612 0.9710  -0.0423 0.0774  662  SER A N   
5054  C CA  . SER A 662  ? 2.4889 2.6978 1.6211 0.9037  -0.0460 0.0668  662  SER A CA  
5055  C C   . SER A 662  ? 2.5896 2.6886 1.6573 0.9024  0.0114  0.0563  662  SER A C   
5056  O O   . SER A 662  ? 2.5457 2.6258 1.6255 0.8918  -0.0011 0.0370  662  SER A O   
5057  C CB  . SER A 662  ? 2.4619 2.7458 1.6788 0.8841  -0.1144 0.0493  662  SER A CB  
5058  O OG  . SER A 662  ? 2.5220 2.7586 1.6899 0.9122  -0.1190 0.0296  662  SER A OG  
5059  N N   . GLN A 663  ? 2.7202 2.7480 1.7215 0.9120  0.0754  0.0684  663  GLN A N   
5060  C CA  . GLN A 663  ? 2.8660 2.7792 1.7885 0.9193  0.1416  0.0601  663  GLN A CA  
5061  C C   . GLN A 663  ? 2.9883 2.8757 1.9302 0.8994  0.1334  0.0359  663  GLN A C   
5062  O O   . GLN A 663  ? 2.9195 2.8292 1.9444 0.8419  0.1264  0.0227  663  GLN A O   
5063  C CB  . GLN A 663  ? 2.7843 2.6587 1.7161 0.8830  0.1994  0.0659  663  GLN A CB  
5064  C CG  . GLN A 663  ? 2.7219 2.6103 1.6207 0.9084  0.2125  0.0902  663  GLN A CG  
5065  C CD  . GLN A 663  ? 2.7508 2.5940 1.5280 0.9853  0.2232  0.1018  663  GLN A CD  
5066  O OE1 . GLN A 663  ? 2.7999 2.5723 1.4990 1.0205  0.2429  0.0928  663  GLN A OE1 
5067  N NE2 . GLN A 663  ? 2.7315 2.6152 1.4886 1.0148  0.2109  0.1214  663  GLN A NE2 
5068  N N   . GLU A 664  ? 3.1829 3.0243 2.0425 0.9526  0.1333  0.0300  664  GLU A N   
5069  C CA  . GLU A 664  ? 3.3467 3.1443 2.1933 0.9506  0.1347  0.0087  664  GLU A CA  
5070  C C   . GLU A 664  ? 3.3758 3.2280 2.3356 0.8877  0.0945  -0.0109 664  GLU A C   
5071  O O   . GLU A 664  ? 3.3068 3.1822 2.3393 0.8317  0.1036  -0.0127 664  GLU A O   
5072  C CB  . GLU A 664  ? 3.4547 3.1256 2.2021 0.9657  0.2187  0.0070  664  GLU A CB  
5073  C CG  . GLU A 664  ? 3.4650 3.1001 2.2360 0.9165  0.2775  0.0084  664  GLU A CG  
5074  C CD  . GLU A 664  ? 3.6008 3.1090 2.2756 0.9303  0.3630  0.0037  664  GLU A CD  
5075  O OE1 . GLU A 664  ? 3.6431 3.1095 2.3057 0.9248  0.3740  -0.0148 664  GLU A OE1 
5076  O OE2 . GLU A 664  ? 3.6677 3.1167 2.2794 0.9461  0.4204  0.0182  664  GLU A OE2 
5077  N N   . ASN A 665  ? 3.5086 3.3791 2.4789 0.9003  0.0503  -0.0269 665  ASN A N   
5078  C CA  . ASN A 665  ? 3.5447 3.4516 2.6067 0.8457  0.0171  -0.0468 665  ASN A CA  
5079  C C   . ASN A 665  ? 3.5274 3.5289 2.7005 0.7969  -0.0238 -0.0399 665  ASN A C   
5080  O O   . ASN A 665  ? 3.5434 3.5977 2.7255 0.8154  -0.0469 -0.0231 665  ASN A O   
5081  C CB  . ASN A 665  ? 3.5731 3.3997 2.6137 0.8156  0.0797  -0.0597 665  ASN A CB  
5082  C CG  . ASN A 665  ? 3.5021 3.3556 2.6213 0.7660  0.0502  -0.0839 665  ASN A CG  
5083  O OD1 . ASN A 665  ? 3.4197 3.3188 2.6241 0.7125  0.0392  -0.0886 665  ASN A OD1 
5084  N ND2 . ASN A 665  ? 3.5397 3.3623 2.6261 0.7864  0.0387  -0.0999 665  ASN A ND2 
5085  N N   . ASP A 666  ? 3.5125 3.5362 2.7670 0.7378  -0.0322 -0.0528 666  ASP A N   
5086  C CA  . ASP A 666  ? 3.4696 3.5712 2.8204 0.6933  -0.0593 -0.0438 666  ASP A CA  
5087  C C   . ASP A 666  ? 3.3517 3.4597 2.7732 0.6331  -0.0481 -0.0576 666  ASP A C   
5088  O O   . ASP A 666  ? 3.2987 3.4280 2.7725 0.6051  -0.0820 -0.0757 666  ASP A O   
5089  C CB  . ASP A 666  ? 3.5414 3.7337 2.9559 0.6956  -0.1335 -0.0398 666  ASP A CB  
5090  C CG  . ASP A 666  ? 3.6241 3.8358 3.0848 0.6777  -0.1806 -0.0621 666  ASP A CG  
5091  O OD1 . ASP A 666  ? 3.6943 3.8451 3.1130 0.6832  -0.1604 -0.0796 666  ASP A OD1 
5092  O OD2 . ASP A 666  ? 3.6075 3.8949 3.1465 0.6581  -0.2374 -0.0622 666  ASP A OD2 
5093  N N   . GLU A 667  ? 3.2890 3.3765 2.7068 0.6173  0.0005  -0.0508 667  GLU A N   
5094  C CA  . GLU A 667  ? 3.1530 3.2798 2.6527 0.5666  0.0006  -0.0562 667  GLU A CA  
5095  C C   . GLU A 667  ? 3.0951 3.2547 2.6689 0.5258  -0.0370 -0.0782 667  GLU A C   
5096  O O   . GLU A 667  ? 3.0460 3.2765 2.6926 0.5058  -0.0863 -0.0707 667  GLU A O   
5097  C CB  . GLU A 667  ? 3.0157 3.2172 2.5634 0.5648  -0.0290 -0.0302 667  GLU A CB  
5098  C CG  . GLU A 667  ? 2.9716 3.1801 2.4640 0.6142  -0.0399 -0.0087 667  GLU A CG  
5099  C CD  . GLU A 667  ? 2.9681 3.1027 2.3655 0.6485  0.0232  -0.0001 667  GLU A CD  
5100  O OE1 . GLU A 667  ? 2.9684 3.0326 2.3318 0.6382  0.0755  -0.0154 667  GLU A OE1 
5101  O OE2 . GLU A 667  ? 2.9729 3.1191 2.3291 0.6858  0.0222  0.0207  667  GLU A OE2 
5102  N N   . PRO A 668  ? 3.0949 3.2031 2.6507 0.5129  -0.0122 -0.1057 668  PRO A N   
5103  C CA  . PRO A 668  ? 3.0365 3.1755 2.6591 0.4755  -0.0478 -0.1285 668  PRO A CA  
5104  C C   . PRO A 668  ? 2.9601 3.1495 2.6611 0.4354  -0.0530 -0.1311 668  PRO A C   
5105  O O   . PRO A 668  ? 2.9269 3.1166 2.6625 0.4059  -0.0535 -0.1578 668  PRO A O   
5106  C CB  . PRO A 668  ? 3.0653 3.1338 2.6422 0.4733  -0.0076 -0.1579 668  PRO A CB  
5107  C CG  . PRO A 668  ? 3.1489 3.1531 2.6309 0.5190  0.0291  -0.1463 668  PRO A CG  
5108  C CD  . PRO A 668  ? 3.1597 3.1793 2.6282 0.5366  0.0441  -0.1169 668  PRO A CD  
5109  N N   . CYS A 669  ? 2.9550 3.1878 2.6808 0.4380  -0.0582 -0.1048 669  CYS A N   
5110  C CA  . CYS A 669  ? 2.8996 3.1810 2.6935 0.4080  -0.0608 -0.1026 669  CYS A CA  
5111  C C   . CYS A 669  ? 2.8593 3.1594 2.7096 0.3734  -0.0824 -0.1296 669  CYS A C   
5112  O O   . CYS A 669  ? 2.8563 3.1613 2.7184 0.3685  -0.1220 -0.1396 669  CYS A O   
5113  C CB  . CYS A 669  ? 2.8753 3.2237 2.7090 0.4132  -0.0994 -0.0695 669  CYS A CB  
5114  S SG  . CYS A 669  ? 3.4300 3.8490 3.3593 0.3767  -0.1264 -0.0654 669  CYS A SG  
5115  N N   . LYS A 670  ? 2.8222 3.1343 2.7062 0.3522  -0.0573 -0.1426 670  LYS A N   
5116  C CA  . LYS A 670  ? 2.7683 3.0942 2.6973 0.3240  -0.0702 -0.1733 670  LYS A CA  
5117  C C   . LYS A 670  ? 2.6808 3.0457 2.6595 0.3083  -0.0569 -0.1766 670  LYS A C   
5118  O O   . LYS A 670  ? 2.6771 3.0209 2.6444 0.3061  -0.0075 -0.1946 670  LYS A O   
5119  C CB  . LYS A 670  ? 2.8188 3.0860 2.7084 0.3200  -0.0341 -0.2112 670  LYS A CB  
5120  C CG  . LYS A 670  ? 2.7976 3.0781 2.7272 0.2938  -0.0446 -0.2490 670  LYS A CG  
5121  C CD  . LYS A 670  ? 2.7875 3.0987 2.7485 0.2866  -0.1092 -0.2449 670  LYS A CD  
5122  C CE  . LYS A 670  ? 2.7585 3.0854 2.7565 0.2639  -0.1225 -0.2813 670  LYS A CE  
5123  N NZ  . LYS A 670  ? 2.7878 3.0702 2.7535 0.2591  -0.0945 -0.3227 670  LYS A NZ  
5124  N N   . GLU A 671  ? 2.6193 3.0402 2.6527 0.2990  -0.0998 -0.1594 671  GLU A N   
5125  C CA  . GLU A 671  ? 2.5324 2.9938 2.6157 0.2867  -0.0951 -0.1646 671  GLU A CA  
5126  C C   . GLU A 671  ? 2.2666 2.7368 2.3474 0.2964  -0.0532 -0.1535 671  GLU A C   
5127  O O   . GLU A 671  ? 2.2782 2.7532 2.3773 0.2889  -0.0243 -0.1800 671  GLU A O   
5128  C CB  . GLU A 671  ? 2.5144 2.9669 2.6138 0.2694  -0.0888 -0.2106 671  GLU A CB  
5129  C CG  . GLU A 671  ? 2.4891 2.9401 2.5979 0.2590  -0.1349 -0.2222 671  GLU A CG  
5130  C CD  . GLU A 671  ? 2.4476 2.8958 2.5715 0.2448  -0.1306 -0.2689 671  GLU A CD  
5131  O OE1 . GLU A 671  ? 2.4223 2.8745 2.5546 0.2425  -0.0923 -0.2947 671  GLU A OE1 
5132  O OE2 . GLU A 671  ? 2.4382 2.8823 2.5662 0.2370  -0.1663 -0.2822 671  GLU A OE2 
5133  N N   . ILE A 672  ? 2.1897 2.6644 2.2483 0.3145  -0.0514 -0.1172 672  ILE A N   
5134  C CA  . ILE A 672  ? 2.0822 2.5726 2.1407 0.3261  -0.0202 -0.0996 672  ILE A CA  
5135  C C   . ILE A 672  ? 1.9488 2.5047 2.0527 0.3290  -0.0555 -0.0617 672  ILE A C   
5136  O O   . ILE A 672  ? 1.9090 2.4921 2.0286 0.3358  -0.0381 -0.0487 672  ILE A O   
5137  C CB  . ILE A 672  ? 2.3692 2.8107 2.3583 0.3492  0.0175  -0.0872 672  ILE A CB  
5138  C CG1 . ILE A 672  ? 2.3567 2.7865 2.3356 0.3548  0.0697  -0.0928 672  ILE A CG1 
5139  C CG2 . ILE A 672  ? 2.3868 2.8509 2.3606 0.3694  -0.0140 -0.0463 672  ILE A CG2 
5140  C CD1 . ILE A 672  ? 2.4113 2.7931 2.3192 0.3807  0.1058  -0.0749 672  ILE A CD1 
5141  N N   . LEU A 673  ? 1.8516 2.4328 1.9780 0.3235  -0.1039 -0.0452 673  LEU A N   
5142  C CA  . LEU A 673  ? 1.7107 2.3510 1.8795 0.3245  -0.1353 -0.0091 673  LEU A CA  
5143  C C   . LEU A 673  ? 1.6453 2.3230 1.8628 0.3160  -0.1316 -0.0109 673  LEU A C   
5144  O O   . LEU A 673  ? 1.6080 2.3336 1.8671 0.3133  -0.1578 0.0159  673  LEU A O   
5145  C CB  . LEU A 673  ? 1.6105 2.2686 1.8032 0.3144  -0.1857 0.0009  673  LEU A CB  
5146  C CG  . LEU A 673  ? 1.4643 2.1484 1.7115 0.2930  -0.2163 -0.0044 673  LEU A CG  
5147  C CD1 . LEU A 673  ? 1.4174 2.1397 1.6985 0.2874  -0.2592 0.0245  673  LEU A CD1 
5148  C CD2 . LEU A 673  ? 1.4336 2.0791 1.6712 0.2801  -0.2208 -0.0430 673  LEU A CD2 
5149  N N   . LEU A 679  ? 3.1119 3.1036 2.8561 -0.5599 0.4088  -0.6827 679  LEU A N   
5150  C CA  . LEU A 679  ? 3.0860 3.1153 2.8235 -0.5541 0.3799  -0.7031 679  LEU A CA  
5151  C C   . LEU A 679  ? 3.0751 3.0664 2.8541 -0.5213 0.3506  -0.6858 679  LEU A C   
5152  O O   . LEU A 679  ? 3.0732 3.0701 2.8408 -0.5192 0.3383  -0.7025 679  LEU A O   
5153  C CB  . LEU A 679  ? 3.0435 3.1519 2.7815 -0.5473 0.3468  -0.7111 679  LEU A CB  
5154  C CG  . LEU A 679  ? 3.0446 3.2036 2.7347 -0.5819 0.3710  -0.7358 679  LEU A CG  
5155  C CD1 . LEU A 679  ? 3.0152 3.2377 2.7165 -0.5674 0.3406  -0.7291 679  LEU A CD1 
5156  C CD2 . LEU A 679  ? 3.0509 3.2405 2.6975 -0.6101 0.3841  -0.7739 679  LEU A CD2 
5157  N N   . GLN A 680  ? 3.0743 3.0275 2.9010 -0.4965 0.3397  -0.6529 680  GLN A N   
5158  C CA  . GLN A 680  ? 3.0671 2.9771 2.9342 -0.4676 0.3159  -0.6348 680  GLN A CA  
5159  C C   . GLN A 680  ? 3.0710 2.9135 2.9267 -0.4777 0.3532  -0.6322 680  GLN A C   
5160  O O   . GLN A 680  ? 3.0680 2.8717 2.9447 -0.4588 0.3399  -0.6230 680  GLN A O   
5161  C CB  . GLN A 680  ? 3.0774 2.9806 3.0043 -0.4364 0.2851  -0.6013 680  GLN A CB  
5162  C CG  . GLN A 680  ? 3.1166 2.9583 3.0780 -0.4289 0.3049  -0.5734 680  GLN A CG  
5163  C CD  . GLN A 680  ? 3.1599 2.9902 3.0999 -0.4531 0.3503  -0.5709 680  GLN A CD  
5164  O OE1 . GLN A 680  ? 3.1769 3.0471 3.0779 -0.4751 0.3643  -0.5886 680  GLN A OE1 
5165  N NE2 . GLN A 680  ? 3.1788 2.9548 3.1441 -0.4488 0.3736  -0.5489 680  GLN A NE2 
5166  N N   . LYS A 681  ? 3.0677 2.8954 2.8877 -0.5071 0.4003  -0.6403 681  LYS A N   
5167  C CA  . LYS A 681  ? 3.0564 2.8197 2.8568 -0.5192 0.4421  -0.6399 681  LYS A CA  
5168  C C   . LYS A 681  ? 3.0730 2.8306 2.8281 -0.5341 0.4523  -0.6689 681  LYS A C   
5169  O O   . LYS A 681  ? 3.0973 2.7981 2.8438 -0.5318 0.4716  -0.6663 681  LYS A O   
5170  C CB  . LYS A 681  ? 3.0436 2.7940 2.8129 -0.5483 0.4910  -0.6424 681  LYS A CB  
5171  C CG  . LYS A 681  ? 2.9836 2.7664 2.7753 -0.5447 0.4820  -0.6269 681  LYS A CG  
5172  C CD  . LYS A 681  ? 2.9803 2.7711 2.7216 -0.5811 0.5261  -0.6426 681  LYS A CD  
5173  C CE  . LYS A 681  ? 2.9450 2.7825 2.6975 -0.5787 0.5109  -0.6342 681  LYS A CE  
5174  N NZ  . LYS A 681  ? 2.9766 2.8272 2.6747 -0.6154 0.5505  -0.6527 681  LYS A NZ  
5175  N N   . LYS A 682  ? 3.0618 2.8791 2.7880 -0.5490 0.4402  -0.6961 682  LYS A N   
5176  C CA  . LYS A 682  ? 3.0775 2.9003 2.7603 -0.5653 0.4484  -0.7268 682  LYS A CA  
5177  C C   . LYS A 682  ? 3.1063 2.9057 2.8128 -0.5353 0.4152  -0.7197 682  LYS A C   
5178  O O   . LYS A 682  ? 3.1091 2.8827 2.7830 -0.5435 0.4291  -0.7370 682  LYS A O   
5179  C CB  . LYS A 682  ? 3.0307 2.9327 2.6869 -0.5848 0.4378  -0.7553 682  LYS A CB  
5180  C CG  . LYS A 682  ? 3.0001 2.9248 2.6331 -0.5879 0.4245  -0.7818 682  LYS A CG  
5181  C CD  . LYS A 682  ? 3.0189 2.9050 2.5973 -0.6195 0.4713  -0.8065 682  LYS A CD  
5182  C CE  . LYS A 682  ? 2.9934 2.8983 2.5502 -0.6214 0.4589  -0.8318 682  LYS A CE  
5183  N NZ  . LYS A 682  ? 3.0220 2.8869 2.5228 -0.6532 0.5065  -0.8568 682  LYS A NZ  
5184  N N   . ILE A 683  ? 3.1370 2.9444 2.8981 -0.5010 0.3713  -0.6947 683  ILE A N   
5185  C CA  . ILE A 683  ? 3.1835 2.9623 2.9708 -0.4708 0.3387  -0.6841 683  ILE A CA  
5186  C C   . ILE A 683  ? 3.2514 2.9581 3.0615 -0.4572 0.3542  -0.6590 683  ILE A C   
5187  O O   . ILE A 683  ? 3.2912 2.9548 3.0940 -0.4466 0.3534  -0.6593 683  ILE A O   
5188  C CB  . ILE A 683  ? 2.6602 2.4786 2.4947 -0.4401 0.2832  -0.6700 683  ILE A CB  
5189  C CG1 . ILE A 683  ? 2.6144 2.5078 2.4347 -0.4523 0.2729  -0.6867 683  ILE A CG1 
5190  C CG2 . ILE A 683  ? 2.6665 2.4712 2.5075 -0.4176 0.2503  -0.6729 683  ILE A CG2 
5191  C CD1 . ILE A 683  ? 2.5520 2.4801 2.4175 -0.4233 0.2259  -0.6687 683  ILE A CD1 
5192  N N   . GLU A 684  ? 3.2721 2.9660 3.1077 -0.4575 0.3700  -0.6376 684  GLU A N   
5193  C CA  . GLU A 684  ? 3.3042 2.9370 3.1730 -0.4407 0.3809  -0.6096 684  GLU A CA  
5194  C C   . GLU A 684  ? 3.3067 2.8813 3.1336 -0.4554 0.4266  -0.6179 684  GLU A C   
5195  O O   . GLU A 684  ? 3.3075 2.8293 3.1574 -0.4388 0.4349  -0.5967 684  GLU A O   
5196  C CB  . GLU A 684  ? 3.3584 2.9939 3.2648 -0.4382 0.3890  -0.5851 684  GLU A CB  
5197  C CG  . GLU A 684  ? 3.3774 3.0435 3.3441 -0.4103 0.3395  -0.5638 684  GLU A CG  
5198  C CD  . GLU A 684  ? 3.4165 3.0654 3.4314 -0.4006 0.3469  -0.5331 684  GLU A CD  
5199  O OE1 . GLU A 684  ? 3.4579 3.0703 3.4623 -0.4135 0.3900  -0.5265 684  GLU A OE1 
5200  O OE2 . GLU A 684  ? 3.4017 3.0723 3.4646 -0.3799 0.3105  -0.5156 684  GLU A OE2 
5201  N N   . GLU A 685  ? 3.3093 2.8943 3.0747 -0.4863 0.4563  -0.6489 685  GLU A N   
5202  C CA  . GLU A 685  ? 3.3300 2.8594 3.0471 -0.5020 0.5003  -0.6608 685  GLU A CA  
5203  C C   . GLU A 685  ? 3.2833 2.7877 2.9941 -0.4829 0.4782  -0.6657 685  GLU A C   
5204  O O   . GLU A 685  ? 3.3164 2.7604 3.0064 -0.4793 0.5026  -0.6628 685  GLU A O   
5205  C CB  . GLU A 685  ? 3.3739 2.9267 3.0273 -0.5443 0.5387  -0.6944 685  GLU A CB  
5206  C CG  . GLU A 685  ? 3.3596 2.9777 2.9979 -0.5525 0.5101  -0.7207 685  GLU A CG  
5207  C CD  . GLU A 685  ? 3.3827 3.0447 2.9746 -0.5932 0.5394  -0.7497 685  GLU A CD  
5208  O OE1 . GLU A 685  ? 3.4090 3.0548 2.9855 -0.6136 0.5770  -0.7468 685  GLU A OE1 
5209  O OE2 . GLU A 685  ? 3.3732 3.0868 2.9445 -0.6048 0.5245  -0.7757 685  GLU A OE2 
5210  N N   . ILE A 686  ? 3.2002 2.7500 2.9270 -0.4697 0.4323  -0.6729 686  ILE A N   
5211  C CA  . ILE A 686  ? 3.1569 2.6884 2.8761 -0.4514 0.4072  -0.6792 686  ILE A CA  
5212  C C   . ILE A 686  ? 3.0988 2.5904 2.8695 -0.4123 0.3753  -0.6480 686  ILE A C   
5213  O O   . ILE A 686  ? 3.0985 2.5885 2.8797 -0.3901 0.3377  -0.6478 686  ILE A O   
5214  C CB  . ILE A 686  ? 3.1282 2.7231 2.8423 -0.4523 0.3720  -0.6997 686  ILE A CB  
5215  C CG1 . ILE A 686  ? 3.1261 2.7722 2.8014 -0.4896 0.3990  -0.7271 686  ILE A CG1 
5216  C CG2 . ILE A 686  ? 3.1461 2.7185 2.8328 -0.4429 0.3598  -0.7142 686  ILE A CG2 
5217  C CD1 . ILE A 686  ? 3.1663 2.7820 2.7766 -0.5231 0.4520  -0.7527 686  ILE A CD1 
5218  N N   . ALA A 687  ? 3.0344 2.4956 2.8374 -0.4045 0.3904  -0.6222 687  ALA A N   
5219  C CA  . ALA A 687  ? 2.9555 2.3690 2.7989 -0.3725 0.3739  -0.5945 687  ALA A CA  
5220  C C   . ALA A 687  ? 2.9353 2.2879 2.7281 -0.3774 0.4099  -0.6034 687  ALA A C   
5221  O O   . ALA A 687  ? 2.9234 2.2273 2.7337 -0.3536 0.4068  -0.5842 687  ALA A O   
5222  C CB  . ALA A 687  ? 2.9358 2.3405 2.8291 -0.3653 0.3835  -0.5656 687  ALA A CB  
5223  N N   . ALA A 688  ? 2.9312 2.2886 2.6599 -0.4092 0.4452  -0.6334 688  ALA A N   
5224  C CA  . ALA A 688  ? 2.9322 2.2345 2.6000 -0.4203 0.4846  -0.6484 688  ALA A CA  
5225  C C   . ALA A 688  ? 2.9034 2.1821 2.5636 -0.3960 0.4538  -0.6507 688  ALA A C   
5226  O O   . ALA A 688  ? 2.9193 2.1436 2.5331 -0.3971 0.4807  -0.6584 688  ALA A O   
5227  C CB  . ALA A 688  ? 2.9532 2.2775 2.5584 -0.4623 0.5231  -0.6829 688  ALA A CB  
5228  N N   . LYS A 689  ? 2.8432 2.1604 2.5448 -0.3745 0.3985  -0.6449 689  LYS A N   
5229  C CA  . LYS A 689  ? 2.8579 2.1496 2.5587 -0.3473 0.3645  -0.6428 689  LYS A CA  
5230  C C   . LYS A 689  ? 2.9178 2.1906 2.6825 -0.3103 0.3273  -0.6092 689  LYS A C   
5231  O O   . LYS A 689  ? 2.9183 2.1983 2.7072 -0.2859 0.2796  -0.6038 689  LYS A O   
5232  C CB  . LYS A 689  ? 2.7520 2.0907 2.4405 -0.3495 0.3312  -0.6649 689  LYS A CB  
5233  C CG  . LYS A 689  ? 2.6326 2.0382 2.3707 -0.3442 0.2909  -0.6593 689  LYS A CG  
5234  C CD  . LYS A 689  ? 2.5644 2.0105 2.2792 -0.3478 0.2665  -0.6840 689  LYS A CD  
5235  C CE  . LYS A 689  ? 2.5468 2.0016 2.1956 -0.3836 0.3105  -0.7173 689  LYS A CE  
5236  N NZ  . LYS A 689  ? 2.5224 1.9901 2.1368 -0.3836 0.2955  -0.7415 689  LYS A NZ  
5237  N N   . TYR A 690  ? 3.0114 2.2606 2.8036 -0.3071 0.3499  -0.5869 690  TYR A N   
5238  C CA  . TYR A 690  ? 3.0999 2.3225 2.9477 -0.2730 0.3229  -0.5557 690  TYR A CA  
5239  C C   . TYR A 690  ? 3.1657 2.3302 2.9813 -0.2534 0.3217  -0.5556 690  TYR A C   
5240  O O   . TYR A 690  ? 3.2005 2.3248 2.9531 -0.2676 0.3642  -0.5707 690  TYR A O   
5241  C CB  . TYR A 690  ? 3.1834 2.3919 3.0646 -0.2747 0.3531  -0.5328 690  TYR A CB  
5242  C CG  . TYR A 690  ? 3.2824 2.4478 3.2032 -0.2425 0.3425  -0.5039 690  TYR A CG  
5243  C CD1 . TYR A 690  ? 3.2816 2.4642 3.2686 -0.2134 0.2879  -0.4837 690  TYR A CD1 
5244  C CD2 . TYR A 690  ? 3.3631 2.4709 3.2545 -0.2410 0.3871  -0.4972 690  TYR A CD2 
5245  C CE1 . TYR A 690  ? 3.3204 2.4685 3.3459 -0.1842 0.2764  -0.4580 690  TYR A CE1 
5246  C CE2 . TYR A 690  ? 3.4024 2.4742 3.3309 -0.2096 0.3768  -0.4703 690  TYR A CE2 
5247  C CZ  . TYR A 690  ? 3.3801 2.4745 3.3770 -0.1815 0.3205  -0.4511 690  TYR A CZ  
5248  O OH  . TYR A 690  ? 3.4047 2.4679 3.4410 -0.1507 0.3089  -0.4249 690  TYR A OH  
5249  N N   . LYS A 691  ? 3.1943 2.3542 3.0518 -0.2211 0.2725  -0.5389 691  LYS A N   
5250  C CA  . LYS A 691  ? 3.2442 2.3535 3.0765 -0.1976 0.2605  -0.5369 691  LYS A CA  
5251  C C   . LYS A 691  ? 3.2378 2.3612 3.1368 -0.1654 0.1999  -0.5153 691  LYS A C   
5252  O O   . LYS A 691  ? 3.2572 2.3524 3.1493 -0.1414 0.1707  -0.5123 691  LYS A O   
5253  C CB  . LYS A 691  ? 3.2634 2.3676 3.0272 -0.2098 0.2635  -0.5678 691  LYS A CB  
5254  C CG  . LYS A 691  ? 3.2015 2.3669 2.9756 -0.2189 0.2289  -0.5841 691  LYS A CG  
5255  C CD  . LYS A 691  ? 3.2019 2.3644 2.9061 -0.2353 0.2415  -0.6163 691  LYS A CD  
5256  C CE  . LYS A 691  ? 3.1458 2.3754 2.8574 -0.2497 0.2190  -0.6342 691  LYS A CE  
5257  N NZ  . LYS A 691  ? 3.1594 2.3903 2.8039 -0.2696 0.2387  -0.6668 691  LYS A NZ  
5258  N N   . HIS A 692  ? 3.1817 2.3491 3.1437 -0.1667 0.1825  -0.5011 692  HIS A N   
5259  C CA  . HIS A 692  ? 3.1448 2.3329 3.1783 -0.1415 0.1281  -0.4803 692  HIS A CA  
5260  C C   . HIS A 692  ? 3.0337 2.2768 3.1127 -0.1552 0.1207  -0.4759 692  HIS A C   
5261  O O   . HIS A 692  ? 2.9999 2.2728 3.0477 -0.1804 0.1404  -0.4951 692  HIS A O   
5262  C CB  . HIS A 692  ? 3.2082 2.3966 3.2283 -0.1253 0.0802  -0.4908 692  HIS A CB  
5263  C CG  . HIS A 692  ? 3.2611 2.4532 3.3463 -0.0962 0.0265  -0.4688 692  HIS A CG  
5264  N ND1 . HIS A 692  ? 3.3129 2.4729 3.4320 -0.0737 0.0216  -0.4453 692  HIS A ND1 
5265  C CD2 . HIS A 692  ? 3.2644 2.4886 3.3866 -0.0864 -0.0245 -0.4672 692  HIS A CD2 
5266  C CE1 . HIS A 692  ? 3.3115 2.4862 3.4874 -0.0530 -0.0310 -0.4311 692  HIS A CE1 
5267  N NE2 . HIS A 692  ? 3.2823 2.4934 3.4597 -0.0606 -0.0591 -0.4441 692  HIS A NE2 
5268  N N   . SER A 693  ? 2.9636 2.2204 3.1162 -0.1387 0.0931  -0.4507 693  SER A N   
5269  C CA  . SER A 693  ? 2.8645 2.1691 3.0614 -0.1489 0.0843  -0.4445 693  SER A CA  
5270  C C   . SER A 693  ? 2.7589 2.1020 2.9370 -0.1554 0.0546  -0.4643 693  SER A C   
5271  O O   . SER A 693  ? 2.7377 2.1145 2.8952 -0.1774 0.0728  -0.4779 693  SER A O   
5272  C CB  . SER A 693  ? 2.8490 2.1596 3.1291 -0.1274 0.0515  -0.4153 693  SER A CB  
5273  O OG  . SER A 693  ? 2.8042 2.1597 3.1251 -0.1333 0.0317  -0.4108 693  SER A OG  
5274  N N   . VAL A 694  ? 2.6890 2.0257 2.8722 -0.1352 0.0091  -0.4660 694  VAL A N   
5275  C CA  . VAL A 694  ? 2.6069 1.9778 2.7851 -0.1339 -0.0286 -0.4797 694  VAL A CA  
5276  C C   . VAL A 694  ? 2.5613 1.9550 2.6756 -0.1577 -0.0037 -0.5088 694  VAL A C   
5277  O O   . VAL A 694  ? 2.5338 1.9677 2.6474 -0.1616 -0.0244 -0.5192 694  VAL A O   
5278  C CB  . VAL A 694  ? 2.5388 1.8878 2.7214 -0.1081 -0.0776 -0.4786 694  VAL A CB  
5279  C CG1 . VAL A 694  ? 2.5091 1.8926 2.6970 -0.1042 -0.1182 -0.4882 694  VAL A CG1 
5280  C CG2 . VAL A 694  ? 2.5385 1.8665 2.7838 -0.0857 -0.1017 -0.4511 694  VAL A CG2 
5281  N N   . VAL A 695  ? 2.5479 1.9169 2.6088 -0.1737 0.0415  -0.5221 695  VAL A N   
5282  C CA  . VAL A 695  ? 2.5129 1.9073 2.5172 -0.2000 0.0688  -0.5500 695  VAL A CA  
5283  C C   . VAL A 695  ? 2.4609 1.8930 2.4798 -0.2217 0.0956  -0.5480 695  VAL A C   
5284  O O   . VAL A 695  ? 2.4319 1.9087 2.4316 -0.2378 0.0968  -0.5653 695  VAL A O   
5285  C CB  . VAL A 695  ? 2.5640 1.9172 2.5006 -0.2118 0.1082  -0.5680 695  VAL A CB  
5286  C CG1 . VAL A 695  ? 2.5576 1.9425 2.4391 -0.2406 0.1339  -0.5989 695  VAL A CG1 
5287  C CG2 . VAL A 695  ? 2.5867 1.9005 2.5075 -0.1881 0.0803  -0.5686 695  VAL A CG2 
5288  N N   . LYS A 696  ? 2.4491 1.8642 2.5024 -0.2213 0.1162  -0.5265 696  LYS A N   
5289  C CA  . LYS A 696  ? 2.4124 1.8603 2.4827 -0.2395 0.1389  -0.5219 696  LYS A CA  
5290  C C   . LYS A 696  ? 2.3683 1.8670 2.4718 -0.2334 0.0992  -0.5200 696  LYS A C   
5291  O O   . LYS A 696  ? 2.3551 1.8957 2.4322 -0.2505 0.1051  -0.5378 696  LYS A O   
5292  C CB  . LYS A 696  ? 2.4178 1.8408 2.5342 -0.2331 0.1566  -0.4942 696  LYS A CB  
5293  C CG  . LYS A 696  ? 2.3998 1.8582 2.5479 -0.2453 0.1677  -0.4840 696  LYS A CG  
5294  C CD  . LYS A 696  ? 2.3483 1.8316 2.4416 -0.2780 0.2076  -0.5071 696  LYS A CD  
5295  C CE  . LYS A 696  ? 2.3158 1.8295 2.4364 -0.2893 0.2208  -0.4959 696  LYS A CE  
5296  N NZ  . LYS A 696  ? 2.3013 1.8432 2.3691 -0.3213 0.2563  -0.5186 696  LYS A NZ  
5297  N N   . LYS A 697  ? 2.3330 1.8273 2.4941 -0.2085 0.0586  -0.4985 697  LYS A N   
5298  C CA  . LYS A 697  ? 2.2851 1.8184 2.4785 -0.1984 0.0169  -0.4950 697  LYS A CA  
5299  C C   . LYS A 697  ? 2.2654 1.8259 2.4110 -0.2032 0.0028  -0.5218 697  LYS A C   
5300  O O   . LYS A 697  ? 2.2509 1.8559 2.3975 -0.2077 -0.0091 -0.5281 697  LYS A O   
5301  C CB  . LYS A 697  ? 2.2784 1.7922 2.5291 -0.1705 -0.0269 -0.4731 697  LYS A CB  
5302  C CG  . LYS A 697  ? 2.2661 1.8104 2.5460 -0.1575 -0.0732 -0.4703 697  LYS A CG  
5303  C CD  . LYS A 697  ? 2.2569 1.8317 2.5767 -0.1626 -0.0703 -0.4558 697  LYS A CD  
5304  C CE  . LYS A 697  ? 2.2466 1.8439 2.5944 -0.1469 -0.1170 -0.4516 697  LYS A CE  
5305  N NZ  . LYS A 697  ? 2.2327 1.8623 2.6070 -0.1520 -0.1141 -0.4412 697  LYS A NZ  
5306  N N   . CYS A 698  ? 2.2589 1.7926 2.3614 -0.2020 0.0059  -0.5375 698  CYS A N   
5307  C CA  . CYS A 698  ? 2.2447 1.8020 2.3004 -0.2073 -0.0034 -0.5639 698  CYS A CA  
5308  C C   . CYS A 698  ? 2.2127 1.8166 2.2358 -0.2346 0.0268  -0.5829 698  CYS A C   
5309  O O   . CYS A 698  ? 2.1615 1.8111 2.1844 -0.2341 0.0065  -0.5916 698  CYS A O   
5310  C CB  . CYS A 698  ? 2.2720 1.7873 2.2808 -0.2051 0.0050  -0.5782 698  CYS A CB  
5311  S SG  . CYS A 698  ? 2.6922 2.1717 2.7193 -0.1709 -0.0483 -0.5688 698  CYS A SG  
5312  N N   . CYS A 699  ? 2.2758 1.8689 2.2707 -0.2580 0.0749  -0.5895 699  CYS A N   
5313  C CA  . CYS A 699  ? 2.3131 1.9519 2.2769 -0.2853 0.1023  -0.6084 699  CYS A CA  
5314  C C   . CYS A 699  ? 2.3303 2.0056 2.3347 -0.2852 0.0947  -0.5926 699  CYS A C   
5315  O O   . CYS A 699  ? 2.3074 2.0348 2.3042 -0.2916 0.0856  -0.6035 699  CYS A O   
5316  C CB  . CYS A 699  ? 2.3646 1.9791 2.2850 -0.3125 0.1572  -0.6202 699  CYS A CB  
5317  S SG  . CYS A 699  ? 2.3442 2.0124 2.2393 -0.3470 0.1922  -0.6364 699  CYS A SG  
5318  N N   . TYR A 700  ? 2.3837 2.0311 2.4311 -0.2768 0.0994  -0.5664 700  TYR A N   
5319  C CA  . TYR A 700  ? 2.4564 2.1294 2.5417 -0.2778 0.0990  -0.5492 700  TYR A CA  
5320  C C   . TYR A 700  ? 2.4724 2.1896 2.5792 -0.2631 0.0562  -0.5479 700  TYR A C   
5321  O O   . TYR A 700  ? 2.4677 2.2322 2.5539 -0.2754 0.0610  -0.5606 700  TYR A O   
5322  C CB  . TYR A 700  ? 2.5386 2.1713 2.6765 -0.2638 0.1001  -0.5191 700  TYR A CB  
5323  C CG  . TYR A 700  ? 2.6278 2.2697 2.7894 -0.2745 0.1254  -0.5035 700  TYR A CG  
5324  C CD1 . TYR A 700  ? 2.6515 2.3119 2.8647 -0.2608 0.0999  -0.4832 700  TYR A CD1 
5325  C CD2 . TYR A 700  ? 2.6899 2.3181 2.8202 -0.2984 0.1762  -0.5092 700  TYR A CD2 
5326  C CE1 . TYR A 700  ? 2.6826 2.3484 2.9155 -0.2700 0.1241  -0.4686 700  TYR A CE1 
5327  C CE2 . TYR A 700  ? 2.7237 2.3570 2.8728 -0.3078 0.2002  -0.4949 700  TYR A CE2 
5328  C CZ  . TYR A 700  ? 2.7182 2.3707 2.9190 -0.2931 0.1739  -0.4744 700  TYR A CZ  
5329  O OH  . TYR A 700  ? 2.7317 2.3872 2.9499 -0.3020 0.1988  -0.4597 700  TYR A OH  
5330  N N   . ASP A 701  ? 2.4869 2.1883 2.6333 -0.2365 0.0146  -0.5330 701  ASP A N   
5331  C CA  . ASP A 701  ? 2.4839 2.2188 2.6475 -0.2200 -0.0274 -0.5319 701  ASP A CA  
5332  C C   . ASP A 701  ? 2.4628 2.2225 2.5782 -0.2227 -0.0370 -0.5596 701  ASP A C   
5333  O O   . ASP A 701  ? 2.4587 2.2490 2.5770 -0.2100 -0.0685 -0.5635 701  ASP A O   
5334  C CB  . ASP A 701  ? 2.4924 2.1999 2.7107 -0.1928 -0.0680 -0.5090 701  ASP A CB  
5335  C CG  . ASP A 701  ? 2.5124 2.1872 2.7197 -0.1786 -0.0910 -0.5158 701  ASP A CG  
5336  O OD1 . ASP A 701  ? 2.5320 2.2049 2.6885 -0.1882 -0.0769 -0.5381 701  ASP A OD1 
5337  O OD2 . ASP A 701  ? 2.5072 2.1576 2.7563 -0.1582 -0.1236 -0.4988 701  ASP A OD2 
5338  N N   . GLY A 702  ? 2.4456 2.1899 2.5160 -0.2394 -0.0075 -0.5785 702  GLY A N   
5339  C CA  . GLY A 702  ? 2.3996 2.1657 2.4214 -0.2463 -0.0084 -0.6066 702  GLY A CA  
5340  C C   . GLY A 702  ? 2.3427 2.1715 2.3418 -0.2626 0.0017  -0.6231 702  GLY A C   
5341  O O   . GLY A 702  ? 2.3134 2.1785 2.2992 -0.2554 -0.0210 -0.6366 702  GLY A O   
5342  N N   . ALA A 703  ? 2.3035 2.1458 2.2969 -0.2842 0.0361  -0.6222 703  ALA A N   
5343  C CA  . ALA A 703  ? 2.2572 2.1612 2.2284 -0.3004 0.0458  -0.6377 703  ALA A CA  
5344  C C   . ALA A 703  ? 2.1892 2.1224 2.1991 -0.2812 0.0152  -0.6190 703  ALA A C   
5345  O O   . ALA A 703  ? 2.1785 2.1659 2.1764 -0.2807 0.0033  -0.6296 703  ALA A O   
5346  C CB  . ALA A 703  ? 2.2848 2.1898 2.2319 -0.3310 0.0936  -0.6443 703  ALA A CB  
5347  N N   . CYS A 704  ? 2.1259 2.0220 2.1827 -0.2641 0.0017  -0.5910 704  CYS A N   
5348  C CA  . CYS A 704  ? 2.0805 1.9944 2.1746 -0.2524 -0.0134 -0.5699 704  CYS A CA  
5349  C C   . CYS A 704  ? 2.0645 2.0424 2.1367 -0.2550 -0.0206 -0.5828 704  CYS A C   
5350  O O   . CYS A 704  ? 2.0686 2.0756 2.1175 -0.2764 0.0081  -0.5913 704  CYS A O   
5351  C CB  . CYS A 704  ? 2.0507 1.9347 2.1944 -0.2229 -0.0531 -0.5468 704  CYS A CB  
5352  S SG  . CYS A 704  ? 1.7284 1.6034 1.9275 -0.2140 -0.0557 -0.5139 704  CYS A SG  
5353  N N   . VAL A 705  ? 2.0575 2.0579 2.1346 -0.2337 -0.0579 -0.5851 705  VAL A N   
5354  C CA  . VAL A 705  ? 2.0516 2.1138 2.1122 -0.2312 -0.0675 -0.5941 705  VAL A CA  
5355  C C   . VAL A 705  ? 2.0705 2.1496 2.1335 -0.2059 -0.1072 -0.5978 705  VAL A C   
5356  O O   . VAL A 705  ? 2.0897 2.1671 2.1821 -0.1831 -0.1345 -0.5789 705  VAL A O   
5357  C CB  . VAL A 705  ? 2.0104 2.0811 2.0996 -0.2232 -0.0707 -0.5708 705  VAL A CB  
5358  C CG1 . VAL A 705  ? 2.0262 2.1174 2.0943 -0.2498 -0.0320 -0.5755 705  VAL A CG1 
5359  C CG2 . VAL A 705  ? 1.9925 2.0075 2.1325 -0.2065 -0.0849 -0.5421 705  VAL A CG2 
5360  N N   . ASN A 706  ? 2.0922 2.1869 2.1233 -0.2094 -0.1099 -0.6217 706  ASN A N   
5361  C CA  . ASN A 706  ? 2.1024 2.2083 2.1365 -0.1831 -0.1479 -0.6237 706  ASN A CA  
5362  C C   . ASN A 706  ? 2.0687 2.2347 2.0658 -0.1869 -0.1485 -0.6500 706  ASN A C   
5363  O O   . ASN A 706  ? 2.0792 2.2466 2.0473 -0.1985 -0.1380 -0.6722 706  ASN A O   
5364  C CB  . ASN A 706  ? 2.1545 2.2027 2.2010 -0.1692 -0.1672 -0.6189 706  ASN A CB  
5365  C CG  . ASN A 706  ? 2.1813 2.2174 2.2544 -0.1376 -0.2096 -0.6036 706  ASN A CG  
5366  O OD1 . ASN A 706  ? 2.1812 2.2572 2.2537 -0.1243 -0.2254 -0.6023 706  ASN A OD1 
5367  N ND2 . ASN A 706  ? 2.2059 2.1861 2.3017 -0.1250 -0.2283 -0.5917 706  ASN A ND2 
5368  N N   . ASN A 707  ? 2.0360 2.2518 2.0352 -0.1758 -0.1610 -0.6465 707  ASN A N   
5369  C CA  . ASN A 707  ? 2.0071 2.2914 1.9749 -0.1798 -0.1599 -0.6702 707  ASN A CA  
5370  C C   . ASN A 707  ? 1.9499 2.2505 1.9168 -0.1508 -0.1945 -0.6735 707  ASN A C   
5371  O O   . ASN A 707  ? 1.9018 2.2621 1.8457 -0.1505 -0.1961 -0.6925 707  ASN A O   
5372  C CB  . ASN A 707  ? 2.0275 2.3680 1.9884 -0.1898 -0.1461 -0.6696 707  ASN A CB  
5373  C CG  . ASN A 707  ? 2.0302 2.3485 2.0232 -0.1747 -0.1556 -0.6389 707  ASN A CG  
5374  O OD1 . ASN A 707  ? 2.0308 2.2902 2.0548 -0.1617 -0.1678 -0.6180 707  ASN A OD1 
5375  N ND2 . ASN A 707  ? 2.0249 2.3917 2.0099 -0.1768 -0.1495 -0.6368 707  ASN A ND2 
5376  N N   . ASP A 708  ? 1.9354 2.1837 1.9270 -0.1266 -0.2220 -0.6556 708  ASP A N   
5377  C CA  . ASP A 708  ? 1.8881 2.1446 1.8768 -0.0984 -0.2543 -0.6578 708  ASP A CA  
5378  C C   . ASP A 708  ? 1.8919 2.1238 1.8608 -0.0998 -0.2571 -0.6758 708  ASP A C   
5379  O O   . ASP A 708  ? 1.8700 2.1110 1.8293 -0.0794 -0.2796 -0.6825 708  ASP A O   
5380  C CB  . ASP A 708  ? 1.8186 2.0372 1.8410 -0.0700 -0.2846 -0.6299 708  ASP A CB  
5381  C CG  . ASP A 708  ? 1.7085 1.9705 1.7366 -0.0559 -0.2922 -0.6185 708  ASP A CG  
5382  O OD1 . ASP A 708  ? 1.6440 1.9707 1.6483 -0.0646 -0.2790 -0.6341 708  ASP A OD1 
5383  O OD2 . ASP A 708  ? 1.6703 1.9023 1.7255 -0.0363 -0.3112 -0.5945 708  ASP A OD2 
5384  N N   . GLU A 709  ? 1.9079 2.1067 1.8683 -0.1233 -0.2328 -0.6834 709  GLU A N   
5385  C CA  . GLU A 709  ? 1.9476 2.1238 1.8822 -0.1284 -0.2291 -0.7026 709  GLU A CA  
5386  C C   . GLU A 709  ? 1.9769 2.1528 1.8865 -0.1632 -0.1884 -0.7206 709  GLU A C   
5387  O O   . GLU A 709  ? 2.0204 2.1898 1.9395 -0.1810 -0.1660 -0.7123 709  GLU A O   
5388  C CB  . GLU A 709  ? 1.9850 2.0888 1.9365 -0.1085 -0.2548 -0.6877 709  GLU A CB  
5389  C CG  . GLU A 709  ? 2.0005 2.0552 1.9915 -0.1048 -0.2606 -0.6597 709  GLU A CG  
5390  C CD  . GLU A 709  ? 2.0077 2.0043 2.0193 -0.0799 -0.2956 -0.6447 709  GLU A CD  
5391  O OE1 . GLU A 709  ? 2.0095 1.9911 1.9982 -0.0703 -0.3089 -0.6578 709  GLU A OE1 
5392  O OE2 . GLU A 709  ? 2.0015 1.9677 2.0514 -0.0709 -0.3091 -0.6206 709  GLU A OE2 
5393  N N   . THR A 710  ? 1.9692 2.1505 1.8453 -0.1726 -0.1777 -0.7453 710  THR A N   
5394  C CA  . THR A 710  ? 2.0052 2.1836 1.8512 -0.2062 -0.1376 -0.7657 710  THR A CA  
5395  C C   . THR A 710  ? 2.0714 2.1796 1.9263 -0.2149 -0.1226 -0.7515 710  THR A C   
5396  O O   . THR A 710  ? 2.0710 2.1334 1.9567 -0.1945 -0.1457 -0.7273 710  THR A O   
5397  C CB  . THR A 710  ? 2.2787 2.4599 2.0882 -0.2106 -0.1318 -0.7924 710  THR A CB  
5398  O OG1 . THR A 710  ? 2.3000 2.4059 2.1050 -0.2006 -0.1393 -0.7862 710  THR A OG1 
5399  C CG2 . THR A 710  ? 2.2625 2.4948 2.0706 -0.1891 -0.1583 -0.8003 710  THR A CG2 
5400  N N   . CYS A 711  ? 2.1337 2.2329 1.9620 -0.2452 -0.0834 -0.7665 711  CYS A N   
5401  C CA  . CYS A 711  ? 2.2011 2.2305 2.0341 -0.2504 -0.0687 -0.7539 711  CYS A CA  
5402  C C   . CYS A 711  ? 2.2248 2.1984 2.0510 -0.2311 -0.0886 -0.7524 711  CYS A C   
5403  O O   . CYS A 711  ? 2.2538 2.1774 2.1080 -0.2122 -0.1091 -0.7297 711  CYS A O   
5404  C CB  . CYS A 711  ? 2.2460 2.2720 2.0475 -0.2863 -0.0202 -0.7703 711  CYS A CB  
5405  S SG  . CYS A 711  ? 2.2302 2.2542 2.0561 -0.3013 0.0024  -0.7508 711  CYS A SG  
5406  N N   . GLU A 712  ? 2.2230 2.2065 2.0127 -0.2354 -0.0837 -0.7767 712  GLU A N   
5407  C CA  . GLU A 712  ? 2.2433 2.1710 2.0197 -0.2178 -0.1005 -0.7769 712  GLU A CA  
5408  C C   . GLU A 712  ? 2.1708 2.0923 1.9721 -0.1827 -0.1491 -0.7626 712  GLU A C   
5409  O O   . GLU A 712  ? 2.1668 2.0377 1.9603 -0.1657 -0.1677 -0.7596 712  GLU A O   
5410  C CB  . GLU A 712  ? 2.3456 2.2765 2.0713 -0.2350 -0.0752 -0.8074 712  GLU A CB  
5411  C CG  . GLU A 712  ? 2.4093 2.4121 2.1210 -0.2382 -0.0784 -0.8294 712  GLU A CG  
5412  C CD  . GLU A 712  ? 2.4917 2.4950 2.1554 -0.2572 -0.0505 -0.8598 712  GLU A CD  
5413  O OE1 . GLU A 712  ? 2.5389 2.5145 2.1766 -0.2833 -0.0126 -0.8695 712  GLU A OE1 
5414  O OE2 . GLU A 712  ? 2.5043 2.5339 2.1552 -0.2460 -0.0651 -0.8737 712  GLU A OE2 
5415  N N   . GLN A 713  ? 2.1136 2.0833 1.9421 -0.1715 -0.1692 -0.7537 713  GLN A N   
5416  C CA  . GLN A 713  ? 2.0705 2.0271 1.9258 -0.1388 -0.2135 -0.7364 713  GLN A CA  
5417  C C   . GLN A 713  ? 2.0301 1.9337 1.9228 -0.1294 -0.2266 -0.7086 713  GLN A C   
5418  O O   . GLN A 713  ? 2.0476 1.9047 1.9528 -0.1080 -0.2563 -0.6967 713  GLN A O   
5419  C CB  . GLN A 713  ? 2.0459 2.0669 1.9172 -0.1288 -0.2287 -0.7339 713  GLN A CB  
5420  C CG  . GLN A 713  ? 2.0421 2.1104 1.8846 -0.1244 -0.2322 -0.7569 713  GLN A CG  
5421  C CD  . GLN A 713  ? 2.0124 2.1555 1.8652 -0.1200 -0.2375 -0.7578 713  GLN A CD  
5422  O OE1 . GLN A 713  ? 1.9989 2.1607 1.8754 -0.1242 -0.2338 -0.7434 713  GLN A OE1 
5423  N NE2 . GLN A 713  ? 2.0026 2.1889 1.8363 -0.1108 -0.2452 -0.7749 713  GLN A NE2 
5424  N N   . ARG A 714  ? 1.9647 1.8764 1.8752 -0.1464 -0.2034 -0.6990 714  ARG A N   
5425  C CA  . ARG A 714  ? 1.9307 1.7960 1.8787 -0.1410 -0.2093 -0.6734 714  ARG A CA  
5426  C C   . ARG A 714  ? 1.9018 1.7044 1.8351 -0.1432 -0.2005 -0.6742 714  ARG A C   
5427  O O   . ARG A 714  ? 1.8863 1.6425 1.8452 -0.1257 -0.2249 -0.6564 714  ARG A O   
5428  C CB  . ARG A 714  ? 1.9391 1.8291 1.9048 -0.1601 -0.1816 -0.6646 714  ARG A CB  
5429  C CG  . ARG A 714  ? 1.9440 1.8877 1.9297 -0.1537 -0.1939 -0.6575 714  ARG A CG  
5430  C CD  . ARG A 714  ? 1.9760 1.9566 1.9571 -0.1788 -0.1587 -0.6605 714  ARG A CD  
5431  N NE  . ARG A 714  ? 2.0271 1.9698 2.0359 -0.1861 -0.1431 -0.6404 714  ARG A NE  
5432  C CZ  . ARG A 714  ? 2.0695 2.0281 2.0754 -0.2085 -0.1094 -0.6399 714  ARG A CZ  
5433  N NH1 . ARG A 714  ? 2.0687 2.0822 2.0447 -0.2276 -0.0885 -0.6590 714  ARG A NH1 
5434  N NH2 . ARG A 714  ? 2.0909 2.0110 2.1241 -0.2121 -0.0963 -0.6202 714  ARG A NH2 
5435  N N   . ALA A 715  ? 1.8957 1.6972 1.7868 -0.1648 -0.1656 -0.6953 715  ALA A N   
5436  C CA  . ALA A 715  ? 1.8911 1.6318 1.7616 -0.1673 -0.1523 -0.6967 715  ALA A CA  
5437  C C   . ALA A 715  ? 1.8781 1.5804 1.7428 -0.1418 -0.1883 -0.6953 715  ALA A C   
5438  O O   . ALA A 715  ? 1.9134 1.5594 1.7832 -0.1312 -0.1971 -0.6838 715  ALA A O   
5439  C CB  . ALA A 715  ? 1.8596 1.6072 1.6791 -0.1945 -0.1090 -0.7228 715  ALA A CB  
5440  N N   . ALA A 716  ? 1.8848 1.6181 1.7375 -0.1312 -0.2093 -0.7070 716  ALA A N   
5441  C CA  . ALA A 716  ? 1.9240 1.6215 1.7684 -0.1066 -0.2443 -0.7064 716  ALA A CA  
5442  C C   . ALA A 716  ? 1.9291 1.5850 1.8181 -0.0863 -0.2775 -0.6790 716  ALA A C   
5443  O O   . ALA A 716  ? 1.9531 1.5538 1.8360 -0.0755 -0.2899 -0.6736 716  ALA A O   
5444  C CB  . ALA A 716  ? 1.9134 1.6554 1.7500 -0.0951 -0.2649 -0.7175 716  ALA A CB  
5445  N N   . ARG A 717  ? 1.9399 1.6233 1.8735 -0.0818 -0.2909 -0.6618 717  ARG A N   
5446  C CA  . ARG A 717  ? 1.9627 1.6152 1.9439 -0.0635 -0.3242 -0.6364 717  ARG A CA  
5447  C C   . ARG A 717  ? 1.9661 1.5760 1.9666 -0.0688 -0.3116 -0.6219 717  ARG A C   
5448  O O   . ARG A 717  ? 1.9538 1.5381 1.9971 -0.0558 -0.3364 -0.6008 717  ARG A O   
5449  C CB  . ARG A 717  ? 1.9768 1.6706 1.9981 -0.0611 -0.3333 -0.6224 717  ARG A CB  
5450  C CG  . ARG A 717  ? 2.0070 1.6812 2.0678 -0.0380 -0.3764 -0.6032 717  ARG A CG  
5451  C CD  . ARG A 717  ? 1.9990 1.7157 2.0902 -0.0365 -0.3801 -0.5918 717  ARG A CD  
5452  N NE  . ARG A 717  ? 1.9767 1.7492 2.0370 -0.0438 -0.3632 -0.6093 717  ARG A NE  
5453  C CZ  . ARG A 717  ? 1.9383 1.7513 1.9936 -0.0638 -0.3297 -0.6140 717  ARG A CZ  
5454  N NH1 . ARG A 717  ? 1.9207 1.7220 1.9983 -0.0784 -0.3074 -0.6022 717  ARG A NH1 
5455  N NH2 . ARG A 717  ? 1.9292 1.7955 1.9571 -0.0690 -0.3185 -0.6309 717  ARG A NH2 
5456  N N   . ILE A 718  ? 2.0033 1.6065 1.9729 -0.0881 -0.2721 -0.6332 718  ILE A N   
5457  C CA  . ILE A 718  ? 2.0502 1.6137 2.0342 -0.0930 -0.2547 -0.6198 718  ILE A CA  
5458  C C   . ILE A 718  ? 2.1410 1.6471 2.1120 -0.0762 -0.2751 -0.6174 718  ILE A C   
5459  O O   . ILE A 718  ? 2.1386 1.6295 2.0620 -0.0736 -0.2753 -0.6357 718  ILE A O   
5460  C CB  . ILE A 718  ? 2.0247 1.5947 1.9750 -0.1194 -0.2030 -0.6330 718  ILE A CB  
5461  C CG1 . ILE A 718  ? 2.0181 1.6356 1.9915 -0.1365 -0.1813 -0.6284 718  ILE A CG1 
5462  C CG2 . ILE A 718  ? 2.0326 1.5488 1.9828 -0.1195 -0.1861 -0.6225 718  ILE A CG2 
5463  C CD1 . ILE A 718  ? 2.0426 1.6629 1.9856 -0.1637 -0.1305 -0.6399 718  ILE A CD1 
5464  N N   . SER A 719  ? 2.2161 1.6909 2.2296 -0.0644 -0.2922 -0.5948 719  SER A N   
5465  C CA  . SER A 719  ? 2.2912 1.7117 2.2943 -0.0479 -0.3118 -0.5907 719  SER A CA  
5466  C C   . SER A 719  ? 2.4175 1.8050 2.4192 -0.0542 -0.2816 -0.5824 719  SER A C   
5467  O O   . SER A 719  ? 2.4716 1.8202 2.4295 -0.0518 -0.2700 -0.5916 719  SER A O   
5468  C CB  . SER A 719  ? 2.2273 1.6355 2.2796 -0.0267 -0.3605 -0.5720 719  SER A CB  
5469  O OG  . SER A 719  ? 2.2363 1.5955 2.2685 -0.0101 -0.3833 -0.5726 719  SER A OG  
5470  N N   . LEU A 720  ? 2.4857 1.8878 2.5331 -0.0619 -0.2668 -0.5649 720  LEU A N   
5471  C CA  . LEU A 720  ? 2.6035 1.9738 2.6643 -0.0634 -0.2431 -0.5507 720  LEU A CA  
5472  C C   . LEU A 720  ? 2.7207 2.0508 2.7217 -0.0681 -0.2113 -0.5639 720  LEU A C   
5473  O O   . LEU A 720  ? 2.7308 2.0205 2.7381 -0.0582 -0.2070 -0.5511 720  LEU A O   
5474  C CB  . LEU A 720  ? 2.6359 2.0361 2.7319 -0.0804 -0.2123 -0.5393 720  LEU A CB  
5475  C CG  . LEU A 720  ? 2.6868 2.1169 2.8495 -0.0746 -0.2391 -0.5202 720  LEU A CG  
5476  C CD1 . LEU A 720  ? 2.6955 2.1476 2.8865 -0.0914 -0.2039 -0.5089 720  LEU A CD1 
5477  C CD2 . LEU A 720  ? 2.7285 2.1305 2.9386 -0.0517 -0.2802 -0.5003 720  LEU A CD2 
5478  N N   . GLY A 721  ? 2.8222 2.1632 2.7656 -0.0829 -0.1882 -0.5892 721  GLY A N   
5479  C CA  . GLY A 721  ? 2.9432 2.2432 2.8255 -0.0881 -0.1576 -0.6035 721  GLY A CA  
5480  C C   . GLY A 721  ? 2.9913 2.3150 2.8239 -0.1163 -0.1124 -0.6283 721  GLY A C   
5481  O O   . GLY A 721  ? 2.9967 2.3487 2.8420 -0.1365 -0.0813 -0.6272 721  GLY A O   
5482  N N   . PRO A 722  ? 3.0086 2.3209 2.7840 -0.1185 -0.1082 -0.6514 722  PRO A N   
5483  C CA  . PRO A 722  ? 2.9877 2.3200 2.7114 -0.1465 -0.0643 -0.6781 722  PRO A CA  
5484  C C   . PRO A 722  ? 2.9626 2.2788 2.6721 -0.1681 -0.0121 -0.6770 722  PRO A C   
5485  O O   . PRO A 722  ? 2.9475 2.2815 2.6184 -0.1954 0.0284  -0.6981 722  PRO A O   
5486  C CB  . PRO A 722  ? 3.0331 2.3271 2.6988 -0.1385 -0.0675 -0.6957 722  PRO A CB  
5487  C CG  . PRO A 722  ? 3.0198 2.3060 2.7130 -0.1084 -0.1251 -0.6840 722  PRO A CG  
5488  C CD  . PRO A 722  ? 3.0125 2.2965 2.7716 -0.0947 -0.1479 -0.6543 722  PRO A CD  
5489  N N   . ARG A 723  ? 2.9344 2.2173 2.6762 -0.1555 -0.0135 -0.6525 723  ARG A N   
5490  C CA  . ARG A 723  ? 2.9125 2.1766 2.6487 -0.1716 0.0331  -0.6465 723  ARG A CA  
5491  C C   . ARG A 723  ? 2.8578 2.1775 2.6212 -0.1950 0.0524  -0.6471 723  ARG A C   
5492  O O   . ARG A 723  ? 2.8820 2.2007 2.6195 -0.2201 0.1002  -0.6557 723  ARG A O   
5493  C CB  . ARG A 723  ? 2.8813 2.1037 2.6565 -0.1476 0.0189  -0.6172 723  ARG A CB  
5494  C CG  . ARG A 723  ? 2.8407 2.0282 2.6187 -0.1160 -0.0268 -0.6093 723  ARG A CG  
5495  C CD  . ARG A 723  ? 2.8024 1.9554 2.6232 -0.0935 -0.0399 -0.5802 723  ARG A CD  
5496  N NE  . ARG A 723  ? 2.7890 1.9022 2.6043 -0.0643 -0.0788 -0.5735 723  ARG A NE  
5497  C CZ  . ARG A 723  ? 2.7546 1.8794 2.6202 -0.0431 -0.1320 -0.5590 723  ARG A CZ  
5498  N NH1 . ARG A 723  ? 2.7079 1.8812 2.6326 -0.0475 -0.1512 -0.5495 723  ARG A NH1 
5499  N NH2 . ARG A 723  ? 2.7749 1.8611 2.6297 -0.0180 -0.1657 -0.5544 723  ARG A NH2 
5500  N N   . CYS A 724  ? 2.7825 2.1478 2.5957 -0.1864 0.0152  -0.6378 724  CYS A N   
5501  C CA  . CYS A 724  ? 2.7200 2.1369 2.5627 -0.2042 0.0278  -0.6350 724  CYS A CA  
5502  C C   . CYS A 724  ? 2.6913 2.1685 2.5220 -0.2155 0.0173  -0.6553 724  CYS A C   
5503  O O   . CYS A 724  ? 2.6513 2.1750 2.4964 -0.2319 0.0297  -0.6570 724  CYS A O   
5504  C CB  . CYS A 724  ? 2.6758 2.0976 2.5900 -0.1865 0.0000  -0.6045 724  CYS A CB  
5505  S SG  . CYS A 724  ? 2.2336 1.6868 2.1948 -0.1619 -0.0645 -0.5953 724  CYS A SG  
5506  N N   . ILE A 725  ? 2.7094 2.1860 2.5128 -0.2059 -0.0051 -0.6705 725  ILE A N   
5507  C CA  . ILE A 725  ? 2.6835 2.2177 2.4744 -0.2147 -0.0141 -0.6902 725  ILE A CA  
5508  C C   . ILE A 725  ? 2.7016 2.2707 2.4588 -0.2491 0.0323  -0.7116 725  ILE A C   
5509  O O   . ILE A 725  ? 2.6838 2.3128 2.4517 -0.2596 0.0298  -0.7187 725  ILE A O   
5510  C CB  . ILE A 725  ? 2.6759 2.1975 2.4316 -0.2027 -0.0345 -0.7067 725  ILE A CB  
5511  C CG1 . ILE A 725  ? 2.6574 2.1552 2.4483 -0.1693 -0.0866 -0.6872 725  ILE A CG1 
5512  C CG2 . ILE A 725  ? 2.6505 2.2342 2.3869 -0.2157 -0.0334 -0.7303 725  ILE A CG2 
5513  C CD1 . ILE A 725  ? 2.6686 2.1508 2.4258 -0.1547 -0.1103 -0.7017 725  ILE A CD1 
5514  N N   . LYS A 726  ? 2.7419 2.2724 2.4564 -0.2665 0.0746  -0.7221 726  LYS A N   
5515  C CA  . LYS A 726  ? 2.7577 2.3135 2.4374 -0.3024 0.1230  -0.7429 726  LYS A CA  
5516  C C   . LYS A 726  ? 2.6610 2.2412 2.3773 -0.3125 0.1351  -0.7271 726  LYS A C   
5517  O O   . LYS A 726  ? 2.6071 2.2436 2.3224 -0.3325 0.1461  -0.7388 726  LYS A O   
5518  C CB  . LYS A 726  ? 2.9035 2.4008 2.5307 -0.3171 0.1674  -0.7539 726  LYS A CB  
5519  C CG  . LYS A 726  ? 3.0234 2.5155 2.5929 -0.3278 0.1805  -0.7836 726  LYS A CG  
5520  C CD  . LYS A 726  ? 3.1414 2.5897 2.6547 -0.3544 0.2376  -0.7992 726  LYS A CD  
5521  C CE  . LYS A 726  ? 3.2102 2.6447 2.6654 -0.3639 0.2521  -0.8276 726  LYS A CE  
5522  N NZ  . LYS A 726  ? 3.2728 2.6596 2.6703 -0.3905 0.3099  -0.8431 726  LYS A NZ  
5523  N N   . ALA A 727  ? 2.6245 2.1625 2.3735 -0.2978 0.1327  -0.7004 727  ALA A N   
5524  C CA  . ALA A 727  ? 2.5771 2.1311 2.3637 -0.3046 0.1441  -0.6824 727  ALA A CA  
5525  C C   . ALA A 727  ? 2.4603 2.0780 2.2846 -0.2995 0.1124  -0.6781 727  ALA A C   
5526  O O   . ALA A 727  ? 2.4339 2.0821 2.2749 -0.3130 0.1270  -0.6727 727  ALA A O   
5527  C CB  . ALA A 727  ? 2.5948 2.0980 2.4203 -0.2827 0.1357  -0.6524 727  ALA A CB  
5528  N N   . PHE A 728  ? 2.3958 2.0302 2.2300 -0.2791 0.0700  -0.6804 728  PHE A N   
5529  C CA  . PHE A 728  ? 2.2955 1.9858 2.1621 -0.2700 0.0372  -0.6760 728  PHE A CA  
5530  C C   . PHE A 728  ? 2.3210 2.0731 2.1538 -0.2913 0.0502  -0.7035 728  PHE A C   
5531  O O   . PHE A 728  ? 2.3268 2.1253 2.1711 -0.3034 0.0579  -0.7030 728  PHE A O   
5532  C CB  . PHE A 728  ? 2.1663 1.8439 2.0588 -0.2375 -0.0140 -0.6651 728  PHE A CB  
5533  C CG  . PHE A 728  ? 2.0429 1.7681 1.9709 -0.2243 -0.0486 -0.6567 728  PHE A CG  
5534  C CD1 . PHE A 728  ? 1.9946 1.7319 1.9677 -0.2214 -0.0527 -0.6347 728  PHE A CD1 
5535  C CD2 . PHE A 728  ? 2.0005 1.7557 1.9153 -0.2136 -0.0759 -0.6703 728  PHE A CD2 
5536  C CE1 . PHE A 728  ? 1.9544 1.7310 1.9567 -0.2083 -0.0831 -0.6265 728  PHE A CE1 
5537  C CE2 . PHE A 728  ? 1.9553 1.7508 1.8999 -0.1996 -0.1065 -0.6618 728  PHE A CE2 
5538  C CZ  . PHE A 728  ? 1.9394 1.7445 1.9267 -0.1970 -0.1099 -0.6399 728  PHE A CZ  
5539  N N   . THR A 729  ? 2.3547 2.1079 2.1457 -0.2957 0.0527  -0.7274 729  THR A N   
5540  C CA  . THR A 729  ? 2.3422 2.1566 2.1019 -0.3156 0.0642  -0.7555 729  THR A CA  
5541  C C   . THR A 729  ? 2.3727 2.2049 2.1053 -0.3523 0.1132  -0.7700 729  THR A C   
5542  O O   . THR A 729  ? 2.3510 2.2459 2.0789 -0.3687 0.1200  -0.7830 729  THR A O   
5543  C CB  . THR A 729  ? 2.7028 2.5098 2.4228 -0.3132 0.0598  -0.7787 729  THR A CB  
5544  O OG1 . THR A 729  ? 2.7267 2.4607 2.4393 -0.2974 0.0552  -0.7690 729  THR A OG1 
5545  C CG2 . THR A 729  ? 2.6766 2.5275 2.4121 -0.2915 0.0175  -0.7812 729  THR A CG2 
5546  N N   . GLU A 730  ? 2.4205 2.1967 2.1342 -0.3645 0.1474  -0.7674 730  GLU A N   
5547  C CA  . GLU A 730  ? 2.4689 2.2522 2.1554 -0.3995 0.1960  -0.7795 730  GLU A CA  
5548  C C   . GLU A 730  ? 2.4601 2.2831 2.1809 -0.4029 0.1928  -0.7650 730  GLU A C   
5549  O O   . GLU A 730  ? 2.4415 2.3282 2.1546 -0.4191 0.1958  -0.7799 730  GLU A O   
5550  C CB  . GLU A 730  ? 2.5178 2.2254 2.1865 -0.4048 0.2297  -0.7713 730  GLU A CB  
5551  C CG  . GLU A 730  ? 2.5436 2.2106 2.1603 -0.4128 0.2507  -0.7921 730  GLU A CG  
5552  C CD  . GLU A 730  ? 2.5490 2.2239 2.1129 -0.4543 0.3038  -0.8204 730  GLU A CD  
5553  O OE1 . GLU A 730  ? 2.5375 2.2065 2.1000 -0.4735 0.3356  -0.8155 730  GLU A OE1 
5554  O OE2 . GLU A 730  ? 2.5581 2.2439 2.0815 -0.4682 0.3145  -0.8478 730  GLU A OE2 
5555  N N   . CYS A 731  ? 2.4632 2.2487 2.2225 -0.3864 0.1859  -0.7352 731  CYS A N   
5556  C CA  . CYS A 731  ? 2.4739 2.2839 2.2641 -0.3901 0.1890  -0.7188 731  CYS A CA  
5557  C C   . CYS A 731  ? 2.4681 2.3451 2.2812 -0.3793 0.1538  -0.7188 731  CYS A C   
5558  O O   . CYS A 731  ? 2.4644 2.3807 2.2843 -0.3908 0.1621  -0.7167 731  CYS A O   
5559  C CB  . CYS A 731  ? 2.4649 2.2232 2.2999 -0.3688 0.1810  -0.6853 731  CYS A CB  
5560  S SG  . CYS A 731  ? 3.1074 2.7848 2.9190 -0.3768 0.2229  -0.6807 731  CYS A SG  
5561  N N   . CYS A 732  ? 2.4802 2.3683 2.3021 -0.3563 0.1152  -0.7209 732  CYS A N   
5562  C CA  . CYS A 732  ? 2.4690 2.4164 2.3118 -0.3421 0.0807  -0.7194 732  CYS A CA  
5563  C C   . CYS A 732  ? 2.4712 2.4858 2.2791 -0.3671 0.0977  -0.7477 732  CYS A C   
5564  O O   . CYS A 732  ? 2.4681 2.5320 2.2868 -0.3707 0.0942  -0.7447 732  CYS A O   
5565  C CB  . CYS A 732  ? 2.4532 2.3924 2.3100 -0.3117 0.0373  -0.7159 732  CYS A CB  
5566  S SG  . CYS A 732  ? 2.3313 2.3377 2.2121 -0.2914 -0.0034 -0.7122 732  CYS A SG  
5567  N N   . VAL A 733  ? 2.4888 2.5060 2.2545 -0.3844 0.1162  -0.7752 733  VAL A N   
5568  C CA  . VAL A 733  ? 2.4654 2.5490 2.1982 -0.4111 0.1341  -0.8048 733  VAL A CA  
5569  C C   . VAL A 733  ? 2.4491 2.5472 2.1722 -0.4400 0.1694  -0.8062 733  VAL A C   
5570  O O   . VAL A 733  ? 2.4134 2.5740 2.1390 -0.4475 0.1656  -0.8112 733  VAL A O   
5571  C CB  . VAL A 733  ? 2.4766 2.5522 2.1643 -0.4292 0.1554  -0.8348 733  VAL A CB  
5572  C CG1 . VAL A 733  ? 2.4902 2.6306 2.1442 -0.4648 0.1832  -0.8659 733  VAL A CG1 
5573  C CG2 . VAL A 733  ? 2.4523 2.5295 2.1459 -0.4015 0.1187  -0.8372 733  VAL A CG2 
5574  N N   . VAL A 734  ? 2.4772 2.5152 2.1887 -0.4543 0.2030  -0.8004 734  VAL A N   
5575  C CA  . VAL A 734  ? 2.4964 2.5358 2.1973 -0.4808 0.2390  -0.7995 734  VAL A CA  
5576  C C   . VAL A 734  ? 2.4892 2.5702 2.2237 -0.4694 0.2185  -0.7810 734  VAL A C   
5577  O O   . VAL A 734  ? 2.5130 2.6421 2.2305 -0.4920 0.2350  -0.7930 734  VAL A O   
5578  C CB  . VAL A 734  ? 2.5138 2.4721 2.2148 -0.4830 0.2673  -0.7829 734  VAL A CB  
5579  C CG1 . VAL A 734  ? 2.5153 2.4710 2.2129 -0.5045 0.3003  -0.7758 734  VAL A CG1 
5580  C CG2 . VAL A 734  ? 2.5424 2.4594 2.1988 -0.4999 0.2968  -0.8040 734  VAL A CG2 
5581  N N   . ALA A 735  ? 2.4537 2.5157 2.2344 -0.4347 0.1827  -0.7523 735  ALA A N   
5582  C CA  . ALA A 735  ? 2.4285 2.5196 2.2423 -0.4213 0.1640  -0.7316 735  ALA A CA  
5583  C C   . ALA A 735  ? 2.4093 2.5726 2.2267 -0.4086 0.1308  -0.7402 735  ALA A C   
5584  O O   . ALA A 735  ? 2.3953 2.5920 2.2308 -0.3998 0.1176  -0.7274 735  ALA A O   
5585  C CB  . ALA A 735  ? 2.4117 2.4505 2.2747 -0.3915 0.1424  -0.6970 735  ALA A CB  
5586  N N   . SER A 736  ? 2.4083 2.5943 2.2076 -0.4062 0.1180  -0.7612 736  SER A N   
5587  C CA  . SER A 736  ? 2.3973 2.6520 2.2002 -0.3917 0.0869  -0.7695 736  SER A CA  
5588  C C   . SER A 736  ? 2.4010 2.7279 2.1699 -0.4209 0.1071  -0.7972 736  SER A C   
5589  O O   . SER A 736  ? 2.3904 2.7779 2.1665 -0.4128 0.0895  -0.7959 736  SER A O   
5590  C CB  . SER A 736  ? 2.3874 2.6343 2.1902 -0.3719 0.0609  -0.7773 736  SER A CB  
5591  O OG  . SER A 736  ? 2.3824 2.5723 2.2199 -0.3417 0.0345  -0.7506 736  SER A OG  
5592  N N   . GLN A 737  ? 2.4222 2.7425 2.1535 -0.4548 0.1441  -0.8225 737  GLN A N   
5593  C CA  . GLN A 737  ? 2.4131 2.7981 2.1102 -0.4886 0.1680  -0.8513 737  GLN A CA  
5594  C C   . GLN A 737  ? 2.4184 2.8094 2.1162 -0.5025 0.1859  -0.8398 737  GLN A C   
5595  O O   . GLN A 737  ? 2.3899 2.8475 2.0749 -0.5161 0.1877  -0.8520 737  GLN A O   
5596  C CB  . GLN A 737  ? 2.4296 2.7938 2.0853 -0.5231 0.2067  -0.8803 737  GLN A CB  
5597  C CG  . GLN A 737  ? 2.4366 2.7385 2.0925 -0.5081 0.2014  -0.8784 737  GLN A CG  
5598  C CD  . GLN A 737  ? 2.4243 2.7663 2.0764 -0.4954 0.1769  -0.8960 737  GLN A CD  
5599  O OE1 . GLN A 737  ? 2.4427 2.8247 2.0634 -0.5217 0.1962  -0.9274 737  GLN A OE1 
5600  N NE2 . GLN A 737  ? 2.3931 2.7222 2.0767 -0.4560 0.1359  -0.8763 737  GLN A NE2 
5601  N N   . LEU A 738  ? 2.4699 2.7909 2.1832 -0.4979 0.1984  -0.8156 738  LEU A N   
5602  C CA  . LEU A 738  ? 2.5244 2.8395 2.2384 -0.5101 0.2184  -0.8024 738  LEU A CA  
5603  C C   . LEU A 738  ? 2.5796 2.9428 2.3188 -0.4873 0.1872  -0.7854 738  LEU A C   
5604  O O   . LEU A 738  ? 2.6035 2.9949 2.3300 -0.5026 0.2016  -0.7859 738  LEU A O   
5605  C CB  . LEU A 738  ? 2.5122 2.7417 2.2446 -0.5041 0.2350  -0.7770 738  LEU A CB  
5606  C CG  . LEU A 738  ? 2.4934 2.7059 2.2203 -0.5219 0.2658  -0.7657 738  LEU A CG  
5607  C CD1 . LEU A 738  ? 2.5151 2.7108 2.1935 -0.5643 0.3163  -0.7902 738  LEU A CD1 
5608  C CD2 . LEU A 738  ? 2.4730 2.6196 2.2414 -0.4982 0.2612  -0.7298 738  LEU A CD2 
5609  N N   . ARG A 739  ? 2.6134 2.9831 2.3852 -0.4505 0.1453  -0.7702 739  ARG A N   
5610  C CA  . ARG A 739  ? 2.6816 3.0890 2.4760 -0.4265 0.1170  -0.7517 739  ARG A CA  
5611  C C   . ARG A 739  ? 2.6884 3.1858 2.4589 -0.4345 0.1088  -0.7746 739  ARG A C   
5612  O O   . ARG A 739  ? 2.6806 3.2179 2.4587 -0.4203 0.0919  -0.7635 739  ARG A O   
5613  C CB  . ARG A 739  ? 2.7439 3.1244 2.5805 -0.3846 0.0762  -0.7264 739  ARG A CB  
5614  C CG  . ARG A 739  ? 2.8170 3.2208 2.6530 -0.3679 0.0485  -0.7401 739  ARG A CG  
5615  C CD  . ARG A 739  ? 2.8892 3.2585 2.7654 -0.3282 0.0104  -0.7134 739  ARG A CD  
5616  N NE  . ARG A 739  ? 2.9542 3.3390 2.8285 -0.3108 -0.0159 -0.7254 739  ARG A NE  
5617  C CZ  . ARG A 739  ? 2.9888 3.3485 2.8912 -0.2771 -0.0511 -0.7080 739  ARG A CZ  
5618  N NH1 . ARG A 739  ? 2.9972 3.3167 2.9345 -0.2579 -0.0648 -0.6779 739  ARG A NH1 
5619  N NH2 . ARG A 739  ? 2.9963 3.3704 2.8915 -0.2634 -0.0716 -0.7212 739  ARG A NH2 
5620  N N   . ALA A 740  ? 2.6963 3.2256 2.4375 -0.4573 0.1216  -0.8066 740  ALA A N   
5621  C CA  . ALA A 740  ? 2.6987 3.3182 2.4170 -0.4696 0.1175  -0.8319 740  ALA A CA  
5622  C C   . ALA A 740  ? 2.7025 3.3465 2.3906 -0.5055 0.1504  -0.8439 740  ALA A C   
5623  O O   . ALA A 740  ? 2.7323 3.4534 2.4044 -0.5141 0.1453  -0.8591 740  ALA A O   
5624  C CB  . ALA A 740  ? 2.7002 3.3446 2.3999 -0.4827 0.1210  -0.8626 740  ALA A CB  
5625  N N   . ASN A 741  ? 2.6668 3.2447 2.3470 -0.5254 0.1839  -0.8364 741  ASN A N   
5626  C CA  . ASN A 741  ? 2.6375 3.2251 2.2824 -0.5649 0.2223  -0.8508 741  ASN A CA  
5627  C C   . ASN A 741  ? 2.7695 3.3295 2.4216 -0.5613 0.2315  -0.8248 741  ASN A C   
5628  O O   . ASN A 741  ? 2.7959 3.3893 2.4194 -0.5863 0.2507  -0.8358 741  ASN A O   
5629  C CB  . ASN A 741  ? 2.5045 3.0446 2.1206 -0.5999 0.2637  -0.8711 741  ASN A CB  
5630  C CG  . ASN A 741  ? 2.3869 2.9773 1.9782 -0.6204 0.2673  -0.9079 741  ASN A CG  
5631  O OD1 . ASN A 741  ? 2.3577 2.9116 1.9473 -0.6202 0.2723  -0.9158 741  ASN A OD1 
5632  N ND2 . ASN A 741  ? 2.3149 2.9917 1.8875 -0.6370 0.2636  -0.9304 741  ASN A ND2 
5633  N N   . ILE A 742  ? 2.8936 3.3928 2.5828 -0.5318 0.2187  -0.7913 742  ILE A N   
5634  C CA  . ILE A 742  ? 3.0124 3.4848 2.7129 -0.5251 0.2259  -0.7645 742  ILE A CA  
5635  C C   . ILE A 742  ? 3.0526 3.5916 2.7562 -0.5062 0.1968  -0.7584 742  ILE A C   
5636  O O   . ILE A 742  ? 3.0665 3.6041 2.7661 -0.5065 0.2046  -0.7436 742  ILE A O   
5637  C CB  . ILE A 742  ? 3.0374 3.4340 2.7830 -0.4958 0.2156  -0.7298 742  ILE A CB  
5638  C CG1 . ILE A 742  ? 3.0540 3.3901 2.8015 -0.5043 0.2331  -0.7349 742  ILE A CG1 
5639  C CG2 . ILE A 742  ? 3.0575 3.4186 2.8106 -0.4969 0.2343  -0.7053 742  ILE A CG2 
5640  C CD1 . ILE A 742  ? 3.0440 3.3124 2.8381 -0.4748 0.2190  -0.7030 742  ILE A CD1 
5641  N N   . SER A 743  ? 3.0690 3.6650 2.7779 -0.4888 0.1642  -0.7697 743  SER A N   
5642  C CA  . SER A 743  ? 3.0743 3.7340 2.7885 -0.4640 0.1319  -0.7628 743  SER A CA  
5643  C C   . SER A 743  ? 3.0576 3.7954 2.7601 -0.4628 0.1115  -0.7901 743  SER A C   
5644  O O   . SER A 743  ? 3.0364 3.7642 2.7484 -0.4578 0.1032  -0.7999 743  SER A O   
5645  C CB  . SER A 743  ? 3.0714 3.6925 2.8289 -0.4202 0.1009  -0.7271 743  SER A CB  
5646  O OG  . SER A 743  ? 3.0584 3.6435 2.8412 -0.4037 0.0850  -0.7244 743  SER A OG  
5647  N N   . LEU A 749  ? 2.8664 3.7889 2.6015 -0.2305 -0.0651 -0.6442 749  LEU A N   
5648  C CA  . LEU A 749  ? 2.8556 3.7099 2.6298 -0.2004 -0.0817 -0.6181 749  LEU A CA  
5649  C C   . LEU A 749  ? 2.8556 3.6867 2.6512 -0.2103 -0.0827 -0.6328 749  LEU A C   
5650  O O   . LEU A 749  ? 2.8562 3.7232 2.6352 -0.2397 -0.0694 -0.6626 749  LEU A O   
5651  C CB  . LEU A 749  ? 2.8473 3.6209 2.6363 -0.2023 -0.0630 -0.5897 749  LEU A CB  
5652  C CG  . LEU A 749  ? 2.8159 3.5279 2.6419 -0.1659 -0.0830 -0.5574 749  LEU A CG  
5653  C CD1 . LEU A 749  ? 2.8139 3.5648 2.6299 -0.1265 -0.1116 -0.5442 749  LEU A CD1 
5654  C CD2 . LEU A 749  ? 2.8217 3.4581 2.6640 -0.1744 -0.0595 -0.5329 749  LEU A CD2 
5655  N N   . GLY A 750  ? 2.8666 3.6355 2.6972 -0.1866 -0.0977 -0.6122 750  GLY A N   
5656  C CA  . GLY A 750  ? 2.8788 3.6215 2.7290 -0.1902 -0.1030 -0.6232 750  GLY A CA  
5657  C C   . GLY A 750  ? 2.9124 3.5644 2.7939 -0.1946 -0.0919 -0.6044 750  GLY A C   
5658  O O   . GLY A 750  ? 2.8940 3.5088 2.8007 -0.1811 -0.1074 -0.6004 750  GLY A O   
5659  N N   . ARG A 751  ? 2.9786 3.5960 2.8584 -0.2130 -0.0650 -0.5928 751  ARG A N   
5660  C CA  . ARG A 751  ? 3.0017 3.5364 2.9128 -0.2190 -0.0508 -0.5744 751  ARG A CA  
5661  C C   . ARG A 751  ? 3.1001 3.6128 3.0035 -0.2556 -0.0207 -0.5939 751  ARG A C   
5662  O O   . ARG A 751  ? 3.1211 3.6417 2.9992 -0.2856 0.0107  -0.6039 751  ARG A O   
5663  C CB  . ARG A 751  ? 2.9331 3.4335 2.8514 -0.2151 -0.0374 -0.5473 751  ARG A CB  
5664  C CG  . ARG A 751  ? 2.8411 3.3457 2.7696 -0.1769 -0.0646 -0.5232 751  ARG A CG  
5665  C CD  . ARG A 751  ? 2.7326 3.1982 2.6994 -0.1470 -0.0947 -0.5083 751  ARG A CD  
5666  N NE  . ARG A 751  ? 2.6520 3.1312 2.6196 -0.1104 -0.1217 -0.4910 751  ARG A NE  
5667  C CZ  . ARG A 751  ? 2.5726 3.0951 2.5303 -0.0870 -0.1500 -0.4998 751  ARG A CZ  
5668  N NH1 . ARG A 751  ? 2.5381 3.0959 2.4859 -0.0970 -0.1554 -0.5262 751  ARG A NH1 
5669  N NH2 . ARG A 751  ? 2.5510 3.0794 2.5075 -0.0528 -0.1715 -0.4820 751  ARG A NH2 
5670  N N   . LEU A 752  ? 3.1533 3.6361 3.0758 -0.2524 -0.0302 -0.5992 752  LEU A N   
5671  C CA  . LEU A 752  ? 3.2145 3.6603 3.1342 -0.2813 -0.0031 -0.6124 752  LEU A CA  
5672  C C   . LEU A 752  ? 3.2003 3.5795 3.1588 -0.2658 -0.0162 -0.5971 752  LEU A C   
5673  O O   . LEU A 752  ? 3.1965 3.5778 3.1702 -0.2408 -0.0480 -0.5952 752  LEU A O   
5674  C CB  . LEU A 752  ? 3.2723 3.7682 3.1576 -0.3040 0.0053  -0.6481 752  LEU A CB  
5675  C CG  . LEU A 752  ? 3.3294 3.7820 3.2085 -0.3315 0.0330  -0.6619 752  LEU A CG  
5676  C CD1 . LEU A 752  ? 3.3683 3.7997 3.2288 -0.3639 0.0749  -0.6631 752  LEU A CD1 
5677  C CD2 . LEU A 752  ? 3.3431 3.8376 3.1962 -0.3451 0.0326  -0.6947 752  LEU A CD2 
5678  N N   . HIS A 753  ? 3.1716 3.4926 3.1449 -0.2807 0.0087  -0.5867 753  HIS A N   
5679  C CA  . HIS A 753  ? 3.1169 3.3735 3.1297 -0.2669 -0.0019 -0.5698 753  HIS A CA  
5680  C C   . HIS A 753  ? 2.9967 3.2073 3.0075 -0.2931 0.0337  -0.5730 753  HIS A C   
5681  O O   . HIS A 753  ? 2.9807 3.1612 3.0020 -0.3023 0.0575  -0.5573 753  HIS A O   
5682  C CB  . HIS A 753  ? 3.1919 3.4165 3.2448 -0.2427 -0.0171 -0.5368 753  HIS A CB  
5683  C CG  . HIS A 753  ? 3.2682 3.5355 3.3092 -0.2303 -0.0266 -0.5296 753  HIS A CG  
5684  N ND1 . HIS A 753  ? 3.3166 3.5936 3.3411 -0.2449 -0.0005 -0.5242 753  HIS A ND1 
5685  C CD2 . HIS A 753  ? 3.2871 3.5873 3.3280 -0.2032 -0.0590 -0.5262 753  HIS A CD2 
5686  C CE1 . HIS A 753  ? 3.3320 3.6471 3.3463 -0.2269 -0.0173 -0.5177 753  HIS A CE1 
5687  N NE2 . HIS A 753  ? 3.3146 3.6444 3.3389 -0.2010 -0.0523 -0.5185 753  HIS A NE2 
5688  N N   . MET A 754  ? 2.9020 3.1044 2.8978 -0.3042 0.0388  -0.5928 754  MET A N   
5689  C CA  . MET A 754  ? 2.8148 2.9704 2.8052 -0.3267 0.0728  -0.5960 754  MET A CA  
5690  C C   . MET A 754  ? 2.7452 2.8380 2.7838 -0.3106 0.0681  -0.5661 754  MET A C   
5691  O O   . MET A 754  ? 2.7320 2.8198 2.8060 -0.2845 0.0383  -0.5457 754  MET A O   
5692  C CB  . MET A 754  ? 2.7781 2.9302 2.7472 -0.3345 0.0727  -0.6195 754  MET A CB  
5693  C CG  . MET A 754  ? 2.7489 2.9677 2.6839 -0.3394 0.0619  -0.6468 754  MET A CG  
5694  S SD  . MET A 754  ? 2.4432 2.6492 2.3683 -0.3340 0.0473  -0.6659 754  MET A SD  
5695  C CE  . MET A 754  ? 1.6698 1.7891 1.6106 -0.3400 0.0700  -0.6522 754  MET A CE  
5696  N N   . LYS A 755  ? 2.7075 2.7531 2.7477 -0.3262 0.0983  -0.5636 755  LYS A N   
5697  C CA  . LYS A 755  ? 2.6714 2.6578 2.7593 -0.3110 0.0933  -0.5377 755  LYS A CA  
5698  C C   . LYS A 755  ? 2.7209 2.6605 2.8000 -0.3300 0.1310  -0.5398 755  LYS A C   
5699  O O   . LYS A 755  ? 2.7154 2.6642 2.7501 -0.3572 0.1651  -0.5599 755  LYS A O   
5700  C CB  . LYS A 755  ? 2.6243 2.6016 2.7512 -0.2981 0.0888  -0.5089 755  LYS A CB  
5701  C CG  . LYS A 755  ? 2.5722 2.5626 2.7319 -0.2679 0.0444  -0.4942 755  LYS A CG  
5702  C CD  . LYS A 755  ? 2.5406 2.5156 2.7169 -0.2491 0.0100  -0.4972 755  LYS A CD  
5703  C CE  . LYS A 755  ? 2.5283 2.4456 2.7499 -0.2404 0.0074  -0.4779 755  LYS A CE  
5704  N NZ  . LYS A 755  ? 2.5073 2.4113 2.7424 -0.2209 -0.0297 -0.4810 755  LYS A NZ  
5705  N N   . THR A 756  ? 2.7760 2.6656 2.8980 -0.3147 0.1238  -0.5188 756  THR A N   
5706  C CA  . THR A 756  ? 2.8496 2.6891 2.9758 -0.3259 0.1583  -0.5117 756  THR A CA  
5707  C C   . THR A 756  ? 2.9216 2.7213 3.1114 -0.3021 0.1396  -0.4815 756  THR A C   
5708  O O   . THR A 756  ? 2.9349 2.7089 3.1442 -0.2868 0.1180  -0.4783 756  THR A O   
5709  C CB  . THR A 756  ? 2.8368 2.6581 2.9256 -0.3373 0.1718  -0.5337 756  THR A CB  
5710  O OG1 . THR A 756  ? 2.8354 2.6955 2.8671 -0.3626 0.1919  -0.5628 756  THR A OG1 
5711  C CG2 . THR A 756  ? 2.8458 2.6113 2.9397 -0.3451 0.2075  -0.5236 756  THR A CG2 
5712  N N   . LEU A 757  ? 2.9815 2.7773 3.2028 -0.2997 0.1481  -0.4597 757  LEU A N   
5713  C CA  . LEU A 757  ? 3.0512 2.8188 3.3379 -0.2778 0.1280  -0.4306 757  LEU A CA  
5714  C C   . LEU A 757  ? 3.1058 2.8253 3.4189 -0.2718 0.1345  -0.4211 757  LEU A C   
5715  O O   . LEU A 757  ? 3.1007 2.7981 3.3855 -0.2875 0.1699  -0.4294 757  LEU A O   
5716  C CB  . LEU A 757  ? 3.1012 2.8686 3.4110 -0.2811 0.1474  -0.4103 757  LEU A CB  
5717  C CG  . LEU A 757  ? 3.1446 2.8862 3.5247 -0.2621 0.1326  -0.3792 757  LEU A CG  
5718  C CD1 . LEU A 757  ? 3.1383 2.8986 3.5456 -0.2400 0.0844  -0.3732 757  LEU A CD1 
5719  C CD2 . LEU A 757  ? 3.1700 2.9030 3.5631 -0.2714 0.1664  -0.3616 757  LEU A CD2 
5720  N N   . LEU A 758  ? 3.1669 2.8706 3.5331 -0.2487 0.0993  -0.4040 758  LEU A N   
5721  C CA  . LEU A 758  ? 3.2283 2.8894 3.6332 -0.2387 0.1006  -0.3889 758  LEU A CA  
5722  C C   . LEU A 758  ? 3.3757 3.0344 3.8381 -0.2144 0.0540  -0.3723 758  LEU A C   
5723  O O   . LEU A 758  ? 3.3784 3.0416 3.8342 -0.2024 0.0187  -0.3824 758  LEU A O   
5724  C CB  . LEU A 758  ? 3.1154 2.7578 3.4825 -0.2418 0.1056  -0.4072 758  LEU A CB  
5725  C CG  . LEU A 758  ? 2.9986 2.5953 3.3826 -0.2400 0.1296  -0.3956 758  LEU A CG  
5726  C CD1 . LEU A 758  ? 2.9648 2.5414 3.3213 -0.2335 0.1173  -0.4102 758  LEU A CD1 
5727  C CD2 . LEU A 758  ? 2.9388 2.5180 3.3985 -0.2221 0.1150  -0.3654 758  LEU A CD2 
5728  N N   . PRO A 759  ? 3.5089 3.1596 4.0269 -0.2080 0.0546  -0.3473 759  PRO A N   
5729  C CA  . PRO A 759  ? 3.5914 3.2380 4.1689 -0.1874 0.0129  -0.3302 759  PRO A CA  
5730  C C   . PRO A 759  ? 3.6838 3.3066 4.2825 -0.1728 -0.0146 -0.3300 759  PRO A C   
5731  O O   . PRO A 759  ? 3.7126 3.3290 4.3620 -0.1568 -0.0497 -0.3167 759  PRO A O   
5732  C CB  . PRO A 759  ? 3.5668 3.2002 4.1981 -0.1884 0.0339  -0.3041 759  PRO A CB  
5733  C CG  . PRO A 759  ? 3.5547 3.1990 4.1442 -0.2084 0.0781  -0.3096 759  PRO A CG  
5734  C CD  . PRO A 759  ? 3.5429 3.1886 4.0675 -0.2217 0.0967  -0.3348 759  PRO A CD  
5735  N N   . VAL A 760  ? 3.3212 4.3450 3.6284 -0.0328 -0.3117 -0.0607 760  VAL A N   
5736  C CA  . VAL A 760  ? 3.3561 4.4563 3.6792 -0.0484 -0.2928 -0.0315 760  VAL A CA  
5737  C C   . VAL A 760  ? 3.2455 4.3029 3.5381 -0.0475 -0.2818 -0.0148 760  VAL A C   
5738  O O   . VAL A 760  ? 3.2402 4.3531 3.5347 -0.0545 -0.2654 0.0041  760  VAL A O   
5739  C CB  . VAL A 760  ? 3.5684 4.7590 3.8950 -0.0396 -0.2821 -0.0509 760  VAL A CB  
5740  C CG1 . VAL A 760  ? 3.6205 4.9044 3.9739 -0.0587 -0.2650 -0.0174 760  VAL A CG1 
5741  C CG2 . VAL A 760  ? 3.6242 4.8421 3.9719 -0.0335 -0.2951 -0.0772 760  VAL A CG2 
5742  N N   . SER A 761  ? 3.1277 4.0881 3.3923 -0.0380 -0.2914 -0.0223 761  SER A N   
5743  C CA  . SER A 761  ? 2.9702 3.8812 3.2055 -0.0360 -0.2829 -0.0086 761  SER A CA  
5744  C C   . SER A 761  ? 2.7661 3.6804 2.9644 -0.0171 -0.2705 -0.0319 761  SER A C   
5745  O O   . SER A 761  ? 2.7487 3.6586 2.9309 -0.0185 -0.2582 -0.0178 761  SER A O   
5746  C CB  . SER A 761  ? 2.9954 3.9465 3.2563 -0.0593 -0.2728 0.0356  761  SER A CB  
5747  O OG  . SER A 761  ? 3.0048 3.9005 3.2403 -0.0577 -0.2677 0.0498  761  SER A OG  
5748  N N   . LYS A 762  ? 2.5506 3.4721 2.7373 0.0005  -0.2745 -0.0679 762  LYS A N   
5749  C CA  . LYS A 762  ? 2.3096 3.2312 2.4645 0.0190  -0.2647 -0.0932 762  LYS A CA  
5750  C C   . LYS A 762  ? 2.2200 3.0426 2.3343 0.0364  -0.2701 -0.1112 762  LYS A C   
5751  O O   . LYS A 762  ? 2.2412 3.0091 2.3477 0.0456  -0.2851 -0.1265 762  LYS A O   
5752  C CB  . LYS A 762  ? 2.1734 3.1533 2.3366 0.0307  -0.2663 -0.1239 762  LYS A CB  
5753  C CG  . LYS A 762  ? 2.0178 3.1081 2.2156 0.0180  -0.2570 -0.1117 762  LYS A CG  
5754  C CD  . LYS A 762  ? 1.8945 3.0339 2.1006 0.0320  -0.2620 -0.1461 762  LYS A CD  
5755  C CE  . LYS A 762  ? 1.7927 3.0421 2.0383 0.0184  -0.2558 -0.1332 762  LYS A CE  
5756  N NZ  . LYS A 762  ? 1.7449 3.0465 1.9951 0.0351  -0.2589 -0.1698 762  LYS A NZ  
5757  N N   . PRO A 763  ? 2.0709 2.8723 2.1591 0.0416  -0.2577 -0.1095 763  PRO A N   
5758  C CA  . PRO A 763  ? 2.0112 2.7242 2.0602 0.0583  -0.2601 -0.1262 763  PRO A CA  
5759  C C   . PRO A 763  ? 1.9105 2.6152 1.9415 0.0794  -0.2630 -0.1640 763  PRO A C   
5760  O O   . PRO A 763  ? 1.9078 2.6354 1.9279 0.0868  -0.2517 -0.1772 763  PRO A O   
5761  C CB  . PRO A 763  ? 1.9871 2.6992 2.0211 0.0550  -0.2438 -0.1117 763  PRO A CB  
5762  C CG  . PRO A 763  ? 1.9876 2.7697 2.0526 0.0345  -0.2367 -0.0802 763  PRO A CG  
5763  C CD  . PRO A 763  ? 2.0186 2.8735 2.1139 0.0303  -0.2413 -0.0872 763  PRO A CD  
5764  N N   . GLU A 764  ? 1.8241 2.4970 1.8534 0.0892  -0.2786 -0.1815 764  GLU A N   
5765  C CA  . GLU A 764  ? 1.7196 2.3662 1.7268 0.1115  -0.2833 -0.2162 764  GLU A CA  
5766  C C   . GLU A 764  ? 1.6374 2.1859 1.6064 0.1244  -0.2866 -0.2207 764  GLU A C   
5767  O O   . GLU A 764  ? 1.6375 2.1427 1.6011 0.1168  -0.2890 -0.2001 764  GLU A O   
5768  C CB  . GLU A 764  ? 1.7219 2.3917 1.7472 0.1173  -0.2986 -0.2342 764  GLU A CB  
5769  C CG  . GLU A 764  ? 1.7343 2.3891 1.7787 0.1058  -0.3119 -0.2175 764  GLU A CG  
5770  C CD  . GLU A 764  ? 1.7375 2.4488 1.8138 0.1045  -0.3232 -0.2295 764  GLU A CD  
5771  O OE1 . GLU A 764  ? 1.7285 2.4587 1.7998 0.1208  -0.3263 -0.2585 764  GLU A OE1 
5772  O OE2 . GLU A 764  ? 1.7413 2.4783 1.8492 0.0871  -0.3292 -0.2100 764  GLU A OE2 
5773  N N   . ILE A 765  ? 1.5580 2.0717 1.5010 0.1442  -0.2870 -0.2469 765  ILE A N   
5774  C CA  . ILE A 765  ? 1.5228 1.9466 1.4274 0.1570  -0.2874 -0.2497 765  ILE A CA  
5775  C C   . ILE A 765  ? 1.5359 1.9222 1.4169 0.1802  -0.2932 -0.2798 765  ILE A C   
5776  O O   . ILE A 765  ? 1.5608 1.9571 1.4342 0.1874  -0.2836 -0.2940 765  ILE A O   
5777  C CB  . ILE A 765  ? 1.4516 1.8652 1.3432 0.1506  -0.2697 -0.2353 765  ILE A CB  
5778  C CG1 . ILE A 765  ? 1.4710 1.7940 1.3251 0.1613  -0.2691 -0.2332 765  ILE A CG1 
5779  C CG2 . ILE A 765  ? 1.4201 1.8766 1.3141 0.1553  -0.2581 -0.2522 765  ILE A CG2 
5780  C CD1 . ILE A 765  ? 1.4546 1.7640 1.3030 0.1497  -0.2568 -0.2092 765  ILE A CD1 
5781  N N   . ARG A 766  ? 1.5260 1.8672 1.3955 0.1924  -0.3095 -0.2895 766  ARG A N   
5782  C CA  . ARG A 766  ? 1.5127 1.8285 1.3649 0.2148  -0.3177 -0.3180 766  ARG A CA  
5783  C C   . ARG A 766  ? 1.5631 1.8056 1.3750 0.2311  -0.3112 -0.3253 766  ARG A C   
5784  O O   . ARG A 766  ? 1.5822 1.7831 1.3736 0.2510  -0.3206 -0.3436 766  ARG A O   
5785  C CB  . ARG A 766  ? 1.4878 1.7870 1.3430 0.2236  -0.3384 -0.3272 766  ARG A CB  
5786  C CG  . ARG A 766  ? 1.4448 1.7999 1.3382 0.2053  -0.3454 -0.3143 766  ARG A CG  
5787  C CD  . ARG A 766  ? 1.4224 1.8567 1.3474 0.2039  -0.3481 -0.3296 766  ARG A CD  
5788  N NE  . ARG A 766  ? 1.4408 1.9293 1.4045 0.1847  -0.3539 -0.3143 766  ARG A NE  
5789  C CZ  . ARG A 766  ? 1.4783 2.0242 1.4718 0.1841  -0.3638 -0.3268 766  ARG A CZ  
5790  N NH1 . ARG A 766  ? 1.5190 2.0750 1.5071 0.2033  -0.3702 -0.3563 766  ARG A NH1 
5791  N NH2 . ARG A 766  ? 1.4619 2.0554 1.4923 0.1645  -0.3677 -0.3097 766  ARG A NH2 
5792  N N   . SER A 767  ? 1.5993 1.8264 1.4005 0.2231  -0.2952 -0.3105 767  SER A N   
5793  C CA  . SER A 767  ? 1.6818 1.8450 1.4484 0.2368  -0.2871 -0.3164 767  SER A CA  
5794  C C   . SER A 767  ? 1.6885 1.8769 1.4603 0.2278  -0.2681 -0.3129 767  SER A C   
5795  O O   . SER A 767  ? 1.6687 1.8916 1.4558 0.2105  -0.2590 -0.2944 767  SER A O   
5796  C CB  . SER A 767  ? 1.7528 1.8399 1.4882 0.2418  -0.2897 -0.3019 767  SER A CB  
5797  O OG  . SER A 767  ? 1.7547 1.8451 1.4947 0.2251  -0.2803 -0.2776 767  SER A OG  
5798  N N   . TYR A 768  ? 1.7198 1.8907 1.4800 0.2401  -0.2628 -0.3310 768  TYR A N   
5799  C CA  . TYR A 768  ? 1.7435 1.9412 1.5119 0.2330  -0.2463 -0.3327 768  TYR A CA  
5800  C C   . TYR A 768  ? 1.6861 1.8236 1.4282 0.2319  -0.2339 -0.3177 768  TYR A C   
5801  O O   . TYR A 768  ? 1.7274 1.7962 1.4403 0.2426  -0.2381 -0.3133 768  TYR A O   
5802  C CB  . TYR A 768  ? 1.8610 2.0688 1.6336 0.2466  -0.2476 -0.3613 768  TYR A CB  
5803  C CG  . TYR A 768  ? 1.9298 2.1643 1.7130 0.2414  -0.2324 -0.3683 768  TYR A CG  
5804  C CD1 . TYR A 768  ? 1.9503 2.2694 1.7652 0.2320  -0.2289 -0.3756 768  TYR A CD1 
5805  C CD2 . TYR A 768  ? 1.9874 2.1644 1.7498 0.2463  -0.2219 -0.3684 768  TYR A CD2 
5806  C CE1 . TYR A 768  ? 1.9726 2.3182 1.7979 0.2285  -0.2166 -0.3843 768  TYR A CE1 
5807  C CE2 . TYR A 768  ? 2.0119 2.2136 1.7869 0.2413  -0.2092 -0.3764 768  TYR A CE2 
5808  C CZ  . TYR A 768  ? 2.0094 2.2952 1.8158 0.2328  -0.2071 -0.3854 768  TYR A CZ  
5809  O OH  . TYR A 768  ? 2.0152 2.3275 1.8348 0.2287  -0.1955 -0.3955 768  TYR A OH  
5810  N N   . PHE A 769  ? 1.5934 1.7588 1.3456 0.2200  -0.2187 -0.3105 769  PHE A N   
5811  C CA  . PHE A 769  ? 1.5559 1.6700 1.2861 0.2190  -0.2052 -0.2987 769  PHE A CA  
5812  C C   . PHE A 769  ? 1.5335 1.6685 1.2736 0.2176  -0.1922 -0.3117 769  PHE A C   
5813  O O   . PHE A 769  ? 1.5243 1.7237 1.2891 0.2058  -0.1860 -0.3109 769  PHE A O   
5814  C CB  . PHE A 769  ? 1.5158 1.6397 1.2490 0.2037  -0.1994 -0.2724 769  PHE A CB  
5815  C CG  . PHE A 769  ? 1.4931 1.5998 1.2218 0.2026  -0.2125 -0.2586 769  PHE A CG  
5816  C CD1 . PHE A 769  ? 1.5141 1.5487 1.2123 0.2146  -0.2186 -0.2553 769  PHE A CD1 
5817  C CD2 . PHE A 769  ? 1.4395 1.6044 1.1959 0.1895  -0.2187 -0.2488 769  PHE A CD2 
5818  C CE1 . PHE A 769  ? 1.5297 1.5511 1.2267 0.2139  -0.2321 -0.2452 769  PHE A CE1 
5819  C CE2 . PHE A 769  ? 1.3897 1.5400 1.1467 0.1871  -0.2314 -0.2369 769  PHE A CE2 
5820  C CZ  . PHE A 769  ? 1.4901 1.5690 1.2182 0.1995  -0.2388 -0.2364 769  PHE A CZ  
5821  N N   . PRO A 770  ? 1.5602 1.6404 1.2814 0.2293  -0.1878 -0.3222 770  PRO A N   
5822  C CA  . PRO A 770  ? 1.6034 1.6882 1.3331 0.2311  -0.1777 -0.3388 770  PRO A CA  
5823  C C   . PRO A 770  ? 1.6515 1.7674 1.3941 0.2165  -0.1620 -0.3298 770  PRO A C   
5824  O O   . PRO A 770  ? 1.6783 1.7771 1.4097 0.2084  -0.1552 -0.3073 770  PRO A O   
5825  C CB  . PRO A 770  ? 1.6306 1.6310 1.3294 0.2438  -0.1748 -0.3381 770  PRO A CB  
5826  C CG  . PRO A 770  ? 1.6469 1.6104 1.3242 0.2542  -0.1886 -0.3318 770  PRO A CG  
5827  C CD  . PRO A 770  ? 1.6078 1.6100 1.2952 0.2423  -0.1932 -0.3161 770  PRO A CD  
5828  N N   . GLU A 771  ? 1.6621 1.8230 1.4283 0.2144  -0.1570 -0.3485 771  GLU A N   
5829  C CA  . GLU A 771  ? 1.6954 1.8855 1.4740 0.2022  -0.1426 -0.3428 771  GLU A CA  
5830  C C   . GLU A 771  ? 1.6866 1.8063 1.4407 0.2020  -0.1309 -0.3281 771  GLU A C   
5831  O O   . GLU A 771  ? 1.6989 1.7552 1.4335 0.2130  -0.1317 -0.3328 771  GLU A O   
5832  C CB  . GLU A 771  ? 1.7710 2.0054 1.5756 0.2037  -0.1399 -0.3700 771  GLU A CB  
5833  C CG  . GLU A 771  ? 1.8357 2.1072 1.6560 0.1919  -0.1258 -0.3675 771  GLU A CG  
5834  C CD  . GLU A 771  ? 1.8856 2.2051 1.7339 0.1943  -0.1250 -0.3975 771  GLU A CD  
5835  O OE1 . GLU A 771  ? 1.8680 2.2600 1.7377 0.1866  -0.1214 -0.4003 771  GLU A OE1 
5836  O OE2 . GLU A 771  ? 1.9328 2.2176 1.7819 0.2048  -0.1285 -0.4183 771  GLU A OE2 
5837  N N   . SER A 772  ? 1.6693 1.8020 1.4243 0.1901  -0.1201 -0.3099 772  SER A N   
5838  C CA  . SER A 772  ? 1.6617 1.7374 1.3962 0.1886  -0.1075 -0.2951 772  SER A CA  
5839  C C   . SER A 772  ? 1.6195 1.6878 1.3642 0.1876  -0.0948 -0.3092 772  SER A C   
5840  O O   . SER A 772  ? 1.6026 1.7139 1.3722 0.1873  -0.0961 -0.3311 772  SER A O   
5841  C CB  . SER A 772  ? 1.6540 1.7464 1.3865 0.1773  -0.1021 -0.2704 772  SER A CB  
5842  O OG  . SER A 772  ? 1.6608 1.7411 1.3806 0.1785  -0.1132 -0.2546 772  SER A OG  
5843  N N   . TRP A 773  ? 1.6134 1.6297 1.3406 0.1867  -0.0825 -0.2971 773  TRP A N   
5844  C CA  . TRP A 773  ? 1.6414 1.6425 1.3787 0.1852  -0.0700 -0.3089 773  TRP A CA  
5845  C C   . TRP A 773  ? 1.7084 1.6710 1.4311 0.1801  -0.0542 -0.2910 773  TRP A C   
5846  O O   . TRP A 773  ? 1.7575 1.6993 1.4589 0.1797  -0.0534 -0.2696 773  TRP A O   
5847  C CB  . TRP A 773  ? 1.6586 1.6125 1.3887 0.1973  -0.0747 -0.3238 773  TRP A CB  
5848  C CG  . TRP A 773  ? 1.6919 1.5771 1.3854 0.2081  -0.0784 -0.3084 773  TRP A CG  
5849  C CD1 . TRP A 773  ? 1.7016 1.5806 1.3785 0.2155  -0.0924 -0.3019 773  TRP A CD1 
5850  C CD2 . TRP A 773  ? 1.7419 1.5564 1.4111 0.2136  -0.0681 -0.2980 773  TRP A CD2 
5851  N NE1 . TRP A 773  ? 1.7344 1.5434 1.3770 0.2263  -0.0924 -0.2895 773  TRP A NE1 
5852  C CE2 . TRP A 773  ? 1.7598 1.5287 1.3959 0.2256  -0.0771 -0.2860 773  TRP A CE2 
5853  C CE3 . TRP A 773  ? 1.7503 1.5373 1.4235 0.2094  -0.0520 -0.2976 773  TRP A CE3 
5854  C CZ2 . TRP A 773  ? 1.8038 1.5026 1.4083 0.2348  -0.0702 -0.2731 773  TRP A CZ2 
5855  C CZ3 . TRP A 773  ? 1.7885 1.5054 1.4319 0.2170  -0.0442 -0.2832 773  TRP A CZ3 
5856  C CH2 . TRP A 773  ? 1.8169 1.4910 1.4250 0.2302  -0.0532 -0.2710 773  TRP A CH2 
5857  N N   . LEU A 774  ? 1.7324 1.6849 1.4679 0.1766  -0.0419 -0.3005 774  LEU A N   
5858  C CA  . LEU A 774  ? 1.7589 1.6897 1.4879 0.1697  -0.0254 -0.2857 774  LEU A CA  
5859  C C   . LEU A 774  ? 1.7059 1.6919 1.4469 0.1591  -0.0222 -0.2760 774  LEU A C   
5860  O O   . LEU A 774  ? 1.6799 1.6478 1.4075 0.1556  -0.0128 -0.2575 774  LEU A O   
5861  C CB  . LEU A 774  ? 1.8278 1.6862 1.5187 0.1775  -0.0213 -0.2650 774  LEU A CB  
5862  C CG  . LEU A 774  ? 1.9072 1.7111 1.5919 0.1799  -0.0081 -0.2659 774  LEU A CG  
5863  C CD1 . LEU A 774  ? 1.9430 1.6852 1.5900 0.1866  -0.0005 -0.2429 774  LEU A CD1 
5864  C CD2 . LEU A 774  ? 1.9135 1.7492 1.6283 0.1673  0.0057  -0.2739 774  LEU A CD2 
5865  N N   . TRP A 775  ? 1.6728 1.7272 1.4391 0.1550  -0.0301 -0.2888 775  TRP A N   
5866  C CA  . TRP A 775  ? 1.6146 1.7308 1.3946 0.1460  -0.0294 -0.2804 775  TRP A CA  
5867  C C   . TRP A 775  ? 1.6204 1.7665 1.4225 0.1376  -0.0163 -0.2876 775  TRP A C   
5868  O O   . TRP A 775  ? 1.5818 1.7914 1.4022 0.1312  -0.0165 -0.2881 775  TRP A O   
5869  C CB  . TRP A 775  ? 1.5563 1.7354 1.3534 0.1462  -0.0428 -0.2908 775  TRP A CB  
5870  C CG  . TRP A 775  ? 1.5280 1.7709 1.3366 0.1380  -0.0438 -0.2783 775  TRP A CG  
5871  C CD1 . TRP A 775  ? 1.5305 1.8434 1.3656 0.1322  -0.0409 -0.2890 775  TRP A CD1 
5872  C CD2 . TRP A 775  ? 1.5224 1.7661 1.3172 0.1352  -0.0489 -0.2525 775  TRP A CD2 
5873  N NE1 . TRP A 775  ? 1.5075 1.8648 1.3447 0.1261  -0.0429 -0.2695 775  TRP A NE1 
5874  C CE2 . TRP A 775  ? 1.4950 1.8097 1.3091 0.1272  -0.0479 -0.2468 775  TRP A CE2 
5875  C CE3 . TRP A 775  ? 1.5375 1.7289 1.3065 0.1392  -0.0546 -0.2342 775  TRP A CE3 
5876  C CZ2 . TRP A 775  ? 1.4726 1.8045 1.2820 0.1221  -0.0522 -0.2218 775  TRP A CZ2 
5877  C CZ3 . TRP A 775  ? 1.5219 1.7311 1.2881 0.1341  -0.0597 -0.2119 775  TRP A CZ3 
5878  C CH2 . TRP A 775  ? 1.4926 1.7701 1.2793 0.1252  -0.0583 -0.2050 775  TRP A CH2 
5879  N N   . GLU A 776  ? 1.6792 1.7796 1.4794 0.1377  -0.0048 -0.2921 776  GLU A N   
5880  C CA  . GLU A 776  ? 1.7220 1.8434 1.5442 0.1295  0.0083  -0.2998 776  GLU A CA  
5881  C C   . GLU A 776  ? 1.7274 1.8426 1.5383 0.1242  0.0191  -0.2776 776  GLU A C   
5882  O O   . GLU A 776  ? 1.7336 1.8027 1.5154 0.1282  0.0199  -0.2569 776  GLU A O   
5883  C CB  . GLU A 776  ? 1.8108 1.8849 1.6393 0.1308  0.0164  -0.3134 776  GLU A CB  
5884  C CG  . GLU A 776  ? 1.9024 1.9020 1.7009 0.1402  0.0143  -0.3040 776  GLU A CG  
5885  C CD  . GLU A 776  ? 1.9969 1.9615 1.8082 0.1426  0.0175  -0.3220 776  GLU A CD  
5886  O OE1 . GLU A 776  ? 2.0291 1.9528 1.8250 0.1524  0.0095  -0.3239 776  GLU A OE1 
5887  O OE2 . GLU A 776  ? 2.0327 2.0114 1.8714 0.1347  0.0273  -0.3346 776  GLU A OE2 
5888  N N   . VAL A 777  ? 1.7215 1.8843 1.5556 0.1165  0.0264  -0.2830 777  VAL A N   
5889  C CA  . VAL A 777  ? 1.7066 1.8601 1.5341 0.1119  0.0386  -0.2662 777  VAL A CA  
5890  C C   . VAL A 777  ? 1.8353 1.9463 1.6682 0.1096  0.0532  -0.2732 777  VAL A C   
5891  O O   . VAL A 777  ? 1.8759 1.9761 1.7236 0.1100  0.0528  -0.2925 777  VAL A O   
5892  C CB  . VAL A 777  ? 1.5676 1.7938 1.4180 0.1055  0.0395  -0.2687 777  VAL A CB  
5893  C CG1 . VAL A 777  ? 1.5006 1.7194 1.3542 0.1006  0.0542  -0.2612 777  VAL A CG1 
5894  C CG2 . VAL A 777  ? 1.5062 1.7651 1.3462 0.1068  0.0282  -0.2516 777  VAL A CG2 
5895  N N   . HIS A 778  ? 1.9134 2.0003 1.7358 0.1071  0.0658  -0.2577 778  HIS A N   
5896  C CA  . HIS A 778  ? 2.0181 2.0677 1.8474 0.1036  0.0813  -0.2622 778  HIS A CA  
5897  C C   . HIS A 778  ? 2.1683 2.2262 1.9989 0.0987  0.0944  -0.2502 778  HIS A C   
5898  O O   . HIS A 778  ? 2.1550 2.2248 1.9696 0.1011  0.0912  -0.2333 778  HIS A O   
5899  C CB  . HIS A 778  ? 2.0231 1.9970 1.8214 0.1111  0.0840  -0.2502 778  HIS A CB  
5900  C CG  . HIS A 778  ? 2.0120 1.9643 1.8156 0.1150  0.0767  -0.2660 778  HIS A CG  
5901  N ND1 . HIS A 778  ? 2.0289 1.9436 1.8432 0.1129  0.0865  -0.2743 778  HIS A ND1 
5902  C CD2 . HIS A 778  ? 1.9905 1.9510 1.7900 0.1215  0.0605  -0.2740 778  HIS A CD2 
5903  C CE1 . HIS A 778  ? 2.0287 1.9289 1.8452 0.1186  0.0758  -0.2874 778  HIS A CE1 
5904  N NE2 . HIS A 778  ? 2.0047 1.9331 1.8119 0.1242  0.0601  -0.2881 778  HIS A NE2 
5905  N N   . LEU A 779  ? 2.3229 2.3739 2.1739 0.0919  0.1089  -0.2591 779  LEU A N   
5906  C CA  . LEU A 779  ? 2.4589 2.5137 2.3116 0.0876  0.1230  -0.2484 779  LEU A CA  
5907  C C   . LEU A 779  ? 2.5895 2.5788 2.4199 0.0898  0.1375  -0.2329 779  LEU A C   
5908  O O   . LEU A 779  ? 2.6334 2.6030 2.4812 0.0838  0.1498  -0.2409 779  LEU A O   
5909  C CB  . LEU A 779  ? 2.4695 2.5712 2.3647 0.0775  0.1304  -0.2691 779  LEU A CB  
5910  C CG  . LEU A 779  ? 2.4827 2.5853 2.3777 0.0741  0.1452  -0.2569 779  LEU A CG  
5911  C CD1 . LEU A 779  ? 2.4662 2.6057 2.3486 0.0784  0.1375  -0.2438 779  LEU A CD1 
5912  C CD2 . LEU A 779  ? 2.4880 2.6222 2.4252 0.0634  0.1558  -0.2769 779  LEU A CD2 
5913  N N   . VAL A 780  ? 2.6616 2.6185 2.4548 0.0984  0.1364  -0.2107 780  VAL A N   
5914  C CA  . VAL A 780  ? 2.7731 2.6684 2.5404 0.1030  0.1494  -0.1954 780  VAL A CA  
5915  C C   . VAL A 780  ? 2.7506 2.6481 2.5143 0.1015  0.1643  -0.1831 780  VAL A C   
5916  O O   . VAL A 780  ? 2.7229 2.6252 2.4663 0.1080  0.1599  -0.1695 780  VAL A O   
5917  C CB  . VAL A 780  ? 2.8690 2.7180 2.5946 0.1159  0.1391  -0.1808 780  VAL A CB  
5918  C CG1 . VAL A 780  ? 2.9699 2.7594 2.6662 0.1224  0.1532  -0.1643 780  VAL A CG1 
5919  C CG2 . VAL A 780  ? 2.9159 2.7583 2.6457 0.1180  0.1260  -0.1938 780  VAL A CG2 
5920  N N   . PRO A 781  ? 2.7834 2.6777 2.5690 0.0930  0.1818  -0.1884 781  PRO A N   
5921  C CA  . PRO A 781  ? 2.7862 2.6799 2.5691 0.0918  0.1981  -0.1771 781  PRO A CA  
5922  C C   . PRO A 781  ? 2.8154 2.6470 2.5590 0.1014  0.2070  -0.1571 781  PRO A C   
5923  O O   . PRO A 781  ? 2.8561 2.6552 2.6031 0.0977  0.2212  -0.1552 781  PRO A O   
5924  C CB  . PRO A 781  ? 2.8163 2.7285 2.6415 0.0778  0.2126  -0.1924 781  PRO A CB  
5925  C CG  . PRO A 781  ? 2.8153 2.7486 2.6678 0.0724  0.2004  -0.2144 781  PRO A CG  
5926  C CD  . PRO A 781  ? 2.8119 2.7100 2.6318 0.0831  0.1864  -0.2073 781  PRO A CD  
5927  N N   . ARG A 782  ? 2.8017 2.6175 2.5092 0.1140  0.1981  -0.1426 782  ARG A N   
5928  C CA  . ARG A 782  ? 2.8411 2.6025 2.5080 0.1259  0.2055  -0.1241 782  ARG A CA  
5929  C C   . ARG A 782  ? 2.8203 2.5312 2.4692 0.1306  0.2048  -0.1217 782  ARG A C   
5930  O O   . ARG A 782  ? 2.8533 2.5189 2.4641 0.1430  0.2074  -0.1066 782  ARG A O   
5931  C CB  . ARG A 782  ? 2.9286 2.6871 2.5989 0.1232  0.2281  -0.1160 782  ARG A CB  
5932  C CG  . ARG A 782  ? 2.9879 2.7926 2.6725 0.1211  0.2294  -0.1171 782  ARG A CG  
5933  C CD  . ARG A 782  ? 3.0864 2.8853 2.7701 0.1208  0.2519  -0.1081 782  ARG A CD  
5934  N NE  . ARG A 782  ? 3.1575 2.9619 2.8751 0.1061  0.2698  -0.1158 782  ARG A NE  
5935  C CZ  . ARG A 782  ? 3.2187 3.0203 2.9434 0.1022  0.2918  -0.1092 782  ARG A CZ  
5936  N NH1 . ARG A 782  ? 3.2448 3.0397 2.9431 0.1133  0.2987  -0.0956 782  ARG A NH1 
5937  N NH2 . ARG A 782  ? 3.2398 3.0463 2.9998 0.0872  0.3067  -0.1168 782  ARG A NH2 
5938  N N   . ARG A 783  ? 2.7592 2.4785 2.4350 0.1220  0.2005  -0.1370 783  ARG A N   
5939  C CA  . ARG A 783  ? 2.7399 2.4129 2.4030 0.1262  0.1989  -0.1363 783  ARG A CA  
5940  C C   . ARG A 783  ? 2.6618 2.3578 2.3587 0.1178  0.1883  -0.1579 783  ARG A C   
5941  O O   . ARG A 783  ? 2.6390 2.3811 2.3754 0.1056  0.1901  -0.1736 783  ARG A O   
5942  C CB  . ARG A 783  ? 2.7938 2.4290 2.4554 0.1231  0.2214  -0.1259 783  ARG A CB  
5943  C CG  . ARG A 783  ? 2.8353 2.4291 2.4523 0.1364  0.2313  -0.1029 783  ARG A CG  
5944  C CD  . ARG A 783  ? 2.8779 2.4555 2.5046 0.1291  0.2573  -0.0930 783  ARG A CD  
5945  N NE  . ARG A 783  ? 2.9061 2.4832 2.5085 0.1365  0.2691  -0.0775 783  ARG A NE  
5946  C CZ  . ARG A 783  ? 2.9209 2.5068 2.5382 0.1286  0.2915  -0.0710 783  ARG A CZ  
5947  N NH1 . ARG A 783  ? 2.9230 2.5175 2.5814 0.1117  0.3045  -0.0784 783  ARG A NH1 
5948  N NH2 . ARG A 783  ? 2.9229 2.5101 2.5159 0.1378  0.3004  -0.0582 783  ARG A NH2 
5949  N N   . LYS A 784  ? 2.6160 2.2810 2.2973 0.1255  0.1765  -0.1598 784  LYS A N   
5950  C CA  . LYS A 784  ? 2.5560 2.2322 2.2668 0.1198  0.1677  -0.1803 784  LYS A CA  
5951  C C   . LYS A 784  ? 2.5468 2.1804 2.2278 0.1330  0.1546  -0.1767 784  LYS A C   
5952  O O   . LYS A 784  ? 2.5505 2.1755 2.1991 0.1444  0.1434  -0.1671 784  LYS A O   
5953  C CB  . LYS A 784  ? 2.4950 2.2373 2.2364 0.1131  0.1543  -0.1997 784  LYS A CB  
5954  C CG  . LYS A 784  ? 2.4690 2.2300 2.2464 0.1070  0.1465  -0.2247 784  LYS A CG  
5955  C CD  . LYS A 784  ? 2.3988 2.2325 2.2078 0.1007  0.1352  -0.2446 784  LYS A CD  
5956  C CE  . LYS A 784  ? 2.3643 2.2189 2.2112 0.0956  0.1281  -0.2724 784  LYS A CE  
5957  N NZ  . LYS A 784  ? 2.3013 2.2304 2.1775 0.0911  0.1175  -0.2924 784  LYS A NZ  
5958  N N   . GLN A 785  ? 2.5299 2.1370 2.2237 0.1318  0.1553  -0.1851 785  GLN A N   
5959  C CA  . GLN A 785  ? 2.5190 2.0811 2.1850 0.1452  0.1442  -0.1814 785  GLN A CA  
5960  C C   . GLN A 785  ? 2.4687 2.0450 2.1663 0.1419  0.1320  -0.2054 785  GLN A C   
5961  O O   . GLN A 785  ? 2.4496 2.0361 2.1848 0.1304  0.1399  -0.2184 785  GLN A O   
5962  C CB  . GLN A 785  ? 2.5832 2.0833 2.2253 0.1503  0.1601  -0.1618 785  GLN A CB  
5963  C CG  . GLN A 785  ? 2.6430 2.0946 2.2624 0.1634  0.1502  -0.1596 785  GLN A CG  
5964  C CD  . GLN A 785  ? 2.7255 2.1193 2.3270 0.1668  0.1679  -0.1398 785  GLN A CD  
5965  O OE1 . GLN A 785  ? 2.7495 2.1424 2.3765 0.1539  0.1863  -0.1369 785  GLN A OE1 
5966  N NE2 . GLN A 785  ? 2.7659 2.1125 2.3241 0.1842  0.1624  -0.1254 785  GLN A NE2 
5967  N N   . LEU A 786  ? 2.4511 2.0286 2.1354 0.1523  0.1124  -0.2126 786  LEU A N   
5968  C CA  . LEU A 786  ? 2.4378 2.0427 2.1550 0.1495  0.0991  -0.2387 786  LEU A CA  
5969  C C   . LEU A 786  ? 2.4821 2.0558 2.1795 0.1639  0.0828  -0.2424 786  LEU A C   
5970  O O   . LEU A 786  ? 2.4839 2.0851 2.1750 0.1700  0.0657  -0.2499 786  LEU A O   
5971  C CB  . LEU A 786  ? 2.3545 2.0327 2.0959 0.1426  0.0895  -0.2542 786  LEU A CB  
5972  C CG  . LEU A 786  ? 2.2916 1.9904 2.0062 0.1481  0.0809  -0.2414 786  LEU A CG  
5973  C CD1 . LEU A 786  ? 2.2251 1.9971 1.9665 0.1412  0.0711  -0.2564 786  LEU A CD1 
5974  C CD2 . LEU A 786  ? 2.2864 1.9658 1.9788 0.1471  0.0959  -0.2186 786  LEU A CD2 
5975  N N   . GLN A 787  ? 2.5176 2.0356 2.2078 0.1689  0.0882  -0.2373 787  GLN A N   
5976  C CA  . GLN A 787  ? 2.5373 2.0186 2.2063 0.1842  0.0735  -0.2393 787  GLN A CA  
5977  C C   . GLN A 787  ? 2.4591 1.9827 2.1514 0.1866  0.0526  -0.2664 787  GLN A C   
5978  O O   . GLN A 787  ? 2.4126 1.9928 2.1419 0.1757  0.0504  -0.2858 787  GLN A O   
5979  C CB  . GLN A 787  ? 2.6378 2.0580 2.3056 0.1870  0.0832  -0.2321 787  GLN A CB  
5980  C CG  . GLN A 787  ? 2.6989 2.1308 2.4169 0.1724  0.0911  -0.2494 787  GLN A CG  
5981  C CD  . GLN A 787  ? 2.8083 2.1766 2.5243 0.1723  0.1051  -0.2349 787  GLN A CD  
5982  O OE1 . GLN A 787  ? 2.8444 2.2028 2.5958 0.1668  0.1042  -0.2502 787  GLN A OE1 
5983  N NE2 . GLN A 787  ? 2.8545 2.1796 2.5296 0.1787  0.1181  -0.2050 787  GLN A NE2 
5984  N N   . PHE A 788  ? 2.4389 1.9363 2.1078 0.2021  0.0374  -0.2672 788  PHE A N   
5985  C CA  . PHE A 788  ? 2.3638 1.8937 2.0488 0.2080  0.0167  -0.2913 788  PHE A CA  
5986  C C   . PHE A 788  ? 2.3533 1.8403 1.9996 0.2269  0.0035  -0.2827 788  PHE A C   
5987  O O   . PHE A 788  ? 2.4000 1.8535 2.0076 0.2339  0.0080  -0.2597 788  PHE A O   
5988  C CB  . PHE A 788  ? 2.2785 1.8819 1.9791 0.2006  0.0092  -0.3011 788  PHE A CB  
5989  C CG  . PHE A 788  ? 2.2316 1.8381 1.8990 0.2031  0.0090  -0.2797 788  PHE A CG  
5990  C CD1 . PHE A 788  ? 2.2179 1.8158 1.8583 0.2160  -0.0068 -0.2757 788  PHE A CD1 
5991  C CD2 . PHE A 788  ? 2.1936 1.8132 1.8593 0.1929  0.0234  -0.2652 788  PHE A CD2 
5992  C CE1 . PHE A 788  ? 2.1828 1.7828 1.7964 0.2182  -0.0085 -0.2578 788  PHE A CE1 
5993  C CE2 . PHE A 788  ? 2.1630 1.7843 1.8004 0.1961  0.0216  -0.2471 788  PHE A CE2 
5994  C CZ  . PHE A 788  ? 2.1582 1.7689 1.7704 0.2084  0.0055  -0.2436 788  PHE A CZ  
5995  N N   . ALA A 789  ? 2.2885 1.7755 1.9443 0.2366  -0.0129 -0.3017 789  ALA A N   
5996  C CA  . ALA A 789  ? 2.2467 1.7003 1.8668 0.2552  -0.0273 -0.2954 789  ALA A CA  
5997  C C   . ALA A 789  ? 2.1739 1.6810 1.7941 0.2573  -0.0439 -0.3048 789  ALA A C   
5998  O O   . ALA A 789  ? 2.1275 1.6932 1.7816 0.2500  -0.0507 -0.3260 789  ALA A O   
5999  C CB  . ALA A 789  ? 2.2835 1.7005 1.9096 0.2670  -0.0364 -0.3082 789  ALA A CB  
6000  N N   . LEU A 790  ? 2.1587 1.6484 1.7424 0.2672  -0.0503 -0.2891 790  LEU A N   
6001  C CA  . LEU A 790  ? 2.1252 1.6657 1.7115 0.2669  -0.0649 -0.2953 790  LEU A CA  
6002  C C   . LEU A 790  ? 2.1506 1.7057 1.7459 0.2784  -0.0853 -0.3164 790  LEU A C   
6003  O O   . LEU A 790  ? 2.1542 1.6663 1.7412 0.2912  -0.0903 -0.3217 790  LEU A O   
6004  C CB  . LEU A 790  ? 2.0926 1.6160 1.6429 0.2710  -0.0648 -0.2726 790  LEU A CB  
6005  C CG  . LEU A 790  ? 2.0939 1.5541 1.6087 0.2770  -0.0506 -0.2492 790  LEU A CG  
6006  C CD1 . LEU A 790  ? 2.1351 1.5380 1.6169 0.2976  -0.0596 -0.2452 790  LEU A CD1 
6007  C CD2 . LEU A 790  ? 2.0503 1.5164 1.5452 0.2738  -0.0463 -0.2311 790  LEU A CD2 
6008  N N   . PRO A 791  ? 2.1998 1.8173 1.8131 0.2740  -0.0969 -0.3278 791  PRO A N   
6009  C CA  . PRO A 791  ? 2.2677 1.9188 1.9012 0.2811  -0.1144 -0.3525 791  PRO A CA  
6010  C C   . PRO A 791  ? 2.3992 2.0090 2.0054 0.3007  -0.1295 -0.3524 791  PRO A C   
6011  O O   . PRO A 791  ? 2.4581 2.0422 2.0328 0.3067  -0.1324 -0.3349 791  PRO A O   
6012  C CB  . PRO A 791  ? 2.1998 1.9233 1.8499 0.2713  -0.1207 -0.3552 791  PRO A CB  
6013  C CG  . PRO A 791  ? 2.1628 1.8916 1.8069 0.2576  -0.1057 -0.3343 791  PRO A CG  
6014  C CD  . PRO A 791  ? 2.1771 1.8328 1.7882 0.2636  -0.0952 -0.3150 791  PRO A CD  
6015  N N   . ASP A 792  ? 2.4762 2.0816 2.0954 0.3114  -0.1403 -0.3734 792  ASP A N   
6016  C CA  . ASP A 792  ? 2.5801 2.1563 2.1777 0.3311  -0.1575 -0.3774 792  ASP A CA  
6017  C C   . ASP A 792  ? 2.4908 2.1153 2.0884 0.3307  -0.1710 -0.3789 792  ASP A C   
6018  O O   . ASP A 792  ? 2.4438 2.1271 2.0701 0.3286  -0.1812 -0.3992 792  ASP A O   
6019  C CB  . ASP A 792  ? 2.7689 2.3461 2.3892 0.3414  -0.1680 -0.4041 792  ASP A CB  
6020  C CG  . ASP A 792  ? 3.0277 2.5667 2.6244 0.3642  -0.1857 -0.4084 792  ASP A CG  
6021  O OD1 . ASP A 792  ? 3.1362 2.6666 2.7055 0.3714  -0.1934 -0.3964 792  ASP A OD1 
6022  O OD2 . ASP A 792  ? 3.1639 2.6818 2.7711 0.3757  -0.1927 -0.4251 792  ASP A OD2 
6023  N N   . SER A 793  ? 2.4543 2.0564 2.0216 0.3325  -0.1712 -0.3579 793  SER A N   
6024  C CA  . SER A 793  ? 2.3588 2.0006 1.9271 0.3324  -0.1853 -0.3586 793  SER A CA  
6025  C C   . SER A 793  ? 2.2891 1.8973 1.8233 0.3361  -0.1864 -0.3364 793  SER A C   
6026  O O   . SER A 793  ? 2.2920 1.8812 1.8132 0.3278  -0.1720 -0.3176 793  SER A O   
6027  C CB  . SER A 793  ? 2.2961 2.0160 1.8997 0.3135  -0.1824 -0.3641 793  SER A CB  
6028  O OG  . SER A 793  ? 2.2490 2.0020 1.8530 0.3115  -0.1942 -0.3597 793  SER A OG  
6029  N N   . LEU A 794  ? 2.2078 1.8121 1.7295 0.3489  -0.2046 -0.3405 794  LEU A N   
6030  C CA  . LEU A 794  ? 2.1424 1.7223 1.6359 0.3538  -0.2103 -0.3242 794  LEU A CA  
6031  C C   . LEU A 794  ? 2.0958 1.7207 1.6059 0.3344  -0.2053 -0.3133 794  LEU A C   
6032  O O   . LEU A 794  ? 2.1054 1.7796 1.6367 0.3285  -0.2171 -0.3195 794  LEU A O   
6033  C CB  . LEU A 794  ? 2.1282 1.7139 1.6175 0.3685  -0.2331 -0.3362 794  LEU A CB  
6034  C CG  . LEU A 794  ? 2.1823 1.7147 1.6428 0.3937  -0.2451 -0.3427 794  LEU A CG  
6035  C CD1 . LEU A 794  ? 2.2115 1.7094 1.6690 0.4004  -0.2355 -0.3475 794  LEU A CD1 
6036  C CD2 . LEU A 794  ? 2.1803 1.7461 1.6547 0.4030  -0.2680 -0.3619 794  LEU A CD2 
6037  N N   . THR A 795  ? 2.0645 1.6726 1.5655 0.3249  -0.1883 -0.2961 795  THR A N   
6038  C CA  . THR A 795  ? 1.9793 1.6248 1.4941 0.3074  -0.1832 -0.2836 795  THR A CA  
6039  C C   . THR A 795  ? 1.9631 1.5650 1.4505 0.3067  -0.1697 -0.2627 795  THR A C   
6040  O O   . THR A 795  ? 1.9422 1.5053 1.4142 0.3107  -0.1559 -0.2582 795  THR A O   
6041  C CB  . THR A 795  ? 2.6562 2.3654 2.2105 0.2890  -0.1742 -0.2911 795  THR A CB  
6042  O OG1 . THR A 795  ? 2.6691 2.3671 2.2302 0.2920  -0.1655 -0.3034 795  THR A OG1 
6043  C CG2 . THR A 795  ? 2.6233 2.3964 2.2071 0.2840  -0.1885 -0.3036 795  THR A CG2 
6044  N N   . THR A 796  ? 1.9414 1.5488 1.4234 0.3020  -0.1738 -0.2499 796  THR A N   
6045  C CA  . THR A 796  ? 1.9458 1.5211 1.4065 0.3002  -0.1605 -0.2317 796  THR A CA  
6046  C C   . THR A 796  ? 1.9590 1.5761 1.4463 0.2802  -0.1456 -0.2258 796  THR A C   
6047  O O   . THR A 796  ? 1.9547 1.6113 1.4607 0.2681  -0.1496 -0.2200 796  THR A O   
6048  C CB  . THR A 796  ? 1.9194 1.4775 1.3619 0.3057  -0.1715 -0.2214 796  THR A CB  
6049  O OG1 . THR A 796  ? 1.9568 1.4747 1.3718 0.3261  -0.1857 -0.2272 796  THR A OG1 
6050  C CG2 . THR A 796  ? 1.9051 1.4329 1.3266 0.3047  -0.1567 -0.2044 796  THR A CG2 
6051  N N   . TRP A 797  ? 1.9607 1.5690 1.4508 0.2767  -0.1288 -0.2270 797  TRP A N   
6052  C CA  . TRP A 797  ? 1.9043 1.5544 1.4213 0.2588  -0.1148 -0.2244 797  TRP A CA  
6053  C C   . TRP A 797  ? 1.8400 1.4777 1.3440 0.2539  -0.1057 -0.2055 797  TRP A C   
6054  O O   . TRP A 797  ? 1.8552 1.4495 1.3361 0.2595  -0.0931 -0.1966 797  TRP A O   
6055  C CB  . TRP A 797  ? 1.9554 1.5951 1.4799 0.2572  -0.0999 -0.2323 797  TRP A CB  
6056  C CG  . TRP A 797  ? 2.0179 1.6778 1.5628 0.2599  -0.1073 -0.2534 797  TRP A CG  
6057  C CD1 . TRP A 797  ? 2.0817 1.7036 1.6185 0.2706  -0.1058 -0.2625 797  TRP A CD1 
6058  C CD2 . TRP A 797  ? 2.0240 1.7477 1.6013 0.2526  -0.1175 -0.2681 797  TRP A CD2 
6059  N NE1 . TRP A 797  ? 2.1032 1.7602 1.6659 0.2710  -0.1155 -0.2838 797  TRP A NE1 
6060  C CE2 . TRP A 797  ? 2.0704 1.7922 1.6579 0.2602  -0.1224 -0.2880 797  TRP A CE2 
6061  C CE3 . TRP A 797  ? 2.0013 1.7844 1.6003 0.2406  -0.1228 -0.2656 797  TRP A CE3 
6062  C CZ2 . TRP A 797  ? 2.0573 1.8368 1.6753 0.2572  -0.1324 -0.3072 797  TRP A CZ2 
6063  C CZ3 . TRP A 797  ? 1.9934 1.8339 1.6216 0.2369  -0.1315 -0.2823 797  TRP A CZ3 
6064  C CH2 . TRP A 797  ? 2.0183 1.8583 1.6557 0.2454  -0.1363 -0.3038 797  TRP A CH2 
6065  N N   . GLU A 798  ? 1.7646 1.4401 1.2839 0.2439  -0.1119 -0.1987 798  GLU A N   
6066  C CA  . GLU A 798  ? 1.7431 1.4122 1.2554 0.2383  -0.1022 -0.1823 798  GLU A CA  
6067  C C   . GLU A 798  ? 1.7096 1.4135 1.2456 0.2242  -0.0854 -0.1830 798  GLU A C   
6068  O O   . GLU A 798  ? 1.6685 1.4288 1.2349 0.2120  -0.0873 -0.1873 798  GLU A O   
6069  C CB  . GLU A 798  ? 1.7275 1.4200 1.2483 0.2327  -0.1149 -0.1730 798  GLU A CB  
6070  C CG  . GLU A 798  ? 1.7295 1.4287 1.2525 0.2242  -0.1042 -0.1581 798  GLU A CG  
6071  C CD  . GLU A 798  ? 1.7492 1.4617 1.2788 0.2203  -0.1175 -0.1474 798  GLU A CD  
6072  O OE1 . GLU A 798  ? 1.7718 1.4786 1.2993 0.2258  -0.1348 -0.1510 798  GLU A OE1 
6073  O OE2 . GLU A 798  ? 1.7484 1.4768 1.2866 0.2116  -0.1111 -0.1355 798  GLU A OE2 
6074  N N   . ILE A 799  ? 1.7355 1.4084 1.2586 0.2261  -0.0687 -0.1789 799  ILE A N   
6075  C CA  . ILE A 799  ? 1.7430 1.4485 1.2905 0.2130  -0.0531 -0.1819 799  ILE A CA  
6076  C C   . ILE A 799  ? 1.7515 1.4637 1.2977 0.2062  -0.0432 -0.1665 799  ILE A C   
6077  O O   . ILE A 799  ? 1.7836 1.4586 1.3100 0.2107  -0.0308 -0.1579 799  ILE A O   
6078  C CB  . ILE A 799  ? 1.5314 1.2090 1.0771 0.2166  -0.0413 -0.1916 799  ILE A CB  
6079  C CG1 . ILE A 799  ? 1.5142 1.2066 1.0769 0.2054  -0.0221 -0.1909 799  ILE A CG1 
6080  C CG2 . ILE A 799  ? 1.5932 1.2033 1.1007 0.2324  -0.0398 -0.1839 799  ILE A CG2 
6081  C CD1 . ILE A 799  ? 1.5369 1.1877 1.0931 0.2098  -0.0098 -0.1954 799  ILE A CD1 
6082  N N   . GLN A 800  ? 1.7656 1.5267 1.3330 0.1960  -0.0494 -0.1625 800  GLN A N   
6083  C CA  . GLN A 800  ? 1.7716 1.5482 1.3433 0.1888  -0.0423 -0.1489 800  GLN A CA  
6084  C C   . GLN A 800  ? 1.7604 1.5682 1.3540 0.1783  -0.0253 -0.1538 800  GLN A C   
6085  O O   . GLN A 800  ? 1.7553 1.5799 1.3654 0.1751  -0.0212 -0.1689 800  GLN A O   
6086  C CB  . GLN A 800  ? 1.7691 1.5859 1.3567 0.1820  -0.0564 -0.1412 800  GLN A CB  
6087  C CG  . GLN A 800  ? 1.7599 1.6400 1.3799 0.1718  -0.0616 -0.1515 800  GLN A CG  
6088  C CD  . GLN A 800  ? 1.7648 1.6602 1.3901 0.1724  -0.0805 -0.1506 800  GLN A CD  
6089  O OE1 . GLN A 800  ? 1.8037 1.6571 1.4085 0.1829  -0.0905 -0.1511 800  GLN A OE1 
6090  N NE2 . GLN A 800  ? 1.7219 1.6794 1.3753 0.1613  -0.0853 -0.1492 800  GLN A NE2 
6091  N N   . GLY A 801  ? 1.7595 1.5749 1.3543 0.1737  -0.0163 -0.1424 801  GLY A N   
6092  C CA  . GLY A 801  ? 1.7431 1.5881 1.3587 0.1643  -0.0006 -0.1471 801  GLY A CA  
6093  C C   . GLY A 801  ? 1.7526 1.6134 1.3709 0.1599  0.0056  -0.1335 801  GLY A C   
6094  O O   . GLY A 801  ? 1.7432 1.5692 1.3435 0.1649  0.0155  -0.1255 801  GLY A O   
6095  N N   . ILE A 802  ? 1.7355 1.6506 1.3766 0.1512  -0.0004 -0.1305 802  ILE A N   
6096  C CA  . ILE A 802  ? 1.7296 1.6670 1.3775 0.1467  0.0042  -0.1182 802  ILE A CA  
6097  C C   . ILE A 802  ? 1.7281 1.6838 1.3909 0.1412  0.0219  -0.1262 802  ILE A C   
6098  O O   . ILE A 802  ? 1.7726 1.7396 1.4492 0.1377  0.0279  -0.1424 802  ILE A O   
6099  C CB  . ILE A 802  ? 1.7315 1.7253 1.4010 0.1389  -0.0075 -0.1122 802  ILE A CB  
6100  C CG1 . ILE A 802  ? 1.7030 1.7514 1.3966 0.1302  0.0012  -0.1121 802  ILE A CG1 
6101  C CG2 . ILE A 802  ? 1.7194 1.7401 1.4020 0.1363  -0.0164 -0.1249 802  ILE A CG2 
6102  C CD1 . ILE A 802  ? 1.7047 1.7601 1.3970 0.1296  -0.0009 -0.0931 802  ILE A CD1 
6103  N N   . GLY A 803  ? 1.6870 1.6461 1.3489 0.1405  0.0295  -0.1160 803  GLY A N   
6104  C CA  . GLY A 803  ? 1.6523 1.6386 1.3332 0.1341  0.0450  -0.1234 803  GLY A CA  
6105  C C   . GLY A 803  ? 1.6781 1.7079 1.3732 0.1298  0.0447  -0.1137 803  GLY A C   
6106  O O   . GLY A 803  ? 1.6521 1.6718 1.3354 0.1339  0.0363  -0.0976 803  GLY A O   
6107  N N   . ILE A 804  ? 1.6813 1.7599 1.4028 0.1221  0.0528  -0.1237 804  ILE A N   
6108  C CA  . ILE A 804  ? 1.6670 1.7843 1.4002 0.1197  0.0537  -0.1142 804  ILE A CA  
6109  C C   . ILE A 804  ? 1.6808 1.8191 1.4315 0.1156  0.0695  -0.1251 804  ILE A C   
6110  O O   . ILE A 804  ? 1.6227 1.7780 1.3915 0.1103  0.0762  -0.1435 804  ILE A O   
6111  C CB  . ILE A 804  ? 1.5634 1.7386 1.3139 0.1148  0.0413  -0.1098 804  ILE A CB  
6112  C CG1 . ILE A 804  ? 1.5055 1.7259 1.2792 0.1087  0.0419  -0.1297 804  ILE A CG1 
6113  C CG2 . ILE A 804  ? 1.5192 1.6738 1.2547 0.1179  0.0256  -0.0961 804  ILE A CG2 
6114  C CD1 . ILE A 804  ? 1.4692 1.7396 1.2539 0.1056  0.0284  -0.1241 804  ILE A CD1 
6115  N N   . SER A 805  ? 1.7678 1.9029 1.5136 0.1187  0.0745  -0.1139 805  SER A N   
6116  C CA  . SER A 805  ? 1.8562 2.0109 1.6178 0.1158  0.0894  -0.1215 805  SER A CA  
6117  C C   . SER A 805  ? 1.8727 2.0458 1.6337 0.1196  0.0873  -0.1069 805  SER A C   
6118  O O   . SER A 805  ? 1.8887 2.0678 1.6425 0.1225  0.0736  -0.0920 805  SER A O   
6119  C CB  . SER A 805  ? 1.8585 1.9631 1.6085 0.1178  0.1048  -0.1266 805  SER A CB  
6120  O OG  . SER A 805  ? 1.8670 1.9768 1.6343 0.1109  0.1115  -0.1454 805  SER A OG  
6121  N N   . ASN A 806  ? 1.9831 2.1655 1.7535 0.1194  0.1005  -0.1112 806  ASN A N   
6122  C CA  . ASN A 806  ? 2.0725 2.2839 1.8486 0.1228  0.0987  -0.1010 806  ASN A CA  
6123  C C   . ASN A 806  ? 2.1282 2.2978 1.8778 0.1332  0.0919  -0.0816 806  ASN A C   
6124  O O   . ASN A 806  ? 2.1275 2.3135 1.8794 0.1379  0.0887  -0.0715 806  ASN A O   
6125  C CB  . ASN A 806  ? 2.1397 2.3763 1.9360 0.1197  0.1146  -0.1133 806  ASN A CB  
6126  C CG  . ASN A 806  ? 2.1911 2.4838 2.0194 0.1103  0.1170  -0.1327 806  ASN A CG  
6127  O OD1 . ASN A 806  ? 2.2210 2.5092 2.0627 0.1042  0.1283  -0.1498 806  ASN A OD1 
6128  N ND2 . ASN A 806  ? 2.2024 2.5485 2.0435 0.1094  0.1057  -0.1300 806  ASN A ND2 
6129  N N   . THR A 807  ? 2.1772 2.2926 1.9021 0.1379  0.0887  -0.0774 807  THR A N   
6130  C CA  . THR A 807  ? 2.1890 2.2640 1.8892 0.1486  0.0795  -0.0614 807  THR A CA  
6131  C C   . THR A 807  ? 2.1158 2.1977 1.8149 0.1479  0.0594  -0.0494 807  THR A C   
6132  O O   . THR A 807  ? 2.1581 2.2303 1.8500 0.1541  0.0482  -0.0346 807  THR A O   
6133  C CB  . THR A 807  ? 2.2463 2.2601 1.9193 0.1558  0.0864  -0.0634 807  THR A CB  
6134  O OG1 . THR A 807  ? 2.2599 2.2620 1.9313 0.1506  0.0856  -0.0721 807  THR A OG1 
6135  C CG2 . THR A 807  ? 2.2604 2.2692 1.9351 0.1569  0.1069  -0.0707 807  THR A CG2 
6136  N N   . GLY A 808  ? 2.0077 2.1077 1.7159 0.1401  0.0550  -0.0563 808  GLY A N   
6137  C CA  . GLY A 808  ? 1.9158 2.0218 1.6237 0.1381  0.0375  -0.0462 808  GLY A CA  
6138  C C   . GLY A 808  ? 1.8884 1.9737 1.5890 0.1359  0.0340  -0.0554 808  GLY A C   
6139  O O   . GLY A 808  ? 1.8622 1.9442 1.5657 0.1332  0.0449  -0.0713 808  GLY A O   
6140  N N   . ILE A 809  ? 1.8727 1.9436 1.5657 0.1370  0.0182  -0.0453 809  ILE A N   
6141  C CA  . ILE A 809  ? 1.8389 1.8890 1.5239 0.1366  0.0124  -0.0529 809  ILE A CA  
6142  C C   . ILE A 809  ? 1.8717 1.8542 1.5270 0.1473  0.0096  -0.0511 809  ILE A C   
6143  O O   . ILE A 809  ? 1.9166 1.8741 1.5603 0.1537  0.0004  -0.0384 809  ILE A O   
6144  C CB  . ILE A 809  ? 1.7850 1.8632 1.4813 0.1312  -0.0039 -0.0433 809  ILE A CB  
6145  C CG1 . ILE A 809  ? 1.7632 1.8094 1.4470 0.1336  -0.0127 -0.0489 809  ILE A CG1 
6146  C CG2 . ILE A 809  ? 1.7672 1.8384 1.4616 0.1338  -0.0152 -0.0225 809  ILE A CG2 
6147  C CD1 . ILE A 809  ? 1.7391 1.8054 1.4327 0.1289  -0.0297 -0.0370 809  ILE A CD1 
6148  N N   . CYS A 810  ? 1.8570 1.8102 1.5001 0.1499  0.0163  -0.0639 810  CYS A N   
6149  C CA  . CYS A 810  ? 1.8589 1.7487 1.4710 0.1617  0.0140  -0.0630 810  CYS A CA  
6150  C C   . CYS A 810  ? 1.8693 1.7385 1.4729 0.1632  0.0098  -0.0733 810  CYS A C   
6151  O O   . CYS A 810  ? 1.8620 1.7168 1.4613 0.1637  0.0219  -0.0843 810  CYS A O   
6152  C CB  . CYS A 810  ? 1.8501 1.7094 1.4461 0.1689  0.0309  -0.0646 810  CYS A CB  
6153  S SG  . CYS A 810  ? 2.2841 2.0690 1.8382 0.1859  0.0299  -0.0628 810  CYS A SG  
6154  N N   . VAL A 811  ? 1.8840 1.7510 1.4864 0.1639  -0.0077 -0.0693 811  VAL A N   
6155  C CA  . VAL A 811  ? 1.8903 1.7318 1.4809 0.1683  -0.0148 -0.0778 811  VAL A CA  
6156  C C   . VAL A 811  ? 1.9277 1.7076 1.4850 0.1821  -0.0100 -0.0791 811  VAL A C   
6157  O O   . VAL A 811  ? 1.9529 1.7039 1.4923 0.1908  -0.0117 -0.0704 811  VAL A O   
6158  C CB  . VAL A 811  ? 1.8941 1.7371 1.4865 0.1685  -0.0352 -0.0709 811  VAL A CB  
6159  C CG1 . VAL A 811  ? 1.9154 1.7384 1.4985 0.1731  -0.0428 -0.0817 811  VAL A CG1 
6160  C CG2 . VAL A 811  ? 1.8467 1.7499 1.4697 0.1558  -0.0407 -0.0641 811  VAL A CG2 
6161  N N   . ALA A 812  ? 1.9291 1.6888 1.4775 0.1851  -0.0046 -0.0899 812  ALA A N   
6162  C CA  . ALA A 812  ? 1.9447 1.6475 1.4599 0.1989  0.0009  -0.0894 812  ALA A CA  
6163  C C   . ALA A 812  ? 1.9473 1.6171 1.4422 0.2096  -0.0160 -0.0906 812  ALA A C   
6164  O O   . ALA A 812  ? 1.9291 1.6206 1.4384 0.2049  -0.0304 -0.0942 812  ALA A O   
6165  C CB  . ALA A 812  ? 1.9800 1.6731 1.4951 0.1973  0.0185  -0.0978 812  ALA A CB  
6166  N N   . ASP A 813  ? 1.9356 1.5550 1.3971 0.2246  -0.0139 -0.0877 813  ASP A N   
6167  C CA  . ASP A 813  ? 1.9316 1.5160 1.3703 0.2374  -0.0294 -0.0902 813  ASP A CA  
6168  C C   . ASP A 813  ? 1.8743 1.4621 1.3194 0.2347  -0.0290 -0.1011 813  ASP A C   
6169  O O   . ASP A 813  ? 1.8496 1.4328 1.2957 0.2323  -0.0128 -0.1049 813  ASP A O   
6170  C CB  . ASP A 813  ? 2.0191 1.5523 1.4190 0.2554  -0.0248 -0.0854 813  ASP A CB  
6171  C CG  . ASP A 813  ? 2.0602 1.5929 1.4560 0.2589  -0.0256 -0.0766 813  ASP A CG  
6172  O OD1 . ASP A 813  ? 2.0605 1.5965 1.4613 0.2605  -0.0442 -0.0744 813  ASP A OD1 
6173  O OD2 . ASP A 813  ? 2.0804 1.6098 1.4699 0.2600  -0.0078 -0.0721 813  ASP A OD2 
6174  N N   . THR A 814  ? 1.8427 1.4417 1.2963 0.2341  -0.0472 -0.1065 814  THR A N   
6175  C CA  . THR A 814  ? 1.8201 1.4286 1.2836 0.2320  -0.0509 -0.1186 814  THR A CA  
6176  C C   . THR A 814  ? 1.8386 1.4003 1.2746 0.2447  -0.0428 -0.1224 814  THR A C   
6177  O O   . THR A 814  ? 1.8652 1.3896 1.2738 0.2550  -0.0343 -0.1147 814  THR A O   
6178  C CB  . THR A 814  ? 1.7889 1.4038 1.2560 0.2347  -0.0733 -0.1221 814  THR A CB  
6179  O OG1 . THR A 814  ? 1.7995 1.4007 1.2603 0.2414  -0.0781 -0.1339 814  THR A OG1 
6180  C CG2 . THR A 814  ? 1.8118 1.3890 1.2529 0.2479  -0.0848 -0.1149 814  THR A CG2 
6181  N N   . VAL A 815  ? 1.8584 1.4220 1.3013 0.2449  -0.0454 -0.1337 815  VAL A N   
6182  C CA  . VAL A 815  ? 1.9239 1.4382 1.3382 0.2593  -0.0417 -0.1358 815  VAL A CA  
6183  C C   . VAL A 815  ? 1.9385 1.4527 1.3568 0.2643  -0.0560 -0.1488 815  VAL A C   
6184  O O   . VAL A 815  ? 1.9689 1.4994 1.4070 0.2580  -0.0514 -0.1591 815  VAL A O   
6185  C CB  . VAL A 815  ? 1.9590 1.4601 1.3736 0.2556  -0.0187 -0.1336 815  VAL A CB  
6186  C CG1 . VAL A 815  ? 1.9904 1.4483 1.3845 0.2678  -0.0168 -0.1370 815  VAL A CG1 
6187  C CG2 . VAL A 815  ? 1.9710 1.4550 1.3681 0.2579  -0.0045 -0.1196 815  VAL A CG2 
6188  N N   . LYS A 816  ? 1.9583 1.4546 1.3586 0.2764  -0.0743 -0.1496 816  LYS A N   
6189  C CA  . LYS A 816  ? 1.9957 1.4915 1.3980 0.2832  -0.0899 -0.1623 816  LYS A CA  
6190  C C   . LYS A 816  ? 2.0648 1.5257 1.4526 0.2921  -0.0804 -0.1665 816  LYS A C   
6191  O O   . LYS A 816  ? 2.0667 1.4885 1.4291 0.2995  -0.0666 -0.1564 816  LYS A O   
6192  C CB  . LYS A 816  ? 2.3204 1.7942 1.7010 0.2975  -0.1104 -0.1621 816  LYS A CB  
6193  C CG  . LYS A 816  ? 2.5171 2.0283 1.9198 0.2879  -0.1253 -0.1606 816  LYS A CG  
6194  C CD  . LYS A 816  ? 2.5001 2.0074 1.8974 0.2843  -0.1191 -0.1468 816  LYS A CD  
6195  C CE  . LYS A 816  ? 2.4455 1.9822 1.8636 0.2758  -0.1347 -0.1431 816  LYS A CE  
6196  N NZ  . LYS A 816  ? 2.4219 1.9485 1.8324 0.2751  -0.1293 -0.1305 816  LYS A NZ  
6197  N N   . ALA A 817  ? 2.1250 1.6009 1.5300 0.2914  -0.0876 -0.1808 817  ALA A N   
6198  C CA  . ALA A 817  ? 2.2326 1.6756 1.6281 0.2995  -0.0804 -0.1853 817  ALA A CA  
6199  C C   . ALA A 817  ? 2.2400 1.6869 1.6413 0.3080  -0.0980 -0.2013 817  ALA A C   
6200  O O   . ALA A 817  ? 2.2411 1.7069 1.6669 0.3027  -0.0966 -0.2143 817  ALA A O   
6201  C CB  . ALA A 817  ? 2.2650 1.7275 1.6874 0.2843  -0.0618 -0.1877 817  ALA A CB  
6202  N N   . LYS A 818  ? 2.2313 1.6613 1.6110 0.3220  -0.1154 -0.2016 818  LYS A N   
6203  C CA  . LYS A 818  ? 2.2430 1.6751 1.6257 0.3324  -0.1334 -0.2169 818  LYS A CA  
6204  C C   . LYS A 818  ? 2.2398 1.6351 1.6120 0.3427  -0.1274 -0.2212 818  LYS A C   
6205  O O   . LYS A 818  ? 2.2409 1.5859 1.5817 0.3533  -0.1171 -0.2087 818  LYS A O   
6206  C CB  . LYS A 818  ? 2.3066 1.7172 1.6627 0.3485  -0.1523 -0.2157 818  LYS A CB  
6207  C CG  . LYS A 818  ? 2.4194 1.7662 1.7303 0.3720  -0.1532 -0.2097 818  LYS A CG  
6208  C CD  . LYS A 818  ? 2.5016 1.8351 1.7920 0.3892  -0.1760 -0.2148 818  LYS A CD  
6209  C CE  . LYS A 818  ? 2.6024 1.8749 1.8431 0.4132  -0.1753 -0.2054 818  LYS A CE  
6210  N NZ  . LYS A 818  ? 2.6362 1.8964 1.8553 0.4302  -0.1971 -0.2100 818  LYS A NZ  
6211  N N   . VAL A 819  ? 2.2389 1.6607 1.6387 0.3396  -0.1337 -0.2387 819  VAL A N   
6212  C CA  . VAL A 819  ? 2.2647 1.6516 1.6574 0.3516  -0.1334 -0.2457 819  VAL A CA  
6213  C C   . VAL A 819  ? 2.2838 1.6683 1.6684 0.3680  -0.1562 -0.2584 819  VAL A C   
6214  O O   . VAL A 819  ? 2.2622 1.6852 1.6593 0.3647  -0.1704 -0.2653 819  VAL A O   
6215  C CB  . VAL A 819  ? 2.2234 1.6406 1.6549 0.3383  -0.1252 -0.2594 819  VAL A CB  
6216  C CG1 . VAL A 819  ? 2.2136 1.6249 1.6510 0.3244  -0.1020 -0.2470 819  VAL A CG1 
6217  C CG2 . VAL A 819  ? 2.1631 1.6511 1.6323 0.3261  -0.1359 -0.2759 819  VAL A CG2 
6218  N N   . PHE A 820  ? 2.3608 1.7003 1.7255 0.3856  -0.1600 -0.2608 820  PHE A N   
6219  C CA  . PHE A 820  ? 2.4346 1.7698 1.7904 0.4032  -0.1823 -0.2738 820  PHE A CA  
6220  C C   . PHE A 820  ? 2.4841 1.7602 1.8114 0.4251  -0.1848 -0.2722 820  PHE A C   
6221  O O   . PHE A 820  ? 2.4825 1.7083 1.7776 0.4328  -0.1724 -0.2536 820  PHE A O   
6222  C CB  . PHE A 820  ? 2.5456 1.8849 1.8823 0.4089  -0.1950 -0.2683 820  PHE A CB  
6223  C CG  . PHE A 820  ? 2.7248 2.0386 2.0375 0.4323  -0.2152 -0.2756 820  PHE A CG  
6224  C CD1 . PHE A 820  ? 2.8444 2.1020 2.1109 0.4520  -0.2157 -0.2623 820  PHE A CD1 
6225  C CD2 . PHE A 820  ? 2.7773 2.1250 2.1131 0.4358  -0.2337 -0.2965 820  PHE A CD2 
6226  C CE1 . PHE A 820  ? 2.9267 2.1618 2.1703 0.4751  -0.2352 -0.2699 820  PHE A CE1 
6227  C CE2 . PHE A 820  ? 2.8491 2.1749 2.1640 0.4580  -0.2531 -0.3046 820  PHE A CE2 
6228  C CZ  . PHE A 820  ? 2.9185 2.1872 2.1869 0.4780  -0.2543 -0.2915 820  PHE A CZ  
6229  N N   . LYS A 821  ? 2.5256 1.8098 1.8654 0.4354  -0.2009 -0.2914 821  LYS A N   
6230  C CA  . LYS A 821  ? 2.5995 1.8305 1.9148 0.4578  -0.2068 -0.2917 821  LYS A CA  
6231  C C   . LYS A 821  ? 2.6387 1.8526 1.9227 0.4803  -0.2276 -0.2936 821  LYS A C   
6232  O O   . LYS A 821  ? 2.6375 1.8935 1.9367 0.4791  -0.2441 -0.3078 821  LYS A O   
6233  C CB  . LYS A 821  ? 2.5730 1.8215 1.9224 0.4574  -0.2128 -0.3135 821  LYS A CB  
6234  C CG  . LYS A 821  ? 2.5755 1.7703 1.9045 0.4807  -0.2208 -0.3154 821  LYS A CG  
6235  C CD  . LYS A 821  ? 2.5587 1.7192 1.8974 0.4753  -0.2034 -0.3088 821  LYS A CD  
6236  C CE  . LYS A 821  ? 2.5791 1.7033 1.9161 0.4954  -0.2157 -0.3196 821  LYS A CE  
6237  N NZ  . LYS A 821  ? 2.5974 1.6817 1.9453 0.4910  -0.2003 -0.3124 821  LYS A NZ  
6238  N N   . ASP A 822  ? 2.1810 1.9919 1.8744 0.4104  -0.1632 -0.0992 822  ASP A N   
6239  C CA  . ASP A 822  ? 2.2298 1.9478 1.8675 0.4092  -0.1570 -0.0806 822  ASP A CA  
6240  C C   . ASP A 822  ? 2.2219 1.8886 1.8456 0.4052  -0.1799 -0.0915 822  ASP A C   
6241  O O   . ASP A 822  ? 2.1949 1.8278 1.7796 0.4232  -0.1760 -0.0815 822  ASP A O   
6242  C CB  . ASP A 822  ? 2.3275 1.9963 1.9584 0.3834  -0.1502 -0.0711 822  ASP A CB  
6243  C CG  . ASP A 822  ? 2.4476 2.1342 2.0657 0.3918  -0.1207 -0.0494 822  ASP A CG  
6244  O OD1 . ASP A 822  ? 2.4677 2.2260 2.1006 0.4126  -0.1080 -0.0473 822  ASP A OD1 
6245  O OD2 . ASP A 822  ? 2.5196 2.1478 2.1122 0.3780  -0.1102 -0.0342 822  ASP A OD2 
6246  N N   . VAL A 823  ? 2.2552 1.9141 1.9102 0.3806  -0.2029 -0.1114 823  VAL A N   
6247  C CA  . VAL A 823  ? 2.2632 1.8845 1.9143 0.3754  -0.2277 -0.1257 823  VAL A CA  
6248  C C   . VAL A 823  ? 2.2694 1.9528 1.9748 0.3688  -0.2497 -0.1536 823  VAL A C   
6249  O O   . VAL A 823  ? 2.2998 2.0205 2.0451 0.3517  -0.2526 -0.1646 823  VAL A O   
6250  C CB  . VAL A 823  ? 2.2393 1.7750 1.8694 0.3505  -0.2369 -0.1230 823  VAL A CB  
6251  C CG1 . VAL A 823  ? 2.1992 1.7111 1.8376 0.3430  -0.2652 -0.1422 823  VAL A CG1 
6252  C CG2 . VAL A 823  ? 2.2679 1.7349 1.8396 0.3585  -0.2191 -0.0974 823  VAL A CG2 
6253  N N   . PHE A 824  ? 2.2520 1.9452 1.9584 0.3824  -0.2651 -0.1652 824  PHE A N   
6254  C CA  . PHE A 824  ? 2.1982 1.9505 1.9527 0.3800  -0.2866 -0.1920 824  PHE A CA  
6255  C C   . PHE A 824  ? 2.1366 1.8615 1.8809 0.3863  -0.3075 -0.2030 824  PHE A C   
6256  O O   . PHE A 824  ? 2.1220 1.8124 1.8269 0.4034  -0.3011 -0.1899 824  PHE A O   
6257  C CB  . PHE A 824  ? 2.2038 2.0491 1.9851 0.4016  -0.2760 -0.1953 824  PHE A CB  
6258  C CG  . PHE A 824  ? 2.2477 2.1055 2.0001 0.4343  -0.2650 -0.1839 824  PHE A CG  
6259  C CD1 . PHE A 824  ? 2.2638 2.1614 2.0318 0.4507  -0.2793 -0.1993 824  PHE A CD1 
6260  C CD2 . PHE A 824  ? 2.2954 2.1240 2.0041 0.4489  -0.2399 -0.1578 824  PHE A CD2 
6261  C CE1 . PHE A 824  ? 2.2848 2.1926 2.0259 0.4809  -0.2682 -0.1884 824  PHE A CE1 
6262  C CE2 . PHE A 824  ? 2.3185 2.1562 1.9997 0.4787  -0.2288 -0.1472 824  PHE A CE2 
6263  C CZ  . PHE A 824  ? 2.3090 2.1862 2.0065 0.4946  -0.2426 -0.1623 824  PHE A CZ  
6264  N N   . LEU A 825  ? 2.0882 1.8276 1.8681 0.3718  -0.3322 -0.2271 825  LEU A N   
6265  C CA  . LEU A 825  ? 2.0134 1.7335 1.7882 0.3778  -0.3527 -0.2389 825  LEU A CA  
6266  C C   . LEU A 825  ? 1.9869 1.7862 1.7960 0.3959  -0.3628 -0.2572 825  LEU A C   
6267  O O   . LEU A 825  ? 1.9748 1.8412 1.8259 0.3926  -0.3649 -0.2709 825  LEU A O   
6268  C CB  . LEU A 825  ? 1.9432 1.6126 1.7272 0.3504  -0.3751 -0.2526 825  LEU A CB  
6269  C CG  . LEU A 825  ? 1.8301 1.5087 1.6281 0.3561  -0.3997 -0.2724 825  LEU A CG  
6270  C CD1 . LEU A 825  ? 1.7962 1.4206 1.5499 0.3700  -0.3999 -0.2605 825  LEU A CD1 
6271  C CD2 . LEU A 825  ? 1.8036 1.4632 1.6291 0.3296  -0.4229 -0.2925 825  LEU A CD2 
6272  N N   . GLU A 826  ? 1.9605 1.7507 1.7511 0.4147  -0.3691 -0.2574 826  GLU A N   
6273  C CA  . GLU A 826  ? 1.9327 1.7857 1.7520 0.4313  -0.3824 -0.2759 826  GLU A CA  
6274  C C   . GLU A 826  ? 1.9230 1.7340 1.7390 0.4245  -0.4070 -0.2890 826  GLU A C   
6275  O O   . GLU A 826  ? 1.9171 1.6560 1.6956 0.4208  -0.4072 -0.2773 826  GLU A O   
6276  C CB  . GLU A 826  ? 1.9464 1.8313 1.7445 0.4645  -0.3645 -0.2622 826  GLU A CB  
6277  C CG  . GLU A 826  ? 2.0049 1.8208 1.7521 0.4743  -0.3578 -0.2445 826  GLU A CG  
6278  C CD  . GLU A 826  ? 2.0436 1.8908 1.7722 0.5075  -0.3427 -0.2340 826  GLU A CD  
6279  O OE1 . GLU A 826  ? 2.0611 1.8683 1.7614 0.5172  -0.3457 -0.2291 826  GLU A OE1 
6280  O OE2 . GLU A 826  ? 2.0470 1.9584 1.7892 0.5239  -0.3277 -0.2307 826  GLU A OE2 
6281  N N   . MET A 827  ? 1.9122 1.7685 1.7674 0.4228  -0.4280 -0.3136 827  MET A N   
6282  C CA  . MET A 827  ? 1.8918 1.7188 1.7476 0.4196  -0.4517 -0.3276 827  MET A CA  
6283  C C   . MET A 827  ? 1.8399 1.7224 1.7063 0.4469  -0.4564 -0.3362 827  MET A C   
6284  O O   . MET A 827  ? 1.8453 1.8029 1.7421 0.4583  -0.4539 -0.3457 827  MET A O   
6285  C CB  . MET A 827  ? 1.8941 1.7269 1.7881 0.3946  -0.4737 -0.3508 827  MET A CB  
6286  C CG  . MET A 827  ? 1.9095 1.6943 1.7995 0.3665  -0.4701 -0.3449 827  MET A CG  
6287  S SD  . MET A 827  ? 1.7881 1.4688 1.6330 0.3556  -0.4771 -0.3334 827  MET A SD  
6288  C CE  . MET A 827  ? 1.3916 1.0786 1.2492 0.3638  -0.5049 -0.3545 827  MET A CE  
6289  N N   . ASN A 828  ? 1.8125 1.6600 1.6545 0.4579  -0.4631 -0.3334 828  ASN A N   
6290  C CA  . ASN A 828  ? 1.7788 1.6769 1.6313 0.4836  -0.4683 -0.3422 828  ASN A CA  
6291  C C   . ASN A 828  ? 1.6936 1.6091 1.5787 0.4769  -0.4972 -0.3687 828  ASN A C   
6292  O O   . ASN A 828  ? 1.6902 1.5575 1.5614 0.4725  -0.5116 -0.3719 828  ASN A O   
6293  C CB  . ASN A 828  ? 1.8879 1.7497 1.6976 0.5035  -0.4568 -0.3240 828  ASN A CB  
6294  C CG  . ASN A 828  ? 1.9772 1.9021 1.7931 0.5354  -0.4501 -0.3253 828  ASN A CG  
6295  O OD1 . ASN A 828  ? 2.0105 1.9927 1.8375 0.5495  -0.4349 -0.3215 828  ASN A OD1 
6296  N ND2 . ASN A 828  ? 2.0145 1.9303 1.8238 0.5476  -0.4613 -0.3307 828  ASN A ND2 
6297  N N   . ILE A 829  ? 1.5859 1.5704 1.5140 0.4765  -0.5055 -0.3879 829  ILE A N   
6298  C CA  . ILE A 829  ? 1.4601 1.4697 1.4208 0.4729  -0.5318 -0.4141 829  ILE A CA  
6299  C C   . ILE A 829  ? 1.3720 1.4265 1.3327 0.5041  -0.5324 -0.4170 829  ILE A C   
6300  O O   . ILE A 829  ? 1.3861 1.4780 1.3369 0.5269  -0.5127 -0.4043 829  ILE A O   
6301  C CB  . ILE A 829  ? 1.4024 1.4684 1.4091 0.4593  -0.5397 -0.4339 829  ILE A CB  
6302  C CG1 . ILE A 829  ? 1.3845 1.4182 1.3887 0.4337  -0.5295 -0.4248 829  ILE A CG1 
6303  C CG2 . ILE A 829  ? 1.3749 1.4446 1.4109 0.4471  -0.5682 -0.4603 829  ILE A CG2 
6304  C CD1 . ILE A 829  ? 1.3907 1.3433 1.3799 0.4080  -0.5412 -0.4245 829  ILE A CD1 
6305  N N   . PRO A 830  ? 1.3010 1.3506 1.2712 0.5060  -0.5541 -0.4329 830  PRO A N   
6306  C CA  . PRO A 830  ? 1.3414 1.4292 1.3119 0.5348  -0.5567 -0.4368 830  PRO A CA  
6307  C C   . PRO A 830  ? 1.5055 1.6802 1.5170 0.5456  -0.5630 -0.4562 830  PRO A C   
6308  O O   . PRO A 830  ? 1.6486 1.8489 1.6897 0.5281  -0.5685 -0.4688 830  PRO A O   
6309  C CB  . PRO A 830  ? 1.2442 1.2918 1.2150 0.5264  -0.5808 -0.4496 830  PRO A CB  
6310  C CG  . PRO A 830  ? 1.2095 1.2002 1.1799 0.4944  -0.5900 -0.4522 830  PRO A CG  
6311  C CD  . PRO A 830  ? 1.2245 1.2360 1.2085 0.4813  -0.5780 -0.4495 830  PRO A CD  
6312  N N   . TYR A 831  ? 1.5126 1.7340 1.5271 0.5742  -0.5625 -0.4594 831  TYR A N   
6313  C CA  . TYR A 831  ? 1.5019 1.8025 1.5569 0.5835  -0.5740 -0.4819 831  TYR A CA  
6314  C C   . TYR A 831  ? 1.4566 1.7374 1.5358 0.5602  -0.6018 -0.5051 831  TYR A C   
6315  O O   . TYR A 831  ? 1.4664 1.7546 1.5710 0.5372  -0.6097 -0.5177 831  TYR A O   
6316  C CB  . TYR A 831  ? 1.5424 1.8862 1.5935 0.6178  -0.5716 -0.4821 831  TYR A CB  
6317  C CG  . TYR A 831  ? 1.5723 2.0049 1.6625 0.6325  -0.5808 -0.5035 831  TYR A CG  
6318  C CD1 . TYR A 831  ? 1.5677 2.0302 1.6685 0.6515  -0.5952 -0.5175 831  TYR A CD1 
6319  C CD2 . TYR A 831  ? 1.5737 2.0609 1.6898 0.6278  -0.5750 -0.5098 831  TYR A CD2 
6320  C CE1 . TYR A 831  ? 1.5673 2.1101 1.7020 0.6660  -0.6038 -0.5372 831  TYR A CE1 
6321  C CE2 . TYR A 831  ? 1.5749 2.1440 1.7263 0.6415  -0.5840 -0.5302 831  TYR A CE2 
6322  C CZ  . TYR A 831  ? 1.5734 2.1696 1.7333 0.6610  -0.5985 -0.5438 831  TYR A CZ  
6323  O OH  . TYR A 831  ? 1.5743 2.2525 1.7683 0.6759  -0.6082 -0.5647 831  TYR A OH  
6324  N N   . SER A 832  ? 1.4247 1.6762 1.4949 0.5650  -0.6164 -0.5101 832  SER A N   
6325  C CA  . SER A 832  ? 1.4561 1.7044 1.5534 0.5487  -0.6434 -0.5349 832  SER A CA  
6326  C C   . SER A 832  ? 1.4521 1.6242 1.5271 0.5370  -0.6554 -0.5317 832  SER A C   
6327  O O   . SER A 832  ? 1.4608 1.5969 1.5026 0.5492  -0.6457 -0.5139 832  SER A O   
6328  C CB  . SER A 832  ? 1.4762 1.7960 1.6009 0.5712  -0.6556 -0.5546 832  SER A CB  
6329  O OG  . SER A 832  ? 1.5024 1.8195 1.6039 0.5979  -0.6503 -0.5441 832  SER A OG  
6330  N N   . VAL A 833  ? 1.4445 1.5940 1.5386 0.5135  -0.6768 -0.5499 833  VAL A N   
6331  C CA  . VAL A 833  ? 1.4275 1.5075 1.5051 0.5006  -0.6918 -0.5506 833  VAL A CA  
6332  C C   . VAL A 833  ? 1.3848 1.4846 1.4922 0.4972  -0.7185 -0.5777 833  VAL A C   
6333  O O   . VAL A 833  ? 1.3736 1.5146 1.5146 0.4879  -0.7272 -0.5967 833  VAL A O   
6334  C CB  . VAL A 833  ? 1.4396 1.4560 1.5070 0.4696  -0.6911 -0.5442 833  VAL A CB  
6335  C CG1 . VAL A 833  ? 1.4538 1.3914 1.4843 0.4645  -0.6927 -0.5298 833  VAL A CG1 
6336  C CG2 . VAL A 833  ? 1.4518 1.4794 1.5138 0.4650  -0.6680 -0.5289 833  VAL A CG2 
6337  N N   . VAL A 834  ? 1.3819 1.4511 1.4770 0.5040  -0.7315 -0.5798 834  VAL A N   
6338  C CA  . VAL A 834  ? 1.3772 1.4531 1.4962 0.4991  -0.7578 -0.6045 834  VAL A CA  
6339  C C   . VAL A 834  ? 1.4344 1.4557 1.5581 0.4671  -0.7716 -0.6129 834  VAL A C   
6340  O O   . VAL A 834  ? 1.4523 1.4119 1.5508 0.4510  -0.7636 -0.5968 834  VAL A O   
6341  C CB  . VAL A 834  ? 1.3611 1.4201 1.4641 0.5170  -0.7664 -0.6027 834  VAL A CB  
6342  C CG1 . VAL A 834  ? 1.3658 1.4124 1.4869 0.5076  -0.7937 -0.6252 834  VAL A CG1 
6343  C CG2 . VAL A 834  ? 1.3297 1.4518 1.4358 0.5495  -0.7568 -0.6003 834  VAL A CG2 
6344  N N   . ARG A 835  ? 1.4754 1.5192 1.6306 0.4584  -0.7920 -0.6384 835  ARG A N   
6345  C CA  . ARG A 835  ? 1.5505 1.5438 1.7115 0.4295  -0.8066 -0.6486 835  ARG A CA  
6346  C C   . ARG A 835  ? 1.5681 1.4879 1.6992 0.4252  -0.8146 -0.6393 835  ARG A C   
6347  O O   . ARG A 835  ? 1.5633 1.4856 1.6877 0.4429  -0.8236 -0.6415 835  ARG A O   
6348  C CB  . ARG A 835  ? 1.5777 1.6112 1.7774 0.4245  -0.8279 -0.6791 835  ARG A CB  
6349  C CG  . ARG A 835  ? 1.6277 1.6075 1.8281 0.4070  -0.8500 -0.6922 835  ARG A CG  
6350  C CD  . ARG A 835  ? 1.6608 1.6703 1.8993 0.3925  -0.8666 -0.7206 835  ARG A CD  
6351  N NE  . ARG A 835  ? 1.6482 1.7114 1.9109 0.4100  -0.8836 -0.7431 835  ARG A NE  
6352  C CZ  . ARG A 835  ? 1.6261 1.7118 1.8803 0.4373  -0.8865 -0.7409 835  ARG A CZ  
6353  N NH1 . ARG A 835  ? 1.6079 1.6684 1.8301 0.4512  -0.8734 -0.7172 835  ARG A NH1 
6354  N NH2 . ARG A 835  ? 1.6125 1.7467 1.8909 0.4508  -0.9025 -0.7632 835  ARG A NH2 
6355  N N   . GLY A 836  ? 1.6181 1.4736 1.7311 0.4022  -0.8109 -0.6285 836  GLY A N   
6356  C CA  . GLY A 836  ? 1.6517 1.4349 1.7368 0.3954  -0.8195 -0.6206 836  GLY A CA  
6357  C C   . GLY A 836  ? 1.6665 1.4247 1.7160 0.4116  -0.8065 -0.5976 836  GLY A C   
6358  O O   . GLY A 836  ? 1.6553 1.3694 1.6854 0.4133  -0.8162 -0.5941 836  GLY A O   
6359  N N   . GLU A 837  ? 1.6605 1.4497 1.7025 0.4240  -0.7848 -0.5828 837  GLU A N   
6360  C CA  . GLU A 837  ? 1.6719 1.4355 1.6784 0.4365  -0.7674 -0.5584 837  GLU A CA  
6361  C C   . GLU A 837  ? 1.7381 1.4527 1.7256 0.4151  -0.7540 -0.5429 837  GLU A C   
6362  O O   . GLU A 837  ? 1.7461 1.4836 1.7524 0.4033  -0.7483 -0.5474 837  GLU A O   
6363  C CB  . GLU A 837  ? 1.6344 1.4637 1.6466 0.4613  -0.7503 -0.5526 837  GLU A CB  
6364  C CG  . GLU A 837  ? 1.4793 1.3222 1.4769 0.4885  -0.7475 -0.5457 837  GLU A CG  
6365  C CD  . GLU A 837  ? 1.4004 1.3192 1.4115 0.5145  -0.7346 -0.5457 837  GLU A CD  
6366  O OE1 . GLU A 837  ? 1.3959 1.3493 1.4187 0.5121  -0.7221 -0.5443 837  GLU A OE1 
6367  O OE2 . GLU A 837  ? 1.3442 1.2886 1.3540 0.5377  -0.7364 -0.5469 837  GLU A OE2 
6368  N N   . GLN A 838  ? 1.7809 1.4292 1.7325 0.4095  -0.7494 -0.5255 838  GLN A N   
6369  C CA  . GLN A 838  ? 1.8063 1.4041 1.7362 0.3902  -0.7361 -0.5094 838  GLN A CA  
6370  C C   . GLN A 838  ? 1.7972 1.4040 1.7047 0.4019  -0.7091 -0.4868 838  GLN A C   
6371  O O   . GLN A 838  ? 1.7613 1.3489 1.6411 0.4156  -0.7010 -0.4723 838  GLN A O   
6372  C CB  . GLN A 838  ? 1.8458 1.3652 1.7487 0.3763  -0.7464 -0.5036 838  GLN A CB  
6373  C CG  . GLN A 838  ? 1.9343 1.3961 1.8092 0.3588  -0.7326 -0.4852 838  GLN A CG  
6374  C CD  . GLN A 838  ? 2.0755 1.4637 1.9146 0.3536  -0.7385 -0.4743 838  GLN A CD  
6375  O OE1 . GLN A 838  ? 2.1275 1.4736 1.9662 0.3378  -0.7547 -0.4823 838  GLN A OE1 
6376  N NE2 . GLN A 838  ? 2.0918 1.4647 1.9004 0.3672  -0.7253 -0.4563 838  GLN A NE2 
6377  N N   . ILE A 839  ? 1.8107 1.4469 1.7306 0.3963  -0.6951 -0.4841 839  ILE A N   
6378  C CA  . ILE A 839  ? 1.8128 1.4751 1.7187 0.4116  -0.6700 -0.4661 839  ILE A CA  
6379  C C   . ILE A 839  ? 1.8711 1.4807 1.7455 0.3987  -0.6515 -0.4440 839  ILE A C   
6380  O O   . ILE A 839  ? 1.9103 1.4881 1.7878 0.3758  -0.6546 -0.4457 839  ILE A O   
6381  C CB  . ILE A 839  ? 1.7960 1.5373 1.7375 0.4186  -0.6649 -0.4773 839  ILE A CB  
6382  C CG1 . ILE A 839  ? 1.7807 1.5621 1.7105 0.4424  -0.6416 -0.4616 839  ILE A CG1 
6383  C CG2 . ILE A 839  ? 1.8023 1.5389 1.7598 0.3944  -0.6627 -0.4811 839  ILE A CG2 
6384  C CD1 . ILE A 839  ? 1.7663 1.5785 1.6936 0.4696  -0.6441 -0.4636 839  ILE A CD1 
6385  N N   . GLN A 840  ? 1.8645 1.4642 1.7081 0.4136  -0.6319 -0.4233 840  GLN A N   
6386  C CA  . GLN A 840  ? 1.8826 1.4375 1.6955 0.4041  -0.6125 -0.4018 840  GLN A CA  
6387  C C   . GLN A 840  ? 1.7951 1.3965 1.6140 0.4120  -0.5896 -0.3923 840  GLN A C   
6388  O O   . GLN A 840  ? 1.7608 1.3960 1.5715 0.4346  -0.5751 -0.3833 840  GLN A O   
6389  C CB  . GLN A 840  ? 1.9760 1.4773 1.7460 0.4120  -0.6051 -0.3837 840  GLN A CB  
6390  C CG  . GLN A 840  ? 2.1153 1.5419 1.8557 0.3915  -0.6020 -0.3710 840  GLN A CG  
6391  C CD  . GLN A 840  ? 2.2195 1.6164 1.9199 0.3993  -0.5778 -0.3461 840  GLN A CD  
6392  O OE1 . GLN A 840  ? 2.2878 1.6186 1.9551 0.3894  -0.5762 -0.3341 840  GLN A OE1 
6393  N NE2 . GLN A 840  ? 2.2163 1.6619 1.9187 0.4178  -0.5588 -0.3382 840  GLN A NE2 
6394  N N   . LEU A 841  ? 1.7669 1.3683 1.5994 0.3932  -0.5860 -0.3937 841  LEU A N   
6395  C CA  . LEU A 841  ? 1.7090 1.3605 1.5544 0.3979  -0.5669 -0.3881 841  LEU A CA  
6396  C C   . LEU A 841  ? 1.7018 1.3165 1.5117 0.3967  -0.5423 -0.3624 841  LEU A C   
6397  O O   . LEU A 841  ? 1.6961 1.2733 1.5000 0.3758  -0.5385 -0.3568 841  LEU A O   
6398  C CB  . LEU A 841  ? 1.6755 1.3522 1.5591 0.3773  -0.5763 -0.4051 841  LEU A CB  
6399  C CG  . LEU A 841  ? 1.5851 1.3368 1.5121 0.3859  -0.5898 -0.4287 841  LEU A CG  
6400  C CD1 . LEU A 841  ? 1.5640 1.3421 1.5275 0.3647  -0.5946 -0.4434 841  LEU A CD1 
6401  C CD2 . LEU A 841  ? 1.5393 1.3518 1.4661 0.4143  -0.5736 -0.4214 841  LEU A CD2 
6402  N N   . LYS A 842  ? 1.6997 1.3262 1.4861 0.4194  -0.5246 -0.3468 842  LYS A N   
6403  C CA  . LYS A 842  ? 1.7305 1.3200 1.4802 0.4199  -0.5009 -0.3221 842  LYS A CA  
6404  C C   . LYS A 842  ? 1.7499 1.3845 1.5116 0.4222  -0.4808 -0.3149 842  LYS A C   
6405  O O   . LYS A 842  ? 1.7242 1.4191 1.5251 0.4203  -0.4856 -0.3297 842  LYS A O   
6406  C CB  . LYS A 842  ? 1.7279 1.2979 1.4413 0.4414  -0.4894 -0.3066 842  LYS A CB  
6407  C CG  . LYS A 842  ? 1.7381 1.2589 1.4357 0.4388  -0.5070 -0.3111 842  LYS A CG  
6408  C CD  . LYS A 842  ? 1.7566 1.2624 1.4203 0.4599  -0.4937 -0.2958 842  LYS A CD  
6409  C CE  . LYS A 842  ? 1.7726 1.2578 1.4328 0.4639  -0.5124 -0.3050 842  LYS A CE  
6410  N NZ  . LYS A 842  ? 1.8057 1.2848 1.4361 0.4858  -0.4969 -0.2903 842  LYS A NZ  
6411  N N   . GLY A 843  ? 1.7918 1.3948 1.5180 0.4260  -0.4581 -0.2916 843  GLY A N   
6412  C CA  . GLY A 843  ? 1.8320 1.4650 1.5617 0.4270  -0.4366 -0.2805 843  GLY A CA  
6413  C C   . GLY A 843  ? 1.8877 1.4582 1.5707 0.4249  -0.4167 -0.2553 843  GLY A C   
6414  O O   . GLY A 843  ? 1.9157 1.4175 1.5690 0.4166  -0.4230 -0.2495 843  GLY A O   
6415  N N   . THR A 844  ? 1.9675 1.5617 1.6431 0.4331  -0.3929 -0.2403 844  THR A N   
6416  C CA  . THR A 844  ? 2.0389 1.5748 1.6702 0.4308  -0.3728 -0.2161 844  THR A CA  
6417  C C   . THR A 844  ? 2.0167 1.5690 1.6595 0.4187  -0.3580 -0.2091 844  THR A C   
6418  O O   . THR A 844  ? 1.9840 1.6062 1.6637 0.4221  -0.3560 -0.2184 844  THR A O   
6419  C CB  . THR A 844  ? 1.8198 1.3465 1.4119 0.4580  -0.3549 -0.1984 844  THR A CB  
6420  O OG1 . THR A 844  ? 1.8058 1.3866 1.3998 0.4776  -0.3318 -0.1877 844  THR A OG1 
6421  C CG2 . THR A 844  ? 1.7178 1.2570 1.3153 0.4721  -0.3706 -0.2106 844  THR A CG2 
6422  N N   . VAL A 845  ? 2.0534 1.5426 1.6680 0.4030  -0.3497 -0.1946 845  VAL A N   
6423  C CA  . VAL A 845  ? 2.0743 1.5751 1.7010 0.3892  -0.3368 -0.1886 845  VAL A CA  
6424  C C   . VAL A 845  ? 2.0836 1.5705 1.6741 0.4015  -0.3077 -0.1629 845  VAL A C   
6425  O O   . VAL A 845  ? 2.0857 1.5080 1.6313 0.4034  -0.3000 -0.1468 845  VAL A O   
6426  C CB  . VAL A 845  ? 1.6432 1.0920 1.2750 0.3584  -0.3496 -0.1941 845  VAL A CB  
6427  C CG1 . VAL A 845  ? 1.6681 1.0275 1.2528 0.3522  -0.3514 -0.1816 845  VAL A CG1 
6428  C CG2 . VAL A 845  ? 1.6425 1.1091 1.2893 0.3453  -0.3345 -0.1877 845  VAL A CG2 
6429  N N   . TYR A 846  ? 2.0859 1.6351 1.6965 0.4102  -0.2918 -0.1595 846  TYR A N   
6430  C CA  . TYR A 846  ? 2.1042 1.6552 1.6826 0.4293  -0.2635 -0.1362 846  TYR A CA  
6431  C C   . TYR A 846  ? 2.2085 1.7244 1.7687 0.4158  -0.2460 -0.1189 846  TYR A C   
6432  O O   . TYR A 846  ? 2.1946 1.7419 1.7857 0.4016  -0.2441 -0.1237 846  TYR A O   
6433  C CB  . TYR A 846  ? 1.9986 1.6360 1.5994 0.4547  -0.2532 -0.1388 846  TYR A CB  
6434  C CG  . TYR A 846  ? 1.9056 1.5586 1.5045 0.4744  -0.2639 -0.1475 846  TYR A CG  
6435  C CD1 . TYR A 846  ? 1.8435 1.5738 1.4814 0.4871  -0.2729 -0.1647 846  TYR A CD1 
6436  C CD2 . TYR A 846  ? 1.8962 1.4846 1.4544 0.4791  -0.2659 -0.1392 846  TYR A CD2 
6437  C CE1 . TYR A 846  ? 1.8023 1.5434 1.4369 0.5051  -0.2824 -0.1720 846  TYR A CE1 
6438  C CE2 . TYR A 846  ? 1.8479 1.4475 1.4042 0.4959  -0.2752 -0.1467 846  TYR A CE2 
6439  C CZ  . TYR A 846  ? 1.8014 1.4760 1.3951 0.5090  -0.2831 -0.1626 846  TYR A CZ  
6440  O OH  . TYR A 846  ? 1.7733 1.4546 1.3627 0.5258  -0.2917 -0.1689 846  TYR A OH  
6441  N N   . ASN A 847  ? 2.3458 1.7935 1.8548 0.4197  -0.2339 -0.0993 847  ASN A N   
6442  C CA  . ASN A 847  ? 2.4714 1.8821 1.9523 0.4135  -0.2128 -0.0784 847  ASN A CA  
6443  C C   . ASN A 847  ? 2.5123 1.9454 1.9671 0.4402  -0.1856 -0.0590 847  ASN A C   
6444  O O   . ASN A 847  ? 2.4820 1.8975 1.9059 0.4595  -0.1807 -0.0518 847  ASN A O   
6445  C CB  . ASN A 847  ? 2.5532 1.8692 1.9924 0.3990  -0.2173 -0.0693 847  ASN A CB  
6446  C CG  . ASN A 847  ? 2.6365 1.9165 2.0620 0.3827  -0.2033 -0.0548 847  ASN A CG  
6447  O OD1 . ASN A 847  ? 2.6631 1.9681 2.0832 0.3915  -0.1801 -0.0402 847  ASN A OD1 
6448  N ND2 . ASN A 847  ? 2.6691 1.8904 2.0884 0.3596  -0.2172 -0.0587 847  ASN A ND2 
6449  N N   . TYR A 848  ? 2.5826 2.0536 2.0500 0.4409  -0.1677 -0.0505 848  TYR A N   
6450  C CA  . TYR A 848  ? 2.6345 2.1377 2.0835 0.4664  -0.1413 -0.0331 848  TYR A CA  
6451  C C   . TYR A 848  ? 2.6941 2.1696 2.1218 0.4590  -0.1197 -0.0132 848  TYR A C   
6452  O O   . TYR A 848  ? 2.7021 2.1900 2.1065 0.4782  -0.0949 0.0053  848  TYR A O   
6453  C CB  . TYR A 848  ? 2.6114 2.2121 2.1062 0.4801  -0.1418 -0.0459 848  TYR A CB  
6454  C CG  . TYR A 848  ? 2.5820 2.2102 2.0789 0.5016  -0.1509 -0.0554 848  TYR A CG  
6455  C CD1 . TYR A 848  ? 2.5826 2.1498 2.0424 0.5068  -0.1567 -0.0516 848  TYR A CD1 
6456  C CD2 . TYR A 848  ? 2.5395 2.2551 2.0741 0.5177  -0.1523 -0.0674 848  TYR A CD2 
6457  C CE1 . TYR A 848  ? 2.5579 2.1494 2.0191 0.5265  -0.1635 -0.0593 848  TYR A CE1 
6458  C CE2 . TYR A 848  ? 2.5144 2.2543 2.0493 0.5384  -0.1592 -0.0749 848  TYR A CE2 
6459  C CZ  . TYR A 848  ? 2.5375 2.2145 2.0358 0.5425  -0.1644 -0.0705 848  TYR A CZ  
6460  O OH  . TYR A 848  ? 2.5465 2.2469 2.0452 0.5629  -0.1704 -0.0775 848  TYR A OH  
6461  N N   . ARG A 849  ? 2.7424 2.1788 2.1776 0.4314  -0.1292 -0.0168 849  ARG A N   
6462  C CA  . ARG A 849  ? 2.8137 2.2051 2.2216 0.4217  -0.1111 0.0027  849  ARG A CA  
6463  C C   . ARG A 849  ? 2.8437 2.1616 2.1892 0.4340  -0.1003 0.0215  849  ARG A C   
6464  O O   . ARG A 849  ? 2.8240 2.1092 2.1529 0.4377  -0.1144 0.0152  849  ARG A O   
6465  C CB  . ARG A 849  ? 2.8777 2.2360 2.3052 0.3895  -0.1266 -0.0070 849  ARG A CB  
6466  C CG  . ARG A 849  ? 2.9812 2.2877 2.3820 0.3766  -0.1102 0.0118  849  ARG A CG  
6467  C CD  . ARG A 849  ? 3.0476 2.4036 2.4566 0.3856  -0.0840 0.0259  849  ARG A CD  
6468  N NE  . ARG A 849  ? 3.1271 2.4350 2.5149 0.3711  -0.0697 0.0425  849  ARG A NE  
6469  C CZ  . ARG A 849  ? 3.1638 2.4892 2.5411 0.3795  -0.0434 0.0611  849  ARG A CZ  
6470  N NH1 . ARG A 849  ? 3.1562 2.5466 2.5416 0.4030  -0.0284 0.0658  849  ARG A NH1 
6471  N NH2 . ARG A 849  ? 3.1944 2.4723 2.5523 0.3653  -0.0318 0.0755  849  ARG A NH2 
6472  N N   . THR A 850  ? 2.8797 2.1737 2.1910 0.4408  -0.0750 0.0443  850  THR A N   
6473  C CA  . THR A 850  ? 2.8988 2.1264 2.1493 0.4540  -0.0617 0.0633  850  THR A CA  
6474  C C   . THR A 850  ? 2.9274 2.0695 2.1502 0.4357  -0.0777 0.0614  850  THR A C   
6475  O O   . THR A 850  ? 2.9661 2.0594 2.1494 0.4449  -0.0788 0.0667  850  THR A O   
6476  C CB  . THR A 850  ? 2.8953 2.1136 2.1160 0.4632  -0.0314 0.0879  850  THR A CB  
6477  O OG1 . THR A 850  ? 2.8920 2.1091 2.1328 0.4413  -0.0299 0.0890  850  THR A OG1 
6478  C CG2 . THR A 850  ? 2.8685 2.1608 2.1008 0.4893  -0.0126 0.0937  850  THR A CG2 
6479  N N   . SER A 851  ? 2.9294 2.0539 2.1726 0.4098  -0.0894 0.0542  851  SER A N   
6480  C CA  . SER A 851  ? 2.9646 2.0148 2.1891 0.3905  -0.1078 0.0494  851  SER A CA  
6481  C C   . SER A 851  ? 2.9561 2.0251 2.2190 0.3792  -0.1379 0.0238  851  SER A C   
6482  O O   . SER A 851  ? 2.8959 2.0365 2.2029 0.3838  -0.1445 0.0093  851  SER A O   
6483  C CB  . SER A 851  ? 3.0142 2.0265 2.2336 0.3695  -0.1021 0.0581  851  SER A CB  
6484  O OG  . SER A 851  ? 3.0231 2.0925 2.2946 0.3561  -0.1046 0.0477  851  SER A OG  
6485  N N   . GLY A 852  ? 3.0096 2.0149 2.2551 0.3653  -0.1562 0.0182  852  GLY A N   
6486  C CA  . GLY A 852  ? 2.9805 1.9962 2.2592 0.3536  -0.1848 -0.0053 852  GLY A CA  
6487  C C   . GLY A 852  ? 2.9117 1.9410 2.2297 0.3293  -0.1947 -0.0163 852  GLY A C   
6488  O O   . GLY A 852  ? 2.9288 1.9606 2.2486 0.3219  -0.1787 -0.0054 852  GLY A O   
6489  N N   . MET A 853  ? 2.8241 1.8617 2.1736 0.3170  -0.2206 -0.0380 853  MET A N   
6490  C CA  . MET A 853  ? 2.7632 1.8023 2.1468 0.2919  -0.2320 -0.0495 853  MET A CA  
6491  C C   . MET A 853  ? 2.7011 1.7261 2.1052 0.2789  -0.2620 -0.0714 853  MET A C   
6492  O O   . MET A 853  ? 2.6753 1.6932 2.0700 0.2892  -0.2752 -0.0785 853  MET A O   
6493  C CB  . MET A 853  ? 2.7491 1.8670 2.1795 0.2905  -0.2227 -0.0550 853  MET A CB  
6494  C CG  . MET A 853  ? 2.7197 1.9132 2.1916 0.3012  -0.2344 -0.0742 853  MET A CG  
6495  S SD  . MET A 853  ? 3.0303 2.3164 2.5467 0.3050  -0.2175 -0.0753 853  MET A SD  
6496  C CE  . MET A 853  ? 3.1701 2.4544 2.6410 0.3319  -0.1857 -0.0473 853  MET A CE  
6497  N N   . GLN A 854  ? 2.6794 1.6986 2.1108 0.2559  -0.2720 -0.0813 854  GLN A N   
6498  C CA  . GLN A 854  ? 2.6509 1.6573 2.1035 0.2425  -0.2997 -0.1022 854  GLN A CA  
6499  C C   . GLN A 854  ? 2.5937 1.6777 2.1045 0.2390  -0.3102 -0.1236 854  GLN A C   
6500  O O   . GLN A 854  ? 2.5843 1.7115 2.1238 0.2323  -0.2986 -0.1236 854  GLN A O   
6501  C CB  . GLN A 854  ? 2.6899 1.6327 2.1319 0.2191  -0.3048 -0.0996 854  GLN A CB  
6502  C CG  . GLN A 854  ? 2.7269 1.5974 2.1126 0.2216  -0.2907 -0.0766 854  GLN A CG  
6503  C CD  . GLN A 854  ? 2.7625 1.5664 2.1348 0.2001  -0.2974 -0.0745 854  GLN A CD  
6504  O OE1 . GLN A 854  ? 2.7564 1.5694 2.1633 0.1819  -0.3095 -0.0888 854  GLN A OE1 
6505  N NE2 . GLN A 854  ? 2.7936 1.5290 2.1145 0.2025  -0.2892 -0.0566 854  GLN A NE2 
6506  N N   . PHE A 855  ? 2.5421 1.6452 2.0703 0.2441  -0.3317 -0.1420 855  PHE A N   
6507  C CA  . PHE A 855  ? 2.4702 1.6384 2.0535 0.2381  -0.3464 -0.1656 855  PHE A CA  
6508  C C   . PHE A 855  ? 2.4899 1.6291 2.0898 0.2200  -0.3730 -0.1847 855  PHE A C   
6509  O O   . PHE A 855  ? 2.5359 1.6046 2.1089 0.2076  -0.3782 -0.1789 855  PHE A O   
6510  C CB  . PHE A 855  ? 2.3797 1.6156 1.9796 0.2614  -0.3473 -0.1732 855  PHE A CB  
6511  C CG  . PHE A 855  ? 2.3176 1.5278 1.8913 0.2766  -0.3587 -0.1744 855  PHE A CG  
6512  C CD1 . PHE A 855  ? 2.2838 1.5032 1.8795 0.2743  -0.3840 -0.1954 855  PHE A CD1 
6513  C CD2 . PHE A 855  ? 2.3014 1.4814 1.8297 0.2939  -0.3436 -0.1549 855  PHE A CD2 
6514  C CE1 . PHE A 855  ? 2.2679 1.4665 1.8412 0.2885  -0.3939 -0.1965 855  PHE A CE1 
6515  C CE2 . PHE A 855  ? 2.2840 1.4427 1.7902 0.3074  -0.3535 -0.1565 855  PHE A CE2 
6516  C CZ  . PHE A 855  ? 2.2647 1.4334 1.7938 0.3046  -0.3786 -0.1771 855  PHE A CZ  
6517  N N   . CYS A 856  ? 2.4552 1.6491 2.0987 0.2192  -0.3897 -0.2074 856  CYS A N   
6518  C CA  . CYS A 856  ? 2.4682 1.6416 2.1311 0.2033  -0.4154 -0.2274 856  CYS A CA  
6519  C C   . CYS A 856  ? 2.4623 1.7110 2.1757 0.2061  -0.4294 -0.2515 856  CYS A C   
6520  O O   . CYS A 856  ? 2.4584 1.7398 2.2102 0.1904  -0.4313 -0.2635 856  CYS A O   
6521  C CB  . CYS A 856  ? 2.4942 1.6260 2.1615 0.1768  -0.4144 -0.2261 856  CYS A CB  
6522  S SG  . CYS A 856  ? 2.9744 2.0839 2.6707 0.1543  -0.4435 -0.2512 856  CYS A SG  
6523  N N   . VAL A 857  ? 2.4505 1.7271 2.1644 0.2257  -0.4389 -0.2588 857  VAL A N   
6524  C CA  . VAL A 857  ? 2.4074 1.7600 2.1672 0.2320  -0.4508 -0.2808 857  VAL A CA  
6525  C C   . VAL A 857  ? 2.4152 1.7570 2.1988 0.2183  -0.4781 -0.3039 857  VAL A C   
6526  O O   . VAL A 857  ? 2.4408 1.7315 2.2011 0.2188  -0.4920 -0.3046 857  VAL A O   
6527  C CB  . VAL A 857  ? 2.3580 1.7495 2.1097 0.2603  -0.4485 -0.2790 857  VAL A CB  
6528  C CG1 . VAL A 857  ? 2.3497 1.7675 2.0857 0.2757  -0.4212 -0.2591 857  VAL A CG1 
6529  C CG2 . VAL A 857  ? 2.3571 1.6906 2.0717 0.2679  -0.4586 -0.2741 857  VAL A CG2 
6530  N N   . LYS A 858  ? 2.3967 1.7876 2.2268 0.2065  -0.4859 -0.3231 858  LYS A N   
6531  C CA  . LYS A 858  ? 2.4074 1.7908 2.2623 0.1932  -0.5113 -0.3462 858  LYS A CA  
6532  C C   . LYS A 858  ? 2.3473 1.8128 2.2490 0.2003  -0.5225 -0.3694 858  LYS A C   
6533  O O   . LYS A 858  ? 2.3369 1.8638 2.2654 0.2022  -0.5110 -0.3716 858  LYS A O   
6534  C CB  . LYS A 858  ? 2.4914 1.8307 2.3533 0.1643  -0.5131 -0.3483 858  LYS A CB  
6535  C CG  . LYS A 858  ? 2.5506 1.9288 2.4406 0.1513  -0.4967 -0.3472 858  LYS A CG  
6536  C CD  . LYS A 858  ? 2.6260 1.9572 2.5230 0.1221  -0.4989 -0.3500 858  LYS A CD  
6537  C CE  . LYS A 858  ? 2.6556 2.0350 2.5892 0.1077  -0.4851 -0.3533 858  LYS A CE  
6538  N NZ  . LYS A 858  ? 2.6978 2.0274 2.6343 0.0796  -0.4826 -0.3521 858  LYS A NZ  
6539  N N   . MET A 859  ? 2.2972 1.7637 2.2076 0.2053  -0.5451 -0.3865 859  MET A N   
6540  C CA  . MET A 859  ? 2.2167 1.7565 2.1681 0.2140  -0.5583 -0.4094 859  MET A CA  
6541  C C   . MET A 859  ? 2.2017 1.7467 2.1905 0.1917  -0.5767 -0.4335 859  MET A C   
6542  O O   . MET A 859  ? 2.2223 1.7060 2.2004 0.1751  -0.5877 -0.4360 859  MET A O   
6543  C CB  . MET A 859  ? 2.1762 1.7195 2.1132 0.2367  -0.5702 -0.4125 859  MET A CB  
6544  C CG  . MET A 859  ? 2.1572 1.7181 2.1225 0.2345  -0.5963 -0.4385 859  MET A CG  
6545  S SD  . MET A 859  ? 1.6673 1.2103 1.6060 0.2583  -0.6090 -0.4372 859  MET A SD  
6546  C CE  . MET A 859  ? 2.5521 2.1840 2.5058 0.2878  -0.5974 -0.4372 859  MET A CE  
6547  N N   . SER A 860  ? 2.1832 1.8021 2.2154 0.1920  -0.5800 -0.4516 860  SER A N   
6548  C CA  . SER A 860  ? 2.2016 1.8323 2.2726 0.1698  -0.5949 -0.4751 860  SER A CA  
6549  C C   . SER A 860  ? 2.1989 1.8398 2.2873 0.1740  -0.6216 -0.4990 860  SER A C   
6550  O O   . SER A 860  ? 2.1794 1.8810 2.2854 0.1932  -0.6282 -0.5104 860  SER A O   
6551  C CB  . SER A 860  ? 2.2015 1.9073 2.3129 0.1653  -0.5848 -0.4837 860  SER A CB  
6552  O OG  . SER A 860  ? 2.2122 1.9609 2.3668 0.1572  -0.6040 -0.5127 860  SER A OG  
6553  N N   . ALA A 861  ? 2.2193 1.8011 2.3028 0.1562  -0.6365 -0.5065 861  ALA A N   
6554  C CA  . ALA A 861  ? 2.1846 1.7687 2.2841 0.1574  -0.6623 -0.5295 861  ALA A CA  
6555  C C   . ALA A 861  ? 2.1371 1.7950 2.2876 0.1533  -0.6721 -0.5564 861  ALA A C   
6556  O O   . ALA A 861  ? 2.1194 1.7759 2.2959 0.1296  -0.6749 -0.5688 861  ALA A O   
6557  C CB  . ALA A 861  ? 2.2101 1.7141 2.2942 0.1371  -0.6740 -0.5311 861  ALA A CB  
6558  N N   . VAL A 862  ? 2.1023 1.8241 2.2669 0.1763  -0.6773 -0.5655 862  VAL A N   
6559  C CA  . VAL A 862  ? 2.0878 1.8812 2.2995 0.1745  -0.6883 -0.5920 862  VAL A CA  
6560  C C   . VAL A 862  ? 2.0761 1.8647 2.2996 0.1764  -0.7147 -0.6148 862  VAL A C   
6561  O O   . VAL A 862  ? 2.0907 1.8597 2.2910 0.1943  -0.7232 -0.6106 862  VAL A O   
6562  C CB  . VAL A 862  ? 2.0769 1.9519 2.3019 0.1984  -0.6783 -0.5911 862  VAL A CB  
6563  C CG1 . VAL A 862  ? 2.0635 2.0121 2.3373 0.1965  -0.6917 -0.6203 862  VAL A CG1 
6564  C CG2 . VAL A 862  ? 2.0756 1.9599 2.2917 0.1963  -0.6519 -0.5697 862  VAL A CG2 
6565  N N   . GLU A 863  ? 2.0320 1.8420 2.2930 0.1583  -0.7271 -0.6392 863  GLU A N   
6566  C CA  . GLU A 863  ? 2.0058 1.7950 2.2775 0.1522  -0.7519 -0.6611 863  GLU A CA  
6567  C C   . GLU A 863  ? 1.9436 1.7201 2.1939 0.1757  -0.7662 -0.6613 863  GLU A C   
6568  O O   . GLU A 863  ? 1.9366 1.6505 2.1673 0.1699  -0.7784 -0.6612 863  GLU A O   
6569  C CB  . GLU A 863  ? 2.0670 1.9202 2.3882 0.1434  -0.7635 -0.6911 863  GLU A CB  
6570  C CG  . GLU A 863  ? 2.2291 2.0553 2.5725 0.1095  -0.7658 -0.7036 863  GLU A CG  
6571  C CD  . GLU A 863  ? 2.3097 2.0835 2.6523 0.0975  -0.7877 -0.7199 863  GLU A CD  
6572  O OE1 . GLU A 863  ? 2.3299 2.0416 2.6368 0.1041  -0.7929 -0.7077 863  GLU A OE1 
6573  O OE2 . GLU A 863  ? 2.3274 2.1218 2.7049 0.0812  -0.7993 -0.7451 863  GLU A OE2 
6574  N N   . GLY A 864  ? 1.8931 1.7291 2.1474 0.2023  -0.7647 -0.6616 864  GLY A N   
6575  C CA  . GLY A 864  ? 1.8787 1.7161 2.1226 0.2239  -0.7804 -0.6674 864  GLY A CA  
6576  C C   . GLY A 864  ? 1.8447 1.6389 2.0444 0.2407  -0.7727 -0.6428 864  GLY A C   
6577  O O   . GLY A 864  ? 1.8454 1.6469 2.0356 0.2615  -0.7826 -0.6449 864  GLY A O   
6578  N N   . ILE A 865  ? 1.8390 1.5872 2.0117 0.2313  -0.7550 -0.6196 865  ILE A N   
6579  C CA  . ILE A 865  ? 1.7956 1.5086 1.9264 0.2474  -0.7441 -0.5949 865  ILE A CA  
6580  C C   . ILE A 865  ? 1.8313 1.4550 1.9278 0.2323  -0.7442 -0.5804 865  ILE A C   
6581  O O   . ILE A 865  ? 1.8354 1.4249 1.9279 0.2113  -0.7348 -0.5729 865  ILE A O   
6582  C CB  . ILE A 865  ? 1.7397 1.4848 1.8623 0.2573  -0.7189 -0.5757 865  ILE A CB  
6583  C CG1 . ILE A 865  ? 1.6964 1.5329 1.8566 0.2688  -0.7172 -0.5905 865  ILE A CG1 
6584  C CG2 . ILE A 865  ? 1.7276 1.4493 1.8110 0.2787  -0.7096 -0.5541 865  ILE A CG2 
6585  C CD1 . ILE A 865  ? 1.6778 1.5517 1.8297 0.2828  -0.6928 -0.5721 865  ILE A CD1 
6586  N N   . CYS A 866  ? 1.8906 1.4780 1.9621 0.2440  -0.7547 -0.5764 866  CYS A N   
6587  C CA  . CYS A 866  ? 1.9881 1.4920 2.0244 0.2331  -0.7565 -0.5629 866  CYS A CA  
6588  C C   . CYS A 866  ? 2.1017 1.5753 2.1035 0.2350  -0.7337 -0.5350 866  CYS A C   
6589  O O   . CYS A 866  ? 2.0365 1.5513 2.0358 0.2508  -0.7180 -0.5247 866  CYS A O   
6590  C CB  . CYS A 866  ? 1.9685 1.4484 1.9890 0.2467  -0.7740 -0.5666 866  CYS A CB  
6591  S SG  . CYS A 866  ? 2.0251 1.4807 2.0652 0.2322  -0.8016 -0.5918 866  CYS A SG  
6592  N N   . THR A 867  ? 2.2868 1.6869 2.2609 0.2196  -0.7321 -0.5229 867  THR A N   
6593  C CA  . THR A 867  ? 2.4343 1.7967 2.3734 0.2187  -0.7112 -0.4968 867  THR A CA  
6594  C C   . THR A 867  ? 2.6213 1.8984 2.5290 0.2032  -0.7152 -0.4870 867  THR A C   
6595  O O   . THR A 867  ? 2.6372 1.8853 2.5528 0.1911  -0.7328 -0.5005 867  THR A O   
6596  C CB  . THR A 867  ? 2.2854 1.6814 2.2398 0.2102  -0.6905 -0.4904 867  THR A CB  
6597  O OG1 . THR A 867  ? 2.2609 1.7089 2.2605 0.2010  -0.6988 -0.5131 867  THR A OG1 
6598  C CG2 . THR A 867  ? 2.2526 1.6912 2.1972 0.2318  -0.6719 -0.4758 867  THR A CG2 
6599  N N   . SER A 868  ? 2.7642 2.0020 2.6356 0.2046  -0.6983 -0.4632 868  SER A N   
6600  C CA  . SER A 868  ? 2.9619 2.1186 2.7972 0.1941  -0.7006 -0.4510 868  SER A CA  
6601  C C   . SER A 868  ? 3.1572 2.2756 2.9946 0.1691  -0.6956 -0.4491 868  SER A C   
6602  O O   . SER A 868  ? 3.1835 2.2353 2.9964 0.1586  -0.7014 -0.4435 868  SER A O   
6603  C CB  . SER A 868  ? 2.9717 2.1009 2.7652 0.2068  -0.6849 -0.4267 868  SER A CB  
6604  O OG  . SER A 868  ? 2.9539 2.1235 2.7474 0.2299  -0.6859 -0.4275 868  SER A OG  
6605  N N   . GLU A 869  ? 3.3161 2.4763 3.1821 0.1599  -0.6843 -0.4531 869  GLU A N   
6606  C CA  . GLU A 869  ? 3.4942 2.6235 3.3674 0.1352  -0.6791 -0.4531 869  GLU A CA  
6607  C C   . GLU A 869  ? 3.5891 2.7218 3.4939 0.1218  -0.6998 -0.4780 869  GLU A C   
6608  O O   . GLU A 869  ? 3.5731 2.7553 3.5053 0.1311  -0.7137 -0.4969 869  GLU A O   
6609  C CB  . GLU A 869  ? 3.5116 2.6833 3.4019 0.1300  -0.6571 -0.4461 869  GLU A CB  
6610  C CG  . GLU A 869  ? 3.5488 2.6871 3.4438 0.1044  -0.6478 -0.4424 869  GLU A CG  
6611  C CD  . GLU A 869  ? 3.5414 2.7114 3.4823 0.0874  -0.6585 -0.4668 869  GLU A CD  
6612  O OE1 . GLU A 869  ? 3.5143 2.7461 3.4871 0.0963  -0.6692 -0.4855 869  GLU A OE1 
6613  O OE2 . GLU A 869  ? 3.5603 2.6933 3.5051 0.0652  -0.6560 -0.4674 869  GLU A OE2 
6614  N N   . SER A 870  ? 3.6962 2.7751 3.5959 0.1007  -0.7015 -0.4779 870  SER A N   
6615  C CA  . SER A 870  ? 3.7585 2.8286 3.6826 0.0872  -0.7208 -0.5001 870  SER A CA  
6616  C C   . SER A 870  ? 3.7582 2.9008 3.7324 0.0825  -0.7240 -0.5220 870  SER A C   
6617  O O   . SER A 870  ? 3.7656 2.9423 3.7582 0.0744  -0.7078 -0.5191 870  SER A O   
6618  C CB  . SER A 870  ? 3.8247 2.8253 3.7342 0.0647  -0.7176 -0.4939 870  SER A CB  
6619  O OG  . SER A 870  ? 3.8501 2.8610 3.7698 0.0503  -0.6969 -0.4853 870  SER A OG  
6620  N N   . LYS A 882  ? 3.1563 2.3216 2.9904 0.1277  -0.5688 -0.3719 882  LYS A N   
6621  C CA  . LYS A 882  ? 3.2061 2.2922 2.9965 0.1203  -0.5605 -0.3515 882  LYS A CA  
6622  C C   . LYS A 882  ? 3.1754 2.2600 2.9362 0.1316  -0.5354 -0.3266 882  LYS A C   
6623  O O   . LYS A 882  ? 3.1473 2.2728 2.9051 0.1521  -0.5294 -0.3227 882  LYS A O   
6624  C CB  . LYS A 882  ? 3.2451 2.2757 3.0059 0.1261  -0.5788 -0.3526 882  LYS A CB  
6625  C CG  . LYS A 882  ? 3.2469 2.2919 2.9874 0.1511  -0.5808 -0.3473 882  LYS A CG  
6626  C CD  . LYS A 882  ? 3.2747 2.2658 2.9891 0.1548  -0.6000 -0.3498 882  LYS A CD  
6627  C CE  . LYS A 882  ? 3.2819 2.2888 3.0282 0.1496  -0.6252 -0.3753 882  LYS A CE  
6628  N NZ  . LYS A 882  ? 3.2905 2.2514 3.0137 0.1549  -0.6445 -0.3785 882  LYS A NZ  
6629  N N   . CYS A 883  ? 3.1862 2.2228 2.9244 0.1189  -0.5203 -0.3096 883  CYS A N   
6630  C CA  . CYS A 883  ? 3.1646 2.1989 2.8753 0.1284  -0.4952 -0.2858 883  CYS A CA  
6631  C C   . CYS A 883  ? 3.1407 2.1209 2.7987 0.1428  -0.4921 -0.2677 883  CYS A C   
6632  O O   . CYS A 883  ? 3.1737 2.0916 2.7965 0.1357  -0.4831 -0.2510 883  CYS A O   
6633  C CB  . CYS A 883  ? 3.1895 2.2030 2.9007 0.1097  -0.4776 -0.2745 883  CYS A CB  
6634  S SG  . CYS A 883  ? 3.8728 2.8963 3.5565 0.1225  -0.4459 -0.2470 883  CYS A SG  
6635  N N   . VAL A 884  ? 3.0956 2.1011 2.7485 0.1631  -0.4989 -0.2712 884  VAL A N   
6636  C CA  . VAL A 884  ? 3.0840 2.0476 2.6900 0.1782  -0.4952 -0.2554 884  VAL A CA  
6637  C C   . VAL A 884  ? 3.0994 2.0747 2.6834 0.1900  -0.4682 -0.2338 884  VAL A C   
6638  O O   . VAL A 884  ? 3.0679 2.0933 2.6576 0.2087  -0.4608 -0.2327 884  VAL A O   
6639  C CB  . VAL A 884  ? 2.6067 1.5950 2.2174 0.1955  -0.5120 -0.2676 884  VAL A CB  
6640  C CG1 . VAL A 884  ? 2.6056 1.5755 2.2328 0.1851  -0.5388 -0.2874 884  VAL A CG1 
6641  C CG2 . VAL A 884  ? 2.5748 1.6476 2.2191 0.2100  -0.5067 -0.2759 884  VAL A CG2 
6642  N N   . ARG A 885  ? 3.1298 2.0585 2.6876 0.1800  -0.4528 -0.2163 885  ARG A N   
6643  C CA  . ARG A 885  ? 3.1230 2.0644 2.6627 0.1895  -0.4259 -0.1960 885  ARG A CA  
6644  C C   . ARG A 885  ? 3.1138 2.0206 2.6051 0.2074  -0.4171 -0.1787 885  ARG A C   
6645  O O   . ARG A 885  ? 3.1281 1.9667 2.5812 0.2038  -0.4208 -0.1698 885  ARG A O   
6646  C CB  . ARG A 885  ? 3.1474 2.0635 2.6840 0.1720  -0.4104 -0.1845 885  ARG A CB  
6647  C CG  . ARG A 885  ? 3.1814 2.0140 2.6837 0.1589  -0.4153 -0.1764 885  ARG A CG  
6648  C CD  . ARG A 885  ? 3.2120 2.0197 2.7030 0.1467  -0.3945 -0.1597 885  ARG A CD  
6649  N NE  . ARG A 885  ? 3.2090 2.0662 2.7472 0.1326  -0.3902 -0.1697 885  ARG A NE  
6650  C CZ  . ARG A 885  ? 3.2362 2.0910 2.7760 0.1222  -0.3704 -0.1574 885  ARG A CZ  
6651  N NH1 . ARG A 885  ? 3.2709 2.0760 2.7666 0.1254  -0.3530 -0.1343 885  ARG A NH1 
6652  N NH2 . ARG A 885  ? 3.2248 2.1275 2.8104 0.1086  -0.3677 -0.1682 885  ARG A NH2 
6653  N N   . GLN A 886  ? 3.0840 2.0401 2.5774 0.2269  -0.4050 -0.1742 886  GLN A N   
6654  C CA  . GLN A 886  ? 3.1056 2.0397 2.5584 0.2458  -0.3967 -0.1603 886  GLN A CA  
6655  C C   . GLN A 886  ? 3.0635 1.9953 2.4906 0.2535  -0.3679 -0.1377 886  GLN A C   
6656  O O   . GLN A 886  ? 3.0736 2.0164 2.5135 0.2429  -0.3554 -0.1324 886  GLN A O   
6657  C CB  . GLN A 886  ? 3.1490 2.1405 2.6219 0.2644  -0.4038 -0.1720 886  GLN A CB  
6658  C CG  . GLN A 886  ? 3.2354 2.1979 2.6707 0.2812  -0.4036 -0.1639 886  GLN A CG  
6659  C CD  . GLN A 886  ? 3.3021 2.2217 2.7299 0.2747  -0.4284 -0.1753 886  GLN A CD  
6660  O OE1 . GLN A 886  ? 3.3378 2.2366 2.7404 0.2868  -0.4322 -0.1723 886  GLN A OE1 
6661  N NE2 . GLN A 886  ? 3.3114 2.2183 2.7614 0.2557  -0.4453 -0.1885 886  GLN A NE2 
6662  N N   . LYS A 887  ? 3.0336 1.9523 2.4253 0.2722  -0.3570 -0.1245 887  LYS A N   
6663  C CA  . LYS A 887  ? 3.0257 1.9409 2.3894 0.2822  -0.3292 -0.1025 887  LYS A CA  
6664  C C   . LYS A 887  ? 2.9645 1.9267 2.3257 0.3072  -0.3182 -0.0989 887  LYS A C   
6665  O O   . LYS A 887  ? 2.9187 1.8660 2.2620 0.3186  -0.3260 -0.1009 887  LYS A O   
6666  C CB  . LYS A 887  ? 3.0750 1.9073 2.3841 0.2792  -0.3230 -0.0850 887  LYS A CB  
6667  C CG  . LYS A 887  ? 3.1127 1.8854 2.4151 0.2574  -0.3385 -0.0893 887  LYS A CG  
6668  C CD  . LYS A 887  ? 3.1182 1.8653 2.4183 0.2560  -0.3647 -0.1039 887  LYS A CD  
6669  C CE  . LYS A 887  ? 3.1466 1.8337 2.4383 0.2359  -0.3802 -0.1079 887  LYS A CE  
6670  N NZ  . LYS A 887  ? 3.1789 1.7920 2.4173 0.2346  -0.3714 -0.0896 887  LYS A NZ  
6671  N N   . VAL A 888  ? 2.9712 1.9902 2.3503 0.3159  -0.2997 -0.0934 888  VAL A N   
6672  C CA  . VAL A 888  ? 2.9497 2.0141 2.3243 0.3413  -0.2860 -0.0878 888  VAL A CA  
6673  C C   . VAL A 888  ? 3.0133 2.0490 2.3430 0.3535  -0.2594 -0.0631 888  VAL A C   
6674  O O   . VAL A 888  ? 3.0605 2.1037 2.3897 0.3497  -0.2416 -0.0514 888  VAL A O   
6675  C CB  . VAL A 888  ? 2.8704 2.0216 2.2911 0.3474  -0.2802 -0.0962 888  VAL A CB  
6676  C CG1 . VAL A 888  ? 2.8260 2.0272 2.2815 0.3548  -0.2998 -0.1176 888  VAL A CG1 
6677  C CG2 . VAL A 888  ? 2.8573 2.0181 2.3054 0.3260  -0.2790 -0.0992 888  VAL A CG2 
6678  N N   . GLU A 889  ? 3.0416 2.0467 2.3344 0.3685  -0.2560 -0.0552 889  GLU A N   
6679  C CA  . GLU A 889  ? 3.1298 2.1076 2.3774 0.3825  -0.2303 -0.0322 889  GLU A CA  
6680  C C   . GLU A 889  ? 3.0774 2.1231 2.3410 0.3993  -0.2080 -0.0246 889  GLU A C   
6681  O O   . GLU A 889  ? 2.9983 2.1112 2.2976 0.4096  -0.2127 -0.0368 889  GLU A O   
6682  C CB  . GLU A 889  ? 3.2792 2.2168 2.4884 0.3957  -0.2319 -0.0278 889  GLU A CB  
6683  C CG  . GLU A 889  ? 3.3927 2.3812 2.6225 0.4131  -0.2391 -0.0396 889  GLU A CG  
6684  C CD  . GLU A 889  ? 3.4874 2.4897 2.7528 0.4020  -0.2690 -0.0632 889  GLU A CD  
6685  O OE1 . GLU A 889  ? 3.5402 2.5085 2.8125 0.3806  -0.2851 -0.0706 889  GLU A OE1 
6686  O OE2 . GLU A 889  ? 3.4967 2.5434 2.7821 0.4158  -0.2758 -0.0739 889  GLU A OE2 
6687  N N   . GLY A 890  ? 3.0944 2.1230 2.3312 0.4026  -0.1841 -0.0045 890  GLY A N   
6688  C CA  . GLY A 890  ? 3.0460 2.1364 2.2980 0.4162  -0.1623 0.0038  890  GLY A CA  
6689  C C   . GLY A 890  ? 2.9240 2.0643 2.1776 0.4433  -0.1537 0.0041  890  GLY A C   
6690  O O   . GLY A 890  ? 2.9219 2.0304 2.1430 0.4560  -0.1525 0.0089  890  GLY A O   
6691  N N   . SER A 891  ? 2.8230 2.0423 2.1147 0.4521  -0.1473 -0.0010 891  SER A N   
6692  C CA  . SER A 891  ? 2.7351 2.0106 2.0320 0.4795  -0.1379 -0.0007 891  SER A CA  
6693  C C   . SER A 891  ? 2.6926 1.9682 1.9943 0.4861  -0.1571 -0.0153 891  SER A C   
6694  O O   . SER A 891  ? 2.7006 1.9826 1.9813 0.5088  -0.1472 -0.0088 891  SER A O   
6695  C CB  . SER A 891  ? 2.7218 1.9755 1.9709 0.5003  -0.1090 0.0236  891  SER A CB  
6696  O OG  . SER A 891  ? 2.7413 1.9967 1.9859 0.4954  -0.0905 0.0377  891  SER A OG  
6697  N N   . SER A 892  ? 2.6619 1.9305 1.9914 0.4664  -0.1839 -0.0347 892  SER A N   
6698  C CA  . SER A 892  ? 2.6263 1.8899 1.9616 0.4695  -0.2047 -0.0495 892  SER A CA  
6699  C C   . SER A 892  ? 2.5883 1.8963 1.9770 0.4559  -0.2296 -0.0741 892  SER A C   
6700  O O   . SER A 892  ? 2.5445 1.9094 1.9698 0.4526  -0.2273 -0.0804 892  SER A O   
6701  C CB  . SER A 892  ? 2.6533 1.8300 1.9495 0.4580  -0.2139 -0.0453 892  SER A CB  
6702  O OG  . SER A 892  ? 2.6818 1.8147 1.9270 0.4709  -0.1922 -0.0240 892  SER A OG  
6703  N N   . SER A 893  ? 2.6032 1.8844 1.9956 0.4480  -0.2531 -0.0882 893  SER A N   
6704  C CA  . SER A 893  ? 2.5824 1.8994 2.0224 0.4354  -0.2783 -0.1124 893  SER A CA  
6705  C C   . SER A 893  ? 2.6119 1.8768 2.0460 0.4216  -0.3030 -0.1239 893  SER A C   
6706  O O   . SER A 893  ? 2.6281 1.8583 2.0330 0.4312  -0.3047 -0.1195 893  SER A O   
6707  C CB  . SER A 893  ? 2.5358 1.9308 2.0067 0.4559  -0.2802 -0.1237 893  SER A CB  
6708  O OG  . SER A 893  ? 2.5021 1.9315 2.0186 0.4436  -0.3045 -0.1476 893  SER A OG  
6709  N N   . HIS A 894  ? 2.6413 1.9024 2.1042 0.3993  -0.3223 -0.1390 894  HIS A N   
6710  C CA  . HIS A 894  ? 2.7679 1.9833 2.2288 0.3858  -0.3471 -0.1513 894  HIS A CA  
6711  C C   . HIS A 894  ? 2.5319 1.7966 2.0361 0.3863  -0.3698 -0.1754 894  HIS A C   
6712  O O   . HIS A 894  ? 2.4810 1.7888 2.0256 0.3763  -0.3771 -0.1888 894  HIS A O   
6713  C CB  . HIS A 894  ? 3.2696 2.4314 2.7252 0.3597  -0.3538 -0.1504 894  HIS A CB  
6714  C CG  . HIS A 894  ? 3.9050 2.9864 3.3207 0.3524  -0.3620 -0.1443 894  HIS A CG  
6715  N ND1 . HIS A 894  ? 4.2540 3.2913 3.6730 0.3314  -0.3815 -0.1535 894  HIS A ND1 
6716  C CD2 . HIS A 894  ? 4.1891 3.2269 3.5604 0.3639  -0.3533 -0.1303 894  HIS A CD2 
6717  C CE1 . HIS A 894  ? 4.5663 3.5377 3.9447 0.3305  -0.3848 -0.1453 894  HIS A CE1 
6718  N NE2 . HIS A 894  ? 4.4233 3.3936 3.7728 0.3494  -0.3681 -0.1316 894  HIS A NE2 
6719  N N   . LEU A 895  ? 2.4087 1.6654 1.9044 0.3974  -0.3810 -0.1811 895  LEU A N   
6720  C CA  . LEU A 895  ? 2.3047 1.6017 1.8377 0.3986  -0.4036 -0.2037 895  LEU A CA  
6721  C C   . LEU A 895  ? 2.1846 1.4731 1.7462 0.3743  -0.4237 -0.2198 895  LEU A C   
6722  O O   . LEU A 895  ? 2.2100 1.4387 1.7532 0.3560  -0.4268 -0.2145 895  LEU A O   
6723  C CB  . LEU A 895  ? 2.3419 1.6068 1.8546 0.4069  -0.4154 -0.2061 895  LEU A CB  
6724  C CG  . LEU A 895  ? 2.3533 1.6714 1.8738 0.4328  -0.4103 -0.2084 895  LEU A CG  
6725  C CD1 . LEU A 895  ? 2.3785 1.6507 1.8562 0.4448  -0.4027 -0.1950 895  LEU A CD1 
6726  C CD2 . LEU A 895  ? 2.3230 1.6876 1.8858 0.4336  -0.4339 -0.2326 895  LEU A CD2 
6727  N N   . VAL A 896  ? 2.0429 1.3911 1.6490 0.3746  -0.4372 -0.2398 896  VAL A N   
6728  C CA  . VAL A 896  ? 1.9292 1.2726 1.5652 0.3527  -0.4580 -0.2578 896  VAL A CA  
6729  C C   . VAL A 896  ? 1.8847 1.2581 1.5442 0.3609  -0.4795 -0.2775 896  VAL A C   
6730  O O   . VAL A 896  ? 1.8764 1.2893 1.5370 0.3832  -0.4751 -0.2775 896  VAL A O   
6731  C CB  . VAL A 896  ? 1.8513 1.2468 1.5245 0.3435  -0.4525 -0.2647 896  VAL A CB  
6732  C CG1 . VAL A 896  ? 1.8525 1.2237 1.5468 0.3172  -0.4701 -0.2787 896  VAL A CG1 
6733  C CG2 . VAL A 896  ? 1.8312 1.2222 1.4847 0.3449  -0.4258 -0.2437 896  VAL A CG2 
6734  N N   . THR A 897  ? 1.8535 1.2065 1.5304 0.3436  -0.5024 -0.2939 897  THR A N   
6735  C CA  . THR A 897  ? 1.7871 1.1723 1.4916 0.3494  -0.5243 -0.3150 897  THR A CA  
6736  C C   . THR A 897  ? 1.8003 1.1728 1.5314 0.3268  -0.5455 -0.3334 897  THR A C   
6737  O O   . THR A 897  ? 1.8325 1.1553 1.5526 0.3066  -0.5452 -0.3282 897  THR A O   
6738  C CB  . THR A 897  ? 1.7555 1.1022 1.4330 0.3593  -0.5336 -0.3125 897  THR A CB  
6739  O OG1 . THR A 897  ? 1.7674 1.0807 1.4538 0.3438  -0.5583 -0.3274 897  THR A OG1 
6740  C CG2 . THR A 897  ? 1.7715 1.0587 1.4002 0.3611  -0.5170 -0.2890 897  THR A CG2 
6741  N N   . PHE A 898  ? 1.7788 1.1959 1.5439 0.3312  -0.5636 -0.3547 898  PHE A N   
6742  C CA  . PHE A 898  ? 1.7632 1.1717 1.5548 0.3127  -0.5862 -0.3749 898  PHE A CA  
6743  C C   . PHE A 898  ? 1.7380 1.1723 1.5448 0.3258  -0.6059 -0.3917 898  PHE A C   
6744  O O   . PHE A 898  ? 1.6944 1.1808 1.5094 0.3474  -0.6012 -0.3932 898  PHE A O   
6745  C CB  . PHE A 898  ? 1.7452 1.2043 1.5775 0.3010  -0.5849 -0.3874 898  PHE A CB  
6746  C CG  . PHE A 898  ? 1.7460 1.1922 1.5690 0.2895  -0.5638 -0.3717 898  PHE A CG  
6747  C CD1 . PHE A 898  ? 1.7566 1.1678 1.5865 0.2640  -0.5672 -0.3745 898  PHE A CD1 
6748  C CD2 . PHE A 898  ? 1.7359 1.2056 1.5435 0.3048  -0.5401 -0.3538 898  PHE A CD2 
6749  C CE1 . PHE A 898  ? 1.7745 1.1748 1.5965 0.2536  -0.5474 -0.3597 898  PHE A CE1 
6750  C CE2 . PHE A 898  ? 1.7509 1.2099 1.5501 0.2949  -0.5206 -0.3391 898  PHE A CE2 
6751  C CZ  . PHE A 898  ? 1.7738 1.1985 1.5806 0.2691  -0.5243 -0.3421 898  PHE A CZ  
6752  N N   . THR A 899  ? 1.7321 1.1300 1.5422 0.3137  -0.6275 -0.4040 899  THR A N   
6753  C CA  . THR A 899  ? 1.6828 1.1091 1.5134 0.3238  -0.6479 -0.4228 899  THR A CA  
6754  C C   . THR A 899  ? 1.6274 1.0861 1.5007 0.3094  -0.6630 -0.4460 899  THR A C   
6755  O O   . THR A 899  ? 1.6227 1.0493 1.4995 0.2872  -0.6646 -0.4474 899  THR A O   
6756  C CB  . THR A 899  ? 1.7270 1.0937 1.5293 0.3246  -0.6614 -0.4199 899  THR A CB  
6757  O OG1 . THR A 899  ? 1.7722 1.0771 1.5645 0.3018  -0.6704 -0.4204 899  THR A OG1 
6758  C CG2 . THR A 899  ? 1.6899 1.0300 1.4518 0.3386  -0.6443 -0.3974 899  THR A CG2 
6759  N N   . VAL A 900  ? 1.6067 1.1307 1.5118 0.3227  -0.6720 -0.4633 900  VAL A N   
6760  C CA  . VAL A 900  ? 1.5770 1.1399 1.5249 0.3123  -0.6881 -0.4883 900  VAL A CA  
6761  C C   . VAL A 900  ? 1.5251 1.1178 1.4895 0.3270  -0.7082 -0.5065 900  VAL A C   
6762  O O   . VAL A 900  ? 1.5208 1.1064 1.4654 0.3449  -0.7090 -0.4996 900  VAL A O   
6763  C CB  . VAL A 900  ? 1.3506 0.9853 1.3306 0.3139  -0.6763 -0.4941 900  VAL A CB  
6764  C CG1 . VAL A 900  ? 1.3759 0.9897 1.3608 0.2895  -0.6665 -0.4895 900  VAL A CG1 
6765  C CG2 . VAL A 900  ? 1.3329 1.0092 1.3017 0.3384  -0.6569 -0.4797 900  VAL A CG2 
6766  N N   . LEU A 901  ? 1.5244 1.1512 1.5255 0.3196  -0.7241 -0.5300 901  LEU A N   
6767  C CA  . LEU A 901  ? 1.5712 1.2270 1.5886 0.3337  -0.7434 -0.5478 901  LEU A CA  
6768  C C   . LEU A 901  ? 1.6244 1.3257 1.6854 0.3246  -0.7584 -0.5746 901  LEU A C   
6769  O O   . LEU A 901  ? 1.6738 1.3409 1.7438 0.3036  -0.7717 -0.5860 901  LEU A O   
6770  C CB  . LEU A 901  ? 1.5688 1.1602 1.5609 0.3316  -0.7578 -0.5454 901  LEU A CB  
6771  C CG  . LEU A 901  ? 1.5696 1.1682 1.5806 0.3341  -0.7834 -0.5677 901  LEU A CG  
6772  C CD1 . LEU A 901  ? 1.5547 1.1253 1.5401 0.3496  -0.7899 -0.5603 901  LEU A CD1 
6773  C CD2 . LEU A 901  ? 1.5982 1.1539 1.6177 0.3083  -0.7971 -0.5791 901  LEU A CD2 
6774  N N   . PRO A 902  ? 1.6221 1.4007 1.7097 0.3408  -0.7559 -0.5847 902  PRO A N   
6775  C CA  . PRO A 902  ? 1.6244 1.4514 1.7542 0.3310  -0.7668 -0.6092 902  PRO A CA  
6776  C C   . PRO A 902  ? 1.6549 1.4944 1.8020 0.3373  -0.7917 -0.6319 902  PRO A C   
6777  O O   . PRO A 902  ? 1.6433 1.4898 1.7782 0.3590  -0.7963 -0.6294 902  PRO A O   
6778  C CB  . PRO A 902  ? 1.6127 1.5168 1.7586 0.3485  -0.7517 -0.6075 902  PRO A CB  
6779  C CG  . PRO A 902  ? 1.5256 1.4146 1.6341 0.3676  -0.7317 -0.5802 902  PRO A CG  
6780  C CD  . PRO A 902  ? 1.5514 1.3770 1.6314 0.3686  -0.7421 -0.5741 902  PRO A CD  
6781  N N   . LEU A 903  ? 1.6945 1.5340 1.8685 0.3183  -0.8071 -0.6533 903  LEU A N   
6782  C CA  . LEU A 903  ? 1.7180 1.5759 1.9126 0.3239  -0.8310 -0.6774 903  LEU A CA  
6783  C C   . LEU A 903  ? 1.7214 1.6588 1.9582 0.3267  -0.8353 -0.6998 903  LEU A C   
6784  O O   . LEU A 903  ? 1.7241 1.7042 1.9793 0.3419  -0.8499 -0.7179 903  LEU A O   
6785  C CB  . LEU A 903  ? 1.7355 1.5286 1.9270 0.3013  -0.8477 -0.6866 903  LEU A CB  
6786  C CG  . LEU A 903  ? 1.7581 1.4650 1.9115 0.2896  -0.8441 -0.6669 903  LEU A CG  
6787  C CD1 . LEU A 903  ? 1.7473 1.4340 1.8691 0.3111  -0.8432 -0.6514 903  LEU A CD1 
6788  C CD2 . LEU A 903  ? 1.7646 1.4453 1.9054 0.2728  -0.8232 -0.6485 903  LEU A CD2 
6789  N N   . GLU A 904  ? 1.7226 1.6799 1.9746 0.3118  -0.8226 -0.6987 904  GLU A N   
6790  C CA  . GLU A 904  ? 1.7632 1.7977 2.0551 0.3135  -0.8250 -0.7189 904  GLU A CA  
6791  C C   . GLU A 904  ? 1.7036 1.8045 1.9957 0.3412  -0.8103 -0.7097 904  GLU A C   
6792  O O   . GLU A 904  ? 1.6780 1.7731 1.9503 0.3449  -0.7886 -0.6866 904  GLU A O   
6793  C CB  . GLU A 904  ? 1.8495 1.8787 2.1612 0.2841  -0.8191 -0.7241 904  GLU A CB  
6794  C CG  . GLU A 904  ? 1.9505 1.9127 2.2612 0.2575  -0.8330 -0.7331 904  GLU A CG  
6795  C CD  . GLU A 904  ? 2.0418 2.0211 2.3873 0.2310  -0.8351 -0.7512 904  GLU A CD  
6796  O OE1 . GLU A 904  ? 2.0540 2.0894 2.4205 0.2303  -0.8223 -0.7519 904  GLU A OE1 
6797  O OE2 . GLU A 904  ? 2.0855 2.0221 2.4372 0.2111  -0.8493 -0.7646 904  GLU A OE2 
6798  N N   . ILE A 905  ? 1.6528 1.8150 1.9661 0.3612  -0.8220 -0.7277 905  ILE A N   
6799  C CA  . ILE A 905  ? 1.5241 1.7509 1.8373 0.3914  -0.8106 -0.7211 905  ILE A CA  
6800  C C   . ILE A 905  ? 1.4434 1.7258 1.7785 0.3871  -0.7960 -0.7217 905  ILE A C   
6801  O O   . ILE A 905  ? 1.3461 1.6331 1.7067 0.3629  -0.8007 -0.7359 905  ILE A O   
6802  C CB  . ILE A 905  ? 1.3138 1.5910 1.6448 0.4137  -0.8285 -0.7418 905  ILE A CB  
6803  C CG1 . ILE A 905  ? 1.3121 1.5320 1.6297 0.4105  -0.8479 -0.7477 905  ILE A CG1 
6804  C CG2 . ILE A 905  ? 1.2249 1.5521 1.5450 0.4480  -0.8155 -0.7295 905  ILE A CG2 
6805  C CD1 . ILE A 905  ? 1.2763 1.5071 1.5772 0.4411  -0.8515 -0.7426 905  ILE A CD1 
6806  N N   . GLY A 906  ? 1.5530 1.8741 1.8767 0.4102  -0.7773 -0.7052 906  GLY A N   
6807  C CA  . GLY A 906  ? 1.6199 2.0009 1.9622 0.4116  -0.7615 -0.7035 906  GLY A CA  
6808  C C   . GLY A 906  ? 1.6791 2.0248 2.0160 0.3859  -0.7460 -0.6896 906  GLY A C   
6809  O O   . GLY A 906  ? 1.6651 2.0378 1.9971 0.3927  -0.7252 -0.6741 906  GLY A O   
6810  N N   . LEU A 907  ? 1.7628 2.0469 2.0995 0.3573  -0.7560 -0.6949 907  LEU A N   
6811  C CA  . LEU A 907  ? 1.8247 2.0651 2.1561 0.3295  -0.7437 -0.6833 907  LEU A CA  
6812  C C   . LEU A 907  ? 1.8560 2.0804 2.1559 0.3384  -0.7178 -0.6526 907  LEU A C   
6813  O O   . LEU A 907  ? 1.8433 2.0473 2.1109 0.3590  -0.7113 -0.6354 907  LEU A O   
6814  C CB  . LEU A 907  ? 1.8803 2.0353 2.1960 0.3069  -0.7558 -0.6838 907  LEU A CB  
6815  C CG  . LEU A 907  ? 1.9807 2.0806 2.2829 0.2811  -0.7414 -0.6675 907  LEU A CG  
6816  C CD1 . LEU A 907  ? 1.9981 2.1435 2.3367 0.2624  -0.7351 -0.6788 907  LEU A CD1 
6817  C CD2 . LEU A 907  ? 2.0551 2.0752 2.3429 0.2615  -0.7553 -0.6701 907  LEU A CD2 
6818  N N   . HIS A 908  ? 1.9144 2.1452 2.2227 0.3220  -0.7025 -0.6455 908  HIS A N   
6819  C CA  . HIS A 908  ? 1.9588 2.1868 2.2404 0.3333  -0.6770 -0.6179 908  HIS A CA  
6820  C C   . HIS A 908  ? 1.9834 2.1601 2.2562 0.3056  -0.6647 -0.6048 908  HIS A C   
6821  O O   . HIS A 908  ? 2.0227 2.1532 2.3023 0.2798  -0.6763 -0.6144 908  HIS A O   
6822  C CB  . HIS A 908  ? 1.9609 2.2803 2.2654 0.3523  -0.6659 -0.6211 908  HIS A CB  
6823  C CG  . HIS A 908  ? 1.8924 2.2806 2.2276 0.3687  -0.6835 -0.6466 908  HIS A CG  
6824  N ND1 . HIS A 908  ? 1.8606 2.2564 2.2271 0.3525  -0.7066 -0.6748 908  HIS A ND1 
6825  C CD2 . HIS A 908  ? 1.8354 2.2892 2.1744 0.4002  -0.6806 -0.6481 908  HIS A CD2 
6826  C CE1 . HIS A 908  ? 1.8233 2.2861 2.2113 0.3734  -0.7177 -0.6927 908  HIS A CE1 
6827  N NE2 . HIS A 908  ? 1.8038 2.3029 2.1756 0.4028  -0.7023 -0.6769 908  HIS A NE2 
6828  N N   . ASN A 909  ? 1.9481 2.1329 2.2049 0.3120  -0.6406 -0.5827 909  ASN A N   
6829  C CA  . ASN A 909  ? 1.9553 2.1030 2.2060 0.2881  -0.6255 -0.5691 909  ASN A CA  
6830  C C   . ASN A 909  ? 1.9261 1.9759 2.1377 0.2742  -0.6239 -0.5518 909  ASN A C   
6831  O O   . ASN A 909  ? 1.9113 1.9143 2.1217 0.2608  -0.6420 -0.5626 909  ASN A O   
6832  C CB  . ASN A 909  ? 2.0189 2.1962 2.3140 0.2616  -0.6332 -0.5910 909  ASN A CB  
6833  C CG  . ASN A 909  ? 2.1094 2.2410 2.3980 0.2348  -0.6187 -0.5776 909  ASN A CG  
6834  O OD1 . ASN A 909  ? 2.1465 2.2455 2.4505 0.2071  -0.6283 -0.5894 909  ASN A OD1 
6835  N ND2 . ASN A 909  ? 2.1364 2.2636 2.4006 0.2434  -0.5949 -0.5520 909  ASN A ND2 
6836  N N   . ILE A 910  ? 1.8808 1.9017 2.0602 0.2782  -0.6017 -0.5248 910  ILE A N   
6837  C CA  . ILE A 910  ? 1.8326 1.7647 1.9744 0.2643  -0.5962 -0.5061 910  ILE A CA  
6838  C C   . ILE A 910  ? 1.8622 1.7933 1.9925 0.2596  -0.5700 -0.4847 910  ILE A C   
6839  O O   . ILE A 910  ? 1.9125 1.8809 2.0324 0.2812  -0.5531 -0.4710 910  ILE A O   
6840  C CB  . ILE A 910  ? 1.7349 1.6247 1.8359 0.2843  -0.5981 -0.4925 910  ILE A CB  
6841  C CG1 . ILE A 910  ? 1.6685 1.5534 1.7798 0.2873  -0.6242 -0.5130 910  ILE A CG1 
6842  C CG2 . ILE A 910  ? 1.7387 1.5431 1.7985 0.2726  -0.5886 -0.4705 910  ILE A CG2 
6843  C CD1 . ILE A 910  ? 1.6435 1.4794 1.7158 0.3028  -0.6279 -0.5009 910  ILE A CD1 
6844  N N   . ASN A 911  ? 1.8189 1.7111 1.9531 0.2319  -0.5662 -0.4824 911  ASN A N   
6845  C CA  . ASN A 911  ? 1.7795 1.6627 1.9006 0.2256  -0.5413 -0.4610 911  ASN A CA  
6846  C C   . ASN A 911  ? 1.8190 1.6261 1.8856 0.2323  -0.5307 -0.4345 911  ASN A C   
6847  O O   . ASN A 911  ? 1.8222 1.5675 1.8685 0.2265  -0.5443 -0.4355 911  ASN A O   
6848  C CB  . ASN A 911  ? 1.7587 1.6269 1.9041 0.1930  -0.5404 -0.4680 911  ASN A CB  
6849  C CG  . ASN A 911  ? 1.6823 1.6281 1.8840 0.1837  -0.5496 -0.4950 911  ASN A CG  
6850  O OD1 . ASN A 911  ? 1.6865 1.6375 1.9124 0.1751  -0.5718 -0.5190 911  ASN A OD1 
6851  N ND2 . ASN A 911  ? 1.6694 1.6729 1.8918 0.1840  -0.5324 -0.4911 911  ASN A ND2 
6852  N N   . PHE A 912  ? 1.8541 1.6661 1.8969 0.2452  -0.5070 -0.4114 912  PHE A N   
6853  C CA  . PHE A 912  ? 1.8691 1.6086 1.8602 0.2496  -0.4950 -0.3859 912  PHE A CA  
6854  C C   . PHE A 912  ? 1.9345 1.6581 1.9165 0.2370  -0.4724 -0.3677 912  PHE A C   
6855  O O   . PHE A 912  ? 1.9421 1.7256 1.9482 0.2392  -0.4595 -0.3680 912  PHE A O   
6856  C CB  . PHE A 912  ? 1.7989 1.5537 1.7624 0.2812  -0.4865 -0.3731 912  PHE A CB  
6857  C CG  . PHE A 912  ? 1.7157 1.4598 1.6734 0.2930  -0.5068 -0.3844 912  PHE A CG  
6858  C CD1 . PHE A 912  ? 1.7079 1.3780 1.6420 0.2822  -0.5200 -0.3836 912  PHE A CD1 
6859  C CD2 . PHE A 912  ? 1.6611 1.4696 1.6371 0.3154  -0.5127 -0.3959 912  PHE A CD2 
6860  C CE1 . PHE A 912  ? 1.6681 1.3298 1.5980 0.2930  -0.5387 -0.3940 912  PHE A CE1 
6861  C CE2 . PHE A 912  ? 1.6224 1.4206 1.5933 0.3262  -0.5311 -0.4060 912  PHE A CE2 
6862  C CZ  . PHE A 912  ? 1.6203 1.3456 1.5687 0.3148  -0.5439 -0.4050 912  PHE A CZ  
6863  N N   . SER A 913  ? 1.9894 1.6331 1.9368 0.2242  -0.4676 -0.3521 913  SER A N   
6864  C CA  . SER A 913  ? 2.0530 1.6734 1.9906 0.2098  -0.4472 -0.3350 913  SER A CA  
6865  C C   . SER A 913  ? 2.1495 1.7003 2.0311 0.2177  -0.4332 -0.3081 913  SER A C   
6866  O O   . SER A 913  ? 2.1445 1.6467 1.9978 0.2237  -0.4445 -0.3064 913  SER A O   
6867  C CB  . SER A 913  ? 2.0588 1.6477 2.0179 0.1781  -0.4572 -0.3469 913  SER A CB  
6868  O OG  . SER A 913  ? 2.0711 1.6308 2.0197 0.1627  -0.4379 -0.3301 913  SER A OG  
6869  N N   . LEU A 914  ? 2.2233 1.7698 2.0885 0.2181  -0.4089 -0.2876 914  LEU A N   
6870  C CA  . LEU A 914  ? 2.3092 1.7806 2.1217 0.2200  -0.3960 -0.2629 914  LEU A CA  
6871  C C   . LEU A 914  ? 2.4498 1.8951 2.2559 0.2024  -0.3774 -0.2479 914  LEU A C   
6872  O O   . LEU A 914  ? 2.4645 1.9615 2.3045 0.1946  -0.3683 -0.2521 914  LEU A O   
6873  C CB  . LEU A 914  ? 2.2155 1.6937 1.9939 0.2490  -0.3829 -0.2464 914  LEU A CB  
6874  C CG  . LEU A 914  ? 2.1121 1.6632 1.9021 0.2689  -0.3640 -0.2399 914  LEU A CG  
6875  C CD1 . LEU A 914  ? 2.0881 1.6698 1.9015 0.2552  -0.3480 -0.2358 914  LEU A CD1 
6876  C CD2 . LEU A 914  ? 2.0904 1.6130 1.8312 0.2913  -0.3468 -0.2165 914  LEU A CD2 
6877  N N   . GLU A 915  ? 2.5670 1.9326 2.3298 0.1965  -0.3718 -0.2305 915  GLU A N   
6878  C CA  . GLU A 915  ? 2.6935 2.0235 2.4470 0.1785  -0.3558 -0.2162 915  GLU A CA  
6879  C C   . GLU A 915  ? 2.7727 2.0582 2.4744 0.1906  -0.3338 -0.1878 915  GLU A C   
6880  O O   . GLU A 915  ? 2.7647 1.9934 2.4250 0.1987  -0.3378 -0.1787 915  GLU A O   
6881  C CB  . GLU A 915  ? 2.7445 2.0140 2.4996 0.1529  -0.3714 -0.2248 915  GLU A CB  
6882  C CG  . GLU A 915  ? 2.7772 2.0874 2.5866 0.1337  -0.3864 -0.2501 915  GLU A CG  
6883  C CD  . GLU A 915  ? 2.8017 2.1164 2.6265 0.1356  -0.4142 -0.2728 915  GLU A CD  
6884  O OE1 . GLU A 915  ? 2.8196 2.0770 2.6110 0.1405  -0.4252 -0.2693 915  GLU A OE1 
6885  O OE2 . GLU A 915  ? 2.7997 2.1757 2.6702 0.1321  -0.4253 -0.2946 915  GLU A OE2 
6886  N N   . THR A 916  ? 2.8875 2.2005 2.5929 0.1912  -0.3106 -0.1742 916  THR A N   
6887  C CA  . THR A 916  ? 3.0026 2.2776 2.6617 0.2016  -0.2873 -0.1469 916  THR A CA  
6888  C C   . THR A 916  ? 3.1418 2.4058 2.8075 0.1828  -0.2707 -0.1365 916  THR A C   
6889  O O   . THR A 916  ? 3.1341 2.4484 2.8454 0.1693  -0.2708 -0.1486 916  THR A O   
6890  C CB  . THR A 916  ? 2.9559 2.2851 2.6080 0.2294  -0.2712 -0.1374 916  THR A CB  
6891  O OG1 . THR A 916  ? 2.9234 2.2593 2.5672 0.2472  -0.2856 -0.1460 916  THR A OG1 
6892  C CG2 . THR A 916  ? 2.9676 2.2565 2.5712 0.2398  -0.2459 -0.1089 916  THR A CG2 
6893  N N   . TRP A 917  ? 3.2880 2.4856 2.9079 0.1819  -0.2564 -0.1142 917  TRP A N   
6894  C CA  . TRP A 917  ? 3.4150 2.5894 3.0328 0.1649  -0.2394 -0.1012 917  TRP A CA  
6895  C C   . TRP A 917  ? 3.4510 2.7037 3.1156 0.1599  -0.2270 -0.1059 917  TRP A C   
6896  O O   . TRP A 917  ? 3.4392 2.6953 3.1335 0.1367  -0.2272 -0.1127 917  TRP A O   
6897  C CB  . TRP A 917  ? 3.5047 2.6275 3.0663 0.1773  -0.2180 -0.0730 917  TRP A CB  
6898  C CG  . TRP A 917  ? 3.6036 2.6600 3.1426 0.1591  -0.2088 -0.0590 917  TRP A CG  
6899  C CD1 . TRP A 917  ? 3.6348 2.6940 3.1715 0.1535  -0.1850 -0.0425 917  TRP A CD1 
6900  C CD2 . TRP A 917  ? 3.6580 2.6349 3.1720 0.1453  -0.2226 -0.0597 917  TRP A CD2 
6901  N NE1 . TRP A 917  ? 3.6856 2.6714 3.1974 0.1370  -0.1829 -0.0327 917  TRP A NE1 
6902  C CE2 . TRP A 917  ? 3.6989 2.6332 3.1960 0.1319  -0.2058 -0.0431 917  TRP A CE2 
6903  C CE3 . TRP A 917  ? 3.6771 2.6158 3.1814 0.1435  -0.2473 -0.0726 917  TRP A CE3 
6904  C CZ2 . TRP A 917  ? 3.7355 2.5905 3.2057 0.1176  -0.2130 -0.0389 917  TRP A CZ2 
6905  C CZ3 . TRP A 917  ? 3.7101 2.5710 3.1881 0.1291  -0.2547 -0.0687 917  TRP A CZ3 
6906  C CH2 . TRP A 917  ? 3.7404 2.5601 3.2013 0.1166  -0.2376 -0.0520 917  TRP A CH2 
6907  N N   . PHE A 918  ? 3.4812 2.7966 3.1521 0.1818  -0.2158 -0.1024 918  PHE A N   
6908  C CA  . PHE A 918  ? 3.5095 2.9040 3.2233 0.1798  -0.2033 -0.1062 918  PHE A CA  
6909  C C   . PHE A 918  ? 3.3901 2.8669 3.1501 0.1876  -0.2180 -0.1298 918  PHE A C   
6910  O O   . PHE A 918  ? 3.3776 2.9289 3.1712 0.1918  -0.2078 -0.1331 918  PHE A O   
6911  C CB  . PHE A 918  ? 3.6154 3.0235 3.3030 0.1978  -0.1741 -0.0811 918  PHE A CB  
6912  C CG  . PHE A 918  ? 3.6649 3.0850 3.3224 0.2287  -0.1698 -0.0730 918  PHE A CG  
6913  C CD1 . PHE A 918  ? 3.6650 3.1685 3.3501 0.2471  -0.1675 -0.0810 918  PHE A CD1 
6914  C CD2 . PHE A 918  ? 3.7087 3.0566 3.3100 0.2395  -0.1674 -0.0575 918  PHE A CD2 
6915  C CE1 . PHE A 918  ? 3.6669 3.1800 3.3235 0.2760  -0.1622 -0.0729 918  PHE A CE1 
6916  C CE2 . PHE A 918  ? 3.7096 3.0670 3.2833 0.2673  -0.1624 -0.0501 918  PHE A CE2 
6917  C CZ  . PHE A 918  ? 3.6883 3.1276 3.2894 0.2857  -0.1593 -0.0574 918  PHE A CZ  
6918  N N   . GLY A 919  ? 3.2840 2.7486 3.0459 0.1899  -0.2420 -0.1464 919  GLY A N   
6919  C CA  . GLY A 919  ? 3.1563 2.6955 2.9608 0.1974  -0.2574 -0.1696 919  GLY A CA  
6920  C C   . GLY A 919  ? 3.0703 2.5910 2.8905 0.1868  -0.2868 -0.1928 919  GLY A C   
6921  O O   . GLY A 919  ? 3.0688 2.5252 2.8544 0.1890  -0.2971 -0.1893 919  GLY A O   
6922  N N   . LYS A 920  ? 2.9691 2.5480 2.8420 0.1755  -0.3002 -0.2168 920  LYS A N   
6923  C CA  . LYS A 920  ? 2.8716 2.4486 2.7658 0.1683  -0.3284 -0.2415 920  LYS A CA  
6924  C C   . LYS A 920  ? 2.7550 2.4252 2.6949 0.1790  -0.3373 -0.2626 920  LYS A C   
6925  O O   . LYS A 920  ? 2.7657 2.4934 2.7481 0.1678  -0.3337 -0.2731 920  LYS A O   
6926  C CB  . LYS A 920  ? 2.8676 2.4044 2.7800 0.1364  -0.3391 -0.2524 920  LYS A CB  
6927  C CG  . LYS A 920  ? 2.8265 2.3625 2.7625 0.1283  -0.3680 -0.2787 920  LYS A CG  
6928  C CD  . LYS A 920  ? 2.8263 2.2993 2.7643 0.0996  -0.3774 -0.2842 920  LYS A CD  
6929  C CE  . LYS A 920  ? 2.7928 2.2540 2.7453 0.0943  -0.4061 -0.3077 920  LYS A CE  
6930  N NZ  . LYS A 920  ? 2.8145 2.1992 2.7558 0.0706  -0.4145 -0.3088 920  LYS A NZ  
6931  N N   . GLU A 921  ? 2.6394 2.3242 2.5707 0.2003  -0.3493 -0.2692 921  GLU A N   
6932  C CA  . GLU A 921  ? 2.5164 2.2901 2.4802 0.2186  -0.3529 -0.2832 921  GLU A CA  
6933  C C   . GLU A 921  ? 2.3868 2.1729 2.3713 0.2196  -0.3809 -0.3084 921  GLU A C   
6934  O O   . GLU A 921  ? 2.3794 2.1060 2.3364 0.2206  -0.3936 -0.3078 921  GLU A O   
6935  C CB  . GLU A 921  ? 2.5537 2.3415 2.4834 0.2502  -0.3356 -0.2635 921  GLU A CB  
6936  C CG  . GLU A 921  ? 2.5731 2.4542 2.5309 0.2728  -0.3336 -0.2728 921  GLU A CG  
6937  C CD  . GLU A 921  ? 2.6192 2.5571 2.5953 0.2745  -0.3116 -0.2642 921  GLU A CD  
6938  O OE1 . GLU A 921  ? 2.6599 2.5809 2.6468 0.2509  -0.3042 -0.2607 921  GLU A OE1 
6939  O OE2 . GLU A 921  ? 2.6144 2.6141 2.5938 0.2999  -0.3014 -0.2606 921  GLU A OE2 
6940  N N   . ILE A 922  ? 2.2522 2.1164 2.2848 0.2200  -0.3905 -0.3307 922  ILE A N   
6941  C CA  . ILE A 922  ? 2.1173 1.9985 2.1717 0.2218  -0.4171 -0.3557 922  ILE A CA  
6942  C C   . ILE A 922  ? 1.9935 1.9524 2.0642 0.2496  -0.4206 -0.3654 922  ILE A C   
6943  O O   . ILE A 922  ? 1.9549 1.9900 2.0572 0.2552  -0.4131 -0.3716 922  ILE A O   
6944  C CB  . ILE A 922  ? 2.0797 1.9722 2.1787 0.1934  -0.4339 -0.3805 922  ILE A CB  
6945  C CG1 . ILE A 922  ? 2.0887 1.8907 2.1676 0.1690  -0.4411 -0.3771 922  ILE A CG1 
6946  C CG2 . ILE A 922  ? 2.0572 1.9933 2.1845 0.2015  -0.4577 -0.4068 922  ILE A CG2 
6947  C CD1 . ILE A 922  ? 2.0706 1.8698 2.1846 0.1465  -0.4645 -0.4042 922  ILE A CD1 
6948  N N   . LEU A 923  ? 1.9333 1.8714 1.9821 0.2667  -0.4325 -0.3669 923  LEU A N   
6949  C CA  . LEU A 923  ? 1.8836 1.8837 1.9408 0.2951  -0.4367 -0.3746 923  LEU A CA  
6950  C C   . LEU A 923  ? 1.8578 1.8731 1.9431 0.2909  -0.4650 -0.4023 923  LEU A C   
6951  O O   . LEU A 923  ? 1.8905 1.8430 1.9595 0.2812  -0.4799 -0.4055 923  LEU A O   
6952  C CB  . LEU A 923  ? 1.8701 1.8325 1.8770 0.3198  -0.4260 -0.3525 923  LEU A CB  
6953  C CG  . LEU A 923  ? 1.8358 1.8222 1.8350 0.3475  -0.4352 -0.3580 923  LEU A CG  
6954  C CD1 . LEU A 923  ? 1.8139 1.8985 1.8499 0.3657  -0.4355 -0.3722 923  LEU A CD1 
6955  C CD2 . LEU A 923  ? 1.8369 1.7806 1.7839 0.3684  -0.4186 -0.3322 923  LEU A CD2 
6956  N N   . VAL A 924  ? 1.8132 1.9116 1.9403 0.2984  -0.4725 -0.4225 924  VAL A N   
6957  C CA  . VAL A 924  ? 1.7557 1.8755 1.9092 0.2983  -0.4991 -0.4494 924  VAL A CA  
6958  C C   . VAL A 924  ? 1.6588 1.8218 1.8065 0.3315  -0.5032 -0.4522 924  VAL A C   
6959  O O   . VAL A 924  ? 1.6145 1.8258 1.7568 0.3549  -0.4867 -0.4413 924  VAL A O   
6960  C CB  . VAL A 924  ? 1.7376 1.9130 1.9456 0.2790  -0.5114 -0.4763 924  VAL A CB  
6961  C CG1 . VAL A 924  ? 1.7419 1.8970 1.9652 0.2683  -0.5393 -0.5000 924  VAL A CG1 
6962  C CG2 . VAL A 924  ? 1.7678 1.9213 1.9858 0.2502  -0.5001 -0.4707 924  VAL A CG2 
6963  N N   . LYS A 925  ? 1.6261 1.7714 1.7759 0.3330  -0.5255 -0.4676 925  LYS A N   
6964  C CA  . LYS A 925  ? 1.5600 1.7214 1.6954 0.3619  -0.5312 -0.4680 925  LYS A CA  
6965  C C   . LYS A 925  ? 1.5147 1.7034 1.6847 0.3572  -0.5588 -0.4982 925  LYS A C   
6966  O O   . LYS A 925  ? 1.5816 1.7516 1.7738 0.3302  -0.5718 -0.5133 925  LYS A O   
6967  C CB  . LYS A 925  ? 1.5458 1.6220 1.6325 0.3641  -0.5286 -0.4486 925  LYS A CB  
6968  C CG  . LYS A 925  ? 1.5111 1.5934 1.5662 0.3951  -0.5158 -0.4316 925  LYS A CG  
6969  C CD  . LYS A 925  ? 1.5134 1.6199 1.5561 0.4056  -0.4886 -0.4112 925  LYS A CD  
6970  C CE  . LYS A 925  ? 1.5061 1.6419 1.5271 0.4405  -0.4761 -0.3990 925  LYS A CE  
6971  N NZ  . LYS A 925  ? 1.5258 1.6708 1.5253 0.4517  -0.4474 -0.3751 925  LYS A NZ  
6972  N N   . THR A 926  ? 1.3994 1.6307 1.5742 0.3827  -0.5674 -0.5073 926  THR A N   
6973  C CA  . THR A 926  ? 1.3092 1.5638 1.5146 0.3795  -0.5942 -0.5360 926  THR A CA  
6974  C C   . THR A 926  ? 1.2683 1.5146 1.4561 0.4029  -0.6055 -0.5378 926  THR A C   
6975  O O   . THR A 926  ? 1.2520 1.5275 1.4238 0.4315  -0.5941 -0.5264 926  THR A O   
6976  C CB  . THR A 926  ? 1.6332 1.9801 1.8864 0.3820  -0.5991 -0.5582 926  THR A CB  
6977  O OG1 . THR A 926  ? 1.6220 2.0230 1.8723 0.4021  -0.5769 -0.5439 926  THR A OG1 
6978  C CG2 . THR A 926  ? 1.6076 1.9508 1.8937 0.3473  -0.6065 -0.5738 926  THR A CG2 
6979  N N   . LEU A 927  ? 1.2551 1.4626 1.4465 0.3909  -0.6277 -0.5524 927  LEU A N   
6980  C CA  . LEU A 927  ? 1.2716 1.4486 1.4389 0.4077  -0.6375 -0.5499 927  LEU A CA  
6981  C C   . LEU A 927  ? 1.2575 1.4864 1.4519 0.4223  -0.6581 -0.5745 927  LEU A C   
6982  O O   . LEU A 927  ? 1.2672 1.4909 1.4853 0.4061  -0.6791 -0.5963 927  LEU A O   
6983  C CB  . LEU A 927  ? 1.3157 1.4017 1.4594 0.3862  -0.6466 -0.5447 927  LEU A CB  
6984  C CG  . LEU A 927  ? 1.3190 1.3455 1.4233 0.3972  -0.6488 -0.5309 927  LEU A CG  
6985  C CD1 . LEU A 927  ? 1.3287 1.2773 1.4218 0.3726  -0.6637 -0.5339 927  LEU A CD1 
6986  C CD2 . LEU A 927  ? 1.2993 1.3654 1.4098 0.4232  -0.6598 -0.5414 927  LEU A CD2 
6987  N N   . ARG A 928  ? 1.2328 1.5087 1.4217 0.4537  -0.6518 -0.5704 928  ARG A N   
6988  C CA  . ARG A 928  ? 1.2095 1.5332 1.4194 0.4714  -0.6697 -0.5912 928  ARG A CA  
6989  C C   . ARG A 928  ? 1.2351 1.5012 1.4293 0.4688  -0.6878 -0.5953 928  ARG A C   
6990  O O   . ARG A 928  ? 1.2504 1.4714 1.4090 0.4794  -0.6804 -0.5767 928  ARG A O   
6991  C CB  . ARG A 928  ? 1.1977 1.5832 1.4021 0.5073  -0.6560 -0.5831 928  ARG A CB  
6992  C CG  . ARG A 928  ? 1.2321 1.7058 1.4704 0.5150  -0.6504 -0.5944 928  ARG A CG  
6993  C CD  . ARG A 928  ? 1.3088 1.8227 1.5300 0.5430  -0.6251 -0.5740 928  ARG A CD  
6994  N NE  . ARG A 928  ? 1.4344 1.8910 1.6197 0.5360  -0.6034 -0.5457 928  ARG A NE  
6995  C CZ  . ARG A 928  ? 1.4839 1.9563 1.6677 0.5322  -0.5832 -0.5325 928  ARG A CZ  
6996  N NH1 . ARG A 928  ? 1.4836 2.0319 1.7016 0.5344  -0.5811 -0.5447 928  ARG A NH1 
6997  N NH2 . ARG A 928  ? 1.4821 1.8942 1.6292 0.5266  -0.5649 -0.5066 928  ARG A NH2 
6998  N N   . VAL A 929  ? 1.2420 1.5085 1.4626 0.4539  -0.7111 -0.6199 929  VAL A N   
6999  C CA  . VAL A 929  ? 1.2465 1.4673 1.4567 0.4531  -0.7303 -0.6269 929  VAL A CA  
7000  C C   . VAL A 929  ? 1.2208 1.5022 1.4564 0.4730  -0.7472 -0.6494 929  VAL A C   
7001  O O   . VAL A 929  ? 1.1845 1.5308 1.4540 0.4741  -0.7516 -0.6674 929  VAL A O   
7002  C CB  . VAL A 929  ? 1.3063 1.4670 1.5215 0.4197  -0.7443 -0.6359 929  VAL A CB  
7003  C CG1 . VAL A 929  ? 1.3088 1.4261 1.5150 0.4197  -0.7650 -0.6444 929  VAL A CG1 
7004  C CG2 . VAL A 929  ? 1.3191 1.4204 1.5073 0.4022  -0.7269 -0.6128 929  VAL A CG2 
7005  N N   . VAL A 930  ? 1.2283 1.4885 1.4477 0.4882  -0.7567 -0.6485 930  VAL A N   
7006  C CA  . VAL A 930  ? 1.2440 1.5610 1.4793 0.5138  -0.7680 -0.6638 930  VAL A CA  
7007  C C   . VAL A 930  ? 1.3107 1.5909 1.5444 0.5109  -0.7907 -0.6762 930  VAL A C   
7008  O O   . VAL A 930  ? 1.3747 1.5863 1.5944 0.4897  -0.7972 -0.6725 930  VAL A O   
7009  C CB  . VAL A 930  ? 1.2570 1.5924 1.4672 0.5453  -0.7502 -0.6438 930  VAL A CB  
7010  C CG1 . VAL A 930  ? 1.2413 1.6362 1.4670 0.5732  -0.7604 -0.6584 930  VAL A CG1 
7011  C CG2 . VAL A 930  ? 1.2601 1.6248 1.4651 0.5505  -0.7251 -0.6272 930  VAL A CG2 
7012  N N   . PRO A 931  ? 1.4245 1.7488 1.3320 0.6997  -0.5180 -0.7799 931  PRO A N   
7013  C CA  . PRO A 931  ? 1.4359 1.7771 1.3844 0.6880  -0.5282 -0.7945 931  PRO A CA  
7014  C C   . PRO A 931  ? 1.3711 1.7137 1.3556 0.6660  -0.5424 -0.8171 931  PRO A C   
7015  O O   . PRO A 931  ? 1.3976 1.7249 1.3651 0.6729  -0.5572 -0.8302 931  PRO A O   
7016  C CB  . PRO A 931  ? 1.4105 1.7605 1.3775 0.6706  -0.5047 -0.7754 931  PRO A CB  
7017  C CG  . PRO A 931  ? 1.3965 1.7347 1.3268 0.6759  -0.4843 -0.7501 931  PRO A CG  
7018  C CD  . PRO A 931  ? 1.3925 1.7174 1.3029 0.6819  -0.4909 -0.7562 931  PRO A CD  
7019  N N   . GLU A 932  ? 1.3346 1.6938 1.3652 0.6402  -0.5380 -0.8211 932  GLU A N   
7020  C CA  . GLU A 932  ? 1.3320 1.6983 1.3985 0.6205  -0.5546 -0.8435 932  GLU A CA  
7021  C C   . GLU A 932  ? 1.2592 1.6357 1.3717 0.5843  -0.5414 -0.8421 932  GLU A C   
7022  O O   . GLU A 932  ? 1.1943 1.5955 1.3393 0.5756  -0.5372 -0.8419 932  GLU A O   
7023  C CB  . GLU A 932  ? 1.3632 1.7536 1.4449 0.6335  -0.5757 -0.8598 932  GLU A CB  
7024  C CG  . GLU A 932  ? 1.4120 1.7979 1.4516 0.6705  -0.5871 -0.8594 932  GLU A CG  
7025  C CD  . GLU A 932  ? 1.4159 1.8057 1.4387 0.6860  -0.5697 -0.8380 932  GLU A CD  
7026  O OE1 . GLU A 932  ? 1.3993 1.7821 1.4228 0.6722  -0.5456 -0.8188 932  GLU A OE1 
7027  O OE2 . GLU A 932  ? 1.4373 1.8357 1.4444 0.7117  -0.5804 -0.8402 932  GLU A OE2 
7028  N N   . GLY A 933  ? 1.3057 1.6629 1.4191 0.5652  -0.5357 -0.8417 933  GLY A N   
7029  C CA  . GLY A 933  ? 1.2993 1.6624 1.4514 0.5311  -0.5223 -0.8390 933  GLY A CA  
7030  C C   . GLY A 933  ? 1.2680 1.6286 1.4187 0.5203  -0.4932 -0.8151 933  GLY A C   
7031  O O   . GLY A 933  ? 1.2222 1.6009 1.3886 0.5175  -0.4808 -0.8054 933  GLY A O   
7032  N N   . VAL A 934  ? 1.3262 1.6641 1.4572 0.5144  -0.4825 -0.8056 934  VAL A N   
7033  C CA  . VAL A 934  ? 1.3918 1.7269 1.5072 0.5128  -0.4567 -0.7807 934  VAL A CA  
7034  C C   . VAL A 934  ? 1.3497 1.6849 1.4872 0.4840  -0.4366 -0.7696 934  VAL A C   
7035  O O   . VAL A 934  ? 1.3342 1.6517 1.4621 0.4762  -0.4324 -0.7671 934  VAL A O   
7036  C CB  . VAL A 934  ? 1.4998 1.8149 1.5663 0.5347  -0.4537 -0.7699 934  VAL A CB  
7037  C CG1 . VAL A 934  ? 1.0465 1.3634 1.1028 0.5266  -0.4268 -0.7439 934  VAL A CG1 
7038  C CG2 . VAL A 934  ? 1.5710 1.8875 1.6074 0.5666  -0.4670 -0.7730 934  VAL A CG2 
7039  N N   . LYS A 935  ? 1.3463 1.7000 1.5087 0.4710  -0.4231 -0.7615 935  LYS A N   
7040  C CA  . LYS A 935  ? 1.3491 1.7058 1.5327 0.4444  -0.4034 -0.7506 935  LYS A CA  
7041  C C   . LYS A 935  ? 1.3882 1.7430 1.5467 0.4481  -0.3821 -0.7264 935  LYS A C   
7042  O O   . LYS A 935  ? 1.3750 1.7332 1.5137 0.4652  -0.3809 -0.7189 935  LYS A O   
7043  C CB  . LYS A 935  ? 1.3476 1.7272 1.5765 0.4267  -0.4034 -0.7594 935  LYS A CB  
7044  C CG  . LYS A 935  ? 0.9573 1.3420 1.2195 0.4093  -0.4181 -0.7790 935  LYS A CG  
7045  C CD  . LYS A 935  ? 1.0682 1.4274 1.3071 0.4155  -0.4327 -0.7882 935  LYS A CD  
7046  C CE  . LYS A 935  ? 1.1035 1.4531 1.3649 0.3880  -0.4335 -0.7952 935  LYS A CE  
7047  N NZ  . LYS A 935  ? 1.1437 1.5030 1.4336 0.3774  -0.4550 -0.8173 935  LYS A NZ  
7048  N N   . ARG A 936  ? 1.4061 1.7550 1.5630 0.4320  -0.3658 -0.7136 936  ARG A N   
7049  C CA  . ARG A 936  ? 1.4236 1.7755 1.5624 0.4298  -0.3455 -0.6909 936  ARG A CA  
7050  C C   . ARG A 936  ? 1.4362 1.7950 1.6019 0.4010  -0.3279 -0.6833 936  ARG A C   
7051  O O   . ARG A 936  ? 1.4733 1.8272 1.6529 0.3859  -0.3259 -0.6865 936  ARG A O   
7052  C CB  . ARG A 936  ? 1.4306 1.7727 1.5297 0.4453  -0.3420 -0.6783 936  ARG A CB  
7053  C CG  . ARG A 936  ? 1.4484 1.7824 1.5463 0.4337  -0.3340 -0.6732 936  ARG A CG  
7054  C CD  . ARG A 936  ? 1.5208 1.8415 1.5815 0.4578  -0.3420 -0.6728 936  ARG A CD  
7055  N NE  . ARG A 936  ? 1.5703 1.8945 1.6089 0.4581  -0.3252 -0.6522 936  ARG A NE  
7056  C CZ  . ARG A 936  ? 1.6223 1.9413 1.6246 0.4810  -0.3269 -0.6458 936  ARG A CZ  
7057  N NH1 . ARG A 936  ? 1.6443 1.9505 1.6262 0.5055  -0.3448 -0.6593 936  ARG A NH1 
7058  N NH2 . ARG A 936  ? 1.6262 1.9549 1.6119 0.4804  -0.3106 -0.6259 936  ARG A NH2 
7059  N N   . GLU A 937  ? 1.4472 1.8150 1.6184 0.3943  -0.3161 -0.6739 937  GLU A N   
7060  C CA  . GLU A 937  ? 1.5407 1.9158 1.7356 0.3687  -0.2994 -0.6672 937  GLU A CA  
7061  C C   . GLU A 937  ? 1.5918 1.9657 1.7631 0.3624  -0.2806 -0.6445 937  GLU A C   
7062  O O   . GLU A 937  ? 1.5219 1.8945 1.6737 0.3702  -0.2765 -0.6351 937  GLU A O   
7063  C CB  . GLU A 937  ? 1.6893 2.0755 1.9117 0.3648  -0.3016 -0.6771 937  GLU A CB  
7064  C CG  . GLU A 937  ? 2.3202 2.7054 2.5247 0.3869  -0.3087 -0.6777 937  GLU A CG  
7065  C CD  . GLU A 937  ? 2.4620 2.8608 2.6959 0.3905  -0.3183 -0.6939 937  GLU A CD  
7066  O OE1 . GLU A 937  ? 2.4651 2.8716 2.7133 0.3995  -0.3367 -0.7110 937  GLU A OE1 
7067  O OE2 . GLU A 937  ? 2.4548 2.8569 2.6956 0.3855  -0.3079 -0.6895 937  GLU A OE2 
7068  N N   . SER A 938  ? 1.6951 2.0693 1.8681 0.3471  -0.2694 -0.6356 938  SER A N   
7069  C CA  . SER A 938  ? 1.7427 2.1191 1.8905 0.3428  -0.2542 -0.6141 938  SER A CA  
7070  C C   . SER A 938  ? 1.8689 2.2515 2.0312 0.3172  -0.2366 -0.6042 938  SER A C   
7071  O O   . SER A 938  ? 1.9611 2.3481 2.1045 0.3101  -0.2235 -0.5861 938  SER A O   
7072  C CB  . SER A 938  ? 1.4637 1.8369 1.6003 0.3471  -0.2552 -0.6114 938  SER A CB  
7073  O OG  . SER A 938  ? 1.2894 1.6598 1.4547 0.3303  -0.2548 -0.6209 938  SER A OG  
7074  N N   . TYR A 939  ? 2.0021 2.3869 2.1979 0.3028  -0.2365 -0.6161 939  TYR A N   
7075  C CA  . TYR A 939  ? 2.1165 2.5071 2.3289 0.2780  -0.2203 -0.6091 939  TYR A CA  
7076  C C   . TYR A 939  ? 1.9588 2.3508 2.1523 0.2685  -0.2052 -0.5915 939  TYR A C   
7077  O O   . TYR A 939  ? 1.8580 2.2546 2.0591 0.2481  -0.1913 -0.5834 939  TYR A O   
7078  C CB  . TYR A 939  ? 2.4976 2.8935 2.7485 0.2665  -0.2226 -0.6247 939  TYR A CB  
7079  C CG  . TYR A 939  ? 2.7087 3.1073 2.9686 0.2729  -0.2264 -0.6329 939  TYR A CG  
7080  C CD1 . TYR A 939  ? 2.7796 3.1765 3.0319 0.2650  -0.2135 -0.6237 939  TYR A CD1 
7081  C CD2 . TYR A 939  ? 2.7923 3.1949 3.0678 0.2867  -0.2431 -0.6503 939  TYR A CD2 
7082  C CE1 . TYR A 939  ? 2.8121 3.2082 3.0694 0.2734  -0.2166 -0.6313 939  TYR A CE1 
7083  C CE2 . TYR A 939  ? 2.8234 3.2306 3.1067 0.2950  -0.2464 -0.6575 939  TYR A CE2 
7084  C CZ  . TYR A 939  ? 2.8315 3.2342 3.1047 0.2894  -0.2328 -0.6478 939  TYR A CZ  
7085  O OH  . TYR A 939  ? 2.8487 3.2526 3.1259 0.3003  -0.2357 -0.6547 939  TYR A OH  
7086  N N   . SER A 940  ? 1.8635 2.2504 2.0309 0.2824  -0.2084 -0.5855 940  SER A N   
7087  C CA  . SER A 940  ? 1.7893 2.1742 1.9343 0.2725  -0.1958 -0.5684 940  SER A CA  
7088  C C   . SER A 940  ? 1.6556 2.0504 1.7805 0.2671  -0.1873 -0.5504 940  SER A C   
7089  O O   . SER A 940  ? 1.6532 2.0526 1.7680 0.2818  -0.1939 -0.5495 940  SER A O   
7090  C CB  . SER A 940  ? 1.8339 2.2082 1.9553 0.2890  -0.2024 -0.5670 940  SER A CB  
7091  O OG  . SER A 940  ? 1.8449 2.2216 1.9482 0.3094  -0.2124 -0.5656 940  SER A OG  
7092  N N   . GLY A 941  ? 1.5228 1.9214 1.6408 0.2466  -0.1729 -0.5363 941  GLY A N   
7093  C CA  . GLY A 941  ? 1.4093 1.8230 1.5102 0.2378  -0.1631 -0.5175 941  GLY A CA  
7094  C C   . GLY A 941  ? 1.3277 1.7427 1.4282 0.2115  -0.1488 -0.5074 941  GLY A C   
7095  O O   . GLY A 941  ? 1.3168 1.7196 1.4318 0.2025  -0.1469 -0.5169 941  GLY A O   
7096  N N   . VAL A 942  ? 1.2642 1.6953 1.3472 0.1999  -0.1392 -0.4883 942  VAL A N   
7097  C CA  . VAL A 942  ? 1.1592 1.5945 1.2409 0.1728  -0.1258 -0.4780 942  VAL A CA  
7098  C C   . VAL A 942  ? 1.0912 1.5527 1.1674 0.1651  -0.1180 -0.4624 942  VAL A C   
7099  O O   . VAL A 942  ? 1.1145 1.5909 1.1793 0.1809  -0.1217 -0.4554 942  VAL A O   
7100  C CB  . VAL A 942  ? 1.1398 1.5675 1.1941 0.1619  -0.1217 -0.4655 942  VAL A CB  
7101  C CG1 . VAL A 942  ? 1.1464 1.5671 1.2033 0.1357  -0.1111 -0.4633 942  VAL A CG1 
7102  C CG2 . VAL A 942  ? 1.1619 1.5667 1.2078 0.1776  -0.1310 -0.4747 942  VAL A CG2 
7103  N N   . THR A 943  ? 0.9988 1.4677 1.0811 0.1423  -0.1070 -0.4563 943  THR A N   
7104  C CA  . THR A 943  ? 0.9380 1.4354 1.0066 0.1332  -0.0991 -0.4367 943  THR A CA  
7105  C C   . THR A 943  ? 0.9362 1.4370 0.9835 0.1106  -0.0919 -0.4220 943  THR A C   
7106  O O   . THR A 943  ? 0.9557 1.4449 1.0067 0.0898  -0.0856 -0.4243 943  THR A O   
7107  C CB  . THR A 943  ? 0.8765 1.3881 0.9620 0.1262  -0.0924 -0.4358 943  THR A CB  
7108  O OG1 . THR A 943  ? 0.8812 1.3896 0.9787 0.1483  -0.0999 -0.4460 943  THR A OG1 
7109  C CG2 . THR A 943  ? 0.8260 1.3702 0.8947 0.1168  -0.0843 -0.4141 943  THR A CG2 
7110  N N   . LEU A 944  ? 0.8963 1.4115 0.9198 0.1147  -0.0932 -0.4072 944  LEU A N   
7111  C CA  . LEU A 944  ? 0.8729 1.3913 0.8736 0.0915  -0.0874 -0.3918 944  LEU A CA  
7112  C C   . LEU A 944  ? 0.9096 1.4564 0.9129 0.0701  -0.0774 -0.3793 944  LEU A C   
7113  O O   . LEU A 944  ? 0.9130 1.4935 0.9187 0.0787  -0.0754 -0.3694 944  LEU A O   
7114  C CB  . LEU A 944  ? 0.8451 1.3771 0.8211 0.1011  -0.0909 -0.3775 944  LEU A CB  
7115  C CG  . LEU A 944  ? 0.8385 1.3362 0.8056 0.1156  -0.0997 -0.3883 944  LEU A CG  
7116  C CD1 . LEU A 944  ? 0.8425 1.3470 0.7797 0.1171  -0.1012 -0.3719 944  LEU A CD1 
7117  C CD2 . LEU A 944  ? 0.8274 1.2901 0.7967 0.0989  -0.0978 -0.3988 944  LEU A CD2 
7118  N N   . ASP A 945  ? 0.9129 1.4454 0.9147 0.0443  -0.0714 -0.3803 945  ASP A N   
7119  C CA  . ASP A 945  ? 0.8928 1.4496 0.8969 0.0214  -0.0622 -0.3699 945  ASP A CA  
7120  C C   . ASP A 945  ? 0.8715 1.4166 0.8539 -0.0082 -0.0582 -0.3620 945  ASP A C   
7121  O O   . ASP A 945  ? 0.8961 1.4104 0.8799 -0.0201 -0.0562 -0.3732 945  ASP A O   
7122  C CB  . ASP A 945  ? 0.9046 1.4499 0.9339 0.0198  -0.0586 -0.3846 945  ASP A CB  
7123  C CG  . ASP A 945  ? 0.8836 1.4617 0.9184 0.0071  -0.0504 -0.3736 945  ASP A CG  
7124  O OD1 . ASP A 945  ? 0.8795 1.4857 0.8967 -0.0083 -0.0468 -0.3552 945  ASP A OD1 
7125  O OD2 . ASP A 945  ? 0.8581 1.4347 0.9143 0.0127  -0.0479 -0.3828 945  ASP A OD2 
7126  N N   . PRO A 946  ? 0.8364 1.4066 0.7976 -0.0211 -0.0567 -0.3425 946  PRO A N   
7127  C CA  . PRO A 946  ? 0.8675 1.4149 0.8028 -0.0485 -0.0555 -0.3366 946  PRO A CA  
7128  C C   . PRO A 946  ? 0.8750 1.4288 0.8097 -0.0777 -0.0483 -0.3336 946  PRO A C   
7129  O O   . PRO A 946  ? 0.8871 1.4122 0.8028 -0.1019 -0.0468 -0.3345 946  PRO A O   
7130  C CB  . PRO A 946  ? 0.8587 1.4379 0.7735 -0.0534 -0.0564 -0.3149 946  PRO A CB  
7131  C CG  . PRO A 946  ? 0.8285 1.4576 0.7609 -0.0307 -0.0556 -0.3077 946  PRO A CG  
7132  C CD  . PRO A 946  ? 0.8009 1.4230 0.7607 -0.0168 -0.0545 -0.3241 946  PRO A CD  
7133  N N   . ARG A 947  ? 0.8712 1.4622 0.8253 -0.0733 -0.0441 -0.3300 947  ARG A N   
7134  C CA  . ARG A 947  ? 0.8674 1.4823 0.8213 -0.0981 -0.0372 -0.3217 947  ARG A CA  
7135  C C   . ARG A 947  ? 0.8559 1.4532 0.8325 -0.0919 -0.0337 -0.3387 947  ARG A C   
7136  O O   . ARG A 947  ? 0.8802 1.5014 0.8651 -0.1018 -0.0279 -0.3344 947  ARG A O   
7137  C CB  . ARG A 947  ? 0.8630 1.5382 0.8213 -0.0934 -0.0347 -0.3030 947  ARG A CB  
7138  C CG  . ARG A 947  ? 0.8692 1.5775 0.8058 -0.1057 -0.0358 -0.2813 947  ARG A CG  
7139  C CD  . ARG A 947  ? 0.8680 1.5952 0.7880 -0.1449 -0.0320 -0.2675 947  ARG A CD  
7140  N NE  . ARG A 947  ? 0.8525 1.6461 0.7762 -0.1488 -0.0282 -0.2477 947  ARG A NE  
7141  C CZ  . ARG A 947  ? 0.8857 1.7207 0.7937 -0.1644 -0.0284 -0.2263 947  ARG A CZ  
7142  N NH1 . ARG A 947  ? 0.9074 1.7210 0.7935 -0.1791 -0.0321 -0.2213 947  ARG A NH1 
7143  N NH2 . ARG A 947  ? 0.8862 1.7858 0.7997 -0.1653 -0.0247 -0.2088 947  ARG A NH2 
7144  N N   . GLY A 948  ? 0.8465 1.4053 0.8343 -0.0745 -0.0373 -0.3575 948  GLY A N   
7145  C CA  . GLY A 948  ? 0.8278 1.3701 0.8381 -0.0698 -0.0338 -0.3738 948  GLY A CA  
7146  C C   . GLY A 948  ? 0.7827 1.3552 0.8160 -0.0614 -0.0293 -0.3722 948  GLY A C   
7147  O O   . GLY A 948  ? 0.7673 1.3259 0.8196 -0.0585 -0.0260 -0.3851 948  GLY A O   
7148  N N   . ILE A 949  ? 0.7544 1.3675 0.7851 -0.0566 -0.0288 -0.3563 949  ILE A N   
7149  C CA  . ILE A 949  ? 0.7456 1.3847 0.7938 -0.0444 -0.0252 -0.3536 949  ILE A CA  
7150  C C   . ILE A 949  ? 0.7469 1.3616 0.8201 -0.0295 -0.0251 -0.3716 949  ILE A C   
7151  O O   . ILE A 949  ? 0.6799 1.3041 0.7654 -0.0314 -0.0193 -0.3715 949  ILE A O   
7152  C CB  . ILE A 949  ? 0.6754 1.3414 0.7210 -0.0214 -0.0295 -0.3438 949  ILE A CB  
7153  C CG1 . ILE A 949  ? 0.8490 1.5414 0.8713 -0.0332 -0.0305 -0.3257 949  ILE A CG1 
7154  C CG2 . ILE A 949  ? 0.6611 1.3549 0.7173 -0.0093 -0.0254 -0.3376 949  ILE A CG2 
7155  C CD1 . ILE A 949  ? 0.8236 1.5591 0.8383 -0.0524 -0.0239 -0.3077 949  ILE A CD1 
7156  N N   . TYR A 950  ? 0.7892 1.3741 0.8697 -0.0145 -0.0321 -0.3862 950  TYR A N   
7157  C CA  . TYR A 950  ? 0.8302 1.3979 0.9355 0.0032  -0.0346 -0.4021 950  TYR A CA  
7158  C C   . TYR A 950  ? 0.8406 1.3800 0.9608 -0.0052 -0.0319 -0.4185 950  TYR A C   
7159  O O   . TYR A 950  ? 0.8647 1.3922 1.0076 0.0059  -0.0336 -0.4315 950  TYR A O   
7160  C CB  . TYR A 950  ? 0.7243 1.2869 0.8315 0.0303  -0.0449 -0.4070 950  TYR A CB  
7161  C CG  . TYR A 950  ? 0.7082 1.2993 0.8121 0.0434  -0.0442 -0.3949 950  TYR A CG  
7162  C CD1 . TYR A 950  ? 0.6556 1.2427 0.7757 0.0571  -0.0446 -0.4015 950  TYR A CD1 
7163  C CD2 . TYR A 950  ? 0.6982 1.3216 0.7816 0.0399  -0.0421 -0.3757 950  TYR A CD2 
7164  C CE1 . TYR A 950  ? 0.6546 1.2648 0.7675 0.0705  -0.0432 -0.3897 950  TYR A CE1 
7165  C CE2 . TYR A 950  ? 0.7173 1.3703 0.7962 0.0535  -0.0405 -0.3636 950  TYR A CE2 
7166  C CZ  . TYR A 950  ? 0.7256 1.3702 0.8178 0.0701  -0.0410 -0.3708 950  TYR A CZ  
7167  O OH  . TYR A 950  ? 0.7169 1.3886 0.7998 0.0861  -0.0393 -0.3580 950  TYR A OH  
7168  N N   . GLY A 951  ? 0.8442 1.3734 0.9504 -0.0252 -0.0277 -0.4173 951  GLY A N   
7169  C CA  . GLY A 951  ? 0.8899 1.3964 1.0072 -0.0337 -0.0231 -0.4309 951  GLY A CA  
7170  C C   . GLY A 951  ? 0.9450 1.4226 1.0447 -0.0398 -0.0255 -0.4371 951  GLY A C   
7171  O O   . GLY A 951  ? 0.9684 1.4266 1.0688 -0.0488 -0.0207 -0.4463 951  GLY A O   
7172  N N   . THR A 952  ? 0.9572 1.4307 1.0393 -0.0335 -0.0328 -0.4317 952  THR A N   
7173  C CA  . THR A 952  ? 0.9496 1.3934 1.0077 -0.0404 -0.0352 -0.4343 952  THR A CA  
7174  C C   . THR A 952  ? 0.9303 1.3790 0.9674 -0.0361 -0.0420 -0.4227 952  THR A C   
7175  O O   . THR A 952  ? 0.9080 1.3843 0.9509 -0.0247 -0.0450 -0.4141 952  THR A O   
7176  C CB  . THR A 952  ? 0.9466 1.3607 1.0172 -0.0241 -0.0392 -0.4532 952  THR A CB  
7177  O OG1 . THR A 952  ? 0.9921 1.3791 1.0369 -0.0216 -0.0449 -0.4532 952  THR A OG1 
7178  C CG2 . THR A 952  ? 0.9085 1.3342 1.0078 -0.0001 -0.0455 -0.4614 952  THR A CG2 
7179  N N   . ILE A 953  ? 0.9231 1.3430 0.9339 -0.0438 -0.0443 -0.4223 953  ILE A N   
7180  C CA  . ILE A 953  ? 0.9663 1.3899 0.9539 -0.0433 -0.0496 -0.4094 953  ILE A CA  
7181  C C   . ILE A 953  ? 1.0949 1.4988 1.0840 -0.0168 -0.0589 -0.4185 953  ILE A C   
7182  O O   . ILE A 953  ? 1.1406 1.5079 1.1239 -0.0103 -0.0616 -0.4311 953  ILE A O   
7183  C CB  . ILE A 953  ? 1.0187 1.4286 0.9717 -0.0732 -0.0463 -0.3980 953  ILE A CB  
7184  C CG1 . ILE A 953  ? 1.0418 1.4061 0.9668 -0.0727 -0.0511 -0.4020 953  ILE A CG1 
7185  C CG2 . ILE A 953  ? 1.0656 1.4711 1.0212 -0.0926 -0.0385 -0.4025 953  ILE A CG2 
7186  C CD1 . ILE A 953  ? 1.0488 1.4036 0.9358 -0.1043 -0.0493 -0.3865 953  ILE A CD1 
7187  N N   . SER A 954  ? 1.0421 1.4721 1.0390 0.0005  -0.0638 -0.4126 954  SER A N   
7188  C CA  . SER A 954  ? 0.9742 1.3928 0.9728 0.0270  -0.0733 -0.4198 954  SER A CA  
7189  C C   . SER A 954  ? 0.9635 1.3830 0.9311 0.0233  -0.0760 -0.4041 954  SER A C   
7190  O O   . SER A 954  ? 0.9691 1.4222 0.9337 0.0260  -0.0760 -0.3901 954  SER A O   
7191  C CB  . SER A 954  ? 0.8927 1.3377 0.9159 0.0490  -0.0772 -0.4234 954  SER A CB  
7192  O OG  . SER A 954  ? 0.8720 1.2984 0.9148 0.0706  -0.0845 -0.4426 954  SER A OG  
7193  N N   . ARG A 955  ? 0.9684 1.3518 0.9113 0.0175  -0.0780 -0.4051 955  ARG A N   
7194  C CA  . ARG A 955  ? 0.9806 1.3624 0.8943 0.0169  -0.0815 -0.3905 955  ARG A CA  
7195  C C   . ARG A 955  ? 1.0419 1.3891 0.9469 0.0397  -0.0898 -0.4011 955  ARG A C   
7196  O O   . ARG A 955  ? 1.0917 1.4212 0.9663 0.0366  -0.0922 -0.3912 955  ARG A O   
7197  C CB  . ARG A 955  ? 0.9897 1.3606 0.8720 -0.0158 -0.0762 -0.3757 955  ARG A CB  
7198  C CG  . ARG A 955  ? 0.9807 1.3915 0.8678 -0.0394 -0.0689 -0.3621 955  ARG A CG  
7199  C CD  . ARG A 955  ? 0.9834 1.3678 0.8439 -0.0725 -0.0646 -0.3572 955  ARG A CD  
7200  N NE  . ARG A 955  ? 0.9231 1.3407 0.7824 -0.1007 -0.0581 -0.3441 955  ARG A NE  
7201  C CZ  . ARG A 955  ? 0.9241 1.3181 0.7616 -0.1303 -0.0548 -0.3423 955  ARG A CZ  
7202  N NH1 . ARG A 955  ? 0.9591 1.2960 0.7747 -0.1320 -0.0569 -0.3529 955  ARG A NH1 
7203  N NH2 . ARG A 955  ? 0.9682 1.3940 0.8039 -0.1566 -0.0498 -0.3305 955  ARG A NH2 
7204  N N   . ARG A 956  ? 1.0041 1.3424 0.9353 0.0619  -0.0944 -0.4209 956  ARG A N   
7205  C CA  . ARG A 956  ? 1.0161 1.3289 0.9437 0.0873  -0.1035 -0.4322 956  ARG A CA  
7206  C C   . ARG A 956  ? 1.0771 1.3968 1.0410 0.1088  -0.1085 -0.4518 956  ARG A C   
7207  O O   . ARG A 956  ? 1.0548 1.3815 1.0420 0.1005  -0.1034 -0.4599 956  ARG A O   
7208  C CB  . ARG A 956  ? 1.0143 1.2798 0.9154 0.0811  -0.1032 -0.4359 956  ARG A CB  
7209  C CG  . ARG A 956  ? 1.0501 1.2989 0.9137 0.0805  -0.1063 -0.4216 956  ARG A CG  
7210  C CD  . ARG A 956  ? 1.1235 1.3203 0.9536 0.0714  -0.1053 -0.4226 956  ARG A CD  
7211  N NE  . ARG A 956  ? 1.1621 1.3303 0.9982 0.0990  -0.1120 -0.4412 956  ARG A NE  
7212  C CZ  . ARG A 956  ? 1.2211 1.3455 1.0247 0.1077  -0.1158 -0.4415 956  ARG A CZ  
7213  N NH1 . ARG A 956  ? 1.2522 1.3536 1.0138 0.0889  -0.1136 -0.4237 956  ARG A NH1 
7214  N NH2 . ARG A 956  ? 1.2327 1.3374 1.0453 0.1353  -0.1220 -0.4591 956  ARG A NH2 
7215  N N   . LYS A 957  ? 1.1561 1.4760 1.1236 0.1356  -0.1187 -0.4584 957  LYS A N   
7216  C CA  . LYS A 957  ? 1.1663 1.4823 1.1617 0.1585  -0.1269 -0.4793 957  LYS A CA  
7217  C C   . LYS A 957  ? 1.1526 1.4497 1.1298 0.1808  -0.1369 -0.4820 957  LYS A C   
7218  O O   . LYS A 957  ? 1.1194 1.4222 1.0740 0.1852  -0.1392 -0.4687 957  LYS A O   
7219  C CB  . LYS A 957  ? 1.1624 1.5089 1.1867 0.1693  -0.1307 -0.4847 957  LYS A CB  
7220  C CG  . LYS A 957  ? 1.2171 1.5596 1.2697 0.1896  -0.1402 -0.5062 957  LYS A CG  
7221  C CD  . LYS A 957  ? 1.2552 1.6133 1.3426 0.1816  -0.1365 -0.5156 957  LYS A CD  
7222  C CE  . LYS A 957  ? 1.3072 1.6572 1.4218 0.1918  -0.1421 -0.5362 957  LYS A CE  
7223  N NZ  . LYS A 957  ? 1.3420 1.6922 1.4648 0.2180  -0.1573 -0.5488 957  LYS A NZ  
7224  N N   . GLU A 958  ? 1.2129 1.4889 1.1989 0.1948  -0.1421 -0.4984 958  GLU A N   
7225  C CA  . GLU A 958  ? 1.2934 1.5533 1.2669 0.2204  -0.1532 -0.5043 958  GLU A CA  
7226  C C   . GLU A 958  ? 1.2920 1.5721 1.2989 0.2428  -0.1642 -0.5213 958  GLU A C   
7227  O O   . GLU A 958  ? 1.2878 1.5761 1.3266 0.2414  -0.1639 -0.5353 958  GLU A O   
7228  C CB  . GLU A 958  ? 1.3900 1.6138 1.3497 0.2234  -0.1524 -0.5116 958  GLU A CB  
7229  C CG  . GLU A 958  ? 1.5006 1.6973 1.4281 0.2426  -0.1600 -0.5088 958  GLU A CG  
7230  C CD  . GLU A 958  ? 1.6031 1.7604 1.5136 0.2473  -0.1586 -0.5159 958  GLU A CD  
7231  O OE1 . GLU A 958  ? 1.6501 1.7787 1.5305 0.2270  -0.1497 -0.5054 958  GLU A OE1 
7232  O OE2 . GLU A 958  ? 1.6244 1.7796 1.5504 0.2718  -0.1668 -0.5322 958  GLU A OE2 
7233  N N   . PHE A 959  ? 1.2778 1.5669 1.2768 0.2620  -0.1739 -0.5195 959  PHE A N   
7234  C CA  . PHE A 959  ? 1.2844 1.5846 1.3077 0.2859  -0.1875 -0.5372 959  PHE A CA  
7235  C C   . PHE A 959  ? 1.3683 1.6473 1.3724 0.3083  -0.1969 -0.5420 959  PHE A C   
7236  O O   . PHE A 959  ? 1.4060 1.6727 1.3752 0.3125  -0.1968 -0.5280 959  PHE A O   
7237  C CB  . PHE A 959  ? 1.1968 1.5194 1.2217 0.2950  -0.1930 -0.5337 959  PHE A CB  
7238  C CG  . PHE A 959  ? 1.1343 1.4737 1.1568 0.2750  -0.1819 -0.5188 959  PHE A CG  
7239  C CD1 . PHE A 959  ? 1.1104 1.4695 1.1578 0.2722  -0.1819 -0.5243 959  PHE A CD1 
7240  C CD2 . PHE A 959  ? 1.1117 1.4473 1.1060 0.2583  -0.1715 -0.4989 959  PHE A CD2 
7241  C CE1 . PHE A 959  ? 1.0858 1.4619 1.1295 0.2558  -0.1714 -0.5097 959  PHE A CE1 
7242  C CE2 . PHE A 959  ? 1.0890 1.4451 1.0820 0.2400  -0.1615 -0.4847 959  PHE A CE2 
7243  C CZ  . PHE A 959  ? 1.0755 1.4526 1.0931 0.2403  -0.1614 -0.4901 959  PHE A CZ  
7244  N N   . PRO A 960  ? 1.3960 1.6723 1.4220 0.3226  -0.2048 -0.5606 960  PRO A N   
7245  C CA  . PRO A 960  ? 1.4859 1.7411 1.4917 0.3448  -0.2131 -0.5645 960  PRO A CA  
7246  C C   . PRO A 960  ? 1.5833 1.8533 1.6018 0.3716  -0.2301 -0.5779 960  PRO A C   
7247  O O   . PRO A 960  ? 1.5692 1.8615 1.6057 0.3723  -0.2353 -0.5821 960  PRO A O   
7248  C CB  . PRO A 960  ? 1.4808 1.7254 1.5019 0.3422  -0.2091 -0.5758 960  PRO A CB  
7249  C CG  . PRO A 960  ? 1.2939 1.5592 1.3486 0.3186  -0.1998 -0.5792 960  PRO A CG  
7250  C CD  . PRO A 960  ? 1.3117 1.6006 1.3770 0.3157  -0.2034 -0.5759 960  PRO A CD  
7251  N N   . TYR A 961  ? 1.6839 1.9394 1.6900 0.3942  -0.2389 -0.5843 961  TYR A N   
7252  C CA  . TYR A 961  ? 1.7720 2.0425 1.7953 0.4197  -0.2562 -0.6010 961  TYR A CA  
7253  C C   . TYR A 961  ? 1.7958 2.0858 1.8634 0.4186  -0.2600 -0.6204 961  TYR A C   
7254  O O   . TYR A 961  ? 1.8189 2.1007 1.8930 0.4148  -0.2533 -0.6237 961  TYR A O   
7255  C CB  . TYR A 961  ? 1.8536 2.1022 1.8479 0.4444  -0.2634 -0.6007 961  TYR A CB  
7256  C CG  . TYR A 961  ? 1.9142 2.1607 1.8809 0.4628  -0.2727 -0.5941 961  TYR A CG  
7257  C CD1 . TYR A 961  ? 1.9414 2.1949 1.9106 0.4919  -0.2899 -0.6072 961  TYR A CD1 
7258  C CD2 . TYR A 961  ? 1.9386 2.1790 1.8766 0.4518  -0.2646 -0.5745 961  TYR A CD2 
7259  C CE1 . TYR A 961  ? 1.9712 2.2226 1.9134 0.5102  -0.2984 -0.6014 961  TYR A CE1 
7260  C CE2 . TYR A 961  ? 1.9769 2.2176 1.8888 0.4698  -0.2723 -0.5678 961  TYR A CE2 
7261  C CZ  . TYR A 961  ? 1.9985 2.2431 1.9118 0.4994  -0.2891 -0.5815 961  TYR A CZ  
7262  O OH  . TYR A 961  ? 2.0397 2.2850 1.9256 0.5185  -0.2968 -0.5750 961  TYR A OH  
7263  N N   . ARG A 962  ? 1.8154 2.1306 1.9120 0.4225  -0.2711 -0.6331 962  ARG A N   
7264  C CA  . ARG A 962  ? 1.8590 2.1959 1.9961 0.4271  -0.2796 -0.6529 962  ARG A CA  
7265  C C   . ARG A 962  ? 1.8191 2.1712 1.9642 0.4477  -0.2998 -0.6660 962  ARG A C   
7266  O O   . ARG A 962  ? 1.7776 2.1389 1.9290 0.4431  -0.3053 -0.6681 962  ARG A O   
7267  C CB  . ARG A 962  ? 1.9512 2.3052 2.1244 0.4010  -0.2704 -0.6567 962  ARG A CB  
7268  C CG  . ARG A 962  ? 2.0619 2.4443 2.2802 0.4034  -0.2805 -0.6768 962  ARG A CG  
7269  C CD  . ARG A 962  ? 2.1510 2.5443 2.3982 0.3849  -0.2676 -0.6796 962  ARG A CD  
7270  N NE  . ARG A 962  ? 2.2063 2.6097 2.4749 0.3589  -0.2594 -0.6772 962  ARG A NE  
7271  C CZ  . ARG A 962  ? 2.2393 2.6633 2.5451 0.3436  -0.2543 -0.6849 962  ARG A CZ  
7272  N NH1 . ARG A 962  ? 2.2563 2.6968 2.5842 0.3521  -0.2565 -0.6957 962  ARG A NH1 
7273  N NH2 . ARG A 962  ? 2.2372 2.6665 2.5576 0.3207  -0.2467 -0.6812 962  ARG A NH2 
7274  N N   . ILE A 963  ? 1.7864 2.1386 1.9270 0.4721  -0.3110 -0.6745 963  ILE A N   
7275  C CA  . ILE A 963  ? 1.7012 2.0684 1.8482 0.4936  -0.3317 -0.6883 963  ILE A CA  
7276  C C   . ILE A 963  ? 1.6851 2.0834 1.8800 0.4895  -0.3405 -0.7077 963  ILE A C   
7277  O O   . ILE A 963  ? 1.6821 2.0897 1.8942 0.4921  -0.3375 -0.7131 963  ILE A O   
7278  C CB  . ILE A 963  ? 1.6024 1.9568 1.7208 0.5224  -0.3398 -0.6874 963  ILE A CB  
7279  C CG1 . ILE A 963  ? 1.5574 1.8777 1.6300 0.5211  -0.3258 -0.6660 963  ILE A CG1 
7280  C CG2 . ILE A 963  ? 1.6045 1.9678 1.7157 0.5432  -0.3592 -0.6961 963  ILE A CG2 
7281  C CD1 . ILE A 963  ? 1.5605 1.8625 1.6008 0.5485  -0.3322 -0.6631 963  ILE A CD1 
7282  N N   . PRO A 964  ? 1.7047 2.1190 1.9205 0.4821  -0.3510 -0.7177 964  PRO A N   
7283  C CA  . PRO A 964  ? 1.7169 2.1622 1.9797 0.4732  -0.3607 -0.7358 964  PRO A CA  
7284  C C   . PRO A 964  ? 1.7805 2.2443 2.0509 0.4985  -0.3809 -0.7510 964  PRO A C   
7285  O O   . PRO A 964  ? 1.8028 2.2573 2.0469 0.5183  -0.3939 -0.7522 964  PRO A O   
7286  C CB  . PRO A 964  ? 1.7069 2.1512 1.9749 0.4589  -0.3657 -0.7386 964  PRO A CB  
7287  C CG  . PRO A 964  ? 1.6639 2.0799 1.8914 0.4565  -0.3527 -0.7190 964  PRO A CG  
7288  C CD  . PRO A 964  ? 1.6784 2.0795 1.8717 0.4785  -0.3517 -0.7101 964  PRO A CD  
7289  N N   . LEU A 965  ? 1.8130 2.3049 2.1177 0.4994  -0.3839 -0.7620 965  LEU A N   
7290  C CA  . LEU A 965  ? 1.9056 2.4164 2.2134 0.5269  -0.4021 -0.7742 965  LEU A CA  
7291  C C   . LEU A 965  ? 1.9448 2.4725 2.2643 0.5311  -0.4257 -0.7900 965  LEU A C   
7292  O O   . LEU A 965  ? 1.9703 2.5230 2.3022 0.5495  -0.4436 -0.8034 965  LEU A O   
7293  C CB  . LEU A 965  ? 1.9331 2.4733 2.2726 0.5308  -0.3990 -0.7811 965  LEU A CB  
7294  C CG  . LEU A 965  ? 2.1223 2.6407 2.4404 0.5368  -0.3793 -0.7677 965  LEU A CG  
7295  C CD1 . LEU A 965  ? 2.1271 2.6785 2.4787 0.5420  -0.3765 -0.7761 965  LEU A CD1 
7296  C CD2 . LEU A 965  ? 2.1562 2.6398 2.4226 0.5639  -0.3803 -0.7574 965  LEU A CD2 
7297  N N   . ASP A 966  ? 1.9342 2.4471 2.2471 0.5150  -0.4261 -0.7882 966  ASP A N   
7298  C CA  . ASP A 966  ? 1.9133 2.4318 2.2277 0.5189  -0.4480 -0.8023 966  ASP A CA  
7299  C C   . ASP A 966  ? 1.8325 2.3202 2.0981 0.5374  -0.4520 -0.7943 966  ASP A C   
7300  O O   . ASP A 966  ? 1.8421 2.3261 2.0998 0.5412  -0.4679 -0.8038 966  ASP A O   
7301  C CB  . ASP A 966  ? 1.9432 2.4666 2.2859 0.4883  -0.4478 -0.8085 966  ASP A CB  
7302  C CG  . ASP A 966  ? 1.9575 2.5195 2.3524 0.4714  -0.4514 -0.8211 966  ASP A CG  
7303  O OD1 . ASP A 966  ? 1.9685 2.5601 2.3807 0.4859  -0.4673 -0.8339 966  ASP A OD1 
7304  O OD2 . ASP A 966  ? 1.9468 2.5119 2.3654 0.4438  -0.4381 -0.8175 966  ASP A OD2 
7305  N N   . LEU A 967  ? 1.7372 2.2024 1.9685 0.5485  -0.4375 -0.7767 967  LEU A N   
7306  C CA  . LEU A 967  ? 1.6839 2.1223 1.8686 0.5636  -0.4378 -0.7657 967  LEU A CA  
7307  C C   . LEU A 967  ? 1.6499 2.0929 1.8170 0.5932  -0.4602 -0.7767 967  LEU A C   
7308  O O   . LEU A 967  ? 1.6693 2.1262 1.8417 0.6111  -0.4683 -0.7828 967  LEU A O   
7309  C CB  . LEU A 967  ? 1.6883 2.1035 1.8409 0.5669  -0.4178 -0.7438 967  LEU A CB  
7310  C CG  . LEU A 967  ? 1.7265 2.1177 1.8299 0.5826  -0.4164 -0.7296 967  LEU A CG  
7311  C CD1 . LEU A 967  ? 1.7338 2.1202 1.8310 0.5732  -0.4181 -0.7295 967  LEU A CD1 
7312  C CD2 . LEU A 967  ? 1.7313 2.1004 1.8063 0.5789  -0.3958 -0.7072 967  LEU A CD2 
7313  N N   . VAL A 968  ? 1.6017 2.0327 1.7459 0.6000  -0.4699 -0.7790 968  VAL A N   
7314  C CA  . VAL A 968  ? 1.5605 1.9918 1.6805 0.6294  -0.4907 -0.7881 968  VAL A CA  
7315  C C   . VAL A 968  ? 1.5748 1.9912 1.6545 0.6550  -0.4848 -0.7727 968  VAL A C   
7316  O O   . VAL A 968  ? 1.5625 1.9568 1.6099 0.6545  -0.4694 -0.7534 968  VAL A O   
7317  C CB  . VAL A 968  ? 1.5223 1.9399 1.6216 0.6316  -0.5004 -0.7929 968  VAL A CB  
7318  C CG1 . VAL A 968  ? 1.4805 1.9099 1.6158 0.6105  -0.5123 -0.8118 968  VAL A CG1 
7319  C CG2 . VAL A 968  ? 1.5206 1.9152 1.5926 0.6234  -0.4800 -0.7721 968  VAL A CG2 
7320  N N   . PRO A 969  ? 1.5953 2.0251 1.6768 0.6770  -0.4971 -0.7806 969  PRO A N   
7321  C CA  . PRO A 969  ? 1.6477 2.0624 1.6911 0.7034  -0.4940 -0.7678 969  PRO A CA  
7322  C C   . PRO A 969  ? 1.7327 2.1219 1.7260 0.7170  -0.4904 -0.7528 969  PRO A C   
7323  O O   . PRO A 969  ? 1.7439 2.1323 1.7276 0.7197  -0.5002 -0.7590 969  PRO A O   
7324  C CB  . PRO A 969  ? 1.6523 2.0905 1.7057 0.7282  -0.5177 -0.7861 969  PRO A CB  
7325  C CG  . PRO A 969  ? 1.6135 2.0837 1.7214 0.7081  -0.5244 -0.8039 969  PRO A CG  
7326  C CD  . PRO A 969  ? 1.5880 2.0511 1.7112 0.6765  -0.5149 -0.8026 969  PRO A CD  
7327  N N   . LYS A 970  ? 1.8274 2.1954 1.7875 0.7261  -0.4764 -0.7329 970  LYS A N   
7328  C CA  . LYS A 970  ? 1.9491 2.2951 1.8604 0.7379  -0.4700 -0.7147 970  LYS A CA  
7329  C C   . LYS A 970  ? 1.9757 2.3184 1.8826 0.7212  -0.4626 -0.7090 970  LYS A C   
7330  O O   . LYS A 970  ? 1.9855 2.3236 1.8623 0.7369  -0.4687 -0.7061 970  LYS A O   
7331  C CB  . LYS A 970  ? 2.0602 2.4068 1.9419 0.7732  -0.4888 -0.7205 970  LYS A CB  
7332  C CG  . LYS A 970  ? 2.1803 2.5148 2.0384 0.7949  -0.4877 -0.7118 970  LYS A CG  
7333  C CD  . LYS A 970  ? 2.2986 2.6253 2.1125 0.8282  -0.4997 -0.7082 970  LYS A CD  
7334  C CE  . LYS A 970  ? 2.3729 2.6888 2.1651 0.8536  -0.5026 -0.7031 970  LYS A CE  
7335  N NZ  . LYS A 970  ? 2.4251 2.7368 2.1767 0.8874  -0.5166 -0.7019 970  LYS A NZ  
7336  N N   . THR A 971  ? 1.9991 2.3449 1.9348 0.6910  -0.4492 -0.7071 971  THR A N   
7337  C CA  . THR A 971  ? 2.0274 2.3691 1.9585 0.6736  -0.4385 -0.6983 971  THR A CA  
7338  C C   . THR A 971  ? 2.0014 2.3352 1.9380 0.6471  -0.4146 -0.6803 971  THR A C   
7339  O O   . THR A 971  ? 2.0086 2.3480 1.9777 0.6297  -0.4094 -0.6858 971  THR A O   
7340  C CB  . THR A 971  ? 2.0426 2.3971 2.0068 0.6608  -0.4493 -0.7180 971  THR A CB  
7341  O OG1 . THR A 971  ? 1.9996 2.3608 2.0019 0.6313  -0.4376 -0.7190 971  THR A OG1 
7342  C CG2 . THR A 971  ? 2.0856 2.4533 2.0626 0.6789  -0.4750 -0.7418 971  THR A CG2 
7343  N N   . GLU A 972  ? 1.9810 2.3036 1.8851 0.6443  -0.4003 -0.6587 972  GLU A N   
7344  C CA  . GLU A 972  ? 1.9371 2.2512 1.8392 0.6195  -0.3778 -0.6392 972  GLU A CA  
7345  C C   . GLU A 972  ? 1.7909 2.1150 1.7245 0.5923  -0.3697 -0.6425 972  GLU A C   
7346  O O   . GLU A 972  ? 1.7349 2.0683 1.6808 0.5940  -0.3794 -0.6549 972  GLU A O   
7347  C CB  . GLU A 972  ? 2.0616 2.3661 1.9194 0.6245  -0.3667 -0.6148 972  GLU A CB  
7348  C CG  . GLU A 972  ? 2.1812 2.4929 2.0163 0.6475  -0.3781 -0.6174 972  GLU A CG  
7349  C CD  . GLU A 972  ? 2.2775 2.5862 2.0707 0.6522  -0.3660 -0.5921 972  GLU A CD  
7350  O OE1 . GLU A 972  ? 2.2887 2.5951 2.0771 0.6293  -0.3472 -0.5725 972  GLU A OE1 
7351  O OE2 . GLU A 972  ? 2.3312 2.6418 2.0961 0.6785  -0.3757 -0.5920 972  GLU A OE2 
7352  N N   . ILE A 973  ? 1.7022 2.0218 1.6466 0.5675  -0.3524 -0.6318 973  ILE A N   
7353  C CA  . ILE A 973  ? 1.5882 1.9167 1.5601 0.5414  -0.3431 -0.6327 973  ILE A CA  
7354  C C   . ILE A 973  ? 1.6364 1.9647 1.5850 0.5312  -0.3285 -0.6118 973  ILE A C   
7355  O O   . ILE A 973  ? 1.6724 1.9924 1.6008 0.5209  -0.3140 -0.5924 973  ILE A O   
7356  C CB  . ILE A 973  ? 1.4223 1.7487 1.4192 0.5194  -0.3316 -0.6325 973  ILE A CB  
7357  C CG1 . ILE A 973  ? 1.3883 1.7189 1.4079 0.5306  -0.3441 -0.6510 973  ILE A CG1 
7358  C CG2 . ILE A 973  ? 1.3495 1.6866 1.3755 0.4947  -0.3241 -0.6353 973  ILE A CG2 
7359  C CD1 . ILE A 973  ? 1.3667 1.6927 1.4026 0.5149  -0.3322 -0.6492 973  ILE A CD1 
7360  N N   . LYS A 974  ? 1.6202 1.9575 1.5707 0.5340  -0.3330 -0.6162 974  LYS A N   
7361  C CA  . LYS A 974  ? 1.5956 1.9389 1.5274 0.5266  -0.3203 -0.5980 974  LYS A CA  
7362  C C   . LYS A 974  ? 1.4941 1.8426 1.4521 0.4963  -0.3060 -0.5940 974  LYS A C   
7363  O O   . LYS A 974  ? 1.4744 1.8240 1.4662 0.4856  -0.3104 -0.6100 974  LYS A O   
7364  C CB  . LYS A 974  ? 1.6578 2.0055 1.5762 0.5475  -0.3322 -0.6057 974  LYS A CB  
7365  C CG  . LYS A 974  ? 1.7341 2.0914 1.6271 0.5487  -0.3208 -0.5867 974  LYS A CG  
7366  C CD  . LYS A 974  ? 1.8381 2.1955 1.7149 0.5740  -0.3343 -0.5971 974  LYS A CD  
7367  C CE  . LYS A 974  ? 1.8805 2.2485 1.7447 0.5718  -0.3233 -0.5841 974  LYS A CE  
7368  N NZ  . LYS A 974  ? 1.9095 2.2738 1.7521 0.5990  -0.3357 -0.5937 974  LYS A NZ  
7369  N N   . ARG A 975  ? 1.4288 1.7825 1.3713 0.4817  -0.2890 -0.5720 975  ARG A N   
7370  C CA  . ARG A 975  ? 1.3429 1.7041 1.3051 0.4549  -0.2753 -0.5661 975  ARG A CA  
7371  C C   . ARG A 975  ? 1.2790 1.6524 1.2169 0.4467  -0.2603 -0.5414 975  ARG A C   
7372  O O   . ARG A 975  ? 1.2993 1.6717 1.2105 0.4479  -0.2545 -0.5250 975  ARG A O   
7373  C CB  . ARG A 975  ? 1.3074 1.6610 1.2924 0.4336  -0.2682 -0.5691 975  ARG A CB  
7374  C CG  . ARG A 975  ? 1.2986 1.6403 1.2609 0.4318  -0.2619 -0.5563 975  ARG A CG  
7375  C CD  . ARG A 975  ? 1.2790 1.6082 1.2615 0.4254  -0.2631 -0.5680 975  ARG A CD  
7376  N NE  . ARG A 975  ? 1.2935 1.6047 1.2484 0.4243  -0.2567 -0.5548 975  ARG A NE  
7377  C CZ  . ARG A 975  ? 1.2750 1.5741 1.2292 0.4028  -0.2440 -0.5470 975  ARG A CZ  
7378  N NH1 . ARG A 975  ? 1.2366 1.5432 1.2189 0.3816  -0.2361 -0.5514 975  ARG A NH1 
7379  N NH2 . ARG A 975  ? 1.2977 1.5748 1.2211 0.4030  -0.2396 -0.5351 975  ARG A NH2 
7380  N N   . ILE A 976  ? 1.2080 1.5938 1.1552 0.4378  -0.2543 -0.5385 976  ILE A N   
7381  C CA  . ILE A 976  ? 1.1535 1.5580 1.0798 0.4330  -0.2414 -0.5161 976  ILE A CA  
7382  C C   . ILE A 976  ? 1.1042 1.5170 1.0450 0.4021  -0.2255 -0.5049 976  ILE A C   
7383  O O   . ILE A 976  ? 1.1171 1.5243 1.0866 0.3882  -0.2249 -0.5167 976  ILE A O   
7384  C CB  . ILE A 976  ? 1.1513 1.5645 1.0730 0.4497  -0.2465 -0.5205 976  ILE A CB  
7385  C CG1 . ILE A 976  ? 1.2144 1.6131 1.1322 0.4766  -0.2657 -0.5405 976  ILE A CG1 
7386  C CG2 . ILE A 976  ? 1.1335 1.5707 1.0265 0.4557  -0.2360 -0.4970 976  ILE A CG2 
7387  C CD1 . ILE A 976  ? 1.2590 1.6499 1.1932 0.4815  -0.2750 -0.5586 976  ILE A CD1 
7388  N N   . LEU A 977  ? 1.0177 1.4457 0.9378 0.3911  -0.2127 -0.4815 977  LEU A N   
7389  C CA  . LEU A 977  ? 0.9217 1.3601 0.8505 0.3612  -0.1977 -0.4684 977  LEU A CA  
7390  C C   . LEU A 977  ? 0.9037 1.3722 0.8229 0.3611  -0.1890 -0.4522 977  LEU A C   
7391  O O   . LEU A 977  ? 0.9322 1.4180 0.8255 0.3723  -0.1869 -0.4367 977  LEU A O   
7392  C CB  . LEU A 977  ? 0.9089 1.3408 0.8187 0.3462  -0.1904 -0.4533 977  LEU A CB  
7393  C CG  . LEU A 977  ? 0.9136 1.3495 0.8304 0.3126  -0.1764 -0.4419 977  LEU A CG  
7394  C CD1 . LEU A 977  ? 0.9067 1.3122 0.8330 0.2998  -0.1770 -0.4526 977  LEU A CD1 
7395  C CD2 . LEU A 977  ? 0.9606 1.4148 0.8484 0.3017  -0.1668 -0.4159 977  LEU A CD2 
7396  N N   . SER A 978  ? 0.8969 1.3737 0.8358 0.3489  -0.1834 -0.4542 978  SER A N   
7397  C CA  . SER A 978  ? 0.9593 1.4662 0.8887 0.3514  -0.1752 -0.4388 978  SER A CA  
7398  C C   . SER A 978  ? 1.0585 1.5839 0.9972 0.3212  -0.1603 -0.4242 978  SER A C   
7399  O O   . SER A 978  ? 1.1113 1.6346 1.0709 0.3116  -0.1574 -0.4313 978  SER A O   
7400  C CB  . SER A 978  ? 0.9495 1.4511 0.8863 0.3723  -0.1833 -0.4533 978  SER A CB  
7401  O OG  . SER A 978  ? 0.8502 1.3796 0.7756 0.3773  -0.1750 -0.4381 978  SER A OG  
7402  N N   . VAL A 979  ? 1.0674 1.6115 0.9888 0.3062  -0.1511 -0.4032 979  VAL A N   
7403  C CA  . VAL A 979  ? 1.0141 1.5763 0.9399 0.2748  -0.1379 -0.3880 979  VAL A CA  
7404  C C   . VAL A 979  ? 0.9984 1.6028 0.9172 0.2770  -0.1295 -0.3701 979  VAL A C   
7405  O O   . VAL A 979  ? 1.0344 1.6654 0.9316 0.2895  -0.1279 -0.3546 979  VAL A O   
7406  C CB  . VAL A 979  ? 0.9911 1.5527 0.8970 0.2574  -0.1335 -0.3729 979  VAL A CB  
7407  C CG1 . VAL A 979  ? 0.9566 1.5284 0.8663 0.2223  -0.1220 -0.3607 979  VAL A CG1 
7408  C CG2 . VAL A 979  ? 1.0096 1.5309 0.9148 0.2630  -0.1425 -0.3884 979  VAL A CG2 
7409  N N   . LYS A 980  ? 0.9680 1.5817 0.9037 0.2661  -0.1235 -0.3709 980  LYS A N   
7410  C CA  . LYS A 980  ? 0.9838 1.6414 0.9111 0.2685  -0.1148 -0.3518 980  LYS A CA  
7411  C C   . LYS A 980  ? 0.9567 1.6328 0.8971 0.2414  -0.1040 -0.3430 980  LYS A C   
7412  O O   . LYS A 980  ? 0.9665 1.6189 0.9270 0.2269  -0.1036 -0.3560 980  LYS A O   
7413  C CB  . LYS A 980  ? 1.0047 1.6671 0.9271 0.3034  -0.1203 -0.3580 980  LYS A CB  
7414  C CG  . LYS A 980  ? 1.0254 1.6447 0.9596 0.3203  -0.1328 -0.3843 980  LYS A CG  
7415  C CD  . LYS A 980  ? 1.0257 1.6334 0.9422 0.3457  -0.1434 -0.3903 980  LYS A CD  
7416  C CE  . LYS A 980  ? 0.9935 1.6293 0.8852 0.3752  -0.1432 -0.3786 980  LYS A CE  
7417  N NZ  . LYS A 980  ? 0.9966 1.6209 0.8705 0.3962  -0.1528 -0.3835 980  LYS A NZ  
7418  N N   . GLY A 981  ? 0.9382 1.6604 0.8669 0.2352  -0.0952 -0.3202 981  GLY A N   
7419  C CA  . GLY A 981  ? 0.8951 1.6398 0.8343 0.2120  -0.0856 -0.3109 981  GLY A CA  
7420  C C   . GLY A 981  ? 0.8689 1.6108 0.8190 0.2312  -0.0862 -0.3199 981  GLY A C   
7421  O O   . GLY A 981  ? 0.8869 1.6244 0.8290 0.2631  -0.0922 -0.3258 981  GLY A O   
7422  N N   . LEU A 982  ? 0.8205 1.5622 0.7864 0.2115  -0.0801 -0.3211 982  LEU A N   
7423  C CA  . LEU A 982  ? 0.8093 1.5481 0.7845 0.2246  -0.0788 -0.3270 982  LEU A CA  
7424  C C   . LEU A 982  ? 0.8664 1.5551 0.8574 0.2347  -0.0872 -0.3523 982  LEU A C   
7425  O O   . LEU A 982  ? 0.8713 1.5330 0.8600 0.2504  -0.0972 -0.3660 982  LEU A O   
7426  C CB  . LEU A 982  ? 0.7700 1.5445 0.7277 0.2537  -0.0770 -0.3136 982  LEU A CB  
7427  C CG  . LEU A 982  ? 0.7356 1.5689 0.6793 0.2453  -0.0685 -0.2869 982  LEU A CG  
7428  C CD1 . LEU A 982  ? 0.7328 1.6040 0.6727 0.2566  -0.0612 -0.2736 982  LEU A CD1 
7429  C CD2 . LEU A 982  ? 0.7251 1.5643 0.6762 0.2051  -0.0635 -0.2803 982  LEU A CD2 
7430  N N   . LEU A 983  ? 0.9064 1.5850 0.9134 0.2243  -0.0830 -0.3578 983  LEU A N   
7431  C CA  . LEU A 983  ? 0.9429 1.5781 0.9674 0.2288  -0.0896 -0.3801 983  LEU A CA  
7432  C C   . LEU A 983  ? 1.0459 1.6692 1.0581 0.2629  -0.0980 -0.3867 983  LEU A C   
7433  O O   . LEU A 983  ? 1.0506 1.6374 1.0709 0.2727  -0.1078 -0.4061 983  LEU A O   
7434  C CB  . LEU A 983  ? 0.8957 1.5282 0.9362 0.2114  -0.0818 -0.3805 983  LEU A CB  
7435  C CG  . LEU A 983  ? 0.8834 1.5087 0.9409 0.1785  -0.0764 -0.3838 983  LEU A CG  
7436  C CD1 . LEU A 983  ? 0.8605 1.4878 0.9109 0.1675  -0.0783 -0.3813 983  LEU A CD1 
7437  C CD2 . LEU A 983  ? 0.9015 1.5539 0.9603 0.1593  -0.0645 -0.3692 983  LEU A CD2 
7438  N N   . VAL A 984  ? 0.7596 1.2887 0.8803 0.1454  0.0300  -0.2056 984  VAL A N   
7439  C CA  . VAL A 984  ? 0.7913 1.3278 0.9088 0.1633  0.0241  -0.1998 984  VAL A CA  
7440  C C   . VAL A 984  ? 0.9733 1.4843 1.0553 0.1758  0.0193  -0.1907 984  VAL A C   
7441  O O   . VAL A 984  ? 0.9787 1.4978 1.0471 0.1848  0.0206  -0.1804 984  VAL A O   
7442  C CB  . VAL A 984  ? 0.7803 1.3557 0.9055 0.1523  0.0351  -0.1876 984  VAL A CB  
7443  C CG1 . VAL A 984  ? 0.7941 1.3811 0.8934 0.1457  0.0443  -0.1688 984  VAL A CG1 
7444  C CG2 . VAL A 984  ? 0.7614 1.3450 0.8980 0.1687  0.0292  -0.1902 984  VAL A CG2 
7445  N N   . GLY A 985  ? 0.9971 1.4743 1.0620 0.1762  0.0139  -0.1951 985  GLY A N   
7446  C CA  . GLY A 985  ? 1.0213 1.4675 1.0473 0.1846  0.0086  -0.1872 985  GLY A CA  
7447  C C   . GLY A 985  ? 1.0255 1.4408 1.0433 0.2095  -0.0096 -0.1942 985  GLY A C   
7448  O O   . GLY A 985  ? 1.0945 1.4925 1.0800 0.2166  -0.0123 -0.1854 985  GLY A O   
7449  N N   . GLU A 986  ? 1.0049 1.4132 1.0497 0.2216  -0.0222 -0.2100 986  GLU A N   
7450  C CA  . GLU A 986  ? 0.9951 1.3820 1.0339 0.2433  -0.0398 -0.2151 986  GLU A CA  
7451  C C   . GLU A 986  ? 0.9692 1.3779 1.0072 0.2468  -0.0347 -0.2082 986  GLU A C   
7452  O O   . GLU A 986  ? 1.0223 1.4150 1.0305 0.2556  -0.0376 -0.2002 986  GLU A O   
7453  C CB  . GLU A 986  ? 0.9915 1.3783 1.0651 0.2541  -0.0535 -0.2333 986  GLU A CB  
7454  C CG  . GLU A 986  ? 1.0428 1.3936 1.1027 0.2742  -0.0753 -0.2386 986  GLU A CG  
7455  C CD  . GLU A 986  ? 1.1108 1.4241 1.1423 0.2741  -0.0786 -0.2349 986  GLU A CD  
7456  O OE1 . GLU A 986  ? 1.1105 1.4070 1.1554 0.2835  -0.0898 -0.2460 986  GLU A OE1 
7457  O OE2 . GLU A 986  ? 1.1621 1.4628 1.1561 0.2641  -0.0692 -0.2206 986  GLU A OE2 
7458  N N   . ILE A 987  ? 0.9114 1.3545 0.9787 0.2393  -0.0260 -0.2110 987  ILE A N   
7459  C CA  . ILE A 987  ? 0.8888 1.3471 0.9552 0.2461  -0.0230 -0.2063 987  ILE A CA  
7460  C C   . ILE A 987  ? 0.9478 1.4105 0.9849 0.2454  -0.0117 -0.1894 987  ILE A C   
7461  O O   . ILE A 987  ? 0.9608 1.4281 0.9891 0.2554  -0.0093 -0.1846 987  ILE A O   
7462  C CB  . ILE A 987  ? 0.8287 1.3209 0.9246 0.2358  -0.0140 -0.2088 987  ILE A CB  
7463  C CG1 . ILE A 987  ? 0.8761 1.3754 1.0028 0.2247  -0.0157 -0.2229 987  ILE A CG1 
7464  C CG2 . ILE A 987  ? 0.7642 1.2567 0.8609 0.2480  -0.0192 -0.2119 987  ILE A CG2 
7465  C CD1 . ILE A 987  ? 0.9048 1.4296 1.0594 0.2165  -0.0120 -0.2303 987  ILE A CD1 
7466  N N   . LEU A 988  ? 0.9893 1.4519 1.0109 0.2326  -0.0033 -0.1807 988  LEU A N   
7467  C CA  . LEU A 988  ? 1.0220 1.4925 1.0155 0.2299  0.0083  -0.1652 988  LEU A CA  
7468  C C   . LEU A 988  ? 1.0836 1.5144 1.0391 0.2400  -0.0005 -0.1636 988  LEU A C   
7469  O O   . LEU A 988  ? 1.1289 1.5585 1.0636 0.2488  0.0036  -0.1568 988  LEU A O   
7470  C CB  . LEU A 988  ? 1.0322 1.5244 1.0233 0.2072  0.0223  -0.1556 988  LEU A CB  
7471  C CG  . LEU A 988  ? 1.0037 1.5433 1.0221 0.1956  0.0350  -0.1495 988  LEU A CG  
7472  C CD1 . LEU A 988  ? 1.0230 1.5789 1.0354 0.1700  0.0463  -0.1411 988  LEU A CD1 
7473  C CD2 . LEU A 988  ? 0.9641 1.5285 0.9803 0.2075  0.0424  -0.1395 988  LEU A CD2 
7474  N N   . SER A 989  ? 1.0907 1.4872 1.0351 0.2391  -0.0122 -0.1700 989  SER A N   
7475  C CA  . SER A 989  ? 1.1179 1.4708 1.0219 0.2475  -0.0230 -0.1681 989  SER A CA  
7476  C C   . SER A 989  ? 1.0869 1.4248 0.9872 0.2674  -0.0355 -0.1733 989  SER A C   
7477  O O   . SER A 989  ? 1.0993 1.4135 0.9635 0.2735  -0.0377 -0.1678 989  SER A O   
7478  C CB  . SER A 989  ? 1.1733 1.4893 1.0686 0.2461  -0.0360 -0.1749 989  SER A CB  
7479  O OG  . SER A 989  ? 1.2467 1.5174 1.0996 0.2541  -0.0484 -0.1721 989  SER A OG  
7480  N N   . ALA A 990  ? 1.0434 1.3948 0.9786 0.2752  -0.0427 -0.1841 990  ALA A N   
7481  C CA  . ALA A 990  ? 1.0629 1.3992 0.9925 0.2911  -0.0547 -0.1895 990  ALA A CA  
7482  C C   . ALA A 990  ? 1.0661 1.4131 0.9777 0.2953  -0.0414 -0.1804 990  ALA A C   
7483  O O   . ALA A 990  ? 1.1306 1.4530 1.0168 0.3065  -0.0483 -0.1808 990  ALA A O   
7484  C CB  . ALA A 990  ? 1.0412 1.3909 1.0106 0.2953  -0.0649 -0.2038 990  ALA A CB  
7485  N N   . VAL A 991  ? 0.9948 1.3778 0.9180 0.2872  -0.0225 -0.1722 991  VAL A N   
7486  C CA  . VAL A 991  ? 1.0123 1.4062 0.9219 0.2954  -0.0103 -0.1648 991  VAL A CA  
7487  C C   . VAL A 991  ? 1.0651 1.4589 0.9420 0.2908  0.0028  -0.1523 991  VAL A C   
7488  O O   . VAL A 991  ? 1.0948 1.4906 0.9522 0.2996  0.0129  -0.1466 991  VAL A O   
7489  C CB  . VAL A 991  ? 0.6759 1.1091 0.6189 0.2943  0.0001  -0.1641 991  VAL A CB  
7490  C CG1 . VAL A 991  ? 0.6719 1.1227 0.6028 0.3034  0.0162  -0.1537 991  VAL A CG1 
7491  C CG2 . VAL A 991  ? 0.6731 1.0965 0.6352 0.3001  -0.0134 -0.1774 991  VAL A CG2 
7492  N N   . LEU A 992  ? 1.0941 1.4831 0.9619 0.2766  0.0031  -0.1489 992  LEU A N   
7493  C CA  . LEU A 992  ? 1.1911 1.5822 1.0266 0.2683  0.0164  -0.1376 992  LEU A CA  
7494  C C   . LEU A 992  ? 1.4344 1.7785 1.2324 0.2630  0.0044  -0.1388 992  LEU A C   
7495  O O   . LEU A 992  ? 1.5167 1.8610 1.2977 0.2461  0.0113  -0.1323 992  LEU A O   
7496  C CB  . LEU A 992  ? 1.0740 1.5107 0.9266 0.2503  0.0335  -0.1283 992  LEU A CB  
7497  C CG  . LEU A 992  ? 0.9655 1.4484 0.8609 0.2507  0.0413  -0.1273 992  LEU A CG  
7498  C CD1 . LEU A 992  ? 0.9201 1.4346 0.8294 0.2280  0.0508  -0.1207 992  LEU A CD1 
7499  C CD2 . LEU A 992  ? 0.9598 1.4692 0.8558 0.2640  0.0543  -0.1204 992  LEU A CD2 
7500  N N   . SER A 993  ? 1.5734 1.8759 1.3561 0.2764  -0.0142 -0.1465 993  SER A N   
7501  C CA  . SER A 993  ? 1.7250 1.9769 1.4665 0.2741  -0.0283 -0.1467 993  SER A CA  
7502  C C   . SER A 993  ? 1.8675 2.0846 1.5834 0.2892  -0.0410 -0.1504 993  SER A C   
7503  O O   . SER A 993  ? 1.9338 2.1098 1.6041 0.2876  -0.0482 -0.1475 993  SER A O   
7504  C CB  . SER A 993  ? 1.7115 1.9451 1.4694 0.2725  -0.0453 -0.1543 993  SER A CB  
7505  O OG  . SER A 993  ? 1.6912 1.9463 1.4607 0.2552  -0.0331 -0.1502 993  SER A OG  
7506  N N   . GLN A 994  ? 1.9469 2.1786 1.6896 0.3018  -0.0439 -0.1569 994  GLN A N   
7507  C CA  . GLN A 994  ? 2.0712 2.2743 1.7907 0.3146  -0.0534 -0.1606 994  GLN A CA  
7508  C C   . GLN A 994  ? 2.0768 2.3066 1.7985 0.3203  -0.0328 -0.1569 994  GLN A C   
7509  O O   . GLN A 994  ? 2.0064 2.2777 1.7645 0.3197  -0.0207 -0.1561 994  GLN A O   
7510  C CB  . GLN A 994  ? 2.1205 2.3161 1.8676 0.3239  -0.0751 -0.1725 994  GLN A CB  
7511  C CG  . GLN A 994  ? 2.1204 2.3597 1.9182 0.3238  -0.0676 -0.1777 994  GLN A CG  
7512  C CD  . GLN A 994  ? 2.1530 2.3914 1.9585 0.3338  -0.0729 -0.1850 994  GLN A CD  
7513  O OE1 . GLN A 994  ? 2.2030 2.4087 1.9879 0.3403  -0.0902 -0.1900 994  GLN A OE1 
7514  N NE2 . GLN A 994  ? 2.1140 2.3861 1.9458 0.3339  -0.0587 -0.1851 994  GLN A NE2 
7515  N N   . GLU A 995  ? 2.1864 2.3906 1.8676 0.3262  -0.0285 -0.1545 995  GLU A N   
7516  C CA  . GLU A 995  ? 2.2436 2.4663 1.9242 0.3361  -0.0099 -0.1525 995  GLU A CA  
7517  C C   . GLU A 995  ? 2.2444 2.4539 1.9357 0.3477  -0.0220 -0.1618 995  GLU A C   
7518  O O   . GLU A 995  ? 2.2340 2.4218 1.9308 0.3472  -0.0448 -0.1695 995  GLU A O   
7519  C CB  . GLU A 995  ? 2.3422 2.5426 1.9731 0.3375  0.0030  -0.1473 995  GLU A CB  
7520  C CG  . GLU A 995  ? 2.3829 2.6197 2.0116 0.3296  0.0283  -0.1374 995  GLU A CG  
7521  C CD  . GLU A 995  ? 2.4467 2.6663 2.0469 0.3117  0.0252  -0.1326 995  GLU A CD  
7522  O OE1 . GLU A 995  ? 2.4907 2.6612 2.0622 0.3090  0.0043  -0.1363 995  GLU A OE1 
7523  O OE2 . GLU A 995  ? 2.4492 2.7038 2.0540 0.2998  0.0430  -0.1249 995  GLU A OE2 
7524  N N   . GLY A 996  ? 2.2552 2.4779 1.9482 0.3581  -0.0068 -0.1611 996  GLY A N   
7525  C CA  . GLY A 996  ? 2.2898 2.4958 1.9847 0.3672  -0.0159 -0.1695 996  GLY A CA  
7526  C C   . GLY A 996  ? 2.2785 2.5005 2.0161 0.3624  -0.0317 -0.1775 996  GLY A C   
7527  O O   . GLY A 996  ? 2.2795 2.4955 2.0286 0.3551  -0.0492 -0.1816 996  GLY A O   
7528  N N   . ILE A 997  ? 2.2812 2.5223 2.0409 0.3670  -0.0251 -0.1801 997  ILE A N   
7529  C CA  . ILE A 997  ? 2.2553 2.5156 2.0558 0.3606  -0.0364 -0.1883 997  ILE A CA  
7530  C C   . ILE A 997  ? 2.3145 2.5488 2.1139 0.3570  -0.0620 -0.1996 997  ILE A C   
7531  O O   . ILE A 997  ? 2.3633 2.5602 2.1266 0.3612  -0.0716 -0.2019 997  ILE A O   
7532  C CB  . ILE A 997  ? 2.1921 2.4634 2.0015 0.3662  -0.0263 -0.1895 997  ILE A CB  
7533  C CG1 . ILE A 997  ? 2.2171 2.4483 1.9963 0.3716  -0.0362 -0.1976 997  ILE A CG1 
7534  C CG2 . ILE A 997  ? 2.1844 2.4730 1.9842 0.3758  -0.0025 -0.1777 997  ILE A CG2 
7535  C CD1 . ILE A 997  ? 2.2107 2.4374 1.9782 0.3810  -0.0226 -0.1963 997  ILE A CD1 
7536  N N   . ASN A 998  ? 2.3035 2.5593 2.1428 0.3489  -0.0730 -0.2068 998  ASN A N   
7537  C CA  . ASN A 998  ? 2.3260 2.5666 2.1724 0.3466  -0.0976 -0.2170 998  ASN A CA  
7538  C C   . ASN A 998  ? 2.2143 2.4850 2.1091 0.3390  -0.1048 -0.2282 998  ASN A C   
7539  O O   . ASN A 998  ? 2.2167 2.5186 2.1410 0.3330  -0.0927 -0.2264 998  ASN A O   
7540  C CB  . ASN A 998  ? 2.4357 2.6620 2.2707 0.3464  -0.1062 -0.2125 998  ASN A CB  
7541  C CG  . ASN A 998  ? 2.5071 2.7331 2.3676 0.3451  -0.1297 -0.2226 998  ASN A CG  
7542  O OD1 . ASN A 998  ? 2.5472 2.7647 2.4113 0.3468  -0.1470 -0.2318 998  ASN A OD1 
7543  N ND2 . ASN A 998  ? 2.5239 2.7592 2.4014 0.3422  -0.1302 -0.2208 998  ASN A ND2 
7544  N N   . ILE A 999  ? 2.0994 2.3619 2.0013 0.3378  -0.1241 -0.2399 999  ILE A N   
7545  C CA  . ILE A 999  ? 1.9473 2.2392 1.8954 0.3298  -0.1324 -0.2530 999  ILE A CA  
7546  C C   . ILE A 999  ? 1.8170 2.1241 1.7960 0.3293  -0.1399 -0.2559 999  ILE A C   
7547  O O   . ILE A 999  ? 1.7947 2.0810 1.7550 0.3357  -0.1471 -0.2499 999  ILE A O   
7548  C CB  . ILE A 999  ? 3.3644 3.6470 3.3112 0.3273  -0.1519 -0.2654 999  ILE A CB  
7549  C CG1 . ILE A 999  ? 3.3962 3.6485 3.2982 0.3289  -0.1472 -0.2619 999  ILE A CG1 
7550  C CG2 . ILE A 999  ? 3.3247 3.6428 3.3177 0.3160  -0.1541 -0.2794 999  ILE A CG2 
7551  C CD1 . ILE A 999  ? 3.3785 3.6414 3.2818 0.3244  -0.1279 -0.2607 999  ILE A CD1 
7552  N N   . LEU A 1000 ? 1.7074 2.0475 1.7305 0.3211  -0.1378 -0.2656 1000 LEU A N   
7553  C CA  . LEU A 1000 ? 1.5933 1.9467 1.6436 0.3206  -0.1392 -0.2678 1000 LEU A CA  
7554  C C   . LEU A 1000 ? 1.5518 1.9132 1.6328 0.3242  -0.1603 -0.2824 1000 LEU A C   
7555  O O   . LEU A 1000 ? 1.5341 1.9111 1.6463 0.3239  -0.1611 -0.2886 1000 LEU A O   
7556  C CB  . LEU A 1000 ? 1.4748 1.8580 1.5497 0.3090  -0.1185 -0.2661 1000 LEU A CB  
7557  C CG  . LEU A 1000 ? 1.3631 1.7394 1.4115 0.3088  -0.1017 -0.2494 1000 LEU A CG  
7558  C CD1 . LEU A 1000 ? 1.3051 1.7120 1.3800 0.2958  -0.0849 -0.2480 1000 LEU A CD1 
7559  C CD2 . LEU A 1000 ? 1.3531 1.7015 1.3766 0.3163  -0.1098 -0.2427 1000 LEU A CD2 
7560  N N   . THR A 1001 ? 1.5332 1.8833 1.6040 0.3282  -0.1777 -0.2879 1001 THR A N   
7561  C CA  . THR A 1001 ? 1.5149 1.8763 1.6156 0.3333  -0.1996 -0.3007 1001 THR A CA  
7562  C C   . THR A 1001 ? 1.6007 1.9322 1.6699 0.3422  -0.2224 -0.2983 1001 THR A C   
7563  O O   . THR A 1001 ? 1.6593 1.9569 1.6810 0.3448  -0.2197 -0.2861 1001 THR A O   
7564  C CB  . THR A 1001 ? 1.3921 1.7916 1.5334 0.3216  -0.1982 -0.3168 1001 THR A CB  
7565  O OG1 . THR A 1001 ? 1.3094 1.7226 1.4537 0.3090  -0.1740 -0.3139 1001 THR A OG1 
7566  C CG2 . THR A 1001 ? 1.3647 1.7925 1.5556 0.3257  -0.2078 -0.3305 1001 THR A CG2 
7567  N N   . HIS A 1002 ? 1.6122 1.9575 1.7076 0.3467  -0.2450 -0.3098 1002 HIS A N   
7568  C CA  . HIS A 1002 ? 1.6927 2.0141 1.7590 0.3510  -0.2676 -0.3082 1002 HIS A CA  
7569  C C   . HIS A 1002 ? 1.3768 1.7066 1.4355 0.3370  -0.2662 -0.3148 1002 HIS A C   
7570  O O   . HIS A 1002 ? 1.4190 1.7294 1.4501 0.3361  -0.2831 -0.3145 1002 HIS A O   
7571  C CB  . HIS A 1002 ? 1.7963 2.1265 1.8896 0.3637  -0.2956 -0.3154 1002 HIS A CB  
7572  C CG  . HIS A 1002 ? 1.9032 2.2114 1.9904 0.3782  -0.2990 -0.3073 1002 HIS A CG  
7573  N ND1 . HIS A 1002 ? 1.9118 2.2426 2.0402 0.3836  -0.2928 -0.3139 1002 HIS A ND1 
7574  C CD2 . HIS A 1002 ? 1.9836 2.2454 2.0239 0.3868  -0.3078 -0.2936 1002 HIS A CD2 
7575  C CE1 . HIS A 1002 ? 1.9501 2.2474 2.0558 0.3954  -0.2979 -0.3043 1002 HIS A CE1 
7576  N NE2 . HIS A 1002 ? 1.9921 2.2478 2.0444 0.3969  -0.3073 -0.2918 1002 HIS A NE2 
7577  N N   . LEU A 1003 ? 1.2911 1.6449 1.3684 0.3247  -0.2457 -0.3201 1003 LEU A N   
7578  C CA  . LEU A 1003 ? 1.2323 1.5943 1.3046 0.3097  -0.2446 -0.3284 1003 LEU A CA  
7579  C C   . LEU A 1003 ? 1.3006 1.6195 1.3124 0.3073  -0.2422 -0.3190 1003 LEU A C   
7580  O O   . LEU A 1003 ? 1.3543 1.6508 1.3356 0.3099  -0.2226 -0.3075 1003 LEU A O   
7581  C CB  . LEU A 1003 ? 1.0897 1.4830 1.1922 0.2963  -0.2237 -0.3357 1003 LEU A CB  
7582  C CG  . LEU A 1003 ? 0.9659 1.4053 1.1295 0.2940  -0.2278 -0.3505 1003 LEU A CG  
7583  C CD1 . LEU A 1003 ? 0.8865 1.3585 1.0756 0.2735  -0.2214 -0.3658 1003 LEU A CD1 
7584  C CD2 . LEU A 1003 ? 0.9568 1.4028 1.1382 0.3064  -0.2550 -0.3560 1003 LEU A CD2 
7585  N N   . PRO A 1004 ? 1.3023 1.6116 1.2976 0.3017  -0.2620 -0.3246 1004 PRO A N   
7586  C CA  . PRO A 1004 ? 1.3124 1.5804 1.2506 0.2968  -0.2674 -0.3200 1004 PRO A CA  
7587  C C   . PRO A 1004 ? 1.3017 1.5477 1.2049 0.2890  -0.2439 -0.3163 1004 PRO A C   
7588  O O   . PRO A 1004 ? 1.2695 1.5390 1.1951 0.2781  -0.2320 -0.3238 1004 PRO A O   
7589  C CB  . PRO A 1004 ? 1.3470 1.6380 1.3041 0.2840  -0.2898 -0.3341 1004 PRO A CB  
7590  C CG  . PRO A 1004 ? 1.2752 1.6235 1.3008 0.2800  -0.2871 -0.3475 1004 PRO A CG  
7591  C CD  . PRO A 1004 ? 1.2543 1.6043 1.2981 0.2979  -0.2821 -0.3395 1004 PRO A CD  
7592  N N   . LYS A 1005 ? 1.3211 1.5200 1.1671 0.2945  -0.2380 -0.3053 1005 LYS A N   
7593  C CA  . LYS A 1005 ? 1.3804 1.5570 1.1946 0.2947  -0.2125 -0.2989 1005 LYS A CA  
7594  C C   . LYS A 1005 ? 1.3930 1.5531 1.1802 0.2800  -0.2083 -0.3060 1005 LYS A C   
7595  O O   . LYS A 1005 ? 1.3747 1.5095 1.1298 0.2836  -0.1881 -0.2996 1005 LYS A O   
7596  C CB  . LYS A 1005 ? 1.4913 1.6251 1.2552 0.3084  -0.2025 -0.2845 1005 LYS A CB  
7597  C CG  . LYS A 1005 ? 1.5794 1.7234 1.3598 0.3213  -0.1988 -0.2751 1005 LYS A CG  
7598  C CD  . LYS A 1005 ? 1.6325 1.7960 1.4302 0.3265  -0.1726 -0.2682 1005 LYS A CD  
7599  C CE  . LYS A 1005 ? 1.7104 1.8426 1.4613 0.3336  -0.1511 -0.2586 1005 LYS A CE  
7600  N NZ  . LYS A 1005 ? 1.6957 1.8548 1.4697 0.3388  -0.1282 -0.2513 1005 LYS A NZ  
7601  N N   . GLY A 1006 ? 1.4275 1.6010 1.2257 0.2637  -0.2264 -0.3187 1006 GLY A N   
7602  C CA  . GLY A 1006 ? 1.4872 1.6341 1.2460 0.2473  -0.2242 -0.3248 1006 GLY A CA  
7603  C C   . GLY A 1006 ? 1.4269 1.5688 1.1781 0.2412  -0.2019 -0.3257 1006 GLY A C   
7604  O O   . GLY A 1006 ? 1.4290 1.5250 1.1259 0.2403  -0.1901 -0.3219 1006 GLY A O   
7605  N N   . SER A 1007 ? 1.3791 1.5671 1.1843 0.2370  -0.1965 -0.3312 1007 SER A N   
7606  C CA  . SER A 1007 ? 1.3324 1.5222 1.1376 0.2286  -0.1785 -0.3330 1007 SER A CA  
7607  C C   . SER A 1007 ? 1.2771 1.4369 1.0516 0.2470  -0.1569 -0.3177 1007 SER A C   
7608  O O   . SER A 1007 ? 1.2385 1.3898 1.0064 0.2657  -0.1533 -0.3066 1007 SER A O   
7609  C CB  . SER A 1007 ? 1.3055 1.5525 1.1771 0.2215  -0.1766 -0.3407 1007 SER A CB  
7610  O OG  . SER A 1007 ? 1.3111 1.5606 1.1830 0.2111  -0.1606 -0.3423 1007 SER A OG  
7611  N N   . ALA A 1008 ? 1.2961 1.4404 1.0514 0.2411  -0.1428 -0.3175 1008 ALA A N   
7612  C CA  . ALA A 1008 ? 1.2982 1.4304 1.0413 0.2585  -0.1216 -0.3039 1008 ALA A CA  
7613  C C   . ALA A 1008 ? 1.2257 1.4094 1.0276 0.2624  -0.1162 -0.3007 1008 ALA A C   
7614  O O   . ALA A 1008 ? 1.2224 1.4112 1.0285 0.2792  -0.1028 -0.2879 1008 ALA A O   
7615  C CB  . ALA A 1008 ? 1.3345 1.4402 1.0469 0.2501  -0.1111 -0.3052 1008 ALA A CB  
7616  N N   . GLU A 1009 ? 1.1699 1.3930 1.0171 0.2455  -0.1263 -0.3131 1009 GLU A N   
7617  C CA  . GLU A 1009 ? 1.1129 1.3825 1.0144 0.2462  -0.1210 -0.3121 1009 GLU A CA  
7618  C C   . GLU A 1009 ? 1.0820 1.3587 0.9948 0.2648  -0.1224 -0.3024 1009 GLU A C   
7619  O O   . GLU A 1009 ? 1.0646 1.3640 1.0022 0.2713  -0.1115 -0.2946 1009 GLU A O   
7620  C CB  . GLU A 1009 ? 1.0693 1.3788 1.0166 0.2254  -0.1318 -0.3295 1009 GLU A CB  
7621  C CG  . GLU A 1009 ? 0.9725 1.3247 0.9693 0.2192  -0.1219 -0.3314 1009 GLU A CG  
7622  C CD  . GLU A 1009 ? 0.9154 1.3098 0.9633 0.2076  -0.1337 -0.3477 1009 GLU A CD  
7623  O OE1 . GLU A 1009 ? 0.9051 1.3061 0.9558 0.1918  -0.1453 -0.3623 1009 GLU A OE1 
7624  O OE2 . GLU A 1009 ? 0.8856 1.3070 0.9702 0.2147  -0.1310 -0.3460 1009 GLU A OE2 
7625  N N   . ALA A 1010 ? 1.0729 1.3284 0.9641 0.2715  -0.1358 -0.3025 1010 ALA A N   
7626  C CA  . ALA A 1010 ? 1.1038 1.3639 1.0038 0.2864  -0.1385 -0.2941 1010 ALA A CA  
7627  C C   . ALA A 1010 ? 1.0900 1.3249 0.9548 0.3027  -0.1213 -0.2779 1010 ALA A C   
7628  O O   . ALA A 1010 ? 1.0339 1.2767 0.9057 0.3134  -0.1156 -0.2684 1010 ALA A O   
7629  C CB  . ALA A 1010 ? 1.1783 1.4261 1.0690 0.2869  -0.1607 -0.2995 1010 ALA A CB  
7630  N N   . GLU A 1011 ? 1.1518 1.3556 0.9767 0.3042  -0.1123 -0.2755 1011 GLU A N   
7631  C CA  . GLU A 1011 ? 1.2043 1.3851 0.9956 0.3212  -0.0951 -0.2617 1011 GLU A CA  
7632  C C   . GLU A 1011 ? 1.1617 1.3754 0.9831 0.3242  -0.0783 -0.2541 1011 GLU A C   
7633  O O   . GLU A 1011 ? 1.1671 1.3882 0.9874 0.3371  -0.0658 -0.2420 1011 GLU A O   
7634  C CB  . GLU A 1011 ? 1.2804 1.4139 1.0175 0.3238  -0.0900 -0.2621 1011 GLU A CB  
7635  C CG  . GLU A 1011 ? 1.3325 1.4274 1.0231 0.3377  -0.0869 -0.2552 1011 GLU A CG  
7636  C CD  . GLU A 1011 ? 1.3651 1.4651 1.0645 0.3352  -0.1039 -0.2570 1011 GLU A CD  
7637  O OE1 . GLU A 1011 ? 1.3932 1.4887 1.0939 0.3221  -0.1241 -0.2675 1011 GLU A OE1 
7638  O OE2 . GLU A 1011 ? 1.3673 1.4770 1.0727 0.3456  -0.0977 -0.2479 1011 GLU A OE2 
7639  N N   . LEU A 1012 ? 1.0947 1.3288 0.9417 0.3102  -0.0785 -0.2613 1012 LEU A N   
7640  C CA  . LEU A 1012 ? 1.0044 1.2697 0.8798 0.3088  -0.0649 -0.2548 1012 LEU A CA  
7641  C C   . LEU A 1012 ? 1.0104 1.3149 0.9284 0.3070  -0.0650 -0.2522 1012 LEU A C   
7642  O O   . LEU A 1012 ? 1.0186 1.3397 0.9437 0.3150  -0.0519 -0.2399 1012 LEU A O   
7643  C CB  . LEU A 1012 ? 0.9092 1.1809 0.7956 0.2907  -0.0667 -0.2646 1012 LEU A CB  
7644  C CG  . LEU A 1012 ? 0.8994 1.1375 0.7449 0.2972  -0.0566 -0.2589 1012 LEU A CG  
7645  C CD1 . LEU A 1012 ? 0.8792 1.1150 0.7258 0.2771  -0.0591 -0.2686 1012 LEU A CD1 
7646  C CD2 . LEU A 1012 ? 0.8787 1.1307 0.7283 0.3139  -0.0400 -0.2424 1012 LEU A CD2 
7647  N N   . MET A 1013 ? 0.9905 1.3089 0.9349 0.2967  -0.0799 -0.2639 1013 MET A N   
7648  C CA  . MET A 1013 ? 0.9670 1.3163 0.9491 0.2945  -0.0815 -0.2637 1013 MET A CA  
7649  C C   . MET A 1013 ? 1.0195 1.3613 0.9868 0.3087  -0.0771 -0.2509 1013 MET A C   
7650  O O   . MET A 1013 ? 1.0268 1.3882 1.0175 0.3072  -0.0767 -0.2487 1013 MET A O   
7651  C CB  . MET A 1013 ? 0.9478 1.3063 0.9544 0.2863  -0.1002 -0.2790 1013 MET A CB  
7652  C CG  . MET A 1013 ? 0.9231 1.3148 0.9741 0.2812  -0.1009 -0.2830 1013 MET A CG  
7653  S SD  . MET A 1013 ? 1.1538 1.5786 1.2397 0.2611  -0.0906 -0.2916 1013 MET A SD  
7654  C CE  . MET A 1013 ? 0.8994 1.3039 0.9608 0.2523  -0.0976 -0.3015 1013 MET A CE  
7655  N N   . SER A 1014 ? 1.0801 1.3908 1.0054 0.3213  -0.0732 -0.2432 1014 SER A N   
7656  C CA  . SER A 1014 ? 1.0927 1.3931 0.9972 0.3331  -0.0676 -0.2317 1014 SER A CA  
7657  C C   . SER A 1014 ? 1.0057 1.3286 0.9156 0.3375  -0.0470 -0.2184 1014 SER A C   
7658  O O   . SER A 1014 ? 0.9640 1.3001 0.8787 0.3388  -0.0413 -0.2102 1014 SER A O   
7659  C CB  . SER A 1014 ? 1.2138 1.4716 1.0688 0.3437  -0.0691 -0.2298 1014 SER A CB  
7660  O OG  . SER A 1014 ? 1.2579 1.5070 1.0909 0.3525  -0.0519 -0.2227 1014 SER A OG  
7661  N N   . VAL A 1015 ? 0.9698 1.2951 0.8754 0.3398  -0.0366 -0.2157 1015 VAL A N   
7662  C CA  . VAL A 1015 ? 0.9688 1.3199 0.8829 0.3445  -0.0188 -0.2030 1015 VAL A CA  
7663  C C   . VAL A 1015 ? 0.9454 1.3370 0.9025 0.3293  -0.0180 -0.2027 1015 VAL A C   
7664  O O   . VAL A 1015 ? 0.9736 1.3913 0.9404 0.3296  -0.0062 -0.1912 1015 VAL A O   
7665  C CB  . VAL A 1015 ? 1.0605 1.4014 0.9599 0.3513  -0.0107 -0.2007 1015 VAL A CB  
7666  C CG1 . VAL A 1015 ? 1.0414 1.3831 0.9569 0.3358  -0.0200 -0.2123 1015 VAL A CG1 
7667  C CG2 . VAL A 1015 ? 1.0550 1.4254 0.9638 0.3595  0.0066  -0.1859 1015 VAL A CG2 
7668  N N   . VAL A 1016 ? 0.8547 1.2516 0.8361 0.3152  -0.0301 -0.2157 1016 VAL A N   
7669  C CA  . VAL A 1016 ? 0.7287 1.1601 0.7493 0.2991  -0.0280 -0.2179 1016 VAL A CA  
7670  C C   . VAL A 1016 ? 0.6462 1.0989 0.6782 0.2963  -0.0208 -0.2086 1016 VAL A C   
7671  O O   . VAL A 1016 ? 0.5860 1.0649 0.6283 0.2916  -0.0083 -0.1983 1016 VAL A O   
7672  C CB  . VAL A 1016 ? 0.6887 1.1217 0.7332 0.2862  -0.0421 -0.2356 1016 VAL A CB  
7673  C CG1 . VAL A 1016 ? 0.6521 1.1125 0.7313 0.2737  -0.0409 -0.2387 1016 VAL A CG1 
7674  C CG2 . VAL A 1016 ? 0.6859 1.1172 0.7323 0.2773  -0.0428 -0.2436 1016 VAL A CG2 
7675  N N   . PRO A 1017 ? 0.6844 1.1245 0.7124 0.2981  -0.0296 -0.2117 1017 PRO A N   
7676  C CA  . PRO A 1017 ? 0.7016 1.1551 0.7355 0.2925  -0.0241 -0.2044 1017 PRO A CA  
7677  C C   . PRO A 1017 ? 0.7309 1.1958 0.7467 0.2971  -0.0084 -0.1876 1017 PRO A C   
7678  O O   . PRO A 1017 ? 0.7048 1.1901 0.7279 0.2874  0.0000  -0.1797 1017 PRO A O   
7679  C CB  . PRO A 1017 ? 0.7089 1.1339 0.7300 0.2983  -0.0393 -0.2107 1017 PRO A CB  
7680  C CG  . PRO A 1017 ? 0.7026 1.1173 0.7342 0.2992  -0.0537 -0.2253 1017 PRO A CG  
7681  C CD  . PRO A 1017 ? 0.7057 1.1183 0.7248 0.3031  -0.0472 -0.2233 1017 PRO A CD  
7682  N N   . VAL A 1018 ? 0.8086 1.2608 0.7995 0.3114  -0.0037 -0.1822 1018 VAL A N   
7683  C CA  . VAL A 1018 ? 0.9063 1.3789 0.8874 0.3164  0.0132  -0.1671 1018 VAL A CA  
7684  C C   . VAL A 1018 ? 0.9153 1.4229 0.9225 0.3097  0.0219  -0.1620 1018 VAL A C   
7685  O O   . VAL A 1018 ? 0.8979 1.4389 0.9194 0.2996  0.0315  -0.1523 1018 VAL A O   
7686  C CB  . VAL A 1018 ? 0.9954 1.4448 0.9416 0.3357  0.0184  -0.1630 1018 VAL A CB  
7687  C CG1 . VAL A 1018 ? 1.0233 1.5010 0.9632 0.3416  0.0374  -0.1478 1018 VAL A CG1 
7688  C CG2 . VAL A 1018 ? 1.0445 1.4541 0.9625 0.3395  0.0065  -0.1694 1018 VAL A CG2 
7689  N N   . PHE A 1019 ? 0.9288 1.4274 0.9399 0.3128  0.0176  -0.1685 1019 PHE A N   
7690  C CA  . PHE A 1019 ? 0.8959 1.4222 0.9258 0.3073  0.0247  -0.1627 1019 PHE A CA  
7691  C C   . PHE A 1019 ? 0.8256 1.3838 0.8853 0.2855  0.0264  -0.1615 1019 PHE A C   
7692  O O   . PHE A 1019 ? 0.8155 1.4069 0.8855 0.2806  0.0367  -0.1488 1019 PHE A O   
7693  C CB  . PHE A 1019 ? 0.9114 1.4192 0.9408 0.3068  0.0174  -0.1724 1019 PHE A CB  
7694  C CG  . PHE A 1019 ? 0.8635 1.3978 0.9142 0.2944  0.0215  -0.1683 1019 PHE A CG  
7695  C CD1 . PHE A 1019 ? 0.8332 1.3947 0.8860 0.3011  0.0329  -0.1519 1019 PHE A CD1 
7696  C CD2 . PHE A 1019 ? 0.8266 1.3614 0.8960 0.2753  0.0142  -0.1806 1019 PHE A CD2 
7697  C CE1 . PHE A 1019 ? 0.8016 1.3866 0.8718 0.2891  0.0350  -0.1467 1019 PHE A CE1 
7698  C CE2 . PHE A 1019 ? 0.7995 1.3559 0.8845 0.2617  0.0180  -0.1765 1019 PHE A CE2 
7699  C CZ  . PHE A 1019 ? 0.7971 1.3772 0.8814 0.2684  0.0275  -0.1589 1019 PHE A CZ  
7700  N N   . TYR A 1020 ? 0.7558 1.3047 0.8293 0.2724  0.0166  -0.1748 1020 TYR A N   
7701  C CA  . TYR A 1020 ? 0.7085 1.2823 0.8066 0.2515  0.0196  -0.1751 1020 TYR A CA  
7702  C C   . TYR A 1020 ? 0.6850 1.2755 0.7771 0.2474  0.0284  -0.1626 1020 TYR A C   
7703  O O   . TYR A 1020 ? 0.6741 1.2964 0.7787 0.2333  0.0375  -0.1529 1020 TYR A O   
7704  C CB  . TYR A 1020 ? 0.7208 1.2816 0.8357 0.2410  0.0088  -0.1930 1020 TYR A CB  
7705  C CG  . TYR A 1020 ? 0.7571 1.3151 0.8827 0.2361  0.0040  -0.2037 1020 TYR A CG  
7706  C CD1 . TYR A 1020 ? 0.7772 1.3551 0.9116 0.2255  0.0112  -0.1980 1020 TYR A CD1 
7707  C CD2 . TYR A 1020 ? 0.8046 1.3394 0.9284 0.2410  -0.0081 -0.2187 1020 TYR A CD2 
7708  C CE1 . TYR A 1020 ? 0.8145 1.3856 0.9528 0.2189  0.0071  -0.2074 1020 TYR A CE1 
7709  C CE2 . TYR A 1020 ? 0.8344 1.3660 0.9641 0.2337  -0.0118 -0.2288 1020 TYR A CE2 
7710  C CZ  . TYR A 1020 ? 0.8562 1.4039 0.9914 0.2224  -0.0038 -0.2233 1020 TYR A CZ  
7711  O OH  . TYR A 1020 ? 0.8988 1.4391 1.0345 0.2128  -0.0074 -0.2334 1020 TYR A OH  
7712  N N   . VAL A 1021 ? 0.6766 1.2458 0.7467 0.2579  0.0258  -0.1619 1021 VAL A N   
7713  C CA  . VAL A 1021 ? 0.6767 1.2594 0.7353 0.2523  0.0350  -0.1500 1021 VAL A CA  
7714  C C   . VAL A 1021 ? 0.6546 1.2735 0.7137 0.2549  0.0490  -0.1339 1021 VAL A C   
7715  O O   . VAL A 1021 ? 0.6259 1.2768 0.6944 0.2393  0.0576  -0.1242 1021 VAL A O   
7716  C CB  . VAL A 1021 ? 0.5847 1.1343 0.6134 0.2624  0.0297  -0.1516 1021 VAL A CB  
7717  C CG1 . VAL A 1021 ? 0.5770 1.1431 0.5866 0.2603  0.0427  -0.1370 1021 VAL A CG1 
7718  C CG2 . VAL A 1021 ? 0.5944 1.1204 0.6261 0.2536  0.0182  -0.1625 1021 VAL A CG2 
7719  N N   . PHE A 1022 ? 0.7043 1.3187 0.7536 0.2747  0.0512  -0.1310 1022 PHE A N   
7720  C CA  . PHE A 1022 ? 0.7548 1.4052 0.8068 0.2816  0.0642  -0.1159 1022 PHE A CA  
7721  C C   . PHE A 1022 ? 0.7591 1.4438 0.8382 0.2684  0.0663  -0.1103 1022 PHE A C   
7722  O O   . PHE A 1022 ? 0.7726 1.4985 0.8610 0.2652  0.0761  -0.0961 1022 PHE A O   
7723  C CB  . PHE A 1022 ? 0.7881 1.4215 0.8222 0.3081  0.0665  -0.1151 1022 PHE A CB  
7724  C CG  . PHE A 1022 ? 0.7751 1.4457 0.8110 0.3200  0.0809  -0.0998 1022 PHE A CG  
7725  C CD1 . PHE A 1022 ? 0.7844 1.4641 0.8035 0.3273  0.0916  -0.0931 1022 PHE A CD1 
7726  C CD2 . PHE A 1022 ? 0.7563 1.4547 0.8112 0.3232  0.0835  -0.0920 1022 PHE A CD2 
7727  C CE1 . PHE A 1022 ? 0.7917 1.5123 0.8166 0.3392  0.1057  -0.0798 1022 PHE A CE1 
7728  C CE2 . PHE A 1022 ? 0.7681 1.5055 0.8284 0.3365  0.0958  -0.0775 1022 PHE A CE2 
7729  C CZ  . PHE A 1022 ? 0.7816 1.5329 0.8291 0.3450  0.1074  -0.0717 1022 PHE A CZ  
7730  N N   . HIS A 1023 ? 0.7590 1.4281 0.8504 0.2598  0.0570  -0.1216 1023 HIS A N   
7731  C CA  . HIS A 1023 ? 0.7303 1.4261 0.8439 0.2441  0.0579  -0.1178 1023 HIS A CA  
7732  C C   . HIS A 1023 ? 0.6706 1.3921 0.7979 0.2172  0.0620  -0.1140 1023 HIS A C   
7733  O O   . HIS A 1023 ? 0.6677 1.4278 0.8062 0.2062  0.0686  -0.1007 1023 HIS A O   
7734  C CB  . HIS A 1023 ? 0.7413 1.4113 0.8610 0.2399  0.0479  -0.1326 1023 HIS A CB  
7735  C CG  . HIS A 1023 ? 0.7401 1.4319 0.8777 0.2222  0.0485  -0.1296 1023 HIS A CG  
7736  N ND1 . HIS A 1023 ? 0.7495 1.4369 0.9020 0.1993  0.0443  -0.1419 1023 HIS A ND1 
7737  C CD2 . HIS A 1023 ? 0.7388 1.4570 0.8809 0.2237  0.0528  -0.1153 1023 HIS A CD2 
7738  C CE1 . HIS A 1023 ? 0.7541 1.4617 0.9167 0.1853  0.0462  -0.1355 1023 HIS A CE1 
7739  N NE2 . HIS A 1023 ? 0.7555 1.4819 0.9121 0.2001  0.0502  -0.1188 1023 HIS A NE2 
7740  N N   . TYR A 1024 ? 0.6167 1.3158 0.7415 0.2068  0.0575  -0.1254 1024 TYR A N   
7741  C CA  . TYR A 1024 ? 0.6013 1.3160 0.7302 0.1830  0.0625  -0.1219 1024 TYR A CA  
7742  C C   . TYR A 1024 ? 0.6228 1.3636 0.7390 0.1813  0.0727  -0.1058 1024 TYR A C   
7743  O O   . TYR A 1024 ? 0.6118 1.3802 0.7322 0.1593  0.0795  -0.0971 1024 TYR A O   
7744  C CB  . TYR A 1024 ? 0.6360 1.3157 0.7604 0.1781  0.0554  -0.1372 1024 TYR A CB  
7745  C CG  . TYR A 1024 ? 0.6916 1.3752 0.8070 0.1587  0.0612  -0.1327 1024 TYR A CG  
7746  C CD1 . TYR A 1024 ? 0.7313 1.4151 0.8580 0.1354  0.0626  -0.1391 1024 TYR A CD1 
7747  C CD2 . TYR A 1024 ? 0.7327 1.4171 0.8249 0.1619  0.0663  -0.1226 1024 TYR A CD2 
7748  C CE1 . TYR A 1024 ? 0.7815 1.4629 0.8945 0.1166  0.0684  -0.1352 1024 TYR A CE1 
7749  C CE2 . TYR A 1024 ? 0.7822 1.4659 0.8605 0.1419  0.0716  -0.1185 1024 TYR A CE2 
7750  C CZ  . TYR A 1024 ? 0.8362 1.5165 0.9239 0.1194  0.0724  -0.1246 1024 TYR A CZ  
7751  O OH  . TYR A 1024 ? 0.9174 1.5909 0.9857 0.0980  0.0782  -0.1207 1024 TYR A OH  
7752  N N   . LEU A 1025 ? 0.6766 1.4083 0.7750 0.2025  0.0744  -0.1025 1025 LEU A N   
7753  C CA  . LEU A 1025 ? 0.7119 1.4688 0.7970 0.1992  0.0851  -0.0891 1025 LEU A CA  
7754  C C   . LEU A 1025 ? 0.6938 1.5039 0.7949 0.1985  0.0941  -0.0731 1025 LEU A C   
7755  O O   . LEU A 1025 ? 0.6676 1.5141 0.7699 0.1812  0.1026  -0.0615 1025 LEU A O   
7756  C CB  . LEU A 1025 ? 0.7435 1.4764 0.8035 0.2216  0.0859  -0.0904 1025 LEU A CB  
7757  C CG  . LEU A 1025 ? 0.7733 1.4678 0.8068 0.2166  0.0817  -0.0974 1025 LEU A CG  
7758  C CD1 . LEU A 1025 ? 0.7998 1.4800 0.8074 0.2366  0.0854  -0.0952 1025 LEU A CD1 
7759  C CD2 . LEU A 1025 ? 0.7758 1.4856 0.8021 0.1892  0.0881  -0.0907 1025 LEU A CD2 
7760  N N   . GLU A 1026 ? 0.7326 1.5456 0.8443 0.2178  0.0916  -0.0725 1026 GLU A N   
7761  C CA  . GLU A 1026 ? 0.7947 1.6545 0.9208 0.2260  0.0983  -0.0572 1026 GLU A CA  
7762  C C   . GLU A 1026 ? 0.8251 1.7103 0.9732 0.2055  0.0950  -0.0523 1026 GLU A C   
7763  O O   . GLU A 1026 ? 0.8565 1.7910 1.0175 0.1928  0.1006  -0.0375 1026 GLU A O   
7764  C CB  . GLU A 1026 ? 0.8372 1.6788 0.9577 0.2590  0.0967  -0.0591 1026 GLU A CB  
7765  C CG  . GLU A 1026 ? 0.8738 1.7559 1.0106 0.2717  0.1005  -0.0447 1026 GLU A CG  
7766  C CD  . GLU A 1026 ? 0.9109 1.8397 1.0502 0.2829  0.1136  -0.0304 1026 GLU A CD  
7767  O OE1 . GLU A 1026 ? 0.9309 1.8557 1.0549 0.2791  0.1203  -0.0327 1026 GLU A OE1 
7768  O OE2 . GLU A 1026 ? 0.9052 1.8742 1.0610 0.2956  0.1168  -0.0173 1026 GLU A OE2 
7769  N N   . THR A 1027 ? 0.8108 1.6639 0.9628 0.2004  0.0856  -0.0648 1027 THR A N   
7770  C CA  . THR A 1027 ? 0.7916 1.6655 0.9610 0.1819  0.0826  -0.0604 1027 THR A CA  
7771  C C   . THR A 1027 ? 0.7995 1.6890 0.9744 0.1469  0.0854  -0.0594 1027 THR A C   
7772  O O   . THR A 1027 ? 0.8183 1.7260 1.0051 0.1269  0.0838  -0.0551 1027 THR A O   
7773  C CB  . THR A 1027 ? 0.7715 1.6105 0.9422 0.1867  0.0733  -0.0731 1027 THR A CB  
7774  O OG1 . THR A 1027 ? 0.7874 1.6347 0.9582 0.2088  0.0719  -0.0640 1027 THR A OG1 
7775  C CG2 . THR A 1027 ? 0.7507 1.5944 0.9337 0.1556  0.0704  -0.0771 1027 THR A CG2 
7776  N N   . GLY A 1028 ? 0.8209 1.7008 0.9831 0.1383  0.0896  -0.0626 1028 GLY A N   
7777  C CA  . GLY A 1028 ? 0.8552 1.7483 1.0167 0.1046  0.0939  -0.0600 1028 GLY A CA  
7778  C C   . GLY A 1028 ? 0.8880 1.8082 1.0369 0.0994  0.1030  -0.0476 1028 GLY A C   
7779  O O   . GLY A 1028 ? 0.8811 1.7914 1.0153 0.0776  0.1067  -0.0496 1028 GLY A O   
7780  N N   . ASN A 1029 ? 0.9573 1.9114 1.1107 0.1193  0.1073  -0.0352 1029 ASN A N   
7781  C CA  . ASN A 1029 ? 1.0464 2.0172 1.1847 0.1227  0.1163  -0.0279 1029 ASN A CA  
7782  C C   . ASN A 1029 ? 1.0388 1.9786 1.1520 0.1007  0.1183  -0.0350 1029 ASN A C   
7783  O O   . ASN A 1029 ? 1.0152 1.9650 1.1245 0.0690  0.1211  -0.0317 1029 ASN A O   
7784  C CB  . ASN A 1029 ? 1.1450 2.1850 1.2975 0.1184  0.1247  -0.0080 1029 ASN A CB  
7785  C CG  . ASN A 1029 ? 1.2605 2.3318 1.4112 0.0786  0.1292  0.0009  1029 ASN A CG  
7786  O OD1 . ASN A 1029 ? 1.3122 2.4237 1.4574 0.0676  0.1385  0.0122  1029 ASN A OD1 
7787  N ND2 . ASN A 1029 ? 1.2865 2.3398 1.4400 0.0549  0.1236  -0.0045 1029 ASN A ND2 
7788  N N   . HIS A 1030 ? 1.0768 1.9737 1.1698 0.1184  0.1161  -0.0452 1030 HIS A N   
7789  C CA  . HIS A 1030 ? 1.0869 1.9447 1.1509 0.1044  0.1159  -0.0524 1030 HIS A CA  
7790  C C   . HIS A 1030 ? 1.0828 1.9313 1.1219 0.1203  0.1207  -0.0504 1030 HIS A C   
7791  O O   . HIS A 1030 ? 1.0903 1.9012 1.0993 0.1130  0.1196  -0.0556 1030 HIS A O   
7792  C CB  . HIS A 1030 ? 1.0605 1.8628 1.1236 0.1081  0.1042  -0.0704 1030 HIS A CB  
7793  C CG  . HIS A 1030 ? 1.0179 1.8255 1.0992 0.0867  0.1022  -0.0740 1030 HIS A CG  
7794  N ND1 . HIS A 1030 ? 1.0072 1.8274 1.0807 0.0539  0.1085  -0.0685 1030 HIS A ND1 
7795  C CD2 . HIS A 1030 ? 0.9896 1.7901 1.0933 0.0912  0.0954  -0.0830 1030 HIS A CD2 
7796  C CE1 . HIS A 1030 ? 0.9857 1.8058 1.0767 0.0399  0.1060  -0.0741 1030 HIS A CE1 
7797  N NE2 . HIS A 1030 ? 0.9683 1.7774 1.0784 0.0619  0.0982  -0.0832 1030 HIS A NE2 
7798  N N   . TRP A 1031 ? 1.0454 1.9272 1.0957 0.1418  0.1264  -0.0427 1031 TRP A N   
7799  C CA  . TRP A 1031 ? 1.0174 1.8957 1.0462 0.1577  0.1334  -0.0409 1031 TRP A CA  
7800  C C   . TRP A 1031 ? 1.0457 1.9312 1.0467 0.1323  0.1422  -0.0350 1031 TRP A C   
7801  O O   . TRP A 1031 ? 1.1089 1.9784 1.0827 0.1393  0.1473  -0.0360 1031 TRP A O   
7802  C CB  . TRP A 1031 ? 0.9715 1.8999 1.0210 0.1791  0.1420  -0.0306 1031 TRP A CB  
7803  C CG  . TRP A 1031 ? 0.9250 1.8347 0.9892 0.2081  0.1344  -0.0368 1031 TRP A CG  
7804  C CD1 . TRP A 1031 ? 0.9019 1.8404 0.9949 0.2162  0.1321  -0.0313 1031 TRP A CD1 
7805  C CD2 . TRP A 1031 ? 0.9342 1.7892 0.9808 0.2313  0.1276  -0.0494 1031 TRP A CD2 
7806  N NE1 . TRP A 1031 ? 0.9031 1.8056 0.9954 0.2429  0.1249  -0.0402 1031 TRP A NE1 
7807  C CE2 . TRP A 1031 ? 0.9343 1.7868 0.9989 0.2520  0.1223  -0.0515 1031 TRP A CE2 
7808  C CE3 . TRP A 1031 ? 0.9688 1.7751 0.9834 0.2354  0.1246  -0.0587 1031 TRP A CE3 
7809  C CZ2 . TRP A 1031 ? 0.9763 1.7805 1.0277 0.2747  0.1149  -0.0629 1031 TRP A CZ2 
7810  C CZ3 . TRP A 1031 ? 1.0044 1.7655 1.0083 0.2588  0.1164  -0.0695 1031 TRP A CZ3 
7811  C CH2 . TRP A 1031 ? 1.0068 1.7673 1.0288 0.2774  0.1120  -0.0718 1031 TRP A CH2 
7812  N N   . ASN A 1032 ? 1.0244 1.9317 1.0281 0.1005  0.1446  -0.0290 1032 ASN A N   
7813  C CA  . ASN A 1032 ? 1.0648 1.9754 1.0370 0.0722  0.1531  -0.0235 1032 ASN A CA  
7814  C C   . ASN A 1032 ? 1.0690 1.9067 1.0047 0.0637  0.1446  -0.0353 1032 ASN A C   
7815  O O   . ASN A 1032 ? 1.0866 1.9126 0.9898 0.0360  0.1493  -0.0323 1032 ASN A O   
7816  C CB  . ASN A 1032 ? 1.0813 2.0388 1.0653 0.0387  0.1585  -0.0125 1032 ASN A CB  
7817  C CG  . ASN A 1032 ? 1.0713 1.9996 1.0638 0.0261  0.1489  -0.0198 1032 ASN A CG  
7818  O OD1 . ASN A 1032 ? 1.0264 1.9521 1.0474 0.0441  0.1411  -0.0249 1032 ASN A OD1 
7819  N ND2 . ASN A 1032 ? 1.1051 2.0064 1.0696 -0.0051 0.1498  -0.0215 1032 ASN A ND2 
7820  N N   . ILE A 1033 ? 1.0411 1.8296 0.9810 0.0864  0.1315  -0.0486 1033 ILE A N   
7821  C CA  . ILE A 1033 ? 1.0616 1.7818 0.9691 0.0840  0.1216  -0.0598 1033 ILE A CA  
7822  C C   . ILE A 1033 ? 1.1207 1.8236 0.9882 0.0845  0.1267  -0.0568 1033 ILE A C   
7823  O O   . ILE A 1033 ? 1.1628 1.8223 0.9910 0.0685  0.1240  -0.0592 1033 ILE A O   
7824  C CB  . ILE A 1033 ? 1.0275 1.7037 0.9450 0.1125  0.1067  -0.0740 1033 ILE A CB  
7825  C CG1 . ILE A 1033 ? 0.9893 1.6731 0.9439 0.1135  0.1003  -0.0805 1033 ILE A CG1 
7826  C CG2 . ILE A 1033 ? 1.0611 1.6711 0.9430 0.1113  0.0960  -0.0834 1033 ILE A CG2 
7827  C CD1 . ILE A 1033 ? 0.9873 1.6249 0.9477 0.1357  0.0850  -0.0961 1033 ILE A CD1 
7828  N N   . PHE A 1034 ? 1.1314 1.8663 1.0074 0.1034  0.1344  -0.0520 1034 PHE A N   
7829  C CA  . PHE A 1034 ? 1.1780 1.8907 1.0186 0.1123  0.1383  -0.0524 1034 PHE A CA  
7830  C C   . PHE A 1034 ? 1.2857 2.0235 1.0974 0.0851  0.1530  -0.0424 1034 PHE A C   
7831  O O   . PHE A 1034 ? 1.2728 2.0773 1.1050 0.0735  0.1666  -0.0316 1034 PHE A O   
7832  C CB  . PHE A 1034 ? 1.0903 1.8229 0.9491 0.1443  0.1423  -0.0528 1034 PHE A CB  
7833  C CG  . PHE A 1034 ? 1.0108 1.7146 0.8915 0.1697  0.1279  -0.0631 1034 PHE A CG  
7834  C CD1 . PHE A 1034 ? 1.0079 1.6470 0.8667 0.1795  0.1126  -0.0747 1034 PHE A CD1 
7835  C CD2 . PHE A 1034 ? 0.9440 1.6855 0.8659 0.1825  0.1287  -0.0609 1034 PHE A CD2 
7836  C CE1 . PHE A 1034 ? 0.9676 1.5850 0.8475 0.1999  0.0995  -0.0846 1034 PHE A CE1 
7837  C CE2 . PHE A 1034 ? 0.8960 1.6097 0.8344 0.2025  0.1159  -0.0710 1034 PHE A CE2 
7838  C CZ  . PHE A 1034 ? 0.9083 1.5627 0.8269 0.2102  0.1019  -0.0830 1034 PHE A CZ  
7839  N N   . HIS A 1035 ? 1.4230 2.1066 1.1854 0.0740  0.1494  -0.0461 1035 HIS A N   
7840  C CA  . HIS A 1035 ? 1.5845 2.2832 1.3107 0.0454  0.1630  -0.0380 1035 HIS A CA  
7841  C C   . HIS A 1035 ? 1.6288 2.3678 1.3600 0.0613  0.1771  -0.0342 1035 HIS A C   
7842  O O   . HIS A 1035 ? 1.6602 2.4556 1.3910 0.0434  0.1943  -0.0248 1035 HIS A O   
7843  C CB  . HIS A 1035 ? 1.7476 2.3679 1.4157 0.0326  0.1533  -0.0436 1035 HIS A CB  
7844  C CG  . HIS A 1035 ? 1.8481 2.4206 1.5166 0.0288  0.1373  -0.0505 1035 HIS A CG  
7845  N ND1 . HIS A 1035 ? 1.9170 2.4672 1.5553 -0.0035 0.1380  -0.0480 1035 HIS A ND1 
7846  C CD2 . HIS A 1035 ? 1.8593 2.4053 1.5561 0.0527  0.1217  -0.0603 1035 HIS A CD2 
7847  C CE1 . HIS A 1035 ? 1.9249 2.4352 1.5735 0.0031  0.1238  -0.0564 1035 HIS A CE1 
7848  N NE2 . HIS A 1035 ? 1.8929 2.4029 1.5787 0.0366  0.1138  -0.0642 1035 HIS A NE2 
7849  N N   . SER A 1036 ? 1.6158 2.3281 1.3536 0.0952  0.1701  -0.0419 1036 SER A N   
7850  C CA  . SER A 1036 ? 1.6169 2.3558 1.3567 0.1160  0.1832  -0.0408 1036 SER A CA  
7851  C C   . SER A 1036 ? 1.5543 2.3728 1.3472 0.1299  0.1952  -0.0333 1036 SER A C   
7852  O O   . SER A 1036 ? 1.5154 2.3782 1.3395 0.1159  0.1959  -0.0264 1036 SER A O   
7853  C CB  . SER A 1036 ? 1.6461 2.3261 1.3737 0.1467  0.1707  -0.0517 1036 SER A CB  
7854  O OG  . SER A 1036 ? 1.6158 2.3014 1.3860 0.1706  0.1608  -0.0557 1036 SER A OG  
7855  N N   . ASP A 1037 ? 1.5255 2.3604 1.3263 0.1576  0.2046  -0.0345 1037 ASP A N   
7856  C CA  . ASP A 1037 ? 1.4479 2.3505 1.2977 0.1771  0.2139  -0.0279 1037 ASP A CA  
7857  C C   . ASP A 1037 ? 1.3211 2.1995 1.1990 0.2007  0.1979  -0.0334 1037 ASP A C   
7858  O O   . ASP A 1037 ? 1.3288 2.1527 1.1917 0.2220  0.1888  -0.0432 1037 ASP A O   
7859  C CB  . ASP A 1037 ? 1.4876 2.4151 1.3338 0.1998  0.2316  -0.0278 1037 ASP A CB  
7860  C CG  . ASP A 1037 ? 1.4326 2.4252 1.3289 0.2254  0.2399  -0.0210 1037 ASP A CG  
7861  O OD1 . ASP A 1037 ? 1.3530 2.3548 1.2826 0.2303  0.2280  -0.0185 1037 ASP A OD1 
7862  O OD2 . ASP A 1037 ? 1.4490 2.4821 1.3497 0.2406  0.2585  -0.0185 1037 ASP A OD2 
7863  N N   . PRO A 1038 ? 1.2231 2.1426 1.1402 0.1946  0.1944  -0.0269 1038 PRO A N   
7864  C CA  . PRO A 1038 ? 1.1566 2.0556 1.0999 0.2089  0.1790  -0.0318 1038 PRO A CA  
7865  C C   . PRO A 1038 ? 1.1178 2.0299 1.0826 0.2451  0.1820  -0.0322 1038 PRO A C   
7866  O O   . PRO A 1038 ? 1.1145 1.9851 1.0826 0.2632  0.1696  -0.0407 1038 PRO A O   
7867  C CB  . PRO A 1038 ? 1.1306 2.0791 1.1041 0.1853  0.1785  -0.0223 1038 PRO A CB  
7868  C CG  . PRO A 1038 ? 1.1759 2.1550 1.1304 0.1535  0.1903  -0.0143 1038 PRO A CG  
7869  C CD  . PRO A 1038 ? 1.2102 2.1967 1.1442 0.1672  0.2044  -0.0144 1038 PRO A CD  
7870  N N   . LEU A 1039 ? 1.0967 2.0667 1.0752 0.2553  0.1988  -0.0231 1039 LEU A N   
7871  C CA  . LEU A 1039 ? 1.0601 2.0471 1.0595 0.2915  0.2035  -0.0218 1039 LEU A CA  
7872  C C   . LEU A 1039 ? 1.0366 1.9592 1.0054 0.3172  0.2016  -0.0340 1039 LEU A C   
7873  O O   . LEU A 1039 ? 1.0009 1.9060 0.9784 0.3451  0.1977  -0.0373 1039 LEU A O   
7874  C CB  . LEU A 1039 ? 1.0623 2.1268 1.0818 0.2980  0.2232  -0.0101 1039 LEU A CB  
7875  C CG  . LEU A 1039 ? 1.0625 2.1581 1.1126 0.3342  0.2273  -0.0052 1039 LEU A CG  
7876  C CD1 . LEU A 1039 ? 1.0263 2.0950 1.0940 0.3414  0.2088  -0.0068 1039 LEU A CD1 
7877  C CD2 . LEU A 1039 ? 1.0595 2.2490 1.1435 0.3317  0.2417  0.0096  1039 LEU A CD2 
7878  N N   . ILE A 1040 ? 1.0522 1.9375 0.9816 0.3053  0.2038  -0.0401 1040 ILE A N   
7879  C CA  . ILE A 1040 ? 1.0598 1.8831 0.9530 0.3239  0.2023  -0.0510 1040 ILE A CA  
7880  C C   . ILE A 1040 ? 1.0832 1.8369 0.9589 0.3178  0.1800  -0.0616 1040 ILE A C   
7881  O O   . ILE A 1040 ? 1.1037 1.8058 0.9591 0.3361  0.1730  -0.0707 1040 ILE A O   
7882  C CB  . ILE A 1040 ? 1.0653 1.8855 0.9213 0.3139  0.2171  -0.0515 1040 ILE A CB  
7883  C CG1 . ILE A 1040 ? 1.1092 1.9266 0.9522 0.3443  0.2333  -0.0548 1040 ILE A CG1 
7884  C CG2 . ILE A 1040 ? 1.0571 1.8125 0.8715 0.2923  0.2032  -0.0589 1040 ILE A CG2 
7885  C CD1 . ILE A 1040 ? 1.3444 2.1325 1.1973 0.3785  0.2265  -0.0601 1040 ILE A CD1 
7886  N N   . GLU A 1041 ? 1.0973 1.8508 0.9806 0.2917  0.1691  -0.0605 1041 GLU A N   
7887  C CA  . GLU A 1041 ? 1.1340 1.8325 1.0113 0.2873  0.1479  -0.0704 1041 GLU A CA  
7888  C C   . GLU A 1041 ? 1.1205 1.8222 1.0291 0.3045  0.1399  -0.0731 1041 GLU A C   
7889  O O   . GLU A 1041 ? 1.0912 1.7475 0.9964 0.3092  0.1237  -0.0834 1041 GLU A O   
7890  C CB  . GLU A 1041 ? 1.1749 1.8774 1.0563 0.2569  0.1409  -0.0684 1041 GLU A CB  
7891  C CG  . GLU A 1041 ? 1.2495 1.8886 1.1098 0.2515  0.1221  -0.0792 1041 GLU A CG  
7892  C CD  . GLU A 1041 ? 1.3816 1.9839 1.1949 0.2444  0.1234  -0.0806 1041 GLU A CD  
7893  O OE1 . GLU A 1041 ? 1.4123 2.0444 1.2121 0.2287  0.1385  -0.0723 1041 GLU A OE1 
7894  O OE2 . GLU A 1041 ? 1.4577 2.0031 1.2464 0.2534  0.1094  -0.0897 1041 GLU A OE2 
7895  N N   . LYS A 1042 ? 1.1287 1.8860 1.0678 0.3124  0.1508  -0.0636 1042 LYS A N   
7896  C CA  . LYS A 1042 ? 1.1701 1.9322 1.1357 0.3286  0.1446  -0.0644 1042 LYS A CA  
7897  C C   . LYS A 1042 ? 1.2528 1.9867 1.2029 0.3603  0.1480  -0.0692 1042 LYS A C   
7898  O O   . LYS A 1042 ? 1.2682 1.9703 1.2206 0.3718  0.1369  -0.0762 1042 LYS A O   
7899  C CB  . LYS A 1042 ? 1.1618 1.9916 1.1638 0.3247  0.1526  -0.0512 1042 LYS A CB  
7900  C CG  . LYS A 1042 ? 1.1950 2.0265 1.2174 0.3465  0.1479  -0.0506 1042 LYS A CG  
7901  C CD  . LYS A 1042 ? 1.2120 2.1111 1.2679 0.3494  0.1558  -0.0358 1042 LYS A CD  
7902  C CE  . LYS A 1042 ? 1.1790 2.0964 1.2611 0.3268  0.1449  -0.0322 1042 LYS A CE  
7903  N NZ  . LYS A 1042 ? 1.1648 2.1437 1.2776 0.3340  0.1499  -0.0171 1042 LYS A NZ  
7904  N N   . GLN A 1043 ? 1.3146 2.0592 1.2468 0.3731  0.1642  -0.0661 1043 GLN A N   
7905  C CA  . GLN A 1043 ? 1.3696 2.0796 1.2791 0.4025  0.1693  -0.0719 1043 GLN A CA  
7906  C C   . GLN A 1043 ? 1.3273 1.9655 1.2071 0.4008  0.1526  -0.0851 1043 GLN A C   
7907  O O   . GLN A 1043 ? 1.3314 1.9350 1.2054 0.4168  0.1451  -0.0916 1043 GLN A O   
7908  C CB  . GLN A 1043 ? 1.4678 2.1931 1.3559 0.4119  0.1901  -0.0690 1043 GLN A CB  
7909  C CG  . GLN A 1043 ? 1.5297 2.3188 1.4457 0.4308  0.2083  -0.0584 1043 GLN A CG  
7910  C CD  . GLN A 1043 ? 1.5525 2.3586 1.5024 0.4424  0.1993  -0.0537 1043 GLN A CD  
7911  O OE1 . GLN A 1043 ? 1.5699 2.3338 1.5095 0.4630  0.1931  -0.0597 1043 GLN A OE1 
7912  N NE2 . GLN A 1043 ? 1.5315 2.3962 1.5183 0.4263  0.1979  -0.0430 1043 GLN A NE2 
7913  N N   . LYS A 1044 ? 1.3052 1.9215 1.1649 0.3803  0.1463  -0.0887 1044 LYS A N   
7914  C CA  . LYS A 1044 ? 1.2953 1.8470 1.1264 0.3773  0.1290  -0.1003 1044 LYS A CA  
7915  C C   . LYS A 1044 ? 1.2600 1.7932 1.1112 0.3791  0.1114  -0.1073 1044 LYS A C   
7916  O O   . LYS A 1044 ? 1.2853 1.7735 1.1179 0.3905  0.1021  -0.1163 1044 LYS A O   
7917  C CB  . LYS A 1044 ? 1.2994 1.8372 1.1143 0.3525  0.1215  -0.1011 1044 LYS A CB  
7918  C CG  . LYS A 1044 ? 1.7767 2.3018 1.5509 0.3488  0.1334  -0.0992 1044 LYS A CG  
7919  C CD  . LYS A 1044 ? 1.7489 2.2671 1.5072 0.3211  0.1281  -0.0971 1044 LYS A CD  
7920  C CE  . LYS A 1044 ? 1.7573 2.2125 1.4921 0.3149  0.1041  -0.1064 1044 LYS A CE  
7921  N NZ  . LYS A 1044 ? 1.7556 2.1978 1.4718 0.2904  0.0982  -0.1041 1044 LYS A NZ  
7922  N N   . LEU A 1045 ? 1.1986 1.7667 1.0860 0.3658  0.1074  -0.1035 1045 LEU A N   
7923  C CA  . LEU A 1045 ? 1.1284 1.6808 1.0347 0.3624  0.0913  -0.1113 1045 LEU A CA  
7924  C C   . LEU A 1045 ? 1.1122 1.6635 1.0250 0.3820  0.0938  -0.1115 1045 LEU A C   
7925  O O   . LEU A 1045 ? 1.1042 1.6209 1.0126 0.3850  0.0811  -0.1213 1045 LEU A O   
7926  C CB  . LEU A 1045 ? 1.0574 1.6424 0.9955 0.3399  0.0872  -0.1082 1045 LEU A CB  
7927  C CG  . LEU A 1045 ? 1.0229 1.5968 0.9481 0.3208  0.0830  -0.1094 1045 LEU A CG  
7928  C CD1 . LEU A 1045 ? 1.0044 1.6027 0.9584 0.2992  0.0787  -0.1084 1045 LEU A CD1 
7929  C CD2 . LEU A 1045 ? 1.0068 1.5236 0.9061 0.3243  0.0672  -0.1215 1045 LEU A CD2 
7930  N N   . LYS A 1046 ? 1.1147 1.7033 1.0369 0.3952  0.1095  -0.1008 1046 LYS A N   
7931  C CA  . LYS A 1046 ? 1.1696 1.7484 1.0902 0.4175  0.1121  -0.1008 1046 LYS A CA  
7932  C C   . LYS A 1046 ? 1.2519 1.7698 1.1320 0.4308  0.1083  -0.1115 1046 LYS A C   
7933  O O   . LYS A 1046 ? 1.2798 1.7617 1.1510 0.4353  0.0978  -0.1195 1046 LYS A O   
7934  C CB  . LYS A 1046 ? 1.1851 1.8080 1.1153 0.4361  0.1309  -0.0881 1046 LYS A CB  
7935  C CG  . LYS A 1046 ? 1.1729 1.8614 1.1425 0.4239  0.1351  -0.0755 1046 LYS A CG  
7936  C CD  . LYS A 1046 ? 1.2247 1.9493 1.2057 0.4500  0.1490  -0.0645 1046 LYS A CD  
7937  C CE  . LYS A 1046 ? 1.2328 2.0332 1.2481 0.4402  0.1581  -0.0497 1046 LYS A CE  
7938  N NZ  . LYS A 1046 ? 1.2543 2.0937 1.2798 0.4701  0.1736  -0.0393 1046 LYS A NZ  
7939  N N   . LYS A 1047 ? 1.2879 1.7937 1.1410 0.4340  0.1165  -0.1117 1047 LYS A N   
7940  C CA  . LYS A 1047 ? 1.3354 1.7829 1.1451 0.4443  0.1139  -0.1209 1047 LYS A CA  
7941  C C   . LYS A 1047 ? 1.2538 1.6588 1.0563 0.4315  0.0914  -0.1327 1047 LYS A C   
7942  O O   . LYS A 1047 ? 1.2382 1.6092 1.0276 0.4398  0.0845  -0.1396 1047 LYS A O   
7943  C CB  . LYS A 1047 ? 1.4537 1.8966 1.2365 0.4412  0.1236  -0.1194 1047 LYS A CB  
7944  C CG  . LYS A 1047 ? 1.6045 1.9883 1.3378 0.4513  0.1235  -0.1276 1047 LYS A CG  
7945  C CD  . LYS A 1047 ? 1.7353 2.1273 1.4443 0.4527  0.1415  -0.1235 1047 LYS A CD  
7946  C CE  . LYS A 1047 ? 1.8644 2.1980 1.5200 0.4632  0.1452  -0.1310 1047 LYS A CE  
7947  N NZ  . LYS A 1047 ? 1.9138 2.1920 1.5440 0.4496  0.1211  -0.1402 1047 LYS A NZ  
7948  N N   . LYS A 1048 ? 1.1924 1.5998 1.0026 0.4114  0.0802  -0.1349 1048 LYS A N   
7949  C CA  . LYS A 1048 ? 1.1220 1.4962 0.9305 0.3993  0.0580  -0.1461 1048 LYS A CA  
7950  C C   . LYS A 1048 ? 1.0558 1.4285 0.8833 0.4005  0.0503  -0.1515 1048 LYS A C   
7951  O O   . LYS A 1048 ? 1.0471 1.3839 0.8615 0.3995  0.0365  -0.1619 1048 LYS A O   
7952  C CB  . LYS A 1048 ? 1.0658 1.4597 0.8966 0.3791  0.0495  -0.1455 1048 LYS A CB  
7953  C CG  . LYS A 1048 ? 1.0823 1.4495 0.8849 0.3722  0.0434  -0.1468 1048 LYS A CG  
7954  C CD  . LYS A 1048 ? 1.0753 1.4372 0.8964 0.3568  0.0246  -0.1532 1048 LYS A CD  
7955  C CE  . LYS A 1048 ? 1.0833 1.4502 0.8969 0.3433  0.0257  -0.1478 1048 LYS A CE  
7956  N NZ  . LYS A 1048 ? 1.0799 1.4293 0.9048 0.3332  0.0052  -0.1559 1048 LYS A NZ  
7957  N N   . LEU A 1049 ? 1.0193 1.4328 0.8763 0.4013  0.0595  -0.1439 1049 LEU A N   
7958  C CA  . LEU A 1049 ? 0.9941 1.4097 0.8685 0.4005  0.0540  -0.1473 1049 LEU A CA  
7959  C C   . LEU A 1049 ? 1.0613 1.4404 0.9049 0.4197  0.0576  -0.1499 1049 LEU A C   
7960  O O   . LEU A 1049 ? 1.0942 1.4489 0.9339 0.4159  0.0472  -0.1583 1049 LEU A O   
7961  C CB  . LEU A 1049 ? 0.9016 1.3694 0.8104 0.3971  0.0635  -0.1361 1049 LEU A CB  
7962  C CG  . LEU A 1049 ? 0.8199 1.2973 0.7560 0.3819  0.0532  -0.1410 1049 LEU A CG  
7963  C CD1 . LEU A 1049 ? 0.7456 1.2301 0.7011 0.3596  0.0424  -0.1478 1049 LEU A CD1 
7964  C CD2 . LEU A 1049 ? 0.7966 1.3175 0.7557 0.3843  0.0636  -0.1281 1049 LEU A CD2 
7965  N N   . LYS A 1050 ? 1.0862 1.4605 0.9061 0.4394  0.0733  -0.1433 1050 LYS A N   
7966  C CA  . LYS A 1050 ? 1.1325 1.4675 0.9191 0.4591  0.0784  -0.1459 1050 LYS A CA  
7967  C C   . LYS A 1050 ? 1.2191 1.4970 0.9646 0.4569  0.0687  -0.1572 1050 LYS A C   
7968  O O   . LYS A 1050 ? 1.2259 1.4647 0.9509 0.4564  0.0598  -0.1655 1050 LYS A O   
7969  C CB  . LYS A 1050 ? 1.1293 1.4806 0.9065 0.4835  0.1002  -0.1355 1050 LYS A CB  
7970  C CG  . LYS A 1050 ? 1.1467 1.4576 0.8922 0.5056  0.1061  -0.1375 1050 LYS A CG  
7971  C CD  . LYS A 1050 ? 1.1657 1.4878 0.8994 0.5336  0.1284  -0.1293 1050 LYS A CD  
7972  C CE  . LYS A 1050 ? 1.2374 1.5008 0.9278 0.5541  0.1320  -0.1344 1050 LYS A CE  
7973  N NZ  . LYS A 1050 ? 1.2733 1.5521 0.9677 0.5839  0.1477  -0.1250 1050 LYS A NZ  
7974  N N   . GLU A 1051 ? 1.3066 1.5775 1.0363 0.4539  0.0699  -0.1575 1051 GLU A N   
7975  C CA  . GLU A 1051 ? 1.4481 1.6630 1.1343 0.4531  0.0609  -0.1669 1051 GLU A CA  
7976  C C   . GLU A 1051 ? 1.4305 1.6312 1.1282 0.4357  0.0383  -0.1773 1051 GLU A C   
7977  O O   . GLU A 1051 ? 1.4656 1.6236 1.1340 0.4356  0.0304  -0.1856 1051 GLU A O   
7978  C CB  . GLU A 1051 ? 1.5834 1.7887 1.2472 0.4497  0.0631  -0.1657 1051 GLU A CB  
7979  C CG  . GLU A 1051 ? 1.6764 1.8877 1.3558 0.4292  0.0444  -0.1690 1051 GLU A CG  
7980  C CD  . GLU A 1051 ? 1.7723 1.9927 1.4398 0.4259  0.0525  -0.1627 1051 GLU A CD  
7981  O OE1 . GLU A 1051 ? 1.8145 2.0339 1.4585 0.4386  0.0725  -0.1576 1051 GLU A OE1 
7982  O OE2 . GLU A 1051 ? 1.7968 2.0246 1.4773 0.4105  0.0394  -0.1632 1051 GLU A OE2 
7983  N N   . GLY A 1052 ? 1.3794 1.6180 1.1204 0.4205  0.0294  -0.1772 1052 GLY A N   
7984  C CA  . GLY A 1052 ? 1.3873 1.6204 1.1454 0.4038  0.0094  -0.1880 1052 GLY A CA  
7985  C C   . GLY A 1052 ? 1.3711 1.5961 1.1310 0.4035  0.0085  -0.1923 1052 GLY A C   
7986  O O   . GLY A 1052 ? 1.3838 1.5911 1.1424 0.3910  -0.0066 -0.2033 1052 GLY A O   
7987  N N   . MET A 1053 ? 1.3874 1.6262 1.1496 0.4167  0.0242  -0.1833 1053 MET A N   
7988  C CA  . MET A 1053 ? 1.4006 1.6291 1.1611 0.4164  0.0234  -0.1858 1053 MET A CA  
7989  C C   . MET A 1053 ? 1.4405 1.6096 1.1490 0.4243  0.0221  -0.1925 1053 MET A C   
7990  O O   . MET A 1053 ? 1.4504 1.5963 1.1490 0.4126  0.0118  -0.2015 1053 MET A O   
7991  C CB  . MET A 1053 ? 1.4317 1.6910 1.2084 0.4304  0.0391  -0.1728 1053 MET A CB  
7992  C CG  . MET A 1053 ? 1.4220 1.6885 1.2153 0.4205  0.0339  -0.1743 1053 MET A CG  
7993  S SD  . MET A 1053 ? 2.7738 3.0636 2.6060 0.3880  0.0159  -0.1861 1053 MET A SD  
7994  C CE  . MET A 1053 ? 0.6135 0.8868 0.4420 0.3749  0.0093  -0.1930 1053 MET A CE  
7995  N N   . LEU A 1054 ? 1.4577 1.6019 1.1308 0.4423  0.0336  -0.1885 1054 LEU A N   
7996  C CA  . LEU A 1054 ? 1.5172 1.5997 1.1338 0.4503  0.0347  -0.1945 1054 LEU A CA  
7997  C C   . LEU A 1054 ? 1.4963 1.5501 1.0972 0.4295  0.0142  -0.2072 1054 LEU A C   
7998  O O   . LEU A 1054 ? 1.5138 1.5251 1.0814 0.4229  0.0071  -0.2154 1054 LEU A O   
7999  C CB  . LEU A 1054 ? 1.6058 1.6718 1.1903 0.4723  0.0526  -0.1882 1054 LEU A CB  
8000  C CG  . LEU A 1054 ? 1.6465 1.7455 1.2463 0.4962  0.0746  -0.1755 1054 LEU A CG  
8001  C CD1 . LEU A 1054 ? 1.6930 1.7780 1.2616 0.5149  0.0927  -0.1720 1054 LEU A CD1 
8002  C CD2 . LEU A 1054 ? 1.6806 1.7645 1.2715 0.5101  0.0803  -0.1730 1054 LEU A CD2 
8003  N N   . SER A 1055 ? 1.4411 1.5190 1.0656 0.4189  0.0042  -0.2082 1055 SER A N   
8004  C CA  . SER A 1055 ? 1.4299 1.4917 1.0495 0.4005  -0.0175 -0.2190 1055 SER A CA  
8005  C C   . SER A 1055 ? 1.3598 1.4048 0.9747 0.3858  -0.0293 -0.2296 1055 SER A C   
8006  O O   . SER A 1055 ? 1.4065 1.4174 0.9920 0.3752  -0.0426 -0.2385 1055 SER A O   
8007  C CB  . SER A 1055 ? 1.4596 1.5669 1.1281 0.3895  -0.0280 -0.2186 1055 SER A CB  
8008  O OG  . SER A 1055 ? 1.4948 1.5979 1.1720 0.3726  -0.0508 -0.2295 1055 SER A OG  
8009  N N   . ILE A 1056 ? 1.2789 1.3476 0.9207 0.3827  -0.0250 -0.2287 1056 ILE A N   
8010  C CA  . ILE A 1056 ? 1.2753 1.3322 0.9152 0.3640  -0.0369 -0.2399 1056 ILE A CA  
8011  C C   . ILE A 1056 ? 1.2972 1.2951 0.8776 0.3685  -0.0314 -0.2423 1056 ILE A C   
8012  O O   . ILE A 1056 ? 1.3112 1.2816 0.8688 0.3507  -0.0436 -0.2533 1056 ILE A O   
8013  C CB  . ILE A 1056 ? 1.0840 1.1914 0.7795 0.3510  -0.0386 -0.2410 1056 ILE A CB  
8014  C CG1 . ILE A 1056 ? 1.0499 1.1396 0.7312 0.3418  -0.0371 -0.2451 1056 ILE A CG1 
8015  C CG2 . ILE A 1056 ? 1.0203 1.1705 0.7507 0.3639  -0.0257 -0.2280 1056 ILE A CG2 
8016  C CD1 . ILE A 1056 ? 1.0499 1.1267 0.7124 0.3621  -0.0196 -0.2329 1056 ILE A CD1 
8017  N N   . MET A 1057 ? 1.3401 1.3172 0.8929 0.3925  -0.0130 -0.2324 1057 MET A N   
8018  C CA  . MET A 1057 ? 1.4666 1.3862 0.9631 0.4012  -0.0046 -0.2331 1057 MET A CA  
8019  C C   . MET A 1057 ? 1.5593 1.4217 1.0025 0.3843  -0.0165 -0.2453 1057 MET A C   
8020  O O   . MET A 1057 ? 1.5870 1.4073 0.9918 0.3794  -0.0154 -0.2493 1057 MET A O   
8021  C CB  . MET A 1057 ? 1.5650 1.4664 1.0343 0.4328  0.0168  -0.2223 1057 MET A CB  
8022  C CG  . MET A 1057 ? 1.6394 1.4977 1.0680 0.4500  0.0298  -0.2189 1057 MET A CG  
8023  S SD  . MET A 1057 ? 2.0190 1.9271 1.4945 0.4658  0.0403  -0.2059 1057 MET A SD  
8024  C CE  . MET A 1057 ? 2.3809 2.3337 1.8835 0.4918  0.0578  -0.1936 1057 MET A CE  
8025  N N   . SER A 1058 ? 1.5549 1.4132 0.9918 0.3750  -0.0281 -0.2503 1058 SER A N   
8026  C CA  . SER A 1058 ? 1.5627 1.3721 0.9506 0.3573  -0.0410 -0.2608 1058 SER A CA  
8027  C C   . SER A 1058 ? 1.5198 1.3348 0.9180 0.3301  -0.0553 -0.2718 1058 SER A C   
8028  O O   . SER A 1058 ? 1.5535 1.3195 0.9010 0.3154  -0.0604 -0.2797 1058 SER A O   
8029  C CB  . SER A 1058 ? 1.5304 1.3525 0.9278 0.3496  -0.0556 -0.2633 1058 SER A CB  
8030  O OG  . SER A 1058 ? 1.4828 1.3370 0.9089 0.3679  -0.0461 -0.2533 1058 SER A OG  
8031  N N   . TYR A 1059 ? 1.4411 1.3161 0.9034 0.3216  -0.0611 -0.2727 1059 TYR A N   
8032  C CA  . TYR A 1059 ? 1.4294 1.3190 0.9091 0.2952  -0.0724 -0.2835 1059 TYR A CA  
8033  C C   . TYR A 1059 ? 1.5095 1.3855 0.9782 0.2992  -0.0595 -0.2795 1059 TYR A C   
8034  O O   . TYR A 1059 ? 1.5244 1.4163 1.0108 0.2774  -0.0658 -0.2872 1059 TYR A O   
8035  C CB  . TYR A 1059 ? 1.3049 1.2634 0.8574 0.2828  -0.0846 -0.2880 1059 TYR A CB  
8036  C CG  . TYR A 1059 ? 1.2627 1.2378 0.8312 0.2828  -0.0982 -0.2899 1059 TYR A CG  
8037  C CD1 . TYR A 1059 ? 1.2792 1.2560 0.8482 0.3048  -0.0908 -0.2789 1059 TYR A CD1 
8038  C CD2 . TYR A 1059 ? 1.2825 1.2729 0.8658 0.2603  -0.1189 -0.3025 1059 TYR A CD2 
8039  C CE1 . TYR A 1059 ? 1.3225 1.3092 0.9013 0.3041  -0.1047 -0.2799 1059 TYR A CE1 
8040  C CE2 . TYR A 1059 ? 1.3370 1.3412 0.9344 0.2616  -0.1341 -0.3034 1059 TYR A CE2 
8041  C CZ  . TYR A 1059 ? 1.3554 1.3546 0.9483 0.2835  -0.1274 -0.2918 1059 TYR A CZ  
8042  O OH  . TYR A 1059 ? 1.3636 1.3711 0.9654 0.2839  -0.1439 -0.2922 1059 TYR A OH  
8043  N N   . ARG A 1060 ? 1.5703 1.4188 1.0112 0.3269  -0.0416 -0.2677 1060 ARG A N   
8044  C CA  . ARG A 1060 ? 1.6347 1.4598 1.0552 0.3321  -0.0316 -0.2636 1060 ARG A CA  
8045  C C   . ARG A 1060 ? 1.7296 1.4780 1.0735 0.3256  -0.0316 -0.2698 1060 ARG A C   
8046  O O   . ARG A 1060 ? 1.7738 1.4763 1.0698 0.3411  -0.0245 -0.2676 1060 ARG A O   
8047  C CB  . ARG A 1060 ? 1.6612 1.4955 1.0899 0.3664  -0.0129 -0.2477 1060 ARG A CB  
8048  C CG  . ARG A 1060 ? 1.5911 1.4243 1.0223 0.3697  -0.0071 -0.2419 1060 ARG A CG  
8049  C CD  . ARG A 1060 ? 1.6085 1.4508 1.0455 0.4060  0.0106  -0.2256 1060 ARG A CD  
8050  N NE  . ARG A 1060 ? 1.7265 1.4990 1.0969 0.4279  0.0216  -0.2222 1060 ARG A NE  
8051  C CZ  . ARG A 1060 ? 1.7719 1.5395 1.1342 0.4643  0.0384  -0.2097 1060 ARG A CZ  
8052  N NH1 . ARG A 1060 ? 1.7614 1.5926 1.1780 0.4804  0.0459  -0.1990 1060 ARG A NH1 
8053  N NH2 . ARG A 1060 ? 1.8158 1.5156 1.1153 0.4848  0.0483  -0.2080 1060 ARG A NH2 
8054  N N   . ASN A 1061 ? 1.7828 1.5146 1.1115 0.3009  -0.0386 -0.2780 1061 ASN A N   
8055  C CA  . ASN A 1061 ? 1.9250 1.5791 1.1749 0.2908  -0.0388 -0.2843 1061 ASN A CA  
8056  C C   . ASN A 1061 ? 1.9997 1.5982 1.2001 0.3199  -0.0215 -0.2736 1061 ASN A C   
8057  O O   . ASN A 1061 ? 1.9668 1.5927 1.1976 0.3496  -0.0095 -0.2609 1061 ASN A O   
8058  C CB  . ASN A 1061 ? 1.9880 1.6412 1.2329 0.2494  -0.0534 -0.2986 1061 ASN A CB  
8059  C CG  . ASN A 1061 ? 2.0639 1.7199 1.3022 0.2221  -0.0698 -0.3118 1061 ASN A CG  
8060  O OD1 . ASN A 1061 ? 2.0513 1.7439 1.3246 0.2289  -0.0754 -0.3110 1061 ASN A OD1 
8061  N ND2 . ASN A 1061 ? 2.1412 1.7571 1.3315 0.1904  -0.0781 -0.3236 1061 ASN A ND2 
8062  N N   . ALA A 1062 ? 2.0935 1.6137 1.2165 0.3119  -0.0203 -0.2789 1062 ALA A N   
8063  C CA  . ALA A 1062 ? 2.1629 1.6182 1.2285 0.3419  -0.0041 -0.2699 1062 ALA A CA  
8064  C C   . ALA A 1062 ? 2.1469 1.6103 1.2269 0.3465  -0.0017 -0.2629 1062 ALA A C   
8065  O O   . ALA A 1062 ? 2.1752 1.6238 1.2467 0.3816  0.0117  -0.2503 1062 ALA A O   
8066  C CB  . ALA A 1062 ? 2.2649 1.6281 1.2375 0.3285  -0.0044 -0.2786 1062 ALA A CB  
8067  N N   . ASP A 1063 ? 2.0962 1.5838 1.1975 0.3100  -0.0151 -0.2715 1063 ASP A N   
8068  C CA  . ASP A 1063 ? 2.0713 1.5615 1.1797 0.3056  -0.0155 -0.2667 1063 ASP A CA  
8069  C C   . ASP A 1063 ? 1.9345 1.5096 1.1278 0.3186  -0.0137 -0.2566 1063 ASP A C   
8070  O O   . ASP A 1063 ? 1.9041 1.4930 1.1135 0.3148  -0.0146 -0.2513 1063 ASP A O   
8071  C CB  . ASP A 1063 ? 2.1158 1.5960 1.2082 0.2569  -0.0295 -0.2819 1063 ASP A CB  
8072  C CG  . ASP A 1063 ? 2.0997 1.6414 1.2439 0.2272  -0.0420 -0.2948 1063 ASP A CG  
8073  O OD1 . ASP A 1063 ? 2.0562 1.6525 1.2551 0.2448  -0.0406 -0.2903 1063 ASP A OD1 
8074  O OD2 . ASP A 1063 ? 2.1354 1.6712 1.2652 0.1867  -0.0532 -0.3094 1063 ASP A OD2 
8075  N N   . TYR A 1064 ? 1.8621 1.4905 1.1051 0.3324  -0.0113 -0.2537 1064 TYR A N   
8076  C CA  . TYR A 1064 ? 1.7605 1.4692 1.0816 0.3425  -0.0092 -0.2447 1064 TYR A CA  
8077  C C   . TYR A 1064 ? 1.7192 1.4859 1.0948 0.3064  -0.0226 -0.2561 1064 TYR A C   
8078  O O   . TYR A 1064 ? 1.7068 1.5411 1.1481 0.3082  -0.0226 -0.2516 1064 TYR A O   
8079  C CB  . TYR A 1064 ? 1.7248 1.4353 1.0508 0.3633  -0.0016 -0.2303 1064 TYR A CB  
8080  C CG  . TYR A 1064 ? 1.7527 1.4305 1.0477 0.4072  0.0134  -0.2179 1064 TYR A CG  
8081  C CD1 . TYR A 1064 ? 1.7104 1.4341 1.0449 0.4331  0.0229  -0.2096 1064 TYR A CD1 
8082  C CD2 . TYR A 1064 ? 1.8282 1.4259 1.0506 0.4222  0.0188  -0.2157 1064 TYR A CD2 
8083  C CE1 . TYR A 1064 ? 1.7584 1.4558 1.0660 0.4733  0.0385  -0.1998 1064 TYR A CE1 
8084  C CE2 . TYR A 1064 ? 1.8807 1.4483 1.0750 0.4651  0.0343  -0.2057 1064 TYR A CE2 
8085  C CZ  . TYR A 1064 ? 1.8335 1.4540 1.0727 0.4905  0.0446  -0.1982 1064 TYR A CZ  
8086  O OH  . TYR A 1064 ? 1.8669 1.4622 1.0807 0.5329  0.0618  -0.1895 1064 TYR A OH  
8087  N N   . SER A 1065 ? 1.6998 1.4404 1.0473 0.2732  -0.0336 -0.2715 1065 SER A N   
8088  C CA  . SER A 1065 ? 1.6193 1.4162 1.0190 0.2406  -0.0459 -0.2844 1065 SER A CA  
8089  C C   . SER A 1065 ? 1.5647 1.3929 0.9934 0.2468  -0.0505 -0.2873 1065 SER A C   
8090  O O   . SER A 1065 ? 1.6047 1.3910 0.9893 0.2514  -0.0518 -0.2901 1065 SER A O   
8091  C CB  . SER A 1065 ? 1.6653 1.4298 1.0275 0.2018  -0.0561 -0.3004 1065 SER A CB  
8092  O OG  . SER A 1065 ? 1.7263 1.4541 1.0468 0.1947  -0.0620 -0.3087 1065 SER A OG  
8093  N N   . TYR A 1066 ? 1.4813 1.3792 0.9802 0.2465  -0.0530 -0.2863 1066 TYR A N   
8094  C CA  . TYR A 1066 ? 1.4601 1.3876 0.9872 0.2486  -0.0603 -0.2901 1066 TYR A CA  
8095  C C   . TYR A 1066 ? 1.4723 1.4099 1.0056 0.2150  -0.0766 -0.3079 1066 TYR A C   
8096  O O   . TYR A 1066 ? 1.4937 1.4304 1.0234 0.1878  -0.0809 -0.3179 1066 TYR A O   
8097  C CB  . TYR A 1066 ? 1.3699 1.3630 0.9649 0.2607  -0.0570 -0.2825 1066 TYR A CB  
8098  C CG  . TYR A 1066 ? 1.3705 1.3615 0.9629 0.2912  -0.0413 -0.2651 1066 TYR A CG  
8099  C CD1 . TYR A 1066 ? 1.3882 1.3618 0.9640 0.2947  -0.0337 -0.2585 1066 TYR A CD1 
8100  C CD2 . TYR A 1066 ? 1.3645 1.3709 0.9695 0.3163  -0.0344 -0.2551 1066 TYR A CD2 
8101  C CE1 . TYR A 1066 ? 1.4198 1.3962 0.9961 0.3243  -0.0203 -0.2420 1066 TYR A CE1 
8102  C CE2 . TYR A 1066 ? 1.3914 1.4017 0.9962 0.3440  -0.0192 -0.2395 1066 TYR A CE2 
8103  C CZ  . TYR A 1066 ? 1.4270 1.4244 1.0195 0.3490  -0.0125 -0.2328 1066 TYR A CZ  
8104  O OH  . TYR A 1066 ? 1.4554 1.4616 1.0509 0.3781  0.0015  -0.2169 1066 TYR A OH  
8105  N N   . SER A 1067 ? 1.4461 1.3949 0.9887 0.2160  -0.0862 -0.3120 1067 SER A N   
8106  C CA  . SER A 1067 ? 1.4508 1.4090 0.9966 0.1863  -0.1031 -0.3282 1067 SER A CA  
8107  C C   . SER A 1067 ? 1.4254 1.4307 1.0196 0.1892  -0.1155 -0.3313 1067 SER A C   
8108  O O   . SER A 1067 ? 1.4279 1.4251 1.0163 0.2119  -0.1138 -0.3220 1067 SER A O   
8109  C CB  . SER A 1067 ? 1.5152 1.4046 0.9843 0.1773  -0.1061 -0.3324 1067 SER A CB  
8110  O OG  . SER A 1067 ? 1.5335 1.4212 0.9919 0.1413  -0.1155 -0.3473 1067 SER A OG  
8111  N N   . VAL A 1068 ? 1.4027 1.4561 1.0435 0.1660  -0.1277 -0.3448 1068 VAL A N   
8112  C CA  . VAL A 1068 ? 1.3779 1.4827 1.0742 0.1697  -0.1398 -0.3482 1068 VAL A CA  
8113  C C   . VAL A 1068 ? 1.4557 1.5394 1.1299 0.1856  -0.1487 -0.3424 1068 VAL A C   
8114  O O   . VAL A 1068 ? 1.4491 1.5489 1.1468 0.2075  -0.1456 -0.3327 1068 VAL A O   
8115  C CB  . VAL A 1068 ? 1.3540 1.4959 1.0813 0.1409  -0.1545 -0.3661 1068 VAL A CB  
8116  C CG1 . VAL A 1068 ? 1.4443 1.5415 1.1121 0.1202  -0.1634 -0.3739 1068 VAL A CG1 
8117  C CG2 . VAL A 1068 ? 1.3017 1.4908 1.0820 0.1490  -0.1684 -0.3689 1068 VAL A CG2 
8118  N N   . TRP A 1069 ? 1.5317 1.5804 1.1604 0.1723  -0.1604 -0.3487 1069 TRP A N   
8119  C CA  . TRP A 1069 ? 1.5794 1.5933 1.1709 0.1870  -0.1663 -0.3413 1069 TRP A CA  
8120  C C   . TRP A 1069 ? 1.6559 1.5946 1.1657 0.1906  -0.1554 -0.3360 1069 TRP A C   
8121  O O   . TRP A 1069 ? 1.6756 1.5875 1.1555 0.1791  -0.1469 -0.3393 1069 TRP A O   
8122  C CB  . TRP A 1069 ? 1.5704 1.6030 1.1735 0.1729  -0.1912 -0.3504 1069 TRP A CB  
8123  C CG  . TRP A 1069 ? 1.4794 1.5819 1.1557 0.1622  -0.2052 -0.3611 1069 TRP A CG  
8124  C CD1 . TRP A 1069 ? 1.4195 1.5654 1.1500 0.1771  -0.2135 -0.3587 1069 TRP A CD1 
8125  C CD2 . TRP A 1069 ? 1.4186 1.5533 1.1188 0.1340  -0.2123 -0.3769 1069 TRP A CD2 
8126  N NE1 . TRP A 1069 ? 1.3607 1.5647 1.1500 0.1622  -0.2248 -0.3724 1069 TRP A NE1 
8127  C CE2 . TRP A 1069 ? 1.3780 1.5793 1.1518 0.1350  -0.2237 -0.3841 1069 TRP A CE2 
8128  C CE3 . TRP A 1069 ? 1.4163 1.5289 1.0811 0.1071  -0.2093 -0.3861 1069 TRP A CE3 
8129  C CZ2 . TRP A 1069 ? 1.3702 1.6206 1.1865 0.1111  -0.2308 -0.4007 1069 TRP A CZ2 
8130  C CZ3 . TRP A 1069 ? 1.4222 1.5824 1.1263 0.0806  -0.2170 -0.4023 1069 TRP A CZ3 
8131  C CH2 . TRP A 1069 ? 1.4035 1.6348 1.1851 0.0829  -0.2272 -0.4099 1069 TRP A CH2 
8132  N N   . LYS A 1070 ? 1.6838 1.5857 1.1546 0.2056  -0.1559 -0.3284 1070 LYS A N   
8133  C CA  . LYS A 1070 ? 1.7210 1.5496 1.1144 0.2146  -0.1419 -0.3225 1070 LYS A CA  
8134  C C   . LYS A 1070 ? 1.7918 1.5728 1.1265 0.1882  -0.1477 -0.3324 1070 LYS A C   
8135  O O   . LYS A 1070 ? 1.8138 1.5937 1.1364 0.1664  -0.1667 -0.3408 1070 LYS A O   
8136  C CB  . LYS A 1070 ? 1.7109 1.5110 1.0747 0.2343  -0.1398 -0.3134 1070 LYS A CB  
8137  C CG  . LYS A 1070 ? 1.6742 1.4769 1.0478 0.2659  -0.1178 -0.3000 1070 LYS A CG  
8138  C CD  . LYS A 1070 ? 1.7317 1.4757 1.0422 0.2841  -0.1047 -0.2924 1070 LYS A CD  
8139  C CE  . LYS A 1070 ? 1.7286 1.4804 1.0436 0.2893  -0.1146 -0.2886 1070 LYS A CE  
8140  N NZ  . LYS A 1070 ? 1.7893 1.4827 1.0396 0.3043  -0.1010 -0.2824 1070 LYS A NZ  
8141  N N   . GLY A 1071 ? 1.8488 1.5894 1.1451 0.1902  -0.1315 -0.3309 1071 GLY A N   
8142  C CA  . GLY A 1071 ? 1.9574 1.6403 1.1858 0.1660  -0.1338 -0.3391 1071 GLY A CA  
8143  C C   . GLY A 1071 ? 1.9741 1.6945 1.2320 0.1314  -0.1469 -0.3528 1071 GLY A C   
8144  O O   . GLY A 1071 ? 2.0751 1.7567 1.2820 0.1036  -0.1516 -0.3619 1071 GLY A O   
8145  N N   . GLY A 1072 ? 1.8806 1.6763 1.2197 0.1320  -0.1519 -0.3548 1072 GLY A N   
8146  C CA  . GLY A 1072 ? 1.8634 1.7054 1.2420 0.1013  -0.1616 -0.3685 1072 GLY A CA  
8147  C C   . GLY A 1072 ? 1.8791 1.7053 1.2456 0.0951  -0.1471 -0.3688 1072 GLY A C   
8148  O O   . GLY A 1072 ? 1.8700 1.6871 1.2404 0.1213  -0.1310 -0.3569 1072 GLY A O   
8149  N N   . SER A 1073 ? 1.9053 1.7288 1.2559 0.0590  -0.1536 -0.3824 1073 SER A N   
8150  C CA  . SER A 1073 ? 1.9143 1.7118 1.2405 0.0481  -0.1417 -0.3834 1073 SER A CA  
8151  C C   . SER A 1073 ? 1.8129 1.6568 1.2009 0.0686  -0.1310 -0.3754 1073 SER A C   
8152  O O   . SER A 1073 ? 1.7311 1.6431 1.1919 0.0749  -0.1364 -0.3768 1073 SER A O   
8153  C CB  . SER A 1073 ? 1.9397 1.7517 1.2615 0.0018  -0.1521 -0.4015 1073 SER A CB  
8154  O OG  . SER A 1073 ? 1.9174 1.7910 1.2899 -0.0128 -0.1699 -0.4122 1073 SER A OG  
8155  N N   . ALA A 1074 ? 1.8398 1.6438 1.1959 0.0801  -0.1163 -0.3665 1074 ALA A N   
8156  C CA  . ALA A 1074 ? 1.7644 1.6050 1.1701 0.1011  -0.1054 -0.3562 1074 ALA A CA  
8157  C C   . ALA A 1074 ? 1.6788 1.5930 1.1551 0.0773  -0.1122 -0.3679 1074 ALA A C   
8158  O O   . ALA A 1074 ? 1.7047 1.6226 1.1728 0.0414  -0.1189 -0.3828 1074 ALA A O   
8159  C CB  . ALA A 1074 ? 1.8243 1.6132 1.1830 0.1065  -0.0931 -0.3482 1074 ALA A CB  
8160  N N   . SER A 1075 ? 1.5635 1.5358 1.1075 0.0960  -0.1100 -0.3620 1075 SER A N   
8161  C CA  . SER A 1075 ? 1.4883 1.5283 1.0998 0.0765  -0.1131 -0.3726 1075 SER A CA  
8162  C C   . SER A 1075 ? 1.4598 1.5078 1.0875 0.0858  -0.0998 -0.3624 1075 SER A C   
8163  O O   . SER A 1075 ? 1.4229 1.4684 1.0569 0.1174  -0.0911 -0.3460 1075 SER A O   
8164  C CB  . SER A 1075 ? 1.4470 1.5475 1.1240 0.0876  -0.1212 -0.3748 1075 SER A CB  
8165  O OG  . SER A 1075 ? 1.4094 1.5469 1.1347 0.1050  -0.1116 -0.3655 1075 SER A OG  
8166  N N   . THR A 1076 ? 1.4526 1.5114 1.0858 0.0559  -0.0985 -0.3725 1076 THR A N   
8167  C CA  . THR A 1076 ? 1.3929 1.4596 1.0391 0.0566  -0.0879 -0.3648 1076 THR A CA  
8168  C C   . THR A 1076 ? 1.3108 1.4400 1.0283 0.0732  -0.0848 -0.3596 1076 THR A C   
8169  O O   . THR A 1076 ? 1.2975 1.4325 1.0267 0.0905  -0.0756 -0.3454 1076 THR A O   
8170  C CB  . THR A 1076 ? 1.3646 1.4431 1.0132 0.0152  -0.0892 -0.3809 1076 THR A CB  
8171  O OG1 . THR A 1076 ? 1.4210 1.4473 1.0167 0.0096  -0.0826 -0.3733 1076 THR A OG1 
8172  C CG2 . THR A 1076 ? 1.2772 1.4275 1.0011 0.0060  -0.0865 -0.3874 1076 THR A CG2 
8173  N N   . TRP A 1077 ? 1.2845 1.4593 1.0475 0.0679  -0.0934 -0.3710 1077 TRP A N   
8174  C CA  . TRP A 1077 ? 1.2225 1.4561 1.0532 0.0801  -0.0919 -0.3693 1077 TRP A CA  
8175  C C   . TRP A 1077 ? 1.1578 1.3839 0.9887 0.1177  -0.0870 -0.3499 1077 TRP A C   
8176  O O   . TRP A 1077 ? 1.0859 1.3315 0.9410 0.1303  -0.0775 -0.3384 1077 TRP A O   
8177  C CB  . TRP A 1077 ? 1.2286 1.5057 1.1015 0.0685  -0.1044 -0.3863 1077 TRP A CB  
8178  C CG  . TRP A 1077 ? 1.2227 1.5573 1.1631 0.0765  -0.1029 -0.3879 1077 TRP A CG  
8179  C CD1 . TRP A 1077 ? 1.2233 1.5979 1.2061 0.0598  -0.0957 -0.3958 1077 TRP A CD1 
8180  C CD2 . TRP A 1077 ? 1.2294 1.5837 1.1987 0.1020  -0.1084 -0.3819 1077 TRP A CD2 
8181  N NE1 . TRP A 1077 ? 1.2045 1.6211 1.2402 0.0743  -0.0958 -0.3952 1077 TRP A NE1 
8182  C CE2 . TRP A 1077 ? 1.2048 1.6092 1.2328 0.1003  -0.1041 -0.3864 1077 TRP A CE2 
8183  C CE3 . TRP A 1077 ? 1.2566 1.5875 1.2041 0.1249  -0.1161 -0.3731 1077 TRP A CE3 
8184  C CZ2 . TRP A 1077 ? 1.1671 1.5962 1.2307 0.1214  -0.1080 -0.3822 1077 TRP A CZ2 
8185  C CZ3 . TRP A 1077 ? 1.2370 1.5946 1.2210 0.1447  -0.1205 -0.3689 1077 TRP A CZ3 
8186  C CH2 . TRP A 1077 ? 1.1793 1.5842 1.2196 0.1431  -0.1168 -0.3732 1077 TRP A CH2 
8187  N N   . LEU A 1078 ? 1.1725 1.3705 0.9744 0.1334  -0.0933 -0.3468 1078 LEU A N   
8188  C CA  . LEU A 1078 ? 1.1444 1.3376 0.9465 0.1663  -0.0890 -0.3308 1078 LEU A CA  
8189  C C   . LEU A 1078 ? 1.1895 1.3501 0.9581 0.1848  -0.0751 -0.3139 1078 LEU A C   
8190  O O   . LEU A 1078 ? 1.1888 1.3661 0.9762 0.2071  -0.0668 -0.2999 1078 LEU A O   
8191  C CB  . LEU A 1078 ? 1.1143 1.2836 0.8906 0.1760  -0.0992 -0.3323 1078 LEU A CB  
8192  C CG  . LEU A 1078 ? 1.0290 1.2094 0.8211 0.2045  -0.0970 -0.3199 1078 LEU A CG  
8193  C CD1 . LEU A 1078 ? 0.9759 1.1785 0.7928 0.2034  -0.1126 -0.3278 1078 LEU A CD1 
8194  C CD2 . LEU A 1078 ? 1.0664 1.1941 0.8023 0.2271  -0.0881 -0.3065 1078 LEU A CD2 
8195  N N   . THR A 1079 ? 1.2303 1.3459 0.9500 0.1749  -0.0729 -0.3150 1079 THR A N   
8196  C CA  . THR A 1079 ? 1.2572 1.3441 0.9485 0.1928  -0.0609 -0.2992 1079 THR A CA  
8197  C C   . THR A 1079 ? 1.1966 1.3316 0.9373 0.1928  -0.0539 -0.2916 1079 THR A C   
8198  O O   . THR A 1079 ? 1.1987 1.3418 0.9467 0.2176  -0.0449 -0.2752 1079 THR A O   
8199  C CB  . THR A 1079 ? 1.4444 1.4723 1.0737 0.1784  -0.0609 -0.3030 1079 THR A CB  
8200  O OG1 . THR A 1079 ? 1.4960 1.4762 1.0750 0.1793  -0.0663 -0.3086 1079 THR A OG1 
8201  C CG2 . THR A 1079 ? 1.4495 1.4481 1.0511 0.2003  -0.0500 -0.2858 1079 THR A CG2 
8202  N N   . ALA A 1080 ? 1.1535 1.3229 0.9288 0.1638  -0.0577 -0.3040 1080 ALA A N   
8203  C CA  . ALA A 1080 ? 1.0755 1.2877 0.8941 0.1600  -0.0511 -0.2980 1080 ALA A CA  
8204  C C   . ALA A 1080 ? 1.0156 1.2649 0.8737 0.1824  -0.0482 -0.2891 1080 ALA A C   
8205  O O   . ALA A 1080 ? 0.9923 1.2488 0.8543 0.2026  -0.0397 -0.2721 1080 ALA A O   
8206  C CB  . ALA A 1080 ? 1.0560 1.3003 0.9068 0.1245  -0.0547 -0.3157 1080 ALA A CB  
8207  N N   . PHE A 1081 ? 0.9636 1.2348 0.8480 0.1785  -0.0560 -0.3004 1081 PHE A N   
8208  C CA  . PHE A 1081 ? 0.9043 1.2108 0.8273 0.1939  -0.0551 -0.2950 1081 PHE A CA  
8209  C C   . PHE A 1081 ? 0.8753 1.1624 0.7743 0.2249  -0.0485 -0.2771 1081 PHE A C   
8210  O O   . PHE A 1081 ? 0.8084 1.1223 0.7322 0.2382  -0.0427 -0.2666 1081 PHE A O   
8211  C CB  . PHE A 1081 ? 0.9283 1.2486 0.8711 0.1876  -0.0676 -0.3098 1081 PHE A CB  
8212  C CG  . PHE A 1081 ? 0.9358 1.2865 0.9143 0.2020  -0.0685 -0.3055 1081 PHE A CG  
8213  C CD1 . PHE A 1081 ? 0.9075 1.3011 0.9345 0.1919  -0.0662 -0.3101 1081 PHE A CD1 
8214  C CD2 . PHE A 1081 ? 0.9980 1.3304 0.9574 0.2243  -0.0712 -0.2971 1081 PHE A CD2 
8215  C CE1 . PHE A 1081 ? 0.8989 1.3138 0.9526 0.2047  -0.0671 -0.3059 1081 PHE A CE1 
8216  C CE2 . PHE A 1081 ? 0.9916 1.3467 0.9780 0.2357  -0.0726 -0.2928 1081 PHE A CE2 
8217  C CZ  . PHE A 1081 ? 0.9403 1.3355 0.9731 0.2262  -0.0708 -0.2970 1081 PHE A CZ  
8218  N N   . ALA A 1082 ? 0.9291 1.1681 0.7772 0.2354  -0.0485 -0.2742 1082 ALA A N   
8219  C CA  . ALA A 1082 ? 0.9599 1.1781 0.7819 0.2654  -0.0401 -0.2585 1082 ALA A CA  
8220  C C   . ALA A 1082 ? 0.9444 1.1747 0.7720 0.2759  -0.0282 -0.2431 1082 ALA A C   
8221  O O   . ALA A 1082 ? 0.9260 1.1846 0.7753 0.2917  -0.0207 -0.2308 1082 ALA A O   
8222  C CB  . ALA A 1082 ? 1.0328 1.1929 0.7963 0.2730  -0.0418 -0.2607 1082 ALA A CB  
8223  N N   . LEU A 1083 ? 0.9410 1.1506 0.7481 0.2654  -0.0276 -0.2437 1083 LEU A N   
8224  C CA  . LEU A 1083 ? 0.8990 1.1272 0.7186 0.2684  -0.0201 -0.2307 1083 LEU A CA  
8225  C C   . LEU A 1083 ? 0.8662 1.1542 0.7417 0.2610  -0.0173 -0.2266 1083 LEU A C   
8226  O O   . LEU A 1083 ? 0.8805 1.1914 0.7691 0.2791  -0.0091 -0.2110 1083 LEU A O   
8227  C CB  . LEU A 1083 ? 0.8723 1.0781 0.6726 0.2450  -0.0242 -0.2377 1083 LEU A CB  
8228  C CG  . LEU A 1083 ? 0.8981 1.0403 0.6360 0.2594  -0.0234 -0.2346 1083 LEU A CG  
8229  C CD1 . LEU A 1083 ? 0.9307 1.0415 0.6406 0.2298  -0.0300 -0.2467 1083 LEU A CD1 
8230  C CD2 . LEU A 1083 ? 0.8796 1.0146 0.6042 0.2903  -0.0139 -0.2140 1083 LEU A CD2 
8231  N N   . ARG A 1084 ? 0.8097 1.1229 0.7168 0.2341  -0.0231 -0.2408 1084 ARG A N   
8232  C CA  . ARG A 1084 ? 0.7904 1.1548 0.7470 0.2265  -0.0202 -0.2390 1084 ARG A CA  
8233  C C   . ARG A 1084 ? 0.8118 1.1932 0.7789 0.2503  -0.0151 -0.2270 1084 ARG A C   
8234  O O   . ARG A 1084 ? 0.8044 1.2158 0.7907 0.2550  -0.0074 -0.2136 1084 ARG A O   
8235  C CB  . ARG A 1084 ? 0.7908 1.1748 0.7778 0.2020  -0.0276 -0.2588 1084 ARG A CB  
8236  C CG  . ARG A 1084 ? 0.7171 1.1389 0.7450 0.2045  -0.0269 -0.2594 1084 ARG A CG  
8237  C CD  . ARG A 1084 ? 0.7098 1.1671 0.7743 0.1823  -0.0228 -0.2635 1084 ARG A CD  
8238  N NE  . ARG A 1084 ? 0.7459 1.2342 0.8429 0.1852  -0.0198 -0.2609 1084 ARG A NE  
8239  C CZ  . ARG A 1084 ? 0.8097 1.3183 0.9387 0.1714  -0.0228 -0.2756 1084 ARG A CZ  
8240  N NH1 . ARG A 1084 ? 0.8596 1.3663 0.9956 0.1543  -0.0288 -0.2944 1084 ARG A NH1 
8241  N NH2 . ARG A 1084 ? 0.7942 1.3248 0.9471 0.1743  -0.0195 -0.2724 1084 ARG A NH2 
8242  N N   . VAL A 1085 ? 0.8596 1.2226 0.8127 0.2629  -0.0194 -0.2315 1085 VAL A N   
8243  C CA  . VAL A 1085 ? 0.8890 1.2670 0.8501 0.2816  -0.0146 -0.2215 1085 VAL A CA  
8244  C C   . VAL A 1085 ? 0.9041 1.2726 0.8409 0.3072  -0.0036 -0.2041 1085 VAL A C   
8245  O O   . VAL A 1085 ? 0.8760 1.2690 0.8249 0.3190  0.0041  -0.1926 1085 VAL A O   
8246  C CB  . VAL A 1085 ? 0.7721 1.1353 0.7270 0.2857  -0.0238 -0.2312 1085 VAL A CB  
8247  C CG1 . VAL A 1085 ? 0.7523 1.1305 0.7135 0.3014  -0.0183 -0.2204 1085 VAL A CG1 
8248  C CG2 . VAL A 1085 ? 0.7237 1.1020 0.7078 0.2633  -0.0351 -0.2488 1085 VAL A CG2 
8249  N N   . LEU A 1086 ? 0.9716 1.3041 0.8731 0.3151  -0.0027 -0.2028 1086 LEU A N   
8250  C CA  . LEU A 1086 ? 1.0447 1.3656 0.9224 0.3417  0.0080  -0.1875 1086 LEU A CA  
8251  C C   . LEU A 1086 ? 1.0233 1.3828 0.9271 0.3407  0.0143  -0.1738 1086 LEU A C   
8252  O O   . LEU A 1086 ? 1.0325 1.4180 0.9456 0.3589  0.0240  -0.1592 1086 LEU A O   
8253  C CB  . LEU A 1086 ? 1.1313 1.3957 0.9596 0.3498  0.0065  -0.1908 1086 LEU A CB  
8254  C CG  . LEU A 1086 ? 1.2610 1.4741 1.0421 0.3661  0.0070  -0.1955 1086 LEU A CG  
8255  C CD1 . LEU A 1086 ? 1.2537 1.4676 1.0227 0.3980  0.0206  -0.1821 1086 LEU A CD1 
8256  C CD2 . LEU A 1086 ? 1.2694 1.4761 1.0529 0.3503  -0.0040 -0.2103 1086 LEU A CD2 
8257  N N   . GLY A 1087 ? 0.9867 1.3506 0.9010 0.3180  0.0087  -0.1787 1087 GLY A N   
8258  C CA  . GLY A 1087 ? 0.9455 1.3426 0.8814 0.3122  0.0123  -0.1663 1087 GLY A CA  
8259  C C   . GLY A 1087 ? 0.8769 1.3256 0.8515 0.3094  0.0176  -0.1592 1087 GLY A C   
8260  O O   . GLY A 1087 ? 0.8918 1.3693 0.8761 0.3240  0.0255  -0.1428 1087 GLY A O   
8261  N N   . GLN A 1088 ? 0.8166 1.2763 0.8119 0.2911  0.0132  -0.1719 1088 GLN A N   
8262  C CA  . GLN A 1088 ? 0.8090 1.3072 0.8334 0.2877  0.0176  -0.1673 1088 GLN A CA  
8263  C C   . GLN A 1088 ? 0.8756 1.3850 0.8925 0.3131  0.0267  -0.1531 1088 GLN A C   
8264  O O   . GLN A 1088 ? 0.8655 1.4144 0.9016 0.3130  0.0341  -0.1399 1088 GLN A O   
8265  C CB  . GLN A 1088 ? 0.7883 1.2803 0.8239 0.2744  0.0101  -0.1842 1088 GLN A CB  
8266  C CG  . GLN A 1088 ? 0.8024 1.2896 0.8486 0.2495  0.0030  -0.1993 1088 GLN A CG  
8267  C CD  . GLN A 1088 ? 0.7968 1.2924 0.8666 0.2349  -0.0033 -0.2152 1088 GLN A CD  
8268  O OE1 . GLN A 1088 ? 0.7846 1.2652 0.8541 0.2233  -0.0114 -0.2316 1088 GLN A OE1 
8269  N NE2 . GLN A 1088 ? 0.7794 1.2992 0.8689 0.2353  0.0003  -0.2105 1088 GLN A NE2 
8270  N N   . VAL A 1089 ? 0.9666 1.4424 0.9544 0.3329  0.0270  -0.1562 1089 VAL A N   
8271  C CA  . VAL A 1089 ? 0.9812 1.4662 0.9607 0.3545  0.0367  -0.1459 1089 VAL A CA  
8272  C C   . VAL A 1089 ? 1.0217 1.5148 0.9909 0.3779  0.0469  -0.1305 1089 VAL A C   
8273  O O   . VAL A 1089 ? 1.0050 1.5182 0.9740 0.3950  0.0576  -0.1201 1089 VAL A O   
8274  C CB  . VAL A 1089 ? 0.9099 1.3555 0.8611 0.3644  0.0332  -0.1557 1089 VAL A CB  
8275  C CG1 . VAL A 1089 ? 0.8898 1.3503 0.8374 0.3777  0.0428  -0.1473 1089 VAL A CG1 
8276  C CG2 . VAL A 1089 ? 0.9048 1.3415 0.8676 0.3430  0.0201  -0.1715 1089 VAL A CG2 
8277  N N   . ASN A 1090 ? 1.0703 1.5491 1.0315 0.3782  0.0436  -0.1292 1090 ASN A N   
8278  C CA  . ASN A 1090 ? 1.1428 1.6305 1.0971 0.4013  0.0513  -0.1141 1090 ASN A CA  
8279  C C   . ASN A 1090 ? 1.1409 1.6915 1.1309 0.3989  0.0578  -0.0981 1090 ASN A C   
8280  O O   . ASN A 1090 ? 1.1490 1.7209 1.1399 0.4225  0.0668  -0.0843 1090 ASN A O   
8281  C CB  . ASN A 1090 ? 1.1926 1.6482 1.1284 0.3989  0.0442  -0.1157 1090 ASN A CB  
8282  C CG  . ASN A 1090 ? 1.2450 1.6966 1.1653 0.4292  0.0508  -0.1011 1090 ASN A CG  
8283  O OD1 . ASN A 1090 ? 1.2247 1.7149 1.1608 0.4486  0.0608  -0.0878 1090 ASN A OD1 
8284  N ND2 . ASN A 1090 ? 1.3137 1.7182 1.2018 0.4339  0.0452  -0.1038 1090 ASN A ND2 
8285  N N   . LYS A 1091 ? 1.1461 1.7272 1.1651 0.3699  0.0535  -0.1002 1091 LYS A N   
8286  C CA  . LYS A 1091 ? 1.1507 1.7909 1.2008 0.3625  0.0592  -0.0854 1091 LYS A CA  
8287  C C   . LYS A 1091 ? 1.1037 1.7670 1.1532 0.3834  0.0712  -0.0767 1091 LYS A C   
8288  O O   . LYS A 1091 ? 1.1113 1.8128 1.1724 0.3976  0.0786  -0.0613 1091 LYS A O   
8289  C CB  . LYS A 1091 ? 1.2273 1.8892 1.3016 0.3292  0.0556  -0.0917 1091 LYS A CB  
8290  C CG  . LYS A 1091 ? 1.3114 1.9791 1.3997 0.3024  0.0481  -0.0940 1091 LYS A CG  
8291  C CD  . LYS A 1091 ? 1.3590 2.0714 1.4753 0.2767  0.0511  -0.0890 1091 LYS A CD  
8292  C CE  . LYS A 1091 ? 1.4165 2.1770 1.5437 0.2886  0.0604  -0.0694 1091 LYS A CE  
8293  N NZ  . LYS A 1091 ? 1.4194 2.2273 1.5705 0.2631  0.0614  -0.0581 1091 LYS A NZ  
8294  N N   . TYR A 1092 ? 1.0570 1.6981 1.0929 0.3845  0.0729  -0.0869 1092 TYR A N   
8295  C CA  . TYR A 1092 ? 1.0459 1.7095 1.0803 0.3971  0.0847  -0.0804 1092 TYR A CA  
8296  C C   . TYR A 1092 ? 1.1500 1.7789 1.1522 0.4273  0.0920  -0.0829 1092 TYR A C   
8297  O O   . TYR A 1092 ? 1.1860 1.8367 1.1857 0.4419  0.1047  -0.0760 1092 TYR A O   
8298  C CB  . TYR A 1092 ? 0.9786 1.6449 1.0185 0.3749  0.0824  -0.0878 1092 TYR A CB  
8299  C CG  . TYR A 1092 ? 0.9286 1.6211 0.9955 0.3451  0.0765  -0.0874 1092 TYR A CG  
8300  C CD1 . TYR A 1092 ? 0.9117 1.6560 1.0022 0.3367  0.0816  -0.0728 1092 TYR A CD1 
8301  C CD2 . TYR A 1092 ? 0.9338 1.6004 1.0025 0.3250  0.0659  -0.1020 1092 TYR A CD2 
8302  C CE1 . TYR A 1092 ? 0.9051 1.6703 1.0165 0.3072  0.0771  -0.0728 1092 TYR A CE1 
8303  C CE2 . TYR A 1092 ? 0.9179 1.6062 1.0098 0.2977  0.0623  -0.1029 1092 TYR A CE2 
8304  C CZ  . TYR A 1092 ? 0.9046 1.6400 1.0158 0.2879  0.0682  -0.0883 1092 TYR A CZ  
8305  O OH  . TYR A 1092 ? 0.8837 1.6378 1.0140 0.2587  0.0656  -0.0893 1092 TYR A OH  
8306  N N   . VAL A 1093 ? 1.1831 1.7573 1.1583 0.4350  0.0848  -0.0934 1093 VAL A N   
8307  C CA  . VAL A 1093 ? 1.2116 1.7467 1.1509 0.4635  0.0922  -0.0957 1093 VAL A CA  
8308  C C   . VAL A 1093 ? 1.2039 1.6986 1.1212 0.4764  0.0873  -0.0975 1093 VAL A C   
8309  O O   . VAL A 1093 ? 1.2024 1.6563 1.1045 0.4619  0.0752  -0.1096 1093 VAL A O   
8310  C CB  . VAL A 1093 ? 1.2393 1.7339 1.1526 0.4583  0.0889  -0.1091 1093 VAL A CB  
8311  C CG1 . VAL A 1093 ? 1.3083 1.7602 1.1807 0.4860  0.0978  -0.1114 1093 VAL A CG1 
8312  C CG2 . VAL A 1093 ? 1.2064 1.7349 1.1363 0.4446  0.0927  -0.1068 1093 VAL A CG2 
8313  N N   . GLU A 1094 ? 1.1922 1.6990 1.1074 0.5033  0.0964  -0.0855 1094 GLU A N   
8314  C CA  . GLU A 1094 ? 1.2028 1.6740 1.0976 0.5154  0.0912  -0.0842 1094 GLU A CA  
8315  C C   . GLU A 1094 ? 1.2213 1.6187 1.0689 0.5179  0.0870  -0.0992 1094 GLU A C   
8316  O O   . GLU A 1094 ? 1.2820 1.6573 1.1063 0.5311  0.0952  -0.1040 1094 GLU A O   
8317  C CB  . GLU A 1094 ? 1.2585 1.7494 1.1538 0.5512  0.1033  -0.0694 1094 GLU A CB  
8318  C CG  . GLU A 1094 ? 1.3456 1.8040 1.2217 0.5653  0.0970  -0.0647 1094 GLU A CG  
8319  C CD  . GLU A 1094 ? 1.4331 1.9115 1.3109 0.6062  0.1089  -0.0499 1094 GLU A CD  
8320  O OE1 . GLU A 1094 ? 1.4500 1.9691 1.3442 0.6229  0.1236  -0.0447 1094 GLU A OE1 
8321  O OE2 . GLU A 1094 ? 1.4799 1.9332 1.3419 0.6222  0.1037  -0.0436 1094 GLU A OE2 
8322  N N   . GLN A 1095 ? 1.1904 1.5493 1.0218 0.5020  0.0742  -0.1073 1095 GLN A N   
8323  C CA  . GLN A 1095 ? 1.2398 1.5294 1.0234 0.5026  0.0702  -0.1213 1095 GLN A CA  
8324  C C   . GLN A 1095 ? 1.3540 1.5988 1.1005 0.5248  0.0723  -0.1170 1095 GLN A C   
8325  O O   . GLN A 1095 ? 1.3665 1.6345 1.1293 0.5319  0.0718  -0.1052 1095 GLN A O   
8326  C CB  . GLN A 1095 ? 1.2087 1.4833 0.9954 0.4672  0.0550  -0.1363 1095 GLN A CB  
8327  C CG  . GLN A 1095 ? 1.2219 1.5431 1.0488 0.4466  0.0522  -0.1393 1095 GLN A CG  
8328  C CD  . GLN A 1095 ? 1.5991 1.9109 1.4125 0.4554  0.0574  -0.1435 1095 GLN A CD  
8329  O OE1 . GLN A 1095 ? 1.6275 1.8939 1.4096 0.4514  0.0514  -0.1554 1095 GLN A OE1 
8330  N NE2 . GLN A 1095 ? 1.5720 1.9275 1.4080 0.4641  0.0679  -0.1337 1095 GLN A NE2 
8331  N N   . ASN A 1096 ? 1.4505 1.6300 1.1450 0.5368  0.0748  -0.1257 1096 ASN A N   
8332  C CA  . ASN A 1096 ? 1.5579 1.6837 1.2069 0.5629  0.0793  -0.1220 1096 ASN A CA  
8333  C C   . ASN A 1096 ? 1.5808 1.6889 1.2237 0.5469  0.0665  -0.1211 1096 ASN A C   
8334  O O   . ASN A 1096 ? 1.5758 1.6629 1.2105 0.5147  0.0541  -0.1333 1096 ASN A O   
8335  C CB  . ASN A 1096 ? 1.6607 1.7139 1.2509 0.5676  0.0821  -0.1349 1096 ASN A CB  
8336  C CG  . ASN A 1096 ? 1.7840 1.7645 1.3154 0.5867  0.0841  -0.1348 1096 ASN A CG  
8337  O OD1 . ASN A 1096 ? 1.8659 1.8091 1.3599 0.6177  0.0978  -0.1335 1096 ASN A OD1 
8338  N ND2 . ASN A 1096 ? 1.7991 1.7548 1.3177 0.5672  0.0711  -0.1373 1096 ASN A ND2 
8339  N N   . GLN A 1097 ? 1.6181 1.7351 1.2645 0.5681  0.0687  -0.1069 1097 GLN A N   
8340  C CA  . GLN A 1097 ? 1.6512 1.7539 1.2926 0.5479  0.0551  -0.1057 1097 GLN A CA  
8341  C C   . GLN A 1097 ? 1.7372 1.7542 1.3148 0.5369  0.0482  -0.1187 1097 GLN A C   
8342  O O   . GLN A 1097 ? 1.7161 1.7213 1.2907 0.4998  0.0368  -0.1311 1097 GLN A O   
8343  C CB  . GLN A 1097 ? 1.6373 1.7637 1.2923 0.5727  0.0563  -0.0867 1097 GLN A CB  
8344  C CG  . GLN A 1097 ? 1.6172 1.7433 1.2770 0.5454  0.0413  -0.0840 1097 GLN A CG  
8345  C CD  . GLN A 1097 ? 1.6434 1.7772 1.3037 0.5718  0.0394  -0.0648 1097 GLN A CD  
8346  O OE1 . GLN A 1097 ? 1.6467 1.7966 1.3124 0.6126  0.0499  -0.0528 1097 GLN A OE1 
8347  N NE2 . GLN A 1097 ? 1.6477 1.7709 1.3026 0.5484  0.0258  -0.0620 1097 GLN A NE2 
8348  N N   . ASN A 1098 ? 1.8812 1.8391 1.4070 0.5690  0.0562  -0.1163 1098 ASN A N   
8349  C CA  . ASN A 1098 ? 1.9797 1.8471 1.4341 0.5616  0.0517  -0.1278 1098 ASN A CA  
8350  C C   . ASN A 1098 ? 1.7920 1.6389 1.2331 0.5220  0.0434  -0.1474 1098 ASN A C   
8351  O O   . ASN A 1098 ? 1.7927 1.5986 1.2028 0.4932  0.0323  -0.1568 1098 ASN A O   
8352  C CB  . ASN A 1098 ? 2.0848 1.8967 1.4884 0.6049  0.0661  -0.1243 1098 ASN A CB  
8353  C CG  . ASN A 1098 ? 2.2113 1.9241 1.5341 0.5969  0.0632  -0.1365 1098 ASN A CG  
8354  O OD1 . ASN A 1098 ? 2.2609 1.9383 1.5515 0.5941  0.0685  -0.1478 1098 ASN A OD1 
8355  N ND2 . ASN A 1098 ? 2.2750 1.9405 1.5612 0.5912  0.0542  -0.1339 1098 ASN A ND2 
8356  N N   . SER A 1099 ? 1.7606 1.6366 1.2243 0.5199  0.0482  -0.1534 1099 SER A N   
8357  C CA  . SER A 1099 ? 1.7068 1.5804 1.1723 0.4833  0.0383  -0.1701 1099 SER A CA  
8358  C C   . SER A 1099 ? 1.6191 1.5304 1.1228 0.4472  0.0251  -0.1738 1099 SER A C   
8359  O O   . SER A 1099 ? 1.6601 1.5340 1.1348 0.4202  0.0152  -0.1844 1099 SER A O   
8360  C CB  . SER A 1099 ? 1.6482 1.5637 1.1464 0.4871  0.0436  -0.1722 1099 SER A CB  
8361  O OG  . SER A 1099 ? 1.5946 1.5314 1.1165 0.4514  0.0311  -0.1852 1099 SER A OG  
8362  N N   . ILE A 1100 ? 1.4857 1.4702 1.0520 0.4460  0.0260  -0.1652 1100 ILE A N   
8363  C CA  . ILE A 1100 ? 1.3730 1.3987 0.9802 0.4107  0.0155  -0.1699 1100 ILE A CA  
8364  C C   . ILE A 1100 ? 1.4241 1.4134 1.0020 0.3940  0.0076  -0.1709 1100 ILE A C   
8365  O O   . ILE A 1100 ? 1.4072 1.4048 0.9966 0.3575  -0.0018 -0.1822 1100 ILE A O   
8366  C CB  . ILE A 1100 ? 1.2183 1.3215 0.8890 0.4144  0.0192  -0.1577 1100 ILE A CB  
8367  C CG1 . ILE A 1100 ? 1.1189 1.2614 0.8227 0.4143  0.0228  -0.1614 1100 ILE A CG1 
8368  C CG2 . ILE A 1100 ? 1.1734 1.3067 0.8749 0.3801  0.0099  -0.1613 1100 ILE A CG2 
8369  C CD1 . ILE A 1100 ? 1.0744 1.2295 0.7984 0.3794  0.0124  -0.1775 1100 ILE A CD1 
8370  N N   . CYS A 1101 ? 1.4755 1.4243 1.0150 0.4206  0.0117  -0.1594 1101 CYS A N   
8371  C CA  . CYS A 1101 ? 1.5167 1.4214 1.0191 0.4065  0.0037  -0.1590 1101 CYS A CA  
8372  C C   . CYS A 1101 ? 1.5427 1.3871 0.9950 0.3776  -0.0031 -0.1779 1101 CYS A C   
8373  O O   . CYS A 1101 ? 1.5223 1.3703 0.9791 0.3391  -0.0123 -0.1885 1101 CYS A O   
8374  C CB  . CYS A 1101 ? 1.5823 1.4454 1.0457 0.4459  0.0090  -0.1433 1101 CYS A CB  
8375  S SG  . CYS A 1101 ? 1.8662 1.7924 1.3792 0.4668  0.0096  -0.1197 1101 CYS A SG  
8376  N N   . ASN A 1102 ? 1.5875 1.3786 0.9919 0.3951  0.0022  -0.1826 1102 ASN A N   
8377  C CA  . ASN A 1102 ? 1.6221 1.3518 0.9717 0.3694  -0.0037 -0.1997 1102 ASN A CA  
8378  C C   . ASN A 1102 ? 1.5697 1.3388 0.9548 0.3319  -0.0117 -0.2165 1102 ASN A C   
8379  O O   . ASN A 1102 ? 1.5839 1.3241 0.9412 0.2974  -0.0203 -0.2310 1102 ASN A O   
8380  C CB  . ASN A 1102 ? 1.6703 1.3394 0.9641 0.3979  0.0051  -0.1999 1102 ASN A CB  
8381  C CG  . ASN A 1102 ? 1.7273 1.3365 0.9684 0.4305  0.0115  -0.1876 1102 ASN A CG  
8382  O OD1 . ASN A 1102 ? 1.7677 1.3498 0.9860 0.4200  0.0050  -0.1842 1102 ASN A OD1 
8383  N ND2 . ASN A 1102 ? 1.7275 1.3139 0.9476 0.4708  0.0246  -0.1809 1102 ASN A ND2 
8384  N N   . SER A 1103 ? 1.5208 1.3552 0.9656 0.3390  -0.0090 -0.2148 1103 SER A N   
8385  C CA  . SER A 1103 ? 1.4670 1.3457 0.9535 0.3074  -0.0172 -0.2294 1103 SER A CA  
8386  C C   . SER A 1103 ? 1.4540 1.3605 0.9673 0.2741  -0.0243 -0.2344 1103 SER A C   
8387  O O   . SER A 1103 ? 1.4440 1.3486 0.9553 0.2396  -0.0326 -0.2509 1103 SER A O   
8388  C CB  . SER A 1103 ? 1.4038 1.3457 0.9486 0.3223  -0.0130 -0.2244 1103 SER A CB  
8389  O OG  . SER A 1103 ? 1.4264 1.3460 0.9478 0.3531  -0.0047 -0.2190 1103 SER A OG  
8390  N N   . LEU A 1104 ? 1.4562 1.3889 0.9932 0.2841  -0.0207 -0.2202 1104 LEU A N   
8391  C CA  . LEU A 1104 ? 1.4458 1.4006 1.0031 0.2540  -0.0260 -0.2225 1104 LEU A CA  
8392  C C   . LEU A 1104 ? 1.5617 1.4505 1.0566 0.2323  -0.0317 -0.2299 1104 LEU A C   
8393  O O   . LEU A 1104 ? 1.5592 1.4522 1.0565 0.1930  -0.0381 -0.2455 1104 LEU A O   
8394  C CB  . LEU A 1104 ? 1.3887 1.3778 0.9750 0.2727  -0.0216 -0.2028 1104 LEU A CB  
8395  C CG  . LEU A 1104 ? 1.2928 1.3614 0.9508 0.2734  -0.0182 -0.1971 1104 LEU A CG  
8396  C CD1 . LEU A 1104 ? 1.2706 1.3643 0.9451 0.2936  -0.0144 -0.1757 1104 LEU A CD1 
8397  C CD2 . LEU A 1104 ? 1.2232 1.3274 0.9169 0.2319  -0.0237 -0.2123 1104 LEU A CD2 
8398  N N   . LEU A 1105 ? 1.6554 1.4827 1.0933 0.2586  -0.0287 -0.2189 1105 LEU A N   
8399  C CA  . LEU A 1105 ? 1.7497 1.5001 1.1151 0.2437  -0.0334 -0.2230 1105 LEU A CA  
8400  C C   . LEU A 1105 ? 1.7892 1.5017 1.1162 0.2135  -0.0383 -0.2435 1105 LEU A C   
8401  O O   . LEU A 1105 ? 1.8618 1.5127 1.1279 0.1917  -0.0428 -0.2504 1105 LEU A O   
8402  C CB  . LEU A 1105 ? 1.8107 1.5004 1.1224 0.2860  -0.0278 -0.2070 1105 LEU A CB  
8403  C CG  . LEU A 1105 ? 1.8206 1.5247 1.1463 0.3102  -0.0268 -0.1863 1105 LEU A CG  
8404  C CD1 . LEU A 1105 ? 1.8587 1.5521 1.1764 0.3650  -0.0169 -0.1697 1105 LEU A CD1 
8405  C CD2 . LEU A 1105 ? 1.8807 1.5273 1.1528 0.2903  -0.0351 -0.1849 1105 LEU A CD2 
8406  N N   . TRP A 1106 ? 1.7498 1.4985 1.1102 0.2115  -0.0381 -0.2529 1106 TRP A N   
8407  C CA  . TRP A 1106 ? 1.7875 1.5092 1.1175 0.1834  -0.0441 -0.2717 1106 TRP A CA  
8408  C C   . TRP A 1106 ? 1.7432 1.5077 1.1085 0.1372  -0.0516 -0.2880 1106 TRP A C   
8409  O O   . TRP A 1106 ? 1.7895 1.5175 1.1128 0.1031  -0.0571 -0.3015 1106 TRP A O   
8410  C CB  . TRP A 1106 ? 1.7742 1.5172 1.1253 0.2016  -0.0424 -0.2739 1106 TRP A CB  
8411  C CG  . TRP A 1106 ? 1.7817 1.5051 1.1074 0.1739  -0.0503 -0.2920 1106 TRP A CG  
8412  C CD1 . TRP A 1106 ? 1.8331 1.4829 1.0845 0.1718  -0.0510 -0.2967 1106 TRP A CD1 
8413  C CD2 . TRP A 1106 ? 1.7446 1.5245 1.1199 0.1446  -0.0589 -0.3077 1106 TRP A CD2 
8414  N NE1 . TRP A 1106 ? 1.8298 1.4888 1.0811 0.1409  -0.0604 -0.3137 1106 TRP A NE1 
8415  C CE2 . TRP A 1106 ? 1.7823 1.5228 1.1114 0.1251  -0.0658 -0.3208 1106 TRP A CE2 
8416  C CE3 . TRP A 1106 ? 1.7011 1.5607 1.1548 0.1336  -0.0614 -0.3119 1106 TRP A CE3 
8417  C CZ2 . TRP A 1106 ? 1.7893 1.5722 1.1516 0.0962  -0.0763 -0.3375 1106 TRP A CZ2 
8418  C CZ3 . TRP A 1106 ? 1.6844 1.5824 1.1701 0.1070  -0.0707 -0.3292 1106 TRP A CZ3 
8419  C CH2 . TRP A 1106 ? 1.7272 1.5895 1.1693 0.0890  -0.0787 -0.3416 1106 TRP A CH2 
8420  N N   . LEU A 1107 ? 1.6794 1.5213 1.1209 0.1353  -0.0509 -0.2874 1107 LEU A N   
8421  C CA  . LEU A 1107 ? 1.6533 1.5421 1.1352 0.0942  -0.0560 -0.3043 1107 LEU A CA  
8422  C C   . LEU A 1107 ? 1.7611 1.6192 1.2089 0.0660  -0.0573 -0.3064 1107 LEU A C   
8423  O O   . LEU A 1107 ? 1.7997 1.6425 1.2242 0.0273  -0.0621 -0.3236 1107 LEU A O   
8424  C CB  . LEU A 1107 ? 1.5208 1.4902 1.0845 0.0996  -0.0532 -0.3011 1107 LEU A CB  
8425  C CG  . LEU A 1107 ? 1.4295 1.4418 1.0387 0.1198  -0.0532 -0.3014 1107 LEU A CG  
8426  C CD1 . LEU A 1107 ? 1.4163 1.4326 1.0333 0.1610  -0.0455 -0.2803 1107 LEU A CD1 
8427  C CD2 . LEU A 1107 ? 1.3425 1.4255 1.0213 0.0995  -0.0549 -0.3124 1107 LEU A CD2 
8428  N N   . VAL A 1108 ? 1.8039 1.6533 1.2474 0.0853  -0.0533 -0.2884 1108 VAL A N   
8429  C CA  . VAL A 1108 ? 1.8441 1.6756 1.2666 0.0596  -0.0551 -0.2875 1108 VAL A CA  
8430  C C   . VAL A 1108 ? 1.9675 1.7116 1.3018 0.0445  -0.0590 -0.2911 1108 VAL A C   
8431  O O   . VAL A 1108 ? 2.0049 1.7345 1.3177 0.0050  -0.0623 -0.3012 1108 VAL A O   
8432  C CB  . VAL A 1108 ? 1.8163 1.6672 1.2615 0.0851  -0.0517 -0.2657 1108 VAL A CB  
8433  C CG1 . VAL A 1108 ? 1.8337 1.6634 1.2645 0.1364  -0.0475 -0.2473 1108 VAL A CG1 
8434  C CG2 . VAL A 1108 ? 1.8666 1.6748 1.2672 0.0646  -0.0556 -0.2613 1108 VAL A CG2 
8435  N N   . GLU A 1109 ? 2.0395 1.7225 1.3191 0.0737  -0.0579 -0.2838 1109 GLU A N   
8436  C CA  . GLU A 1109 ? 2.1597 1.7506 1.3473 0.0599  -0.0612 -0.2869 1109 GLU A CA  
8437  C C   . GLU A 1109 ? 2.1999 1.7704 1.3561 0.0194  -0.0656 -0.3099 1109 GLU A C   
8438  O O   . GLU A 1109 ? 2.2753 1.7831 1.3634 -0.0101 -0.0692 -0.3172 1109 GLU A O   
8439  C CB  . GLU A 1109 ? 2.2244 1.7485 1.3571 0.1070  -0.0571 -0.2702 1109 GLU A CB  
8440  C CG  . GLU A 1109 ? 2.2067 1.7459 1.3624 0.1467  -0.0537 -0.2470 1109 GLU A CG  
8441  C CD  . GLU A 1109 ? 2.2622 1.7309 1.3589 0.1925  -0.0491 -0.2319 1109 GLU A CD  
8442  O OE1 . GLU A 1109 ? 2.2258 1.7257 1.3579 0.2367  -0.0426 -0.2166 1109 GLU A OE1 
8443  O OE2 . GLU A 1109 ? 2.3416 1.7231 1.3549 0.1838  -0.0515 -0.2359 1109 GLU A OE2 
8444  N N   . ASN A 1110 ? 2.1531 1.7759 1.3571 0.0174  -0.0661 -0.3207 1110 ASN A N   
8445  C CA  . ASN A 1110 ? 2.1737 1.7841 1.3525 -0.0181 -0.0715 -0.3414 1110 ASN A CA  
8446  C C   . ASN A 1110 ? 2.0963 1.7868 1.3425 -0.0565 -0.0751 -0.3604 1110 ASN A C   
8447  O O   . ASN A 1110 ? 2.1267 1.8106 1.3509 -0.0982 -0.0800 -0.3791 1110 ASN A O   
8448  C CB  . ASN A 1110 ? 2.1991 1.7915 1.3629 0.0086  -0.0713 -0.3400 1110 ASN A CB  
8449  C CG  . ASN A 1110 ? 2.2775 1.7916 1.3758 0.0490  -0.0654 -0.3227 1110 ASN A CG  
8450  O OD1 . ASN A 1110 ? 2.2615 1.7934 1.3883 0.0928  -0.0592 -0.3077 1110 ASN A OD1 
8451  N ND2 . ASN A 1110 ? 2.3707 1.7970 1.3796 0.0342  -0.0667 -0.3253 1110 ASN A ND2 
8452  N N   . TYR A 1111 ? 2.0114 1.7777 1.3387 -0.0431 -0.0722 -0.3560 1111 TYR A N   
8453  C CA  . TYR A 1111 ? 1.9449 1.7905 1.3430 -0.0682 -0.0747 -0.3736 1111 TYR A CA  
8454  C C   . TYR A 1111 ? 1.9090 1.8101 1.3616 -0.0871 -0.0707 -0.3766 1111 TYR A C   
8455  O O   . TYR A 1111 ? 1.8273 1.8012 1.3539 -0.0864 -0.0694 -0.3826 1111 TYR A O   
8456  C CB  . TYR A 1111 ? 1.8859 1.7739 1.3331 -0.0362 -0.0758 -0.3700 1111 TYR A CB  
8457  C CG  . TYR A 1111 ? 1.9341 1.7764 1.3314 -0.0320 -0.0813 -0.3741 1111 TYR A CG  
8458  C CD1 . TYR A 1111 ? 1.9381 1.8072 1.3488 -0.0598 -0.0896 -0.3932 1111 TYR A CD1 
8459  C CD2 . TYR A 1111 ? 1.9796 1.7517 1.3146 -0.0014 -0.0781 -0.3593 1111 TYR A CD2 
8460  C CE1 . TYR A 1111 ? 1.9915 1.8186 1.3537 -0.0599 -0.0957 -0.3968 1111 TYR A CE1 
8461  C CE2 . TYR A 1111 ? 2.0352 1.7613 1.3195 -0.0004 -0.0823 -0.3637 1111 TYR A CE2 
8462  C CZ  . TYR A 1111 ? 2.0441 1.7977 1.3413 -0.0313 -0.0917 -0.3823 1111 TYR A CZ  
8463  O OH  . TYR A 1111 ? 2.1033 1.8136 1.3497 -0.0345 -0.0972 -0.3869 1111 TYR A OH  
8464  N N   . GLN A 1112 ? 1.9606 1.8225 1.3718 -0.1050 -0.0688 -0.3726 1112 GLN A N   
8465  C CA  . GLN A 1112 ? 1.9391 1.8423 1.3881 -0.1302 -0.0649 -0.3766 1112 GLN A CA  
8466  C C   . GLN A 1112 ? 2.0472 1.9117 1.4426 -0.1796 -0.0666 -0.3917 1112 GLN A C   
8467  O O   . GLN A 1112 ? 2.1297 1.9177 1.4489 -0.1820 -0.0688 -0.3833 1112 GLN A O   
8468  C CB  . GLN A 1112 ? 1.8984 1.7919 1.3488 -0.1018 -0.0613 -0.3528 1112 GLN A CB  
8469  C CG  . GLN A 1112 ? 1.8313 1.7591 1.3115 -0.1295 -0.0576 -0.3548 1112 GLN A CG  
8470  C CD  . GLN A 1112 ? 1.7859 1.7189 1.2803 -0.0983 -0.0555 -0.3299 1112 GLN A CD  
8471  O OE1 . GLN A 1112 ? 1.8290 1.7088 1.2766 -0.0693 -0.0580 -0.3113 1112 GLN A OE1 
8472  N NE2 . GLN A 1112 ? 1.6993 1.6974 1.2582 -0.1041 -0.0506 -0.3297 1112 GLN A NE2 
8473  N N   . LEU A 1113 ? 2.0502 1.9674 1.4846 -0.2190 -0.0654 -0.4144 1113 LEU A N   
8474  C CA  . LEU A 1113 ? 2.1221 2.0129 1.5112 -0.2718 -0.0660 -0.4326 1113 LEU A CA  
8475  C C   . LEU A 1113 ? 2.1757 2.0339 1.5318 -0.2906 -0.0627 -0.4249 1113 LEU A C   
8476  O O   . LEU A 1113 ? 2.1362 2.0113 1.5219 -0.2666 -0.0598 -0.4082 1113 LEU A O   
8477  C CB  . LEU A 1113 ? 2.0480 2.0161 1.4988 -0.3060 -0.0639 -0.4592 1113 LEU A CB  
8478  C CG  . LEU A 1113 ? 1.9916 1.9921 1.4719 -0.2926 -0.0699 -0.4683 1113 LEU A CG  
8479  C CD1 . LEU A 1113 ? 1.9092 2.0058 1.4836 -0.2979 -0.0671 -0.4840 1113 LEU A CD1 
8480  C CD2 . LEU A 1113 ? 2.0523 2.0102 1.4692 -0.3265 -0.0760 -0.4828 1113 LEU A CD2 
8481  N N   . ASP A 1114 ? 2.2787 2.0888 1.5705 -0.3354 -0.0641 -0.4370 1114 ASP A N   
8482  C CA  . ASP A 1114 ? 2.3487 2.1192 1.5980 -0.3604 -0.0626 -0.4315 1114 ASP A CA  
8483  C C   . ASP A 1114 ? 2.2629 2.1055 1.5779 -0.3877 -0.0546 -0.4426 1114 ASP A C   
8484  O O   . ASP A 1114 ? 2.2996 2.1244 1.5839 -0.4311 -0.0519 -0.4511 1114 ASP A O   
8485  C CB  . ASP A 1114 ? 2.4947 2.1909 1.6521 -0.4046 -0.0661 -0.4430 1114 ASP A CB  
8486  C CG  . ASP A 1114 ? 2.6366 2.2302 1.7035 -0.3782 -0.0729 -0.4225 1114 ASP A CG  
8487  O OD1 . ASP A 1114 ? 2.6420 2.2177 1.7101 -0.3376 -0.0743 -0.3984 1114 ASP A OD1 
8488  O OD2 . ASP A 1114 ? 2.7332 2.2647 1.7273 -0.3982 -0.0767 -0.4308 1114 ASP A OD2 
8489  N N   . ASN A 1115 ? 2.1518 2.0724 1.5538 -0.3629 -0.0503 -0.4428 1115 ASN A N   
8490  C CA  . ASN A 1115 ? 2.0532 2.0400 1.5202 -0.3790 -0.0416 -0.4496 1115 ASN A CA  
8491  C C   . ASN A 1115 ? 1.9125 1.9336 1.4334 -0.3303 -0.0404 -0.4285 1115 ASN A C   
8492  O O   . ASN A 1115 ? 1.8365 1.9033 1.4055 -0.3353 -0.0336 -0.4275 1115 ASN A O   
8493  C CB  . ASN A 1115 ? 2.0401 2.0993 1.5653 -0.4102 -0.0353 -0.4795 1115 ASN A CB  
8494  C CG  . ASN A 1115 ? 2.0049 2.1090 1.5823 -0.3768 -0.0388 -0.4828 1115 ASN A CG  
8495  O OD1 . ASN A 1115 ? 1.9723 2.1369 1.6004 -0.3942 -0.0360 -0.5051 1115 ASN A OD1 
8496  N ND2 . ASN A 1115 ? 2.0085 2.0838 1.5736 -0.3288 -0.0451 -0.4608 1115 ASN A ND2 
8497  N N   . GLY A 1116 ? 1.8917 1.8879 1.4002 -0.2847 -0.0465 -0.4118 1116 GLY A N   
8498  C CA  . GLY A 1116 ? 1.7945 1.8228 1.3509 -0.2382 -0.0453 -0.3921 1116 GLY A CA  
8499  C C   . GLY A 1116 ? 1.6791 1.7681 1.3017 -0.2164 -0.0439 -0.3999 1116 GLY A C   
8500  O O   . GLY A 1116 ? 1.6409 1.7513 1.2967 -0.1769 -0.0433 -0.3838 1116 GLY A O   
8501  N N   . SER A 1117 ? 1.6060 1.7241 1.2479 -0.2420 -0.0439 -0.4243 1117 SER A N   
8502  C CA  . SER A 1117 ? 1.5444 1.7161 1.2455 -0.2202 -0.0452 -0.4314 1117 SER A CA  
8503  C C   . SER A 1117 ? 1.5924 1.7232 1.2567 -0.1903 -0.0537 -0.4228 1117 SER A C   
8504  O O   . SER A 1117 ? 1.6801 1.7429 1.2724 -0.1946 -0.0576 -0.4174 1117 SER A O   
8505  C CB  . SER A 1117 ? 1.5142 1.7407 1.2574 -0.2563 -0.0428 -0.4606 1117 SER A CB  
8506  O OG  . SER A 1117 ? 1.5622 1.7592 1.2595 -0.2840 -0.0485 -0.4756 1117 SER A OG  
8507  N N   . PHE A 1118 ? 1.5244 1.6916 1.2334 -0.1605 -0.0563 -0.4213 1118 PHE A N   
8508  C CA  . PHE A 1118 ? 1.5279 1.6571 1.2031 -0.1306 -0.0633 -0.4120 1118 PHE A CA  
8509  C C   . PHE A 1118 ? 1.5150 1.6614 1.1976 -0.1445 -0.0711 -0.4311 1118 PHE A C   
8510  O O   . PHE A 1118 ? 1.4686 1.6788 1.2136 -0.1514 -0.0718 -0.4450 1118 PHE A O   
8511  C CB  . PHE A 1118 ? 1.4889 1.6378 1.1992 -0.0842 -0.0614 -0.3928 1118 PHE A CB  
8512  C CG  . PHE A 1118 ? 1.5195 1.6294 1.1977 -0.0605 -0.0572 -0.3691 1118 PHE A CG  
8513  C CD1 . PHE A 1118 ? 1.5223 1.6257 1.1913 -0.0796 -0.0528 -0.3652 1118 PHE A CD1 
8514  C CD2 . PHE A 1118 ? 1.5456 1.6263 1.2027 -0.0191 -0.0577 -0.3508 1118 PHE A CD2 
8515  C CE1 . PHE A 1118 ? 1.5370 1.6074 1.1782 -0.0563 -0.0508 -0.3424 1118 PHE A CE1 
8516  C CE2 . PHE A 1118 ? 1.5553 1.6058 1.1869 0.0048  -0.0539 -0.3292 1118 PHE A CE2 
8517  C CZ  . PHE A 1118 ? 1.5480 1.5943 1.1727 -0.0131 -0.0514 -0.3246 1118 PHE A CZ  
8518  N N   . LYS A 1119 ? 1.5740 1.6634 1.1921 -0.1488 -0.0774 -0.4318 1119 LYS A N   
8519  C CA  . LYS A 1119 ? 1.5738 1.6799 1.1967 -0.1615 -0.0865 -0.4480 1119 LYS A CA  
8520  C C   . LYS A 1119 ? 1.5464 1.6539 1.1820 -0.1205 -0.0920 -0.4366 1119 LYS A C   
8521  O O   . LYS A 1119 ? 1.5619 1.6255 1.1654 -0.0876 -0.0891 -0.4170 1119 LYS A O   
8522  C CB  . LYS A 1119 ? 1.7674 1.8141 1.3124 -0.1950 -0.0912 -0.4578 1119 LYS A CB  
8523  C CG  . LYS A 1119 ? 1.9417 1.8932 1.3971 -0.1834 -0.0891 -0.4408 1119 LYS A CG  
8524  C CD  . LYS A 1119 ? 2.3806 2.2690 1.7549 -0.2128 -0.0954 -0.4508 1119 LYS A CD  
8525  C CE  . LYS A 1119 ? 2.4231 2.2697 1.7405 -0.2585 -0.0926 -0.4602 1119 LYS A CE  
8526  N NZ  . LYS A 1119 ? 2.4818 2.2331 1.7141 -0.2453 -0.0898 -0.4429 1119 LYS A NZ  
8527  N N   . GLU A 1120 ? 1.5483 1.7072 1.2311 -0.1217 -0.0999 -0.4487 1120 GLU A N   
8528  C CA  . GLU A 1120 ? 1.5794 1.7293 1.2606 -0.0881 -0.1071 -0.4390 1120 GLU A CA  
8529  C C   . GLU A 1120 ? 1.6880 1.7806 1.2978 -0.1027 -0.1149 -0.4432 1120 GLU A C   
8530  O O   . GLU A 1120 ? 1.7268 1.8186 1.3168 -0.1426 -0.1186 -0.4601 1120 GLU A O   
8531  C CB  . GLU A 1120 ? 1.5319 1.7550 1.2896 -0.0793 -0.1143 -0.4476 1120 GLU A CB  
8532  C CG  . GLU A 1120 ? 1.5550 1.7689 1.3079 -0.0509 -0.1248 -0.4402 1120 GLU A CG  
8533  C CD  . GLU A 1120 ? 1.5535 1.7204 1.2739 -0.0112 -0.1188 -0.4168 1120 GLU A CD  
8534  O OE1 . GLU A 1120 ? 1.4985 1.6947 1.2618 0.0174  -0.1162 -0.4067 1120 GLU A OE1 
8535  O OE2 . GLU A 1120 ? 1.6041 1.7040 1.2545 -0.0088 -0.1162 -0.4091 1120 GLU A OE2 
8536  N N   . ASN A 1121 ? 1.7194 1.7626 1.2878 -0.0720 -0.1162 -0.4282 1121 ASN A N   
8537  C CA  . ASN A 1121 ? 1.8040 1.7821 1.2960 -0.0813 -0.1221 -0.4296 1121 ASN A CA  
8538  C C   . ASN A 1121 ? 1.8439 1.8505 1.3521 -0.0898 -0.1368 -0.4406 1121 ASN A C   
8539  O O   . ASN A 1121 ? 1.8653 1.8797 1.3601 -0.1275 -0.1449 -0.4574 1121 ASN A O   
8540  C CB  . ASN A 1121 ? 1.8098 1.7215 1.2499 -0.0426 -0.1150 -0.4086 1121 ASN A CB  
8541  C CG  . ASN A 1121 ? 1.8398 1.6798 1.1992 -0.0477 -0.1196 -0.4092 1121 ASN A CG  
8542  O OD1 . ASN A 1121 ? 1.8880 1.6822 1.1885 -0.0792 -0.1206 -0.4176 1121 ASN A OD1 
8543  N ND2 . ASN A 1121 ? 1.8066 1.6328 1.1584 -0.0184 -0.1219 -0.4003 1121 ASN A ND2 
8544  N N   . SER A 1122 ? 1.8426 1.8653 1.3784 -0.0557 -0.1406 -0.4308 1122 SER A N   
8545  C CA  . SER A 1122 ? 1.8685 1.9155 1.4190 -0.0586 -0.1563 -0.4381 1122 SER A CA  
8546  C C   . SER A 1122 ? 1.8576 1.9897 1.4846 -0.0797 -0.1652 -0.4556 1122 SER A C   
8547  O O   . SER A 1122 ? 1.8405 2.0116 1.5084 -0.0922 -0.1576 -0.4626 1122 SER A O   
8548  C CB  . SER A 1122 ? 1.8110 1.8575 1.3772 -0.0166 -0.1573 -0.4227 1122 SER A CB  
8549  O OG  . SER A 1122 ? 1.7197 1.8362 1.3676 -0.0021 -0.1576 -0.4228 1122 SER A OG  
8550  N N   . GLN A 1123 ? 1.8965 2.0580 1.5431 -0.0826 -0.1816 -0.4625 1123 GLN A N   
8551  C CA  . GLN A 1123 ? 1.8839 2.1282 1.6035 -0.1005 -0.1918 -0.4801 1123 GLN A CA  
8552  C C   . GLN A 1123 ? 1.7341 2.0359 1.5327 -0.0690 -0.1914 -0.4754 1123 GLN A C   
8553  O O   . GLN A 1123 ? 1.6942 2.0662 1.5599 -0.0781 -0.1971 -0.4894 1123 GLN A O   
8554  C CB  . GLN A 1123 ? 2.0267 2.2813 1.7336 -0.1201 -0.2118 -0.4903 1123 GLN A CB  
8555  C CG  . GLN A 1123 ? 2.2103 2.4061 1.8344 -0.1557 -0.2123 -0.4960 1123 GLN A CG  
8556  C CD  . GLN A 1123 ? 2.3397 2.5659 1.9639 -0.1872 -0.2317 -0.5111 1123 GLN A CD  
8557  O OE1 . GLN A 1123 ? 2.3356 2.6408 2.0262 -0.2042 -0.2396 -0.5272 1123 GLN A OE1 
8558  N NE2 . GLN A 1123 ? 2.4547 2.6186 2.0032 -0.1963 -0.2391 -0.5065 1123 GLN A NE2 
8559  N N   . TYR A 1124 ? 1.6404 1.9123 1.4300 -0.0325 -0.1839 -0.4562 1124 TYR A N   
8560  C CA  . TYR A 1124 ? 1.4900 1.8072 1.3441 -0.0025 -0.1848 -0.4502 1124 TYR A CA  
8561  C C   . TYR A 1124 ? 1.4102 1.7908 1.3323 -0.0133 -0.1781 -0.4623 1124 TYR A C   
8562  O O   . TYR A 1124 ? 1.3842 1.7567 1.3020 -0.0208 -0.1626 -0.4607 1124 TYR A O   
8563  C CB  . TYR A 1124 ? 1.4228 1.7001 1.2551 0.0316  -0.1724 -0.4288 1124 TYR A CB  
8564  C CG  . TYR A 1124 ? 1.3073 1.6230 1.1960 0.0613  -0.1731 -0.4211 1124 TYR A CG  
8565  C CD1 . TYR A 1124 ? 1.2866 1.6019 1.1788 0.0816  -0.1867 -0.4154 1124 TYR A CD1 
8566  C CD2 . TYR A 1124 ? 1.2333 1.5810 1.1664 0.0675  -0.1604 -0.4192 1124 TYR A CD2 
8567  C CE1 . TYR A 1124 ? 1.2148 1.5592 1.1525 0.1076  -0.1876 -0.4081 1124 TYR A CE1 
8568  C CE2 . TYR A 1124 ? 1.1584 1.5362 1.1373 0.0927  -0.1604 -0.4121 1124 TYR A CE2 
8569  C CZ  . TYR A 1124 ? 1.1239 1.4988 1.1041 0.1129  -0.1739 -0.4066 1124 TYR A CZ  
8570  O OH  . TYR A 1124 ? 1.0220 1.4206 1.0412 0.1363  -0.1739 -0.3995 1124 TYR A OH  
8571  N N   . GLN A 1125 ? 1.3634 1.8060 1.3469 -0.0139 -0.1902 -0.4745 1125 GLN A N   
8572  C CA  . GLN A 1125 ? 1.2966 1.8016 1.3501 -0.0184 -0.1833 -0.4862 1125 GLN A CA  
8573  C C   . GLN A 1125 ? 1.1763 1.6898 1.2627 0.0181  -0.1799 -0.4724 1125 GLN A C   
8574  O O   . GLN A 1125 ? 1.1158 1.6378 1.2173 0.0396  -0.1940 -0.4680 1125 GLN A O   
8575  C CB  . GLN A 1125 ? 1.3812 1.9500 1.4857 -0.0338 -0.1983 -0.5066 1125 GLN A CB  
8576  C CG  . GLN A 1125 ? 1.5071 2.0809 1.5878 -0.0760 -0.2010 -0.5236 1125 GLN A CG  
8577  C CD  . GLN A 1125 ? 1.5776 2.1641 1.6662 -0.1038 -0.1823 -0.5347 1125 GLN A CD  
8578  O OE1 . GLN A 1125 ? 1.5934 2.1465 1.6625 -0.0956 -0.1664 -0.5229 1125 GLN A OE1 
8579  N NE2 . GLN A 1125 ? 1.5991 2.2363 1.7167 -0.1378 -0.1842 -0.5576 1125 GLN A NE2 
8580  N N   . PRO A 1126 ? 1.1299 1.6397 1.2248 0.0238  -0.1621 -0.4652 1126 PRO A N   
8581  C CA  . PRO A 1126 ? 1.1060 1.6188 1.2243 0.0564  -0.1582 -0.4507 1126 PRO A CA  
8582  C C   . PRO A 1126 ? 1.1016 1.6765 1.2924 0.0587  -0.1594 -0.4636 1126 PRO A C   
8583  O O   . PRO A 1126 ? 1.1146 1.7038 1.3317 0.0826  -0.1698 -0.4599 1126 PRO A O   
8584  C CB  . PRO A 1126 ? 1.0737 1.5568 1.1665 0.0573  -0.1390 -0.4377 1126 PRO A CB  
8585  C CG  . PRO A 1126 ? 1.1133 1.5754 1.1687 0.0253  -0.1339 -0.4462 1126 PRO A CG  
8586  C CD  . PRO A 1126 ? 1.1338 1.6344 1.2143 0.0004  -0.1455 -0.4685 1126 PRO A CD  
8587  N N   . ILE A 1127 ? 1.1035 1.7115 1.3233 0.0342  -0.1485 -0.4787 1127 ILE A N   
8588  C CA  . ILE A 1127 ? 1.0799 1.7490 1.3693 0.0331  -0.1478 -0.4949 1127 ILE A CA  
8589  C C   . ILE A 1127 ? 1.0947 1.8056 1.4076 0.0046  -0.1546 -0.5188 1127 ILE A C   
8590  O O   . ILE A 1127 ? 1.1078 1.7999 1.3816 -0.0222 -0.1549 -0.5238 1127 ILE A O   
8591  C CB  . ILE A 1127 ? 1.1165 1.7999 1.4314 0.0283  -0.1268 -0.4952 1127 ILE A CB  
8592  C CG1 . ILE A 1127 ? 1.1331 1.7760 1.3990 0.0111  -0.1126 -0.4856 1127 ILE A CG1 
8593  C CG2 . ILE A 1127 ? 1.0961 1.7771 1.4301 0.0600  -0.1244 -0.4811 1127 ILE A CG2 
8594  C CD1 . ILE A 1127 ? 1.1800 1.8077 1.4088 -0.0200 -0.1155 -0.4958 1127 ILE A CD1 
8595  N N   . LYS A 1128 ? 1.1059 1.8734 1.4820 0.0114  -0.1604 -0.5335 1128 LYS A N   
8596  C CA  . LYS A 1128 ? 1.1297 1.9528 1.5446 -0.0155 -0.1621 -0.5590 1128 LYS A CA  
8597  C C   . LYS A 1128 ? 1.1601 2.0140 1.6153 -0.0251 -0.1412 -0.5700 1128 LYS A C   
8598  O O   . LYS A 1128 ? 1.1484 2.0177 1.6413 -0.0005 -0.1375 -0.5673 1128 LYS A O   
8599  C CB  . LYS A 1128 ? 1.0996 1.9677 1.5620 0.0034  -0.1829 -0.5675 1128 LYS A CB  
8600  C CG  . LYS A 1128 ? 1.0691 2.0118 1.5941 -0.0149 -0.1828 -0.5951 1128 LYS A CG  
8601  C CD  . LYS A 1128 ? 1.0792 2.0398 1.5878 -0.0492 -0.1925 -0.6090 1128 LYS A CD  
8602  C CE  . LYS A 1128 ? 1.0847 2.0199 1.5495 -0.0893 -0.1742 -0.6139 1128 LYS A CE  
8603  N NZ  . LYS A 1128 ? 1.0928 2.0686 1.5636 -0.1285 -0.1789 -0.6360 1128 LYS A NZ  
8604  N N   . LEU A 1129 ? 1.2032 2.0610 1.6455 -0.0617 -0.1270 -0.5818 1129 LEU A N   
8605  C CA  . LEU A 1129 ? 1.2267 2.1149 1.7062 -0.0751 -0.1065 -0.5943 1129 LEU A CA  
8606  C C   . LEU A 1129 ? 1.2828 2.2432 1.8213 -0.0944 -0.1060 -0.6240 1129 LEU A C   
8607  O O   . LEU A 1129 ? 1.3345 2.3175 1.8752 -0.1058 -0.1206 -0.6345 1129 LEU A O   
8608  C CB  . LEU A 1129 ? 1.2018 2.0504 1.6330 -0.1036 -0.0893 -0.5887 1129 LEU A CB  
8609  C CG  . LEU A 1129 ? 1.1883 1.9677 1.5574 -0.0903 -0.0879 -0.5610 1129 LEU A CG  
8610  C CD1 . LEU A 1129 ? 1.1893 1.9421 1.5234 -0.1198 -0.0710 -0.5594 1129 LEU A CD1 
8611  C CD2 . LEU A 1129 ? 1.1642 1.9325 1.5474 -0.0514 -0.0878 -0.5424 1129 LEU A CD2 
8612  N N   . GLN A 1130 ? 1.2826 2.2808 1.8689 -0.0985 -0.0891 -0.6382 1130 GLN A N   
8613  C CA  . GLN A 1130 ? 1.2698 2.3390 1.9128 -0.1180 -0.0854 -0.6680 1130 GLN A CA  
8614  C C   . GLN A 1130 ? 1.2133 2.2821 1.8280 -0.1677 -0.0717 -0.6817 1130 GLN A C   
8615  O O   . GLN A 1130 ? 1.1957 2.2115 1.7564 -0.1833 -0.0615 -0.6686 1130 GLN A O   
8616  C CB  . GLN A 1130 ? 1.3211 2.4289 2.0251 -0.1022 -0.0710 -0.6794 1130 GLN A CB  
8617  C CG  . GLN A 1130 ? 1.3755 2.4561 2.0853 -0.0578 -0.0760 -0.6595 1130 GLN A CG  
8618  C CD  . GLN A 1130 ? 1.3972 2.5205 2.1711 -0.0403 -0.0648 -0.6745 1130 GLN A CD  
8619  O OE1 . GLN A 1130 ? 1.4057 2.5913 2.2338 -0.0475 -0.0629 -0.7000 1130 GLN A OE1 
8620  N NE2 . GLN A 1130 ? 1.3947 2.4849 2.1619 -0.0178 -0.0568 -0.6592 1130 GLN A NE2 
8621  N N   . GLY A 1131 ? 1.2118 2.3401 1.8619 -0.1932 -0.0718 -0.7079 1131 GLY A N   
8622  C CA  . GLY A 1131 ? 1.2422 2.3735 1.8666 -0.2442 -0.0576 -0.7236 1131 GLY A CA  
8623  C C   . GLY A 1131 ? 1.2961 2.4661 1.9227 -0.2734 -0.0692 -0.7417 1131 GLY A C   
8624  O O   . GLY A 1131 ? 1.3215 2.5158 1.9681 -0.2537 -0.0905 -0.7409 1131 GLY A O   
8625  N N   . THR A 1132 ? 1.2846 2.4602 1.8886 -0.3229 -0.0554 -0.7582 1132 THR A N   
8626  C CA  . THR A 1132 ? 1.2914 2.4978 1.8860 -0.3595 -0.0642 -0.7755 1132 THR A CA  
8627  C C   . THR A 1132 ? 1.3113 2.4396 1.8182 -0.3684 -0.0775 -0.7546 1132 THR A C   
8628  O O   . THR A 1132 ? 1.3010 2.3578 1.7571 -0.3550 -0.0740 -0.7316 1132 THR A O   
8629  C CB  . THR A 1132 ? 1.3196 2.5560 1.9166 -0.4124 -0.0423 -0.8013 1132 THR A CB  
8630  O OG1 . THR A 1132 ? 1.2925 2.5473 1.9304 -0.4048 -0.0200 -0.8083 1132 THR A OG1 
8631  C CG2 . THR A 1132 ? 1.3334 2.6546 1.9779 -0.4377 -0.0479 -0.8301 1132 THR A CG2 
8632  N N   . LEU A 1133 ? 1.3683 2.5083 1.8547 -0.3915 -0.0924 -0.7622 1133 LEU A N   
8633  C CA  . LEU A 1133 ? 1.4536 2.5116 1.8510 -0.3986 -0.1039 -0.7421 1133 LEU A CA  
8634  C C   . LEU A 1133 ? 1.5352 2.5155 1.8604 -0.4190 -0.0878 -0.7305 1133 LEU A C   
8635  O O   . LEU A 1133 ? 1.5967 2.5004 1.8604 -0.4008 -0.0937 -0.7057 1133 LEU A O   
8636  C CB  . LEU A 1133 ? 1.4718 2.5484 1.8463 -0.4325 -0.1189 -0.7546 1133 LEU A CB  
8637  C CG  . LEU A 1133 ? 1.4307 2.5317 1.8337 -0.3972 -0.1444 -0.7468 1133 LEU A CG  
8638  C CD1 . LEU A 1133 ? 1.3750 2.5769 1.8819 -0.3780 -0.1470 -0.7653 1133 LEU A CD1 
8639  C CD2 . LEU A 1133 ? 1.4702 2.5555 1.8205 -0.4273 -0.1618 -0.7488 1133 LEU A CD2 
8640  N N   . PRO A 1134 ? 1.5304 2.5307 1.8631 -0.4562 -0.0675 -0.7483 1134 PRO A N   
8641  C CA  . PRO A 1134 ? 1.5705 2.5042 1.8415 -0.4777 -0.0518 -0.7391 1134 PRO A CA  
8642  C C   . PRO A 1134 ? 1.5680 2.4778 1.8545 -0.4398 -0.0427 -0.7200 1134 PRO A C   
8643  O O   . PRO A 1134 ? 1.5787 2.4140 1.8066 -0.4255 -0.0443 -0.6953 1134 PRO A O   
8644  C CB  . PRO A 1134 ? 1.5609 2.5445 1.8545 -0.5283 -0.0335 -0.7687 1134 PRO A CB  
8645  C CG  . PRO A 1134 ? 1.5598 2.6208 1.9012 -0.5425 -0.0427 -0.7920 1134 PRO A CG  
8646  C CD  . PRO A 1134 ? 1.5205 2.6096 1.9141 -0.4876 -0.0599 -0.7809 1134 PRO A CD  
8647  N N   . VAL A 1135 ? 1.5358 2.5093 1.9000 -0.4249 -0.0327 -0.7323 1135 VAL A N   
8648  C CA  . VAL A 1135 ? 1.4805 2.4409 1.8677 -0.3883 -0.0247 -0.7162 1135 VAL A CA  
8649  C C   . VAL A 1135 ? 1.4729 2.3775 1.8270 -0.3446 -0.0405 -0.6855 1135 VAL A C   
8650  O O   . VAL A 1135 ? 1.4767 2.3194 1.7825 -0.3365 -0.0366 -0.6639 1135 VAL A O   
8651  C CB  . VAL A 1135 ? 1.4236 2.4620 1.9025 -0.3653 -0.0202 -0.7322 1135 VAL A CB  
8652  C CG1 . VAL A 1135 ? 1.3837 2.4021 1.8804 -0.3163 -0.0216 -0.7104 1135 VAL A CG1 
8653  C CG2 . VAL A 1135 ? 1.4113 2.4969 1.9254 -0.4010 0.0028  -0.7589 1135 VAL A CG2 
8654  N N   . GLU A 1136 ? 1.4718 2.4006 1.8524 -0.3173 -0.0585 -0.6841 1136 GLU A N   
8655  C CA  . GLU A 1136 ? 1.4631 2.3433 1.8138 -0.2772 -0.0739 -0.6574 1136 GLU A CA  
8656  C C   . GLU A 1136 ? 1.5153 2.3113 1.7795 -0.2861 -0.0732 -0.6371 1136 GLU A C   
8657  O O   . GLU A 1136 ? 1.5213 2.2756 1.7654 -0.2622 -0.0683 -0.6158 1136 GLU A O   
8658  C CB  . GLU A 1136 ? 1.4447 2.3506 1.8096 -0.2657 -0.0958 -0.6616 1136 GLU A CB  
8659  C CG  . GLU A 1136 ? 1.4502 2.3013 1.7759 -0.2294 -0.1112 -0.6353 1136 GLU A CG  
8660  C CD  . GLU A 1136 ? 1.4260 2.3163 1.7943 -0.2016 -0.1311 -0.6370 1136 GLU A CD  
8661  O OE1 . GLU A 1136 ? 1.3915 2.3456 1.8040 -0.2187 -0.1369 -0.6591 1136 GLU A OE1 
8662  O OE2 . GLU A 1136 ? 1.4344 2.2928 1.7914 -0.1636 -0.1410 -0.6163 1136 GLU A OE2 
8663  N N   . ALA A 1137 ? 1.5741 2.3453 1.7861 -0.3207 -0.0777 -0.6440 1137 ALA A N   
8664  C CA  . ALA A 1137 ? 1.6329 2.3190 1.7582 -0.3274 -0.0780 -0.6253 1137 ALA A CA  
8665  C C   . ALA A 1137 ? 1.6244 2.2797 1.7333 -0.3299 -0.0615 -0.6148 1137 ALA A C   
8666  O O   . ALA A 1137 ? 1.6349 2.2299 1.6986 -0.3080 -0.0620 -0.5907 1137 ALA A O   
8667  C CB  . ALA A 1137 ? 1.6988 2.3650 1.7706 -0.3732 -0.0816 -0.6388 1137 ALA A CB  
8668  N N   . ARG A 1138 ? 1.6068 2.3051 1.7527 -0.3568 -0.0467 -0.6330 1138 ARG A N   
8669  C CA  . ARG A 1138 ? 1.5989 2.2745 1.7349 -0.3604 -0.0316 -0.6237 1138 ARG A CA  
8670  C C   . ARG A 1138 ? 1.5125 2.1854 1.6767 -0.3106 -0.0330 -0.6021 1138 ARG A C   
8671  O O   . ARG A 1138 ? 1.5102 2.1272 1.6302 -0.2907 -0.0350 -0.5776 1138 ARG A O   
8672  C CB  . ARG A 1138 ? 1.6437 2.3749 1.8246 -0.3954 -0.0149 -0.6492 1138 ARG A CB  
8673  C CG  . ARG A 1138 ? 1.6880 2.3954 1.8544 -0.4072 0.0010  -0.6416 1138 ARG A CG  
8674  C CD  . ARG A 1138 ? 1.7490 2.4797 1.9156 -0.4610 0.0165  -0.6668 1138 ARG A CD  
8675  N NE  . ARG A 1138 ? 1.8091 2.5046 1.9476 -0.4747 0.0291  -0.6563 1138 ARG A NE  
8676  C CZ  . ARG A 1138 ? 1.8730 2.5638 1.9883 -0.5231 0.0423  -0.6709 1138 ARG A CZ  
8677  N NH1 . ARG A 1138 ? 1.9025 2.6235 2.0198 -0.5640 0.0461  -0.6980 1138 ARG A NH1 
8678  N NH2 . ARG A 1138 ? 1.8886 2.5452 1.9775 -0.5322 0.0514  -0.6582 1138 ARG A NH2 
8679  N N   . GLU A 1139 ? 1.4317 2.1653 1.6684 -0.2906 -0.0323 -0.6117 1139 GLU A N   
8680  C CA  . GLU A 1139 ? 1.3392 2.0762 1.6068 -0.2454 -0.0339 -0.5942 1139 GLU A CA  
8681  C C   . GLU A 1139 ? 1.3600 2.0427 1.5820 -0.2134 -0.0471 -0.5683 1139 GLU A C   
8682  O O   . GLU A 1139 ? 1.3499 1.9973 1.5508 -0.1928 -0.0434 -0.5463 1139 GLU A O   
8683  C CB  . GLU A 1139 ? 1.2707 2.0715 1.6095 -0.2260 -0.0398 -0.6090 1139 GLU A CB  
8684  C CG  . GLU A 1139 ? 1.2021 2.0598 1.6015 -0.2384 -0.0243 -0.6297 1139 GLU A CG  
8685  C CD  . GLU A 1139 ? 1.1621 2.0100 1.5754 -0.2181 -0.0129 -0.6158 1139 GLU A CD  
8686  O OE1 . GLU A 1139 ? 1.1465 2.0274 1.6114 -0.1900 -0.0134 -0.6182 1139 GLU A OE1 
8687  O OE2 . GLU A 1139 ? 1.1663 1.9721 1.5370 -0.2307 -0.0042 -0.6021 1139 GLU A OE2 
8688  N N   . ASN A 1140 ? 1.3642 2.0442 1.5734 -0.2097 -0.0623 -0.5718 1140 ASN A N   
8689  C CA  . ASN A 1140 ? 1.3838 2.0154 1.5510 -0.1804 -0.0749 -0.5505 1140 ASN A CA  
8690  C C   . ASN A 1140 ? 1.3512 1.9156 1.4530 -0.1811 -0.0689 -0.5305 1140 ASN A C   
8691  O O   . ASN A 1140 ? 1.3337 1.8667 1.4191 -0.1481 -0.0702 -0.5081 1140 ASN A O   
8692  C CB  . ASN A 1140 ? 1.4925 2.1222 1.6383 -0.1932 -0.0898 -0.5607 1140 ASN A CB  
8693  C CG  . ASN A 1140 ? 1.5929 2.1845 1.7086 -0.1599 -0.1038 -0.5421 1140 ASN A CG  
8694  O OD1 . ASN A 1140 ? 1.6738 2.2496 1.7581 -0.1690 -0.1162 -0.5459 1140 ASN A OD1 
8695  N ND2 . ASN A 1140 ? 1.5958 2.1720 1.7184 -0.1229 -0.1016 -0.5221 1140 ASN A ND2 
8696  N N   . SER A 1141 ? 1.3445 1.8879 1.4089 -0.2191 -0.0621 -0.5388 1141 SER A N   
8697  C CA  . SER A 1141 ? 1.3511 1.8291 1.3512 -0.2217 -0.0573 -0.5206 1141 SER A CA  
8698  C C   . SER A 1141 ? 1.2593 1.7380 1.2783 -0.2007 -0.0474 -0.5034 1141 SER A C   
8699  O O   . SER A 1141 ? 1.2485 1.6862 1.2365 -0.1724 -0.0493 -0.4801 1141 SER A O   
8700  C CB  . SER A 1141 ? 1.4087 1.8662 1.3674 -0.2702 -0.0518 -0.5345 1141 SER A CB  
8701  O OG  . SER A 1141 ? 1.4605 1.8468 1.3496 -0.2699 -0.0502 -0.5157 1141 SER A OG  
8702  N N   . LEU A 1142 ? 1.1910 1.7170 1.2597 -0.2156 -0.0364 -0.5154 1142 LEU A N   
8703  C CA  . LEU A 1142 ? 1.1010 1.6335 1.1915 -0.1983 -0.0272 -0.5004 1142 LEU A CA  
8704  C C   . LEU A 1142 ? 1.0756 1.6013 1.1746 -0.1520 -0.0351 -0.4814 1142 LEU A C   
8705  O O   . LEU A 1142 ? 1.0778 1.5655 1.1443 -0.1311 -0.0353 -0.4582 1142 LEU A O   
8706  C CB  . LEU A 1142 ? 1.0137 1.6071 1.1692 -0.2116 -0.0160 -0.5186 1142 LEU A CB  
8707  C CG  . LEU A 1142 ? 0.9391 1.5366 1.0987 -0.2341 -0.0007 -0.5181 1142 LEU A CG  
8708  C CD1 . LEU A 1142 ? 0.8925 1.5489 1.1105 -0.2552 0.0109  -0.5442 1142 LEU A CD1 
8709  C CD2 . LEU A 1142 ? 0.8868 1.4684 1.0442 -0.2068 0.0022  -0.4923 1142 LEU A CD2 
8710  N N   . TYR A 1143 ? 1.0499 1.6124 1.1909 -0.1367 -0.0424 -0.4915 1143 TYR A N   
8711  C CA  . TYR A 1143 ? 1.0088 1.5715 1.1653 -0.0946 -0.0491 -0.4757 1143 TYR A CA  
8712  C C   . TYR A 1143 ? 1.0164 1.5225 1.1162 -0.0728 -0.0548 -0.4530 1143 TYR A C   
8713  O O   . TYR A 1143 ? 0.9840 1.4796 1.0833 -0.0450 -0.0523 -0.4333 1143 TYR A O   
8714  C CB  . TYR A 1143 ? 0.9740 1.5735 1.1711 -0.0815 -0.0604 -0.4887 1143 TYR A CB  
8715  C CG  . TYR A 1143 ? 0.9560 1.5421 1.1533 -0.0403 -0.0689 -0.4704 1143 TYR A CG  
8716  C CD1 . TYR A 1143 ? 0.9082 1.5183 1.1455 -0.0182 -0.0649 -0.4641 1143 TYR A CD1 
8717  C CD2 . TYR A 1143 ? 0.9905 1.5356 1.1424 -0.0256 -0.0799 -0.4593 1143 TYR A CD2 
8718  C CE1 . TYR A 1143 ? 0.9152 1.5106 1.1480 0.0163  -0.0722 -0.4476 1143 TYR A CE1 
8719  C CE2 . TYR A 1143 ? 0.9788 1.5103 1.1276 0.0097  -0.0866 -0.4432 1143 TYR A CE2 
8720  C CZ  . TYR A 1143 ? 0.9422 1.4997 1.1317 0.0298  -0.0829 -0.4374 1143 TYR A CZ  
8721  O OH  . TYR A 1143 ? 0.9361 1.4787 1.1192 0.0619  -0.0891 -0.4219 1143 TYR A OH  
8722  N N   . LEU A 1144 ? 1.0504 1.5198 1.1012 -0.0860 -0.0615 -0.4562 1144 LEU A N   
8723  C CA  . LEU A 1144 ? 1.0973 1.5076 1.0894 -0.0657 -0.0649 -0.4357 1144 LEU A CA  
8724  C C   . LEU A 1144 ? 1.1189 1.5019 1.0854 -0.0652 -0.0549 -0.4189 1144 LEU A C   
8725  O O   . LEU A 1144 ? 1.1125 1.4850 1.0768 -0.0354 -0.0522 -0.3984 1144 LEU A O   
8726  C CB  . LEU A 1144 ? 1.1239 1.4949 1.0630 -0.0826 -0.0733 -0.4435 1144 LEU A CB  
8727  C CG  . LEU A 1144 ? 1.1293 1.4408 1.0115 -0.0554 -0.0781 -0.4249 1144 LEU A CG  
8728  C CD1 . LEU A 1144 ? 1.1061 1.4334 1.0102 -0.0286 -0.0876 -0.4232 1144 LEU A CD1 
8729  C CD2 . LEU A 1144 ? 1.1812 1.4380 0.9948 -0.0789 -0.0819 -0.4302 1144 LEU A CD2 
8730  N N   . THR A 1145 ? 1.1367 1.5102 1.0842 -0.0996 -0.0497 -0.4276 1145 THR A N   
8731  C CA  . THR A 1145 ? 1.1398 1.4839 1.0578 -0.1017 -0.0429 -0.4117 1145 THR A CA  
8732  C C   . THR A 1145 ? 1.0955 1.4721 1.0561 -0.0807 -0.0358 -0.3975 1145 THR A C   
8733  O O   . THR A 1145 ? 1.1009 1.4536 1.0403 -0.0579 -0.0345 -0.3754 1145 THR A O   
8734  C CB  . THR A 1145 ? 1.2170 1.5510 1.1124 -0.1468 -0.0384 -0.4254 1145 THR A CB  
8735  O OG1 . THR A 1145 ? 1.2467 1.5508 1.1006 -0.1670 -0.0452 -0.4387 1145 THR A OG1 
8736  C CG2 . THR A 1145 ? 1.2522 1.5441 1.1049 -0.1471 -0.0351 -0.4066 1145 THR A CG2 
8737  N N   . ALA A 1146 ? 1.0440 1.4746 1.0634 -0.0869 -0.0313 -0.4097 1146 ALA A N   
8738  C CA  . ALA A 1146 ? 1.0565 1.5134 1.1108 -0.0679 -0.0248 -0.3961 1146 ALA A CA  
8739  C C   . ALA A 1146 ? 1.0710 1.5146 1.1185 -0.0259 -0.0296 -0.3761 1146 ALA A C   
8740  O O   . ALA A 1146 ? 1.0487 1.4813 1.0847 -0.0084 -0.0260 -0.3550 1146 ALA A O   
8741  C CB  . ALA A 1146 ? 1.0242 1.5346 1.1383 -0.0781 -0.0195 -0.4136 1146 ALA A CB  
8742  N N   . PHE A 1147 ? 1.0940 1.5404 1.1485 -0.0115 -0.0380 -0.3835 1147 PHE A N   
8743  C CA  . PHE A 1147 ? 1.0841 1.5174 1.1308 0.0253  -0.0432 -0.3685 1147 PHE A CA  
8744  C C   . PHE A 1147 ? 1.1008 1.4852 1.0936 0.0423  -0.0430 -0.3489 1147 PHE A C   
8745  O O   . PHE A 1147 ? 1.0966 1.4789 1.0883 0.0674  -0.0390 -0.3297 1147 PHE A O   
8746  C CB  . PHE A 1147 ? 1.0882 1.5221 1.1372 0.0291  -0.0545 -0.3822 1147 PHE A CB  
8747  C CG  . PHE A 1147 ? 1.0664 1.4926 1.1138 0.0637  -0.0604 -0.3702 1147 PHE A CG  
8748  C CD1 . PHE A 1147 ? 1.0154 1.4698 1.0980 0.0715  -0.0685 -0.3802 1147 PHE A CD1 
8749  C CD2 . PHE A 1147 ? 1.0880 1.4790 1.0984 0.0882  -0.0579 -0.3497 1147 PHE A CD2 
8750  C CE1 . PHE A 1147 ? 1.0031 1.4475 1.0805 0.1002  -0.0743 -0.3694 1147 PHE A CE1 
8751  C CE2 . PHE A 1147 ? 1.0804 1.4651 1.0883 0.1167  -0.0619 -0.3402 1147 PHE A CE2 
8752  C CZ  . PHE A 1147 ? 1.0381 1.4475 1.0774 0.1213  -0.0704 -0.3500 1147 PHE A CZ  
8753  N N   . THR A 1148 ? 1.1440 1.4884 1.0907 0.0289  -0.0472 -0.3544 1148 THR A N   
8754  C CA  . THR A 1148 ? 1.2051 1.4970 1.0963 0.0457  -0.0468 -0.3373 1148 THR A CA  
8755  C C   . THR A 1148 ? 1.1178 1.4087 1.0053 0.0467  -0.0391 -0.3207 1148 THR A C   
8756  O O   . THR A 1148 ? 1.1300 1.3918 0.9872 0.0714  -0.0374 -0.3016 1148 THR A O   
8757  C CB  . THR A 1148 ? 1.1638 1.4049 0.9985 0.0304  -0.0533 -0.3472 1148 THR A CB  
8758  O OG1 . THR A 1148 ? 1.2272 1.4172 1.0079 0.0328  -0.0508 -0.3344 1148 THR A OG1 
8759  C CG2 . THR A 1148 ? 1.1365 1.3980 0.9852 -0.0100 -0.0561 -0.3715 1148 THR A CG2 
8760  N N   . VAL A 1149 ? 1.0623 1.3871 0.9820 0.0211  -0.0344 -0.3275 1149 VAL A N   
8761  C CA  . VAL A 1149 ? 1.0468 1.3758 0.9668 0.0233  -0.0286 -0.3102 1149 VAL A CA  
8762  C C   . VAL A 1149 ? 0.9885 1.3460 0.9388 0.0554  -0.0250 -0.2935 1149 VAL A C   
8763  O O   . VAL A 1149 ? 0.9949 1.3342 0.9234 0.0822  -0.0242 -0.2738 1149 VAL A O   
8764  C CB  . VAL A 1149 ? 0.8261 1.1783 0.7652 -0.0152 -0.0237 -0.3209 1149 VAL A CB  
8765  C CG1 . VAL A 1149 ? 0.8073 1.1852 0.7684 -0.0110 -0.0175 -0.3036 1149 VAL A CG1 
8766  C CG2 . VAL A 1149 ? 0.8395 1.1475 0.7281 -0.0426 -0.0266 -0.3270 1149 VAL A CG2 
8767  N N   . ILE A 1150 ? 0.9174 1.3180 0.9158 0.0531  -0.0227 -0.3022 1150 ILE A N   
8768  C CA  . ILE A 1150 ? 0.8327 1.2607 0.8591 0.0782  -0.0191 -0.2887 1150 ILE A CA  
8769  C C   . ILE A 1150 ? 0.8399 1.2420 0.8380 0.1130  -0.0209 -0.2727 1150 ILE A C   
8770  O O   . ILE A 1150 ? 0.8386 1.2550 0.8447 0.1331  -0.0163 -0.2553 1150 ILE A O   
8771  C CB  . ILE A 1150 ? 0.7573 1.2159 0.8238 0.0771  -0.0206 -0.3038 1150 ILE A CB  
8772  C CG1 . ILE A 1150 ? 0.7717 1.2433 0.8549 0.0433  -0.0210 -0.3275 1150 ILE A CG1 
8773  C CG2 . ILE A 1150 ? 0.6627 1.1547 0.7624 0.0893  -0.0146 -0.2929 1150 ILE A CG2 
8774  C CD1 . ILE A 1150 ? 0.7570 1.2686 0.8890 0.0367  -0.0189 -0.3415 1150 ILE A CD1 
8775  N N   . GLY A 1151 ? 0.8647 1.2293 0.8286 0.1187  -0.0271 -0.2795 1151 GLY A N   
8776  C CA  . GLY A 1151 ? 0.9076 1.2406 0.8382 0.1507  -0.0277 -0.2665 1151 GLY A CA  
8777  C C   . GLY A 1151 ? 0.9501 1.2578 0.8480 0.1629  -0.0239 -0.2486 1151 GLY A C   
8778  O O   . GLY A 1151 ? 0.9483 1.2665 0.8503 0.1888  -0.0186 -0.2307 1151 GLY A O   
8779  N N   . ILE A 1152 ? 1.0043 1.2791 0.8692 0.1441  -0.0268 -0.2533 1152 ILE A N   
8780  C CA  . ILE A 1152 ? 1.0618 1.3050 0.8901 0.1565  -0.0255 -0.2366 1152 ILE A CA  
8781  C C   . ILE A 1152 ? 1.0835 1.3690 0.9454 0.1591  -0.0207 -0.2210 1152 ILE A C   
8782  O O   . ILE A 1152 ? 1.1012 1.3872 0.9563 0.1857  -0.0176 -0.2015 1152 ILE A O   
8783  C CB  . ILE A 1152 ? 1.0508 1.2548 0.8409 0.1281  -0.0302 -0.2456 1152 ILE A CB  
8784  C CG1 . ILE A 1152 ? 1.0183 1.1855 0.7769 0.1181  -0.0353 -0.2636 1152 ILE A CG1 
8785  C CG2 . ILE A 1152 ? 0.6996 0.8681 0.4504 0.1437  -0.0303 -0.2263 1152 ILE A CG2 
8786  C CD1 . ILE A 1152 ? 0.9954 1.1396 0.7294 0.0784  -0.0396 -0.2802 1152 ILE A CD1 
8787  N N   . ARG A 1153 ? 1.0784 1.4009 0.9769 0.1297  -0.0197 -0.2307 1153 ARG A N   
8788  C CA  . ARG A 1153 ? 1.0721 1.4398 1.0069 0.1257  -0.0149 -0.2191 1153 ARG A CA  
8789  C C   . ARG A 1153 ? 1.0190 1.4147 0.9760 0.1566  -0.0101 -0.2054 1153 ARG A C   
8790  O O   . ARG A 1153 ? 1.0357 1.4484 0.9971 0.1711  -0.0071 -0.1861 1153 ARG A O   
8791  C CB  . ARG A 1153 ? 1.1129 1.5140 1.0848 0.0917  -0.0129 -0.2364 1153 ARG A CB  
8792  C CG  . ARG A 1153 ? 1.2060 1.5922 1.1623 0.0556  -0.0146 -0.2463 1153 ARG A CG  
8793  C CD  . ARG A 1153 ? 1.2733 1.6546 1.2132 0.0548  -0.0150 -0.2261 1153 ARG A CD  
8794  N NE  . ARG A 1153 ? 1.2957 1.6739 1.2293 0.0157  -0.0152 -0.2337 1153 ARG A NE  
8795  C CZ  . ARG A 1153 ? 1.3228 1.6823 1.2290 0.0092  -0.0188 -0.2192 1153 ARG A CZ  
8796  N NH1 . ARG A 1153 ? 1.3215 1.6667 1.2078 0.0416  -0.0227 -0.1968 1153 ARG A NH1 
8797  N NH2 . ARG A 1153 ? 1.3596 1.7145 1.2578 -0.0292 -0.0188 -0.2274 1153 ARG A NH2 
8798  N N   . LYS A 1154 ? 0.9740 1.3755 0.9441 0.1658  -0.0100 -0.2151 1154 LYS A N   
8799  C CA  . LYS A 1154 ? 0.9479 1.3791 0.9412 0.1885  -0.0049 -0.2044 1154 LYS A CA  
8800  C C   . LYS A 1154 ? 1.0102 1.4275 0.9794 0.2224  -0.0016 -0.1855 1154 LYS A C   
8801  O O   . LYS A 1154 ? 0.9829 1.4323 0.9706 0.2380  0.0044  -0.1707 1154 LYS A O   
8802  C CB  . LYS A 1154 ? 0.9169 1.3479 0.9210 0.1923  -0.0076 -0.2186 1154 LYS A CB  
8803  C CG  . LYS A 1154 ? 0.8680 1.3347 0.9135 0.1715  -0.0071 -0.2303 1154 LYS A CG  
8804  C CD  . LYS A 1154 ? 0.8512 1.3530 0.9220 0.1814  -0.0005 -0.2172 1154 LYS A CD  
8805  C CE  . LYS A 1154 ? 0.8311 1.3585 0.9369 0.1642  -0.0004 -0.2304 1154 LYS A CE  
8806  N NZ  . LYS A 1154 ? 0.8253 1.3686 0.9432 0.1805  0.0024  -0.2228 1154 LYS A NZ  
8807  N N   . ALA A 1155 ? 1.0942 1.4630 1.0207 0.2329  -0.0050 -0.1868 1155 ALA A N   
8808  C CA  . ALA A 1155 ? 1.1623 1.5073 1.0596 0.2684  -0.0012 -0.1733 1155 ALA A CA  
8809  C C   . ALA A 1155 ? 1.2726 1.5947 1.1424 0.2763  -0.0022 -0.1604 1155 ALA A C   
8810  O O   . ALA A 1155 ? 1.3199 1.6274 1.1694 0.3084  0.0019  -0.1471 1155 ALA A O   
8811  C CB  . ALA A 1155 ? 1.1582 1.4575 1.0215 0.2778  -0.0038 -0.1853 1155 ALA A CB  
8812  N N   . PHE A 1156 ? 1.3207 1.6383 1.1884 0.2476  -0.0077 -0.1646 1156 PHE A N   
8813  C CA  . PHE A 1156 ? 1.3976 1.6817 1.2302 0.2511  -0.0117 -0.1543 1156 PHE A CA  
8814  C C   . PHE A 1156 ? 1.3835 1.6879 1.2219 0.2840  -0.0078 -0.1306 1156 PHE A C   
8815  O O   . PHE A 1156 ? 1.4234 1.6906 1.2254 0.3057  -0.0097 -0.1202 1156 PHE A O   
8816  C CB  . PHE A 1156 ? 1.4175 1.7086 1.2568 0.2119  -0.0171 -0.1596 1156 PHE A CB  
8817  C CG  . PHE A 1156 ? 1.4685 1.7364 1.2791 0.2149  -0.0222 -0.1442 1156 PHE A CG  
8818  C CD1 . PHE A 1156 ? 1.5342 1.7366 1.2890 0.2122  -0.0282 -0.1483 1156 PHE A CD1 
8819  C CD2 . PHE A 1156 ? 1.4565 1.7671 1.2938 0.2188  -0.0221 -0.1253 1156 PHE A CD2 
8820  C CE1 . PHE A 1156 ? 1.5712 1.7477 1.2963 0.2160  -0.0344 -0.1336 1156 PHE A CE1 
8821  C CE2 . PHE A 1156 ? 1.4939 1.7839 1.3053 0.2224  -0.0290 -0.1102 1156 PHE A CE2 
8822  C CZ  . PHE A 1156 ? 1.5582 1.7794 1.3130 0.2220  -0.0355 -0.1142 1156 PHE A CZ  
8823  N N   . ASP A 1157 ? 1.3267 1.6905 1.2103 0.2880  -0.0021 -0.1222 1157 ASP A N   
8824  C CA  . ASP A 1157 ? 1.3345 1.7320 1.2323 0.3121  0.0010  -0.0996 1157 ASP A CA  
8825  C C   . ASP A 1157 ? 1.3540 1.7327 1.2296 0.3577  0.0068  -0.0886 1157 ASP A C   
8826  O O   . ASP A 1157 ? 1.3502 1.7516 1.2328 0.3796  0.0079  -0.0697 1157 ASP A O   
8827  C CB  . ASP A 1157 ? 1.3337 1.8001 1.2826 0.3003  0.0059  -0.0936 1157 ASP A CB  
8828  C CG  . ASP A 1157 ? 1.3961 1.8904 1.3629 0.2709  0.0006  -0.0867 1157 ASP A CG  
8829  O OD1 . ASP A 1157 ? 1.4509 1.9160 1.3911 0.2685  -0.0070 -0.0809 1157 ASP A OD1 
8830  O OD2 . ASP A 1157 ? 1.3745 1.9158 1.3777 0.2497  0.0038  -0.0867 1157 ASP A OD2 
8831  N N   . ILE A 1158 ? 1.3601 1.6992 1.2091 0.3720  0.0106  -0.1001 1158 ILE A N   
8832  C CA  . ILE A 1158 ? 1.3265 1.6447 1.1517 0.4148  0.0183  -0.0913 1158 ILE A CA  
8833  C C   . ILE A 1158 ? 1.4247 1.6727 1.1947 0.4261  0.0134  -0.0922 1158 ILE A C   
8834  O O   . ILE A 1158 ? 1.4911 1.7083 1.2318 0.4622  0.0196  -0.0861 1158 ILE A O   
8835  C CB  . ILE A 1158 ? 1.2393 1.5426 1.0555 0.4251  0.0254  -0.1027 1158 ILE A CB  
8836  C CG1 . ILE A 1158 ? 1.1196 1.4500 0.9664 0.3923  0.0225  -0.1169 1158 ILE A CG1 
8837  C CG2 . ILE A 1158 ? 1.2165 1.5453 1.0413 0.4639  0.0380  -0.0892 1158 ILE A CG2 
8838  C CD1 . ILE A 1158 ? 1.0994 1.3942 0.9240 0.3917  0.0228  -0.1329 1158 ILE A CD1 
8839  N N   . CYS A 1159 ? 1.4353 1.6548 1.1881 0.3938  0.0032  -0.1012 1159 CYS A N   
8840  C CA  . CYS A 1159 ? 1.5162 1.6632 1.2104 0.3985  -0.0027 -0.1026 1159 CYS A CA  
8841  C C   . CYS A 1159 ? 1.5706 1.7088 1.2579 0.3648  -0.0140 -0.1029 1159 CYS A C   
8842  O O   . CYS A 1159 ? 1.6395 1.7196 1.2822 0.3445  -0.0200 -0.1153 1159 CYS A O   
8843  C CB  . CYS A 1159 ? 1.5034 1.5913 1.1549 0.3928  -0.0019 -0.1216 1159 CYS A CB  
8844  S SG  . CYS A 1159 ? 2.3623 2.3522 1.9306 0.4169  -0.0032 -0.1200 1159 CYS A SG  
8845  N N   . PRO A 1160 ? 1.5815 1.7756 1.3096 0.3561  -0.0166 -0.0897 1160 PRO A N   
8846  C CA  . PRO A 1160 ? 1.5766 1.7534 1.2889 0.3261  -0.0274 -0.0884 1160 PRO A CA  
8847  C C   . PRO A 1160 ? 1.6415 1.7393 1.2874 0.3430  -0.0332 -0.0850 1160 PRO A C   
8848  O O   . PRO A 1160 ? 1.6444 1.7296 1.2756 0.3846  -0.0313 -0.0694 1160 PRO A O   
8849  C CB  . PRO A 1160 ? 1.5863 1.8255 1.3403 0.3319  -0.0292 -0.0674 1160 PRO A CB  
8850  C CG  . PRO A 1160 ? 1.5766 1.8549 1.3577 0.3731  -0.0191 -0.0561 1160 PRO A CG  
8851  C CD  . PRO A 1160 ? 1.5476 1.8168 1.3299 0.3706  -0.0109 -0.0747 1160 PRO A CD  
8852  N N   . LEU A 1161 ? 1.6591 1.7030 1.2636 0.3108  -0.0393 -0.1005 1161 LEU A N   
8853  C CA  . LEU A 1161 ? 1.7376 1.6951 1.2698 0.3231  -0.0433 -0.1020 1161 LEU A CA  
8854  C C   . LEU A 1161 ? 1.7942 1.7160 1.2940 0.2796  -0.0537 -0.1094 1161 LEU A C   
8855  O O   . LEU A 1161 ? 1.7870 1.7200 1.2984 0.2379  -0.0537 -0.1285 1161 LEU A O   
8856  C CB  . LEU A 1161 ? 1.7050 1.6252 1.2110 0.3265  -0.0367 -0.1198 1161 LEU A CB  
8857  C CG  . LEU A 1161 ? 1.7363 1.5683 1.1675 0.3518  -0.0366 -0.1193 1161 LEU A CG  
8858  C CD1 . LEU A 1161 ? 1.6900 1.4795 1.0813 0.3678  -0.0449 -0.1016 1161 LEU A CD1 
8859  C CD2 . LEU A 1161 ? 1.6923 1.5301 1.1301 0.3952  -0.0249 -0.1157 1161 LEU A CD2 
8860  N N   . VAL A 1162 ? 1.8610 1.7405 1.3201 0.2893  -0.0626 -0.0947 1162 VAL A N   
8861  C CA  . VAL A 1162 ? 1.9138 1.7642 1.3436 0.2459  -0.0729 -0.0993 1162 VAL A CA  
8862  C C   . VAL A 1162 ? 1.9216 1.7416 1.3279 0.2062  -0.0705 -0.1262 1162 VAL A C   
8863  O O   . VAL A 1162 ? 1.8621 1.7143 1.2947 0.1619  -0.0707 -0.1399 1162 VAL A O   
8864  C CB  . VAL A 1162 ? 2.0497 1.8238 1.4106 0.2625  -0.0837 -0.0847 1162 VAL A CB  
8865  C CG1 . VAL A 1162 ? 2.0443 1.8532 1.4277 0.2643  -0.0937 -0.0626 1162 VAL A CG1 
8866  C CG2 . VAL A 1162 ? 2.1202 1.8472 1.4454 0.3168  -0.0788 -0.0771 1162 VAL A CG2 
8867  N N   . LYS A 1163 ? 1.9851 1.7466 1.3441 0.2231  -0.0673 -0.1341 1163 LYS A N   
8868  C CA  . LYS A 1163 ? 2.0260 1.7457 1.3479 0.1854  -0.0674 -0.1581 1163 LYS A CA  
8869  C C   . LYS A 1163 ? 1.9581 1.7457 1.3413 0.1550  -0.0619 -0.1768 1163 LYS A C   
8870  O O   . LYS A 1163 ? 1.9606 1.7394 1.3327 0.1106  -0.0637 -0.1965 1163 LYS A O   
8871  C CB  . LYS A 1163 ? 2.0763 1.7250 1.3384 0.2108  -0.0642 -0.1623 1163 LYS A CB  
8872  C CG  . LYS A 1163 ? 2.1257 1.7001 1.3168 0.1719  -0.0691 -0.1798 1163 LYS A CG  
8873  C CD  . LYS A 1163 ? 2.1720 1.6796 1.3055 0.1920  -0.0651 -0.1859 1163 LYS A CD  
8874  C CE  . LYS A 1163 ? 2.2202 1.6668 1.2909 0.1453  -0.0694 -0.2063 1163 LYS A CE  
8875  N NZ  . LYS A 1163 ? 2.2420 1.6619 1.2885 0.1510  -0.0639 -0.2193 1163 LYS A NZ  
8876  N N   . ILE A 1164 ? 1.9029 1.7582 1.3499 0.1787  -0.0552 -0.1709 1164 ILE A N   
8877  C CA  . ILE A 1164 ? 1.8686 1.7826 1.3706 0.1549  -0.0504 -0.1881 1164 ILE A CA  
8878  C C   . ILE A 1164 ? 1.8328 1.8137 1.3922 0.1297  -0.0503 -0.1865 1164 ILE A C   
8879  O O   . ILE A 1164 ? 1.7903 1.8203 1.3965 0.1078  -0.0464 -0.2010 1164 ILE A O   
8880  C CB  . ILE A 1164 ? 1.5412 1.4809 1.0714 0.1880  -0.0429 -0.1886 1164 ILE A CB  
8881  C CG1 . ILE A 1164 ? 1.4691 1.4897 1.0720 0.2006  -0.0377 -0.1790 1164 ILE A CG1 
8882  C CG2 . ILE A 1164 ? 1.5850 1.4677 1.0651 0.2311  -0.0408 -0.1772 1164 ILE A CG2 
8883  C CD1 . ILE A 1164 ? 1.4504 1.4901 1.0738 0.2311  -0.0306 -0.1791 1164 ILE A CD1 
8884  N N   . ASP A 1165 ? 1.8843 1.8646 1.4376 0.1326  -0.0550 -0.1687 1165 ASP A N   
8885  C CA  . ASP A 1165 ? 1.8581 1.8913 1.4541 0.1022  -0.0556 -0.1673 1165 ASP A CA  
8886  C C   . ASP A 1165 ? 1.8741 1.8793 1.4422 0.0508  -0.0590 -0.1859 1165 ASP A C   
8887  O O   . ASP A 1165 ? 1.8216 1.8693 1.4281 0.0168  -0.0545 -0.2016 1165 ASP A O   
8888  C CB  . ASP A 1165 ? 1.8915 1.9358 1.4899 0.1214  -0.0609 -0.1409 1165 ASP A CB  
8889  C CG  . ASP A 1165 ? 1.8603 1.9550 1.4969 0.0871  -0.0618 -0.1388 1165 ASP A CG  
8890  O OD1 . ASP A 1165 ? 1.7901 1.9435 1.4812 0.0727  -0.0541 -0.1483 1165 ASP A OD1 
8891  O OD2 . ASP A 1165 ? 1.9049 1.9765 1.5132 0.0749  -0.0705 -0.1272 1165 ASP A OD2 
8892  N N   . THR A 1166 ? 1.9337 1.8654 1.4324 0.0458  -0.0662 -0.1842 1166 THR A N   
8893  C CA  . THR A 1166 ? 1.9675 1.8592 1.4255 -0.0018 -0.0687 -0.2042 1166 THR A CA  
8894  C C   . THR A 1166 ? 1.9202 1.8412 1.4078 -0.0239 -0.0617 -0.2305 1166 THR A C   
8895  O O   . THR A 1166 ? 1.9009 1.8567 1.4170 -0.0645 -0.0583 -0.2471 1166 THR A O   
8896  C CB  . THR A 1166 ? 2.0614 1.8606 1.4341 0.0060  -0.0755 -0.2021 1166 THR A CB  
8897  O OG1 . THR A 1166 ? 2.1163 1.8814 1.4552 0.0230  -0.0841 -0.1787 1166 THR A OG1 
8898  C CG2 . THR A 1166 ? 2.0955 1.8555 1.4252 -0.0463 -0.0766 -0.2261 1166 THR A CG2 
8899  N N   . ALA A 1167 ? 1.8847 1.7909 1.3646 0.0031  -0.0597 -0.2343 1167 ALA A N   
8900  C CA  . ALA A 1167 ? 1.8093 1.7420 1.3157 -0.0136 -0.0554 -0.2574 1167 ALA A CA  
8901  C C   . ALA A 1167 ? 1.6647 1.6807 1.2508 -0.0248 -0.0493 -0.2642 1167 ALA A C   
8902  O O   . ALA A 1167 ? 1.6249 1.6674 1.2336 -0.0606 -0.0467 -0.2859 1167 ALA A O   
8903  C CB  . ALA A 1167 ? 1.8190 1.7317 1.3127 0.0235  -0.0544 -0.2552 1167 ALA A CB  
8904  N N   . LEU A 1168 ? 1.5991 1.6562 1.2265 0.0055  -0.0465 -0.2460 1168 LEU A N   
8905  C CA  . LEU A 1168 ? 1.5094 1.6401 1.2076 -0.0022 -0.0402 -0.2508 1168 LEU A CA  
8906  C C   . LEU A 1168 ? 1.5622 1.7128 1.2740 -0.0489 -0.0383 -0.2631 1168 LEU A C   
8907  O O   . LEU A 1168 ? 1.5420 1.7391 1.2999 -0.0695 -0.0325 -0.2798 1168 LEU A O   
8908  C CB  . LEU A 1168 ? 1.4169 1.5827 1.1472 0.0320  -0.0380 -0.2273 1168 LEU A CB  
8909  C CG  . LEU A 1168 ? 1.3563 1.5570 1.1258 0.0582  -0.0332 -0.2299 1168 LEU A CG  
8910  C CD1 . LEU A 1168 ? 1.3236 1.5692 1.1313 0.0855  -0.0292 -0.2096 1168 LEU A CD1 
8911  C CD2 . LEU A 1168 ? 1.2934 1.5285 1.1004 0.0289  -0.0301 -0.2542 1168 LEU A CD2 
8912  N N   . ILE A 1169 ? 1.6284 1.7407 1.2969 -0.0648 -0.0431 -0.2546 1169 ILE A N   
8913  C CA  . ILE A 1169 ? 1.5947 1.7170 1.2654 -0.1110 -0.0414 -0.2643 1169 ILE A CA  
8914  C C   . ILE A 1169 ? 1.6212 1.7253 1.2720 -0.1507 -0.0397 -0.2920 1169 ILE A C   
8915  O O   . ILE A 1169 ? 1.5767 1.7254 1.2691 -0.1785 -0.0324 -0.3114 1169 ILE A O   
8916  C CB  . ILE A 1169 ? 1.6156 1.6990 1.2420 -0.1134 -0.0490 -0.2440 1169 ILE A CB  
8917  C CG1 . ILE A 1169 ? 1.5454 1.6785 1.2154 -0.0994 -0.0477 -0.2238 1169 ILE A CG1 
8918  C CG2 . ILE A 1169 ? 1.6469 1.6989 1.2351 -0.1648 -0.0503 -0.2584 1169 ILE A CG2 
8919  C CD1 . ILE A 1169 ? 1.5660 1.6714 1.2054 -0.0687 -0.0571 -0.1948 1169 ILE A CD1 
8920  N N   . LYS A 1170 ? 1.7021 1.7413 1.2888 -0.1525 -0.0460 -0.2943 1170 LYS A N   
8921  C CA  . LYS A 1170 ? 1.7619 1.7822 1.3244 -0.1901 -0.0451 -0.3204 1170 LYS A CA  
8922  C C   . LYS A 1170 ? 1.6587 1.7405 1.2839 -0.1923 -0.0385 -0.3401 1170 LYS A C   
8923  O O   . LYS A 1170 ? 1.6275 1.7313 1.2671 -0.2304 -0.0341 -0.3642 1170 LYS A O   
8924  C CB  . LYS A 1170 ? 1.9082 1.8553 1.4004 -0.1774 -0.0523 -0.3183 1170 LYS A CB  
8925  C CG  . LYS A 1170 ? 2.0675 1.9414 1.4870 -0.1750 -0.0600 -0.3005 1170 LYS A CG  
8926  C CD  . LYS A 1170 ? 2.1754 2.0402 1.5747 -0.2252 -0.0600 -0.3081 1170 LYS A CD  
8927  C CE  . LYS A 1170 ? 2.2702 2.1126 1.6358 -0.2745 -0.0580 -0.3359 1170 LYS A CE  
8928  N NZ  . LYS A 1170 ? 2.3074 2.1443 1.6545 -0.3276 -0.0560 -0.3454 1170 LYS A NZ  
8929  N N   . ALA A 1171 ? 1.6126 1.7219 1.2744 -0.1503 -0.0382 -0.3296 1171 ALA A N   
8930  C CA  . ALA A 1171 ? 1.5770 1.7435 1.2993 -0.1460 -0.0337 -0.3446 1171 ALA A CA  
8931  C C   . ALA A 1171 ? 1.5301 1.7572 1.3114 -0.1648 -0.0253 -0.3509 1171 ALA A C   
8932  O O   . ALA A 1171 ? 1.5129 1.7721 1.3224 -0.1954 -0.0202 -0.3742 1171 ALA A O   
8933  C CB  . ALA A 1171 ? 1.5748 1.7478 1.3129 -0.0974 -0.0357 -0.3298 1171 ALA A CB  
8934  N N   . ASP A 1172 ? 1.5256 1.7692 1.3252 -0.1462 -0.0234 -0.3303 1172 ASP A N   
8935  C CA  . ASP A 1172 ? 1.4891 1.7838 1.3377 -0.1634 -0.0150 -0.3332 1172 ASP A CA  
8936  C C   . ASP A 1172 ? 1.5049 1.8003 1.3458 -0.2146 -0.0099 -0.3537 1172 ASP A C   
8937  O O   . ASP A 1172 ? 1.4523 1.7938 1.3391 -0.2354 -0.0006 -0.3702 1172 ASP A O   
8938  C CB  . ASP A 1172 ? 1.5138 1.8073 1.3579 -0.1472 -0.0163 -0.3060 1172 ASP A CB  
8939  C CG  . ASP A 1172 ? 1.4984 1.8364 1.3910 -0.1147 -0.0129 -0.2936 1172 ASP A CG  
8940  O OD1 . ASP A 1172 ? 1.4755 1.8390 1.4012 -0.1009 -0.0105 -0.3046 1172 ASP A OD1 
8941  O OD2 . ASP A 1172 ? 1.5126 1.8602 1.4086 -0.1042 -0.0132 -0.2724 1172 ASP A OD2 
8942  N N   . ASN A 1173 ? 1.5778 1.8191 1.3575 -0.2346 -0.0154 -0.3523 1173 ASN A N   
8943  C CA  . ASN A 1173 ? 1.6227 1.8542 1.3817 -0.2864 -0.0110 -0.3707 1173 ASN A CA  
8944  C C   . ASN A 1173 ? 1.5741 1.8393 1.3640 -0.3099 -0.0044 -0.4018 1173 ASN A C   
8945  O O   . ASN A 1173 ? 1.5437 1.8533 1.3747 -0.3365 0.0063  -0.4188 1173 ASN A O   
8946  C CB  . ASN A 1173 ? 1.7638 1.9211 1.4423 -0.2998 -0.0200 -0.3633 1173 ASN A CB  
8947  C CG  . ASN A 1173 ? 1.8639 1.9961 1.5130 -0.3068 -0.0237 -0.3420 1173 ASN A CG  
8948  O OD1 . ASN A 1173 ? 1.9534 2.0360 1.5447 -0.3371 -0.0279 -0.3428 1173 ASN A OD1 
8949  N ND2 . ASN A 1173 ? 1.8389 2.0051 1.5257 -0.2805 -0.0229 -0.3226 1173 ASN A ND2 
8950  N N   . PHE A 1174 ? 1.5710 1.8167 1.3421 -0.2991 -0.0106 -0.4092 1174 PHE A N   
8951  C CA  . PHE A 1174 ? 1.5351 1.8163 1.3369 -0.3182 -0.0068 -0.4376 1174 PHE A CA  
8952  C C   . PHE A 1174 ? 1.4356 1.7889 1.3163 -0.3135 0.0027  -0.4488 1174 PHE A C   
8953  O O   . PHE A 1174 ? 1.4312 1.8214 1.3415 -0.3458 0.0115  -0.4734 1174 PHE A O   
8954  C CB  . PHE A 1174 ? 1.5449 1.8049 1.3286 -0.2924 -0.0164 -0.4372 1174 PHE A CB  
8955  C CG  . PHE A 1174 ? 1.4987 1.8017 1.3198 -0.3060 -0.0152 -0.4637 1174 PHE A CG  
8956  C CD1 . PHE A 1174 ? 1.5311 1.8239 1.3244 -0.3481 -0.0148 -0.4856 1174 PHE A CD1 
8957  C CD2 . PHE A 1174 ? 1.4384 1.7918 1.3208 -0.2766 -0.0154 -0.4662 1174 PHE A CD2 
8958  C CE1 . PHE A 1174 ? 1.5123 1.8511 1.3436 -0.3597 -0.0148 -0.5096 1174 PHE A CE1 
8959  C CE2 . PHE A 1174 ? 1.4156 1.8103 1.3340 -0.2864 -0.0164 -0.4894 1174 PHE A CE2 
8960  C CZ  . PHE A 1174 ? 1.4519 1.8424 1.3472 -0.3274 -0.0162 -0.5111 1174 PHE A CZ  
8961  N N   . LEU A 1175 ? 1.3766 1.7487 1.2893 -0.2735 0.0016  -0.4311 1175 LEU A N   
8962  C CA  . LEU A 1175 ? 1.3121 1.7453 1.2946 -0.2643 0.0096  -0.4400 1175 LEU A CA  
8963  C C   . LEU A 1175 ? 1.2874 1.7482 1.2934 -0.2972 0.0228  -0.4490 1175 LEU A C   
8964  O O   . LEU A 1175 ? 1.2464 1.7508 1.2962 -0.3150 0.0321  -0.4723 1175 LEU A O   
8965  C CB  . LEU A 1175 ? 1.2922 1.7328 1.2948 -0.2166 0.0055  -0.4173 1175 LEU A CB  
8966  C CG  . LEU A 1175 ? 1.2990 1.7213 1.2889 -0.1819 -0.0054 -0.4110 1175 LEU A CG  
8967  C CD1 . LEU A 1175 ? 1.2687 1.6976 1.2749 -0.1392 -0.0071 -0.3878 1175 LEU A CD1 
8968  C CD2 . LEU A 1175 ? 1.2799 1.7338 1.3028 -0.1868 -0.0072 -0.4354 1175 LEU A CD2 
8969  N N   . LEU A 1176 ? 1.3097 1.7450 1.2862 -0.3048 0.0235  -0.4306 1176 LEU A N   
8970  C CA  . LEU A 1176 ? 1.3082 1.7596 1.2941 -0.3418 0.0354  -0.4385 1176 LEU A CA  
8971  C C   . LEU A 1176 ? 1.3934 1.8488 1.3717 -0.3869 0.0422  -0.4679 1176 LEU A C   
8972  O O   . LEU A 1176 ? 1.3900 1.8874 1.4090 -0.4101 0.0557  -0.4899 1176 LEU A O   
8973  C CB  . LEU A 1176 ? 1.2856 1.6954 1.2227 -0.3493 0.0305  -0.4148 1176 LEU A CB  
8974  C CG  . LEU A 1176 ? 1.2207 1.6317 1.1651 -0.3105 0.0250  -0.3850 1176 LEU A CG  
8975  C CD1 . LEU A 1176 ? 1.2437 1.6192 1.1424 -0.3247 0.0200  -0.3647 1176 LEU A CD1 
8976  C CD2 . LEU A 1176 ? 1.1609 1.6244 1.1644 -0.3045 0.0358  -0.3887 1176 LEU A CD2 
8977  N N   . GLU A 1177 ? 1.4740 1.8835 1.3969 -0.3994 0.0336  -0.4683 1177 GLU A N   
8978  C CA  . GLU A 1177 ? 1.5424 1.9457 1.4429 -0.4472 0.0389  -0.4936 1177 GLU A CA  
8979  C C   . GLU A 1177 ? 1.5198 1.9691 1.4642 -0.4506 0.0426  -0.5214 1177 GLU A C   
8980  O O   . GLU A 1177 ? 1.5641 2.0240 1.5032 -0.4924 0.0499  -0.5463 1177 GLU A O   
8981  C CB  . GLU A 1177 ? 1.6681 2.0010 1.4885 -0.4587 0.0273  -0.4840 1177 GLU A CB  
8982  C CG  . GLU A 1177 ? 1.7711 2.0561 1.5382 -0.4775 0.0250  -0.4658 1177 GLU A CG  
8983  C CD  . GLU A 1177 ? 1.9098 2.1296 1.5977 -0.5085 0.0180  -0.4689 1177 GLU A CD  
8984  O OE1 . GLU A 1177 ? 1.9665 2.1640 1.6195 -0.5517 0.0224  -0.4738 1177 GLU A OE1 
8985  O OE2 . GLU A 1177 ? 1.9603 2.1482 1.6174 -0.4914 0.0083  -0.4670 1177 GLU A OE2 
8986  N N   . ASN A 1178 ? 1.4542 1.9324 1.4417 -0.4087 0.0376  -0.5177 1178 ASN A N   
8987  C CA  . ASN A 1178 ? 1.4013 1.9189 1.4256 -0.4071 0.0365  -0.5410 1178 ASN A CA  
8988  C C   . ASN A 1178 ? 1.3133 1.8903 1.4122 -0.3768 0.0395  -0.5482 1178 ASN A C   
8989  O O   . ASN A 1178 ? 1.3021 1.9108 1.4309 -0.3709 0.0354  -0.5648 1178 ASN A O   
8990  C CB  . ASN A 1178 ? 1.4142 1.8920 1.3941 -0.3935 0.0212  -0.5345 1178 ASN A CB  
8991  C CG  . ASN A 1178 ? 1.4315 1.8986 1.3783 -0.4372 0.0215  -0.5564 1178 ASN A CG  
8992  O OD1 . ASN A 1178 ? 1.4052 1.9239 1.3935 -0.4576 0.0276  -0.5831 1178 ASN A OD1 
8993  N ND2 . ASN A 1178 ? 1.4844 1.8845 1.3549 -0.4523 0.0149  -0.5458 1178 ASN A ND2 
8994  N N   . THR A 1179 ? 1.2485 1.8391 1.3751 -0.3587 0.0459  -0.5355 1179 THR A N   
8995  C CA  . THR A 1179 ? 1.1713 1.8117 1.3635 -0.3323 0.0500  -0.5420 1179 THR A CA  
8996  C C   . THR A 1179 ? 1.1182 1.8075 1.3560 -0.3620 0.0668  -0.5709 1179 THR A C   
8997  O O   . THR A 1179 ? 1.0720 1.8053 1.3557 -0.3574 0.0678  -0.5921 1179 THR A O   
8998  C CB  . THR A 1179 ? 0.9752 1.6072 1.1733 -0.3042 0.0514  -0.5163 1179 THR A CB  
8999  O OG1 . THR A 1179 ? 1.0122 1.5981 1.1643 -0.2803 0.0385  -0.4889 1179 THR A OG1 
9000  C CG2 . THR A 1179 ? 0.8287 1.5015 1.0857 -0.2718 0.0534  -0.5192 1179 THR A CG2 
9001  N N   . LEU A 1180 ? 1.1264 1.8065 1.3487 -0.3938 0.0797  -0.5717 1180 LEU A N   
9002  C CA  . LEU A 1180 ? 1.1033 1.8215 1.3718 -0.4022 0.0972  -0.5845 1180 LEU A CA  
9003  C C   . LEU A 1180 ? 1.1549 1.9277 1.4759 -0.4197 0.1107  -0.6191 1180 LEU A C   
9004  O O   . LEU A 1180 ? 1.1396 1.9455 1.5089 -0.4054 0.1211  -0.6264 1180 LEU A O   
9005  C CB  . LEU A 1180 ? 1.0694 1.7618 1.3074 -0.4273 0.1068  -0.5722 1180 LEU A CB  
9006  C CG  . LEU A 1180 ? 0.9919 1.6829 1.2456 -0.3905 0.1046  -0.5481 1180 LEU A CG  
9007  C CD1 . LEU A 1180 ? 0.9831 1.6542 1.2122 -0.4114 0.1128  -0.5333 1180 LEU A CD1 
9008  C CD2 . LEU A 1180 ? 0.9328 1.6699 1.2499 -0.3674 0.1118  -0.5632 1180 LEU A CD2 
9009  N N   . PRO A 1181 ? 1.1842 1.9668 1.4954 -0.4510 0.1113  -0.6407 1181 PRO A N   
9010  C CA  . PRO A 1181 ? 1.1457 1.9899 1.5160 -0.4559 0.1195  -0.6727 1181 PRO A CA  
9011  C C   . PRO A 1181 ? 1.1165 1.9769 1.5184 -0.4068 0.1028  -0.6650 1181 PRO A C   
9012  O O   . PRO A 1181 ? 1.1150 1.9781 1.5090 -0.4036 0.0891  -0.6691 1181 PRO A O   
9013  C CB  . PRO A 1181 ? 1.1519 1.9946 1.4923 -0.4983 0.1192  -0.6911 1181 PRO A CB  
9014  C CG  . PRO A 1181 ? 1.1939 1.9737 1.4609 -0.5254 0.1179  -0.6732 1181 PRO A CG  
9015  C CD  . PRO A 1181 ? 1.2056 1.9456 1.4525 -0.4851 0.1058  -0.6382 1181 PRO A CD  
9016  N N   . ALA A 1182 ? 1.0955 1.9618 1.5271 -0.3708 0.1036  -0.6525 1182 ALA A N   
9017  C CA  . ALA A 1182 ? 1.0561 1.9212 1.5031 -0.3222 0.0864  -0.6368 1182 ALA A CA  
9018  C C   . ALA A 1182 ? 1.0702 1.9853 1.5669 -0.3093 0.0798  -0.6590 1182 ALA A C   
9019  O O   . ALA A 1182 ? 1.0719 2.0361 1.6193 -0.3180 0.0927  -0.6845 1182 ALA A O   
9020  C CB  . ALA A 1182 ? 0.9828 1.8426 1.4475 -0.2932 0.0912  -0.6206 1182 ALA A CB  
9021  N N   . GLN A 1183 ? 1.0671 1.9697 1.5483 -0.2888 0.0595  -0.6492 1183 GLN A N   
9022  C CA  . GLN A 1183 ? 1.0176 1.9649 1.5389 -0.2781 0.0489  -0.6674 1183 GLN A CA  
9023  C C   . GLN A 1183 ? 0.9309 1.8953 1.4935 -0.2293 0.0381  -0.6600 1183 GLN A C   
9024  O O   . GLN A 1183 ? 0.9122 1.9284 1.5307 -0.2184 0.0369  -0.6797 1183 GLN A O   
9025  C CB  . GLN A 1183 ? 1.0773 2.0008 1.5538 -0.2902 0.0330  -0.6637 1183 GLN A CB  
9026  C CG  . GLN A 1183 ? 1.1115 2.0865 1.6260 -0.2926 0.0238  -0.6860 1183 GLN A CG  
9027  C CD  . GLN A 1183 ? 1.1242 2.1608 1.6893 -0.3212 0.0413  -0.7184 1183 GLN A CD  
9028  O OE1 . GLN A 1183 ? 1.1300 2.1631 1.6920 -0.3451 0.0612  -0.7245 1183 GLN A OE1 
9029  N NE2 . GLN A 1183 ? 1.1179 2.2132 1.7303 -0.3196 0.0341  -0.7398 1183 GLN A NE2 
9030  N N   . SER A 1184 ? 0.8866 1.8075 1.4208 -0.2001 0.0300  -0.6315 1184 SER A N   
9031  C CA  . SER A 1184 ? 0.8428 1.7713 1.4095 -0.1571 0.0238  -0.6222 1184 SER A CA  
9032  C C   . SER A 1184 ? 0.8199 1.7106 1.3643 -0.1414 0.0300  -0.5976 1184 SER A C   
9033  O O   . SER A 1184 ? 0.8273 1.6754 1.3218 -0.1477 0.0287  -0.5772 1184 SER A O   
9034  C CB  . SER A 1184 ? 0.8713 1.7922 1.4319 -0.1275 0.0004  -0.6122 1184 SER A CB  
9035  O OG  . SER A 1184 ? 0.8719 1.7664 1.4266 -0.0907 -0.0056 -0.5895 1184 SER A OG  
9036  N N   . THR A 1185 ? 0.7716 1.6783 1.3528 -0.1199 0.0359  -0.5994 1185 THR A N   
9037  C CA  . THR A 1185 ? 0.7502 1.6255 1.3139 -0.1017 0.0396  -0.5761 1185 THR A CA  
9038  C C   . THR A 1185 ? 0.7613 1.5956 1.2820 -0.0791 0.0236  -0.5477 1185 THR A C   
9039  O O   . THR A 1185 ? 0.7383 1.5403 1.2227 -0.0823 0.0279  -0.5268 1185 THR A O   
9040  C CB  . THR A 1185 ? 0.7195 1.6143 1.3261 -0.0737 0.0413  -0.5821 1185 THR A CB  
9041  O OG1 . THR A 1185 ? 0.6970 1.6255 1.3410 -0.0933 0.0601  -0.6072 1185 THR A OG1 
9042  C CG2 . THR A 1185 ? 0.7111 1.5708 1.2942 -0.0544 0.0426  -0.5564 1185 THR A CG2 
9043  N N   . PHE A 1186 ? 0.7858 1.6234 1.3116 -0.0564 0.0053  -0.5475 1186 PHE A N   
9044  C CA  . PHE A 1186 ? 0.7965 1.5959 1.2795 -0.0377 -0.0095 -0.5243 1186 PHE A CA  
9045  C C   . PHE A 1186 ? 0.8470 1.6152 1.2797 -0.0616 -0.0073 -0.5150 1186 PHE A C   
9046  O O   . PHE A 1186 ? 0.8767 1.6105 1.2733 -0.0541 -0.0062 -0.4921 1186 PHE A O   
9047  C CB  . PHE A 1186 ? 0.7581 1.5677 1.2515 -0.0188 -0.0292 -0.5299 1186 PHE A CB  
9048  C CG  . PHE A 1186 ? 0.7516 1.5194 1.1977 -0.0019 -0.0429 -0.5079 1186 PHE A CG  
9049  C CD1 . PHE A 1186 ? 0.7417 1.4901 1.1811 0.0312  -0.0507 -0.4897 1186 PHE A CD1 
9050  C CD2 . PHE A 1186 ? 0.7724 1.5167 1.1768 -0.0199 -0.0465 -0.5056 1186 PHE A CD2 
9051  C CE1 . PHE A 1186 ? 0.7520 1.4622 1.1474 0.0462  -0.0608 -0.4704 1186 PHE A CE1 
9052  C CE2 . PHE A 1186 ? 0.7927 1.4956 1.1518 -0.0032 -0.0570 -0.4861 1186 PHE A CE2 
9053  C CZ  . PHE A 1186 ? 0.7814 1.4690 1.1375 0.0300  -0.0634 -0.4688 1186 PHE A CZ  
9054  N N   . THR A 1187 ? 0.8628 1.6426 1.2918 -0.0897 -0.0074 -0.5327 1187 THR A N   
9055  C CA  . THR A 1187 ? 0.8636 1.6099 1.2414 -0.1159 -0.0048 -0.5262 1187 THR A CA  
9056  C C   . THR A 1187 ? 0.8471 1.5755 1.2076 -0.1281 0.0095  -0.5133 1187 THR A C   
9057  O O   . THR A 1187 ? 0.8605 1.5493 1.1759 -0.1247 0.0073  -0.4919 1187 THR A O   
9058  C CB  . THR A 1187 ? 0.8558 1.6235 1.2374 -0.1540 -0.0012 -0.5515 1187 THR A CB  
9059  O OG1 . THR A 1187 ? 0.8375 1.6353 1.2469 -0.1454 -0.0137 -0.5668 1187 THR A OG1 
9060  C CG2 . THR A 1187 ? 0.8920 1.6143 1.2109 -0.1766 -0.0030 -0.5429 1187 THR A CG2 
9061  N N   . LEU A 1188 ? 0.7918 1.5504 1.1885 -0.1418 0.0240  -0.5266 1188 LEU A N   
9062  C CA  . LEU A 1188 ? 0.7848 1.5316 1.1680 -0.1598 0.0384  -0.5178 1188 LEU A CA  
9063  C C   . LEU A 1188 ? 0.7769 1.4972 1.1400 -0.1323 0.0344  -0.4888 1188 LEU A C   
9064  O O   . LEU A 1188 ? 0.7933 1.4828 1.1161 -0.1378 0.0341  -0.4699 1188 LEU A O   
9065  C CB  . LEU A 1188 ? 0.7597 1.5430 1.1892 -0.1705 0.0541  -0.5364 1188 LEU A CB  
9066  C CG  . LEU A 1188 ? 0.7106 1.4878 1.1294 -0.1994 0.0714  -0.5345 1188 LEU A CG  
9067  C CD1 . LEU A 1188 ? 0.7083 1.4775 1.0995 -0.2424 0.0774  -0.5457 1188 LEU A CD1 
9068  C CD2 . LEU A 1188 ? 0.6672 1.4774 1.1334 -0.1991 0.0854  -0.5520 1188 LEU A CD2 
9069  N N   . ALA A 1189 ? 0.7524 1.4858 1.1442 -0.1021 0.0310  -0.4856 1189 ALA A N   
9070  C CA  . ALA A 1189 ? 0.7853 1.4994 1.1631 -0.0759 0.0284  -0.4598 1189 ALA A CA  
9071  C C   . ALA A 1189 ? 0.7881 1.4661 1.1192 -0.0626 0.0184  -0.4362 1189 ALA A C   
9072  O O   . ALA A 1189 ? 0.7683 1.4305 1.0780 -0.0585 0.0218  -0.4150 1189 ALA A O   
9073  C CB  . ALA A 1189 ? 0.7732 1.5016 1.1828 -0.0444 0.0223  -0.4620 1189 ALA A CB  
9074  N N   . ILE A 1190 ? 0.8418 1.5075 1.1570 -0.0552 0.0062  -0.4397 1190 ILE A N   
9075  C CA  . ILE A 1190 ? 0.8831 1.5110 1.1515 -0.0425 -0.0017 -0.4193 1190 ILE A CA  
9076  C C   . ILE A 1190 ? 0.9000 1.5093 1.1366 -0.0702 0.0050  -0.4148 1190 ILE A C   
9077  O O   . ILE A 1190 ? 0.8978 1.4898 1.1117 -0.0646 0.0077  -0.3936 1190 ILE A O   
9078  C CB  . ILE A 1190 ? 0.8856 1.4993 1.1384 -0.0306 -0.0158 -0.4246 1190 ILE A CB  
9079  C CG1 . ILE A 1190 ? 0.8692 1.4977 1.1497 -0.0013 -0.0242 -0.4254 1190 ILE A CG1 
9080  C CG2 . ILE A 1190 ? 0.9117 1.4809 1.1115 -0.0181 -0.0213 -0.4044 1190 ILE A CG2 
9081  C CD1 . ILE A 1190 ? 0.8962 1.5018 1.1511 0.0161  -0.0387 -0.4218 1190 ILE A CD1 
9082  N N   . SER A 1191 ? 0.9225 1.5376 1.1585 -0.1014 0.0077  -0.4350 1191 SER A N   
9083  C CA  . SER A 1191 ? 0.9149 1.5115 1.1202 -0.1320 0.0142  -0.4328 1191 SER A CA  
9084  C C   . SER A 1191 ? 0.8828 1.4820 1.0908 -0.1316 0.0228  -0.4154 1191 SER A C   
9085  O O   . SER A 1191 ? 0.8797 1.4513 1.0517 -0.1300 0.0210  -0.3952 1191 SER A O   
9086  C CB  . SER A 1191 ? 0.9104 1.5284 1.1315 -0.1704 0.0218  -0.4605 1191 SER A CB  
9087  O OG  . SER A 1191 ? 0.9448 1.5301 1.1188 -0.1984 0.0217  -0.4593 1191 SER A OG  
9088  N N   . ALA A 1192 ? 0.8428 1.4749 1.0926 -0.1319 0.0318  -0.4227 1192 ALA A N   
9089  C CA  . ALA A 1192 ? 0.8118 1.4486 1.0647 -0.1339 0.0403  -0.4071 1192 ALA A CA  
9090  C C   . ALA A 1192 ? 0.8669 1.4866 1.0997 -0.1020 0.0330  -0.3783 1192 ALA A C   
9091  O O   . ALA A 1192 ? 0.9066 1.5081 1.1092 -0.1063 0.0322  -0.3597 1192 ALA A O   
9092  C CB  . ALA A 1192 ? 0.7469 1.4164 1.0447 -0.1354 0.0506  -0.4203 1192 ALA A CB  
9093  N N   . TYR A 1193 ? 0.8556 1.4814 1.1042 -0.0701 0.0273  -0.3747 1193 TYR A N   
9094  C CA  . TYR A 1193 ? 0.8522 1.4662 1.0844 -0.0407 0.0226  -0.3489 1193 TYR A CA  
9095  C C   . TYR A 1193 ? 0.8827 1.4647 1.0713 -0.0351 0.0158  -0.3335 1193 TYR A C   
9096  O O   . TYR A 1193 ? 0.9134 1.4888 1.0859 -0.0208 0.0155  -0.3109 1193 TYR A O   
9097  C CB  . TYR A 1193 ? 0.8415 1.4596 1.0891 -0.0088 0.0158  -0.3491 1193 TYR A CB  
9098  C CG  . TYR A 1193 ? 0.8405 1.4451 1.0671 0.0198  0.0119  -0.3240 1193 TYR A CG  
9099  C CD1 . TYR A 1193 ? 0.8514 1.4683 1.0824 0.0227  0.0187  -0.3071 1193 TYR A CD1 
9100  C CD2 . TYR A 1193 ? 0.8344 1.4141 1.0346 0.0418  0.0025  -0.3175 1193 TYR A CD2 
9101  C CE1 . TYR A 1193 ? 0.8570 1.4672 1.0707 0.0475  0.0165  -0.2847 1193 TYR A CE1 
9102  C CE2 . TYR A 1193 ? 0.8428 1.4119 1.0241 0.0680  0.0012  -0.2954 1193 TYR A CE2 
9103  C CZ  . TYR A 1193 ? 0.8397 1.4268 1.0297 0.0709  0.0084  -0.2792 1193 TYR A CZ  
9104  O OH  . TYR A 1193 ? 0.8126 1.3964 0.9876 0.0950  0.0086  -0.2580 1193 TYR A OH  
9105  N N   . ALA A 1194 ? 0.8509 1.4131 1.0193 -0.0468 0.0107  -0.3459 1194 ALA A N   
9106  C CA  . ALA A 1194 ? 0.8672 1.3913 0.9892 -0.0388 0.0038  -0.3325 1194 ALA A CA  
9107  C C   . ALA A 1194 ? 0.8496 1.3612 0.9472 -0.0576 0.0071  -0.3199 1194 ALA A C   
9108  O O   . ALA A 1194 ? 0.8620 1.3490 0.9275 -0.0412 0.0026  -0.2995 1194 ALA A O   
9109  C CB  . ALA A 1194 ? 0.9013 1.4041 1.0040 -0.0477 -0.0029 -0.3499 1194 ALA A CB  
9110  N N   . LEU A 1195 ? 0.8345 1.3625 0.9464 -0.0921 0.0146  -0.3325 1195 LEU A N   
9111  C CA  . LEU A 1195 ? 0.8317 1.3483 0.9204 -0.1154 0.0171  -0.3221 1195 LEU A CA  
9112  C C   . LEU A 1195 ? 0.8318 1.3701 0.9363 -0.1015 0.0205  -0.3010 1195 LEU A C   
9113  O O   . LEU A 1195 ? 0.8638 1.3894 0.9449 -0.0903 0.0161  -0.2783 1195 LEU A O   
9114  C CB  . LEU A 1195 ? 0.7933 1.3208 0.8917 -0.1589 0.0255  -0.3443 1195 LEU A CB  
9115  C CG  . LEU A 1195 ? 0.8267 1.3419 0.9159 -0.1745 0.0231  -0.3687 1195 LEU A CG  
9116  C CD1 . LEU A 1195 ? 0.8112 1.3544 0.9295 -0.2101 0.0341  -0.3961 1195 LEU A CD1 
9117  C CD2 . LEU A 1195 ? 0.8701 1.3370 0.9023 -0.1842 0.0150  -0.3626 1195 LEU A CD2 
9118  N N   . SER A 1196 ? 0.8143 1.3854 0.9583 -0.1003 0.0278  -0.3085 1196 SER A N   
9119  C CA  . SER A 1196 ? 0.8235 1.4166 0.9838 -0.0850 0.0312  -0.2901 1196 SER A CA  
9120  C C   . SER A 1196 ? 0.8785 1.4599 1.0157 -0.0550 0.0238  -0.2632 1196 SER A C   
9121  O O   . SER A 1196 ? 0.8431 1.4406 0.9827 -0.0511 0.0257  -0.2436 1196 SER A O   
9122  C CB  . SER A 1196 ? 0.7980 1.4121 0.9931 -0.0698 0.0347  -0.3013 1196 SER A CB  
9123  O OG  . SER A 1196 ? 0.7996 1.4261 1.0011 -0.0468 0.0350  -0.2822 1196 SER A OG  
9124  N N   . LEU A 1197 ? 1.0029 1.5568 1.1171 -0.0342 0.0158  -0.2628 1197 LEU A N   
9125  C CA  . LEU A 1197 ? 1.1346 1.6748 1.2259 -0.0028 0.0101  -0.2396 1197 LEU A CA  
9126  C C   . LEU A 1197 ? 1.2362 1.7438 1.2873 -0.0092 0.0040  -0.2300 1197 LEU A C   
9127  O O   . LEU A 1197 ? 1.2637 1.7390 1.2844 0.0126  -0.0022 -0.2243 1197 LEU A O   
9128  C CB  . LEU A 1197 ? 1.1800 1.7067 1.2676 0.0290  0.0059  -0.2429 1197 LEU A CB  
9129  C CG  . LEU A 1197 ? 1.1944 1.7439 1.3159 0.0356  0.0089  -0.2555 1197 LEU A CG  
9130  C CD1 . LEU A 1197 ? 1.2353 1.7648 1.3442 0.0650  0.0028  -0.2568 1197 LEU A CD1 
9131  C CD2 . LEU A 1197 ? 1.1766 1.7597 1.3237 0.0396  0.0155  -0.2432 1197 LEU A CD2 
9132  N N   . GLY A 1198 ? 1.3051 1.8173 1.3525 -0.0397 0.0058  -0.2284 1198 GLY A N   
9133  C CA  . GLY A 1198 ? 1.4086 1.8866 1.4151 -0.0485 -0.0013 -0.2193 1198 GLY A CA  
9134  C C   . GLY A 1198 ? 1.4370 1.9317 1.4466 -0.0781 0.0008  -0.2108 1198 GLY A C   
9135  O O   . GLY A 1198 ? 1.4501 1.9763 1.4784 -0.0705 0.0025  -0.1931 1198 GLY A O   
9136  N N   . ASP A 1199 ? 1.4362 1.9096 1.4254 -0.1145 0.0006  -0.2236 1199 ASP A N   
9137  C CA  . ASP A 1199 ? 1.3846 1.8731 1.3772 -0.1506 0.0044  -0.2209 1199 ASP A CA  
9138  C C   . ASP A 1199 ? 1.2444 1.7625 1.2735 -0.1770 0.0174  -0.2438 1199 ASP A C   
9139  O O   . ASP A 1199 ? 1.2388 1.7463 1.2674 -0.1973 0.0217  -0.2686 1199 ASP A O   
9140  C CB  . ASP A 1199 ? 1.4862 1.9339 1.4339 -0.1795 -0.0018 -0.2228 1199 ASP A CB  
9141  C CG  . ASP A 1199 ? 1.5442 2.0050 1.4944 -0.2234 0.0038  -0.2259 1199 ASP A CG  
9142  O OD1 . ASP A 1199 ? 1.5121 2.0117 1.4934 -0.2262 0.0100  -0.2183 1199 ASP A OD1 
9143  O OD2 . ASP A 1199 ? 1.6170 2.0470 1.5350 -0.2569 0.0026  -0.2363 1199 ASP A OD2 
9144  N N   . LYS A 1200 ? 1.1155 1.6705 1.1751 -0.1769 0.0241  -0.2361 1200 LYS A N   
9145  C CA  . LYS A 1200 ? 1.0331 1.6131 1.1263 -0.1969 0.0371  -0.2571 1200 LYS A CA  
9146  C C   . LYS A 1200 ? 1.0773 1.6626 1.1649 -0.2410 0.0442  -0.2595 1200 LYS A C   
9147  O O   . LYS A 1200 ? 1.1149 1.7258 1.2266 -0.2551 0.0548  -0.2633 1200 LYS A O   
9148  C CB  . LYS A 1200 ? 0.9526 1.5630 1.0785 -0.1699 0.0411  -0.2502 1200 LYS A CB  
9149  C CG  . LYS A 1200 ? 0.9799 1.5979 1.0971 -0.1424 0.0333  -0.2200 1200 LYS A CG  
9150  C CD  . LYS A 1200 ? 1.0079 1.6429 1.1463 -0.1056 0.0339  -0.2144 1200 LYS A CD  
9151  C CE  . LYS A 1200 ? 1.0130 1.6812 1.1770 -0.1127 0.0430  -0.2099 1200 LYS A CE  
9152  N NZ  . LYS A 1200 ? 1.0120 1.6974 1.1839 -0.0784 0.0408  -0.1917 1200 LYS A NZ  
9153  N N   . THR A 1201 ? 1.0691 1.6259 1.1205 -0.2644 0.0384  -0.2574 1201 THR A N   
9154  C CA  . THR A 1201 ? 1.0344 1.5910 1.0760 -0.3111 0.0457  -0.2635 1201 THR A CA  
9155  C C   . THR A 1201 ? 1.0774 1.6024 1.0898 -0.3433 0.0462  -0.2825 1201 THR A C   
9156  O O   . THR A 1201 ? 1.0848 1.6076 1.0883 -0.3856 0.0544  -0.2927 1201 THR A O   
9157  C CB  . THR A 1201 ? 1.0157 1.5730 1.0367 -0.3187 0.0376  -0.2351 1201 THR A CB  
9158  O OG1 . THR A 1201 ? 1.0341 1.5612 1.0202 -0.2988 0.0214  -0.2174 1201 THR A OG1 
9159  C CG2 . THR A 1201 ? 0.9631 1.5588 1.0135 -0.2997 0.0403  -0.2177 1201 THR A CG2 
9160  N N   . HIS A 1202 ? 1.1349 1.6333 1.1287 -0.3263 0.0381  -0.2878 1202 HIS A N   
9161  C CA  . HIS A 1202 ? 1.2050 1.6759 1.1725 -0.3599 0.0404  -0.3095 1202 HIS A CA  
9162  C C   . HIS A 1202 ? 1.2200 1.7209 1.2227 -0.3894 0.0586  -0.3377 1202 HIS A C   
9163  O O   . HIS A 1202 ? 1.1896 1.7219 1.2358 -0.3696 0.0660  -0.3481 1202 HIS A O   
9164  C CB  . HIS A 1202 ? 1.2070 1.6535 1.1599 -0.3394 0.0333  -0.3188 1202 HIS A CB  
9165  C CG  . HIS A 1202 ? 1.2660 1.6782 1.1802 -0.3766 0.0334  -0.3367 1202 HIS A CG  
9166  N ND1 . HIS A 1202 ? 1.3326 1.6951 1.1947 -0.3711 0.0204  -0.3286 1202 HIS A ND1 
9167  C CD2 . HIS A 1202 ? 1.2658 1.6847 1.1830 -0.4215 0.0457  -0.3627 1202 HIS A CD2 
9168  C CE1 . HIS A 1202 ? 1.3495 1.6883 1.1820 -0.4127 0.0240  -0.3486 1202 HIS A CE1 
9169  N NE2 . HIS A 1202 ? 1.3225 1.6974 1.1893 -0.4441 0.0397  -0.3698 1202 HIS A NE2 
9170  N N   . PRO A 1203 ? 1.2781 1.7678 1.2605 -0.4366 0.0660  -0.3498 1203 PRO A N   
9171  C CA  . PRO A 1203 ? 1.2615 1.7766 1.2715 -0.4712 0.0855  -0.3767 1203 PRO A CA  
9172  C C   . PRO A 1203 ? 1.2172 1.7534 1.2633 -0.4576 0.0925  -0.4039 1203 PRO A C   
9173  O O   . PRO A 1203 ? 1.1957 1.7668 1.2876 -0.4498 0.1046  -0.4176 1203 PRO A O   
9174  C CB  . PRO A 1203 ? 1.3308 1.8149 1.2964 -0.5206 0.0875  -0.3862 1203 PRO A CB  
9175  C CG  . PRO A 1203 ? 1.3611 1.8072 1.2776 -0.5129 0.0684  -0.3552 1203 PRO A CG  
9176  C CD  . PRO A 1203 ? 1.3297 1.7746 1.2544 -0.4595 0.0551  -0.3389 1203 PRO A CD  
9177  N N   . GLN A 1204 ? 1.1691 1.6814 1.1911 -0.4546 0.0836  -0.4104 1204 GLN A N   
9178  C CA  . GLN A 1204 ? 1.0916 1.6198 1.1400 -0.4398 0.0850  -0.4325 1204 GLN A CA  
9179  C C   . GLN A 1204 ? 0.9816 1.5391 1.0749 -0.3928 0.0829  -0.4270 1204 GLN A C   
9180  O O   . GLN A 1204 ? 0.9181 1.5092 1.0553 -0.3896 0.0927  -0.4483 1204 GLN A O   
9181  C CB  . GLN A 1204 ? 1.1240 1.6113 1.1258 -0.4390 0.0714  -0.4298 1204 GLN A CB  
9182  C CG  . GLN A 1204 ? 1.0967 1.5950 1.1156 -0.4282 0.0702  -0.4506 1204 GLN A CG  
9183  C CD  . GLN A 1204 ? 1.0480 1.5827 1.1019 -0.4594 0.0864  -0.4846 1204 GLN A CD  
9184  O OE1 . GLN A 1204 ? 1.0152 1.5628 1.0768 -0.4923 0.1005  -0.4943 1204 GLN A OE1 
9185  N NE2 . GLN A 1204 ? 1.0430 1.5966 1.1197 -0.4493 0.0850  -0.5035 1204 GLN A NE2 
9186  N N   . PHE A 1205 ? 0.9768 1.5215 1.0586 -0.3565 0.0702  -0.3987 1205 PHE A N   
9187  C CA  . PHE A 1205 ? 0.9310 1.5014 1.0510 -0.3153 0.0690  -0.3914 1205 PHE A CA  
9188  C C   . PHE A 1205 ? 0.9014 1.5070 1.0628 -0.3258 0.0845  -0.4028 1205 PHE A C   
9189  O O   . PHE A 1205 ? 0.8856 1.5164 1.0861 -0.3101 0.0894  -0.4191 1205 PHE A O   
9190  C CB  . PHE A 1205 ? 0.8034 1.3604 0.9055 -0.2817 0.0570  -0.3578 1205 PHE A CB  
9191  C CG  . PHE A 1205 ? 0.7337 1.3179 0.8720 -0.2455 0.0578  -0.3488 1205 PHE A CG  
9192  C CD1 . PHE A 1205 ? 0.7315 1.3241 0.8918 -0.2166 0.0545  -0.3584 1205 PHE A CD1 
9193  C CD2 . PHE A 1205 ? 0.6809 1.2799 0.8268 -0.2421 0.0609  -0.3298 1205 PHE A CD2 
9194  C CE1 . PHE A 1205 ? 0.7008 1.3131 0.8882 -0.1855 0.0546  -0.3495 1205 PHE A CE1 
9195  C CE2 . PHE A 1205 ? 0.6454 1.2658 0.8186 -0.2124 0.0620  -0.3215 1205 PHE A CE2 
9196  C CZ  . PHE A 1205 ? 0.6570 1.2824 0.8499 -0.1842 0.0590  -0.3314 1205 PHE A CZ  
9197  N N   . ARG A 1206 ? 0.8938 1.4989 1.0445 -0.3524 0.0917  -0.3945 1206 ARG A N   
9198  C CA  . ARG A 1206 ? 0.8830 1.5150 1.0658 -0.3653 0.1078  -0.4047 1206 ARG A CA  
9199  C C   . ARG A 1206 ? 0.8608 1.5127 1.0742 -0.3840 0.1223  -0.4409 1206 ARG A C   
9200  O O   . ARG A 1206 ? 0.8199 1.4967 1.0708 -0.3776 0.1341  -0.4539 1206 ARG A O   
9201  C CB  . ARG A 1206 ? 0.9430 1.5669 1.1017 -0.3979 0.1130  -0.3911 1206 ARG A CB  
9202  C CG  . ARG A 1206 ? 1.0164 1.6279 1.1491 -0.3805 0.0986  -0.3555 1206 ARG A CG  
9203  C CD  . ARG A 1206 ? 1.0918 1.7161 1.2263 -0.3974 0.1062  -0.3420 1206 ARG A CD  
9204  N NE  . ARG A 1206 ? 1.1689 1.7869 1.2780 -0.3896 0.0929  -0.3081 1206 ARG A NE  
9205  C CZ  . ARG A 1206 ? 1.2366 1.8338 1.3079 -0.4149 0.0853  -0.2949 1206 ARG A CZ  
9206  N NH1 . ARG A 1206 ? 1.2622 1.8380 1.3112 -0.4518 0.0898  -0.3129 1206 ARG A NH1 
9207  N NH2 . ARG A 1206 ? 1.2428 1.8408 1.2971 -0.4034 0.0725  -0.2635 1206 ARG A NH2 
9208  N N   . SER A 1207 ? 0.8501 1.4909 1.0463 -0.4064 0.1212  -0.4570 1207 SER A N   
9209  C CA  . SER A 1207 ? 0.8158 1.4800 1.0412 -0.4240 0.1337  -0.4917 1207 SER A CA  
9210  C C   . SER A 1207 ? 0.7646 1.4515 1.0294 -0.3825 0.1278  -0.4984 1207 SER A C   
9211  O O   . SER A 1207 ? 0.7542 1.4712 1.0625 -0.3751 0.1388  -0.5161 1207 SER A O   
9212  C CB  . SER A 1207 ? 0.8440 1.4889 1.0360 -0.4554 0.1308  -0.5045 1207 SER A CB  
9213  O OG  . SER A 1207 ? 0.8272 1.4979 1.0434 -0.4850 0.1465  -0.5392 1207 SER A OG  
9214  N N   . ILE A 1208 ? 0.7237 1.3930 0.9705 -0.3544 0.1100  -0.4831 1208 ILE A N   
9215  C CA  . ILE A 1208 ? 0.6219 1.3072 0.8979 -0.3177 0.1015  -0.4888 1208 ILE A CA  
9216  C C   . ILE A 1208 ? 0.5249 1.2293 0.8358 -0.2877 0.1047  -0.4819 1208 ILE A C   
9217  O O   . ILE A 1208 ? 0.4693 1.2004 0.8211 -0.2723 0.1079  -0.4994 1208 ILE A O   
9218  C CB  . ILE A 1208 ? 0.6144 1.2699 0.8564 -0.2937 0.0826  -0.4702 1208 ILE A CB  
9219  C CG1 . ILE A 1208 ? 0.6132 1.2317 0.8013 -0.3210 0.0784  -0.4613 1208 ILE A CG1 
9220  C CG2 . ILE A 1208 ? 0.6281 1.2964 0.8880 -0.2799 0.0754  -0.4878 1208 ILE A CG2 
9221  C CD1 . ILE A 1208 ? 0.6157 1.2082 0.7734 -0.3132 0.0649  -0.4617 1208 ILE A CD1 
9222  N N   . VAL A 1209 ? 0.5051 1.1957 0.7983 -0.2805 0.1035  -0.4563 1209 VAL A N   
9223  C CA  . VAL A 1209 ? 0.5345 1.2385 0.8524 -0.2577 0.1075  -0.4481 1209 VAL A CA  
9224  C C   . VAL A 1209 ? 0.6099 1.3356 0.9587 -0.2777 0.1261  -0.4712 1209 VAL A C   
9225  O O   . VAL A 1209 ? 0.6010 1.3407 0.9797 -0.2562 0.1300  -0.4759 1209 VAL A O   
9226  C CB  . VAL A 1209 ? 0.5385 1.2283 0.8304 -0.2568 0.1055  -0.4184 1209 VAL A CB  
9227  C CG1 . VAL A 1209 ? 0.5206 1.2224 0.8342 -0.2353 0.1097  -0.4107 1209 VAL A CG1 
9228  C CG2 . VAL A 1209 ? 0.5614 1.2290 0.8208 -0.2376 0.0889  -0.3950 1209 VAL A CG2 
9229  N N   . SER A 1210 ? 0.6785 1.4036 1.0168 -0.3192 0.1380  -0.4850 1210 SER A N   
9230  C CA  . SER A 1210 ? 0.7380 1.4847 1.1062 -0.3404 0.1578  -0.5123 1210 SER A CA  
9231  C C   . SER A 1210 ? 0.7719 1.5458 1.1817 -0.3217 0.1570  -0.5380 1210 SER A C   
9232  O O   . SER A 1210 ? 0.7765 1.5676 1.2221 -0.2980 0.1614  -0.5467 1210 SER A O   
9233  C CB  . SER A 1210 ? 0.7808 1.5212 1.1271 -0.3901 0.1702  -0.5246 1210 SER A CB  
9234  O OG  . SER A 1210 ? 0.8025 1.5695 1.1832 -0.4073 0.1884  -0.5583 1210 SER A OG  
9235  N N   . ALA A 1211 ? 0.7760 1.5526 1.1791 -0.3323 0.1503  -0.5493 1211 ALA A N   
9236  C CA  . ALA A 1211 ? 0.7620 1.5662 1.2013 -0.3143 0.1453  -0.5703 1211 ALA A CA  
9237  C C   . ALA A 1211 ? 0.7220 1.5345 1.1899 -0.2682 0.1368  -0.5624 1211 ALA A C   
9238  O O   . ALA A 1211 ? 0.6894 1.5272 1.1986 -0.2565 0.1454  -0.5801 1211 ALA A O   
9239  C CB  . ALA A 1211 ? 0.7803 1.5708 1.1920 -0.3166 0.1295  -0.5663 1211 ALA A CB  
9240  N N   . LEU A 1212 ? 0.7440 1.5327 1.1869 -0.2421 0.1202  -0.5354 1212 LEU A N   
9241  C CA  . LEU A 1212 ? 0.7413 1.5322 1.2027 -0.1990 0.1094  -0.5256 1212 LEU A CA  
9242  C C   . LEU A 1212 ? 0.7226 1.5209 1.2073 -0.1911 0.1219  -0.5282 1212 LEU A C   
9243  O O   . LEU A 1212 ? 0.7221 1.5367 1.2416 -0.1659 0.1205  -0.5396 1212 LEU A O   
9244  C CB  . LEU A 1212 ? 0.7264 1.4873 1.1509 -0.1777 0.0942  -0.4937 1212 LEU A CB  
9245  C CG  . LEU A 1212 ? 0.6935 1.4509 1.1285 -0.1372 0.0852  -0.4795 1212 LEU A CG  
9246  C CD1 . LEU A 1212 ? 0.6850 1.4627 1.1555 -0.1146 0.0775  -0.4977 1212 LEU A CD1 
9247  C CD2 . LEU A 1212 ? 0.6968 1.4287 1.0964 -0.1190 0.0715  -0.4522 1212 LEU A CD2 
9248  N N   . LYS A 1213 ? 0.6967 1.4806 1.1594 -0.2136 0.1336  -0.5172 1213 LYS A N   
9249  C CA  . LYS A 1213 ? 0.6645 1.4448 1.1353 -0.2061 0.1437  -0.5122 1213 LYS A CA  
9250  C C   . LYS A 1213 ? 0.7084 1.5109 1.2167 -0.2143 0.1603  -0.5426 1213 LYS A C   
9251  O O   . LYS A 1213 ? 0.7019 1.5035 1.2267 -0.1990 0.1676  -0.5459 1213 LYS A O   
9252  C CB  . LYS A 1213 ? 0.5957 1.3566 1.0306 -0.2315 0.1507  -0.4921 1213 LYS A CB  
9253  C CG  . LYS A 1213 ? 0.5818 1.3324 1.0131 -0.2184 0.1550  -0.4773 1213 LYS A CG  
9254  C CD  . LYS A 1213 ? 0.6025 1.3364 0.9953 -0.2279 0.1499  -0.4466 1213 LYS A CD  
9255  C CE  . LYS A 1213 ? 0.6187 1.3444 1.0021 -0.2336 0.1599  -0.4349 1213 LYS A CE  
9256  N NZ  . LYS A 1213 ? 0.6251 1.3421 0.9796 -0.2263 0.1487  -0.4025 1213 LYS A NZ  
9257  N N   . ARG A 1214 ? 0.7775 1.5989 1.2977 -0.2387 0.1666  -0.5654 1214 ARG A N   
9258  C CA  . ARG A 1214 ? 0.8879 1.7363 1.4463 -0.2492 0.1842  -0.5971 1214 ARG A CA  
9259  C C   . ARG A 1214 ? 0.8915 1.7645 1.4917 -0.2116 0.1729  -0.6102 1214 ARG A C   
9260  O O   . ARG A 1214 ? 0.9115 1.8046 1.5497 -0.2000 0.1831  -0.6308 1214 ARG A O   
9261  C CB  . ARG A 1214 ? 1.0269 1.8879 1.5792 -0.2924 0.1950  -0.6159 1214 ARG A CB  
9262  C CG  . ARG A 1214 ? 1.1684 2.0692 1.7669 -0.3007 0.2095  -0.6530 1214 ARG A CG  
9263  C CD  . ARG A 1214 ? 1.2984 2.2068 1.8825 -0.3507 0.2234  -0.6702 1214 ARG A CD  
9264  N NE  . ARG A 1214 ? 1.3913 2.2774 1.9317 -0.3660 0.2077  -0.6524 1214 ARG A NE  
9265  C CZ  . ARG A 1214 ? 1.4640 2.3369 1.9700 -0.4104 0.2151  -0.6551 1214 ARG A CZ  
9266  N NH1 . ARG A 1214 ? 1.4973 2.3790 2.0078 -0.4463 0.2388  -0.6754 1214 ARG A NH1 
9267  N NH2 . ARG A 1214 ? 1.4875 2.3350 1.9514 -0.4192 0.1992  -0.6376 1214 ARG A NH2 
9268  N N   . GLU A 1215 ? 0.8924 1.7621 1.4841 -0.1910 0.1512  -0.5974 1215 GLU A N   
9269  C CA  . GLU A 1215 ? 0.8558 1.7517 1.4859 -0.1600 0.1384  -0.6108 1215 GLU A CA  
9270  C C   . GLU A 1215 ? 0.8042 1.6939 1.4528 -0.1190 0.1321  -0.6042 1215 GLU A C   
9271  O O   . GLU A 1215 ? 0.8081 1.7238 1.4974 -0.0954 0.1269  -0.6213 1215 GLU A O   
9272  C CB  . GLU A 1215 ? 0.8444 1.7378 1.4570 -0.1552 0.1179  -0.6020 1215 GLU A CB  
9273  C CG  . GLU A 1215 ? 0.8559 1.7712 1.4710 -0.1906 0.1237  -0.6228 1215 GLU A CG  
9274  C CD  . GLU A 1215 ? 0.8728 1.8361 1.5431 -0.1905 0.1325  -0.6559 1215 GLU A CD  
9275  O OE1 . GLU A 1215 ? 0.8781 1.8566 1.5834 -0.1544 0.1252  -0.6597 1215 GLU A OE1 
9276  O OE2 . GLU A 1215 ? 0.8833 1.8693 1.5618 -0.2259 0.1466  -0.6780 1215 GLU A OE2 
9277  N N   . ALA A 1216 ? 0.7278 1.5836 1.3457 -0.1126 0.1331  -0.5802 1216 ALA A N   
9278  C CA  . ALA A 1216 ? 0.6684 1.5068 1.2880 -0.0754 0.1240  -0.5670 1216 ALA A CA  
9279  C C   . ALA A 1216 ? 0.6485 1.4973 1.3043 -0.0592 0.1344  -0.5868 1216 ALA A C   
9280  O O   . ALA A 1216 ? 0.6688 1.5402 1.3504 -0.0781 0.1521  -0.6118 1216 ALA A O   
9281  C CB  . ALA A 1216 ? 0.6479 1.4515 1.2242 -0.0800 0.1253  -0.5381 1216 ALA A CB  
9282  N N   . LEU A 1217 ? 0.6244 1.4542 1.2795 -0.0241 0.1237  -0.5758 1217 LEU A N   
9283  C CA  . LEU A 1217 ? 0.6043 1.4347 1.2878 -0.0025 0.1309  -0.5914 1217 LEU A CA  
9284  C C   . LEU A 1217 ? 0.6173 1.4044 1.2694 0.0135  0.1305  -0.5708 1217 LEU A C   
9285  O O   . LEU A 1217 ? 0.5637 1.3263 1.1785 0.0159  0.1199  -0.5439 1217 LEU A O   
9286  C CB  . LEU A 1217 ? 0.5782 1.4360 1.3033 0.0306  0.1138  -0.6060 1217 LEU A CB  
9287  C CG  . LEU A 1217 ? 0.5517 1.4442 1.2919 0.0199  0.1028  -0.6140 1217 LEU A CG  
9288  C CD1 . LEU A 1217 ? 0.5350 1.4246 1.2739 0.0516  0.0749  -0.6015 1217 LEU A CD1 
9289  C CD2 . LEU A 1217 ? 0.5559 1.4980 1.3461 0.0075  0.1148  -0.6483 1217 LEU A CD2 
9290  N N   . VAL A 1218 ? 0.6737 1.4508 1.3400 0.0255  0.1421  -0.5839 1218 VAL A N   
9291  C CA  . VAL A 1218 ? 0.7254 1.4578 1.3545 0.0291  0.1476  -0.5665 1218 VAL A CA  
9292  C C   . VAL A 1218 ? 0.7294 1.4459 1.3752 0.0639  0.1453  -0.5770 1218 VAL A C   
9293  O O   . VAL A 1218 ? 0.6779 1.4195 1.3667 0.0751  0.1512  -0.6033 1218 VAL A O   
9294  C CB  . VAL A 1218 ? 0.8011 1.5248 1.4145 -0.0080 0.1740  -0.5721 1218 VAL A CB  
9295  C CG1 . VAL A 1218 ? 0.7961 1.5079 1.3666 -0.0389 0.1750  -0.5469 1218 VAL A CG1 
9296  C CG2 . VAL A 1218 ? 0.8551 1.6187 1.5088 -0.0250 0.1878  -0.6022 1218 VAL A CG2 
9297  N N   . LYS A 1219 ? 0.8115 1.4864 1.4225 0.0809  0.1368  -0.5565 1219 LYS A N   
9298  C CA  . LYS A 1219 ? 0.9742 1.6246 1.5927 0.1156  0.1323  -0.5637 1219 LYS A CA  
9299  C C   . LYS A 1219 ? 1.0952 1.7001 1.6751 0.1013  0.1518  -0.5583 1219 LYS A C   
9300  O O   . LYS A 1219 ? 1.1203 1.6995 1.6542 0.0817  0.1534  -0.5347 1219 LYS A O   
9301  C CB  . LYS A 1219 ? 1.0319 1.6669 1.6400 0.1504  0.1034  -0.5465 1219 LYS A CB  
9302  C CG  . LYS A 1219 ? 1.8160 2.4825 2.4732 0.1858  0.0835  -0.5628 1219 LYS A CG  
9303  C CD  . LYS A 1219 ? 1.6348 2.3090 2.2850 0.2003  0.0555  -0.5457 1219 LYS A CD  
9304  C CE  . LYS A 1219 ? 1.4468 2.0927 2.0887 0.2413  0.0306  -0.5365 1219 LYS A CE  
9305  N NZ  . LYS A 1219 ? 1.4255 2.0731 2.0501 0.2480  0.0069  -0.5176 1219 LYS A NZ  
9306  N N   . GLY A 1220 ? 1.1577 1.7549 1.7572 0.1105  0.1671  -0.5811 1220 GLY A N   
9307  C CA  . GLY A 1220 ? 1.2047 1.7535 1.7677 0.1000  0.1868  -0.5803 1220 GLY A CA  
9308  C C   . GLY A 1220 ? 1.2169 1.7680 1.7604 0.0515  0.2124  -0.5816 1220 GLY A C   
9309  O O   . GLY A 1220 ? 1.1944 1.7725 1.7346 0.0242  0.2106  -0.5715 1220 GLY A O   
9310  N N   . ASN A 1221 ? 1.2817 1.8024 1.8101 0.0402  0.2360  -0.5939 1221 ASN A N   
9311  C CA  . ASN A 1221 ? 1.2853 1.8052 1.7915 -0.0086 0.2606  -0.5953 1221 ASN A CA  
9312  C C   . ASN A 1221 ? 1.2731 1.7407 1.7155 -0.0326 0.2701  -0.5745 1221 ASN A C   
9313  O O   . ASN A 1221 ? 1.3184 1.7393 1.7376 -0.0206 0.2790  -0.5791 1221 ASN A O   
9314  C CB  . ASN A 1221 ? 1.3301 1.8642 1.8679 -0.0176 0.2864  -0.6287 1221 ASN A CB  
9315  C CG  . ASN A 1221 ? 1.3407 1.8695 1.8502 -0.0702 0.3110  -0.6292 1221 ASN A CG  
9316  O OD1 . ASN A 1221 ? 1.3735 1.8643 1.8557 -0.0850 0.3333  -0.6368 1221 ASN A OD1 
9317  N ND2 . ASN A 1221 ? 1.3071 1.8692 1.8172 -0.0997 0.3061  -0.6190 1221 ASN A ND2 
9318  N N   . PRO A 1222 ? 1.1949 1.6703 1.6080 -0.0682 0.2691  -0.5524 1222 PRO A N   
9319  C CA  . PRO A 1222 ? 1.1144 1.6376 1.5472 -0.0874 0.2619  -0.5473 1222 PRO A CA  
9320  C C   . PRO A 1222 ? 1.0847 1.6290 1.5358 -0.0550 0.2333  -0.5347 1222 PRO A C   
9321  O O   . PRO A 1222 ? 1.1243 1.6488 1.5771 -0.0182 0.2200  -0.5329 1222 PRO A O   
9322  C CB  . PRO A 1222 ? 1.1137 1.6236 1.4978 -0.1285 0.2675  -0.5223 1222 PRO A CB  
9323  C CG  . PRO A 1222 ? 1.1629 1.6201 1.5026 -0.1329 0.2786  -0.5159 1222 PRO A CG  
9324  C CD  . PRO A 1222 ? 1.1971 1.6307 1.5505 -0.0878 0.2712  -0.5270 1222 PRO A CD  
9325  N N   . PRO A 1223 ? 0.9889 1.5684 1.4489 -0.0687 0.2234  -0.5252 1223 PRO A N   
9326  C CA  . PRO A 1223 ? 0.8903 1.4827 1.3576 -0.0409 0.1973  -0.5103 1223 PRO A CA  
9327  C C   . PRO A 1223 ? 0.8408 1.3963 1.2701 -0.0251 0.1868  -0.4869 1223 PRO A C   
9328  O O   . PRO A 1223 ? 0.8102 1.3486 1.1996 -0.0509 0.1936  -0.4677 1223 PRO A O   
9329  C CB  . PRO A 1223 ? 0.8512 1.4680 1.3079 -0.0695 0.1939  -0.4949 1223 PRO A CB  
9330  C CG  . PRO A 1223 ? 0.8832 1.5170 1.3533 -0.1011 0.2130  -0.5137 1223 PRO A CG  
9331  C CD  . PRO A 1223 ? 0.9730 1.5767 1.4311 -0.1098 0.2345  -0.5262 1223 PRO A CD  
9332  N N   . ILE A 1224 ? 0.8283 1.3721 1.2685 0.0148  0.1704  -0.4886 1224 ILE A N   
9333  C CA  . ILE A 1224 ? 0.8063 1.3240 1.2125 0.0312  0.1541  -0.4637 1224 ILE A CA  
9334  C C   . ILE A 1224 ? 0.7742 1.3175 1.1954 0.0503  0.1313  -0.4540 1224 ILE A C   
9335  O O   . ILE A 1224 ? 0.7732 1.3072 1.1643 0.0513  0.1208  -0.4299 1224 ILE A O   
9336  C CB  . ILE A 1224 ? 0.8196 1.2937 1.2113 0.0585  0.1509  -0.4669 1224 ILE A CB  
9337  C CG1 . ILE A 1224 ? 0.8872 1.3321 1.2585 0.0358  0.1758  -0.4765 1224 ILE A CG1 
9338  C CG2 . ILE A 1224 ? 0.7893 1.2366 1.1404 0.0692  0.1350  -0.4400 1224 ILE A CG2 
9339  C CD1 . ILE A 1224 ? 0.9626 1.3491 1.2911 0.0474  0.1768  -0.4692 1224 ILE A CD1 
9340  N N   . TYR A 1225 ? 0.7272 1.3034 1.1934 0.0632  0.1253  -0.4736 1225 TYR A N   
9341  C CA  . TYR A 1225 ? 0.6817 1.2840 1.1638 0.0774  0.1055  -0.4684 1225 TYR A CA  
9342  C C   . TYR A 1225 ? 0.6321 1.2749 1.1442 0.0567  0.1122  -0.4835 1225 TYR A C   
9343  O O   . TYR A 1225 ? 0.6307 1.2895 1.1731 0.0506  0.1247  -0.5076 1225 TYR A O   
9344  C CB  . TYR A 1225 ? 0.7112 1.3134 1.2192 0.1175  0.0865  -0.4788 1225 TYR A CB  
9345  C CG  . TYR A 1225 ? 0.7642 1.3230 1.2428 0.1423  0.0762  -0.4660 1225 TYR A CG  
9346  C CD1 . TYR A 1225 ? 0.7860 1.3233 1.2237 0.1428  0.0665  -0.4397 1225 TYR A CD1 
9347  C CD2 . TYR A 1225 ? 0.8081 1.3456 1.2976 0.1649  0.0768  -0.4802 1225 TYR A CD2 
9348  C CE1 . TYR A 1225 ? 0.8318 1.3261 1.2374 0.1622  0.0578  -0.4281 1225 TYR A CE1 
9349  C CE2 . TYR A 1225 ? 0.8589 1.3496 1.3151 0.1864  0.0669  -0.4680 1225 TYR A CE2 
9350  C CZ  . TYR A 1225 ? 0.8603 1.3291 1.2734 0.1833  0.0574  -0.4421 1225 TYR A CZ  
9351  O OH  . TYR A 1225 ? 0.8938 1.3140 1.2703 0.2019  0.0480  -0.4308 1225 TYR A OH  
9352  N N   . ARG A 1226 ? 0.6240 1.2823 1.1272 0.0476  0.1033  -0.4702 1226 ARG A N   
9353  C CA  . ARG A 1226 ? 0.6591 1.3523 1.1875 0.0321  0.1045  -0.4838 1226 ARG A CA  
9354  C C   . ARG A 1226 ? 0.6669 1.3693 1.1987 0.0535  0.0819  -0.4765 1226 ARG A C   
9355  O O   . ARG A 1226 ? 0.6773 1.3584 1.1834 0.0710  0.0694  -0.4560 1226 ARG A O   
9356  C CB  . ARG A 1226 ? 0.7044 1.4005 1.2086 -0.0055 0.1169  -0.4726 1226 ARG A CB  
9357  C CG  . ARG A 1226 ? 0.7127 1.4379 1.2325 -0.0261 0.1180  -0.4842 1226 ARG A CG  
9358  C CD  . ARG A 1226 ? 0.6963 1.4193 1.1874 -0.0620 0.1280  -0.4707 1226 ARG A CD  
9359  N NE  . ARG A 1226 ? 0.6769 1.3805 1.1457 -0.0779 0.1423  -0.4613 1226 ARG A NE  
9360  C CZ  . ARG A 1226 ? 0.6106 1.3131 1.0867 -0.0991 0.1618  -0.4779 1226 ARG A CZ  
9361  N NH1 . ARG A 1226 ? 0.5600 1.2835 1.0689 -0.1066 0.1705  -0.5060 1226 ARG A NH1 
9362  N NH2 . ARG A 1226 ? 0.5935 1.2741 1.0423 -0.1141 0.1731  -0.4662 1226 ARG A NH2 
9363  N N   . PHE A 1227 ? 0.6423 1.3753 1.2029 0.0500  0.0776  -0.4935 1227 PHE A N   
9364  C CA  . PHE A 1227 ? 0.6021 1.3442 1.1615 0.0621  0.0581  -0.4877 1227 PHE A CA  
9365  C C   . PHE A 1227 ? 0.5707 1.3477 1.1602 0.0452  0.0613  -0.5106 1227 PHE A C   
9366  O O   . PHE A 1227 ? 0.5659 1.3615 1.1836 0.0330  0.0763  -0.5323 1227 PHE A O   
9367  C CB  . PHE A 1227 ? 0.6273 1.3632 1.1984 0.0993  0.0388  -0.4882 1227 PHE A CB  
9368  C CG  . PHE A 1227 ? 0.6649 1.4152 1.2763 0.1138  0.0417  -0.5118 1227 PHE A CG  
9369  C CD1 . PHE A 1227 ? 0.6499 1.4377 1.3034 0.1180  0.0359  -0.5345 1227 PHE A CD1 
9370  C CD2 . PHE A 1227 ? 0.6818 1.4084 1.2882 0.1224  0.0511  -0.5115 1227 PHE A CD2 
9371  C CE1 . PHE A 1227 ? 0.6348 1.4398 1.3288 0.1337  0.0392  -0.5565 1227 PHE A CE1 
9372  C CE2 . PHE A 1227 ? 0.6624 1.3991 1.3045 0.1386  0.0544  -0.5331 1227 PHE A CE2 
9373  C CZ  . PHE A 1227 ? 0.6459 1.4240 1.3342 0.1456  0.0484  -0.5556 1227 PHE A CZ  
9374  N N   . TRP A 1228 ? 0.5711 1.3562 1.1533 0.0431  0.0486  -0.5070 1228 TRP A N   
9375  C CA  . TRP A 1228 ? 0.5841 1.4037 1.1951 0.0285  0.0487  -0.5304 1228 TRP A CA  
9376  C C   . TRP A 1228 ? 0.8149 1.6539 1.4534 0.0546  0.0285  -0.5410 1228 TRP A C   
9377  O O   . TRP A 1228 ? 0.8120 1.6324 1.4373 0.0820  0.0112  -0.5264 1228 TRP A O   
9378  C CB  . TRP A 1228 ? 0.5588 1.3767 1.1429 -0.0020 0.0520  -0.5250 1228 TRP A CB  
9379  C CG  . TRP A 1228 ? 0.5752 1.3781 1.1335 -0.0303 0.0696  -0.5151 1228 TRP A CG  
9380  C CD1 . TRP A 1228 ? 0.5864 1.3986 1.1397 -0.0668 0.0829  -0.5248 1228 TRP A CD1 
9381  C CD2 . TRP A 1228 ? 0.5782 1.3545 1.1097 -0.0265 0.0746  -0.4926 1228 TRP A CD2 
9382  N NE1 . TRP A 1228 ? 0.5813 1.3739 1.1068 -0.0849 0.0946  -0.5090 1228 TRP A NE1 
9383  C CE2 . TRP A 1228 ? 0.5795 1.3524 1.0926 -0.0610 0.0899  -0.4893 1228 TRP A CE2 
9384  C CE3 . TRP A 1228 ? 0.5602 1.3154 1.0794 0.0005  0.0674  -0.4751 1228 TRP A CE3 
9385  C CZ2 . TRP A 1228 ? 0.5631 1.3163 1.0493 -0.0685 0.0975  -0.4690 1228 TRP A CZ2 
9386  C CZ3 . TRP A 1228 ? 0.5481 1.2838 1.0397 -0.0084 0.0764  -0.4558 1228 TRP A CZ3 
9387  C CH2 . TRP A 1228 ? 0.5449 1.2815 1.0216 -0.0422 0.0909  -0.4527 1228 TRP A CH2 
9388  N N   . LYS A 1229 ? 0.8101 1.6884 1.4872 0.0449  0.0312  -0.5670 1229 LYS A N   
9389  C CA  . LYS A 1229 ? 0.8389 1.7434 1.5457 0.0650  0.0125  -0.5787 1229 LYS A CA  
9390  C C   . LYS A 1229 ? 0.9404 1.8543 1.6309 0.0413  0.0069  -0.5804 1229 LYS A C   
9391  O O   . LYS A 1229 ? 0.9512 1.8606 1.6221 0.0094  0.0211  -0.5808 1229 LYS A O   
9392  C CB  . LYS A 1229 ? 0.8179 1.7652 1.5799 0.0661  0.0219  -0.6079 1229 LYS A CB  
9393  C CG  . LYS A 1229 ? 0.8465 1.8081 1.6440 0.1051  0.0053  -0.6146 1229 LYS A CG  
9394  C CD  . LYS A 1229 ? 1.2680 2.2699 2.1221 0.1096  0.0192  -0.6436 1229 LYS A CD  
9395  C CE  . LYS A 1229 ? 1.1934 2.2572 2.0938 0.0961  0.0180  -0.6709 1229 LYS A CE  
9396  N NZ  . LYS A 1229 ? 1.1329 2.2210 2.0516 0.1173  -0.0105 -0.6714 1229 LYS A NZ  
9397  N N   . ASP A 1230 ? 1.0871 2.0114 1.7824 0.0553  -0.0141 -0.5813 1230 ASP A N   
9398  C CA  . ASP A 1230 ? 1.1862 2.1095 1.8557 0.0344  -0.0218 -0.5801 1230 ASP A CA  
9399  C C   . ASP A 1230 ? 1.2653 2.2266 1.9553 -0.0016 -0.0100 -0.6051 1230 ASP A C   
9400  O O   . ASP A 1230 ? 1.2551 2.2007 1.9108 -0.0315 -0.0027 -0.6016 1230 ASP A O   
9401  C CB  . ASP A 1230 ? 1.2444 2.1689 1.9130 0.0575  -0.0477 -0.5757 1230 ASP A CB  
9402  C CG  . ASP A 1230 ? 1.3110 2.2394 1.9577 0.0339  -0.0551 -0.5799 1230 ASP A CG  
9403  O OD1 . ASP A 1230 ? 1.3338 2.2455 1.9494 0.0050  -0.0424 -0.5770 1230 ASP A OD1 
9404  O OD2 . ASP A 1230 ? 1.3336 2.2792 1.9909 0.0429  -0.0741 -0.5856 1230 ASP A OD2 
9405  N N   . ASN A 1231 ? 1.3379 2.3488 2.0829 0.0023  -0.0090 -0.6301 1231 ASN A N   
9406  C CA  . ASN A 1231 ? 1.4370 2.4916 2.2111 -0.0309 0.0065  -0.6576 1231 ASN A CA  
9407  C C   . ASN A 1231 ? 1.5194 2.5532 2.2654 -0.0652 0.0300  -0.6561 1231 ASN A C   
9408  O O   . ASN A 1231 ? 1.5210 2.5091 2.2263 -0.0625 0.0329  -0.6329 1231 ASN A O   
9409  C CB  . ASN A 1231 ? 1.4833 2.5841 2.3215 -0.0135 0.0131  -0.6803 1231 ASN A CB  
9410  C CG  . ASN A 1231 ? 1.5326 2.6160 2.3740 -0.0120 0.0354  -0.6796 1231 ASN A CG  
9411  O OD1 . ASN A 1231 ? 1.5588 2.6150 2.3962 0.0186  0.0311  -0.6653 1231 ASN A OD1 
9412  N ND2 . ASN A 1231 ? 1.5472 2.6435 2.3915 -0.0478 0.0593  -0.6952 1231 ASN A ND2 
9413  N N   . LEU A 1232 ? 1.5856 2.6551 2.3545 -0.0977 0.0470  -0.6813 1232 LEU A N   
9414  C CA  . LEU A 1232 ? 1.6280 2.6807 2.3734 -0.1328 0.0701  -0.6827 1232 LEU A CA  
9415  C C   . LEU A 1232 ? 1.7254 2.8252 2.5192 -0.1504 0.0918  -0.7141 1232 LEU A C   
9416  O O   . LEU A 1232 ? 1.7798 2.9215 2.5964 -0.1727 0.0944  -0.7374 1232 LEU A O   
9417  C CB  . LEU A 1232 ? 1.5261 2.5596 2.2245 -0.1687 0.0681  -0.6784 1232 LEU A CB  
9418  C CG  . LEU A 1232 ? 1.4040 2.4329 2.0841 -0.2135 0.0908  -0.6883 1232 LEU A CG  
9419  C CD1 . LEU A 1232 ? 1.3679 2.3411 1.9954 -0.2166 0.0932  -0.6599 1232 LEU A CD1 
9420  C CD2 . LEU A 1232 ? 1.3769 2.4185 2.0403 -0.2499 0.0887  -0.7025 1232 LEU A CD2 
9421  N N   . GLN A 1233 ? 1.7948 2.8876 2.6027 -0.1413 0.1080  -0.7153 1233 GLN A N   
9422  C CA  . GLN A 1233 ? 1.8710 3.0035 2.7236 -0.1550 0.1319  -0.7452 1233 GLN A CA  
9423  C C   . GLN A 1233 ? 2.0104 3.2106 2.9269 -0.1463 0.1295  -0.7757 1233 GLN A C   
9424  O O   . GLN A 1233 ? 1.9797 3.2192 2.9319 -0.1653 0.1510  -0.8038 1233 GLN A O   
9425  C CB  . GLN A 1233 ? 1.9894 3.1111 2.8123 -0.2059 0.1548  -0.7523 1233 GLN A CB  
9426  C CG  . GLN A 1233 ? 2.1146 3.2397 2.9089 -0.2416 0.1486  -0.7551 1233 GLN A CG  
9427  C CD  . GLN A 1233 ? 2.2129 3.3220 2.9724 -0.2928 0.1693  -0.7610 1233 GLN A CD  
9428  O OE1 . GLN A 1233 ? 2.2492 3.3822 3.0328 -0.3141 0.1931  -0.7840 1233 GLN A OE1 
9429  N NE2 . GLN A 1233 ? 2.2470 3.3136 2.9476 -0.3127 0.1601  -0.7405 1233 GLN A NE2 
9430  N N   . HIS A 1234 ? 2.0355 3.2507 2.9659 -0.1190 0.1035  -0.7703 1234 HIS A N   
9431  C CA  . HIS A 1234 ? 2.0466 3.3285 3.0395 -0.1053 0.0964  -0.7957 1234 HIS A CA  
9432  C C   . HIS A 1234 ? 2.0949 3.3867 3.1312 -0.0571 0.0922  -0.7977 1234 HIS A C   
9433  O O   . HIS A 1234 ? 2.0828 3.4278 3.1750 -0.0351 0.0835  -0.8157 1234 HIS A O   
9434  C CB  . HIS A 1234 ? 1.9982 3.2900 2.9805 -0.1029 0.0691  -0.7882 1234 HIS A CB  
9435  C CG  . HIS A 1234 ? 1.9696 3.2480 2.9057 -0.1497 0.0721  -0.7871 1234 HIS A CG  
9436  N ND1 . HIS A 1234 ? 1.9659 3.2775 2.9121 -0.1937 0.0930  -0.8124 1234 HIS A ND1 
9437  C CD2 . HIS A 1234 ? 1.9685 3.1996 2.8443 -0.1595 0.0576  -0.7640 1234 HIS A CD2 
9438  C CE1 . HIS A 1234 ? 1.9714 3.2546 2.8634 -0.2292 0.0900  -0.8043 1234 HIS A CE1 
9439  N NE2 . HIS A 1234 ? 1.9738 3.2078 2.8230 -0.2081 0.0688  -0.7750 1234 HIS A NE2 
9440  N N   . LYS A 1235 ? 2.1831 3.4203 3.1889 -0.0407 0.0965  -0.7771 1235 LYS A N   
9441  C CA  . LYS A 1235 ? 2.2716 3.5039 3.3061 -0.0050 0.1026  -0.7806 1235 LYS A CA  
9442  C C   . LYS A 1235 ? 2.3930 3.6765 3.4916 0.0329  0.0892  -0.7982 1235 LYS A C   
9443  O O   . LYS A 1235 ? 2.4164 3.7290 3.5604 0.0444  0.1057  -0.8207 1235 LYS A O   
9444  C CB  . LYS A 1235 ? 2.2459 3.4773 3.2850 -0.0302 0.1366  -0.7973 1235 LYS A CB  
9445  C CG  . LYS A 1235 ? 2.2113 3.3930 3.1880 -0.0681 0.1497  -0.7796 1235 LYS A CG  
9446  C CD  . LYS A 1235 ? 2.1798 3.2990 3.1141 -0.0463 0.1434  -0.7489 1235 LYS A CD  
9447  C CE  . LYS A 1235 ? 2.1511 3.2275 3.0284 -0.0831 0.1559  -0.7316 1235 LYS A CE  
9448  N NZ  . LYS A 1235 ? 2.1258 3.1985 2.9707 -0.1075 0.1435  -0.7207 1235 LYS A NZ  
9449  N N   . ASP A 1236 ? 2.4850 3.7796 3.5875 0.0528  0.0595  -0.7883 1236 ASP A N   
9450  C CA  . ASP A 1236 ? 2.5924 3.9250 3.7499 0.0960  0.0423  -0.7986 1236 ASP A CA  
9451  C C   . ASP A 1236 ? 2.6709 3.9514 3.8146 0.1343  0.0411  -0.7827 1236 ASP A C   
9452  O O   . ASP A 1236 ? 2.6753 3.9750 3.8626 0.1713  0.0371  -0.7938 1236 ASP A O   
9453  C CB  . ASP A 1236 ? 2.6291 3.9784 3.7865 0.1077  0.0089  -0.7886 1236 ASP A CB  
9454  C CG  . ASP A 1236 ? 2.6678 4.0776 3.8934 0.1430  -0.0080 -0.8060 1236 ASP A CG  
9455  O OD1 . ASP A 1236 ? 2.6861 4.0996 3.9457 0.1758  -0.0018 -0.8145 1236 ASP A OD1 
9456  O OD2 . ASP A 1236 ? 2.6807 4.1339 3.9247 0.1381  -0.0279 -0.8112 1236 ASP A OD2 
9457  N N   . SER A 1237 ? 2.7315 3.9461 3.8128 0.1240  0.0449  -0.7569 1237 SER A N   
9458  C CA  . SER A 1237 ? 2.7829 3.9403 3.8380 0.1497  0.0478  -0.7399 1237 SER A CA  
9459  C C   . SER A 1237 ? 2.8032 3.9399 3.8580 0.1965  0.0185  -0.7239 1237 SER A C   
9460  O O   . SER A 1237 ? 2.8686 3.9610 3.9064 0.2215  0.0193  -0.7129 1237 SER A O   
9461  C CB  . SER A 1237 ? 2.7934 3.9574 3.8763 0.1514  0.0760  -0.7610 1237 SER A CB  
9462  O OG  . SER A 1237 ? 2.8022 3.9033 3.8474 0.1677  0.0807  -0.7428 1237 SER A OG  
9463  N N   . SER A 1238 ? 2.7378 3.9043 3.8081 0.2064  -0.0077 -0.7227 1238 SER A N   
9464  C CA  . SER A 1238 ? 2.6879 3.8283 3.7467 0.2455  -0.0382 -0.7037 1238 SER A CA  
9465  C C   . SER A 1238 ? 2.6121 3.6848 3.5994 0.2385  -0.0437 -0.6713 1238 SER A C   
9466  O O   . SER A 1238 ? 2.5337 3.6007 3.4924 0.2248  -0.0574 -0.6582 1238 SER A O   
9467  C CB  . SER A 1238 ? 2.7706 3.9616 3.8624 0.2543  -0.0651 -0.7107 1238 SER A CB  
9468  O OG  . SER A 1238 ? 2.8135 4.0141 3.8804 0.2174  -0.0666 -0.7070 1238 SER A OG  
9469  N N   . VAL A 1239 ? 2.4324 3.4543 3.3899 0.2468  -0.0316 -0.6592 1239 VAL A N   
9470  C CA  . VAL A 1239 ? 2.3851 3.3451 3.2795 0.2473  -0.0383 -0.6285 1239 VAL A CA  
9471  C C   . VAL A 1239 ? 2.3573 3.2869 3.2466 0.2902  -0.0604 -0.6170 1239 VAL A C   
9472  O O   . VAL A 1239 ? 2.3564 3.2315 3.2037 0.2988  -0.0584 -0.5983 1239 VAL A O   
9473  C CB  . VAL A 1239 ? 2.4068 3.3303 3.2673 0.2246  -0.0108 -0.6213 1239 VAL A CB  
9474  C CG1 . VAL A 1239 ? 2.4113 3.3683 3.2860 0.1848  0.0127  -0.6383 1239 VAL A CG1 
9475  C CG2 . VAL A 1239 ? 2.4667 3.3682 3.3368 0.2471  -0.0007 -0.6273 1239 VAL A CG2 
9476  N N   . PRO A 1240 ? 2.3764 3.3416 3.3060 0.3157  -0.0832 -0.6274 1240 PRO A N   
9477  C CA  . PRO A 1240 ? 2.3876 3.3423 3.3362 0.3597  -0.1014 -0.6282 1240 PRO A CA  
9478  C C   . PRO A 1240 ? 2.3375 3.2194 3.2290 0.3779  -0.1114 -0.6014 1240 PRO A C   
9479  O O   . PRO A 1240 ? 2.3895 3.2535 3.2635 0.3983  -0.1391 -0.5867 1240 PRO A O   
9480  C CB  . PRO A 1240 ? 2.4289 3.4277 3.4090 0.3734  -0.1312 -0.6330 1240 PRO A CB  
9481  C CG  . PRO A 1240 ? 2.4159 3.4160 3.3635 0.3397  -0.1327 -0.6223 1240 PRO A CG  
9482  C CD  . PRO A 1240 ? 2.3817 3.3884 3.3253 0.3032  -0.0995 -0.6313 1240 PRO A CD  
9483  N N   . ASN A 1241 ? 2.2153 3.0553 3.0757 0.3684  -0.0888 -0.5952 1241 ASN A N   
9484  C CA  . ASN A 1241 ? 2.0981 2.8695 2.9022 0.3820  -0.0956 -0.5707 1241 ASN A CA  
9485  C C   . ASN A 1241 ? 1.8403 2.5915 2.6021 0.3766  -0.1150 -0.5470 1241 ASN A C   
9486  O O   . ASN A 1241 ? 1.8118 2.5175 2.5374 0.3972  -0.1327 -0.5289 1241 ASN A O   
9487  C CB  . ASN A 1241 ? 2.2647 3.0141 3.0806 0.4256  -0.1130 -0.5733 1241 ASN A CB  
9488  C CG  . ASN A 1241 ? 2.3786 3.1372 3.2303 0.4361  -0.0925 -0.5959 1241 ASN A CG  
9489  O OD1 . ASN A 1241 ? 2.3958 3.1509 3.2409 0.4098  -0.0627 -0.6025 1241 ASN A OD1 
9490  N ND2 . ASN A 1241 ? 2.4321 3.2004 3.3199 0.4757  -0.1090 -0.6074 1241 ASN A ND2 
9491  N N   . THR A 1242 ? 1.5894 2.3711 2.3527 0.3490  -0.1117 -0.5476 1242 THR A N   
9492  C CA  . THR A 1242 ? 1.3684 2.1322 2.0935 0.3456  -0.1297 -0.5275 1242 THR A CA  
9493  C C   . THR A 1242 ? 1.0830 1.8561 1.7873 0.3101  -0.1165 -0.5219 1242 THR A C   
9494  O O   . THR A 1242 ? 0.9809 1.7978 1.7157 0.2890  -0.1067 -0.5387 1242 THR A O   
9495  C CB  . THR A 1242 ? 1.4202 2.2124 2.1719 0.3651  -0.1588 -0.5332 1242 THR A CB  
9496  O OG1 . THR A 1242 ? 1.4190 2.2755 2.2269 0.3539  -0.1533 -0.5584 1242 THR A OG1 
9497  C CG2 . THR A 1242 ? 1.4592 2.2286 2.2166 0.4049  -0.1796 -0.5308 1242 THR A CG2 
9498  N N   . GLY A 1243 ? 0.9312 1.6614 1.5814 0.3047  -0.1170 -0.4979 1243 GLY A N   
9499  C CA  . GLY A 1243 ? 0.8052 1.5348 1.4276 0.2763  -0.1068 -0.4882 1243 GLY A CA  
9500  C C   . GLY A 1243 ? 0.7069 1.4528 1.3277 0.2744  -0.1251 -0.4881 1243 GLY A C   
9501  O O   . GLY A 1243 ? 0.7209 1.4864 1.3677 0.2919  -0.1452 -0.4973 1243 GLY A O   
9502  N N   . THR A 1244 ? 0.6349 1.3713 1.2230 0.2537  -0.1190 -0.4770 1244 THR A N   
9503  C CA  . THR A 1244 ? 0.6149 1.3696 1.2028 0.2444  -0.1310 -0.4814 1244 THR A CA  
9504  C C   . THR A 1244 ? 0.7199 1.4502 1.2617 0.2263  -0.1232 -0.4654 1244 THR A C   
9505  O O   . THR A 1244 ? 0.7444 1.4693 1.2750 0.2085  -0.1029 -0.4611 1244 THR A O   
9506  C CB  . THR A 1244 ? 0.5418 1.3452 1.1724 0.2240  -0.1217 -0.5055 1244 THR A CB  
9507  O OG1 . THR A 1244 ? 0.5276 1.3664 1.2046 0.2410  -0.1373 -0.5229 1244 THR A OG1 
9508  C CG2 . THR A 1244 ? 0.5292 1.3376 1.1384 0.1989  -0.1214 -0.5050 1244 THR A CG2 
9509  N N   . ALA A 1245 ? 0.8110 1.5271 1.3258 0.2305  -0.1394 -0.4571 1245 ALA A N   
9510  C CA  . ALA A 1245 ? 0.8421 1.5340 1.3121 0.2156  -0.1328 -0.4431 1245 ALA A CA  
9511  C C   . ALA A 1245 ? 0.8403 1.5486 1.3150 0.1862  -0.1125 -0.4505 1245 ALA A C   
9512  O O   . ALA A 1245 ? 0.8158 1.5024 1.2602 0.1777  -0.0990 -0.4360 1245 ALA A O   
9513  C CB  . ALA A 1245 ? 0.8699 1.5554 1.3206 0.2175  -0.1519 -0.4425 1245 ALA A CB  
9514  N N   . ARG A 1246 ? 0.8633 1.6108 1.3749 0.1703  -0.1109 -0.4726 1246 ARG A N   
9515  C CA  . ARG A 1246 ? 0.8672 1.6293 1.3812 0.1393  -0.0926 -0.4815 1246 ARG A CA  
9516  C C   . ARG A 1246 ? 0.8181 1.5898 1.3530 0.1320  -0.0725 -0.4854 1246 ARG A C   
9517  O O   . ARG A 1246 ? 0.8040 1.5669 1.3209 0.1114  -0.0561 -0.4797 1246 ARG A O   
9518  C CB  . ARG A 1246 ? 0.8702 1.6697 1.4101 0.1202  -0.0973 -0.5041 1246 ARG A CB  
9519  C CG  . ARG A 1246 ? 0.8856 1.6833 1.4051 0.0863  -0.0827 -0.5077 1246 ARG A CG  
9520  C CD  . ARG A 1246 ? 0.9368 1.7681 1.4749 0.0645  -0.0874 -0.5293 1246 ARG A CD  
9521  N NE  . ARG A 1246 ? 1.0391 1.8627 1.5609 0.0747  -0.1090 -0.5262 1246 ARG A NE  
9522  C CZ  . ARG A 1246 ? 1.1379 1.9471 1.6244 0.0552  -0.1139 -0.5264 1246 ARG A CZ  
9523  N NH1 . ARG A 1246 ? 1.1649 1.9654 1.6295 0.0255  -0.0991 -0.5294 1246 ARG A NH1 
9524  N NH2 . ARG A 1246 ? 1.1838 1.9840 1.6534 0.0642  -0.1339 -0.5234 1246 ARG A NH2 
9525  N N   . MET A 1247 ? 0.7677 1.5550 1.3380 0.1489  -0.0743 -0.4946 1247 MET A N   
9526  C CA  . MET A 1247 ? 0.7251 1.5101 1.3054 0.1453  -0.0559 -0.4949 1247 MET A CA  
9527  C C   . MET A 1247 ? 0.7187 1.4656 1.2542 0.1434  -0.0472 -0.4698 1247 MET A C   
9528  O O   . MET A 1247 ? 0.7034 1.4484 1.2261 0.1199  -0.0307 -0.4662 1247 MET A O   
9529  C CB  . MET A 1247 ? 0.6964 1.4851 1.3049 0.1724  -0.0628 -0.5009 1247 MET A CB  
9530  C CG  . MET A 1247 ? 0.6777 1.4720 1.3058 0.1658  -0.0428 -0.5097 1247 MET A CG  
9531  S SD  . MET A 1247 ? 0.8608 1.6874 1.5458 0.1905  -0.0519 -0.5337 1247 MET A SD  
9532  C CE  . MET A 1247 ? 0.5839 1.4566 1.2962 0.1800  -0.0656 -0.5508 1247 MET A CE  
9533  N N   . VAL A 1248 ? 0.7459 1.4639 1.2575 0.1675  -0.0590 -0.4524 1248 VAL A N   
9534  C CA  . VAL A 1248 ? 0.7240 1.4101 1.1942 0.1674  -0.0518 -0.4282 1248 VAL A CA  
9535  C C   . VAL A 1248 ? 0.6694 1.3504 1.1117 0.1488  -0.0465 -0.4193 1248 VAL A C   
9536  O O   . VAL A 1248 ? 0.6368 1.3048 1.0553 0.1400  -0.0348 -0.4038 1248 VAL A O   
9537  C CB  . VAL A 1248 ? 0.4393 1.0940 0.8824 0.1948  -0.0665 -0.4109 1248 VAL A CB  
9538  C CG1 . VAL A 1248 ? 0.3975 1.0265 0.7985 0.1917  -0.0577 -0.3868 1248 VAL A CG1 
9539  C CG2 . VAL A 1248 ? 0.4567 1.1064 0.9186 0.2141  -0.0715 -0.4164 1248 VAL A CG2 
9540  N N   . GLU A 1249 ? 0.6440 1.3346 1.0879 0.1428  -0.0554 -0.4286 1249 GLU A N   
9541  C CA  . GLU A 1249 ? 0.6840 1.3631 1.0968 0.1263  -0.0506 -0.4203 1249 GLU A CA  
9542  C C   . GLU A 1249 ? 0.6923 1.3860 1.1141 0.0982  -0.0325 -0.4266 1249 GLU A C   
9543  O O   . GLU A 1249 ? 0.7082 1.3877 1.1051 0.0900  -0.0225 -0.4107 1249 GLU A O   
9544  C CB  . GLU A 1249 ? 0.7451 1.4267 1.1518 0.1219  -0.0632 -0.4297 1249 GLU A CB  
9545  C CG  . GLU A 1249 ? 0.8146 1.4814 1.1883 0.1020  -0.0563 -0.4236 1249 GLU A CG  
9546  C CD  . GLU A 1249 ? 0.9181 1.5564 1.2537 0.1125  -0.0688 -0.4141 1249 GLU A CD  
9547  O OE1 . GLU A 1249 ? 0.9833 1.6165 1.3206 0.1334  -0.0829 -0.4127 1249 GLU A OE1 
9548  O OE2 . GLU A 1249 ? 0.9364 1.5547 1.2383 0.1005  -0.0651 -0.4079 1249 GLU A OE2 
9549  N N   . THR A 1250 ? 0.6624 1.3862 1.1199 0.0828  -0.0282 -0.4498 1250 THR A N   
9550  C CA  . THR A 1250 ? 0.6111 1.3475 1.0734 0.0512  -0.0110 -0.4582 1250 THR A CA  
9551  C C   . THR A 1250 ? 0.5224 1.2509 0.9802 0.0479  0.0034  -0.4464 1250 THR A C   
9552  O O   . THR A 1250 ? 0.4715 1.1896 0.9053 0.0303  0.0129  -0.4347 1250 THR A O   
9553  C CB  . THR A 1250 ? 0.6454 1.4188 1.1493 0.0347  -0.0065 -0.4872 1250 THR A CB  
9554  O OG1 . THR A 1250 ? 0.6749 1.4640 1.2143 0.0474  -0.0017 -0.4967 1250 THR A OG1 
9555  C CG2 . THR A 1250 ? 0.6362 1.4233 1.1494 0.0397  -0.0229 -0.4993 1250 THR A CG2 
9556  N N   . THR A 1251 ? 0.5007 1.2320 0.9786 0.0649  0.0040  -0.4484 1251 THR A N   
9557  C CA  . THR A 1251 ? 0.5094 1.2317 0.9803 0.0593  0.0180  -0.4382 1251 THR A CA  
9558  C C   . THR A 1251 ? 0.5254 1.2232 0.9554 0.0632  0.0171  -0.4101 1251 THR A C   
9559  O O   . THR A 1251 ? 0.5465 1.2412 0.9629 0.0465  0.0294  -0.3996 1251 THR A O   
9560  C CB  . THR A 1251 ? 0.5132 1.2362 1.0076 0.0775  0.0185  -0.4457 1251 THR A CB  
9561  O OG1 . THR A 1251 ? 0.5578 1.2556 1.0298 0.1028  0.0081  -0.4267 1251 THR A OG1 
9562  C CG2 . THR A 1251 ? 0.4805 1.2277 1.0142 0.0877  0.0103  -0.4697 1251 THR A CG2 
9563  N N   . ALA A 1252 ? 0.5192 1.2015 0.9292 0.0840  0.0031  -0.3981 1252 ALA A N   
9564  C CA  . ALA A 1252 ? 0.5570 1.2211 0.9309 0.0870  0.0041  -0.3736 1252 ALA A CA  
9565  C C   . ALA A 1252 ? 0.5730 1.2395 0.9325 0.0633  0.0106  -0.3712 1252 ALA A C   
9566  O O   . ALA A 1252 ? 0.5544 1.2164 0.8948 0.0548  0.0183  -0.3545 1252 ALA A O   
9567  C CB  . ALA A 1252 ? 0.5858 1.2311 0.9394 0.1133  -0.0107 -0.3629 1252 ALA A CB  
9568  N N   . TYR A 1253 ? 0.6117 1.2853 0.9790 0.0515  0.0072  -0.3877 1253 TYR A N   
9569  C CA  . TYR A 1253 ? 0.6499 1.3204 0.9990 0.0269  0.0130  -0.3862 1253 TYR A CA  
9570  C C   . TYR A 1253 ? 0.6428 1.3254 1.0001 -0.0001 0.0286  -0.3881 1253 TYR A C   
9571  O O   . TYR A 1253 ? 0.6793 1.3534 1.0128 -0.0136 0.0332  -0.3743 1253 TYR A O   
9572  C CB  . TYR A 1253 ? 0.6887 1.3638 1.0419 0.0146  0.0072  -0.4053 1253 TYR A CB  
9573  C CG  . TYR A 1253 ? 0.7419 1.3950 1.0683 0.0332  -0.0066 -0.3973 1253 TYR A CG  
9574  C CD1 . TYR A 1253 ? 0.7605 1.3872 1.0474 0.0385  -0.0075 -0.3769 1253 TYR A CD1 
9575  C CD2 . TYR A 1253 ? 0.7506 1.4087 1.0903 0.0467  -0.0190 -0.4094 1253 TYR A CD2 
9576  C CE1 . TYR A 1253 ? 0.7694 1.3721 1.0287 0.0559  -0.0185 -0.3702 1253 TYR A CE1 
9577  C CE2 . TYR A 1253 ? 0.7676 1.4024 1.0788 0.0619  -0.0313 -0.4019 1253 TYR A CE2 
9578  C CZ  . TYR A 1253 ? 0.7807 1.3862 1.0507 0.0662  -0.0300 -0.3829 1253 TYR A CZ  
9579  O OH  . TYR A 1253 ? 0.8356 1.4144 1.0748 0.0820  -0.0409 -0.3765 1253 TYR A OH  
9580  N N   . ALA A 1254 ? 0.5731 1.2743 0.9627 -0.0080 0.0364  -0.4057 1254 ALA A N   
9581  C CA  . ALA A 1254 ? 0.4879 1.1972 0.8835 -0.0323 0.0524  -0.4073 1254 ALA A CA  
9582  C C   . ALA A 1254 ? 0.4750 1.1734 0.8510 -0.0244 0.0555  -0.3822 1254 ALA A C   
9583  O O   . ALA A 1254 ? 0.4456 1.1398 0.7996 -0.0404 0.0602  -0.3670 1254 ALA A O   
9584  C CB  . ALA A 1254 ? 0.4340 1.1619 0.8669 -0.0359 0.0604  -0.4311 1254 ALA A CB  
9585  N N   . LEU A 1255 ? 0.5066 1.2005 0.8887 -0.0003 0.0516  -0.3774 1255 LEU A N   
9586  C CA  . LEU A 1255 ? 0.5669 1.2517 0.9289 0.0070  0.0540  -0.3540 1255 LEU A CA  
9587  C C   . LEU A 1255 ? 0.5559 1.2350 0.8887 0.0079  0.0503  -0.3312 1255 LEU A C   
9588  O O   . LEU A 1255 ? 0.5173 1.1986 0.8356 0.0004  0.0563  -0.3131 1255 LEU A O   
9589  C CB  . LEU A 1255 ? 0.6246 1.2986 0.9875 0.0369  0.0457  -0.3496 1255 LEU A CB  
9590  C CG  . LEU A 1255 ? 0.6376 1.3029 0.9749 0.0439  0.0474  -0.3243 1255 LEU A CG  
9591  C CD1 . LEU A 1255 ? 0.6323 1.3030 0.9667 0.0194  0.0622  -0.3195 1255 LEU A CD1 
9592  C CD2 . LEU A 1255 ? 0.6360 1.2859 0.9665 0.0728  0.0378  -0.3186 1255 LEU A CD2 
9593  N N   . LEU A 1256 ? 0.5974 1.2690 0.9208 0.0182  0.0402  -0.3317 1256 LEU A N   
9594  C CA  . LEU A 1256 ? 0.6701 1.3327 0.9648 0.0250  0.0363  -0.3105 1256 LEU A CA  
9595  C C   . LEU A 1256 ? 0.7119 1.3775 0.9961 -0.0024 0.0421  -0.3077 1256 LEU A C   
9596  O O   . LEU A 1256 ? 0.7342 1.4004 1.0000 -0.0034 0.0435  -0.2868 1256 LEU A O   
9597  C CB  . LEU A 1256 ? 0.7074 1.3535 0.9887 0.0478  0.0238  -0.3108 1256 LEU A CB  
9598  C CG  . LEU A 1256 ? 0.7169 1.3521 0.9883 0.0790  0.0163  -0.2996 1256 LEU A CG  
9599  C CD1 . LEU A 1256 ? 0.7645 1.3804 1.0152 0.0932  0.0064  -0.2992 1256 LEU A CD1 
9600  C CD2 . LEU A 1256 ? 0.6729 1.3116 0.9299 0.0870  0.0215  -0.2760 1256 LEU A CD2 
9601  N N   . THR A 1257 ? 0.6992 1.3680 0.9951 -0.0246 0.0452  -0.3286 1257 THR A N   
9602  C CA  . THR A 1257 ? 0.6694 1.3389 0.9546 -0.0562 0.0514  -0.3294 1257 THR A CA  
9603  C C   . THR A 1257 ? 0.6061 1.2875 0.8936 -0.0727 0.0620  -0.3189 1257 THR A C   
9604  O O   . THR A 1257 ? 0.5717 1.2528 0.8393 -0.0777 0.0618  -0.2976 1257 THR A O   
9605  C CB  . THR A 1257 ? 0.5281 1.2028 0.8291 -0.0802 0.0557  -0.3572 1257 THR A CB  
9606  O OG1 . THR A 1257 ? 0.5497 1.2165 0.8502 -0.0657 0.0452  -0.3680 1257 THR A OG1 
9607  C CG2 . THR A 1257 ? 0.5165 1.1850 0.7975 -0.1130 0.0604  -0.3565 1257 THR A CG2 
9608  N N   . SER A 1258 ? 0.5888 1.2805 0.9000 -0.0794 0.0708  -0.3332 1258 SER A N   
9609  C CA  . SER A 1258 ? 0.6279 1.3272 0.9391 -0.0946 0.0815  -0.3245 1258 SER A CA  
9610  C C   . SER A 1258 ? 0.6332 1.3342 0.9263 -0.0809 0.0780  -0.2958 1258 SER A C   
9611  O O   . SER A 1258 ? 0.6142 1.3219 0.8935 -0.1002 0.0821  -0.2807 1258 SER A O   
9612  C CB  . SER A 1258 ? 0.6331 1.3361 0.9689 -0.0927 0.0894  -0.3428 1258 SER A CB  
9613  O OG  . SER A 1258 ? 0.6415 1.3499 0.9961 -0.1105 0.0957  -0.3689 1258 SER A OG  
9614  N N   . LEU A 1259 ? 0.6502 1.3470 0.9432 -0.0492 0.0705  -0.2886 1259 LEU A N   
9615  C CA  . LEU A 1259 ? 0.6205 1.3225 0.8977 -0.0361 0.0685  -0.2629 1259 LEU A CA  
9616  C C   . LEU A 1259 ? 0.6238 1.3312 0.8826 -0.0413 0.0649  -0.2443 1259 LEU A C   
9617  O O   . LEU A 1259 ? 0.6096 1.3311 0.8584 -0.0435 0.0665  -0.2228 1259 LEU A O   
9618  C CB  . LEU A 1259 ? 0.5649 1.2583 0.8408 -0.0014 0.0604  -0.2594 1259 LEU A CB  
9619  C CG  . LEU A 1259 ? 0.5181 1.2086 0.8015 0.0027  0.0650  -0.2636 1259 LEU A CG  
9620  C CD1 . LEU A 1259 ? 0.5383 1.2166 0.8175 0.0345  0.0558  -0.2611 1259 LEU A CD1 
9621  C CD2 . LEU A 1259 ? 0.4813 1.1833 0.7536 -0.0143 0.0741  -0.2465 1259 LEU A CD2 
9622  N N   . ASN A 1260 ? 0.6352 1.3315 0.8888 -0.0443 0.0596  -0.2526 1260 ASN A N   
9623  C CA  . ASN A 1260 ? 0.6683 1.3631 0.9015 -0.0492 0.0552  -0.2365 1260 ASN A CA  
9624  C C   . ASN A 1260 ? 0.7059 1.4123 0.9352 -0.0841 0.0618  -0.2308 1260 ASN A C   
9625  O O   . ASN A 1260 ? 0.7446 1.4637 0.9625 -0.0862 0.0600  -0.2082 1260 ASN A O   
9626  C CB  . ASN A 1260 ? 0.6580 1.3308 0.8799 -0.0441 0.0475  -0.2472 1260 ASN A CB  
9627  C CG  . ASN A 1260 ? 0.6877 1.3483 0.8924 -0.0104 0.0384  -0.2331 1260 ASN A CG  
9628  O OD1 . ASN A 1260 ? 0.7132 1.3829 0.9078 0.0016  0.0371  -0.2108 1260 ASN A OD1 
9629  N ND2 . ASN A 1260 ? 0.6866 1.3280 0.8879 0.0050  0.0324  -0.2463 1260 ASN A ND2 
9630  N N   . LEU A 1261 ? 0.6648 1.3686 0.9043 -0.1117 0.0697  -0.2513 1261 LEU A N   
9631  C CA  . LEU A 1261 ? 0.6018 1.3123 0.8355 -0.1490 0.0774  -0.2496 1261 LEU A CA  
9632  C C   . LEU A 1261 ? 0.5867 1.3133 0.8268 -0.1592 0.0867  -0.2418 1261 LEU A C   
9633  O O   . LEU A 1261 ? 0.5751 1.3032 0.8168 -0.1904 0.0973  -0.2507 1261 LEU A O   
9634  C CB  . LEU A 1261 ? 0.5557 1.2563 0.7965 -0.1743 0.0841  -0.2769 1261 LEU A CB  
9635  C CG  . LEU A 1261 ? 0.5339 1.2177 0.7692 -0.1666 0.0763  -0.2899 1261 LEU A CG  
9636  C CD1 . LEU A 1261 ? 0.5458 1.2276 0.7925 -0.1959 0.0858  -0.3190 1261 LEU A CD1 
9637  C CD2 . LEU A 1261 ? 0.5002 1.1698 0.7050 -0.1645 0.0653  -0.2715 1261 LEU A CD2 
9638  N N   . LYS A 1262 ? 0.5915 1.3278 0.8320 -0.1340 0.0832  -0.2255 1262 LYS A N   
9639  C CA  . LYS A 1262 ? 0.5728 1.3210 0.8152 -0.1408 0.0912  -0.2178 1262 LYS A CA  
9640  C C   . LYS A 1262 ? 0.5294 1.2694 0.7802 -0.1663 0.1043  -0.2385 1262 LYS A C   
9641  O O   . LYS A 1262 ? 0.5180 1.2641 0.7616 -0.1888 0.1128  -0.2321 1262 LYS A O   
9642  C CB  . LYS A 1262 ? 0.6249 1.3949 0.8532 -0.1530 0.0894  -0.1906 1262 LYS A CB  
9643  C CG  . LYS A 1262 ? 0.7365 1.5114 0.9569 -0.1310 0.0768  -0.1743 1262 LYS A CG  
9644  C CD  . LYS A 1262 ? 0.8373 1.6384 1.0538 -0.1136 0.0729  -0.1476 1262 LYS A CD  
9645  C CE  . LYS A 1262 ? 0.8996 1.6954 1.1143 -0.0740 0.0635  -0.1414 1262 LYS A CE  
9646  N NZ  . LYS A 1262 ? 0.9261 1.6948 1.1474 -0.0549 0.0631  -0.1636 1262 LYS A NZ  
9647  N N   . ASP A 1263 ? 0.5007 1.2274 0.7668 -0.1611 0.1058  -0.2636 1263 ASP A N   
9648  C CA  . ASP A 1263 ? 0.5179 1.2372 0.7964 -0.1813 0.1187  -0.2876 1263 ASP A CA  
9649  C C   . ASP A 1263 ? 0.4876 1.2016 0.7701 -0.1737 0.1259  -0.2899 1263 ASP A C   
9650  O O   . ASP A 1263 ? 0.5430 1.2476 0.8401 -0.1751 0.1342  -0.3118 1263 ASP A O   
9651  C CB  . ASP A 1263 ? 0.5422 1.2551 0.8403 -0.1695 0.1160  -0.3125 1263 ASP A CB  
9652  C CG  . ASP A 1263 ? 0.8847 1.5962 1.1929 -0.2011 0.1292  -0.3376 1263 ASP A CG  
9653  O OD1 . ASP A 1263 ? 0.8771 1.5868 1.1825 -0.2239 0.1429  -0.3413 1263 ASP A OD1 
9654  O OD2 . ASP A 1263 ? 0.8590 1.5704 1.1756 -0.2036 0.1263  -0.3538 1263 ASP A OD2 
9655  N N   . ILE A 1264 ? 0.4577 1.1776 0.7253 -0.1672 0.1232  -0.2671 1264 ILE A N   
9656  C CA  . ILE A 1264 ? 0.4929 1.2040 0.7567 -0.1548 0.1266  -0.2645 1264 ILE A CA  
9657  C C   . ILE A 1264 ? 0.5417 1.2328 0.8136 -0.1570 0.1372  -0.2861 1264 ILE A C   
9658  O O   . ILE A 1264 ? 0.5597 1.2381 0.8391 -0.1292 0.1326  -0.2931 1264 ILE A O   
9659  C CB  . ILE A 1264 ? 0.4330 1.1560 0.6750 -0.1710 0.1293  -0.2401 1264 ILE A CB  
9660  C CG1 . ILE A 1264 ? 0.4038 1.1480 0.6419 -0.1582 0.1171  -0.2186 1264 ILE A CG1 
9661  C CG2 . ILE A 1264 ? 0.2338 0.9435 0.4659 -0.1602 0.1327  -0.2372 1264 ILE A CG2 
9662  C CD1 . ILE A 1264 ? 0.3884 1.1534 0.6106 -0.1678 0.1170  -0.1931 1264 ILE A CD1 
9663  N N   . ASN A 1265 ? 0.5916 1.2775 0.8597 -0.1890 0.1512  -0.2963 1265 ASN A N   
9664  C CA  . ASN A 1265 ? 0.6826 1.3473 0.9583 -0.1883 0.1625  -0.3181 1265 ASN A CA  
9665  C C   . ASN A 1265 ? 0.6859 1.3484 0.9931 -0.1640 0.1588  -0.3433 1265 ASN A C   
9666  O O   . ASN A 1265 ? 0.7078 1.3548 1.0240 -0.1409 0.1582  -0.3542 1265 ASN A O   
9667  C CB  . ASN A 1265 ? 0.7414 1.3983 1.0047 -0.2287 0.1806  -0.3258 1265 ASN A CB  
9668  C CG  . ASN A 1265 ? 0.8249 1.4695 1.0569 -0.2449 0.1875  -0.3091 1265 ASN A CG  
9669  O OD1 . ASN A 1265 ? 0.8823 1.5043 1.1075 -0.2303 0.1905  -0.3133 1265 ASN A OD1 
9670  N ND2 . ASN A 1265 ? 0.8280 1.4867 1.0389 -0.2758 0.1890  -0.2897 1265 ASN A ND2 
9671  N N   . TYR A 1266 ? 0.6773 1.3549 0.9993 -0.1702 0.1555  -0.3522 1266 TYR A N   
9672  C CA  . TYR A 1266 ? 0.6613 1.3433 1.0143 -0.1537 0.1528  -0.3776 1266 TYR A CA  
9673  C C   . TYR A 1266 ? 0.6983 1.3744 1.0608 -0.1133 0.1389  -0.3758 1266 TYR A C   
9674  O O   . TYR A 1266 ? 0.7469 1.4186 1.1319 -0.0950 0.1390  -0.3954 1266 TYR A O   
9675  C CB  . TYR A 1266 ? 0.5845 1.2818 0.9422 -0.1613 0.1454  -0.3788 1266 TYR A CB  
9676  C CG  . TYR A 1266 ? 0.5242 1.2304 0.9120 -0.1544 0.1451  -0.4064 1266 TYR A CG  
9677  C CD1 . TYR A 1266 ? 0.5224 1.2299 0.9314 -0.1635 0.1595  -0.4318 1266 TYR A CD1 
9678  C CD2 . TYR A 1266 ? 0.4897 1.2039 0.8840 -0.1400 0.1310  -0.4075 1266 TYR A CD2 
9679  C CE1 . TYR A 1266 ? 0.5415 1.2641 0.9818 -0.1583 0.1598  -0.4580 1266 TYR A CE1 
9680  C CE2 . TYR A 1266 ? 0.4846 1.2111 0.9066 -0.1371 0.1306  -0.4333 1266 TYR A CE2 
9681  C CZ  . TYR A 1266 ? 0.5136 1.2475 0.9610 -0.1465 0.1451  -0.4587 1266 TYR A CZ  
9682  O OH  . TYR A 1266 ? 0.5054 1.2585 0.9849 -0.1448 0.1463  -0.4859 1266 TYR A OH  
9683  N N   . VAL A 1267 ? 0.6465 1.3231 0.9901 -0.1003 0.1273  -0.3513 1267 VAL A N   
9684  C CA  . VAL A 1267 ? 0.5693 1.2430 0.9162 -0.0651 0.1114  -0.3455 1267 VAL A CA  
9685  C C   . VAL A 1267 ? 0.5843 1.2387 0.9255 -0.0447 0.1099  -0.3436 1267 VAL A C   
9686  O O   . VAL A 1267 ? 0.5790 1.2266 0.9321 -0.0164 0.0991  -0.3510 1267 VAL A O   
9687  C CB  . VAL A 1267 ? 0.5375 1.2195 0.8645 -0.0624 0.1026  -0.3209 1267 VAL A CB  
9688  C CG1 . VAL A 1267 ? 0.5386 1.2121 0.8489 -0.0393 0.0953  -0.3022 1267 VAL A CG1 
9689  C CG2 . VAL A 1267 ? 0.5059 1.1955 0.8420 -0.0544 0.0927  -0.3268 1267 VAL A CG2 
9690  N N   . ASN A 1268 ? 0.6398 1.2829 0.9606 -0.0606 0.1204  -0.3344 1268 ASN A N   
9691  C CA  . ASN A 1268 ? 0.7621 1.3800 1.0706 -0.0433 0.1192  -0.3325 1268 ASN A CA  
9692  C C   . ASN A 1268 ? 0.7897 1.3950 1.1217 -0.0141 0.1120  -0.3532 1268 ASN A C   
9693  O O   . ASN A 1268 ? 0.8491 1.4463 1.1783 0.0139  0.0975  -0.3472 1268 ASN A O   
9694  C CB  . ASN A 1268 ? 0.8545 1.4564 1.1403 -0.0698 0.1351  -0.3292 1268 ASN A CB  
9695  C CG  . ASN A 1268 ? 0.9287 1.5446 1.1887 -0.0958 0.1391  -0.3047 1268 ASN A CG  
9696  O OD1 . ASN A 1268 ? 0.9418 1.5706 1.1927 -0.0849 0.1289  -0.2853 1268 ASN A OD1 
9697  N ND2 . ASN A 1268 ? 0.9592 1.5734 1.2070 -0.1303 0.1539  -0.3055 1268 ASN A ND2 
9698  N N   . PRO A 1269 ? 0.7932 1.3991 1.1492 -0.0202 0.1215  -0.3776 1269 PRO A N   
9699  C CA  . PRO A 1269 ? 0.7680 1.3659 1.1501 0.0083  0.1150  -0.3980 1269 PRO A CA  
9700  C C   . PRO A 1269 ? 0.7020 1.3185 1.1067 0.0319  0.0969  -0.4020 1269 PRO A C   
9701  O O   . PRO A 1269 ? 0.6781 1.2887 1.0990 0.0610  0.0846  -0.4115 1269 PRO A O   
9702  C CB  . PRO A 1269 ? 0.8130 1.4209 1.2206 -0.0095 0.1315  -0.4234 1269 PRO A CB  
9703  C CG  . PRO A 1269 ? 0.8299 1.4437 1.2183 -0.0491 0.1468  -0.4152 1269 PRO A CG  
9704  C CD  . PRO A 1269 ? 0.8062 1.4283 1.1717 -0.0531 0.1367  -0.3884 1269 PRO A CD  
9705  N N   . VAL A 1270 ? 0.6180 1.2556 1.0218 0.0181  0.0949  -0.3948 1270 VAL A N   
9706  C CA  . VAL A 1270 ? 0.5645 1.2129 0.9768 0.0374  0.0779  -0.3930 1270 VAL A CA  
9707  C C   . VAL A 1270 ? 0.5240 1.1528 0.9123 0.0625  0.0641  -0.3736 1270 VAL A C   
9708  O O   . VAL A 1270 ? 0.5475 1.1691 0.9453 0.0892  0.0503  -0.3794 1270 VAL A O   
9709  C CB  . VAL A 1270 ? 0.5337 1.2004 0.9410 0.0166  0.0796  -0.3869 1270 VAL A CB  
9710  C CG1 . VAL A 1270 ? 0.5003 1.1653 0.8928 0.0351  0.0638  -0.3711 1270 VAL A CG1 
9711  C CG2 . VAL A 1270 ? 0.5359 1.2233 0.9729 0.0016  0.0855  -0.4117 1270 VAL A CG2 
9712  N N   . ILE A 1271 ? 0.4801 1.1013 0.8371 0.0539  0.0675  -0.3508 1271 ILE A N   
9713  C CA  . ILE A 1271 ? 0.4680 1.0709 0.8022 0.0769  0.0558  -0.3347 1271 ILE A CA  
9714  C C   . ILE A 1271 ? 0.4788 1.0535 0.8069 0.0916  0.0540  -0.3396 1271 ILE A C   
9715  O O   . ILE A 1271 ? 0.5167 1.0737 0.8332 0.1152  0.0409  -0.3340 1271 ILE A O   
9716  C CB  . ILE A 1271 ? 0.4944 1.1007 0.7976 0.0690  0.0578  -0.3080 1271 ILE A CB  
9717  C CG1 . ILE A 1271 ? 0.5014 1.0961 0.7806 0.0527  0.0693  -0.2963 1271 ILE A CG1 
9718  C CG2 . ILE A 1271 ? 0.4820 1.1126 0.7892 0.0537  0.0606  -0.3027 1271 ILE A CG2 
9719  C CD1 . ILE A 1271 ? 0.5306 1.0962 0.7881 0.0716  0.0626  -0.2903 1271 ILE A CD1 
9720  N N   . LYS A 1272 ? 0.5032 1.0691 0.8356 0.0787  0.0667  -0.3504 1272 LYS A N   
9721  C CA  . LYS A 1272 ? 0.6124 1.1454 0.9363 0.0975  0.0628  -0.3554 1272 LYS A CA  
9722  C C   . LYS A 1272 ? 0.6545 1.1879 1.0036 0.1297  0.0444  -0.3685 1272 LYS A C   
9723  O O   . LYS A 1272 ? 0.7020 1.2079 1.0357 0.1528  0.0319  -0.3639 1272 LYS A O   
9724  C CB  . LYS A 1272 ? 0.6663 1.1860 0.9933 0.0822  0.0798  -0.3693 1272 LYS A CB  
9725  C CG  . LYS A 1272 ? 0.6805 1.1652 1.0056 0.1055  0.0757  -0.3804 1272 LYS A CG  
9726  C CD  . LYS A 1272 ? 0.7127 1.1554 0.9900 0.1011  0.0794  -0.3648 1272 LYS A CD  
9727  C CE  . LYS A 1272 ? 0.7810 1.1866 1.0580 0.1190  0.0803  -0.3803 1272 LYS A CE  
9728  N NZ  . LYS A 1272 ? 0.8490 1.2029 1.0751 0.1236  0.0776  -0.3663 1272 LYS A NZ  
9729  N N   . TRP A 1273 ? 0.6118 1.1765 0.9969 0.1288  0.0423  -0.3841 1273 TRP A N   
9730  C CA  . TRP A 1273 ? 0.5606 1.1349 0.9760 0.1548  0.0257  -0.3993 1273 TRP A CA  
9731  C C   . TRP A 1273 ? 0.5056 1.0820 0.9099 0.1695  0.0075  -0.3871 1273 TRP A C   
9732  O O   . TRP A 1273 ? 0.5366 1.1025 0.9450 0.1952  -0.0098 -0.3899 1273 TRP A O   
9733  C CB  . TRP A 1273 ? 0.5370 1.1451 0.9954 0.1432  0.0340  -0.4238 1273 TRP A CB  
9734  C CG  . TRP A 1273 ? 0.5247 1.1572 1.0200 0.1613  0.0190  -0.4411 1273 TRP A CG  
9735  C CD1 . TRP A 1273 ? 0.5520 1.1951 1.0840 0.1786  0.0154  -0.4627 1273 TRP A CD1 
9736  C CD2 . TRP A 1273 ? 0.5076 1.1597 1.0073 0.1617  0.0068  -0.4389 1273 TRP A CD2 
9737  N NE1 . TRP A 1273 ? 0.5341 1.2066 1.0949 0.1887  0.0004  -0.4736 1273 TRP A NE1 
9738  C CE2 . TRP A 1273 ? 0.5053 1.1807 1.0441 0.1774  -0.0048 -0.4593 1273 TRP A CE2 
9739  C CE3 . TRP A 1273 ? 0.5140 1.1650 0.9870 0.1513  0.0044  -0.4217 1273 TRP A CE3 
9740  C CZ2 . TRP A 1273 ? 0.5124 1.2079 1.0604 0.1794  -0.0186 -0.4625 1273 TRP A CZ2 
9741  C CZ3 . TRP A 1273 ? 0.5198 1.1864 1.0009 0.1553  -0.0084 -0.4256 1273 TRP A CZ3 
9742  C CH2 . TRP A 1273 ? 0.5177 1.2056 1.0344 0.1678  -0.0198 -0.4456 1273 TRP A CH2 
9743  N N   . LEU A 1274 ? 0.4511 1.0383 0.8391 0.1547  0.0109  -0.3732 1274 LEU A N   
9744  C CA  . LEU A 1274 ? 0.5124 1.0906 0.8787 0.1703  -0.0039 -0.3583 1274 LEU A CA  
9745  C C   . LEU A 1274 ? 0.6016 1.1456 0.9335 0.1860  -0.0105 -0.3422 1274 LEU A C   
9746  O O   . LEU A 1274 ? 0.6396 1.1671 0.9686 0.2090  -0.0268 -0.3439 1274 LEU A O   
9747  C CB  . LEU A 1274 ? 0.5554 1.1487 0.9090 0.1546  0.0015  -0.3463 1274 LEU A CB  
9748  C CG  . LEU A 1274 ? 0.5877 1.2065 0.9671 0.1453  0.0003  -0.3616 1274 LEU A CG  
9749  C CD1 . LEU A 1274 ? 0.5923 1.2173 0.9525 0.1345  0.0026  -0.3483 1274 LEU A CD1 
9750  C CD2 . LEU A 1274 ? 0.6005 1.2203 0.9972 0.1665  -0.0175 -0.3744 1274 LEU A CD2 
9751  N N   . SER A 1275 ? 0.6014 1.1347 0.9056 0.1719  0.0017  -0.3268 1275 SER A N   
9752  C CA  . SER A 1275 ? 0.6889 1.1892 0.9568 0.1817  -0.0023 -0.3122 1275 SER A CA  
9753  C C   . SER A 1275 ? 0.7104 1.1807 0.9790 0.1999  -0.0112 -0.3224 1275 SER A C   
9754  O O   . SER A 1275 ? 0.7197 1.1573 0.9552 0.2007  -0.0098 -0.3127 1275 SER A O   
9755  C CB  . SER A 1275 ? 0.8005 1.2990 1.0431 0.1574  0.0151  -0.2976 1275 SER A CB  
9756  O OG  . SER A 1275 ? 0.8752 1.3666 1.0838 0.1583  0.0140  -0.2768 1275 SER A OG  
9757  N N   . GLU A 1276 ? 0.7495 1.2309 1.0544 0.2140  -0.0205 -0.3419 1276 GLU A N   
9758  C CA  . GLU A 1276 ? 0.8334 1.2917 1.1475 0.2359  -0.0312 -0.3540 1276 GLU A CA  
9759  C C   . GLU A 1276 ? 0.8249 1.3060 1.1763 0.2543  -0.0478 -0.3691 1276 GLU A C   
9760  O O   . GLU A 1276 ? 0.8563 1.3345 1.2325 0.2724  -0.0562 -0.3845 1276 GLU A O   
9761  C CB  . GLU A 1276 ? 0.8961 1.3547 1.2288 0.2260  -0.0154 -0.3690 1276 GLU A CB  
9762  C CG  . GLU A 1276 ? 0.9480 1.3724 1.2418 0.2117  -0.0012 -0.3582 1276 GLU A CG  
9763  C CD  . GLU A 1276 ? 0.9463 1.3553 1.2536 0.2135  0.0085  -0.3755 1276 GLU A CD  
9764  O OE1 . GLU A 1276 ? 0.9131 1.3461 1.2656 0.2245  0.0064  -0.3965 1276 GLU A OE1 
9765  O OE2 . GLU A 1276 ? 0.9755 1.3483 1.2468 0.2036  0.0187  -0.3682 1276 GLU A OE2 
9766  N N   . GLU A 1277 ? 0.7847 1.2898 1.1405 0.2483  -0.0514 -0.3654 1277 GLU A N   
9767  C CA  . GLU A 1277 ? 0.7838 1.3129 1.1699 0.2602  -0.0670 -0.3782 1277 GLU A CA  
9768  C C   . GLU A 1277 ? 0.7877 1.2994 1.1446 0.2737  -0.0844 -0.3639 1277 GLU A C   
9769  O O   . GLU A 1277 ? 0.7948 1.2952 1.1547 0.2958  -0.1050 -0.3674 1277 GLU A O   
9770  C CB  . GLU A 1277 ? 0.7579 1.3263 1.1700 0.2381  -0.0554 -0.3881 1277 GLU A CB  
9771  C CG  . GLU A 1277 ? 0.7433 1.3435 1.1970 0.2441  -0.0663 -0.4087 1277 GLU A CG  
9772  C CD  . GLU A 1277 ? 0.7583 1.3656 1.2472 0.2593  -0.0698 -0.4271 1277 GLU A CD  
9773  O OE1 . GLU A 1277 ? 0.7651 1.4007 1.2905 0.2682  -0.0812 -0.4440 1277 GLU A OE1 
9774  O OE2 . GLU A 1277 ? 0.7771 1.3607 1.2559 0.2630  -0.0616 -0.4247 1277 GLU A OE2 
9775  N N   . GLN A 1278 ? 0.8013 1.3115 1.1302 0.2602  -0.0757 -0.3481 1278 GLN A N   
9776  C CA  . GLN A 1278 ? 0.8697 1.3588 1.1622 0.2699  -0.0863 -0.3320 1278 GLN A CA  
9777  C C   . GLN A 1278 ? 0.9453 1.3968 1.2144 0.2899  -0.1009 -0.3263 1278 GLN A C   
9778  O O   . GLN A 1278 ? 0.9565 1.3908 1.2215 0.2907  -0.0958 -0.3268 1278 GLN A O   
9779  C CB  . GLN A 1278 ? 0.9612 1.4497 1.2236 0.2543  -0.0704 -0.3137 1278 GLN A CB  
9780  C CG  . GLN A 1278 ? 1.3393 1.8603 1.6197 0.2330  -0.0551 -0.3168 1278 GLN A CG  
9781  C CD  . GLN A 1278 ? 0.7469 1.2876 1.0481 0.2330  -0.0633 -0.3293 1278 GLN A CD  
9782  O OE1 . GLN A 1278 ? 0.7231 1.2704 1.0124 0.2250  -0.0585 -0.3227 1278 GLN A OE1 
9783  N NE2 . GLN A 1278 ? 0.7314 1.2811 1.0624 0.2414  -0.0755 -0.3473 1278 GLN A NE2 
9784  N N   . ARG A 1279 ? 0.9551 1.3909 1.2067 0.3052  -0.1196 -0.3216 1279 ARG A N   
9785  C CA  . ARG A 1279 ? 0.9628 1.3629 1.1947 0.3254  -0.1382 -0.3185 1279 ARG A CA  
9786  C C   . ARG A 1279 ? 0.9217 1.2886 1.1013 0.3229  -0.1344 -0.2985 1279 ARG A C   
9787  O O   . ARG A 1279 ? 0.8977 1.2757 1.0636 0.3092  -0.1199 -0.2890 1279 ARG A O   
9788  C CB  . ARG A 1279 ? 1.0260 1.4306 1.2700 0.3412  -0.1622 -0.3260 1279 ARG A CB  
9789  C CG  . ARG A 1279 ? 1.0536 1.4992 1.3526 0.3413  -0.1651 -0.3470 1279 ARG A CG  
9790  C CD  . ARG A 1279 ? 1.1281 1.5727 1.4512 0.3644  -0.1892 -0.3584 1279 ARG A CD  
9791  N NE  . ARG A 1279 ? 1.1952 1.6055 1.4831 0.3803  -0.2123 -0.3473 1279 ARG A NE  
9792  C CZ  . ARG A 1279 ? 1.2357 1.6451 1.5391 0.4004  -0.2379 -0.3541 1279 ARG A CZ  
9793  N NH1 . ARG A 1279 ? 1.2091 1.6540 1.5658 0.4082  -0.2422 -0.3726 1279 ARG A NH1 
9794  N NH2 . ARG A 1279 ? 1.2882 1.6630 1.5543 0.4122  -0.2590 -0.3426 1279 ARG A NH2 
9795  N N   . TYR A 1280 ? 0.9491 1.2754 1.0983 0.3359  -0.1473 -0.2921 1280 TYR A N   
9796  C CA  . TYR A 1280 ? 0.9851 1.2784 1.0798 0.3320  -0.1440 -0.2733 1280 TYR A CA  
9797  C C   . TYR A 1280 ? 0.7443 1.0463 0.8210 0.3281  -0.1418 -0.2645 1280 TYR A C   
9798  O O   . TYR A 1280 ? 0.7238 1.0295 0.8075 0.3377  -0.1567 -0.2697 1280 TYR A O   
9799  C CB  . TYR A 1280 ? 1.0206 1.2663 1.0845 0.3488  -0.1646 -0.2697 1280 TYR A CB  
9800  C CG  . TYR A 1280 ? 1.0328 1.2432 1.0401 0.3471  -0.1674 -0.2531 1280 TYR A CG  
9801  C CD1 . TYR A 1280 ? 1.1253 1.2934 1.1018 0.3627  -0.1909 -0.2497 1280 TYR A CD1 
9802  C CD2 . TYR A 1280 ? 0.9835 1.2030 0.9678 0.3303  -0.1471 -0.2410 1280 TYR A CD2 
9803  C CE1 . TYR A 1280 ? 1.1687 1.3013 1.0895 0.3593  -0.1930 -0.2352 1280 TYR A CE1 
9804  C CE2 . TYR A 1280 ? 1.0550 1.2441 0.9879 0.3285  -0.1482 -0.2271 1280 TYR A CE2 
9805  C CZ  . TYR A 1280 ? 1.1435 1.2876 1.0432 0.3420  -0.1706 -0.2246 1280 TYR A CZ  
9806  O OH  . TYR A 1280 ? 1.2043 1.3158 1.0498 0.3382  -0.1711 -0.2116 1280 TYR A OH  
9807  N N   . GLY A 1281 ? 0.7482 1.0547 0.8016 0.3140  -0.1227 -0.2516 1281 GLY A N   
9808  C CA  . GLY A 1281 ? 0.7754 1.0916 0.8156 0.3127  -0.1186 -0.2451 1281 GLY A CA  
9809  C C   . GLY A 1281 ? 0.8183 1.1747 0.8890 0.3034  -0.1058 -0.2497 1281 GLY A C   
9810  O O   . GLY A 1281 ? 0.8559 1.2242 0.9139 0.2944  -0.0893 -0.2391 1281 GLY A O   
9811  N N   . GLY A 1282 ? 0.8229 1.2003 0.9319 0.3051  -0.1132 -0.2649 1282 GLY A N   
9812  C CA  . GLY A 1282 ? 0.8802 1.2917 1.0141 0.2933  -0.1008 -0.2696 1282 GLY A CA  
9813  C C   . GLY A 1282 ? 1.0319 1.4670 1.2101 0.2916  -0.1080 -0.2888 1282 GLY A C   
9814  O O   . GLY A 1282 ? 1.0352 1.4653 1.2309 0.3006  -0.1207 -0.2989 1282 GLY A O   
9815  N N   . GLY A 1283 ? 1.1666 1.6269 1.3623 0.2806  -0.1004 -0.2945 1283 GLY A N   
9816  C CA  . GLY A 1283 ? 1.2715 1.7606 1.5105 0.2723  -0.1010 -0.3131 1283 GLY A CA  
9817  C C   . GLY A 1283 ? 1.2857 1.7843 1.5548 0.2811  -0.1193 -0.3311 1283 GLY A C   
9818  O O   . GLY A 1283 ? 1.2268 1.7538 1.5279 0.2708  -0.1175 -0.3460 1283 GLY A O   
9819  N N   . PHE A 1284 ? 1.4253 1.9017 1.6843 0.2991  -0.1368 -0.3296 1284 PHE A N   
9820  C CA  . PHE A 1284 ? 1.5698 2.0528 1.8498 0.3113  -0.1593 -0.3427 1284 PHE A CA  
9821  C C   . PHE A 1284 ? 1.4399 1.9544 1.7472 0.3019  -0.1641 -0.3579 1284 PHE A C   
9822  O O   . PHE A 1284 ? 1.4910 1.9978 1.7842 0.3067  -0.1800 -0.3579 1284 PHE A O   
9823  C CB  . PHE A 1284 ? 1.8554 2.3401 2.1627 0.3243  -0.1677 -0.3521 1284 PHE A CB  
9824  C CG  . PHE A 1284 ? 2.2290 2.7090 2.5448 0.3437  -0.1956 -0.3584 1284 PHE A CG  
9825  C CD1 . PHE A 1284 ? 2.4414 2.8839 2.7153 0.3560  -0.2121 -0.3450 1284 PHE A CD1 
9826  C CD2 . PHE A 1284 ? 2.3924 2.9069 2.7581 0.3491  -0.2054 -0.3778 1284 PHE A CD2 
9827  C CE1 . PHE A 1284 ? 2.6340 3.0718 2.9141 0.3729  -0.2396 -0.3496 1284 PHE A CE1 
9828  C CE2 . PHE A 1284 ? 2.5594 3.0741 2.9354 0.3676  -0.2328 -0.3828 1284 PHE A CE2 
9829  C CZ  . PHE A 1284 ? 2.7124 3.1878 3.0449 0.3793  -0.2507 -0.3681 1284 PHE A CZ  
9830  N N   . TYR A 1285 ? 1.2481 1.7966 1.5924 0.2874  -0.1520 -0.3719 1285 TYR A N   
9831  C CA  . TYR A 1285 ? 1.1097 1.6876 1.4795 0.2788  -0.1598 -0.3880 1285 TYR A CA  
9832  C C   . TYR A 1285 ? 1.0622 1.6283 1.3980 0.2671  -0.1573 -0.3805 1285 TYR A C   
9833  O O   . TYR A 1285 ? 1.1015 1.6659 1.4242 0.2532  -0.1391 -0.3742 1285 TYR A O   
9834  C CB  . TYR A 1285 ? 1.0270 1.6443 1.4429 0.2639  -0.1467 -0.4063 1285 TYR A CB  
9835  C CG  . TYR A 1285 ? 0.9988 1.6229 1.4451 0.2774  -0.1473 -0.4139 1285 TYR A CG  
9836  C CD1 . TYR A 1285 ? 1.0077 1.6192 1.4569 0.3022  -0.1682 -0.4134 1285 TYR A CD1 
9837  C CD2 . TYR A 1285 ? 0.9637 1.6025 1.4318 0.2657  -0.1271 -0.4212 1285 TYR A CD2 
9838  C CE1 . TYR A 1285 ? 0.9947 1.6062 1.4673 0.3169  -0.1689 -0.4197 1285 TYR A CE1 
9839  C CE2 . TYR A 1285 ? 0.9405 1.5793 1.4314 0.2788  -0.1262 -0.4282 1285 TYR A CE2 
9840  C CZ  . TYR A 1285 ? 0.9633 1.5876 1.4561 0.3054  -0.1471 -0.4275 1285 TYR A CZ  
9841  O OH  . TYR A 1285 ? 0.9808 1.6005 1.4935 0.3205  -0.1465 -0.4345 1285 TYR A OH  
9842  N N   . SER A 1286 ? 0.9556 1.5105 1.2739 0.2732  -0.1757 -0.3804 1286 SER A N   
9843  C CA  . SER A 1286 ? 0.8872 1.4281 1.1717 0.2614  -0.1733 -0.3759 1286 SER A CA  
9844  C C   . SER A 1286 ? 0.8415 1.3587 1.0896 0.2569  -0.1536 -0.3593 1286 SER A C   
9845  O O   . SER A 1286 ? 0.8370 1.3397 1.0728 0.2660  -0.1456 -0.3462 1286 SER A O   
9846  C CB  . SER A 1286 ? 0.8627 1.4363 1.1732 0.2411  -0.1731 -0.3943 1286 SER A CB  
9847  O OG  . SER A 1286 ? 0.8495 1.4087 1.1283 0.2252  -0.1627 -0.3903 1286 SER A OG  
9848  N N   . THR A 1287 ? 0.8394 1.3527 1.0690 0.2428  -0.1464 -0.3597 1287 THR A N   
9849  C CA  . THR A 1287 ? 0.8989 1.3881 1.0914 0.2426  -0.1311 -0.3435 1287 THR A CA  
9850  C C   . THR A 1287 ? 0.9776 1.4863 1.1858 0.2261  -0.1126 -0.3448 1287 THR A C   
9851  O O   . THR A 1287 ? 0.9948 1.5055 1.2034 0.2279  -0.0992 -0.3337 1287 THR A O   
9852  C CB  . THR A 1287 ? 0.8824 1.3467 1.0364 0.2387  -0.1351 -0.3421 1287 THR A CB  
9853  O OG1 . THR A 1287 ? 0.8586 1.3423 1.0318 0.2226  -0.1441 -0.3603 1287 THR A OG1 
9854  C CG2 . THR A 1287 ? 0.9194 1.3513 1.0388 0.2553  -0.1476 -0.3333 1287 THR A CG2 
9855  N N   . GLN A 1288 ? 1.0094 1.5317 1.2274 0.2079  -0.1128 -0.3584 1288 GLN A N   
9856  C CA  . GLN A 1288 ? 1.0227 1.5549 1.2434 0.1889  -0.0971 -0.3594 1288 GLN A CA  
9857  C C   . GLN A 1288 ? 1.0345 1.5918 1.2875 0.1828  -0.0845 -0.3600 1288 GLN A C   
9858  O O   . GLN A 1288 ? 1.0732 1.6289 1.3166 0.1755  -0.0705 -0.3499 1288 GLN A O   
9859  C CB  . GLN A 1288 ? 1.0095 1.5536 1.2374 0.1676  -0.1013 -0.3772 1288 GLN A CB  
9860  C CG  . GLN A 1288 ? 1.0495 1.5603 1.2319 0.1669  -0.1070 -0.3731 1288 GLN A CG  
9861  C CD  . GLN A 1288 ? 1.0554 1.5412 1.2025 0.1640  -0.0933 -0.3593 1288 GLN A CD  
9862  O OE1 . GLN A 1288 ? 1.0652 1.5649 1.2243 0.1483  -0.0816 -0.3610 1288 GLN A OE1 
9863  N NE2 . GLN A 1288 ? 1.0538 1.5017 1.1563 0.1793  -0.0946 -0.3458 1288 GLN A NE2 
9864  N N   . ASP A 1289 ? 1.0088 1.5883 1.2989 0.1859  -0.0895 -0.3715 1289 ASP A N   
9865  C CA  . ASP A 1289 ? 0.9926 1.5879 1.3059 0.1816  -0.0767 -0.3704 1289 ASP A CA  
9866  C C   . ASP A 1289 ? 0.9917 1.5651 1.2783 0.1965  -0.0718 -0.3487 1289 ASP A C   
9867  O O   . ASP A 1289 ? 1.0262 1.6012 1.3050 0.1883  -0.0572 -0.3375 1289 ASP A O   
9868  C CB  . ASP A 1289 ? 0.9892 1.6050 1.3419 0.1879  -0.0836 -0.3855 1289 ASP A CB  
9869  C CG  . ASP A 1289 ? 1.0162 1.6156 1.3604 0.2115  -0.1015 -0.3816 1289 ASP A CG  
9870  O OD1 . ASP A 1289 ? 1.0206 1.6124 1.3505 0.2140  -0.1144 -0.3839 1289 ASP A OD1 
9871  O OD2 . ASP A 1289 ? 1.0414 1.6320 1.3882 0.2258  -0.1027 -0.3755 1289 ASP A OD2 
9872  N N   . THR A 1290 ? 0.9431 1.4970 1.2143 0.2168  -0.0842 -0.3425 1290 THR A N   
9873  C CA  . THR A 1290 ? 0.8637 1.3992 1.1114 0.2292  -0.0794 -0.3240 1290 THR A CA  
9874  C C   . THR A 1290 ? 0.7664 1.2950 0.9866 0.2249  -0.0652 -0.3070 1290 THR A C   
9875  O O   . THR A 1290 ? 0.7335 1.2615 0.9455 0.2267  -0.0556 -0.2937 1290 THR A O   
9876  C CB  . THR A 1290 ? 0.8840 1.3941 1.1109 0.2500  -0.0954 -0.3191 1290 THR A CB  
9877  O OG1 . THR A 1290 ? 0.8889 1.4077 1.1447 0.2564  -0.1088 -0.3329 1290 THR A OG1 
9878  C CG2 . THR A 1290 ? 0.8505 1.3421 1.0500 0.2591  -0.0880 -0.3002 1290 THR A CG2 
9879  N N   . ILE A 1291 ? 0.7227 1.2467 0.9282 0.2191  -0.0638 -0.3071 1291 ILE A N   
9880  C CA  . ILE A 1291 ? 0.7041 1.2236 0.8867 0.2179  -0.0508 -0.2907 1291 ILE A CA  
9881  C C   . ILE A 1291 ? 0.6650 1.2093 0.8692 0.1989  -0.0378 -0.2908 1291 ILE A C   
9882  O O   . ILE A 1291 ? 0.6854 1.2357 0.8823 0.1983  -0.0270 -0.2757 1291 ILE A O   
9883  C CB  . ILE A 1291 ? 0.5876 1.0872 0.7407 0.2197  -0.0523 -0.2887 1291 ILE A CB  
9884  C CG1 . ILE A 1291 ? 0.5292 1.0274 0.6630 0.2214  -0.0389 -0.2714 1291 ILE A CG1 
9885  C CG2 . ILE A 1291 ? 0.5858 1.0925 0.7524 0.2018  -0.0569 -0.3062 1291 ILE A CG2 
9886  C CD1 . ILE A 1291 ? 0.5083 0.9868 0.6162 0.2199  -0.0388 -0.2713 1291 ILE A CD1 
9887  N N   . ASN A 1292 ? 0.5946 1.1548 0.8253 0.1820  -0.0388 -0.3081 1292 ASN A N   
9888  C CA  . ASN A 1292 ? 0.5597 1.1407 0.8081 0.1604  -0.0264 -0.3102 1292 ASN A CA  
9889  C C   . ASN A 1292 ? 0.5676 1.1603 0.8328 0.1591  -0.0199 -0.3074 1292 ASN A C   
9890  O O   . ASN A 1292 ? 0.6015 1.2000 0.8592 0.1533  -0.0093 -0.2931 1292 ASN A O   
9891  C CB  . ASN A 1292 ? 0.5351 1.1285 0.8042 0.1418  -0.0284 -0.3309 1292 ASN A CB  
9892  C CG  . ASN A 1292 ? 0.5575 1.1351 0.8015 0.1377  -0.0324 -0.3314 1292 ASN A CG  
9893  O OD1 . ASN A 1292 ? 0.5684 1.1316 0.7845 0.1413  -0.0277 -0.3155 1292 ASN A OD1 
9894  N ND2 . ASN A 1292 ? 0.5526 1.1319 0.8045 0.1309  -0.0413 -0.3492 1292 ASN A ND2 
9895  N N   . ALA A 1293 ? 0.5502 1.1448 0.8358 0.1657  -0.0271 -0.3202 1293 ALA A N   
9896  C CA  . ALA A 1293 ? 0.5812 1.1774 0.8758 0.1676  -0.0222 -0.3174 1293 ALA A CA  
9897  C C   . ALA A 1293 ? 0.6203 1.2040 0.8862 0.1769  -0.0179 -0.2953 1293 ALA A C   
9898  O O   . ALA A 1293 ? 0.6179 1.2071 0.8832 0.1676  -0.0075 -0.2877 1293 ALA A O   
9899  C CB  . ALA A 1293 ? 0.6058 1.1978 0.9187 0.1813  -0.0341 -0.3313 1293 ALA A CB  
9900  N N   . ILE A 1294 ? 0.6812 1.2480 0.9214 0.1939  -0.0251 -0.2851 1294 ILE A N   
9901  C CA  . ILE A 1294 ? 0.7047 1.2647 0.9191 0.2007  -0.0186 -0.2649 1294 ILE A CA  
9902  C C   . ILE A 1294 ? 0.7111 1.2902 0.9233 0.1860  -0.0051 -0.2534 1294 ILE A C   
9903  O O   . ILE A 1294 ? 0.7319 1.3218 0.9420 0.1772  0.0047  -0.2427 1294 ILE A O   
9904  C CB  . ILE A 1294 ? 0.7060 1.2443 0.8907 0.2212  -0.0262 -0.2560 1294 ILE A CB  
9905  C CG1 . ILE A 1294 ? 0.6960 1.2130 0.8770 0.2357  -0.0408 -0.2633 1294 ILE A CG1 
9906  C CG2 . ILE A 1294 ? 0.7014 1.2419 0.8630 0.2246  -0.0155 -0.2356 1294 ILE A CG2 
9907  C CD1 . ILE A 1294 ? 0.6875 1.1892 0.8445 0.2443  -0.0393 -0.2501 1294 ILE A CD1 
9908  N N   . GLU A 1295 ? 0.7000 1.2819 0.9106 0.1824  -0.0053 -0.2553 1295 GLU A N   
9909  C CA  . GLU A 1295 ? 0.6831 1.2807 0.8893 0.1710  0.0051  -0.2430 1295 GLU A CA  
9910  C C   . GLU A 1295 ? 0.6008 1.2181 0.8265 0.1483  0.0141  -0.2452 1295 GLU A C   
9911  O O   . GLU A 1295 ? 0.5882 1.2198 0.8086 0.1410  0.0230  -0.2301 1295 GLU A O   
9912  C CB  . GLU A 1295 ? 0.7660 1.3592 0.9681 0.1662  0.0027  -0.2482 1295 GLU A CB  
9913  C CG  . GLU A 1295 ? 0.8289 1.4346 1.0218 0.1595  0.0113  -0.2321 1295 GLU A CG  
9914  C CD  . GLU A 1295 ? 0.8929 1.4871 1.0739 0.1562  0.0085  -0.2350 1295 GLU A CD  
9915  O OE1 . GLU A 1295 ? 0.8919 1.4622 1.0543 0.1718  0.0013  -0.2384 1295 GLU A OE1 
9916  O OE2 . GLU A 1295 ? 0.9286 1.5345 1.1149 0.1365  0.0133  -0.2335 1295 GLU A OE2 
9917  N N   . GLY A 1296 ? 0.5399 1.1591 0.7878 0.1365  0.0123  -0.2642 1296 GLY A N   
9918  C CA  . GLY A 1296 ? 0.5436 1.1768 0.8085 0.1150  0.0220  -0.2690 1296 GLY A CA  
9919  C C   . GLY A 1296 ? 0.5346 1.1671 0.7910 0.1161  0.0276  -0.2573 1296 GLY A C   
9920  O O   . GLY A 1296 ? 0.5317 1.1772 0.7787 0.1044  0.0365  -0.2420 1296 GLY A O   
9921  N N   . LEU A 1297 ? 0.5289 1.1455 0.7866 0.1293  0.0217  -0.2643 1297 LEU A N   
9922  C CA  . LEU A 1297 ? 0.5475 1.1550 0.7878 0.1330  0.0249  -0.2523 1297 LEU A CA  
9923  C C   . LEU A 1297 ? 0.6070 1.2258 0.8248 0.1315  0.0316  -0.2291 1297 LEU A C   
9924  O O   . LEU A 1297 ? 0.6030 1.2272 0.8104 0.1192  0.0402  -0.2186 1297 LEU A O   
9925  C CB  . LEU A 1297 ? 0.5236 1.1061 0.7566 0.1564  0.0121  -0.2576 1297 LEU A CB  
9926  C CG  . LEU A 1297 ? 0.5341 1.1079 0.7832 0.1516  0.0125  -0.2726 1297 LEU A CG  
9927  C CD1 . LEU A 1297 ? 0.5134 1.0892 0.7919 0.1588  0.0031  -0.2949 1297 LEU A CD1 
9928  C CD2 . LEU A 1297 ? 0.5748 1.1225 0.8007 0.1635  0.0083  -0.2655 1297 LEU A CD2 
9929  N N   . THR A 1298 ? 0.6409 1.2635 0.8499 0.1441  0.0282  -0.2210 1298 THR A N   
9930  C CA  . THR A 1298 ? 0.6528 1.2898 0.8440 0.1460  0.0350  -0.1999 1298 THR A CA  
9931  C C   . THR A 1298 ? 0.6319 1.2961 0.8329 0.1229  0.0442  -0.1930 1298 THR A C   
9932  O O   . THR A 1298 ? 0.6034 1.2829 0.8005 0.1064  0.0528  -0.1828 1298 THR A O   
9933  C CB  . THR A 1298 ? 0.6261 1.2582 0.8035 0.1681  0.0304  -0.1929 1298 THR A CB  
9934  O OG1 . THR A 1298 ? 0.6421 1.2466 0.8154 0.1852  0.0188  -0.2056 1298 THR A OG1 
9935  C CG2 . THR A 1298 ? 0.6245 1.2662 0.7820 0.1766  0.0367  -0.1742 1298 THR A CG2 
9936  N N   . GLU A 1299 ? 0.6628 1.3301 0.8739 0.1200  0.0415  -0.1995 1299 GLU A N   
9937  C CA  . GLU A 1299 ? 0.6810 1.3701 0.8972 0.1014  0.0472  -0.1918 1299 GLU A CA  
9938  C C   . GLU A 1299 ? 0.6720 1.3746 0.8970 0.0719  0.0560  -0.1927 1299 GLU A C   
9939  O O   . GLU A 1299 ? 0.7085 1.4345 0.9306 0.0560  0.0620  -0.1779 1299 GLU A O   
9940  C CB  . GLU A 1299 ? 0.7031 1.3827 0.9246 0.1012  0.0414  -0.2033 1299 GLU A CB  
9941  C CG  . GLU A 1299 ? 0.7757 1.4696 0.9909 0.0950  0.0432  -0.1898 1299 GLU A CG  
9942  C CD  . GLU A 1299 ? 0.8465 1.5398 1.0446 0.1214  0.0407  -0.1740 1299 GLU A CD  
9943  O OE1 . GLU A 1299 ? 0.8922 1.5617 1.0803 0.1408  0.0341  -0.1812 1299 GLU A OE1 
9944  O OE2 . GLU A 1299 ? 0.8487 1.5664 1.0434 0.1221  0.0455  -0.1549 1299 GLU A OE2 
9945  N N   . TYR A 1300 ? 0.6103 1.2980 0.8452 0.0652  0.0565  -0.2100 1300 TYR A N   
9946  C CA  . TYR A 1300 ? 0.5708 1.2627 0.8086 0.0401  0.0660  -0.2123 1300 TYR A CA  
9947  C C   . TYR A 1300 ? 0.5318 1.2272 0.7518 0.0371  0.0714  -0.1970 1300 TYR A C   
9948  O O   . TYR A 1300 ? 0.4658 1.1725 0.6816 0.0121  0.0802  -0.1908 1300 TYR A O   
9949  C CB  . TYR A 1300 ? 0.6145 1.2870 0.8675 0.0388  0.0653  -0.2361 1300 TYR A CB  
9950  C CG  . TYR A 1300 ? 0.6158 1.2811 0.8660 0.0201  0.0752  -0.2401 1300 TYR A CG  
9951  C CD1 . TYR A 1300 ? 0.6278 1.2966 0.8897 -0.0054 0.0843  -0.2524 1300 TYR A CD1 
9952  C CD2 . TYR A 1300 ? 0.6031 1.2541 0.8352 0.0271  0.0759  -0.2325 1300 TYR A CD2 
9953  C CE1 . TYR A 1300 ? 0.6414 1.2991 0.8971 -0.0224 0.0944  -0.2567 1300 TYR A CE1 
9954  C CE2 . TYR A 1300 ? 0.6236 1.2618 0.8476 0.0098  0.0850  -0.2363 1300 TYR A CE2 
9955  C CZ  . TYR A 1300 ? 0.6623 1.3033 0.8981 -0.0143 0.0945  -0.2485 1300 TYR A CZ  
9956  O OH  . TYR A 1300 ? 0.7190 1.3426 0.9428 -0.0320 0.1050  -0.2528 1300 TYR A OH  
9957  N N   . SER A 1301 ? 0.5948 1.2784 0.8017 0.0595  0.0664  -0.1916 1301 SER A N   
9958  C CA  . SER A 1301 ? 0.6466 1.3312 0.8330 0.0531  0.0723  -0.1784 1301 SER A CA  
9959  C C   . SER A 1301 ? 0.5889 1.3085 0.7696 0.0466  0.0770  -0.1569 1301 SER A C   
9960  O O   . SER A 1301 ? 0.5448 1.2784 0.7109 0.0333  0.0839  -0.1432 1301 SER A O   
9961  C CB  . SER A 1301 ? 0.7323 1.3907 0.9027 0.0767  0.0655  -0.1797 1301 SER A CB  
9962  O OG  . SER A 1301 ? 0.7829 1.4117 0.9476 0.0724  0.0653  -0.1917 1301 SER A OG  
9963  N N   . LEU A 1302 ? 0.5868 1.3197 0.7788 0.0563  0.0728  -0.1549 1302 LEU A N   
9964  C CA  . LEU A 1302 ? 0.6357 1.4030 0.8284 0.0531  0.0753  -0.1364 1302 LEU A CA  
9965  C C   . LEU A 1302 ? 0.6607 1.4478 0.8617 0.0225  0.0800  -0.1332 1302 LEU A C   
9966  O O   . LEU A 1302 ? 0.7325 1.5507 0.9294 0.0072  0.0851  -0.1158 1302 LEU A O   
9967  C CB  . LEU A 1302 ? 0.6853 1.4483 0.8823 0.0774  0.0679  -0.1377 1302 LEU A CB  
9968  C CG  . LEU A 1302 ? 0.7311 1.4875 0.9150 0.1060  0.0658  -0.1316 1302 LEU A CG  
9969  C CD1 . LEU A 1302 ? 0.7324 1.4711 0.9154 0.1306  0.0581  -0.1376 1302 LEU A CD1 
9970  C CD2 . LEU A 1302 ? 0.7421 1.5367 0.9206 0.1036  0.0731  -0.1095 1302 LEU A CD2 
9971  N N   . LEU A 1303 ? 0.5860 1.3568 0.7981 0.0128  0.0782  -0.1499 1303 LEU A N   
9972  C CA  . LEU A 1303 ? 0.5110 1.2931 0.7285 -0.0196 0.0831  -0.1509 1303 LEU A CA  
9973  C C   . LEU A 1303 ? 0.4487 1.2317 0.6586 -0.0489 0.0929  -0.1507 1303 LEU A C   
9974  O O   . LEU A 1303 ? 0.4375 1.2428 0.6432 -0.0747 0.0975  -0.1387 1303 LEU A O   
9975  C CB  . LEU A 1303 ? 0.5083 1.2712 0.7378 -0.0222 0.0797  -0.1711 1303 LEU A CB  
9976  C CG  . LEU A 1303 ? 0.4744 1.2335 0.7108 -0.0536 0.0852  -0.1841 1303 LEU A CG  
9977  C CD1 . LEU A 1303 ? 0.4410 1.1953 0.6736 -0.0758 0.0955  -0.1888 1303 LEU A CD1 
9978  C CD2 . LEU A 1303 ? 0.4973 1.2759 0.7297 -0.0713 0.0839  -0.1708 1303 LEU A CD2 
9979  N N   . VAL A 1304 ? 0.4467 1.2030 0.6526 -0.0453 0.0956  -0.1639 1304 VAL A N   
9980  C CA  . VAL A 1304 ? 0.5062 1.2552 0.6974 -0.0700 0.1053  -0.1632 1304 VAL A CA  
9981  C C   . VAL A 1304 ? 0.5161 1.2738 0.6873 -0.0654 0.1068  -0.1459 1304 VAL A C   
9982  O O   . VAL A 1304 ? 0.5714 1.3211 0.7400 -0.0372 0.1007  -0.1449 1304 VAL A O   
9983  C CB  . VAL A 1304 ? 0.5624 1.2730 0.7557 -0.0648 0.1071  -0.1860 1304 VAL A CB  
9984  C CG1 . VAL A 1304 ? 0.6214 1.3159 0.7920 -0.0853 0.1167  -0.1842 1304 VAL A CG1 
9985  C CG2 . VAL A 1304 ? 0.5366 1.2389 0.7506 -0.0726 0.1085  -0.2070 1304 VAL A CG2 
9986  N N   . LYS A 1305 ? 0.8747 1.7914 0.8889 0.1347  -0.0095 -0.2520 1305 LYS A N   
9987  C CA  . LYS A 1305 ? 0.8869 1.8489 0.8878 0.1394  -0.0110 -0.2367 1305 LYS A CA  
9988  C C   . LYS A 1305 ? 0.9306 1.8709 0.9307 0.1364  -0.0182 -0.2455 1305 LYS A C   
9989  O O   . LYS A 1305 ? 0.9521 1.8494 0.9635 0.1192  -0.0213 -0.2617 1305 LYS A O   
9990  C CB  . LYS A 1305 ? 0.8967 1.9138 0.8947 0.1127  -0.0049 -0.2175 1305 LYS A CB  
9991  C CG  . LYS A 1305 ? 0.9764 2.0547 0.9596 0.1289  -0.0039 -0.1965 1305 LYS A CG  
9992  C CD  . LYS A 1305 ? 1.1186 2.2591 1.0979 0.1236  0.0034  -0.1757 1305 LYS A CD  
9993  C CE  . LYS A 1305 ? 1.2779 2.4191 1.2523 0.1562  0.0069  -0.1737 1305 LYS A CE  
9994  N NZ  . LYS A 1305 ? 1.2646 2.4654 1.2366 0.1466  0.0138  -0.1543 1305 LYS A NZ  
9995  N N   . GLN A 1306 ? 0.9597 1.9306 0.9455 0.1549  -0.0206 -0.2345 1306 GLN A N   
9996  C CA  . GLN A 1306 ? 0.9567 1.9099 0.9387 0.1535  -0.0272 -0.2407 1306 GLN A CA  
9997  C C   . GLN A 1306 ? 0.9695 1.9314 0.9541 0.1132  -0.0252 -0.2354 1306 GLN A C   
9998  O O   . GLN A 1306 ? 0.9929 1.9725 0.9823 0.0885  -0.0195 -0.2287 1306 GLN A O   
9999  C CB  . GLN A 1306 ? 1.4436 2.4314 1.4077 0.1829  -0.0292 -0.2283 1306 GLN A CB  
10000 C CG  . GLN A 1306 ? 2.0997 3.0435 2.0585 0.2176  -0.0379 -0.2455 1306 GLN A CG  
10001 C CD  . GLN A 1306 ? 1.2081 2.1812 1.1474 0.2444  -0.0406 -0.2350 1306 GLN A CD  
10002 O OE1 . GLN A 1306 ? 1.1974 2.1815 1.1318 0.2321  -0.0421 -0.2293 1306 GLN A OE1 
10003 N NE2 . GLN A 1306 ? 1.2245 2.2064 1.1506 0.2820  -0.0411 -0.2329 1306 GLN A NE2 
10004 N N   . LEU A 1307 ? 0.9290 1.8752 0.9081 0.1059  -0.0301 -0.2386 1307 LEU A N   
10005 C CA  . LEU A 1307 ? 0.9236 1.8795 0.8988 0.0677  -0.0282 -0.2305 1307 LEU A CA  
10006 C C   . LEU A 1307 ? 0.9077 1.8743 0.8680 0.0669  -0.0317 -0.2217 1307 LEU A C   
10007 O O   . LEU A 1307 ? 0.9151 1.8382 0.8736 0.0703  -0.0377 -0.2350 1307 LEU A O   
10008 C CB  . LEU A 1307 ? 0.9347 1.8372 0.9205 0.0436  -0.0295 -0.2487 1307 LEU A CB  
10009 C CG  . LEU A 1307 ? 0.9375 1.8063 0.9406 0.0426  -0.0276 -0.2651 1307 LEU A CG  
10010 C CD1 . LEU A 1307 ? 0.9855 1.8196 0.9979 0.0762  -0.0329 -0.2821 1307 LEU A CD1 
10011 C CD2 . LEU A 1307 ? 0.9419 1.7726 0.9481 0.0123  -0.0279 -0.2763 1307 LEU A CD2 
10012 N N   . ARG A 1308 ? 0.8812 1.9086 0.8308 0.0609  -0.0276 -0.1982 1308 ARG A N   
10013 C CA  . ARG A 1308 ? 0.8355 1.8854 0.7696 0.0553  -0.0290 -0.1843 1308 ARG A CA  
10014 C C   . ARG A 1308 ? 0.7896 1.7825 0.7187 0.0435  -0.0349 -0.1979 1308 ARG A C   
10015 O O   . ARG A 1308 ? 0.7568 1.7237 0.6852 0.0102  -0.0347 -0.2019 1308 ARG A O   
10016 C CB  . ARG A 1308 ? 0.8169 1.9260 0.7447 0.0227  -0.0234 -0.1603 1308 ARG A CB  
10017 C CG  . ARG A 1308 ? 0.8295 1.9437 0.7423 -0.0042 -0.0248 -0.1488 1308 ARG A CG  
10018 C CD  . ARG A 1308 ? 0.8454 2.0393 0.7515 -0.0218 -0.0195 -0.1203 1308 ARG A CD  
10019 N NE  . ARG A 1308 ? 0.8795 2.0870 0.7691 -0.0382 -0.0206 -0.1058 1308 ARG A NE  
10020 C CZ  . ARG A 1308 ? 0.9295 2.0889 0.8084 -0.0683 -0.0241 -0.1114 1308 ARG A CZ  
10021 N NH1 . ARG A 1308 ? 0.9172 2.0151 0.8009 -0.0844 -0.0266 -0.1316 1308 ARG A NH1 
10022 N NH2 . ARG A 1308 ? 0.9683 2.1404 0.8301 -0.0814 -0.0248 -0.0966 1308 ARG A NH2 
10023 N N   . LEU A 1309 ? 0.7994 1.7730 0.7230 0.0731  -0.0403 -0.2051 1309 LEU A N   
10024 C CA  . LEU A 1309 ? 0.8147 1.7365 0.7317 0.0698  -0.0467 -0.2177 1309 LEU A CA  
10025 C C   . LEU A 1309 ? 0.8368 1.7722 0.7350 0.0426  -0.0457 -0.2008 1309 LEU A C   
10026 O O   . LEU A 1309 ? 0.8156 1.8045 0.7025 0.0444  -0.0424 -0.1791 1309 LEU A O   
10027 C CB  . LEU A 1309 ? 0.7966 1.7012 0.7105 0.1107  -0.0533 -0.2280 1309 LEU A CB  
10028 C CG  . LEU A 1309 ? 0.7725 1.6369 0.7019 0.1366  -0.0584 -0.2518 1309 LEU A CG  
10029 C CD1 . LEU A 1309 ? 0.7848 1.6579 0.7054 0.1766  -0.0629 -0.2528 1309 LEU A CD1 
10030 C CD2 . LEU A 1309 ? 0.7424 1.5467 0.6784 0.1281  -0.0646 -0.2726 1309 LEU A CD2 
10031 N N   . SER A 1310 ? 0.7721 1.6583 0.6655 0.0185  -0.0484 -0.2105 1310 SER A N   
10032 C CA  . SER A 1310 ? 0.8086 1.6942 0.6802 -0.0065 -0.0485 -0.1965 1310 SER A CA  
10033 C C   . SER A 1310 ? 0.8784 1.6954 0.7423 -0.0221 -0.0530 -0.2122 1310 SER A C   
10034 O O   . SER A 1310 ? 0.8343 1.6389 0.6835 -0.0575 -0.0514 -0.2050 1310 SER A O   
10035 C CB  . SER A 1310 ? 0.8347 1.7726 0.6993 -0.0418 -0.0422 -0.1729 1310 SER A CB  
10036 O OG  . SER A 1310 ? 0.8736 1.7900 0.7170 -0.0765 -0.0430 -0.1648 1310 SER A OG  
10037 N N   . MET A 1311 ? 0.9138 1.6865 0.7866 0.0052  -0.0589 -0.2340 1311 MET A N   
10038 C CA  . MET A 1311 ? 0.9686 1.6811 0.8303 0.0021  -0.0643 -0.2471 1311 MET A CA  
10039 C C   . MET A 1311 ? 1.0394 1.7499 0.8755 0.0038  -0.0669 -0.2342 1311 MET A C   
10040 O O   . MET A 1311 ? 1.0194 1.7789 0.8460 0.0051  -0.0639 -0.2134 1311 MET A O   
10041 C CB  . MET A 1311 ? 0.8222 1.4983 0.7016 0.0336  -0.0706 -0.2720 1311 MET A CB  
10042 C CG  . MET A 1311 ? 0.8075 1.4605 0.7066 0.0245  -0.0690 -0.2884 1311 MET A CG  
10043 S SD  . MET A 1311 ? 1.0451 1.6911 0.9723 0.0616  -0.0737 -0.3094 1311 MET A SD  
10044 C CE  . MET A 1311 ? 1.0668 1.7726 1.0031 0.0623  -0.0663 -0.2941 1311 MET A CE  
10045 N N   . ASP A 1312 ? 1.0818 1.7355 0.9066 0.0056  -0.0723 -0.2468 1312 ASP A N   
10046 C CA  . ASP A 1312 ? 1.1421 1.7800 0.9385 0.0030  -0.0748 -0.2359 1312 ASP A CA  
10047 C C   . ASP A 1312 ? 1.1147 1.6954 0.9102 0.0273  -0.0829 -0.2576 1312 ASP A C   
10048 O O   . ASP A 1312 ? 1.1316 1.6629 0.9087 0.0144  -0.0851 -0.2621 1312 ASP A O   
10049 C CB  . ASP A 1312 ? 1.2254 1.8485 0.9983 -0.0404 -0.0711 -0.2225 1312 ASP A CB  
10050 C CG  . ASP A 1312 ? 1.3216 1.9587 1.0659 -0.0506 -0.0703 -0.1999 1312 ASP A CG  
10051 O OD1 . ASP A 1312 ? 1.3465 1.9859 1.0854 -0.0206 -0.0740 -0.1992 1312 ASP A OD1 
10052 O OD2 . ASP A 1312 ? 1.3660 2.0121 1.0928 -0.0895 -0.0662 -0.1827 1312 ASP A OD2 
10053 N N   . ILE A 1313 ? 1.0756 1.6633 0.8905 0.0632  -0.0877 -0.2714 1313 ILE A N   
10054 C CA  . ILE A 1313 ? 1.0663 1.6077 0.8895 0.0873  -0.0961 -0.2953 1313 ILE A CA  
10055 C C   . ILE A 1313 ? 1.1446 1.6518 0.9415 0.0948  -0.1014 -0.2937 1313 ILE A C   
10056 O O   . ILE A 1313 ? 1.2348 1.7599 1.0083 0.0910  -0.0996 -0.2741 1313 ILE A O   
10057 C CB  . ILE A 1313 ? 0.9932 1.5532 0.8368 0.1225  -0.1011 -0.3067 1313 ILE A CB  
10058 C CG1 . ILE A 1313 ? 0.9736 1.5805 0.8333 0.1168  -0.0943 -0.2985 1313 ILE A CG1 
10059 C CG2 . ILE A 1313 ? 0.9806 1.5005 0.8438 0.1382  -0.1083 -0.3336 1313 ILE A CG2 
10060 C CD1 . ILE A 1313 ? 0.9749 1.5716 0.8635 0.1276  -0.0963 -0.3187 1313 ILE A CD1 
10061 N N   . ASP A 1314 ? 1.1175 1.5766 0.9180 0.1062  -0.1078 -0.3141 1314 ASP A N   
10062 C CA  . ASP A 1314 ? 1.1328 1.5562 0.9084 0.1177  -0.1136 -0.3145 1314 ASP A CA  
10063 C C   . ASP A 1314 ? 1.1050 1.4975 0.8966 0.1472  -0.1231 -0.3399 1314 ASP A C   
10064 O O   . ASP A 1314 ? 1.1083 1.4715 0.9128 0.1418  -0.1237 -0.3561 1314 ASP A O   
10065 C CB  . ASP A 1314 ? 1.1761 1.5602 0.9235 0.0875  -0.1100 -0.3066 1314 ASP A CB  
10066 C CG  . ASP A 1314 ? 1.2478 1.5795 0.9746 0.1043  -0.1173 -0.3159 1314 ASP A CG  
10067 O OD1 . ASP A 1314 ? 1.2351 1.5350 0.9761 0.1194  -0.1224 -0.3381 1314 ASP A OD1 
10068 O OD2 . ASP A 1314 ? 1.3229 1.6474 1.0188 0.1035  -0.1178 -0.3002 1314 ASP A OD2 
10069 N N   . VAL A 1315 ? 1.0940 1.4956 0.8842 0.1788  -0.1307 -0.3432 1315 VAL A N   
10070 C CA  . VAL A 1315 ? 1.0861 1.4627 0.8899 0.2084  -0.1416 -0.3666 1315 VAL A CA  
10071 C C   . VAL A 1315 ? 1.1238 1.4612 0.8967 0.2146  -0.1460 -0.3641 1315 VAL A C   
10072 O O   . VAL A 1315 ? 1.1597 1.5023 0.9030 0.2091  -0.1432 -0.3441 1315 VAL A O   
10073 C CB  . VAL A 1315 ? 1.0693 1.4771 0.8886 0.2380  -0.1480 -0.3730 1315 VAL A CB  
10074 C CG1 . VAL A 1315 ? 0.9718 1.4065 0.7654 0.2472  -0.1467 -0.3526 1315 VAL A CG1 
10075 C CG2 . VAL A 1315 ? 0.9565 1.3413 0.7911 0.2660  -0.1604 -0.3976 1315 VAL A CG2 
10076 N N   . SER A 1316 ? 1.1679 1.4664 0.9460 0.2246  -0.1521 -0.3829 1316 SER A N   
10077 C CA  . SER A 1316 ? 1.2784 1.5326 1.0241 0.2273  -0.1549 -0.3801 1316 SER A CA  
10078 C C   . SER A 1316 ? 1.3440 1.5655 1.1008 0.2509  -0.1644 -0.4040 1316 SER A C   
10079 O O   . SER A 1316 ? 1.3371 1.5601 1.1250 0.2510  -0.1651 -0.4214 1316 SER A O   
10080 C CB  . SER A 1316 ? 1.3037 1.5340 1.0257 0.1909  -0.1449 -0.3660 1316 SER A CB  
10081 O OG  . SER A 1316 ? 1.3630 1.5569 1.0438 0.1909  -0.1462 -0.3546 1316 SER A OG  
10082 N N   . TYR A 1317 ? 1.4103 1.6043 1.1416 0.2711  -0.1714 -0.4040 1317 TYR A N   
10083 C CA  . TYR A 1317 ? 1.4692 1.6369 1.2103 0.2957  -0.1810 -0.4257 1317 TYR A CA  
10084 C C   . TYR A 1317 ? 1.5060 1.6293 1.2320 0.2809  -0.1760 -0.4283 1317 TYR A C   
10085 O O   . TYR A 1317 ? 1.5414 1.6359 1.2293 0.2634  -0.1700 -0.4114 1317 TYR A O   
10086 C CB  . TYR A 1317 ? 1.5541 1.7104 1.2719 0.3256  -0.1910 -0.4246 1317 TYR A CB  
10087 C CG  . TYR A 1317 ? 1.5969 1.7931 1.3286 0.3456  -0.1977 -0.4260 1317 TYR A CG  
10088 C CD1 . TYR A 1317 ? 1.6393 1.8574 1.3497 0.3410  -0.1932 -0.4049 1317 TYR A CD1 
10089 C CD2 . TYR A 1317 ? 1.6079 1.8207 1.3732 0.3686  -0.2085 -0.4484 1317 TYR A CD2 
10090 C CE1 . TYR A 1317 ? 1.6591 1.9126 1.3793 0.3619  -0.1992 -0.4067 1317 TYR A CE1 
10091 C CE2 . TYR A 1317 ? 1.6314 1.8758 1.4059 0.3874  -0.2155 -0.4510 1317 TYR A CE2 
10092 C CZ  . TYR A 1317 ? 1.6632 1.9270 1.4141 0.3856  -0.2107 -0.4305 1317 TYR A CZ  
10093 O OH  . TYR A 1317 ? 1.6722 1.9656 1.4290 0.4075  -0.2178 -0.4339 1317 TYR A OH  
10094 N N   . LYS A 1318 ? 1.4957 1.6122 1.2493 0.2882  -0.1785 -0.4490 1318 LYS A N   
10095 C CA  . LYS A 1318 ? 1.5423 1.6158 1.2806 0.2780  -0.1737 -0.4532 1318 LYS A CA  
10096 C C   . LYS A 1318 ? 1.6514 1.6737 1.3408 0.2859  -0.1754 -0.4447 1318 LYS A C   
10097 O O   . LYS A 1318 ? 1.6641 1.6492 1.3225 0.2635  -0.1676 -0.4351 1318 LYS A O   
10098 C CB  . LYS A 1318 ? 1.5172 1.5946 1.2921 0.2924  -0.1775 -0.4775 1318 LYS A CB  
10099 C CG  . LYS A 1318 ? 1.5819 1.6108 1.3346 0.2972  -0.1760 -0.4842 1318 LYS A CG  
10100 C CD  . LYS A 1318 ? 1.5867 1.6151 1.3625 0.2821  -0.1683 -0.4953 1318 LYS A CD  
10101 C CE  . LYS A 1318 ? 1.5666 1.6300 1.3931 0.3008  -0.1744 -0.5168 1318 LYS A CE  
10102 N NZ  . LYS A 1318 ? 1.5625 1.6254 1.4093 0.2866  -0.1659 -0.5264 1318 LYS A NZ  
10103 N N   . HIS A 1319 ? 1.7518 1.7693 1.4316 0.3174  -0.1859 -0.4484 1319 HIS A N   
10104 C CA  . HIS A 1319 ? 1.8691 1.8369 1.4994 0.3271  -0.1877 -0.4389 1319 HIS A CA  
10105 C C   . HIS A 1319 ? 2.0223 1.9952 1.6223 0.3286  -0.1890 -0.4183 1319 HIS A C   
10106 O O   . HIS A 1319 ? 2.0649 1.9990 1.6190 0.3155  -0.1843 -0.4007 1319 HIS A O   
10107 C CB  . HIS A 1319 ? 1.8192 1.7682 1.4532 0.3636  -0.1981 -0.4577 1319 HIS A CB  
10108 C CG  . HIS A 1319 ? 1.7734 1.7301 1.4442 0.3666  -0.1978 -0.4788 1319 HIS A CG  
10109 N ND1 . HIS A 1319 ? 1.7272 1.7314 1.4494 0.3776  -0.2037 -0.4958 1319 HIS A ND1 
10110 C CD2 . HIS A 1319 ? 1.8002 1.7232 1.4628 0.3592  -0.1917 -0.4852 1319 HIS A CD2 
10111 C CE1 . HIS A 1319 ? 1.7195 1.7222 1.4657 0.3765  -0.2011 -0.5110 1319 HIS A CE1 
10112 N NE2 . HIS A 1319 ? 1.7663 1.7211 1.4772 0.3666  -0.1936 -0.5051 1319 HIS A NE2 
10113 N N   . LYS A 1320 ? 2.1332 2.1519 1.7567 0.3445  -0.1952 -0.4205 1320 LYS A N   
10114 C CA  . LYS A 1320 ? 2.2971 2.3293 1.8951 0.3466  -0.1953 -0.4007 1320 LYS A CA  
10115 C C   . LYS A 1320 ? 2.3849 2.4302 1.9699 0.3081  -0.1827 -0.3776 1320 LYS A C   
10116 O O   . LYS A 1320 ? 2.3814 2.4456 1.9910 0.2845  -0.1759 -0.3799 1320 LYS A O   
10117 C CB  . LYS A 1320 ? 2.3200 2.3994 1.9465 0.3724  -0.2046 -0.4099 1320 LYS A CB  
10118 C CG  . LYS A 1320 ? 2.3858 2.4892 1.9902 0.3725  -0.2026 -0.3887 1320 LYS A CG  
10119 C CD  . LYS A 1320 ? 2.4880 2.5551 2.0438 0.3845  -0.2047 -0.3746 1320 LYS A CD  
10120 C CE  . LYS A 1320 ? 2.5186 2.6133 2.0521 0.3844  -0.2016 -0.3520 1320 LYS A CE  
10121 N NZ  . LYS A 1320 ? 2.5752 2.6367 2.0622 0.3998  -0.2046 -0.3389 1320 LYS A NZ  
10122 N N   . GLY A 1321 ? 2.4458 2.4841 1.9926 0.3020  -0.1798 -0.3548 1321 GLY A N   
10123 C CA  . GLY A 1321 ? 2.4449 2.5033 1.9791 0.2662  -0.1686 -0.3309 1321 GLY A CA  
10124 C C   . GLY A 1321 ? 2.3800 2.4970 1.9556 0.2566  -0.1650 -0.3335 1321 GLY A C   
10125 O O   . GLY A 1321 ? 2.3845 2.5290 1.9952 0.2805  -0.1719 -0.3517 1321 GLY A O   
10126 N N   . ALA A 1322 ? 2.2918 2.4274 1.8622 0.2209  -0.1544 -0.3152 1322 ALA A N   
10127 C CA  . ALA A 1322 ? 2.1748 2.3652 1.7810 0.2104  -0.1499 -0.3154 1322 ALA A CA  
10128 C C   . ALA A 1322 ? 2.0772 2.3154 1.6968 0.2376  -0.1543 -0.3139 1322 ALA A C   
10129 O O   . ALA A 1322 ? 2.0484 2.2947 1.6418 0.2462  -0.1545 -0.2977 1322 ALA A O   
10130 C CB  . ALA A 1322 ? 2.1394 2.3442 1.7326 0.1675  -0.1383 -0.2929 1322 ALA A CB  
10131 N N   . LEU A 1323 ? 2.0513 2.3191 1.7096 0.2517  -0.1577 -0.3309 1323 LEU A N   
10132 C CA  . LEU A 1323 ? 1.9630 2.2792 1.6331 0.2711  -0.1597 -0.3274 1323 LEU A CA  
10133 C C   . LEU A 1323 ? 2.0004 2.3587 1.6768 0.2422  -0.1480 -0.3091 1323 LEU A C   
10134 O O   . LEU A 1323 ? 2.0921 2.4390 1.7574 0.2078  -0.1397 -0.2971 1323 LEU A O   
10135 C CB  . LEU A 1323 ? 1.6571 1.9792 1.3615 0.2992  -0.1698 -0.3544 1323 LEU A CB  
10136 C CG  . LEU A 1323 ? 1.4061 1.7726 1.1354 0.3140  -0.1716 -0.3595 1323 LEU A CG  
10137 C CD1 . LEU A 1323 ? 1.2888 1.6890 0.9969 0.3272  -0.1699 -0.3411 1323 LEU A CD1 
10138 C CD2 . LEU A 1323 ? 1.2474 1.6030 1.0014 0.3423  -0.1846 -0.3874 1323 LEU A CD2 
10139 N N   . HIS A 1324 ? 1.9311 2.3370 1.6227 0.2565  -0.1476 -0.3067 1324 HIS A N   
10140 C CA  . HIS A 1324 ? 1.8959 2.3495 1.5901 0.2345  -0.1368 -0.2864 1324 HIS A CA  
10141 C C   . HIS A 1324 ? 1.8453 2.3031 1.5606 0.2028  -0.1296 -0.2884 1324 HIS A C   
10142 O O   . HIS A 1324 ? 1.8170 2.2466 1.5522 0.2021  -0.1330 -0.3088 1324 HIS A O   
10143 C CB  . HIS A 1324 ? 1.8957 2.3965 1.5999 0.2629  -0.1387 -0.2854 1324 HIS A CB  
10144 C CG  . HIS A 1324 ? 1.9479 2.4567 1.6866 0.2764  -0.1428 -0.3068 1324 HIS A CG  
10145 N ND1 . HIS A 1324 ? 1.9553 2.4944 1.7139 0.2592  -0.1351 -0.3028 1324 HIS A ND1 
10146 C CD2 . HIS A 1324 ? 1.9769 2.4675 1.7324 0.3048  -0.1541 -0.3317 1324 HIS A CD2 
10147 C CE1 . HIS A 1324 ? 1.9584 2.4944 1.7434 0.2762  -0.1410 -0.3239 1324 HIS A CE1 
10148 N NE2 . HIS A 1324 ? 1.9764 2.4836 1.7606 0.3028  -0.1527 -0.3419 1324 HIS A NE2 
10149 N N   . ASN A 1325 ? 1.8685 2.3652 1.5790 0.1771  -0.1196 -0.2664 1325 ASN A N   
10150 C CA  . ASN A 1325 ? 1.8828 2.3880 1.6083 0.1446  -0.1122 -0.2645 1325 ASN A CA  
10151 C C   . ASN A 1325 ? 1.8017 2.3672 1.5257 0.1278  -0.1030 -0.2402 1325 ASN A C   
10152 O O   . ASN A 1325 ? 1.8009 2.3815 1.4998 0.1109  -0.0984 -0.2172 1325 ASN A O   
10153 C CB  . ASN A 1325 ? 2.0018 2.4586 1.7083 0.1133  -0.1101 -0.2629 1325 ASN A CB  
10154 C CG  . ASN A 1325 ? 2.0882 2.5335 1.7555 0.0994  -0.1081 -0.2411 1325 ASN A CG  
10155 O OD1 . ASN A 1325 ? 2.1207 2.5303 1.7685 0.1180  -0.1142 -0.2452 1325 ASN A OD1 
10156 N ND2 . ASN A 1325 ? 2.1034 2.5785 1.7584 0.0653  -0.0996 -0.2173 1325 ASN A ND2 
10157 N N   . TYR A 1326 ? 1.7405 2.3413 1.4909 0.1311  -0.1002 -0.2444 1326 TYR A N   
10158 C CA  . TYR A 1326 ? 1.7326 2.3981 1.4830 0.1259  -0.0925 -0.2224 1326 TYR A CA  
10159 C C   . TYR A 1326 ? 1.5870 2.2834 1.3562 0.1016  -0.0853 -0.2179 1326 TYR A C   
10160 O O   . TYR A 1326 ? 1.5584 2.2414 1.3511 0.1066  -0.0870 -0.2362 1326 TYR A O   
10161 C CB  . TYR A 1326 ? 1.8289 2.5231 1.5865 0.1678  -0.0963 -0.2271 1326 TYR A CB  
10162 C CG  . TYR A 1326 ? 1.9109 2.5835 1.6949 0.1899  -0.1028 -0.2541 1326 TYR A CG  
10163 C CD1 . TYR A 1326 ? 1.9295 2.6365 1.7329 0.1999  -0.1000 -0.2561 1326 TYR A CD1 
10164 C CD2 . TYR A 1326 ? 1.9724 2.5901 1.7610 0.2006  -0.1119 -0.2770 1326 TYR A CD2 
10165 C CE1 . TYR A 1326 ? 1.9505 2.6347 1.7765 0.2180  -0.1061 -0.2801 1326 TYR A CE1 
10166 C CE2 . TYR A 1326 ? 1.9920 2.5922 1.8056 0.2184  -0.1181 -0.3010 1326 TYR A CE2 
10167 C CZ  . TYR A 1326 ? 1.9830 2.6148 1.8150 0.2259  -0.1152 -0.3025 1326 TYR A CZ  
10168 O OH  . TYR A 1326 ? 1.9812 2.5923 1.8367 0.2414  -0.1216 -0.3259 1326 TYR A OH  
10169 N N   . LYS A 1327 ? 1.4989 2.2411 1.2574 0.0762  -0.0774 -0.1923 1327 LYS A N   
10170 C CA  . LYS A 1327 ? 1.3845 2.1689 1.1589 0.0556  -0.0704 -0.1841 1327 LYS A CA  
10171 C C   . LYS A 1327 ? 1.2416 2.0627 1.0379 0.0889  -0.0702 -0.1908 1327 LYS A C   
10172 O O   . LYS A 1327 ? 1.2194 2.0843 1.0102 0.1124  -0.0687 -0.1788 1327 LYS A O   
10173 C CB  . LYS A 1327 ? 1.4288 2.2619 1.1862 0.0235  -0.0629 -0.1535 1327 LYS A CB  
10174 C CG  . LYS A 1327 ? 1.4623 2.3339 1.2336 -0.0058 -0.0566 -0.1449 1327 LYS A CG  
10175 C CD  . LYS A 1327 ? 1.5158 2.3958 1.2685 -0.0558 -0.0524 -0.1246 1327 LYS A CD  
10176 C CE  . LYS A 1327 ? 1.4771 2.3725 1.2440 -0.0867 -0.0487 -0.1251 1327 LYS A CE  
10177 N NZ  . LYS A 1327 ? 1.4512 2.2814 1.2272 -0.0915 -0.0523 -0.1513 1327 LYS A NZ  
10178 N N   . MET A 1328 ? 1.1391 1.9394 0.9581 0.0909  -0.0716 -0.2100 1328 MET A N   
10179 C CA  . MET A 1328 ? 0.9983 1.8254 0.8371 0.1166  -0.0710 -0.2170 1328 MET A CA  
10180 C C   . MET A 1328 ? 0.9902 1.8737 0.8355 0.0973  -0.0621 -0.1990 1328 MET A C   
10181 O O   . MET A 1328 ? 0.9854 1.8706 0.8292 0.0596  -0.0579 -0.1911 1328 MET A O   
10182 C CB  . MET A 1328 ? 0.8902 1.6688 0.7499 0.1238  -0.0761 -0.2445 1328 MET A CB  
10183 C CG  . MET A 1328 ? 0.8193 1.6173 0.6983 0.1428  -0.0749 -0.2517 1328 MET A CG  
10184 S SD  . MET A 1328 ? 0.7922 1.5289 0.6906 0.1638  -0.0845 -0.2852 1328 MET A SD  
10185 C CE  . MET A 1328 ? 1.4334 2.1766 1.3208 0.2102  -0.0924 -0.2890 1328 MET A CE  
10186 N N   . THR A 1329 ? 0.9961 1.9245 0.8469 0.1239  -0.0596 -0.1929 1329 THR A N   
10187 C CA  . THR A 1329 ? 0.9779 1.9711 0.8325 0.1116  -0.0511 -0.1724 1329 THR A CA  
10188 C C   . THR A 1329 ? 0.9495 1.9699 0.8122 0.1496  -0.0503 -0.1754 1329 THR A C   
10189 O O   . THR A 1329 ? 0.9597 1.9508 0.8220 0.1836  -0.0566 -0.1914 1329 THR A O   
10190 C CB  . THR A 1329 ? 0.9979 2.0452 0.8344 0.0982  -0.0461 -0.1441 1329 THR A CB  
10191 O OG1 . THR A 1329 ? 1.0058 2.0533 0.8273 0.1298  -0.0494 -0.1423 1329 THR A OG1 
10192 C CG2 . THR A 1329 ? 1.0288 2.0551 0.8556 0.0519  -0.0454 -0.1372 1329 THR A CG2 
10193 N N   . ASP A 1330 ? 0.9304 2.0047 0.7988 0.1458  -0.0433 -0.1608 1330 ASP A N   
10194 C CA  . ASP A 1330 ? 0.9581 2.0487 0.8295 0.1865  -0.0432 -0.1652 1330 ASP A CA  
10195 C C   . ASP A 1330 ? 0.9938 2.1165 0.8467 0.2209  -0.0436 -0.1541 1330 ASP A C   
10196 O O   . ASP A 1330 ? 1.0215 2.1542 0.8703 0.2597  -0.0444 -0.1577 1330 ASP A O   
10197 C CB  . ASP A 1330 ? 0.9650 2.1022 0.8461 0.1804  -0.0359 -0.1540 1330 ASP A CB  
10198 C CG  . ASP A 1330 ? 0.9624 2.0777 0.8582 0.1414  -0.0343 -0.1602 1330 ASP A CG  
10199 O OD1 . ASP A 1330 ? 0.9206 1.9769 0.8282 0.1410  -0.0386 -0.1832 1330 ASP A OD1 
10200 O OD2 . ASP A 1330 ? 0.9884 2.1502 0.8835 0.1112  -0.0285 -0.1409 1330 ASP A OD2 
10201 N N   . LYS A 1331 ? 1.0043 2.1410 0.8436 0.2071  -0.0430 -0.1405 1331 LYS A N   
10202 C CA  . LYS A 1331 ? 1.0231 2.1912 0.8438 0.2387  -0.0427 -0.1292 1331 LYS A CA  
10203 C C   . LYS A 1331 ? 1.0367 2.1467 0.8514 0.2747  -0.0526 -0.1533 1331 LYS A C   
10204 O O   . LYS A 1331 ? 1.0380 2.1504 0.8484 0.3145  -0.0547 -0.1607 1331 LYS A O   
10205 C CB  . LYS A 1331 ? 1.0333 2.2275 0.8410 0.2103  -0.0393 -0.1081 1331 LYS A CB  
10206 C CG  . LYS A 1331 ? 0.9985 2.2474 0.8126 0.1705  -0.0311 -0.0857 1331 LYS A CG  
10207 C CD  . LYS A 1331 ? 0.9774 2.2926 0.7969 0.1933  -0.0248 -0.0735 1331 LYS A CD  
10208 C CE  . LYS A 1331 ? 0.9863 2.3752 0.8089 0.1583  -0.0165 -0.0457 1331 LYS A CE  
10209 N NZ  . LYS A 1331 ? 0.9856 2.4586 0.8005 0.1852  -0.0094 -0.0221 1331 LYS A NZ  
10210 N N   . ASN A 1332 ? 1.0554 2.1124 0.8683 0.2604  -0.0590 -0.1655 1332 ASN A N   
10211 C CA  . ASN A 1332 ? 1.1010 2.0947 0.9143 0.2855  -0.0699 -0.1925 1332 ASN A CA  
10212 C C   . ASN A 1332 ? 1.1285 2.0679 0.9628 0.2654  -0.0741 -0.2144 1332 ASN A C   
10213 O O   . ASN A 1332 ? 1.1443 2.0685 0.9835 0.2289  -0.0722 -0.2122 1332 ASN A O   
10214 C CB  . ASN A 1332 ? 1.1509 2.1201 0.9482 0.2831  -0.0747 -0.1920 1332 ASN A CB  
10215 C CG  . ASN A 1332 ? 1.1686 2.0937 0.9726 0.2439  -0.0764 -0.1986 1332 ASN A CG  
10216 O OD1 . ASN A 1332 ? 1.1404 2.0864 0.9468 0.2067  -0.0693 -0.1835 1332 ASN A OD1 
10217 N ND2 . ASN A 1332 ? 1.1761 2.0402 0.9823 0.2528  -0.0861 -0.2216 1332 ASN A ND2 
10218 N N   . PHE A 1333 ? 1.1308 2.0381 0.9761 0.2879  -0.0800 -0.2359 1333 PHE A N   
10219 C CA  . PHE A 1333 ? 1.0949 1.9457 0.9590 0.2714  -0.0855 -0.2584 1333 PHE A CA  
10220 C C   . PHE A 1333 ? 1.1742 1.9803 1.0381 0.3027  -0.0973 -0.2821 1333 PHE A C   
10221 O O   . PHE A 1333 ? 1.2042 1.9636 1.0777 0.2947  -0.1042 -0.3002 1333 PHE A O   
10222 C CB  . PHE A 1333 ? 0.9713 1.8237 0.8559 0.2528  -0.0802 -0.2619 1333 PHE A CB  
10223 C CG  . PHE A 1333 ? 0.8738 1.7589 0.7583 0.2760  -0.0764 -0.2563 1333 PHE A CG  
10224 C CD1 . PHE A 1333 ? 0.8304 1.6830 0.7244 0.2962  -0.0815 -0.2756 1333 PHE A CD1 
10225 C CD2 . PHE A 1333 ? 0.8634 1.8117 0.7378 0.2766  -0.0675 -0.2313 1333 PHE A CD2 
10226 C CE1 . PHE A 1333 ? 0.8354 1.7128 0.7253 0.3185  -0.0778 -0.2700 1333 PHE A CE1 
10227 C CE2 . PHE A 1333 ? 0.7765 1.7537 0.6486 0.3009  -0.0638 -0.2261 1333 PHE A CE2 
10228 C CZ  . PHE A 1333 ? 0.7778 1.7170 0.6561 0.3222  -0.0689 -0.2455 1333 PHE A CZ  
10229 N N   . LEU A 1334 ? 1.1573 1.9794 1.0083 0.3393  -0.0998 -0.2816 1334 LEU A N   
10230 C CA  . LEU A 1334 ? 1.1076 1.8883 0.9554 0.3704  -0.1122 -0.3043 1334 LEU A CA  
10231 C C   . LEU A 1334 ? 1.2015 1.9776 1.0295 0.3843  -0.1179 -0.3023 1334 LEU A C   
10232 O O   . LEU A 1334 ? 1.2310 2.0058 1.0419 0.4193  -0.1242 -0.3071 1334 LEU A O   
10233 C CB  . LEU A 1334 ? 0.9897 1.7783 0.8294 0.4047  -0.1138 -0.3083 1334 LEU A CB  
10234 C CG  . LEU A 1334 ? 0.8985 1.7268 0.7387 0.4066  -0.1036 -0.2936 1334 LEU A CG  
10235 C CD1 . LEU A 1334 ? 0.8478 1.6480 0.7096 0.3940  -0.1037 -0.3074 1334 LEU A CD1 
10236 C CD2 . LEU A 1334 ? 0.8668 1.7541 0.7039 0.3833  -0.0911 -0.2650 1334 LEU A CD2 
10237 N N   . GLY A 1335 ? 1.2575 2.0286 1.0856 0.3568  -0.1156 -0.2951 1335 GLY A N   
10238 C CA  . GLY A 1335 ? 1.3575 2.1130 1.1683 0.3656  -0.1217 -0.2955 1335 GLY A CA  
10239 C C   . GLY A 1335 ? 1.4301 2.1421 1.2381 0.3947  -0.1363 -0.3200 1335 GLY A C   
10240 O O   . GLY A 1335 ? 1.4378 2.1257 1.2581 0.4097  -0.1437 -0.3402 1335 GLY A O   
10241 N N   . ARG A 1336 ? 1.5163 2.2193 1.3064 0.4019  -0.1406 -0.3170 1336 ARG A N   
10242 C CA  . ARG A 1336 ? 1.6174 2.2852 1.4003 0.4299  -0.1548 -0.3371 1336 ARG A CA  
10243 C C   . ARG A 1336 ? 1.5178 2.1387 1.3250 0.4165  -0.1630 -0.3610 1336 ARG A C   
10244 O O   . ARG A 1336 ? 1.5070 2.1215 1.3291 0.3841  -0.1565 -0.3576 1336 ARG A O   
10245 C CB  . ARG A 1336 ? 1.8098 2.4809 1.5685 0.4317  -0.1547 -0.3239 1336 ARG A CB  
10246 C CG  . ARG A 1336 ? 1.9531 2.6306 1.7132 0.3915  -0.1442 -0.3059 1336 ARG A CG  
10247 C CD  . ARG A 1336 ? 2.1045 2.7575 1.8459 0.3879  -0.1478 -0.3024 1336 ARG A CD  
10248 N NE  . ARG A 1336 ? 2.2102 2.8558 1.9524 0.3480  -0.1397 -0.2898 1336 ARG A NE  
10249 C CZ  . ARG A 1336 ? 2.3095 2.9436 2.0292 0.3366  -0.1380 -0.2766 1336 ARG A CZ  
10250 N NH1 . ARG A 1336 ? 2.3584 2.9906 2.0547 0.3627  -0.1433 -0.2736 1336 ARG A NH1 
10251 N NH2 . ARG A 1336 ? 2.3338 2.9562 2.0518 0.2992  -0.1311 -0.2663 1336 ARG A NH2 
10252 N N   . PRO A 1337 ? 1.4283 2.0181 1.2398 0.4407  -0.1772 -0.3852 1337 PRO A N   
10253 C CA  . PRO A 1337 ? 1.3313 1.8804 1.1624 0.4301  -0.1860 -0.4060 1337 PRO A CA  
10254 C C   . PRO A 1337 ? 1.2992 1.8361 1.1132 0.4308  -0.1890 -0.4013 1337 PRO A C   
10255 O O   . PRO A 1337 ? 1.2830 1.8435 1.0721 0.4345  -0.1828 -0.3806 1337 PRO A O   
10256 C CB  . PRO A 1337 ? 1.3522 1.8792 1.1902 0.4565  -0.2007 -0.4309 1337 PRO A CB  
10257 C CG  . PRO A 1337 ? 1.3927 1.9429 1.2231 0.4704  -0.1963 -0.4243 1337 PRO A CG  
10258 C CD  . PRO A 1337 ? 1.4188 2.0093 1.2242 0.4724  -0.1846 -0.3963 1337 PRO A CD  
10259 N N   . VAL A 1338 ? 1.3029 1.8053 1.1292 0.4272  -0.1977 -0.4187 1338 VAL A N   
10260 C CA  . VAL A 1338 ? 1.3804 1.8655 1.1892 0.4272  -0.2004 -0.4144 1338 VAL A CA  
10261 C C   . VAL A 1338 ? 1.4645 1.9148 1.2884 0.4371  -0.2144 -0.4399 1338 VAL A C   
10262 O O   . VAL A 1338 ? 1.4743 1.9102 1.3257 0.4207  -0.2145 -0.4529 1338 VAL A O   
10263 C CB  . VAL A 1338 ? 1.8873 2.3725 1.6917 0.3926  -0.1872 -0.3958 1338 VAL A CB  
10264 C CG1 . VAL A 1338 ? 1.8919 2.3383 1.6973 0.3852  -0.1921 -0.4058 1338 VAL A CG1 
10265 C CG2 . VAL A 1338 ? 1.9051 2.4182 1.6793 0.3898  -0.1779 -0.3679 1338 VAL A CG2 
10266 N N   . GLU A 1339 ? 1.5229 1.9624 1.3297 0.4643  -0.2263 -0.4472 1339 GLU A N   
10267 C CA  . GLU A 1339 ? 1.5867 1.9979 1.4078 0.4746  -0.2405 -0.4709 1339 GLU A CA  
10268 C C   . GLU A 1339 ? 1.5809 1.9717 1.3947 0.4609  -0.2370 -0.4649 1339 GLU A C   
10269 O O   . GLU A 1339 ? 1.5773 1.9678 1.3612 0.4627  -0.2325 -0.4473 1339 GLU A O   
10270 C CB  . GLU A 1339 ? 1.6842 2.0917 1.4901 0.5099  -0.2562 -0.4829 1339 GLU A CB  
10271 C CG  . GLU A 1339 ? 1.7491 2.1578 1.5733 0.5221  -0.2664 -0.5029 1339 GLU A CG  
10272 C CD  . GLU A 1339 ? 1.8295 2.2390 1.6306 0.5570  -0.2797 -0.5106 1339 GLU A CD  
10273 O OE1 . GLU A 1339 ? 1.8653 2.2598 1.6592 0.5738  -0.2927 -0.5218 1339 GLU A OE1 
10274 O OE2 . GLU A 1339 ? 1.8435 2.2684 1.6326 0.5687  -0.2774 -0.5056 1339 GLU A OE2 
10275 N N   . VAL A 1340 ? 1.6014 1.9747 1.4413 0.4463  -0.2381 -0.4788 1340 VAL A N   
10276 C CA  . VAL A 1340 ? 1.6470 1.9971 1.4791 0.4325  -0.2336 -0.4738 1340 VAL A CA  
10277 C C   . VAL A 1340 ? 1.6922 2.0238 1.5137 0.4593  -0.2478 -0.4859 1340 VAL A C   
10278 O O   . VAL A 1340 ? 1.7170 2.0444 1.5614 0.4728  -0.2604 -0.5085 1340 VAL A O   
10279 C CB  . VAL A 1340 ? 1.6538 1.9934 1.5171 0.4103  -0.2293 -0.4849 1340 VAL A CB  
10280 C CG1 . VAL A 1340 ? 1.6852 1.9946 1.5390 0.4055  -0.2289 -0.4860 1340 VAL A CG1 
10281 C CG2 . VAL A 1340 ? 1.6334 1.9899 1.5034 0.3816  -0.2141 -0.4706 1340 VAL A CG2 
10282 N N   . LEU A 1341 ? 1.7178 2.0399 1.5039 0.4672  -0.2464 -0.4706 1341 LEU A N   
10283 C CA  . LEU A 1341 ? 1.7557 2.0627 1.5273 0.4967  -0.2606 -0.4807 1341 LEU A CA  
10284 C C   . LEU A 1341 ? 1.8202 2.0977 1.5988 0.4946  -0.2640 -0.4914 1341 LEU A C   
10285 O O   . LEU A 1341 ? 1.8131 2.0869 1.6136 0.5099  -0.2769 -0.5137 1341 LEU A O   
10286 C CB  . LEU A 1341 ? 1.7682 2.0759 1.4968 0.5093  -0.2583 -0.4599 1341 LEU A CB  
10287 C CG  . LEU A 1341 ? 2.0036 2.3334 1.7144 0.5367  -0.2651 -0.4573 1341 LEU A CG  
10288 C CD1 . LEU A 1341 ? 1.9889 2.3215 1.7191 0.5632  -0.2834 -0.4846 1341 LEU A CD1 
10289 C CD2 . LEU A 1341 ? 1.9853 2.3472 1.6898 0.5252  -0.2525 -0.4382 1341 LEU A CD2 
10290 N N   . LEU A 1342 ? 1.8528 2.1100 1.6121 0.4751  -0.2524 -0.4755 1342 LEU A N   
10291 C CA  . LEU A 1342 ? 1.8827 2.1062 1.6319 0.4815  -0.2561 -0.4812 1342 LEU A CA  
10292 C C   . LEU A 1342 ? 1.8496 2.0687 1.6363 0.4793  -0.2607 -0.5039 1342 LEU A C   
10293 O O   . LEU A 1342 ? 1.8036 2.0424 1.6241 0.4657  -0.2583 -0.5128 1342 LEU A O   
10294 C CB  . LEU A 1342 ? 1.8873 2.0845 1.6006 0.4611  -0.2430 -0.4579 1342 LEU A CB  
10295 C CG  . LEU A 1342 ? 1.8447 2.0618 1.5324 0.4533  -0.2350 -0.4336 1342 LEU A CG  
10296 C CD1 . LEU A 1342 ? 1.8637 2.0567 1.5143 0.4297  -0.2226 -0.4088 1342 LEU A CD1 
10297 C CD2 . LEU A 1342 ? 1.8469 2.0784 1.5187 0.4857  -0.2457 -0.4339 1342 LEU A CD2 
10298 N N   . ASN A 1343 ? 1.9037 2.0984 1.6833 0.4953  -0.2677 -0.5129 1343 ASN A N   
10299 C CA  . ASN A 1343 ? 1.9522 2.1441 1.7645 0.4970  -0.2723 -0.5336 1343 ASN A CA  
10300 C C   . ASN A 1343 ? 1.9483 2.1149 1.7559 0.4727  -0.2584 -0.5269 1343 ASN A C   
10301 O O   . ASN A 1343 ? 1.9678 2.1024 1.7541 0.4808  -0.2583 -0.5264 1343 ASN A O   
10302 C CB  . ASN A 1343 ? 2.0636 2.2472 1.8722 0.5305  -0.2880 -0.5481 1343 ASN A CB  
10303 C CG  . ASN A 1343 ? 2.1604 2.3724 1.9844 0.5535  -0.3046 -0.5621 1343 ASN A CG  
10304 O OD1 . ASN A 1343 ? 2.1909 2.4147 2.0412 0.5697  -0.3180 -0.5830 1343 ASN A OD1 
10305 N ND2 . ASN A 1343 ? 2.1931 2.4172 2.0005 0.5545  -0.3037 -0.5508 1343 ASN A ND2 
10306 N N   . ASP A 1344 ? 1.9213 2.1009 1.7466 0.4440  -0.2470 -0.5222 1344 ASP A N   
10307 C CA  . ASP A 1344 ? 1.8814 2.0380 1.6987 0.4176  -0.2330 -0.5140 1344 ASP A CA  
10308 C C   . ASP A 1344 ? 1.8378 2.0198 1.6921 0.3940  -0.2256 -0.5191 1344 ASP A C   
10309 O O   . ASP A 1344 ? 1.8311 2.0447 1.7077 0.3947  -0.2289 -0.5227 1344 ASP A O   
10310 C CB  . ASP A 1344 ? 1.8374 1.9742 1.6107 0.4008  -0.2229 -0.4883 1344 ASP A CB  
10311 C CG  . ASP A 1344 ? 1.7740 1.8668 1.5197 0.3864  -0.2143 -0.4814 1344 ASP A CG  
10312 O OD1 . ASP A 1344 ? 1.7469 1.8297 1.5113 0.3846  -0.2130 -0.4954 1344 ASP A OD1 
10313 O OD2 . ASP A 1344 ? 1.7556 1.8231 1.4594 0.3768  -0.2089 -0.4618 1344 ASP A OD2 
10314 N N   . ASP A 1345 ? 1.7946 1.9609 1.6535 0.3743  -0.2157 -0.5197 1345 ASP A N   
10315 C CA  . ASP A 1345 ? 1.7380 1.9265 1.6267 0.3499  -0.2070 -0.5214 1345 ASP A CA  
10316 C C   . ASP A 1345 ? 1.3626 1.5610 1.2318 0.3274  -0.1974 -0.4993 1345 ASP A C   
10317 O O   . ASP A 1345 ? 1.3961 1.5718 1.2276 0.3173  -0.1915 -0.4820 1345 ASP A O   
10318 C CB  . ASP A 1345 ? 1.7463 1.9150 1.6423 0.3360  -0.1987 -0.5278 1345 ASP A CB  
10319 C CG  . ASP A 1345 ? 1.8100 1.9642 1.7135 0.3611  -0.2071 -0.5454 1345 ASP A CG  
10320 O OD1 . ASP A 1345 ? 1.8184 1.9716 1.7429 0.3556  -0.2026 -0.5564 1345 ASP A OD1 
10321 O OD2 . ASP A 1345 ? 1.8421 1.9875 1.7299 0.3870  -0.2178 -0.5479 1345 ASP A OD2 
10322 N N   . LEU A 1346 ? 1.3103 1.5430 1.2038 0.3200  -0.1959 -0.4992 1346 LEU A N   
10323 C CA  . LEU A 1346 ? 1.2692 1.5191 1.1486 0.3000  -0.1865 -0.4787 1346 LEU A CA  
10324 C C   . LEU A 1346 ? 1.2850 1.5353 1.1710 0.2673  -0.1730 -0.4721 1346 LEU A C   
10325 O O   . LEU A 1346 ? 1.3156 1.5615 1.2264 0.2622  -0.1713 -0.4862 1346 LEU A O   
10326 C CB  . LEU A 1346 ? 1.1801 1.4655 1.0786 0.3109  -0.1913 -0.4813 1346 LEU A CB  
10327 C CG  . LEU A 1346 ? 1.1499 1.4559 1.0285 0.2973  -0.1828 -0.4586 1346 LEU A CG  
10328 C CD1 . LEU A 1346 ? 1.1762 1.4669 1.0148 0.3030  -0.1834 -0.4430 1346 LEU A CD1 
10329 C CD2 . LEU A 1346 ? 1.1278 1.4662 1.0216 0.3112  -0.1873 -0.4613 1346 LEU A CD2 
10330 N N   . ILE A 1347 ? 1.2443 1.5026 1.1085 0.2453  -0.1636 -0.4508 1347 ILE A N   
10331 C CA  . ILE A 1347 ? 1.1521 1.4158 1.0215 0.2133  -0.1514 -0.4434 1347 ILE A CA  
10332 C C   . ILE A 1347 ? 1.0639 1.3606 0.9260 0.1941  -0.1434 -0.4228 1347 ILE A C   
10333 O O   . ILE A 1347 ? 1.0703 1.3610 0.9010 0.1781  -0.1384 -0.4039 1347 ILE A O   
10334 C CB  . ILE A 1347 ? 1.1733 1.3977 1.0147 0.1933  -0.1450 -0.4374 1347 ILE A CB  
10335 C CG1 . ILE A 1347 ? 1.2124 1.3969 1.0397 0.2138  -0.1524 -0.4489 1347 ILE A CG1 
10336 C CG2 . ILE A 1347 ? 1.1554 1.3805 1.0148 0.1698  -0.1362 -0.4425 1347 ILE A CG2 
10337 C CD1 . ILE A 1347 ? 1.2754 1.4150 1.0697 0.1945  -0.1458 -0.4428 1347 ILE A CD1 
10338 N N   . VAL A 1348 ? 0.9963 1.3270 0.8865 0.1946  -0.1419 -0.4262 1348 VAL A N   
10339 C CA  . VAL A 1348 ? 0.9767 1.3418 0.8655 0.1749  -0.1329 -0.4085 1348 VAL A CA  
10340 C C   . VAL A 1348 ? 1.1074 1.4617 0.9897 0.1406  -0.1225 -0.4014 1348 VAL A C   
10341 O O   . VAL A 1348 ? 1.1425 1.4732 1.0374 0.1360  -0.1217 -0.4159 1348 VAL A O   
10342 C CB  . VAL A 1348 ? 0.8831 1.2783 0.8042 0.1862  -0.1344 -0.4177 1348 VAL A CB  
10343 C CG1 . VAL A 1348 ? 0.8821 1.3178 0.7994 0.1761  -0.1270 -0.3990 1348 VAL A CG1 
10344 C CG2 . VAL A 1348 ? 0.8748 1.2685 0.8037 0.2193  -0.1466 -0.4312 1348 VAL A CG2 
10345 N N   . SER A 1349 ? 1.0825 1.4548 0.9454 0.1165  -0.1147 -0.3800 1349 SER A N   
10346 C CA  . SER A 1349 ? 1.1015 1.4577 0.9528 0.0830  -0.1065 -0.3740 1349 SER A CA  
10347 C C   . SER A 1349 ? 1.1565 1.5419 0.9907 0.0531  -0.0984 -0.3499 1349 SER A C   
10348 O O   . SER A 1349 ? 1.1724 1.5382 0.9751 0.0314  -0.0960 -0.3369 1349 SER A O   
10349 C CB  . SER A 1349 ? 1.1038 1.4063 0.9296 0.0800  -0.1089 -0.3793 1349 SER A CB  
10350 O OG  . SER A 1349 ? 1.1177 1.4093 0.9165 0.0918  -0.1139 -0.3698 1349 SER A OG  
10351 N N   . THR A 1350 ? 1.1618 1.5933 1.0165 0.0516  -0.0944 -0.3444 1350 THR A N   
10352 C CA  . THR A 1350 ? 1.1756 1.6449 1.0215 0.0241  -0.0866 -0.3229 1350 THR A CA  
10353 C C   . THR A 1350 ? 1.1696 1.6182 0.9956 -0.0143 -0.0810 -0.3156 1350 THR A C   
10354 O O   . THR A 1350 ? 1.1503 1.5637 0.9805 -0.0224 -0.0801 -0.3302 1350 THR A O   
10355 C CB  . THR A 1350 ? 1.2698 1.7822 1.1446 0.0276  -0.0825 -0.3237 1350 THR A CB  
10356 O OG1 . THR A 1350 ? 1.2947 1.8536 1.1602 0.0081  -0.0762 -0.3007 1350 THR A OG1 
10357 C CG2 . THR A 1350 ? 1.2481 1.7419 1.1405 0.0141  -0.0788 -0.3380 1350 THR A CG2 
10358 N N   . GLY A 1351 ? 1.1639 1.6385 0.9687 -0.0382 -0.0771 -0.2926 1351 GLY A N   
10359 C CA  . GLY A 1351 ? 1.1611 1.6228 0.9443 -0.0783 -0.0725 -0.2826 1351 GLY A CA  
10360 C C   . GLY A 1351 ? 1.0988 1.5807 0.9020 -0.0943 -0.0670 -0.2867 1351 GLY A C   
10361 O O   . GLY A 1351 ? 1.0607 1.5442 0.8923 -0.0746 -0.0672 -0.3031 1351 GLY A O   
10362 N N   . PHE A 1352 ? 1.1147 1.6113 0.9025 -0.1310 -0.0625 -0.2720 1352 PHE A N   
10363 C CA  . PHE A 1352 ? 1.0726 1.5978 0.8796 -0.1449 -0.0573 -0.2734 1352 PHE A CA  
10364 C C   . PHE A 1352 ? 1.0246 1.6147 0.8580 -0.1248 -0.0552 -0.2652 1352 PHE A C   
10365 O O   . PHE A 1352 ? 1.0239 1.6135 0.8813 -0.0934 -0.0570 -0.2793 1352 PHE A O   
10366 C CB  . PHE A 1352 ? 1.0630 1.5876 0.8470 -0.1898 -0.0539 -0.2614 1352 PHE A CB  
10367 C CG  . PHE A 1352 ? 1.0094 1.5727 0.8130 -0.2024 -0.0487 -0.2603 1352 PHE A CG  
10368 C CD1 . PHE A 1352 ? 0.9648 1.5200 0.7954 -0.1833 -0.0469 -0.2789 1352 PHE A CD1 
10369 C CD2 . PHE A 1352 ? 1.0011 1.6115 0.7966 -0.2326 -0.0458 -0.2400 1352 PHE A CD2 
10370 C CE1 . PHE A 1352 ? 0.9133 1.5031 0.7608 -0.1928 -0.0418 -0.2773 1352 PHE A CE1 
10371 C CE2 . PHE A 1352 ? 0.9499 1.5975 0.7629 -0.2416 -0.0413 -0.2388 1352 PHE A CE2 
10372 C CZ  . PHE A 1352 ? 0.9143 1.5500 0.7524 -0.2209 -0.0392 -0.2574 1352 PHE A CZ  
10373 N N   . GLY A 1353 ? 1.0029 1.6481 0.8310 -0.1416 -0.0518 -0.2429 1353 GLY A N   
10374 C CA  . GLY A 1353 ? 0.9685 1.6743 0.8168 -0.1188 -0.0497 -0.2340 1353 GLY A CA  
10375 C C   . GLY A 1353 ? 0.9456 1.6706 0.8224 -0.1058 -0.0465 -0.2439 1353 GLY A C   
10376 O O   . GLY A 1353 ? 0.9311 1.6431 0.8120 -0.1256 -0.0436 -0.2504 1353 GLY A O   
10377 N N   . SER A 1354 ? 0.9202 1.6734 0.8140 -0.0720 -0.0471 -0.2450 1354 SER A N   
10378 C CA  . SER A 1354 ? 0.8825 1.6646 0.7989 -0.0598 -0.0433 -0.2479 1354 SER A CA  
10379 C C   . SER A 1354 ? 0.8407 1.6358 0.7704 -0.0183 -0.0459 -0.2531 1354 SER A C   
10380 O O   . SER A 1354 ? 0.8428 1.6505 0.7625 -0.0003 -0.0491 -0.2459 1354 SER A O   
10381 C CB  . SER A 1354 ? 0.8989 1.7426 0.8109 -0.0807 -0.0375 -0.2253 1354 SER A CB  
10382 O OG  . SER A 1354 ? 0.8883 1.7848 0.8006 -0.0575 -0.0367 -0.2100 1354 SER A OG  
10383 N N   . GLY A 1355 ? 0.8004 1.5931 0.7503 -0.0039 -0.0444 -0.2645 1355 GLY A N   
10384 C CA  . GLY A 1355 ? 0.7828 1.5801 0.7435 0.0342  -0.0475 -0.2716 1355 GLY A CA  
10385 C C   . GLY A 1355 ? 0.8047 1.5475 0.7796 0.0506  -0.0535 -0.2971 1355 GLY A C   
10386 O O   . GLY A 1355 ? 0.8480 1.5541 0.8283 0.0334  -0.0536 -0.3096 1355 GLY A O   
10387 N N   . LEU A 1356 ? 0.8131 1.5510 0.7929 0.0839  -0.0589 -0.3051 1356 LEU A N   
10388 C CA  . LEU A 1356 ? 0.8385 1.5298 0.8330 0.0991  -0.0657 -0.3290 1356 LEU A CA  
10389 C C   . LEU A 1356 ? 0.9507 1.6304 0.9380 0.1296  -0.0750 -0.3354 1356 LEU A C   
10390 O O   . LEU A 1356 ? 1.0071 1.7059 0.9910 0.1551  -0.0769 -0.3321 1356 LEU A O   
10391 C CB  . LEU A 1356 ? 0.8068 1.4969 0.8202 0.1073  -0.0634 -0.3373 1356 LEU A CB  
10392 C CG  . LEU A 1356 ? 0.7555 1.4282 0.7838 0.0827  -0.0580 -0.3452 1356 LEU A CG  
10393 C CD1 . LEU A 1356 ? 0.7096 1.3953 0.7503 0.0874  -0.0530 -0.3446 1356 LEU A CD1 
10394 C CD2 . LEU A 1356 ? 0.7463 1.3736 0.7869 0.0871  -0.0645 -0.3668 1356 LEU A CD2 
10395 N N   . ALA A 1357 ? 0.9140 1.5615 0.8968 0.1286  -0.0809 -0.3448 1357 ALA A N   
10396 C CA  . ALA A 1357 ? 0.8443 1.4803 0.8188 0.1574  -0.0904 -0.3513 1357 ALA A CA  
10397 C C   . ALA A 1357 ? 0.8085 1.4022 0.8005 0.1712  -0.0994 -0.3768 1357 ALA A C   
10398 O O   . ALA A 1357 ? 0.7879 1.3534 0.7881 0.1564  -0.0998 -0.3873 1357 ALA A O   
10399 C CB  . ALA A 1357 ? 0.8158 1.4533 0.7671 0.1505  -0.0913 -0.3395 1357 ALA A CB  
10400 N N   . THR A 1358 ? 0.7620 1.3523 0.7588 0.1994  -0.1066 -0.3867 1358 THR A N   
10401 C CA  . THR A 1358 ? 0.7514 1.3062 0.7650 0.2119  -0.1165 -0.4104 1358 THR A CA  
10402 C C   . THR A 1358 ? 0.7882 1.3238 0.7909 0.2285  -0.1270 -0.4183 1358 THR A C   
10403 O O   . THR A 1358 ? 0.7927 1.3365 0.7800 0.2527  -0.1330 -0.4156 1358 THR A O   
10404 C CB  . THR A 1358 ? 1.0047 1.5569 1.0297 0.2313  -0.1208 -0.4206 1358 THR A CB  
10405 O OG1 . THR A 1358 ? 1.0061 1.5812 1.0109 0.2542  -0.1218 -0.4094 1358 THR A OG1 
10406 C CG2 . THR A 1358 ? 0.9806 1.5362 1.0237 0.2130  -0.1122 -0.4205 1358 THR A CG2 
10407 N N   . VAL A 1359 ? 0.7716 1.2812 0.7811 0.2173  -0.1292 -0.4281 1359 VAL A N   
10408 C CA  . VAL A 1359 ? 0.8436 1.3298 0.8483 0.2348  -0.1405 -0.4404 1359 VAL A CA  
10409 C C   . VAL A 1359 ? 0.9083 1.3758 0.9356 0.2517  -0.1517 -0.4640 1359 VAL A C   
10410 O O   . VAL A 1359 ? 0.8753 1.3304 0.9268 0.2397  -0.1506 -0.4763 1359 VAL A O   
10411 C CB  . VAL A 1359 ? 0.7958 1.2596 0.7968 0.2179  -0.1385 -0.4420 1359 VAL A CB  
10412 C CG1 . VAL A 1359 ? 0.8135 1.2545 0.8084 0.2387  -0.1506 -0.4542 1359 VAL A CG1 
10413 C CG2 . VAL A 1359 ? 0.8040 1.2801 0.7811 0.1976  -0.1289 -0.4201 1359 VAL A CG2 
10414 N N   . HIS A 1360 ? 0.9106 1.3769 0.9295 0.2787  -0.1625 -0.4701 1360 HIS A N   
10415 C CA  . HIS A 1360 ? 0.9516 1.3968 0.9872 0.2944  -0.1763 -0.4933 1360 HIS A CA  
10416 C C   . HIS A 1360 ? 0.9768 1.4105 0.9972 0.3130  -0.1869 -0.4983 1360 HIS A C   
10417 O O   . HIS A 1360 ? 1.0224 1.4661 1.0157 0.3223  -0.1857 -0.4842 1360 HIS A O   
10418 C CB  . HIS A 1360 ? 0.9977 1.4447 1.0350 0.3123  -0.1830 -0.5004 1360 HIS A CB  
10419 C CG  . HIS A 1360 ? 0.9962 1.4492 1.0489 0.2980  -0.1747 -0.4983 1360 HIS A CG  
10420 N ND1 . HIS A 1360 ? 0.9795 1.4557 1.0215 0.2880  -0.1617 -0.4786 1360 HIS A ND1 
10421 C CD2 . HIS A 1360 ? 0.9927 1.4328 1.0700 0.2922  -0.1776 -0.5128 1360 HIS A CD2 
10422 C CE1 . HIS A 1360 ? 0.9753 1.4509 1.0334 0.2781  -0.1568 -0.4812 1360 HIS A CE1 
10423 N NE2 . HIS A 1360 ? 0.9891 1.4417 1.0684 0.2797  -0.1659 -0.5015 1360 HIS A NE2 
10424 N N   . VAL A 1361 ? 0.9317 1.3469 0.9696 0.3197  -0.1978 -0.5183 1361 VAL A N   
10425 C CA  . VAL A 1361 ? 0.9529 1.3563 0.9774 0.3376  -0.2084 -0.5241 1361 VAL A CA  
10426 C C   . VAL A 1361 ? 0.9741 1.3661 1.0170 0.3538  -0.2246 -0.5476 1361 VAL A C   
10427 O O   . VAL A 1361 ? 0.9671 1.3504 1.0343 0.3470  -0.2282 -0.5618 1361 VAL A O   
10428 C CB  . VAL A 1361 ? 0.9282 1.3204 0.9485 0.3235  -0.2023 -0.5191 1361 VAL A CB  
10429 C CG1 . VAL A 1361 ? 0.8553 1.2304 0.8877 0.3349  -0.2138 -0.5375 1361 VAL A CG1 
10430 C CG2 . VAL A 1361 ? 0.8619 1.2580 0.8473 0.3250  -0.1969 -0.4987 1361 VAL A CG2 
10431 N N   . THR A 1362 ? 1.0035 1.3972 1.0335 0.3757  -0.2345 -0.5515 1362 THR A N   
10432 C CA  . THR A 1362 ? 1.0004 1.3842 1.0467 0.3882  -0.2502 -0.5735 1362 THR A CA  
10433 C C   . THR A 1362 ? 0.9817 1.3570 1.0188 0.4101  -0.2655 -0.5847 1362 THR A C   
10434 O O   . THR A 1362 ? 0.9603 1.3369 0.9680 0.4304  -0.2698 -0.5781 1362 THR A O   
10435 C CB  . THR A 1362 ? 1.0343 1.4200 1.0718 0.3972  -0.2521 -0.5730 1362 THR A CB  
10436 O OG1 . THR A 1362 ? 1.0571 1.4291 1.1119 0.4033  -0.2670 -0.5950 1362 THR A OG1 
10437 C CG2 . THR A 1362 ? 1.0571 1.4501 1.0578 0.4203  -0.2533 -0.5610 1362 THR A CG2 
10438 N N   . THR A 1363 ? 1.0040 1.3733 1.0665 0.4056  -0.2727 -0.6006 1363 THR A N   
10439 C CA  . THR A 1363 ? 1.0943 1.4575 1.1510 0.4230  -0.2847 -0.6095 1363 THR A CA  
10440 C C   . THR A 1363 ? 1.1842 1.5442 1.2552 0.4386  -0.3053 -0.6329 1363 THR A C   
10441 O O   . THR A 1363 ? 1.1891 1.5514 1.2934 0.4268  -0.3100 -0.6478 1363 THR A O   
10442 C CB  . THR A 1363 ? 1.8110 2.1710 1.8812 0.4103  -0.2779 -0.6090 1363 THR A CB  
10443 O OG1 . THR A 1363 ? 1.7999 2.1614 1.9012 0.4120  -0.2894 -0.6298 1363 THR A OG1 
10444 C CG2 . THR A 1363 ? 1.7927 2.1558 1.8716 0.3829  -0.2591 -0.5961 1363 THR A CG2 
10445 N N   . VAL A 1364 ? 1.2277 1.5839 1.2726 0.4644  -0.3177 -0.6355 1364 VAL A N   
10446 C CA  . VAL A 1364 ? 1.2172 1.5695 1.2683 0.4811  -0.3389 -0.6570 1364 VAL A CA  
10447 C C   . VAL A 1364 ? 1.2668 1.6203 1.3231 0.4945  -0.3514 -0.6682 1364 VAL A C   
10448 O O   . VAL A 1364 ? 1.3004 1.6518 1.3351 0.5053  -0.3477 -0.6576 1364 VAL A O   
10449 C CB  . VAL A 1364 ? 1.1934 1.5405 1.2092 0.5047  -0.3461 -0.6541 1364 VAL A CB  
10450 C CG1 . VAL A 1364 ? 1.2288 1.5708 1.2403 0.5275  -0.3690 -0.6738 1364 VAL A CG1 
10451 C CG2 . VAL A 1364 ? 1.1728 1.5163 1.1879 0.4973  -0.3417 -0.6524 1364 VAL A CG2 
10452 N N   . VAL A 1365 ? 1.2699 1.6271 1.3538 0.4942  -0.3668 -0.6896 1365 VAL A N   
10453 C CA  . VAL A 1365 ? 1.2979 1.6604 1.3869 0.5093  -0.3796 -0.7005 1365 VAL A CA  
10454 C C   . VAL A 1365 ? 1.3969 1.7633 1.5018 0.5171  -0.4026 -0.7244 1365 VAL A C   
10455 O O   . VAL A 1365 ? 1.4297 1.7938 1.5506 0.5031  -0.4058 -0.7328 1365 VAL A O   
10456 C CB  . VAL A 1365 ? 1.2138 1.5840 1.3276 0.4943  -0.3688 -0.6979 1365 VAL A CB  
10457 C CG1 . VAL A 1365 ? 1.1803 1.5651 1.3405 0.4769  -0.3744 -0.7153 1365 VAL A CG1 
10458 C CG2 . VAL A 1365 ? 1.2133 1.5815 1.3098 0.5151  -0.3733 -0.6960 1365 VAL A CG2 
10459 N N   . HIS A 1366 ? 1.4343 1.8048 1.5313 0.5398  -0.4192 -0.7348 1366 HIS A N   
10460 C CA  . HIS A 1366 ? 1.4380 1.8149 1.5507 0.5463  -0.4429 -0.7584 1366 HIS A CA  
10461 C C   . HIS A 1366 ? 1.3790 1.7775 1.5288 0.5409  -0.4493 -0.7705 1366 HIS A C   
10462 O O   . HIS A 1366 ? 1.3768 1.7811 1.5205 0.5541  -0.4466 -0.7651 1366 HIS A O   
10463 C CB  . HIS A 1366 ? 1.5001 1.8699 1.5771 0.5777  -0.4594 -0.7633 1366 HIS A CB  
10464 C CG  . HIS A 1366 ? 1.5444 1.8962 1.5817 0.5884  -0.4546 -0.7521 1366 HIS A CG  
10465 N ND1 . HIS A 1366 ? 1.5485 1.8947 1.5697 0.5806  -0.4323 -0.7294 1366 HIS A ND1 
10466 C CD2 . HIS A 1366 ? 1.5956 1.9358 1.6050 0.6077  -0.4691 -0.7603 1366 HIS A CD2 
10467 C CE1 . HIS A 1366 ? 1.5802 1.9152 1.5669 0.5951  -0.4328 -0.7235 1366 HIS A CE1 
10468 N NE2 . HIS A 1366 ? 1.6112 1.9407 1.5888 0.6127  -0.4547 -0.7421 1366 HIS A NE2 
10469 N N   . LYS A 1367 ? 1.3644 1.7753 1.5517 0.5221  -0.4576 -0.7862 1367 LYS A N   
10470 C CA  . LYS A 1367 ? 1.3837 1.8222 1.6081 0.5192  -0.4662 -0.7991 1367 LYS A CA  
10471 C C   . LYS A 1367 ? 1.3857 1.8370 1.6203 0.5288  -0.4939 -0.8218 1367 LYS A C   
10472 O O   . LYS A 1367 ? 1.4100 1.8448 1.6260 0.5328  -0.5064 -0.8293 1367 LYS A O   
10473 C CB  . LYS A 1367 ? 1.4062 1.8592 1.6723 0.4888  -0.4524 -0.7981 1367 LYS A CB  
10474 C CG  . LYS A 1367 ? 1.4299 1.8716 1.7067 0.4632  -0.4474 -0.7984 1367 LYS A CG  
10475 C CD  . LYS A 1367 ? 1.4204 1.8751 1.7310 0.4365  -0.4286 -0.7918 1367 LYS A CD  
10476 C CE  . LYS A 1367 ? 1.4165 1.8661 1.7107 0.4419  -0.4079 -0.7729 1367 LYS A CE  
10477 N NZ  . LYS A 1367 ? 1.3970 1.8669 1.7262 0.4251  -0.3954 -0.7719 1367 LYS A NZ  
10478 N N   . THR A 1368 ? 1.2974 1.6551 1.7474 0.4531  -0.3518 -0.7689 1368 THR A N   
10479 C CA  . THR A 1368 ? 1.2505 1.6312 1.7326 0.4542  -0.3701 -0.7656 1368 THR A CA  
10480 C C   . THR A 1368 ? 1.2200 1.6519 1.7462 0.4451  -0.3602 -0.7664 1368 THR A C   
10481 O O   . THR A 1368 ? 1.2305 1.6862 1.7868 0.4428  -0.3746 -0.7637 1368 THR A O   
10482 C CB  . THR A 1368 ? 1.2677 1.6469 1.7674 0.4779  -0.3856 -0.7694 1368 THR A CB  
10483 O OG1 . THR A 1368 ? 1.2673 1.6850 1.8086 0.4908  -0.3732 -0.7768 1368 THR A OG1 
10484 C CG2 . THR A 1368 ? 1.2758 1.6054 1.7333 0.4891  -0.3890 -0.7705 1368 THR A CG2 
10485 N N   . SER A 1369 ? 1.1932 1.6414 1.7223 0.4389  -0.3359 -0.7699 1369 SER A N   
10486 C CA  . SER A 1369 ? 1.1777 1.6760 1.7517 0.4336  -0.3234 -0.7718 1369 SER A CA  
10487 C C   . SER A 1369 ? 1.1768 1.6863 1.7426 0.4180  -0.2988 -0.7717 1369 SER A C   
10488 O O   . SER A 1369 ? 1.1493 1.6332 1.6791 0.4157  -0.2864 -0.7730 1369 SER A O   
10489 C CB  . SER A 1369 ? 1.1958 1.7217 1.8082 0.4552  -0.3187 -0.7797 1369 SER A CB  
10490 O OG  . SER A 1369 ? 1.2339 1.7501 1.8545 0.4716  -0.3416 -0.7796 1369 SER A OG  
10491 N N   . THR A 1370 ? 1.2162 1.7652 1.8171 0.4072  -0.2922 -0.7700 1370 THR A N   
10492 C CA  . THR A 1370 ? 1.2697 1.8336 1.8676 0.3933  -0.2684 -0.7696 1370 THR A CA  
10493 C C   . THR A 1370 ? 1.3929 1.9986 2.0330 0.4030  -0.2509 -0.7764 1370 THR A C   
10494 O O   . THR A 1370 ? 1.4124 2.0274 2.0474 0.3981  -0.2278 -0.7786 1370 THR A O   
10495 C CB  . THR A 1370 ? 1.1987 1.7712 1.7984 0.3708  -0.2717 -0.7614 1370 THR A CB  
10496 O OG1 . THR A 1370 ? 1.1640 1.6943 1.7176 0.3622  -0.2821 -0.7551 1370 THR A OG1 
10497 C CG2 . THR A 1370 ? 1.1800 1.7754 1.7856 0.3575  -0.2465 -0.7608 1370 THR A CG2 
10498 N N   . SER A 1371 ? 1.4870 2.1175 2.1679 0.4178  -0.2616 -0.7794 1371 SER A N   
10499 C CA  . SER A 1371 ? 1.5885 2.2641 2.3163 0.4273  -0.2453 -0.7847 1371 SER A CA  
10500 C C   . SER A 1371 ? 1.6568 2.3298 2.3671 0.4295  -0.2165 -0.7902 1371 SER A C   
10501 O O   . SER A 1371 ? 1.6733 2.3800 2.4084 0.4234  -0.1964 -0.7910 1371 SER A O   
10502 C CB  . SER A 1371 ? 1.6431 2.3297 2.4008 0.4519  -0.2581 -0.7893 1371 SER A CB  
10503 O OG  . SER A 1371 ? 1.6875 2.3374 2.4120 0.4695  -0.2564 -0.7949 1371 SER A OG  
10504 N N   . GLU A 1372 ? 1.7114 2.3430 2.3776 0.4378  -0.2150 -0.7939 1372 GLU A N   
10505 C CA  . GLU A 1372 ? 1.7581 2.3788 2.3983 0.4392  -0.1907 -0.7994 1372 GLU A CA  
10506 C C   . GLU A 1372 ? 1.6341 2.2632 2.2619 0.4169  -0.1743 -0.7946 1372 GLU A C   
10507 O O   . GLU A 1372 ? 1.6260 2.2859 2.2759 0.4152  -0.1533 -0.7969 1372 GLU A O   
10508 C CB  . GLU A 1372 ? 1.9240 2.4930 2.5130 0.4460  -0.1968 -0.8022 1372 GLU A CB  
10509 C CG  . GLU A 1372 ? 2.0552 2.5912 2.6131 0.4339  -0.2183 -0.7943 1372 GLU A CG  
10510 C CD  . GLU A 1372 ? 2.1724 2.6594 2.6765 0.4341  -0.2197 -0.7955 1372 GLU A CD  
10511 O OE1 . GLU A 1372 ? 2.2327 2.7056 2.7233 0.4474  -0.2097 -0.8036 1372 GLU A OE1 
10512 O OE2 . GLU A 1372 ? 2.1914 2.6536 2.6668 0.4208  -0.2309 -0.7881 1372 GLU A OE2 
10513 N N   . GLU A 1373 ? 1.5178 2.1195 2.1109 0.4006  -0.1840 -0.7875 1373 GLU A N   
10514 C CA  . GLU A 1373 ? 1.3946 1.9933 1.9639 0.3805  -0.1702 -0.7822 1373 GLU A CA  
10515 C C   . GLU A 1373 ? 1.3207 1.9609 1.9230 0.3695  -0.1528 -0.7801 1373 GLU A C   
10516 O O   . GLU A 1373 ? 1.3121 1.9883 1.9615 0.3743  -0.1534 -0.7814 1373 GLU A O   
10517 C CB  . GLU A 1373 ? 1.3140 1.8848 1.8542 0.3657  -0.1875 -0.7731 1373 GLU A CB  
10518 C CG  . GLU A 1373 ? 1.2550 1.7833 1.7603 0.3743  -0.2037 -0.7738 1373 GLU A CG  
10519 C CD  . GLU A 1373 ? 1.1734 1.6766 1.6545 0.3617  -0.2211 -0.7644 1373 GLU A CD  
10520 O OE1 . GLU A 1373 ? 1.1233 1.6422 1.6174 0.3474  -0.2230 -0.7578 1373 GLU A OE1 
10521 O OE2 . GLU A 1373 ? 1.1468 1.6134 1.5952 0.3662  -0.2321 -0.7636 1373 GLU A OE2 
10522 N N   . VAL A 1374 ? 1.2609 1.8955 1.8378 0.3545  -0.1375 -0.7762 1374 VAL A N   
10523 C CA  . VAL A 1374 ? 1.1951 1.8635 1.7958 0.3429  -0.1187 -0.7736 1374 VAL A CA  
10524 C C   . VAL A 1374 ? 1.1690 1.8420 1.7734 0.3225  -0.1266 -0.7637 1374 VAL A C   
10525 O O   . VAL A 1374 ? 1.1834 1.8292 1.7496 0.3104  -0.1292 -0.7573 1374 VAL A O   
10526 C CB  . VAL A 1374 ? 1.1742 1.8333 1.7426 0.3382  -0.0959 -0.7748 1374 VAL A CB  
10527 C CG1 . VAL A 1374 ? 1.1666 1.8639 1.7655 0.3327  -0.0731 -0.7748 1374 VAL A CG1 
10528 C CG2 . VAL A 1374 ? 1.1776 1.8139 1.7211 0.3549  -0.0917 -0.7839 1374 VAL A CG2 
10529 N N   . CYS A 1375 ? 1.1589 1.8668 1.8094 0.3184  -0.1295 -0.7621 1375 CYS A N   
10530 C CA  . CYS A 1375 ? 1.1159 1.8265 1.7702 0.2985  -0.1381 -0.7532 1375 CYS A CA  
10531 C C   . CYS A 1375 ? 1.1166 1.8435 1.7719 0.2812  -0.1160 -0.7482 1375 CYS A C   
10532 O O   . CYS A 1375 ? 1.0915 1.8548 1.7829 0.2806  -0.0997 -0.7504 1375 CYS A O   
10533 C CB  . CYS A 1375 ? 1.0832 1.8152 1.7801 0.2992  -0.1591 -0.7526 1375 CYS A CB  
10534 S SG  . CYS A 1375 ? 2.0920 2.7838 2.7611 0.3013  -0.1924 -0.7492 1375 CYS A SG  
10535 N N   . SER A 1376 ? 1.1284 1.8272 1.7431 0.2677  -0.1156 -0.7409 1376 SER A N   
10536 C CA  . SER A 1376 ? 1.1417 1.8473 1.7473 0.2517  -0.0957 -0.7351 1376 SER A CA  
10537 C C   . SER A 1376 ? 1.1789 1.8914 1.7993 0.2332  -0.1042 -0.7272 1376 SER A C   
10538 O O   . SER A 1376 ? 1.1968 1.9166 1.8147 0.2183  -0.0889 -0.7216 1376 SER A O   
10539 C CB  . SER A 1376 ? 1.1263 1.7967 1.6773 0.2499  -0.0895 -0.7318 1376 SER A CB  
10540 O OG  . SER A 1376 ? 1.1040 1.7532 1.6358 0.2658  -0.0987 -0.7379 1376 SER A OG  
10541 N N   . PHE A 1377 ? 1.1664 1.8752 1.8012 0.2344  -0.1289 -0.7271 1377 PHE A N   
10542 C CA  . PHE A 1377 ? 1.1292 1.8406 1.7770 0.2178  -0.1419 -0.7208 1377 PHE A CA  
10543 C C   . PHE A 1377 ? 1.1573 1.8950 1.8525 0.2225  -0.1606 -0.7249 1377 PHE A C   
10544 O O   . PHE A 1377 ? 1.1671 1.8987 1.8657 0.2388  -0.1761 -0.7300 1377 PHE A O   
10545 C CB  . PHE A 1377 ? 1.1041 1.7715 1.7068 0.2129  -0.1582 -0.7147 1377 PHE A CB  
10546 C CG  . PHE A 1377 ? 1.1175 1.7630 1.6804 0.2015  -0.1435 -0.7072 1377 PHE A CG  
10547 C CD1 . PHE A 1377 ? 1.1206 1.7729 1.6877 0.1832  -0.1345 -0.7008 1377 PHE A CD1 
10548 C CD2 . PHE A 1377 ? 1.1454 1.7633 1.6665 0.2089  -0.1387 -0.7063 1377 PHE A CD2 
10549 C CE1 . PHE A 1377 ? 1.1265 1.7578 1.6561 0.1739  -0.1208 -0.6932 1377 PHE A CE1 
10550 C CE2 . PHE A 1377 ? 1.1511 1.7507 1.6367 0.1991  -0.1257 -0.6987 1377 PHE A CE2 
10551 C CZ  . PHE A 1377 ? 1.1430 1.7492 1.6327 0.1824  -0.1167 -0.6920 1377 PHE A CZ  
10552 N N   . TYR A 1378 ? 1.1466 1.9128 1.8780 0.2078  -0.1601 -0.7224 1378 TYR A N   
10553 C CA  . TYR A 1378 ? 1.1036 1.8973 1.8820 0.2101  -0.1797 -0.7253 1378 TYR A CA  
10554 C C   . TYR A 1378 ? 1.0854 1.8480 1.8418 0.2022  -0.2070 -0.7210 1378 TYR A C   
10555 O O   . TYR A 1378 ? 1.0544 1.7969 1.7866 0.1843  -0.2067 -0.7144 1378 TYR A O   
10556 C CB  . TYR A 1378 ? 1.0723 1.9123 1.9018 0.1966  -0.1681 -0.7244 1378 TYR A CB  
10557 C CG  . TYR A 1378 ? 1.0298 1.9091 1.8935 0.2069  -0.1429 -0.7294 1378 TYR A CG  
10558 C CD1 . TYR A 1378 ? 1.0074 1.9044 1.8952 0.2296  -0.1456 -0.7368 1378 TYR A CD1 
10559 C CD2 . TYR A 1378 ? 1.0155 1.9131 1.8868 0.1939  -0.1160 -0.7263 1378 TYR A CD2 
10560 C CE1 . TYR A 1378 ? 1.0044 1.9355 1.9219 0.2399  -0.1216 -0.7414 1378 TYR A CE1 
10561 C CE2 . TYR A 1378 ? 1.0084 1.9405 1.9091 0.2034  -0.0919 -0.7307 1378 TYR A CE2 
10562 C CZ  . TYR A 1378 ? 1.0002 1.9490 1.9240 0.2267  -0.0945 -0.7383 1378 TYR A CZ  
10563 O OH  . TYR A 1378 ? 0.9875 1.9689 1.9388 0.2374  -0.0694 -0.7427 1378 TYR A OH  
10564 N N   . LEU A 1379 ? 1.1121 1.8682 1.8742 0.2161  -0.2303 -0.7246 1379 LEU A N   
10565 C CA  . LEU A 1379 ? 1.1841 1.9071 1.9208 0.2099  -0.2561 -0.7207 1379 LEU A CA  
10566 C C   . LEU A 1379 ? 1.2770 2.0210 2.0529 0.2101  -0.2820 -0.7227 1379 LEU A C   
10567 O O   . LEU A 1379 ? 1.3046 2.0872 2.1276 0.2215  -0.2840 -0.7279 1379 LEU A O   
10568 C CB  . LEU A 1379 ? 1.1673 1.8472 1.8569 0.2243  -0.2639 -0.7210 1379 LEU A CB  
10569 C CG  . LEU A 1379 ? 1.1523 1.8081 1.7992 0.2217  -0.2422 -0.7178 1379 LEU A CG  
10570 C CD1 . LEU A 1379 ? 1.1462 1.7617 1.7495 0.2352  -0.2502 -0.7180 1379 LEU A CD1 
10571 C CD2 . LEU A 1379 ? 1.1545 1.7966 1.7822 0.1999  -0.2381 -0.7099 1379 LEU A CD2 
10572 N N   . LYS A 1380 ? 1.3137 2.0312 2.0685 0.1976  -0.3020 -0.7182 1380 LYS A N   
10573 C CA  . LYS A 1380 ? 1.3304 2.0564 2.1095 0.1980  -0.3311 -0.7196 1380 LYS A CA  
10574 C C   . LYS A 1380 ? 1.3237 1.9973 2.0507 0.1918  -0.3497 -0.7149 1380 LYS A C   
10575 O O   . LYS A 1380 ? 1.3210 1.9635 2.0071 0.1802  -0.3386 -0.7096 1380 LYS A O   
10576 C CB  . LYS A 1380 ? 1.1348 1.9069 1.9686 0.1817  -0.3332 -0.7196 1380 LYS A CB  
10577 C CG  . LYS A 1380 ? 1.2154 1.9880 2.0435 0.1557  -0.3167 -0.7143 1380 LYS A CG  
10578 C CD  . LYS A 1380 ? 1.1883 2.0121 2.0777 0.1398  -0.3182 -0.7148 1380 LYS A CD  
10579 C CE  . LYS A 1380 ? 0.9702 1.7851 1.8489 0.1109  -0.3100 -0.7090 1380 LYS A CE  
10580 N NZ  . LYS A 1380 ? 0.9645 1.8186 1.8952 0.0920  -0.3202 -0.7089 1380 LYS A NZ  
10581 N N   . ILE A 1381 ? 1.3371 1.9998 2.0641 0.2017  -0.3770 -0.7166 1381 ILE A N   
10582 C CA  . ILE A 1381 ? 1.3150 1.9278 1.9937 0.1979  -0.3966 -0.7125 1381 ILE A CA  
10583 C C   . ILE A 1381 ? 1.4039 2.0222 2.1024 0.2045  -0.4286 -0.7150 1381 ILE A C   
10584 O O   . ILE A 1381 ? 1.4504 2.1009 2.1882 0.2202  -0.4346 -0.7199 1381 ILE A O   
10585 C CB  . ILE A 1381 ? 1.2064 1.7774 1.8348 0.2124  -0.3902 -0.7112 1381 ILE A CB  
10586 C CG1 . ILE A 1381 ? 1.1978 1.7182 1.7715 0.2016  -0.3965 -0.7045 1381 ILE A CG1 
10587 C CG2 . ILE A 1381 ? 1.1687 1.7347 1.8005 0.2353  -0.4074 -0.7154 1381 ILE A CG2 
10588 C CD1 . ILE A 1381 ? 1.1981 1.6776 1.7287 0.2169  -0.4026 -0.7032 1381 ILE A CD1 
10589 N N   . ASP A 1382 ? 1.4287 2.0153 2.0994 0.1928  -0.4492 -0.7115 1382 ASP A N   
10590 C CA  . ASP A 1382 ? 1.4646 2.0449 2.1404 0.2003  -0.4817 -0.7132 1382 ASP A CA  
10591 C C   . ASP A 1382 ? 1.4921 2.0246 2.1208 0.1870  -0.4998 -0.7087 1382 ASP A C   
10592 O O   . ASP A 1382 ? 1.4721 1.9806 2.0699 0.1709  -0.4869 -0.7044 1382 ASP A O   
10593 C CB  . ASP A 1382 ? 1.5082 2.1446 2.2509 0.1985  -0.4945 -0.7172 1382 ASP A CB  
10594 C CG  . ASP A 1382 ? 1.5407 2.2086 2.3146 0.1739  -0.4835 -0.7160 1382 ASP A CG  
10595 O OD1 . ASP A 1382 ? 1.5325 2.2171 2.3152 0.1701  -0.4542 -0.7156 1382 ASP A OD1 
10596 O OD2 . ASP A 1382 ? 1.5742 2.2504 2.3642 0.1581  -0.5042 -0.7155 1382 ASP A OD2 
10597 N N   . THR A 1383 ? 1.5433 2.0599 2.1644 0.1949  -0.5292 -0.7096 1383 THR A N   
10598 C CA  . THR A 1383 ? 1.5815 2.0518 2.1576 0.1835  -0.5489 -0.7059 1383 THR A CA  
10599 C C   . THR A 1383 ? 1.5957 2.0867 2.2013 0.1658  -0.5724 -0.7074 1383 THR A C   
10600 O O   . THR A 1383 ? 1.5793 2.0990 2.2224 0.1733  -0.5949 -0.7108 1383 THR A O   
10601 C CB  . THR A 1383 ? 1.5963 2.0219 2.1289 0.2021  -0.5658 -0.7048 1383 THR A CB  
10602 O OG1 . THR A 1383 ? 1.5987 2.0499 2.1617 0.2248  -0.5701 -0.7089 1383 THR A OG1 
10603 C CG2 . THR A 1383 ? 1.5797 1.9582 2.0548 0.2051  -0.5466 -0.6999 1383 THR A CG2 
10604 N N   . GLN A 1384 ? 1.6222 2.0977 2.2100 0.1423  -0.5670 -0.7045 1384 GLN A N   
10605 C CA  . GLN A 1384 ? 1.6914 2.1773 2.2975 0.1216  -0.5886 -0.7054 1384 GLN A CA  
10606 C C   . GLN A 1384 ? 1.7557 2.1869 2.3090 0.1192  -0.6152 -0.7036 1384 GLN A C   
10607 O O   . GLN A 1384 ? 1.7595 2.1400 2.2560 0.1285  -0.6102 -0.7002 1384 GLN A O   
10608 C CB  . GLN A 1384 ? 1.7201 2.2120 2.3295 0.0965  -0.5686 -0.7031 1384 GLN A CB  
10609 C CG  . GLN A 1384 ? 1.7347 2.2778 2.3924 0.0968  -0.5405 -0.7043 1384 GLN A CG  
10610 C CD  . GLN A 1384 ? 1.7746 2.3267 2.4406 0.0703  -0.5239 -0.7020 1384 GLN A CD  
10611 O OE1 . GLN A 1384 ? 1.8073 2.3143 2.4245 0.0569  -0.5191 -0.6979 1384 GLN A OE1 
10612 N NE2 . GLN A 1384 ? 1.7688 2.3788 2.4963 0.0631  -0.5140 -0.7043 1384 GLN A NE2 
10613 N N   . ASP A 1385 ? 1.8042 2.2456 2.3759 0.1061  -0.6433 -0.7058 1385 ASP A N   
10614 C CA  . ASP A 1385 ? 1.8638 2.2525 2.3842 0.1013  -0.6699 -0.7045 1385 ASP A CA  
10615 C C   . ASP A 1385 ? 1.8899 2.2492 2.3809 0.0731  -0.6686 -0.7026 1385 ASP A C   
10616 O O   . ASP A 1385 ? 1.9174 2.2168 2.3456 0.0698  -0.6753 -0.6998 1385 ASP A O   
10617 C CB  . ASP A 1385 ? 1.8831 2.2927 2.4324 0.1083  -0.7063 -0.7082 1385 ASP A CB  
10618 C CG  . ASP A 1385 ? 1.8756 2.2909 2.4305 0.1389  -0.7106 -0.7090 1385 ASP A CG  
10619 O OD1 . ASP A 1385 ? 1.8949 2.2589 2.3938 0.1526  -0.7098 -0.7063 1385 ASP A OD1 
10620 O OD2 . ASP A 1385 ? 1.8558 2.3259 2.4706 0.1495  -0.7143 -0.7121 1385 ASP A OD2 
10621 N N   . ILE A 1386 ? 1.8843 2.2843 2.4195 0.0532  -0.6583 -0.7037 1386 ILE A N   
10622 C CA  . ILE A 1386 ? 1.8974 2.2736 2.4105 0.0248  -0.6563 -0.7022 1386 ILE A CA  
10623 C C   . ILE A 1386 ? 1.8720 2.1923 2.3204 0.0237  -0.6308 -0.6967 1386 ILE A C   
10624 O O   . ILE A 1386 ? 1.8671 2.1313 2.2555 0.0323  -0.6377 -0.6942 1386 ILE A O   
10625 C CB  . ILE A 1386 ? 2.6771 3.1112 3.2535 0.0046  -0.6444 -0.7038 1386 ILE A CB  
10626 C CG1 . ILE A 1386 ? 2.6560 3.1592 3.3075 0.0144  -0.6566 -0.7080 1386 ILE A CG1 
10627 C CG2 . ILE A 1386 ? 2.7090 3.1256 3.2745 -0.0266 -0.6576 -0.7040 1386 ILE A CG2 
10628 C CD1 . ILE A 1386 ? 2.6359 3.1995 3.3529 -0.0038 -0.6431 -0.7090 1386 ILE A CD1 
10629 N N   . TYR A 1399 ? 2.6270 2.7600 2.8769 0.0828  -0.6839 -0.6903 1399 TYR A N   
10630 C CA  . TYR A 1399 ? 2.6342 2.7561 2.8714 0.1087  -0.6932 -0.6899 1399 TYR A CA  
10631 C C   . TYR A 1399 ? 2.4223 2.6010 2.7164 0.1236  -0.6784 -0.6920 1399 TYR A C   
10632 O O   . TYR A 1399 ? 2.4054 2.6240 2.7454 0.1317  -0.6965 -0.6962 1399 TYR A O   
10633 C CB  . TYR A 1399 ? 2.8295 2.8877 2.9950 0.1186  -0.6794 -0.6836 1399 TYR A CB  
10634 C CG  . TYR A 1399 ? 3.0012 3.0391 3.1444 0.1445  -0.6856 -0.6819 1399 TYR A CG  
10635 C CD1 . TYR A 1399 ? 3.0908 3.1280 3.2386 0.1544  -0.7173 -0.6850 1399 TYR A CD1 
10636 C CD2 . TYR A 1399 ? 3.0468 3.0640 3.1620 0.1584  -0.6599 -0.6767 1399 TYR A CD2 
10637 C CE1 . TYR A 1399 ? 3.1397 3.1550 3.2643 0.1779  -0.7219 -0.6830 1399 TYR A CE1 
10638 C CE2 . TYR A 1399 ? 3.0912 3.0878 3.1848 0.1806  -0.6646 -0.6749 1399 TYR A CE2 
10639 C CZ  . TYR A 1399 ? 3.1352 3.1298 3.2329 0.1903  -0.6950 -0.6780 1399 TYR A CZ  
10640 O OH  . TYR A 1399 ? 3.1528 3.1247 3.2274 0.2120  -0.6989 -0.6758 1399 TYR A OH  
10641 N N   . LYS A 1400 ? 2.2168 2.3986 2.5071 0.1273  -0.6457 -0.6889 1400 LYS A N   
10642 C CA  . LYS A 1400 ? 1.9865 2.2212 2.3289 0.1379  -0.6272 -0.6911 1400 LYS A CA  
10643 C C   . LYS A 1400 ? 1.7964 2.0282 2.1269 0.1330  -0.5914 -0.6871 1400 LYS A C   
10644 O O   . LYS A 1400 ? 1.7877 1.9715 2.0638 0.1311  -0.5802 -0.6816 1400 LYS A O   
10645 C CB  . LYS A 1400 ? 1.9392 2.1779 2.2866 0.1645  -0.6346 -0.6925 1400 LYS A CB  
10646 C CG  . LYS A 1400 ? 1.9405 2.1180 2.2236 0.1775  -0.6422 -0.6883 1400 LYS A CG  
10647 C CD  . LYS A 1400 ? 1.9094 2.0898 2.1955 0.2034  -0.6400 -0.6887 1400 LYS A CD  
10648 C CE  . LYS A 1400 ? 1.9082 2.1156 2.2304 0.2160  -0.6678 -0.6935 1400 LYS A CE  
10649 N NZ  . LYS A 1400 ? 1.8920 2.0918 2.2077 0.2415  -0.6664 -0.6934 1400 LYS A NZ  
10650 N N   . ARG A 1401 ? 1.6448 1.9282 2.0262 0.1314  -0.5734 -0.6895 1401 ARG A N   
10651 C CA  . ARG A 1401 ? 1.4913 1.7781 1.8671 0.1249  -0.5402 -0.6860 1401 ARG A CA  
10652 C C   . ARG A 1401 ? 1.4414 1.7811 1.8674 0.1344  -0.5204 -0.6891 1401 ARG A C   
10653 O O   . ARG A 1401 ? 1.4427 1.8297 1.9232 0.1363  -0.5300 -0.6944 1401 ARG A O   
10654 C CB  . ARG A 1401 ? 1.3782 1.6643 1.7552 0.0988  -0.5366 -0.6847 1401 ARG A CB  
10655 C CG  . ARG A 1401 ? 1.2569 1.5762 1.6617 0.0899  -0.5070 -0.6836 1401 ARG A CG  
10656 C CD  . ARG A 1401 ? 1.2033 1.5633 1.6571 0.0695  -0.5124 -0.6870 1401 ARG A CD  
10657 N NE  . ARG A 1401 ? 1.1809 1.5241 1.6151 0.0484  -0.4951 -0.6827 1401 ARG A NE  
10658 C CZ  . ARG A 1401 ? 1.1508 1.5290 1.6238 0.0295  -0.4859 -0.6837 1401 ARG A CZ  
10659 N NH1 . ARG A 1401 ? 1.1266 1.5626 1.6637 0.0290  -0.4916 -0.6887 1401 ARG A NH1 
10660 N NH2 . ARG A 1401 ? 1.1544 1.5094 1.6018 0.0115  -0.4700 -0.6791 1401 ARG A NH2 
10661 N N   . ILE A 1402 ? 1.3933 1.7252 1.8009 0.1403  -0.4930 -0.6857 1402 ILE A N   
10662 C CA  . ILE A 1402 ? 1.3115 1.6877 1.7591 0.1494  -0.4726 -0.6887 1402 ILE A CA  
10663 C C   . ILE A 1402 ? 1.3040 1.7110 1.7782 0.1329  -0.4499 -0.6880 1402 ILE A C   
10664 O O   . ILE A 1402 ? 1.2996 1.6818 1.7426 0.1199  -0.4359 -0.6827 1402 ILE A O   
10665 C CB  . ILE A 1402 ? 1.2485 1.6033 1.6646 0.1656  -0.4554 -0.6861 1402 ILE A CB  
10666 C CG1 . ILE A 1402 ? 1.2410 1.5667 1.6323 0.1834  -0.4748 -0.6866 1402 ILE A CG1 
10667 C CG2 . ILE A 1402 ? 1.2073 1.6059 1.6628 0.1737  -0.4354 -0.6899 1402 ILE A CG2 
10668 C CD1 . ILE A 1402 ? 1.2223 1.5278 1.5847 0.1985  -0.4592 -0.6841 1402 ILE A CD1 
10669 N N   . VAL A 1403 ? 1.3126 1.7731 1.8435 0.1348  -0.4447 -0.6930 1403 VAL A N   
10670 C CA  . VAL A 1403 ? 1.3435 1.8363 1.9029 0.1201  -0.4220 -0.6924 1403 VAL A CA  
10671 C C   . VAL A 1403 ? 1.3765 1.9024 1.9615 0.1346  -0.3993 -0.6952 1403 VAL A C   
10672 O O   . VAL A 1403 ? 1.3809 1.9509 2.0158 0.1429  -0.4021 -0.7007 1403 VAL A O   
10673 C CB  . VAL A 1403 ? 1.3483 1.8789 1.9570 0.1035  -0.4352 -0.6954 1403 VAL A CB  
10674 C CG1 . VAL A 1403 ? 1.3347 1.9068 1.9814 0.0919  -0.4096 -0.6954 1403 VAL A CG1 
10675 C CG2 . VAL A 1403 ? 1.3808 1.8758 1.9596 0.0845  -0.4532 -0.6925 1403 VAL A CG2 
10676 N N   . ALA A 1404 ? 1.3813 1.8844 1.9303 0.1379  -0.3772 -0.6912 1404 ALA A N   
10677 C CA  . ALA A 1404 ? 1.3578 1.8843 1.9207 0.1503  -0.3542 -0.6935 1404 ALA A CA  
10678 C C   . ALA A 1404 ? 1.3496 1.9012 1.9300 0.1359  -0.3284 -0.6916 1404 ALA A C   
10679 O O   . ALA A 1404 ? 1.3262 1.8566 1.8811 0.1195  -0.3208 -0.6857 1404 ALA A O   
10680 C CB  . ALA A 1404 ? 1.3274 1.8155 1.8413 0.1635  -0.3469 -0.6904 1404 ALA A CB  
10681 N N   . CYS A 1405 ? 1.3658 1.9610 1.9882 0.1429  -0.3145 -0.6963 1405 CYS A N   
10682 C CA  . CYS A 1405 ? 1.3714 1.9937 2.0131 0.1313  -0.2886 -0.6949 1405 CYS A CA  
10683 C C   . CYS A 1405 ? 1.3497 1.9877 1.9953 0.1466  -0.2666 -0.6979 1405 CYS A C   
10684 O O   . CYS A 1405 ? 1.3744 2.0085 2.0164 0.1661  -0.2727 -0.7022 1405 CYS A O   
10685 C CB  . CYS A 1405 ? 1.3739 2.0427 2.0739 0.1201  -0.2928 -0.6980 1405 CYS A CB  
10686 S SG  . CYS A 1405 ? 1.6148 2.2765 2.3252 0.1102  -0.3283 -0.6985 1405 CYS A SG  
10687 N N   . ALA A 1406 ? 1.3196 1.9741 1.9715 0.1373  -0.2409 -0.6957 1406 ALA A N   
10688 C CA  . ALA A 1406 ? 1.2730 1.9441 1.9286 0.1495  -0.2176 -0.6986 1406 ALA A CA  
10689 C C   . ALA A 1406 ? 1.2977 1.9988 1.9767 0.1361  -0.1924 -0.6968 1406 ALA A C   
10690 O O   . ALA A 1406 ? 1.2840 1.9801 1.9595 0.1164  -0.1895 -0.6913 1406 ALA A O   
10691 C CB  . ALA A 1406 ? 1.2363 1.8668 1.8364 0.1572  -0.2104 -0.6950 1406 ALA A CB  
10692 N N   . SER A 1407 ? 1.3132 2.0435 2.0143 0.1469  -0.1736 -0.7014 1407 SER A N   
10693 C CA  . SER A 1407 ? 1.3221 2.0723 2.0320 0.1371  -0.1454 -0.6990 1407 SER A CA  
10694 C C   . SER A 1407 ? 1.3341 2.0808 2.0238 0.1529  -0.1265 -0.7020 1407 SER A C   
10695 O O   . SER A 1407 ? 1.3522 2.0989 2.0437 0.1717  -0.1338 -0.7082 1407 SER A O   
10696 C CB  . SER A 1407 ? 1.3004 2.1013 2.0715 0.1313  -0.1398 -0.7022 1407 SER A CB  
10697 O OG  . SER A 1407 ? 1.2808 2.1011 2.0585 0.1273  -0.1096 -0.7010 1407 SER A OG  
10698 N N   . TYR A 1408 ? 1.3121 2.0534 1.9798 0.1451  -0.1027 -0.6973 1408 TYR A N   
10699 C CA  . TYR A 1408 ? 1.2921 2.0278 1.9362 0.1584  -0.0849 -0.6999 1408 TYR A CA  
10700 C C   . TYR A 1408 ? 1.2723 2.0498 1.9568 0.1653  -0.0658 -0.7061 1408 TYR A C   
10701 O O   . TYR A 1408 ? 1.2909 2.0949 2.0029 0.1526  -0.0512 -0.7037 1408 TYR A O   
10702 C CB  . TYR A 1408 ? 1.3127 2.0218 1.9111 0.1487  -0.0688 -0.6917 1408 TYR A CB  
10703 C CG  . TYR A 1408 ? 1.3500 2.0548 1.9243 0.1609  -0.0511 -0.6944 1408 TYR A CG  
10704 C CD1 . TYR A 1408 ? 1.3696 2.0693 1.9389 0.1796  -0.0590 -0.7018 1408 TYR A CD1 
10705 C CD2 . TYR A 1408 ? 1.3799 2.0842 1.9350 0.1536  -0.0269 -0.6895 1408 TYR A CD2 
10706 C CE1 . TYR A 1408 ? 1.4026 2.0968 1.9487 0.1899  -0.0440 -0.7050 1408 TYR A CE1 
10707 C CE2 . TYR A 1408 ? 1.4143 2.1138 1.9456 0.1645  -0.0120 -0.6923 1408 TYR A CE2 
10708 C CZ  . TYR A 1408 ? 1.4327 2.1272 1.9597 0.1823  -0.0209 -0.7004 1408 TYR A CZ  
10709 O OH  . TYR A 1408 ? 1.4606 2.1485 1.9621 0.1924  -0.0071 -0.7039 1408 TYR A OH  
10710 N N   . LYS A 1409 ? 1.2486 2.0310 1.9363 0.1854  -0.0654 -0.7140 1409 LYS A N   
10711 C CA  . LYS A 1409 ? 1.2275 2.0458 1.9481 0.1952  -0.0452 -0.7204 1409 LYS A CA  
10712 C C   . LYS A 1409 ? 1.2886 2.0955 1.9739 0.1954  -0.0190 -0.7190 1409 LYS A C   
10713 O O   . LYS A 1409 ? 1.2978 2.0775 1.9442 0.2062  -0.0197 -0.7213 1409 LYS A O   
10714 C CB  . LYS A 1409 ? 1.1651 1.9897 1.9010 0.2181  -0.0559 -0.7297 1409 LYS A CB  
10715 C CG  . LYS A 1409 ? 1.0958 1.9256 1.8588 0.2220  -0.0846 -0.7315 1409 LYS A CG  
10716 C CD  . LYS A 1409 ? 1.0568 1.8846 1.8248 0.2463  -0.0942 -0.7400 1409 LYS A CD  
10717 C CE  . LYS A 1409 ? 1.0547 1.9270 1.8737 0.2587  -0.0811 -0.7466 1409 LYS A CE  
10718 N NZ  . LYS A 1409 ? 1.0588 1.9296 1.8856 0.2833  -0.0910 -0.7547 1409 LYS A NZ  
10719 N N   . PRO A 1410 ? 1.3250 2.1516 2.0221 0.1829  0.0038  -0.7150 1410 PRO A N   
10720 C CA  . PRO A 1410 ? 1.3853 2.1982 2.0445 0.1837  0.0273  -0.7133 1410 PRO A CA  
10721 C C   . PRO A 1410 ? 1.4902 2.3124 2.1503 0.2034  0.0403  -0.7227 1410 PRO A C   
10722 O O   . PRO A 1410 ? 1.4785 2.3329 2.1819 0.2131  0.0442  -0.7292 1410 PRO A O   
10723 C CB  . PRO A 1410 ? 1.3517 2.1857 2.0283 0.1661  0.0482  -0.7070 1410 PRO A CB  
10724 C CG  . PRO A 1410 ? 1.3315 2.1696 2.0313 0.1511  0.0299  -0.7022 1410 PRO A CG  
10725 C CD  . PRO A 1410 ? 1.3287 2.1806 2.0614 0.1644  0.0074  -0.7098 1410 PRO A CD  
10726 N N   . SER A 1411 ? 1.6192 2.4119 2.2305 0.2095  0.0459  -0.7232 1411 SER A N   
10727 C CA  . SER A 1411 ? 1.7802 2.5746 2.3821 0.2264  0.0596  -0.7320 1411 SER A CA  
10728 C C   . SER A 1411 ? 1.9451 2.7624 2.5566 0.2217  0.0900  -0.7309 1411 SER A C   
10729 O O   . SER A 1411 ? 1.9532 2.7717 2.5592 0.2049  0.0998  -0.7222 1411 SER A O   
10730 C CB  . SER A 1411 ? 1.7967 2.5512 2.3412 0.2312  0.0548  -0.7320 1411 SER A CB  
10731 O OG  . SER A 1411 ? 1.7954 2.5249 2.3248 0.2296  0.0284  -0.7289 1411 SER A OG  
10732 N N   . ARG A 1412 ? 2.1044 2.9382 2.7292 0.2367  0.1058  -0.7396 1412 ARG A N   
10733 C CA  . ARG A 1412 ? 2.2730 3.1281 2.9058 0.2343  0.1367  -0.7393 1412 ARG A CA  
10734 C C   . ARG A 1412 ? 2.2758 3.1057 2.8587 0.2219  0.1488  -0.7314 1412 ARG A C   
10735 O O   . ARG A 1412 ? 2.2950 3.0904 2.8320 0.2228  0.1372  -0.7301 1412 ARG A O   
10736 C CB  . ARG A 1412 ? 2.4441 3.3060 3.0783 0.2551  0.1511  -0.7503 1412 ARG A CB  
10737 C CG  . ARG A 1412 ? 2.6020 3.4243 3.1802 0.2654  0.1460  -0.7554 1412 ARG A CG  
10738 C CD  . ARG A 1412 ? 2.7515 3.5762 3.3208 0.2825  0.1672  -0.7653 1412 ARG A CD  
10739 N NE  . ARG A 1412 ? 2.8639 3.6507 3.3718 0.2850  0.1690  -0.7675 1412 ARG A NE  
10740 C CZ  . ARG A 1412 ? 2.9585 3.7361 3.4428 0.2980  0.1856  -0.7761 1412 ARG A CZ  
10741 N NH1 . ARG A 1412 ? 2.9933 3.7966 3.5102 0.3112  0.2035  -0.7833 1412 ARG A NH1 
10742 N NH2 . ARG A 1412 ? 2.9950 3.7376 3.4228 0.2979  0.1842  -0.7775 1412 ARG A NH2 
10743 N N   . GLU A 1413 ? 2.2536 3.1013 2.8463 0.2106  0.1722  -0.7259 1413 GLU A N   
10744 C CA  . GLU A 1413 ? 2.2302 3.0560 2.7774 0.1990  0.1857  -0.7175 1413 GLU A CA  
10745 C C   . GLU A 1413 ? 2.0400 2.8491 2.5760 0.1814  0.1698  -0.7065 1413 GLU A C   
10746 O O   . GLU A 1413 ? 2.0211 2.8162 2.5275 0.1695  0.1811  -0.6975 1413 GLU A O   
10747 C CB  . GLU A 1413 ? 2.3767 3.1701 2.8685 0.2100  0.1860  -0.7215 1413 GLU A CB  
10748 C CG  . GLU A 1413 ? 2.5081 3.3092 3.0019 0.2287  0.1992  -0.7334 1413 GLU A CG  
10749 C CD  . GLU A 1413 ? 2.6142 3.4282 3.1024 0.2280  0.2322  -0.7331 1413 GLU A CD  
10750 O OE1 . GLU A 1413 ? 2.6574 3.4579 3.1130 0.2161  0.2431  -0.7244 1413 GLU A OE1 
10751 O OE2 . GLU A 1413 ? 2.6469 3.4835 3.1619 0.2402  0.2478  -0.7412 1413 GLU A OE2 
10752 N N   . GLU A 1414 ? 1.8649 2.6739 2.4225 0.1806  0.1440  -0.7071 1414 GLU A N   
10753 C CA  . GLU A 1414 ? 1.6714 2.4585 2.2123 0.1663  0.1269  -0.6977 1414 GLU A CA  
10754 C C   . GLU A 1414 ? 1.5812 2.3852 2.1513 0.1472  0.1319  -0.6900 1414 GLU A C   
10755 O O   . GLU A 1414 ? 1.5660 2.4047 2.1844 0.1448  0.1392  -0.6929 1414 GLU A O   
10756 C CB  . GLU A 1414 ? 1.5580 2.3308 2.1006 0.1733  0.0965  -0.7011 1414 GLU A CB  
10757 C CG  . GLU A 1414 ? 1.4605 2.1942 1.9500 0.1772  0.0847  -0.6984 1414 GLU A CG  
10758 C CD  . GLU A 1414 ? 1.3789 2.0999 1.8707 0.1876  0.0580  -0.7036 1414 GLU A CD  
10759 O OE1 . GLU A 1414 ? 1.3413 2.0823 1.8745 0.1908  0.0468  -0.7083 1414 GLU A OE1 
10760 O OE2 . GLU A 1414 ? 1.3627 2.0544 1.8152 0.1926  0.0480  -0.7027 1414 GLU A OE2 
10761 N N   . SER A 1415 ? 1.5244 2.3026 2.0639 0.1336  0.1274  -0.6799 1415 SER A N   
10762 C CA  . SER A 1415 ? 1.4936 2.2783 2.0509 0.1135  0.1303  -0.6716 1415 SER A CA  
10763 C C   . SER A 1415 ? 1.4763 2.2713 2.0715 0.1076  0.1061  -0.6732 1415 SER A C   
10764 O O   . SER A 1415 ? 1.4843 2.2661 2.0747 0.1167  0.0825  -0.6771 1415 SER A O   
10765 C CB  . SER A 1415 ? 1.4825 2.2310 1.9890 0.1035  0.1325  -0.6604 1415 SER A CB  
10766 O OG  . SER A 1415 ? 1.4714 2.2121 1.9859 0.0864  0.1230  -0.6531 1415 SER A OG  
10767 N N   . SER A 1416 ? 1.4695 2.2868 2.1009 0.0915  0.1118  -0.6699 1416 SER A N   
10768 C CA  . SER A 1416 ? 1.4696 2.3001 2.1400 0.0840  0.0891  -0.6715 1416 SER A CA  
10769 C C   . SER A 1416 ? 1.4689 2.2634 2.1109 0.0729  0.0676  -0.6649 1416 SER A C   
10770 O O   . SER A 1416 ? 1.4500 2.2514 2.1194 0.0642  0.0487  -0.6655 1416 SER A O   
10771 C CB  . SER A 1416 ? 1.4802 2.3494 2.2018 0.0689  0.1025  -0.6702 1416 SER A CB  
10772 O OG  . SER A 1416 ? 1.4975 2.3568 2.1990 0.0525  0.1242  -0.6611 1416 SER A OG  
10773 N N   . SER A 1417 ? 1.4958 2.2523 2.0830 0.0736  0.0706  -0.6585 1417 SER A N   
10774 C CA  . SER A 1417 ? 1.4993 2.2196 2.0553 0.0626  0.0557  -0.6506 1417 SER A CA  
10775 C C   . SER A 1417 ? 1.4667 2.1711 2.0190 0.0714  0.0258  -0.6546 1417 SER A C   
10776 O O   . SER A 1417 ? 1.5255 2.2088 2.0691 0.0614  0.0092  -0.6504 1417 SER A O   
10777 C CB  . SER A 1417 ? 1.5221 2.2087 2.0218 0.0630  0.0686  -0.6419 1417 SER A CB  
10778 O OG  . SER A 1417 ? 1.5183 2.1975 1.9938 0.0816  0.0686  -0.6460 1417 SER A OG  
10779 N N   . GLY A 1418 ? 1.3570 2.0693 1.9137 0.0903  0.0197  -0.6627 1418 GLY A N   
10780 C CA  . GLY A 1418 ? 1.2724 1.9673 1.8213 0.1007  -0.0069 -0.6663 1418 GLY A CA  
10781 C C   . GLY A 1418 ? 1.2486 1.9087 1.7460 0.1114  -0.0098 -0.6635 1418 GLY A C   
10782 O O   . GLY A 1418 ? 1.2229 1.8719 1.6893 0.1109  0.0077  -0.6585 1418 GLY A O   
10783 N N   . SER A 1419 ? 1.2344 1.8769 1.7224 0.1206  -0.0326 -0.6662 1419 SER A N   
10784 C CA  . SER A 1419 ? 1.2038 1.8201 1.6517 0.1332  -0.0363 -0.6656 1419 SER A CA  
10785 C C   . SER A 1419 ? 1.1355 1.7189 1.5348 0.1275  -0.0308 -0.6546 1419 SER A C   
10786 O O   . SER A 1419 ? 1.1413 1.7165 1.5325 0.1134  -0.0238 -0.6466 1419 SER A O   
10787 C CB  . SER A 1419 ? 1.2014 1.8057 1.6511 0.1437  -0.0616 -0.6703 1419 SER A CB  
10788 O OG  . SER A 1419 ? 1.1911 1.7718 1.6034 0.1547  -0.0637 -0.6695 1419 SER A OG  
10789 N N   . SER A 1420 ? 1.0712 1.6367 1.4390 0.1391  -0.0334 -0.6545 1420 SER A N   
10790 C CA  . SER A 1420 ? 1.0348 1.5690 1.3564 0.1376  -0.0321 -0.6443 1420 SER A CA  
10791 C C   . SER A 1420 ? 1.0484 1.5563 1.3568 0.1389  -0.0543 -0.6414 1420 SER A C   
10792 O O   . SER A 1420 ? 1.0780 1.5914 1.4107 0.1414  -0.0706 -0.6476 1420 SER A O   
10793 C CB  . SER A 1420 ? 0.9910 1.5207 1.2874 0.1494  -0.0260 -0.6460 1420 SER A CB  
10794 O OG  . SER A 1420 ? 0.9578 1.4694 1.2409 0.1593  -0.0447 -0.6480 1420 SER A OG  
10795 N N   . HIS A 1421 ? 1.0306 1.5098 1.2996 0.1384  -0.0549 -0.6316 1421 HIS A N   
10796 C CA  . HIS A 1421 ? 1.0020 1.4539 1.2545 0.1407  -0.0742 -0.6281 1421 HIS A CA  
10797 C C   . HIS A 1421 ? 0.9226 1.3799 1.1918 0.1524  -0.0908 -0.6381 1421 HIS A C   
10798 O O   . HIS A 1421 ? 0.8724 1.3357 1.1374 0.1628  -0.0883 -0.6429 1421 HIS A O   
10799 C CB  . HIS A 1421 ? 1.0544 1.4791 1.2628 0.1428  -0.0703 -0.6169 1421 HIS A CB  
10800 C CG  . HIS A 1421 ? 1.0578 1.4585 1.2471 0.1510  -0.0875 -0.6151 1421 HIS A CG  
10801 N ND1 . HIS A 1421 ? 1.0559 1.4407 1.2131 0.1574  -0.0857 -0.6080 1421 HIS A ND1 
10802 C CD2 . HIS A 1421 ? 1.0560 1.4462 1.2537 0.1540  -0.1067 -0.6190 1421 HIS A CD2 
10803 C CE1 . HIS A 1421 ? 1.0669 1.4327 1.2143 0.1635  -0.1019 -0.6076 1421 HIS A CE1 
10804 N NE2 . HIS A 1421 ? 1.0646 1.4319 1.2347 0.1619  -0.1148 -0.6142 1421 HIS A NE2 
10805 N N   . ALA A 1422 ? 0.9017 1.3563 1.1892 0.1504  -0.1078 -0.6413 1422 ALA A N   
10806 C CA  . ALA A 1422 ? 0.9394 1.3998 1.2458 0.1615  -0.1244 -0.6507 1422 ALA A CA  
10807 C C   . ALA A 1422 ? 0.9860 1.4215 1.2836 0.1618  -0.1462 -0.6487 1422 ALA A C   
10808 O O   . ALA A 1422 ? 0.9788 1.3960 1.2624 0.1517  -0.1490 -0.6415 1422 ALA A O   
10809 C CB  . ALA A 1422 ? 0.9098 1.4054 1.2615 0.1617  -0.1224 -0.6603 1422 ALA A CB  
10810 N N   . VAL A 1423 ? 1.0245 1.4572 1.3280 0.1738  -0.1613 -0.6552 1423 VAL A N   
10811 C CA  . VAL A 1423 ? 1.0657 1.4735 1.3590 0.1759  -0.1825 -0.6538 1423 VAL A CA  
10812 C C   . VAL A 1423 ? 1.0830 1.5087 1.4121 0.1821  -0.1979 -0.6637 1423 VAL A C   
10813 O O   . VAL A 1423 ? 1.1077 1.5590 1.4614 0.1901  -0.1925 -0.6717 1423 VAL A O   
10814 C CB  . VAL A 1423 ? 0.8448 1.2233 1.1027 0.1854  -0.1883 -0.6498 1423 VAL A CB  
10815 C CG1 . VAL A 1423 ? 0.8515 1.2276 1.0853 0.1851  -0.1704 -0.6439 1423 VAL A CG1 
10816 C CG2 . VAL A 1423 ? 0.8421 1.2237 1.1118 0.1990  -0.2007 -0.6584 1423 VAL A CG2 
10817 N N   . MET A 1424 ? 1.0866 1.4992 1.4182 0.1779  -0.2162 -0.6628 1424 MET A N   
10818 C CA  . MET A 1424 ? 1.0247 1.4454 1.3822 0.1852  -0.2367 -0.6704 1424 MET A CA  
10819 C C   . MET A 1424 ? 1.0607 1.4441 1.3857 0.1937  -0.2535 -0.6676 1424 MET A C   
10820 O O   . MET A 1424 ? 1.0887 1.4406 1.3778 0.1885  -0.2539 -0.6591 1424 MET A O   
10821 C CB  . MET A 1424 ? 0.9284 1.3622 1.3122 0.1727  -0.2460 -0.6712 1424 MET A CB  
10822 C CG  . MET A 1424 ? 0.9015 1.3514 1.2938 0.1575  -0.2270 -0.6676 1424 MET A CG  
10823 S SD  . MET A 1424 ? 0.9679 1.4355 1.3937 0.1396  -0.2362 -0.6686 1424 MET A SD  
10824 C CE  . MET A 1424 ? 0.8729 1.3708 1.3455 0.1510  -0.2564 -0.6790 1424 MET A CE  
10825 N N   . ASP A 1425 ? 1.0906 1.4766 1.4271 0.2073  -0.2664 -0.6743 1425 ASP A N   
10826 C CA  . ASP A 1425 ? 1.1289 1.4800 1.4339 0.2168  -0.2796 -0.6718 1425 ASP A CA  
10827 C C   . ASP A 1425 ? 1.1738 1.5268 1.4987 0.2251  -0.3022 -0.6780 1425 ASP A C   
10828 O O   . ASP A 1425 ? 1.1882 1.5611 1.5381 0.2368  -0.3045 -0.6858 1425 ASP A O   
10829 C CB  . ASP A 1425 ? 1.1491 1.4970 1.4397 0.2271  -0.2685 -0.6730 1425 ASP A CB  
10830 C CG  . ASP A 1425 ? 1.2050 1.5211 1.4691 0.2381  -0.2818 -0.6718 1425 ASP A CG  
10831 O OD1 . ASP A 1425 ? 1.2127 1.5174 1.4550 0.2427  -0.2731 -0.6698 1425 ASP A OD1 
10832 O OD2 . ASP A 1425 ? 1.2385 1.5409 1.5032 0.2418  -0.3009 -0.6728 1425 ASP A OD2 
10833 N N   . ILE A 1426 ? 1.1605 1.4916 1.4726 0.2195  -0.3188 -0.6743 1426 ILE A N   
10834 C CA  . ILE A 1426 ? 1.1178 1.4451 1.4422 0.2269  -0.3429 -0.6787 1426 ILE A CA  
10835 C C   . ILE A 1426 ? 1.1056 1.3925 1.3928 0.2374  -0.3554 -0.6756 1426 ILE A C   
10836 O O   . ILE A 1426 ? 1.0935 1.3460 1.3434 0.2321  -0.3575 -0.6680 1426 ILE A O   
10837 C CB  . ILE A 1426 ? 1.1112 1.4385 1.4439 0.2138  -0.3557 -0.6773 1426 ILE A CB  
10838 C CG1 . ILE A 1426 ? 1.0765 1.4349 1.4349 0.1994  -0.3394 -0.6774 1426 ILE A CG1 
10839 C CG2 . ILE A 1426 ? 1.1253 1.4642 1.4854 0.2215  -0.3797 -0.6837 1426 ILE A CG2 
10840 C CD1 . ILE A 1426 ? 1.0874 1.4649 1.4767 0.1886  -0.3533 -0.6802 1426 ILE A CD1 
10841 N N   . SER A 1427 ? 1.1098 1.4006 1.4072 0.2527  -0.3623 -0.6813 1427 SER A N   
10842 C CA  . SER A 1427 ? 1.1080 1.3640 1.3775 0.2642  -0.3772 -0.6798 1427 SER A CA  
10843 C C   . SER A 1427 ? 1.1114 1.3576 1.3838 0.2619  -0.4010 -0.6798 1427 SER A C   
10844 O O   . SER A 1427 ? 1.1068 1.3839 1.4178 0.2599  -0.4096 -0.6853 1427 SER A O   
10845 C CB  . SER A 1427 ? 0.9903 1.2582 1.2763 0.2807  -0.3772 -0.6871 1427 SER A CB  
10846 O OG  . SER A 1427 ? 1.0037 1.2437 1.2724 0.2937  -0.3944 -0.6875 1427 SER A OG  
10847 N N   . LEU A 1428 ? 1.0958 1.2999 1.3275 0.2613  -0.4112 -0.6734 1428 LEU A N   
10848 C CA  . LEU A 1428 ? 1.1052 1.2942 1.3333 0.2605  -0.4357 -0.6736 1428 LEU A CA  
10849 C C   . LEU A 1428 ? 1.1268 1.3012 1.3501 0.2778  -0.4521 -0.6765 1428 LEU A C   
10850 O O   . LEU A 1428 ? 1.1176 1.2713 1.3172 0.2870  -0.4447 -0.6742 1428 LEU A O   
10851 C CB  . LEU A 1428 ? 1.0745 1.2231 1.2584 0.2505  -0.4380 -0.6651 1428 LEU A CB  
10852 C CG  . LEU A 1428 ? 1.0409 1.2021 1.2284 0.2338  -0.4211 -0.6620 1428 LEU A CG  
10853 C CD1 . LEU A 1428 ? 1.0524 1.1711 1.1925 0.2257  -0.4189 -0.6529 1428 LEU A CD1 
10854 C CD2 . LEU A 1428 ? 0.9978 1.1951 1.2280 0.2238  -0.4288 -0.6678 1428 LEU A CD2 
10855 N N   . PRO A 1429 ? 1.1271 1.3136 1.3745 0.2821  -0.4744 -0.6813 1429 PRO A N   
10856 C CA  . PRO A 1429 ? 1.1244 1.2964 1.3680 0.2994  -0.4930 -0.6839 1429 PRO A CA  
10857 C C   . PRO A 1429 ? 1.1478 1.2661 1.3379 0.3020  -0.5017 -0.6768 1429 PRO A C   
10858 O O   . PRO A 1429 ? 1.1329 1.2276 1.2937 0.2900  -0.4997 -0.6708 1429 PRO A O   
10859 C CB  . PRO A 1429 ? 1.1114 1.3100 1.3918 0.2989  -0.5148 -0.6888 1429 PRO A CB  
10860 C CG  . PRO A 1429 ? 1.0953 1.3370 1.4143 0.2858  -0.5012 -0.6917 1429 PRO A CG  
10861 C CD  . PRO A 1429 ? 1.0908 1.3147 1.3794 0.2718  -0.4808 -0.6855 1429 PRO A CD  
10862 N N   . THR A 1430 ? 1.1800 1.2780 1.3562 0.3181  -0.5098 -0.6774 1430 THR A N   
10863 C CA  . THR A 1430 ? 1.2176 1.2648 1.3417 0.3218  -0.5114 -0.6700 1430 THR A CA  
10864 C C   . THR A 1430 ? 1.2921 1.3103 1.3888 0.3143  -0.5288 -0.6657 1430 THR A C   
10865 O O   . THR A 1430 ? 1.3390 1.3619 1.4489 0.3174  -0.5518 -0.6692 1430 THR A O   
10866 C CB  . THR A 1430 ? 1.2063 1.2375 1.3232 0.3404  -0.5188 -0.6719 1430 THR A CB  
10867 O OG1 . THR A 1430 ? 1.1810 1.2504 1.3389 0.3481  -0.5110 -0.6796 1430 THR A OG1 
10868 C CG2 . THR A 1430 ? 1.1912 1.1833 1.2642 0.3428  -0.5061 -0.6649 1430 THR A CG2 
10869 N N   . GLY A 1431 ? 1.3078 1.2972 1.3668 0.3044  -0.5172 -0.6580 1431 GLY A N   
10870 C CA  . GLY A 1431 ? 1.3368 1.2954 1.3647 0.2955  -0.5294 -0.6536 1431 GLY A CA  
10871 C C   . GLY A 1431 ? 1.3565 1.3411 1.4122 0.2822  -0.5397 -0.6579 1431 GLY A C   
10872 O O   . GLY A 1431 ? 1.3169 1.3025 1.3818 0.2841  -0.5637 -0.6615 1431 GLY A O   
10873 N N   . ILE A 1432 ? 1.3863 1.3914 1.4549 0.2683  -0.5218 -0.6571 1432 ILE A N   
10874 C CA  . ILE A 1432 ? 1.4240 1.4562 1.5214 0.2534  -0.5278 -0.6609 1432 ILE A CA  
10875 C C   . ILE A 1432 ? 1.4300 1.4609 1.5160 0.2387  -0.5051 -0.6561 1432 ILE A C   
10876 O O   . ILE A 1432 ? 1.4457 1.5154 1.5671 0.2317  -0.4913 -0.6590 1432 ILE A O   
10877 C CB  . ILE A 1432 ? 1.1826 1.2721 1.3417 0.2558  -0.5275 -0.6692 1432 ILE A CB  
10878 C CG1 . ILE A 1432 ? 1.2447 1.3408 1.4197 0.2746  -0.5439 -0.6738 1432 ILE A CG1 
10879 C CG2 . ILE A 1432 ? 1.1413 1.2600 1.3327 0.2397  -0.5356 -0.6728 1432 ILE A CG2 
10880 C CD1 . ILE A 1432 ? 1.3094 1.4045 1.4937 0.2767  -0.5752 -0.6771 1432 ILE A CD1 
10881 N N   . SER A 1433 ? 1.4428 1.4289 1.4789 0.2348  -0.5002 -0.6483 1433 SER A N   
10882 C CA  . SER A 1433 ? 1.4268 1.4059 1.4460 0.2226  -0.4780 -0.6422 1433 SER A CA  
10883 C C   . SER A 1433 ? 1.4031 1.4157 1.4559 0.2061  -0.4738 -0.6459 1433 SER A C   
10884 O O   . SER A 1433 ? 1.4023 1.4256 1.4742 0.1988  -0.4928 -0.6511 1433 SER A O   
10885 C CB  . SER A 1433 ? 1.4846 1.4086 1.4466 0.2194  -0.4805 -0.6344 1433 SER A CB  
10886 O OG  . SER A 1433 ? 1.5166 1.4053 1.4445 0.2335  -0.4867 -0.6306 1433 SER A OG  
10887 N N   . ALA A 1434 ? 1.3876 1.4164 1.4472 0.1996  -0.4495 -0.6428 1434 ALA A N   
10888 C CA  . ALA A 1434 ? 1.4172 1.4744 1.5055 0.1832  -0.4439 -0.6455 1434 ALA A CA  
10889 C C   . ALA A 1434 ? 1.4512 1.4722 1.5014 0.1700  -0.4407 -0.6393 1434 ALA A C   
10890 O O   . ALA A 1434 ? 1.4876 1.4647 1.4904 0.1750  -0.4386 -0.6325 1434 ALA A O   
10891 C CB  . ALA A 1434 ? 1.4158 1.5095 1.5316 0.1827  -0.4197 -0.6456 1434 ALA A CB  
10892 N N   . ASN A 1435 ? 1.4466 1.4850 1.5168 0.1532  -0.4393 -0.6416 1435 ASN A N   
10893 C CA  . ASN A 1435 ? 1.4831 1.4845 1.5169 0.1392  -0.4387 -0.6368 1435 ASN A CA  
10894 C C   . ASN A 1435 ? 1.4574 1.4480 1.4697 0.1340  -0.4109 -0.6286 1435 ASN A C   
10895 O O   . ASN A 1435 ? 1.4347 1.4427 1.4639 0.1197  -0.4005 -0.6289 1435 ASN A O   
10896 C CB  . ASN A 1435 ? 1.4991 1.5174 1.5602 0.1217  -0.4548 -0.6431 1435 ASN A CB  
10897 C CG  . ASN A 1435 ? 1.5493 1.5224 1.5680 0.1076  -0.4590 -0.6394 1435 ASN A CG  
10898 O OD1 . ASN A 1435 ? 1.5632 1.4947 1.5339 0.1110  -0.4465 -0.6316 1435 ASN A OD1 
10899 N ND2 . ASN A 1435 ? 1.5861 1.5669 1.6222 0.0916  -0.4768 -0.6449 1435 ASN A ND2 
10900 N N   . GLU A 1436 ? 1.4932 1.4541 1.4673 0.1456  -0.3991 -0.6208 1436 GLU A N   
10901 C CA  . GLU A 1436 ? 1.5129 1.4669 1.4685 0.1439  -0.3727 -0.6123 1436 GLU A CA  
10902 C C   . GLU A 1436 ? 1.5095 1.4612 1.4645 0.1257  -0.3652 -0.6111 1436 GLU A C   
10903 O O   . GLU A 1436 ? 1.4980 1.4734 1.4695 0.1204  -0.3459 -0.6088 1436 GLU A O   
10904 C CB  . GLU A 1436 ? 1.5813 1.4880 1.4839 0.1543  -0.3668 -0.6028 1436 GLU A CB  
10905 C CG  . GLU A 1436 ? 1.6158 1.5191 1.5013 0.1567  -0.3395 -0.5928 1436 GLU A CG  
10906 C CD  . GLU A 1436 ? 1.6243 1.5414 1.5140 0.1719  -0.3298 -0.5895 1436 GLU A CD  
10907 O OE1 . GLU A 1436 ? 1.6347 1.5718 1.5487 0.1794  -0.3419 -0.5965 1436 GLU A OE1 
10908 O OE2 . GLU A 1436 ? 1.6035 1.5106 1.4716 0.1761  -0.3104 -0.5799 1436 GLU A OE2 
10909 N N   . GLU A 1437 ? 1.5511 1.4730 1.4859 0.1156  -0.3811 -0.6127 1437 GLU A N   
10910 C CA  . GLU A 1437 ? 1.5419 1.4510 1.4668 0.0975  -0.3744 -0.6109 1437 GLU A CA  
10911 C C   . GLU A 1437 ? 1.5433 1.5029 1.5225 0.0842  -0.3729 -0.6175 1437 GLU A C   
10912 O O   . GLU A 1437 ? 1.5410 1.5078 1.5239 0.0735  -0.3548 -0.6142 1437 GLU A O   
10913 C CB  . GLU A 1437 ? 1.6083 1.4712 1.4973 0.0887  -0.3941 -0.6122 1437 GLU A CB  
10914 C CG  . GLU A 1437 ? 2.1982 2.0231 2.0499 0.1037  -0.4088 -0.6107 1437 GLU A CG  
10915 C CD  . GLU A 1437 ? 2.1518 1.9402 1.9566 0.1172  -0.3895 -0.5996 1437 GLU A CD  
10916 O OE1 . GLU A 1437 ? 2.1437 1.9102 1.9227 0.1110  -0.3717 -0.5927 1437 GLU A OE1 
10917 O OE2 . GLU A 1437 ? 2.1062 1.8878 1.9005 0.1337  -0.3921 -0.5976 1437 GLU A OE2 
10918 N N   . ASP A 1438 ? 1.5291 1.5234 1.5502 0.0855  -0.3911 -0.6265 1438 ASP A N   
10919 C CA  . ASP A 1438 ? 1.5159 1.5617 1.5925 0.0740  -0.3897 -0.6328 1438 ASP A CA  
10920 C C   . ASP A 1438 ? 1.4626 1.5381 1.5571 0.0769  -0.3617 -0.6293 1438 ASP A C   
10921 O O   . ASP A 1438 ? 1.4558 1.5529 1.5721 0.0628  -0.3497 -0.6295 1438 ASP A O   
10922 C CB  . ASP A 1438 ? 1.5277 1.6094 1.6474 0.0812  -0.4107 -0.6418 1438 ASP A CB  
10923 C CG  . ASP A 1438 ? 1.5609 1.6283 1.6793 0.0722  -0.4401 -0.6469 1438 ASP A CG  
10924 O OD1 . ASP A 1438 ? 1.5873 1.6241 1.6793 0.0564  -0.4431 -0.6449 1438 ASP A OD1 
10925 O OD2 . ASP A 1438 ? 1.5551 1.6412 1.6978 0.0810  -0.4606 -0.6529 1438 ASP A OD2 
10926 N N   . LEU A 1439 ? 1.3910 1.4666 1.4753 0.0948  -0.3520 -0.6261 1439 LEU A N   
10927 C CA  . LEU A 1439 ? 1.3066 1.4104 1.4062 0.1002  -0.3278 -0.6233 1439 LEU A CA  
10928 C C   . LEU A 1439 ? 1.2944 1.3742 1.3607 0.0939  -0.3058 -0.6136 1439 LEU A C   
10929 O O   . LEU A 1439 ? 1.2777 1.3818 1.3619 0.0869  -0.2877 -0.6122 1439 LEU A O   
10930 C CB  . LEU A 1439 ? 1.2473 1.3537 1.3421 0.1202  -0.3269 -0.6230 1439 LEU A CB  
10931 C CG  . LEU A 1439 ? 1.2111 1.3401 1.3370 0.1298  -0.3466 -0.6320 1439 LEU A CG  
10932 C CD1 . LEU A 1439 ? 1.2031 1.3196 1.3106 0.1483  -0.3465 -0.6300 1439 LEU A CD1 
10933 C CD2 . LEU A 1439 ? 1.1746 1.3572 1.3550 0.1268  -0.3415 -0.6392 1439 LEU A CD2 
10934 N N   . LYS A 1440 ? 1.3247 1.3558 1.3413 0.0974  -0.3071 -0.6065 1440 LYS A N   
10935 C CA  . LYS A 1440 ? 1.3660 1.3674 1.3463 0.0917  -0.2886 -0.5967 1440 LYS A CA  
10936 C C   . LYS A 1440 ? 1.3422 1.3554 1.3410 0.0717  -0.2848 -0.5991 1440 LYS A C   
10937 O O   . LYS A 1440 ? 1.3215 1.3353 1.3137 0.0658  -0.2642 -0.5930 1440 LYS A O   
10938 C CB  . LYS A 1440 ? 1.4690 1.4133 1.3963 0.0944  -0.2964 -0.5911 1440 LYS A CB  
10939 C CG  . LYS A 1440 ? 1.5514 1.4737 1.4493 0.1134  -0.2955 -0.5854 1440 LYS A CG  
10940 C CD  . LYS A 1440 ? 1.6217 1.5337 1.4942 0.1207  -0.2703 -0.5736 1440 LYS A CD  
10941 C CE  . LYS A 1440 ? 1.7317 1.5926 1.5508 0.1308  -0.2680 -0.5640 1440 LYS A CE  
10942 N NZ  . LYS A 1440 ? 1.7659 1.6083 1.5720 0.1415  -0.2860 -0.5667 1440 LYS A NZ  
10943 N N   . ALA A 1441 ? 1.3779 1.4001 1.3998 0.0611  -0.3055 -0.6076 1441 ALA A N   
10944 C CA  . ALA A 1441 ? 1.4097 1.4421 1.4508 0.0397  -0.3057 -0.6106 1441 ALA A CA  
10945 C C   . ALA A 1441 ? 1.4368 1.5171 1.5194 0.0352  -0.2870 -0.6115 1441 ALA A C   
10946 O O   . ALA A 1441 ? 1.4609 1.5421 1.5457 0.0199  -0.2742 -0.6089 1441 ALA A O   
10947 C CB  . ALA A 1441 ? 1.4172 1.4599 1.4837 0.0311  -0.3337 -0.6202 1441 ALA A CB  
10948 N N   . LEU A 1442 ? 1.4262 1.5443 1.5400 0.0487  -0.2852 -0.6154 1442 LEU A N   
10949 C CA  . LEU A 1442 ? 1.4147 1.5812 1.5713 0.0455  -0.2696 -0.6180 1442 LEU A CA  
10950 C C   . LEU A 1442 ? 1.4986 1.6613 1.6354 0.0487  -0.2421 -0.6093 1442 LEU A C   
10951 O O   . LEU A 1442 ? 1.5415 1.7228 1.6946 0.0372  -0.2263 -0.6080 1442 LEU A O   
10952 C CB  . LEU A 1442 ? 1.3419 1.5471 1.5366 0.0591  -0.2781 -0.6258 1442 LEU A CB  
10953 C CG  . LEU A 1442 ? 1.3293 1.5516 1.5577 0.0496  -0.3013 -0.6342 1442 LEU A CG  
10954 C CD1 . LEU A 1442 ? 1.3137 1.5578 1.5668 0.0656  -0.3176 -0.6414 1442 LEU A CD1 
10955 C CD2 . LEU A 1442 ? 1.3223 1.5827 1.5927 0.0327  -0.2916 -0.6370 1442 LEU A CD2 
10956 N N   . VAL A 1443 ? 1.5068 1.6455 1.6086 0.0641  -0.2365 -0.6030 1443 VAL A N   
10957 C CA  . VAL A 1443 ? 1.5348 1.6728 1.6186 0.0694  -0.2120 -0.5943 1443 VAL A CA  
10958 C C   . VAL A 1443 ? 1.5666 1.6634 1.6070 0.0623  -0.1998 -0.5837 1443 VAL A C   
10959 O O   . VAL A 1443 ? 1.5703 1.6697 1.6008 0.0622  -0.1787 -0.5765 1443 VAL A O   
10960 C CB  . VAL A 1443 ? 1.5306 1.6666 1.6003 0.0894  -0.2106 -0.5917 1443 VAL A CB  
10961 C CG1 . VAL A 1443 ? 1.5397 1.6844 1.6275 0.0980  -0.2326 -0.6005 1443 VAL A CG1 
10962 C CG2 . VAL A 1443 ? 1.5580 1.6483 1.5760 0.0957  -0.2052 -0.5806 1443 VAL A CG2 
10963 N N   . GLU A 1444 ? 1.6335 1.6909 1.6464 0.0567  -0.2131 -0.5828 1444 GLU A N   
10964 C CA  . GLU A 1444 ? 1.7000 1.7095 1.6624 0.0560  -0.2030 -0.5722 1444 GLU A CA  
10965 C C   . GLU A 1444 ? 1.6829 1.6804 1.6398 0.0370  -0.1936 -0.5697 1444 GLU A C   
10966 O O   . GLU A 1444 ? 1.6826 1.6364 1.5967 0.0346  -0.1865 -0.5617 1444 GLU A O   
10967 C CB  . GLU A 1444 ? 1.8261 1.7935 1.7550 0.0614  -0.2210 -0.5721 1444 GLU A CB  
10968 C CG  . GLU A 1444 ? 1.9450 1.8614 1.8185 0.0668  -0.2105 -0.5605 1444 GLU A CG  
10969 C CD  . GLU A 1444 ? 2.0242 1.9084 1.8679 0.0800  -0.2245 -0.5595 1444 GLU A CD  
10970 O OE1 . GLU A 1444 ? 2.0164 1.9219 1.8758 0.0933  -0.2302 -0.5620 1444 GLU A OE1 
10971 O OE2 . GLU A 1444 ? 2.0824 1.9184 1.8854 0.0771  -0.2292 -0.5561 1444 GLU A OE2 
10972 N N   . GLY A 1445 ? 1.6905 1.7260 1.6903 0.0237  -0.1925 -0.5764 1445 GLY A N   
10973 C CA  . GLY A 1445 ? 1.7425 1.7673 1.7407 0.0030  -0.1858 -0.5751 1445 GLY A CA  
10974 C C   . GLY A 1445 ? 1.7486 1.8085 1.7742 -0.0042 -0.1645 -0.5735 1445 GLY A C   
10975 O O   . GLY A 1445 ? 1.7298 1.8334 1.7903 0.0032  -0.1602 -0.5775 1445 GLY A O   
10976 N N   . VAL A 1446 ? 1.7676 1.8059 1.7747 -0.0185 -0.1507 -0.5675 1446 VAL A N   
10977 C CA  . VAL A 1446 ? 1.7552 1.8225 1.7848 -0.0273 -0.1295 -0.5652 1446 VAL A CA  
10978 C C   . VAL A 1446 ? 1.7122 1.8343 1.8021 -0.0352 -0.1359 -0.5758 1446 VAL A C   
10979 O O   . VAL A 1446 ? 1.6817 1.8394 1.7978 -0.0355 -0.1194 -0.5757 1446 VAL A O   
10980 C CB  . VAL A 1446 ? 1.8092 1.8443 1.8158 -0.0467 -0.1187 -0.5595 1446 VAL A CB  
10981 C CG1 . VAL A 1446 ? 1.8080 1.8694 1.8316 -0.0532 -0.0939 -0.5552 1446 VAL A CG1 
10982 C CG2 . VAL A 1446 ? 1.8325 1.8083 1.7780 -0.0396 -0.1145 -0.5495 1446 VAL A CG2 
10983 N N   . ASP A 1447 ? 1.7125 1.8405 1.8236 -0.0414 -0.1600 -0.5849 1447 ASP A N   
10984 C CA  . ASP A 1447 ? 1.7083 1.8893 1.8783 -0.0461 -0.1685 -0.5949 1447 ASP A CA  
10985 C C   . ASP A 1447 ? 1.6618 1.8698 1.8484 -0.0239 -0.1738 -0.5992 1447 ASP A C   
10986 O O   . ASP A 1447 ? 1.6426 1.8889 1.8732 -0.0223 -0.1863 -0.6082 1447 ASP A O   
10987 C CB  . ASP A 1447 ? 1.7611 1.9393 1.9489 -0.0622 -0.1934 -0.6025 1447 ASP A CB  
10988 C CG  . ASP A 1447 ? 1.8089 1.9487 1.9635 -0.0531 -0.2165 -0.6038 1447 ASP A CG  
10989 O OD1 . ASP A 1447 ? 1.8089 1.9154 1.9197 -0.0375 -0.2104 -0.5971 1447 ASP A OD1 
10990 O OD2 . ASP A 1447 ? 1.8346 1.9780 2.0072 -0.0617 -0.2406 -0.6113 1447 ASP A OD2 
10991 N N   . GLN A 1448 ? 1.6397 1.8281 1.7913 -0.0067 -0.1641 -0.5924 1448 GLN A N   
10992 C CA  . GLN A 1448 ? 1.6017 1.8055 1.7606 0.0137  -0.1718 -0.5961 1448 GLN A CA  
10993 C C   . GLN A 1448 ? 1.5578 1.8164 1.7704 0.0161  -0.1710 -0.6048 1448 GLN A C   
10994 O O   . GLN A 1448 ? 1.5556 1.8407 1.7860 0.0125  -0.1515 -0.6036 1448 GLN A O   
10995 C CB  . GLN A 1448 ? 1.6025 1.7877 1.7240 0.0299  -0.1571 -0.5871 1448 GLN A CB  
10996 C CG  . GLN A 1448 ? 1.6103 1.8143 1.7344 0.0302  -0.1314 -0.5816 1448 GLN A CG  
10997 C CD  . GLN A 1448 ? 1.6250 1.8166 1.7176 0.0481  -0.1214 -0.5739 1448 GLN A CD  
10998 O OE1 . GLN A 1448 ? 1.6127 1.8096 1.7067 0.0626  -0.1314 -0.5770 1448 GLN A OE1 
10999 N NE2 . GLN A 1448 ? 1.6407 1.8157 1.7048 0.0469  -0.1018 -0.5633 1448 GLN A NE2 
11000 N N   . LEU A 1449 ? 1.5472 1.8210 1.7841 0.0223  -0.1923 -0.6133 1449 LEU A N   
11001 C CA  . LEU A 1449 ? 1.5370 1.8608 1.8240 0.0284  -0.1940 -0.6220 1449 LEU A CA  
11002 C C   . LEU A 1449 ? 1.4664 1.7955 1.7433 0.0495  -0.1875 -0.6217 1449 LEU A C   
11003 O O   . LEU A 1449 ? 1.4286 1.7910 1.7289 0.0550  -0.1731 -0.6242 1449 LEU A O   
11004 C CB  . LEU A 1449 ? 1.6080 1.9431 1.9237 0.0263  -0.2211 -0.6307 1449 LEU A CB  
11005 C CG  . LEU A 1449 ? 1.6486 2.0312 2.0148 0.0361  -0.2284 -0.6401 1449 LEU A CG  
11006 C CD1 . LEU A 1449 ? 1.6507 2.0769 2.0546 0.0307  -0.2065 -0.6416 1449 LEU A CD1 
11007 C CD2 . LEU A 1449 ? 1.6776 2.0681 2.0701 0.0303  -0.2561 -0.6469 1449 LEU A CD2 
11008 N N   . PHE A 1450 ? 1.4329 1.7279 1.6739 0.0609  -0.1979 -0.6186 1450 PHE A N   
11009 C CA  . PHE A 1450 ? 1.3915 1.6852 1.6163 0.0790  -0.1915 -0.6167 1450 PHE A CA  
11010 C C   . PHE A 1450 ? 1.4029 1.6612 1.5797 0.0805  -0.1777 -0.6050 1450 PHE A C   
11011 O O   . PHE A 1450 ? 1.4256 1.6574 1.5801 0.0690  -0.1744 -0.5990 1450 PHE A O   
11012 C CB  . PHE A 1450 ? 1.3689 1.6554 1.5938 0.0923  -0.2131 -0.6219 1450 PHE A CB  
11013 C CG  . PHE A 1450 ? 1.3472 1.6682 1.6191 0.0923  -0.2273 -0.6327 1450 PHE A CG  
11014 C CD1 . PHE A 1450 ? 1.3752 1.6974 1.6646 0.0793  -0.2429 -0.6362 1450 PHE A CD1 
11015 C CD2 . PHE A 1450 ? 1.3185 1.6714 1.6179 0.1049  -0.2249 -0.6392 1450 PHE A CD2 
11016 C CE1 . PHE A 1450 ? 1.3541 1.7119 1.6906 0.0798  -0.2568 -0.6455 1450 PHE A CE1 
11017 C CE2 . PHE A 1450 ? 1.3110 1.6969 1.6553 0.1063  -0.2373 -0.6485 1450 PHE A CE2 
11018 C CZ  . PHE A 1450 ? 1.3248 1.7146 1.6889 0.0940  -0.2534 -0.6513 1450 PHE A CZ  
11019 N N   . THR A 1451 ? 1.3603 1.6182 1.5213 0.0947  -0.1694 -0.6017 1451 THR A N   
11020 C CA  . THR A 1451 ? 1.3266 1.5575 1.4465 0.0976  -0.1550 -0.5900 1451 THR A CA  
11021 C C   . THR A 1451 ? 1.3184 1.5260 1.4122 0.1119  -0.1651 -0.5872 1451 THR A C   
11022 O O   . THR A 1451 ? 1.3224 1.5029 1.3796 0.1166  -0.1574 -0.5769 1451 THR A O   
11023 C CB  . THR A 1451 ? 1.2782 1.5334 1.4029 0.1006  -0.1335 -0.5872 1451 THR A CB  
11024 O OG1 . THR A 1451 ? 1.2516 1.5154 1.3739 0.1159  -0.1351 -0.5888 1451 THR A OG1 
11025 C CG2 . THR A 1451 ? 1.2654 1.5591 1.4315 0.0912  -0.1260 -0.5947 1451 THR A CG2 
11026 N N   . ASP A 1452 ? 1.3081 1.5263 1.4211 0.1194  -0.1818 -0.5958 1452 ASP A N   
11027 C CA  . ASP A 1452 ? 1.3119 1.5081 1.4007 0.1328  -0.1908 -0.5931 1452 ASP A CA  
11028 C C   . ASP A 1452 ? 1.3322 1.5337 1.4386 0.1405  -0.2114 -0.6023 1452 ASP A C   
11029 O O   . ASP A 1452 ? 1.3136 1.5454 1.4493 0.1465  -0.2127 -0.6103 1452 ASP A O   
11030 C CB  . ASP A 1452 ? 1.2448 1.4488 1.3219 0.1423  -0.1760 -0.5878 1452 ASP A CB  
11031 C CG  . ASP A 1452 ? 1.1919 1.3651 1.2337 0.1522  -0.1793 -0.5797 1452 ASP A CG  
11032 O OD1 . ASP A 1452 ? 1.1877 1.3644 1.2323 0.1626  -0.1871 -0.5830 1452 ASP A OD1 
11033 O OD2 . ASP A 1452 ? 1.1609 1.3049 1.1721 0.1493  -0.1740 -0.5699 1452 ASP A OD2 
11034 N N   . TYR A 1453 ? 1.3714 1.5403 1.4563 0.1413  -0.2269 -0.6007 1453 TYR A N   
11035 C CA  . TYR A 1453 ? 1.3748 1.5394 1.4669 0.1497  -0.2476 -0.6074 1453 TYR A CA  
11036 C C   . TYR A 1453 ? 1.3705 1.5073 1.4293 0.1627  -0.2495 -0.6012 1453 TYR A C   
11037 O O   . TYR A 1453 ? 1.3816 1.4971 1.4088 0.1638  -0.2373 -0.5909 1453 TYR A O   
11038 C CB  . TYR A 1453 ? 1.3926 1.5400 1.4843 0.1409  -0.2659 -0.6105 1453 TYR A CB  
11039 C CG  . TYR A 1453 ? 1.4231 1.5219 1.4689 0.1426  -0.2722 -0.6030 1453 TYR A CG  
11040 C CD1 . TYR A 1453 ? 1.4684 1.5415 1.4819 0.1369  -0.2582 -0.5932 1453 TYR A CD1 
11041 C CD2 . TYR A 1453 ? 1.4467 1.5239 1.4796 0.1511  -0.2911 -0.6052 1453 TYR A CD2 
11042 C CE1 . TYR A 1453 ? 1.5087 1.5359 1.4784 0.1399  -0.2620 -0.5858 1453 TYR A CE1 
11043 C CE2 . TYR A 1453 ? 1.4909 1.5218 1.4792 0.1535  -0.2953 -0.5979 1453 TYR A CE2 
11044 C CZ  . TYR A 1453 ? 1.5013 1.5072 1.4580 0.1479  -0.2802 -0.5882 1453 TYR A CZ  
11045 O OH  . TYR A 1453 ? 1.4875 1.4462 1.3983 0.1512  -0.2823 -0.5806 1453 TYR A OH  
11046 N N   . GLN A 1454 ? 1.3746 1.5123 1.4415 0.1726  -0.2644 -0.6071 1454 GLN A N   
11047 C CA  . GLN A 1454 ? 1.3727 1.4820 1.4092 0.1839  -0.2686 -0.6018 1454 GLN A CA  
11048 C C   . GLN A 1454 ? 1.3743 1.4852 1.4241 0.1932  -0.2877 -0.6100 1454 GLN A C   
11049 O O   . GLN A 1454 ? 1.3502 1.4930 1.4346 0.1959  -0.2905 -0.6190 1454 GLN A O   
11050 C CB  . GLN A 1454 ? 1.3713 1.4895 1.3997 0.1897  -0.2512 -0.5960 1454 GLN A CB  
11051 C CG  . GLN A 1454 ? 1.3679 1.5264 1.4303 0.1912  -0.2442 -0.6037 1454 GLN A CG  
11052 C CD  . GLN A 1454 ? 1.3845 1.5472 1.4354 0.1983  -0.2320 -0.5990 1454 GLN A CD  
11053 O OE1 . GLN A 1454 ? 1.3923 1.5332 1.4207 0.2058  -0.2361 -0.5941 1454 GLN A OE1 
11054 N NE2 . GLN A 1454 ? 1.3845 1.5751 1.4501 0.1953  -0.2171 -0.6002 1454 GLN A NE2 
11055 N N   . ILE A 1455 ? 1.3749 1.4505 1.3967 0.1986  -0.3006 -0.6069 1455 ILE A N   
11056 C CA  . ILE A 1455 ? 1.3647 1.4374 1.3940 0.2089  -0.3181 -0.6133 1455 ILE A CA  
11057 C C   . ILE A 1455 ? 1.3494 1.4073 1.3575 0.2200  -0.3130 -0.6082 1455 ILE A C   
11058 O O   . ILE A 1455 ? 1.3550 1.3771 1.3279 0.2237  -0.3156 -0.6006 1455 ILE A O   
11059 C CB  . ILE A 1455 ? 1.4813 1.5243 1.4948 0.2084  -0.3394 -0.6145 1455 ILE A CB  
11060 C CG1 . ILE A 1455 ? 1.4851 1.5472 1.5270 0.1975  -0.3499 -0.6217 1455 ILE A CG1 
11061 C CG2 . ILE A 1455 ? 1.4854 1.5202 1.4993 0.2214  -0.3554 -0.6189 1455 ILE A CG2 
11062 C CD1 . ILE A 1455 ? 1.4941 1.5434 1.5206 0.1835  -0.3418 -0.6164 1455 ILE A CD1 
11063 N N   . LYS A 1456 ? 1.3450 1.4300 1.3740 0.2248  -0.3053 -0.6123 1456 LYS A N   
11064 C CA  . LYS A 1456 ? 1.3415 1.4160 1.3561 0.2346  -0.3031 -0.6095 1456 LYS A CA  
11065 C C   . LYS A 1456 ? 1.2893 1.3680 1.3205 0.2441  -0.3186 -0.6188 1456 LYS A C   
11066 O O   . LYS A 1456 ? 1.2537 1.3597 1.3183 0.2445  -0.3241 -0.6286 1456 LYS A O   
11067 C CB  . LYS A 1456 ? 1.3794 1.4758 1.3996 0.2336  -0.2842 -0.6071 1456 LYS A CB  
11068 C CG  . LYS A 1456 ? 1.4555 1.5390 1.4583 0.2415  -0.2818 -0.6030 1456 LYS A CG  
11069 C CD  . LYS A 1456 ? 1.4987 1.6034 1.5051 0.2395  -0.2645 -0.6002 1456 LYS A CD  
11070 C CE  . LYS A 1456 ? 1.5323 1.6174 1.5110 0.2429  -0.2588 -0.5899 1456 LYS A CE  
11071 N NZ  . LYS A 1456 ? 1.5484 1.6100 1.4987 0.2402  -0.2526 -0.5768 1456 LYS A NZ  
11072 N N   . ASP A 1457 ? 1.2957 1.3460 1.3026 0.2523  -0.3251 -0.6151 1457 ASP A N   
11073 C CA  . ASP A 1457 ? 1.3100 1.3592 1.3268 0.2628  -0.3379 -0.6224 1457 ASP A CA  
11074 C C   . ASP A 1457 ? 1.2703 1.3397 1.3198 0.2650  -0.3526 -0.6334 1457 ASP A C   
11075 O O   . ASP A 1457 ? 1.2539 1.3448 1.3283 0.2715  -0.3539 -0.6416 1457 ASP A O   
11076 C CB  . ASP A 1457 ? 1.3451 1.4066 1.3665 0.2671  -0.3267 -0.6236 1457 ASP A CB  
11077 C CG  . ASP A 1457 ? 1.4053 1.4423 1.3936 0.2673  -0.3177 -0.6125 1457 ASP A CG  
11078 O OD1 . ASP A 1457 ? 1.4567 1.4623 1.4175 0.2679  -0.3230 -0.6050 1457 ASP A OD1 
11079 O OD2 . ASP A 1457 ? 1.4036 1.4524 1.3928 0.2666  -0.3053 -0.6109 1457 ASP A OD2 
11080 N N   . GLY A 1458 ? 1.2496 1.3115 1.2985 0.2600  -0.3642 -0.6334 1458 GLY A N   
11081 C CA  . GLY A 1458 ? 1.2078 1.2858 1.2858 0.2630  -0.3817 -0.6427 1458 GLY A CA  
11082 C C   . GLY A 1458 ? 1.1596 1.2816 1.2790 0.2565  -0.3741 -0.6494 1458 GLY A C   
11083 O O   . GLY A 1458 ? 1.1480 1.2940 1.3007 0.2612  -0.3847 -0.6580 1458 GLY A O   
11084 N N   . HIS A 1459 ? 1.1235 1.2562 1.2408 0.2463  -0.3556 -0.6450 1459 HIS A N   
11085 C CA  . HIS A 1459 ? 1.1040 1.2773 1.2576 0.2393  -0.3449 -0.6503 1459 HIS A CA  
11086 C C   . HIS A 1459 ? 1.0725 1.2438 1.2180 0.2246  -0.3364 -0.6444 1459 HIS A C   
11087 O O   . HIS A 1459 ? 1.0567 1.2069 1.1711 0.2211  -0.3251 -0.6356 1459 HIS A O   
11088 C CB  . HIS A 1459 ? 1.1134 1.3059 1.2740 0.2432  -0.3264 -0.6517 1459 HIS A CB  
11089 C CG  . HIS A 1459 ? 1.1677 1.3636 1.3376 0.2570  -0.3322 -0.6584 1459 HIS A CG  
11090 N ND1 . HIS A 1459 ? 1.1875 1.4141 1.3950 0.2631  -0.3352 -0.6685 1459 HIS A ND1 
11091 C CD2 . HIS A 1459 ? 1.1938 1.3651 1.3396 0.2660  -0.3345 -0.6562 1459 HIS A CD2 
11092 C CE1 . HIS A 1459 ? 1.1909 1.4097 1.3952 0.2757  -0.3394 -0.6725 1459 HIS A CE1 
11093 N NE2 . HIS A 1459 ? 1.1942 1.3793 1.3613 0.2770  -0.3393 -0.6653 1459 HIS A NE2 
11094 N N   . VAL A 1460 ? 1.0811 1.2736 1.2543 0.2158  -0.3418 -0.6489 1460 VAL A N   
11095 C CA  . VAL A 1460 ? 1.1069 1.3030 1.2775 0.2008  -0.3301 -0.6444 1460 VAL A CA  
11096 C C   . VAL A 1460 ? 1.1425 1.3730 1.3358 0.1986  -0.3090 -0.6461 1460 VAL A C   
11097 O O   . VAL A 1460 ? 1.1590 1.4212 1.3864 0.2043  -0.3086 -0.6543 1460 VAL A O   
11098 C CB  . VAL A 1460 ? 1.1184 1.3245 1.3111 0.1903  -0.3441 -0.6485 1460 VAL A CB  
11099 C CG1 . VAL A 1460 ? 1.1154 1.3356 1.3163 0.1744  -0.3288 -0.6457 1460 VAL A CG1 
11100 C CG2 . VAL A 1460 ? 1.1494 1.3153 1.3106 0.1897  -0.3632 -0.6453 1460 VAL A CG2 
11101 N N   . ILE A 1461 ? 1.1350 1.3585 1.3082 0.1911  -0.2910 -0.6384 1461 ILE A N   
11102 C CA  . ILE A 1461 ? 1.1023 1.3526 1.2881 0.1907  -0.2703 -0.6388 1461 ILE A CA  
11103 C C   . ILE A 1461 ? 1.1056 1.3619 1.2892 0.1769  -0.2544 -0.6334 1461 ILE A C   
11104 O O   . ILE A 1461 ? 1.1051 1.3373 1.2556 0.1733  -0.2453 -0.6236 1461 ILE A O   
11105 C CB  . ILE A 1461 ? 1.0416 1.2781 1.2012 0.2001  -0.2618 -0.6341 1461 ILE A CB  
11106 C CG1 . ILE A 1461 ? 1.0282 1.2768 1.2047 0.2127  -0.2690 -0.6426 1461 ILE A CG1 
11107 C CG2 . ILE A 1461 ? 0.9982 1.2473 1.1521 0.1952  -0.2396 -0.6291 1461 ILE A CG2 
11108 C CD1 . ILE A 1461 ? 1.0349 1.2598 1.1817 0.2217  -0.2685 -0.6381 1461 ILE A CD1 
11109 N N   . LEU A 1462 ? 1.1052 1.3944 1.3250 0.1698  -0.2504 -0.6394 1462 LEU A N   
11110 C CA  . LEU A 1462 ? 1.1216 1.4180 1.3435 0.1555  -0.2364 -0.6351 1462 LEU A CA  
11111 C C   . LEU A 1462 ? 1.1461 1.4669 1.3759 0.1556  -0.2138 -0.6345 1462 LEU A C   
11112 O O   . LEU A 1462 ? 1.1425 1.4853 1.3904 0.1649  -0.2108 -0.6409 1462 LEU A O   
11113 C CB  . LEU A 1462 ? 1.0902 1.4054 1.3459 0.1450  -0.2465 -0.6411 1462 LEU A CB  
11114 C CG  . LEU A 1462 ? 0.9246 1.2113 1.1665 0.1426  -0.2692 -0.6407 1462 LEU A CG  
11115 C CD1 . LEU A 1462 ? 0.9333 1.2402 1.2094 0.1306  -0.2803 -0.6463 1462 LEU A CD1 
11116 C CD2 . LEU A 1462 ? 0.9396 1.1863 1.1362 0.1370  -0.2638 -0.6305 1462 LEU A CD2 
11117 N N   . GLN A 1463 ? 1.1496 1.4644 1.3636 0.1456  -0.1980 -0.6267 1463 GLN A N   
11118 C CA  . GLN A 1463 ? 1.1142 1.4477 1.3293 0.1451  -0.1762 -0.6246 1463 GLN A CA  
11119 C C   . GLN A 1463 ? 1.0831 1.4230 1.3035 0.1298  -0.1631 -0.6206 1463 GLN A C   
11120 O O   . GLN A 1463 ? 1.0689 1.3816 1.2657 0.1217  -0.1644 -0.6132 1463 GLN A O   
11121 C CB  . GLN A 1463 ? 1.1386 1.4484 1.3139 0.1518  -0.1684 -0.6153 1463 GLN A CB  
11122 C CG  . GLN A 1463 ? 1.1546 1.4654 1.3242 0.1659  -0.1722 -0.6182 1463 GLN A CG  
11123 C CD  . GLN A 1463 ? 1.1949 1.4888 1.3290 0.1694  -0.1613 -0.6077 1463 GLN A CD  
11124 O OE1 . GLN A 1463 ? 1.2004 1.4897 1.3237 0.1788  -0.1641 -0.6077 1463 GLN A OE1 
11125 N NE2 . GLN A 1463 ? 1.2226 1.5074 1.3391 0.1616  -0.1487 -0.5983 1463 GLN A NE2 
11126 N N   . LEU A 1464 ? 1.0718 1.4455 1.3213 0.1260  -0.1498 -0.6252 1464 LEU A N   
11127 C CA  . LEU A 1464 ? 1.0739 1.4552 1.3276 0.1116  -0.1337 -0.6208 1464 LEU A CA  
11128 C C   . LEU A 1464 ? 1.0892 1.4967 1.3517 0.1139  -0.1123 -0.6216 1464 LEU A C   
11129 O O   . LEU A 1464 ? 1.0490 1.4724 1.3203 0.1256  -0.1113 -0.6275 1464 LEU A O   
11130 C CB  . LEU A 1464 ? 1.0776 1.4755 1.3666 0.0990  -0.1416 -0.6262 1464 LEU A CB  
11131 C CG  . LEU A 1464 ? 1.0324 1.4519 1.3599 0.1029  -0.1610 -0.6369 1464 LEU A CG  
11132 C CD1 . LEU A 1464 ? 1.0029 1.4370 1.3416 0.1209  -0.1661 -0.6442 1464 LEU A CD1 
11133 C CD2 . LEU A 1464 ? 1.0358 1.4900 1.4072 0.0903  -0.1561 -0.6415 1464 LEU A CD2 
11134 N N   . ASN A 1465 ? 1.1488 1.5584 1.4067 0.1024  -0.0950 -0.6156 1465 ASN A N   
11135 C CA  . ASN A 1465 ? 1.1903 1.6210 1.4508 0.1035  -0.0730 -0.6150 1465 ASN A CA  
11136 C C   . ASN A 1465 ? 1.1952 1.6669 1.4997 0.1037  -0.0664 -0.6252 1465 ASN A C   
11137 O O   . ASN A 1465 ? 1.1805 1.6688 1.4856 0.1077  -0.0495 -0.6262 1465 ASN A O   
11138 C CB  . ASN A 1465 ? 1.2244 1.6422 1.4632 0.0916  -0.0552 -0.6044 1465 ASN A CB  
11139 C CG  . ASN A 1465 ? 1.2399 1.6170 1.4402 0.0891  -0.0614 -0.5941 1465 ASN A CG  
11140 O OD1 . ASN A 1465 ? 1.2169 1.5759 1.3826 0.0937  -0.0518 -0.5848 1465 ASN A OD1 
11141 N ND2 . ASN A 1465 ? 1.2498 1.6119 1.4552 0.0821  -0.0775 -0.5956 1465 ASN A ND2 
11142 N N   . SER A 1466 ? 1.2220 1.7099 1.5627 0.0996  -0.0794 -0.6324 1466 SER A N   
11143 C CA  . SER A 1466 ? 1.2486 1.7775 1.6352 0.0994  -0.0729 -0.6413 1466 SER A CA  
11144 C C   . SER A 1466 ? 1.2297 1.7736 1.6536 0.0995  -0.0937 -0.6491 1466 SER A C   
11145 O O   . SER A 1466 ? 1.2107 1.7333 1.6263 0.0941  -0.1116 -0.6470 1466 SER A O   
11146 C CB  . SER A 1466 ? 1.2876 1.8311 1.6861 0.0839  -0.0528 -0.6372 1466 SER A CB  
11147 O OG  . SER A 1466 ? 1.3086 1.8928 1.7564 0.0821  -0.0483 -0.6452 1466 SER A OG  
11148 N N   . ILE A 1467 ? 1.2367 1.8172 1.7012 0.1058  -0.0910 -0.6580 1467 ILE A N   
11149 C CA  . ILE A 1467 ? 1.2614 1.8623 1.7670 0.1058  -0.1095 -0.6650 1467 ILE A CA  
11150 C C   . ILE A 1467 ? 1.2964 1.9416 1.8520 0.0984  -0.0970 -0.6691 1467 ILE A C   
11151 O O   . ILE A 1467 ? 1.3271 2.0030 1.9191 0.1091  -0.0992 -0.6772 1467 ILE A O   
11152 C CB  . ILE A 1467 ? 1.2039 1.8053 1.7139 0.1251  -0.1250 -0.6725 1467 ILE A CB  
11153 C CG1 . ILE A 1467 ? 1.1492 1.7080 1.6112 0.1320  -0.1362 -0.6680 1467 ILE A CG1 
11154 C CG2 . ILE A 1467 ? 1.2230 1.8434 1.7733 0.1255  -0.1462 -0.6786 1467 ILE A CG2 
11155 C CD1 . ILE A 1467 ? 1.1168 1.6720 1.5827 0.1488  -0.1542 -0.6747 1467 ILE A CD1 
11156 N N   . PRO A 1468 ? 1.3261 1.9740 1.8839 0.0799  -0.0838 -0.6631 1468 PRO A N   
11157 C CA  . PRO A 1468 ? 1.3114 1.9986 1.9111 0.0700  -0.0664 -0.6646 1468 PRO A CA  
11158 C C   . PRO A 1468 ? 1.3164 2.0465 1.9683 0.0810  -0.0705 -0.6743 1468 PRO A C   
11159 O O   . PRO A 1468 ? 1.2808 2.0128 1.9481 0.0884  -0.0940 -0.6792 1468 PRO A O   
11160 C CB  . PRO A 1468 ? 1.3102 1.9914 1.9192 0.0479  -0.0752 -0.6600 1468 PRO A CB  
11161 C CG  . PRO A 1468 ? 1.3148 1.9454 1.8679 0.0446  -0.0816 -0.6523 1468 PRO A CG  
11162 C CD  . PRO A 1468 ? 1.3216 1.9324 1.8446 0.0657  -0.0893 -0.6544 1468 PRO A CD  
11163 N N   . SER A 1469 ? 1.3365 2.0995 2.0139 0.0830  -0.0474 -0.6767 1469 SER A N   
11164 C CA  . SER A 1469 ? 1.3551 2.1616 2.0854 0.0932  -0.0484 -0.6851 1469 SER A CA  
11165 C C   . SER A 1469 ? 1.3755 2.2161 2.1562 0.0757  -0.0496 -0.6843 1469 SER A C   
11166 O O   . SER A 1469 ? 1.4011 2.2781 2.2313 0.0815  -0.0582 -0.6902 1469 SER A O   
11167 C CB  . SER A 1469 ? 1.3535 2.1782 2.0858 0.1057  -0.0224 -0.6886 1469 SER A CB  
11168 O OG  . SER A 1469 ? 1.3568 2.1500 2.0429 0.1206  -0.0233 -0.6897 1469 SER A OG  
11169 N N   . SER A 1470 ? 1.3575 2.1858 2.1254 0.0542  -0.0412 -0.6766 1470 SER A N   
11170 C CA  . SER A 1470 ? 1.3535 2.2105 2.1658 0.0337  -0.0420 -0.6749 1470 SER A CA  
11171 C C   . SER A 1470 ? 1.3172 2.1913 2.1667 0.0354  -0.0719 -0.6801 1470 SER A C   
11172 O O   . SER A 1470 ? 1.3246 2.2438 2.2313 0.0315  -0.0730 -0.6833 1470 SER A O   
11173 C CB  . SER A 1470 ? 1.3857 2.2097 2.1654 0.0108  -0.0394 -0.6659 1470 SER A CB  
11174 O OG  . SER A 1470 ? 1.4135 2.1915 2.1487 0.0125  -0.0610 -0.6638 1470 SER A OG  
11175 N N   . ASP A 1471 ? 1.3118 2.1496 2.1281 0.0416  -0.0962 -0.6806 1471 ASP A N   
11176 C CA  . ASP A 1471 ? 1.3043 2.1504 2.1465 0.0441  -0.1271 -0.6850 1471 ASP A CA  
11177 C C   . ASP A 1471 ? 1.2229 2.0274 2.0197 0.0605  -0.1455 -0.6864 1471 ASP A C   
11178 O O   . ASP A 1471 ? 1.1874 1.9717 1.9486 0.0743  -0.1332 -0.6861 1471 ASP A O   
11179 C CB  . ASP A 1471 ? 1.3934 2.2368 2.2478 0.0184  -0.1411 -0.6812 1471 ASP A CB  
11180 C CG  . ASP A 1471 ? 1.4744 2.2674 2.2722 0.0031  -0.1362 -0.6733 1471 ASP A CG  
11181 O OD1 . ASP A 1471 ? 1.5148 2.3081 2.3208 -0.0206 -0.1337 -0.6691 1471 ASP A OD1 
11182 O OD2 . ASP A 1471 ? 1.4821 2.2351 2.2275 0.0146  -0.1347 -0.6711 1471 ASP A OD2 
11183 N N   . PHE A 1472 ? 1.1688 1.9608 1.9669 0.0588  -0.1751 -0.6877 1472 PHE A N   
11184 C CA  . PHE A 1472 ? 1.1041 1.8562 1.8601 0.0735  -0.1930 -0.6885 1472 PHE A CA  
11185 C C   . PHE A 1472 ? 1.0925 1.7934 1.7932 0.0620  -0.1967 -0.6814 1472 PHE A C   
11186 O O   . PHE A 1472 ? 1.0901 1.7839 1.7863 0.0410  -0.1912 -0.6763 1472 PHE A O   
11187 C CB  . PHE A 1472 ? 1.0955 1.8579 1.8778 0.0807  -0.2234 -0.6937 1472 PHE A CB  
11188 C CG  . PHE A 1472 ? 1.0829 1.8777 1.8988 0.1026  -0.2232 -0.7007 1472 PHE A CG  
11189 C CD1 . PHE A 1472 ? 1.0964 1.9415 1.9635 0.1034  -0.2061 -0.7036 1472 PHE A CD1 
11190 C CD2 . PHE A 1472 ? 1.0858 1.8597 1.8811 0.1229  -0.2385 -0.7041 1472 PHE A CD2 
11191 C CE1 . PHE A 1472 ? 1.1009 1.9748 1.9982 0.1253  -0.2046 -0.7101 1472 PHE A CE1 
11192 C CE2 . PHE A 1472 ? 1.0902 1.8912 1.9145 0.1440  -0.2377 -0.7106 1472 PHE A CE2 
11193 C CZ  . PHE A 1472 ? 1.0981 1.9490 1.9733 0.1457  -0.2208 -0.7138 1472 PHE A CZ  
11194 N N   . LEU A 1473 ? 1.0768 1.7409 1.7349 0.0762  -0.2061 -0.6809 1473 LEU A N   
11195 C CA  . LEU A 1473 ? 1.0990 1.7125 1.7032 0.0687  -0.2116 -0.6741 1473 LEU A CA  
11196 C C   . LEU A 1473 ? 1.1387 1.7275 1.7268 0.0795  -0.2398 -0.6765 1473 LEU A C   
11197 O O   . LEU A 1473 ? 1.1297 1.7208 1.7174 0.0993  -0.2446 -0.6808 1473 LEU A O   
11198 C CB  . LEU A 1473 ? 1.0504 1.6412 1.6125 0.0753  -0.1895 -0.6690 1473 LEU A CB  
11199 C CG  . LEU A 1473 ? 1.0643 1.6036 1.5707 0.0693  -0.1931 -0.6610 1473 LEU A CG  
11200 C CD1 . LEU A 1473 ? 1.0721 1.6014 1.5544 0.0598  -0.1671 -0.6533 1473 LEU A CD1 
11201 C CD2 . LEU A 1473 ? 1.0626 1.5718 1.5339 0.0876  -0.2045 -0.6610 1473 LEU A CD2 
11202 N N   . CYS A 1474 ? 1.1677 1.7308 1.7404 0.0662  -0.2582 -0.6739 1474 CYS A N   
11203 C CA  . CYS A 1474 ? 1.1482 1.6913 1.7110 0.0742  -0.2872 -0.6766 1474 CYS A CA  
11204 C C   . CYS A 1474 ? 1.1860 1.6724 1.6898 0.0717  -0.2952 -0.6705 1474 CYS A C   
11205 O O   . CYS A 1474 ? 1.2201 1.6845 1.7024 0.0545  -0.2908 -0.6652 1474 CYS A O   
11206 C CB  . CYS A 1474 ? 1.1168 1.6872 1.7237 0.0633  -0.3079 -0.6809 1474 CYS A CB  
11207 S SG  . CYS A 1474 ? 1.2380 1.8652 1.9067 0.0811  -0.3116 -0.6895 1474 CYS A SG  
11208 N N   . VAL A 1475 ? 1.2081 1.6700 1.6845 0.0894  -0.3052 -0.6709 1475 VAL A N   
11209 C CA  . VAL A 1475 ? 1.2528 1.6623 1.6774 0.0894  -0.3179 -0.6660 1475 VAL A CA  
11210 C C   . VAL A 1475 ? 1.3059 1.7146 1.7448 0.0901  -0.3484 -0.6709 1475 VAL A C   
11211 O O   . VAL A 1475 ? 1.2963 1.7391 1.7754 0.1000  -0.3583 -0.6775 1475 VAL A O   
11212 C CB  . VAL A 1475 ? 1.2136 1.5965 1.6007 0.1082  -0.3128 -0.6633 1475 VAL A CB  
11213 C CG1 . VAL A 1475 ? 1.2019 1.6118 1.6175 0.1265  -0.3183 -0.6703 1475 VAL A CG1 
11214 C CG2 . VAL A 1475 ? 1.2204 1.5534 1.5611 0.1103  -0.3297 -0.6592 1475 VAL A CG2 
11215 N N   . ARG A 1476 ? 1.3414 1.7112 1.7472 0.0799  -0.3632 -0.6676 1476 ARG A N   
11216 C CA  . ARG A 1476 ? 1.3368 1.6938 1.7415 0.0831  -0.3937 -0.6712 1476 ARG A CA  
11217 C C   . ARG A 1476 ? 1.3033 1.5996 1.6448 0.0860  -0.4013 -0.6656 1476 ARG A C   
11218 O O   . ARG A 1476 ? 1.2772 1.5432 1.5815 0.0784  -0.3860 -0.6589 1476 ARG A O   
11219 C CB  . ARG A 1476 ? 1.3846 1.7661 1.8267 0.0649  -0.4099 -0.6752 1476 ARG A CB  
11220 C CG  . ARG A 1476 ? 1.4551 1.8333 1.8943 0.0412  -0.3963 -0.6714 1476 ARG A CG  
11221 C CD  . ARG A 1476 ? 1.5108 1.9428 2.0029 0.0334  -0.3771 -0.6734 1476 ARG A CD  
11222 N NE  . ARG A 1476 ? 1.5925 2.0094 2.0614 0.0206  -0.3512 -0.6670 1476 ARG A NE  
11223 C CZ  . ARG A 1476 ? 1.6421 2.0933 2.1435 0.0090  -0.3308 -0.6665 1476 ARG A CZ  
11224 N NH1 . ARG A 1476 ? 1.6433 2.1495 2.2057 0.0078  -0.3320 -0.6721 1476 ARG A NH1 
11225 N NH2 . ARG A 1476 ? 1.6550 2.0846 2.1269 -0.0009 -0.3084 -0.6598 1476 ARG A NH2 
11226 N N   . PHE A 1477 ? 1.2985 1.5774 1.6277 0.0987  -0.4235 -0.6679 1477 PHE A N   
11227 C CA  . PHE A 1477 ? 1.3045 1.5263 1.5747 0.1038  -0.4313 -0.6628 1477 PHE A CA  
11228 C C   . PHE A 1477 ? 1.3236 1.5332 1.5899 0.1154  -0.4601 -0.6667 1477 PHE A C   
11229 O O   . PHE A 1477 ? 1.3188 1.5627 1.6237 0.1266  -0.4694 -0.6724 1477 PHE A O   
11230 C CB  . PHE A 1477 ? 1.2669 1.4695 1.5044 0.1162  -0.4090 -0.6567 1477 PHE A CB  
11231 C CG  . PHE A 1477 ? 1.2551 1.4772 1.5092 0.1363  -0.4079 -0.6600 1477 PHE A CG  
11232 C CD1 . PHE A 1477 ? 1.2679 1.4600 1.4930 0.1515  -0.4206 -0.6590 1477 PHE A CD1 
11233 C CD2 . PHE A 1477 ? 1.2309 1.4991 1.5273 0.1399  -0.3935 -0.6640 1477 PHE A CD2 
11234 C CE1 . PHE A 1477 ? 1.2559 1.4632 1.4946 0.1692  -0.4194 -0.6621 1477 PHE A CE1 
11235 C CE2 . PHE A 1477 ? 1.2276 1.5102 1.5362 0.1581  -0.3923 -0.6674 1477 PHE A CE2 
11236 C CZ  . PHE A 1477 ? 1.2343 1.4861 1.5141 0.1724  -0.4055 -0.6665 1477 PHE A CZ  
11237 N N   . ARG A 1478 ? 1.3273 1.4870 1.5458 0.1133  -0.4738 -0.6633 1478 ARG A N   
11238 C CA  . ARG A 1478 ? 1.3381 1.4831 1.5500 0.1213  -0.5030 -0.6667 1478 ARG A CA  
11239 C C   . ARG A 1478 ? 1.3417 1.4555 1.5176 0.1420  -0.5027 -0.6635 1478 ARG A C   
11240 O O   . ARG A 1478 ? 1.2780 1.3690 1.4217 0.1465  -0.4822 -0.6572 1478 ARG A O   
11241 C CB  . ARG A 1478 ? 1.3724 1.4817 1.5546 0.1053  -0.5207 -0.6660 1478 ARG A CB  
11242 C CG  . ARG A 1478 ? 1.3822 1.5117 1.5882 0.0821  -0.5152 -0.6672 1478 ARG A CG  
11243 C CD  . ARG A 1478 ? 1.4577 1.5472 1.6302 0.0664  -0.5352 -0.6671 1478 ARG A CD  
11244 N NE  . ARG A 1478 ? 1.4803 1.5171 1.5945 0.0608  -0.5197 -0.6600 1478 ARG A NE  
11245 C CZ  . ARG A 1478 ? 1.5028 1.5292 1.6085 0.0406  -0.5106 -0.6582 1478 ARG A CZ  
11246 N NH1 . ARG A 1478 ? 1.5239 1.5899 1.6766 0.0229  -0.5155 -0.6630 1478 ARG A NH1 
11247 N NH2 . ARG A 1478 ? 1.5113 1.4879 1.5622 0.0383  -0.4961 -0.6513 1478 ARG A NH2 
11248 N N   . ILE A 1479 ? 1.4343 1.5471 1.6159 0.1542  -0.5260 -0.6673 1479 ILE A N   
11249 C CA  . ILE A 1479 ? 1.5167 1.6055 1.6716 0.1747  -0.5267 -0.6650 1479 ILE A CA  
11250 C C   . ILE A 1479 ? 1.6140 1.6664 1.7389 0.1814  -0.5549 -0.6653 1479 ILE A C   
11251 O O   . ILE A 1479 ? 1.6448 1.7145 1.7955 0.1789  -0.5791 -0.6707 1479 ILE A O   
11252 C CB  . ILE A 1479 ? 1.5036 1.6364 1.7034 0.1893  -0.5219 -0.6699 1479 ILE A CB  
11253 C CG1 . ILE A 1479 ? 1.5149 1.6857 1.7635 0.1897  -0.5449 -0.6774 1479 ILE A CG1 
11254 C CG2 . ILE A 1479 ? 1.4953 1.6609 1.7199 0.1844  -0.4934 -0.6695 1479 ILE A CG2 
11255 C CD1 . ILE A 1479 ? 1.4760 1.6983 1.7773 0.2004  -0.5359 -0.6827 1479 ILE A CD1 
11256 N N   . PHE A 1480 ? 1.6808 1.6835 1.7515 0.1902  -0.5519 -0.6591 1480 PHE A N   
11257 C CA  . PHE A 1480 ? 1.8280 1.7907 1.8637 0.1972  -0.5771 -0.6587 1480 PHE A CA  
11258 C C   . PHE A 1480 ? 1.7583 1.7086 1.7825 0.2188  -0.5813 -0.6577 1480 PHE A C   
11259 O O   . PHE A 1480 ? 1.7454 1.6755 1.7430 0.2270  -0.5629 -0.6521 1480 PHE A O   
11260 C CB  . PHE A 1480 ? 2.0997 2.0057 2.0754 0.1881  -0.5775 -0.6527 1480 PHE A CB  
11261 C CG  . PHE A 1480 ? 2.2071 2.1018 2.1627 0.1799  -0.5480 -0.6463 1480 PHE A CG  
11262 C CD1 . PHE A 1480 ? 2.1925 2.0872 2.1401 0.1908  -0.5238 -0.6409 1480 PHE A CD1 
11263 C CD2 . PHE A 1480 ? 2.2567 2.1377 2.1986 0.1611  -0.5453 -0.6452 1480 PHE A CD2 
11264 C CE1 . PHE A 1480 ? 2.1710 2.0558 2.0998 0.1841  -0.4979 -0.6342 1480 PHE A CE1 
11265 C CE2 . PHE A 1480 ? 2.2290 2.0975 2.1505 0.1547  -0.5183 -0.6386 1480 PHE A CE2 
11266 C CZ  . PHE A 1480 ? 2.1904 2.0620 2.1061 0.1668  -0.4948 -0.6328 1480 PHE A CZ  
11267 N N   . GLU A 1481 ? 1.7605 1.7220 1.8041 0.2273  -0.6065 -0.6628 1481 GLU A N   
11268 C CA  . GLU A 1481 ? 1.7440 1.6941 1.7790 0.2481  -0.6132 -0.6624 1481 GLU A CA  
11269 C C   . GLU A 1481 ? 1.7596 1.6501 1.7302 0.2550  -0.6075 -0.6544 1481 GLU A C   
11270 O O   . GLU A 1481 ? 1.8076 1.6596 1.7424 0.2588  -0.6273 -0.6528 1481 GLU A O   
11271 C CB  . GLU A 1481 ? 1.7623 1.7241 1.8185 0.2552  -0.6454 -0.6679 1481 GLU A CB  
11272 C CG  . GLU A 1481 ? 2.1487 2.1751 2.2754 0.2546  -0.6506 -0.6755 1481 GLU A CG  
11273 C CD  . GLU A 1481 ? 2.1536 2.1927 2.3022 0.2660  -0.6817 -0.6799 1481 GLU A CD  
11274 O OE1 . GLU A 1481 ? 2.1802 2.1770 2.2881 0.2754  -0.6997 -0.6772 1481 GLU A OE1 
11275 O OE2 . GLU A 1481 ? 2.1287 2.2207 2.3355 0.2661  -0.6878 -0.6855 1481 GLU A OE2 
11276 N N   . LEU A 1482 ? 1.7224 1.6061 1.6787 0.2570  -0.5805 -0.6492 1482 LEU A N   
11277 C CA  . LEU A 1482 ? 1.7171 1.5478 1.6153 0.2624  -0.5720 -0.6406 1482 LEU A CA  
11278 C C   . LEU A 1482 ? 1.7016 1.5012 1.5744 0.2783  -0.5902 -0.6397 1482 LEU A C   
11279 O O   . LEU A 1482 ? 1.7325 1.4825 1.5544 0.2800  -0.5965 -0.6343 1482 LEU A O   
11280 C CB  . LEU A 1482 ? 1.7045 1.5411 1.6001 0.2646  -0.5416 -0.6353 1482 LEU A CB  
11281 C CG  . LEU A 1482 ? 1.7454 1.5331 1.5873 0.2723  -0.5311 -0.6258 1482 LEU A CG  
11282 C CD1 . LEU A 1482 ? 1.7238 1.5098 1.5531 0.2650  -0.5027 -0.6186 1482 LEU A CD1 
11283 C CD2 . LEU A 1482 ? 1.7495 1.5339 1.5922 0.2890  -0.5328 -0.6257 1482 LEU A CD2 
11284 N N   . PHE A 1483 ? 1.6403 1.4669 1.5465 0.2906  -0.5979 -0.6447 1483 PHE A N   
11285 C CA  . PHE A 1483 ? 1.6477 1.4483 1.5347 0.3060  -0.6181 -0.6446 1483 PHE A CA  
11286 C C   . PHE A 1483 ? 1.6741 1.5154 1.6109 0.3154  -0.6352 -0.6527 1483 PHE A C   
11287 O O   . PHE A 1483 ? 1.6558 1.5466 1.6430 0.3098  -0.6304 -0.6585 1483 PHE A O   
11288 C CB  . PHE A 1483 ? 1.6016 1.3675 1.4517 0.3178  -0.6034 -0.6375 1483 PHE A CB  
11289 C CG  . PHE A 1483 ? 1.5257 1.3206 1.4020 0.3209  -0.5792 -0.6378 1483 PHE A CG  
11290 C CD1 . PHE A 1483 ? 1.4799 1.3278 1.4117 0.3202  -0.5764 -0.6455 1483 PHE A CD1 
11291 C CD2 . PHE A 1483 ? 1.5088 1.2774 1.3537 0.3248  -0.5595 -0.6302 1483 PHE A CD2 
11292 C CE1 . PHE A 1483 ? 1.4085 1.2800 1.3605 0.3231  -0.5546 -0.6462 1483 PHE A CE1 
11293 C CE2 . PHE A 1483 ? 1.4500 1.2440 1.3174 0.3269  -0.5392 -0.6308 1483 PHE A CE2 
11294 C CZ  . PHE A 1483 ? 1.4005 1.2449 1.3201 0.3260  -0.5369 -0.6391 1483 PHE A CZ  
11295 N N   . GLU A 1484 ? 1.7557 1.5758 1.6782 0.3301  -0.6552 -0.6528 1484 GLU A N   
11296 C CA  . GLU A 1484 ? 1.8042 1.6597 1.7711 0.3398  -0.6752 -0.6599 1484 GLU A CA  
11297 C C   . GLU A 1484 ? 1.7773 1.6502 1.7653 0.3543  -0.6609 -0.6614 1484 GLU A C   
11298 O O   . GLU A 1484 ? 1.8016 1.6388 1.7557 0.3661  -0.6575 -0.6571 1484 GLU A O   
11299 C CB  . GLU A 1484 ? 1.9344 1.7570 1.8736 0.3489  -0.7059 -0.6589 1484 GLU A CB  
11300 C CG  . GLU A 1484 ? 2.0572 1.8464 1.9581 0.3351  -0.7196 -0.6563 1484 GLU A CG  
11301 C CD  . GLU A 1484 ? 2.1408 1.8753 1.9794 0.3317  -0.7020 -0.6479 1484 GLU A CD  
11302 O OE1 . GLU A 1484 ? 2.1462 1.8716 1.9741 0.3391  -0.6798 -0.6437 1484 GLU A OE1 
11303 O OE2 . GLU A 1484 ? 2.1861 1.8866 1.9864 0.3216  -0.7103 -0.6453 1484 GLU A OE2 
11304 N N   . VAL A 1485 ? 1.7316 1.6572 1.7735 0.3526  -0.6510 -0.6675 1485 VAL A N   
11305 C CA  . VAL A 1485 ? 1.6661 1.6091 1.7295 0.3667  -0.6380 -0.6702 1485 VAL A CA  
11306 C C   . VAL A 1485 ? 1.6396 1.6092 1.7404 0.3813  -0.6588 -0.6762 1485 VAL A C   
11307 O O   . VAL A 1485 ? 1.6199 1.6156 1.7493 0.3766  -0.6775 -0.6797 1485 VAL A O   
11308 C CB  . VAL A 1485 ? 1.8609 1.8432 1.9573 0.3585  -0.6104 -0.6731 1485 VAL A CB  
11309 C CG1 . VAL A 1485 ? 1.8436 1.8002 1.9033 0.3471  -0.5876 -0.6664 1485 VAL A CG1 
11310 C CG2 . VAL A 1485 ? 1.8558 1.8884 2.0023 0.3476  -0.6141 -0.6788 1485 VAL A CG2 
11311 N N   . GLY A 1486 ? 1.5864 1.5493 1.6869 0.3988  -0.6549 -0.6772 1486 GLY A N   
11312 C CA  . GLY A 1486 ? 1.5830 1.5636 1.7125 0.4170  -0.6734 -0.6818 1486 GLY A CA  
11313 C C   . GLY A 1486 ? 1.5263 1.5687 1.7195 0.4165  -0.6678 -0.6892 1486 GLY A C   
11314 O O   . GLY A 1486 ? 1.5395 1.6119 1.7566 0.3999  -0.6618 -0.6908 1486 GLY A O   
11315 N N   . PHE A 1487 ? 1.4947 1.5554 1.7153 0.4349  -0.6692 -0.6936 1487 PHE A N   
11316 C CA  . PHE A 1487 ? 1.4695 1.5884 1.7500 0.4361  -0.6604 -0.7005 1487 PHE A CA  
11317 C C   . PHE A 1487 ? 1.3981 1.5237 1.6754 0.4231  -0.6293 -0.7008 1487 PHE A C   
11318 O O   . PHE A 1487 ? 1.3823 1.4846 1.6356 0.4291  -0.6127 -0.6999 1487 PHE A O   
11319 C CB  . PHE A 1487 ? 1.5288 1.6567 1.8295 0.4601  -0.6626 -0.7045 1487 PHE A CB  
11320 C CG  . PHE A 1487 ? 1.6025 1.6844 1.8655 0.4767  -0.6820 -0.7007 1487 PHE A CG  
11321 C CD1 . PHE A 1487 ? 1.6365 1.7315 1.9238 0.4965  -0.7031 -0.7029 1487 PHE A CD1 
11322 C CD2 . PHE A 1487 ? 1.6289 1.6544 1.8321 0.4731  -0.6786 -0.6943 1487 PHE A CD2 
11323 C CE1 . PHE A 1487 ? 1.6791 1.7300 1.9299 0.5125  -0.7207 -0.6989 1487 PHE A CE1 
11324 C CE2 . PHE A 1487 ? 1.6717 1.6535 1.8388 0.4882  -0.6953 -0.6904 1487 PHE A CE2 
11325 C CZ  . PHE A 1487 ? 1.6955 1.6889 1.8853 0.5080  -0.7166 -0.6927 1487 PHE A CZ  
11326 N N   . LEU A 1488 ? 1.3574 1.5127 1.6565 0.4044  -0.6218 -0.7015 1488 LEU A N   
11327 C CA  . LEU A 1488 ? 1.3162 1.4740 1.6069 0.3913  -0.5932 -0.7006 1488 LEU A CA  
11328 C C   . LEU A 1488 ? 1.3009 1.5063 1.6393 0.3954  -0.5757 -0.7073 1488 LEU A C   
11329 O O   . LEU A 1488 ? 1.3059 1.5537 1.6922 0.3990  -0.5846 -0.7119 1488 LEU A O   
11330 C CB  . LEU A 1488 ? 1.2954 1.4493 1.5725 0.3685  -0.5905 -0.6964 1488 LEU A CB  
11331 C CG  . LEU A 1488 ? 1.2731 1.4694 1.5893 0.3515  -0.5900 -0.6989 1488 LEU A CG  
11332 C CD1 . LEU A 1488 ? 1.2430 1.4953 1.6159 0.3537  -0.5756 -0.7054 1488 LEU A CD1 
11333 C CD2 . LEU A 1488 ? 1.2690 1.4451 1.5537 0.3318  -0.5753 -0.6935 1488 LEU A CD2 
11334 N N   . SER A 1489 ? 1.2547 1.4525 1.5792 0.3954  -0.5512 -0.7076 1489 SER A N   
11335 C CA  . SER A 1489 ? 1.1877 1.4262 1.5496 0.3966  -0.5301 -0.7137 1489 SER A CA  
11336 C C   . SER A 1489 ? 1.1334 1.3898 1.5000 0.3749  -0.5130 -0.7117 1489 SER A C   
11337 O O   . SER A 1489 ? 1.1467 1.3744 1.4777 0.3616  -0.5129 -0.7053 1489 SER A O   
11338 C CB  . SER A 1489 ? 1.1332 1.3518 1.4753 0.4084  -0.5144 -0.7156 1489 SER A CB  
11339 O OG  . SER A 1489 ? 1.0984 1.3098 1.4197 0.3946  -0.4917 -0.7130 1489 SER A OG  
11340 N N   . PRO A 1490 ? 1.0966 1.3995 1.5065 0.3718  -0.4983 -0.7169 1490 PRO A N   
11341 C CA  . PRO A 1490 ? 1.0451 1.3714 1.4675 0.3519  -0.4835 -0.7154 1490 PRO A CA  
11342 C C   . PRO A 1490 ? 1.0578 1.3663 1.4494 0.3446  -0.4598 -0.7126 1490 PRO A C   
11343 O O   . PRO A 1490 ? 1.0260 1.3222 1.4037 0.3549  -0.4488 -0.7146 1490 PRO A O   
11344 C CB  . PRO A 1490 ? 1.0219 1.4025 1.5009 0.3558  -0.4747 -0.7223 1490 PRO A CB  
11345 C CG  . PRO A 1490 ? 1.0534 1.4397 1.5510 0.3777  -0.4881 -0.7269 1490 PRO A CG  
11346 C CD  . PRO A 1490 ? 1.0744 1.4093 1.5232 0.3883  -0.4937 -0.7243 1490 PRO A CD  
11347 N N   . ALA A 1491 ? 1.1019 1.4084 1.4821 0.3260  -0.4527 -0.7077 1491 ALA A N   
11348 C CA  . ALA A 1491 ? 1.0970 1.3977 1.4571 0.3167  -0.4287 -0.7046 1491 ALA A CA  
11349 C C   . ALA A 1491 ? 1.1204 1.4690 1.5235 0.3118  -0.4121 -0.7096 1491 ALA A C   
11350 O O   . ALA A 1491 ? 1.0918 1.4745 1.5377 0.3192  -0.4182 -0.7157 1491 ALA A O   
11351 C CB  . ALA A 1491 ? 1.0735 1.3481 1.4004 0.3006  -0.4288 -0.6964 1491 ALA A CB  
11352 N N   . THR A 1492 ? 1.1407 1.4918 1.5322 0.2994  -0.3911 -0.7065 1492 THR A N   
11353 C CA  . THR A 1492 ? 1.1131 1.5025 1.5353 0.2964  -0.3704 -0.7108 1492 THR A CA  
11354 C C   . THR A 1492 ? 1.1412 1.5393 1.5607 0.2771  -0.3565 -0.7057 1492 THR A C   
11355 O O   . THR A 1492 ? 1.1526 1.5207 1.5351 0.2676  -0.3549 -0.6983 1492 THR A O   
11356 C CB  . THR A 1492 ? 1.0519 1.4330 1.4578 0.3056  -0.3542 -0.7132 1492 THR A CB  
11357 O OG1 . THR A 1492 ? 0.9112 1.2483 1.2701 0.3062  -0.3583 -0.7073 1492 THR A OG1 
11358 C CG2 . THR A 1492 ? 0.9101 1.3033 1.3389 0.3241  -0.3597 -0.7212 1492 THR A CG2 
11359 N N   . PHE A 1493 ? 1.1052 1.5444 1.5644 0.2718  -0.3458 -0.7095 1493 PHE A N   
11360 C CA  . PHE A 1493 ? 1.0657 1.5167 1.5269 0.2535  -0.3312 -0.7052 1493 PHE A CA  
11361 C C   . PHE A 1493 ? 1.0971 1.5710 1.5688 0.2547  -0.3059 -0.7081 1493 PHE A C   
11362 O O   . PHE A 1493 ? 1.0949 1.6071 1.6079 0.2584  -0.2990 -0.7141 1493 PHE A O   
11363 C CB  . PHE A 1493 ? 0.9835 1.4651 1.4847 0.2437  -0.3402 -0.7067 1493 PHE A CB  
11364 C CG  . PHE A 1493 ? 0.9072 1.4064 1.4172 0.2257  -0.3224 -0.7034 1493 PHE A CG  
11365 C CD1 . PHE A 1493 ? 0.8731 1.3462 1.3437 0.2162  -0.3087 -0.6965 1493 PHE A CD1 
11366 C CD2 . PHE A 1493 ? 0.8878 1.4295 1.4457 0.2182  -0.3197 -0.7066 1493 PHE A CD2 
11367 C CE1 . PHE A 1493 ? 0.8687 1.3553 1.3450 0.2003  -0.2922 -0.6930 1493 PHE A CE1 
11368 C CE2 . PHE A 1493 ? 0.8675 1.4234 1.4323 0.2010  -0.3029 -0.7032 1493 PHE A CE2 
11369 C CZ  . PHE A 1493 ? 0.8664 1.3933 1.3889 0.1922  -0.2891 -0.6964 1493 PHE A CZ  
11370 N N   . THR A 1494 ? 1.1232 1.5738 1.5572 0.2516  -0.2921 -0.7034 1494 THR A N   
11371 C CA  . THR A 1494 ? 1.1082 1.5742 1.5431 0.2525  -0.2684 -0.7054 1494 THR A CA  
11372 C C   . THR A 1494 ? 0.9695 1.4386 1.3934 0.2351  -0.2513 -0.6985 1494 THR A C   
11373 O O   . THR A 1494 ? 0.8512 1.2960 1.2493 0.2249  -0.2563 -0.6907 1494 THR A O   
11374 C CB  . THR A 1494 ? 1.0814 1.5213 1.4847 0.2646  -0.2667 -0.7066 1494 THR A CB  
11375 O OG1 . THR A 1494 ? 1.0729 1.5141 1.4588 0.2603  -0.2452 -0.7048 1494 THR A OG1 
11376 C CG2 . THR A 1494 ? 1.0671 1.4655 1.4334 0.2648  -0.2832 -0.7001 1494 THR A CG2 
11377 N N   . VAL A 1495 ? 0.9598 1.4585 1.4040 0.2324  -0.2312 -0.7014 1495 VAL A N   
11378 C CA  . VAL A 1495 ? 1.0318 1.5339 1.4650 0.2175  -0.2130 -0.6950 1495 VAL A CA  
11379 C C   . VAL A 1495 ? 1.0685 1.5880 1.5031 0.2208  -0.1896 -0.6981 1495 VAL A C   
11380 O O   . VAL A 1495 ? 1.1204 1.6721 1.5895 0.2256  -0.1811 -0.7051 1495 VAL A O   
11381 C CB  . VAL A 1495 ? 0.8383 1.3611 1.3000 0.2026  -0.2137 -0.6930 1495 VAL A CB  
11382 C CG1 . VAL A 1495 ? 0.9542 1.5096 1.4637 0.2086  -0.2230 -0.7009 1495 VAL A CG1 
11383 C CG2 . VAL A 1495 ? 0.8347 1.3736 1.2979 0.1912  -0.1892 -0.6896 1495 VAL A CG2 
11384 N N   . TYR A 1496 ? 1.1018 1.5993 1.4976 0.2186  -0.1797 -0.6924 1496 TYR A N   
11385 C CA  . TYR A 1496 ? 1.0859 1.5921 1.4716 0.2205  -0.1587 -0.6939 1496 TYR A CA  
11386 C C   . TYR A 1496 ? 1.0899 1.5895 1.4528 0.2064  -0.1443 -0.6840 1496 TYR A C   
11387 O O   . TYR A 1496 ? 1.0727 1.5561 1.4233 0.1967  -0.1510 -0.6761 1496 TYR A O   
11388 C CB  . TYR A 1496 ? 1.0703 1.5540 1.4272 0.2320  -0.1622 -0.6960 1496 TYR A CB  
11389 C CG  . TYR A 1496 ? 1.0896 1.5376 1.4107 0.2296  -0.1748 -0.6876 1496 TYR A CG  
11390 C CD1 . TYR A 1496 ? 1.0736 1.5100 1.3809 0.2174  -0.1751 -0.6777 1496 TYR A CD1 
11391 C CD2 . TYR A 1496 ? 1.0971 1.5218 1.3971 0.2396  -0.1851 -0.6892 1496 TYR A CD2 
11392 C CE1 . TYR A 1496 ? 1.0614 1.4662 1.3368 0.2161  -0.1846 -0.6698 1496 TYR A CE1 
11393 C CE2 . TYR A 1496 ? 1.0911 1.4845 1.3596 0.2373  -0.1949 -0.6807 1496 TYR A CE2 
11394 C CZ  . TYR A 1496 ? 1.0772 1.4617 1.3343 0.2259  -0.1943 -0.6710 1496 TYR A CZ  
11395 O OH  . TYR A 1496 ? 1.0757 1.4298 1.3023 0.2238  -0.2022 -0.6619 1496 TYR A OH  
11396 N N   . GLU A 1497 ? 1.0936 1.6040 1.4493 0.2060  -0.1244 -0.6845 1497 GLU A N   
11397 C CA  . GLU A 1497 ? 1.0748 1.5792 1.4064 0.1950  -0.1090 -0.6752 1497 GLU A CA  
11398 C C   . GLU A 1497 ? 1.0655 1.5418 1.3542 0.1978  -0.1103 -0.6690 1497 GLU A C   
11399 O O   . GLU A 1497 ? 1.0360 1.5087 1.3143 0.2073  -0.1104 -0.6740 1497 GLU A O   
11400 C CB  . GLU A 1497 ? 1.0537 1.5848 1.3991 0.1940  -0.0870 -0.6792 1497 GLU A CB  
11401 C CG  . GLU A 1497 ? 1.0380 1.5730 1.3749 0.1806  -0.0701 -0.6707 1497 GLU A CG  
11402 C CD  . GLU A 1497 ? 1.0192 1.5858 1.3824 0.1792  -0.0505 -0.6759 1497 GLU A CD  
11403 O OE1 . GLU A 1497 ? 0.9759 1.5622 1.3670 0.1886  -0.0513 -0.6859 1497 GLU A OE1 
11404 O OE2 . GLU A 1497 ? 1.0436 1.6147 1.3993 0.1693  -0.0336 -0.6697 1497 GLU A OE2 
11405 N N   . TYR A 1498 ? 1.0996 1.5564 1.3636 0.1893  -0.1105 -0.6578 1498 TYR A N   
11406 C CA  . TYR A 1498 ? 1.1264 1.5570 1.3531 0.1923  -0.1144 -0.6506 1498 TYR A CA  
11407 C C   . TYR A 1498 ? 1.1138 1.5495 1.3248 0.1973  -0.1030 -0.6527 1498 TYR A C   
11408 O O   . TYR A 1498 ? 1.0943 1.5193 1.2929 0.2053  -0.1108 -0.6558 1498 TYR A O   
11409 C CB  . TYR A 1498 ? 1.1467 1.5581 1.3487 0.1830  -0.1119 -0.6373 1498 TYR A CB  
11410 C CG  . TYR A 1498 ? 1.1804 1.5641 1.3496 0.1873  -0.1204 -0.6296 1498 TYR A CG  
11411 C CD1 . TYR A 1498 ? 1.2129 1.5810 1.3814 0.1940  -0.1381 -0.6324 1498 TYR A CD1 
11412 C CD2 . TYR A 1498 ? 1.1931 1.5668 1.3327 0.1850  -0.1106 -0.6189 1498 TYR A CD2 
11413 C CE1 . TYR A 1498 ? 1.2295 1.5735 1.3699 0.1976  -0.1447 -0.6251 1498 TYR A CE1 
11414 C CE2 . TYR A 1498 ? 1.2136 1.5652 1.3270 0.1890  -0.1179 -0.6114 1498 TYR A CE2 
11415 C CZ  . TYR A 1498 ? 1.2360 1.5729 1.3503 0.1950  -0.1345 -0.6146 1498 TYR A CZ  
11416 O OH  . TYR A 1498 ? 1.2669 1.5822 1.3562 0.1988  -0.1409 -0.6068 1498 TYR A OH  
11417 N N   . HIS A 1499 ? 1.1031 1.5541 1.3137 0.1919  -0.0847 -0.6511 1499 HIS A N   
11418 C CA  . HIS A 1499 ? 1.0818 1.5362 1.2734 0.1952  -0.0734 -0.6521 1499 HIS A CA  
11419 C C   . HIS A 1499 ? 1.1274 1.5983 1.3364 0.2039  -0.0698 -0.6657 1499 HIS A C   
11420 O O   . HIS A 1499 ? 1.1663 1.6356 1.3568 0.2079  -0.0639 -0.6685 1499 HIS A O   
11421 C CB  . HIS A 1499 ? 1.0178 1.4787 1.1972 0.1868  -0.0552 -0.6441 1499 HIS A CB  
11422 C CG  . HIS A 1499 ? 0.9705 1.4115 1.1243 0.1810  -0.0570 -0.6302 1499 HIS A CG  
11423 N ND1 . HIS A 1499 ? 0.9765 1.4175 1.1277 0.1716  -0.0466 -0.6217 1499 HIS A ND1 
11424 C CD2 . HIS A 1499 ? 0.9734 1.3931 1.1030 0.1836  -0.0676 -0.6230 1499 HIS A CD2 
11425 C CE1 . HIS A 1499 ? 0.9939 1.4133 1.1189 0.1697  -0.0504 -0.6099 1499 HIS A CE1 
11426 N NE2 . HIS A 1499 ? 0.9872 1.3946 1.0998 0.1770  -0.0629 -0.6102 1499 HIS A NE2 
11427 N N   . ARG A 1500 ? 1.1133 1.5996 1.3568 0.2068  -0.0734 -0.6739 1500 ARG A N   
11428 C CA  . ARG A 1500 ? 1.0943 1.5931 1.3544 0.2175  -0.0719 -0.6866 1500 ARG A CA  
11429 C C   . ARG A 1500 ? 1.0692 1.5696 1.3567 0.2246  -0.0888 -0.6932 1500 ARG A C   
11430 O O   . ARG A 1500 ? 1.0899 1.6125 1.4124 0.2257  -0.0867 -0.6985 1500 ARG A O   
11431 C CB  . ARG A 1500 ? 1.1207 1.6454 1.3967 0.2165  -0.0510 -0.6915 1500 ARG A CB  
11432 C CG  . ARG A 1500 ? 1.1400 1.6764 1.4231 0.2040  -0.0384 -0.6834 1500 ARG A CG  
11433 C CD  . ARG A 1500 ? 1.1739 1.7403 1.5002 0.2039  -0.0304 -0.6900 1500 ARG A CD  
11434 N NE  . ARG A 1500 ? 1.1960 1.7813 1.5256 0.2032  -0.0071 -0.6928 1500 ARG A NE  
11435 C CZ  . ARG A 1500 ? 1.2060 1.8199 1.5725 0.2044  0.0037  -0.6989 1500 ARG A CZ  
11436 N NH1 . ARG A 1500 ? 1.1898 1.8181 1.5944 0.2066  -0.0082 -0.7031 1500 ARG A NH1 
11437 N NH2 . ARG A 1500 ? 1.2294 1.8580 1.5948 0.2040  0.0263  -0.7007 1500 ARG A NH2 
11438 N N   . PRO A 1501 ? 1.0088 1.4858 1.2802 0.2298  -0.1055 -0.6926 1501 PRO A N   
11439 C CA  . PRO A 1501 ? 1.0181 1.4875 1.3037 0.2390  -0.1237 -0.6984 1501 PRO A CA  
11440 C C   . PRO A 1501 ? 1.0609 1.5475 1.3716 0.2509  -0.1207 -0.7111 1501 PRO A C   
11441 O O   . PRO A 1501 ? 1.0564 1.5372 1.3788 0.2604  -0.1350 -0.7165 1501 PRO A O   
11442 C CB  . PRO A 1501 ? 1.0125 1.4529 1.2641 0.2425  -0.1332 -0.6957 1501 PRO A CB  
11443 C CG  . PRO A 1501 ? 1.0107 1.4430 1.2339 0.2328  -0.1245 -0.6851 1501 PRO A CG  
11444 C CD  . PRO A 1501 ? 1.0018 1.4564 1.2343 0.2264  -0.1059 -0.6844 1501 PRO A CD  
11445 N N   . ASP A 1502 ? 1.1338 1.6388 1.4492 0.2513  -0.1018 -0.7156 1502 ASP A N   
11446 C CA  . ASP A 1502 ? 1.1853 1.7050 1.5208 0.2640  -0.0959 -0.7277 1502 ASP A CA  
11447 C C   . ASP A 1502 ? 1.2369 1.7839 1.6174 0.2646  -0.0975 -0.7299 1502 ASP A C   
11448 O O   . ASP A 1502 ? 1.2631 1.8284 1.6710 0.2756  -0.0938 -0.7389 1502 ASP A O   
11449 C CB  . ASP A 1502 ? 1.1932 1.7219 1.5158 0.2641  -0.0739 -0.7314 1502 ASP A CB  
11450 C CG  . ASP A 1502 ? 1.1634 1.6764 1.4464 0.2533  -0.0677 -0.7224 1502 ASP A CG  
11451 O OD1 . ASP A 1502 ? 1.1255 1.6129 1.3797 0.2521  -0.0797 -0.7179 1502 ASP A OD1 
11452 O OD2 . ASP A 1502 ? 1.1680 1.6955 1.4497 0.2463  -0.0500 -0.7193 1502 ASP A OD2 
11453 N N   . LYS A 1503 ? 1.2697 1.8190 1.6576 0.2528  -0.1035 -0.7213 1503 LYS A N   
11454 C CA  . LYS A 1503 ? 1.3322 1.9083 1.7625 0.2496  -0.1059 -0.7219 1503 LYS A CA  
11455 C C   . LYS A 1503 ? 1.1561 1.7243 1.6012 0.2521  -0.1310 -0.7213 1503 LYS A C   
11456 O O   . LYS A 1503 ? 1.0994 1.6791 1.5662 0.2429  -0.1374 -0.7174 1503 LYS A O   
11457 C CB  . LYS A 1503 ? 1.3760 1.9633 1.8071 0.2332  -0.0922 -0.7138 1503 LYS A CB  
11458 C CG  . LYS A 1503 ? 1.4164 2.0289 1.8587 0.2324  -0.0668 -0.7171 1503 LYS A CG  
11459 C CD  . LYS A 1503 ? 1.4555 2.0588 1.8718 0.2422  -0.0555 -0.7227 1503 LYS A CD  
11460 C CE  . LYS A 1503 ? 1.5076 2.1405 1.9476 0.2468  -0.0334 -0.7296 1503 LYS A CE  
11461 N NZ  . LYS A 1503 ? 1.5516 2.1769 1.9731 0.2603  -0.0246 -0.7387 1503 LYS A NZ  
11462 N N   . GLN A 1504 ? 1.1781 1.7258 1.6106 0.2645  -0.1450 -0.7255 1504 GLN A N   
11463 C CA  . GLN A 1504 ? 1.0831 1.6161 1.5198 0.2685  -0.1691 -0.7246 1504 GLN A CA  
11464 C C   . GLN A 1504 ? 1.0913 1.6502 1.5723 0.2779  -0.1770 -0.7315 1504 GLN A C   
11465 O O   . GLN A 1504 ? 0.8497 1.4089 1.3384 0.2936  -0.1802 -0.7393 1504 GLN A O   
11466 C CB  . GLN A 1504 ? 1.0822 1.5800 1.4844 0.2778  -0.1803 -0.7254 1504 GLN A CB  
11467 C CG  . GLN A 1504 ? 1.6315 2.0967 1.9944 0.2676  -0.1878 -0.7146 1504 GLN A CG  
11468 C CD  . GLN A 1504 ? 1.3631 1.7965 1.6878 0.2732  -0.1913 -0.7139 1504 GLN A CD  
11469 O OE1 . GLN A 1504 ? 1.2951 1.7052 1.5886 0.2658  -0.1941 -0.7049 1504 GLN A OE1 
11470 N NE2 . GLN A 1504 ? 1.3988 1.8314 1.7266 0.2862  -0.1909 -0.7232 1504 GLN A NE2 
11471 N N   . CYS A 1505 ? 1.0113 1.5917 1.5211 0.2677  -0.1800 -0.7283 1505 CYS A N   
11472 C CA  . CYS A 1505 ? 1.0299 1.6305 1.5801 0.2742  -0.1959 -0.7323 1505 CYS A CA  
11473 C C   . CYS A 1505 ? 1.0424 1.6139 1.5763 0.2759  -0.2223 -0.7290 1505 CYS A C   
11474 O O   . CYS A 1505 ? 0.9814 1.5314 1.4913 0.2634  -0.2291 -0.7212 1505 CYS A O   
11475 C CB  . CYS A 1505 ? 1.0258 1.6631 1.6169 0.2621  -0.1906 -0.7306 1505 CYS A CB  
11476 S SG  . CYS A 1505 ? 1.6787 2.3524 2.3286 0.2742  -0.2058 -0.7374 1505 CYS A SG  
11477 N N   . THR A 1506 ? 1.0539 1.6239 1.6001 0.2922  -0.2364 -0.7348 1506 THR A N   
11478 C CA  . THR A 1506 ? 1.0903 1.6291 1.6161 0.2962  -0.2599 -0.7321 1506 THR A CA  
11479 C C   . THR A 1506 ? 1.1088 1.6696 1.6749 0.3055  -0.2769 -0.7363 1506 THR A C   
11480 O O   . THR A 1506 ? 1.1026 1.6948 1.7044 0.3161  -0.2694 -0.7430 1506 THR A O   
11481 C CB  . THR A 1506 ? 1.1537 1.6606 1.6454 0.3091  -0.2609 -0.7346 1506 THR A CB  
11482 O OG1 . THR A 1506 ? 1.2024 1.6969 1.6628 0.3017  -0.2425 -0.7319 1506 THR A OG1 
11483 C CG2 . THR A 1506 ? 1.1498 1.6203 1.6143 0.3108  -0.2831 -0.7300 1506 THR A CG2 
11484 N N   . MET A 1507 ? 1.1301 1.6739 1.6895 0.3016  -0.2996 -0.7321 1507 MET A N   
11485 C CA  . MET A 1507 ? 1.0933 1.6562 1.6890 0.3083  -0.3205 -0.7346 1507 MET A CA  
11486 C C   . MET A 1507 ? 1.0598 1.5863 1.6289 0.3118  -0.3468 -0.7311 1507 MET A C   
11487 O O   . MET A 1507 ? 1.0110 1.5080 1.5459 0.2993  -0.3518 -0.7244 1507 MET A O   
11488 C CB  . MET A 1507 ? 1.0637 1.6605 1.6949 0.2919  -0.3201 -0.7323 1507 MET A CB  
11489 C CG  . MET A 1507 ? 1.0585 1.6899 1.7398 0.2985  -0.3364 -0.7360 1507 MET A CG  
11490 S SD  . MET A 1507 ? 0.9169 1.5706 1.6212 0.2725  -0.3395 -0.7308 1507 MET A SD  
11491 C CE  . MET A 1507 ? 0.8638 1.4852 1.5168 0.2566  -0.3176 -0.7246 1507 MET A CE  
11492 N N   . PHE A 1508 ? 1.0686 1.5957 1.6516 0.3296  -0.3626 -0.7354 1508 PHE A N   
11493 C CA  . PHE A 1508 ? 1.1139 1.6113 1.6777 0.3335  -0.3891 -0.7324 1508 PHE A CA  
11494 C C   . PHE A 1508 ? 1.2325 1.7527 1.8263 0.3222  -0.4056 -0.7303 1508 PHE A C   
11495 O O   . PHE A 1508 ? 1.2926 1.8582 1.9344 0.3200  -0.4005 -0.7335 1508 PHE A O   
11496 C CB  . PHE A 1508 ? 1.0558 1.5512 1.6301 0.3568  -0.4007 -0.7376 1508 PHE A CB  
11497 C CG  . PHE A 1508 ? 0.9724 1.4330 1.5091 0.3684  -0.3929 -0.7391 1508 PHE A CG  
11498 C CD1 . PHE A 1508 ? 0.9847 1.3993 1.4714 0.3634  -0.3979 -0.7334 1508 PHE A CD1 
11499 C CD2 . PHE A 1508 ? 0.9480 1.4209 1.4995 0.3850  -0.3815 -0.7462 1508 PHE A CD2 
11500 C CE1 . PHE A 1508 ? 0.9910 1.3739 1.4442 0.3730  -0.3913 -0.7345 1508 PHE A CE1 
11501 C CE2 . PHE A 1508 ? 0.9634 1.4024 1.4794 0.3947  -0.3753 -0.7479 1508 PHE A CE2 
11502 C CZ  . PHE A 1508 ? 0.9791 1.3736 1.4465 0.3880  -0.3805 -0.7420 1508 PHE A CZ  
11503 N N   . TYR A 1509 ? 1.2501 1.7393 1.8162 0.3148  -0.4254 -0.7251 1509 TYR A N   
11504 C CA  . TYR A 1509 ? 1.2213 1.7264 1.8119 0.3054  -0.4467 -0.7238 1509 TYR A CA  
11505 C C   . TYR A 1509 ? 1.2824 1.7430 1.8344 0.3098  -0.4712 -0.7201 1509 TYR A C   
11506 O O   . TYR A 1509 ? 1.3130 1.7323 1.8198 0.3160  -0.4679 -0.7176 1509 TYR A O   
11507 C CB  . TYR A 1509 ? 1.1191 1.6321 1.7103 0.2807  -0.4384 -0.7196 1509 TYR A CB  
11508 C CG  . TYR A 1509 ? 1.0716 1.5346 1.6056 0.2703  -0.4392 -0.7128 1509 TYR A CG  
11509 C CD1 . TYR A 1509 ? 1.0582 1.5091 1.5806 0.2523  -0.4492 -0.7084 1509 TYR A CD1 
11510 C CD2 . TYR A 1509 ? 1.0829 1.5098 1.5740 0.2792  -0.4300 -0.7107 1509 TYR A CD2 
11511 C CE1 . TYR A 1509 ? 1.0744 1.4781 1.5431 0.2445  -0.4486 -0.7019 1509 TYR A CE1 
11512 C CE2 . TYR A 1509 ? 1.0899 1.4728 1.5304 0.2710  -0.4296 -0.7038 1509 TYR A CE2 
11513 C CZ  . TYR A 1509 ? 1.0899 1.4610 1.5189 0.2544  -0.4384 -0.6993 1509 TYR A CZ  
11514 O OH  . TYR A 1509 ? 1.0927 1.4191 1.4704 0.2478  -0.4364 -0.6921 1509 TYR A OH  
11515 N N   . SER A 1510 ? 1.2900 1.7580 1.8585 0.3059  -0.4958 -0.7197 1510 SER A N   
11516 C CA  . SER A 1510 ? 1.3004 1.7242 1.8294 0.3095  -0.5193 -0.7160 1510 SER A CA  
11517 C C   . SER A 1510 ? 1.3358 1.7516 1.8566 0.2894  -0.5332 -0.7123 1510 SER A C   
11518 O O   . SER A 1510 ? 1.3103 1.7617 1.8667 0.2748  -0.5306 -0.7134 1510 SER A O   
11519 C CB  . SER A 1510 ? 1.3070 1.7359 1.8535 0.3304  -0.5415 -0.7193 1510 SER A CB  
11520 O OG  . SER A 1510 ? 1.3121 1.6891 1.8090 0.3371  -0.5580 -0.7154 1510 SER A OG  
11521 N N   . THR A 1511 ? 1.3754 1.7421 1.8471 0.2884  -0.5475 -0.7077 1511 THR A N   
11522 C CA  . THR A 1511 ? 1.4009 1.7482 1.8516 0.2691  -0.5581 -0.7038 1511 THR A CA  
11523 C C   . THR A 1511 ? 1.5334 1.8802 1.9936 0.2716  -0.5913 -0.7050 1511 THR A C   
11524 O O   . THR A 1511 ? 1.5737 1.8913 2.0045 0.2595  -0.6063 -0.7018 1511 THR A O   
11525 C CB  . THR A 1511 ? 1.3450 1.6358 1.7316 0.2667  -0.5516 -0.6975 1511 THR A CB  
11526 O OG1 . THR A 1511 ? 1.3438 1.6201 1.7115 0.2455  -0.5501 -0.6936 1511 THR A OG1 
11527 C CG2 . THR A 1511 ? 1.3468 1.5972 1.6989 0.2808  -0.5740 -0.6957 1511 THR A CG2 
11528 N N   . SER A 1512 ? 1.6270 2.0047 2.1266 0.2881  -0.6032 -0.7095 1512 SER A N   
11529 C CA  . SER A 1512 ? 1.7621 2.1440 2.2752 0.2924  -0.6365 -0.7105 1512 SER A CA  
11530 C C   . SER A 1512 ? 1.8830 2.3159 2.4559 0.3085  -0.6442 -0.7156 1512 SER A C   
11531 O O   . SER A 1512 ? 1.8794 2.3276 2.4681 0.3243  -0.6271 -0.7182 1512 SER A O   
11532 C CB  . SER A 1512 ? 1.7786 2.1033 2.2358 0.3038  -0.6540 -0.7070 1512 SER A CB  
11533 O OG  . SER A 1512 ? 1.7790 2.0960 2.2315 0.3270  -0.6484 -0.7081 1512 SER A OG  
11534 N N   . ASN A 1513 ? 2.0296 2.4881 2.6350 0.3046  -0.6705 -0.7168 1513 ASN A N   
11535 C CA  . ASN A 1513 ? 2.1556 2.6674 2.8230 0.3191  -0.6798 -0.7207 1513 ASN A CA  
11536 C C   . ASN A 1513 ? 2.2610 2.7553 2.9186 0.3434  -0.7049 -0.7206 1513 ASN A C   
11537 O O   . ASN A 1513 ? 2.2872 2.8225 2.9935 0.3591  -0.7141 -0.7233 1513 ASN A O   
11538 C CB  . ASN A 1513 ? 2.1962 2.7545 2.9135 0.3007  -0.6943 -0.7218 1513 ASN A CB  
11539 C CG  . ASN A 1513 ? 2.2200 2.7725 2.9245 0.2717  -0.6802 -0.7201 1513 ASN A CG  
11540 O OD1 . ASN A 1513 ? 2.2026 2.7552 2.9003 0.2663  -0.6495 -0.7199 1513 ASN A OD1 
11541 N ND2 . ASN A 1513 ? 2.2542 2.8004 2.9541 0.2529  -0.7030 -0.7188 1513 ASN A ND2 
11542 N N   . ILE A 1514 ? 2.3249 2.7584 2.9195 0.3472  -0.7150 -0.7170 1514 ILE A N   
11543 C CA  . ILE A 1514 ? 2.3760 2.7854 2.9533 0.3673  -0.7425 -0.7158 1514 ILE A CA  
11544 C C   . ILE A 1514 ? 2.3781 2.8059 2.9813 0.3955  -0.7381 -0.7185 1514 ILE A C   
11545 O O   . ILE A 1514 ? 2.3681 2.7783 2.9522 0.4058  -0.7145 -0.7192 1514 ILE A O   
11546 C CB  . ILE A 1514 ? 2.5712 2.9078 3.0713 0.3671  -0.7484 -0.7109 1514 ILE A CB  
11547 C CG1 . ILE A 1514 ? 2.5585 2.8719 3.0273 0.3400  -0.7464 -0.7082 1514 ILE A CG1 
11548 C CG2 . ILE A 1514 ? 2.6158 2.9290 3.0990 0.3839  -0.7816 -0.7092 1514 ILE A CG2 
11549 C CD1 . ILE A 1514 ? 2.5666 2.8103 2.9600 0.3389  -0.7447 -0.7030 1514 ILE A CD1 
11550 N N   . LYS A 1515 ? 3.4749 2.7407 2.9587 0.8442  -1.0580 0.0211  1515 LYS A N   
11551 C CA  . LYS A 1515 ? 3.4730 2.7169 2.9913 0.8320  -1.0484 0.0180  1515 LYS A CA  
11552 C C   . LYS A 1515 ? 3.5734 2.7292 3.0154 0.8388  -1.0437 0.0329  1515 LYS A C   
11553 O O   . LYS A 1515 ? 3.6461 2.7685 3.0142 0.8499  -1.0421 0.0436  1515 LYS A O   
11554 C CB  . LYS A 1515 ? 3.4241 2.6557 2.9962 0.8404  -1.0887 0.0179  1515 LYS A CB  
11555 C CG  . LYS A 1515 ? 3.3125 2.6159 2.9466 0.8400  -1.1056 0.0069  1515 LYS A CG  
11556 C CD  . LYS A 1515 ? 3.2824 2.5606 2.9555 0.8528  -1.1510 0.0102  1515 LYS A CD  
11557 C CE  . LYS A 1515 ? 3.1923 2.5363 2.9173 0.8540  -1.1701 0.0008  1515 LYS A CE  
11558 N NZ  . LYS A 1515 ? 3.1810 2.5005 2.9419 0.8671  -1.2153 0.0043  1515 LYS A NZ  
11559 N N   . ILE A 1516 ? 3.5694 2.6884 3.0307 0.8320  -1.0418 0.0332  1516 ILE A N   
11560 C CA  . ILE A 1516 ? 3.6270 2.6607 3.0271 0.8350  -1.0369 0.0457  1516 ILE A CA  
11561 C C   . ILE A 1516 ? 3.6130 2.6693 3.0457 0.8097  -0.9946 0.0345  1516 ILE A C   
11562 O O   . ILE A 1516 ? 3.5566 2.6824 3.0147 0.7908  -0.9564 0.0217  1516 ILE A O   
11563 C CB  . ILE A 1516 ? 3.9837 2.9629 3.2842 0.8476  -1.0333 0.0604  1516 ILE A CB  
11564 C CG1 . ILE A 1516 ? 3.9517 2.9915 3.2380 0.8339  -0.9899 0.0519  1516 ILE A CG1 
11565 C CG2 . ILE A 1516 ? 4.0117 2.9473 3.2732 0.8748  -1.0811 0.0744  1516 ILE A CG2 
11566 C CD1 . ILE A 1516 ? 3.9614 3.0097 3.2461 0.8108  -0.9421 0.0450  1516 ILE A CD1 
11567 N N   . GLN A 1517 ? 3.6686 2.6657 3.1006 0.8093  -1.0023 0.0394  1517 GLN A N   
11568 C CA  . GLN A 1517 ? 3.6674 2.6860 3.1419 0.7860  -0.9683 0.0280  1517 GLN A CA  
11569 C C   . GLN A 1517 ? 3.7500 2.7241 3.1617 0.7757  -0.9338 0.0334  1517 GLN A C   
11570 O O   . GLN A 1517 ? 3.8205 2.7320 3.1510 0.7884  -0.9402 0.0477  1517 GLN A O   
11571 C CB  . GLN A 1517 ? 3.6538 2.6438 3.1792 0.7892  -0.9954 0.0272  1517 GLN A CB  
11572 C CG  . GLN A 1517 ? 3.5522 2.5951 3.1553 0.7940  -1.0235 0.0184  1517 GLN A CG  
11573 C CD  . GLN A 1517 ? 3.5307 2.5309 3.1723 0.8021  -1.0562 0.0206  1517 GLN A CD  
11574 O OE1 . GLN A 1517 ? 3.5837 2.4987 3.1768 0.8164  -1.0793 0.0349  1517 GLN A OE1 
11575 N NE2 . GLN A 1517 ? 3.4516 2.5107 3.1807 0.7928  -1.0584 0.0062  1517 GLN A NE2 
11576 N N   . LYS A 1518 ? 3.7378 2.7463 3.1886 0.7517  -0.8967 0.0212  1518 LYS A N   
11577 C CA  . LYS A 1518 ? 3.8065 2.7699 3.2140 0.7388  -0.8656 0.0245  1518 LYS A CA  
11578 C C   . LYS A 1518 ? 3.8041 2.8056 3.2838 0.7164  -0.8425 0.0100  1518 LYS A C   
11579 O O   . LYS A 1518 ? 3.7620 2.7791 3.3058 0.7190  -0.8653 0.0043  1518 LYS A O   
11580 C CB  . LYS A 1518 ? 3.8043 2.7858 3.1570 0.7296  -0.8271 0.0247  1518 LYS A CB  
11581 C CG  . LYS A 1518 ? 3.7958 2.7816 3.1031 0.7473  -0.8423 0.0323  1518 LYS A CG  
11582 C CD  . LYS A 1518 ? 3.8685 2.7914 3.0790 0.7528  -0.8293 0.0453  1518 LYS A CD  
11583 C CE  . LYS A 1518 ? 3.9042 2.8048 3.0942 0.7322  -0.7898 0.0432  1518 LYS A CE  
11584 N NZ  . LYS A 1518 ? 3.9704 2.7785 3.1304 0.7386  -0.8098 0.0542  1518 LYS A NZ  
11585 N N   . VAL A 1519 ? 3.8610 2.8776 3.3310 0.6944  -0.7976 0.0039  1519 VAL A N   
11586 C CA  . VAL A 1519 ? 3.8733 2.9317 3.4112 0.6715  -0.7722 -0.0106 1519 VAL A CA  
11587 C C   . VAL A 1519 ? 3.8813 3.0033 3.4229 0.6463  -0.7197 -0.0217 1519 VAL A C   
11588 O O   . VAL A 1519 ? 3.7983 3.0055 3.4000 0.6337  -0.7042 -0.0358 1519 VAL A O   
11589 C CB  . VAL A 1519 ? 2.6698 1.6509 2.1973 0.6714  -0.7808 -0.0047 1519 VAL A CB  
11590 C CG1 . VAL A 1519 ? 2.6523 1.6631 2.2161 0.6439  -0.7397 -0.0170 1519 VAL A CG1 
11591 C CG2 . VAL A 1519 ? 2.6508 1.6064 2.2213 0.6888  -0.8277 -0.0023 1519 VAL A CG2 
11592 N N   . CYS A 1520 ? 3.9899 3.0693 3.4660 0.6391  -0.6932 -0.0151 1520 CYS A N   
11593 C CA  . CYS A 1520 ? 4.0200 3.1502 3.4850 0.6176  -0.6444 -0.0230 1520 CYS A CA  
11594 C C   . CYS A 1520 ? 4.0114 3.2110 3.5449 0.5894  -0.6082 -0.0402 1520 CYS A C   
11595 O O   . CYS A 1520 ? 3.9344 3.2053 3.5395 0.5837  -0.6105 -0.0525 1520 CYS A O   
11596 C CB  . CYS A 1520 ? 3.9911 3.1670 3.4371 0.6254  -0.6428 -0.0230 1520 CYS A CB  
11597 S SG  . CYS A 1520 ? 4.9225 4.0180 4.2561 0.6445  -0.6508 -0.0040 1520 CYS A SG  
11598 N N   . GLU A 1521 ? 4.1012 3.2778 3.6086 0.5713  -0.5741 -0.0406 1521 GLU A N   
11599 C CA  . GLU A 1521 ? 4.1011 3.3341 3.6630 0.5429  -0.5361 -0.0556 1521 GLU A CA  
11600 C C   . GLU A 1521 ? 4.0543 3.3604 3.6166 0.5250  -0.4950 -0.0646 1521 GLU A C   
11601 O O   . GLU A 1521 ? 4.0168 3.3714 3.5869 0.5327  -0.5014 -0.0670 1521 GLU A O   
11602 C CB  . GLU A 1521 ? 4.1992 3.3687 3.7356 0.5319  -0.5216 -0.0518 1521 GLU A CB  
11603 C CG  . GLU A 1521 ? 4.3025 3.4110 3.7479 0.5312  -0.5030 -0.0403 1521 GLU A CG  
11604 C CD  . GLU A 1521 ? 4.3092 3.4523 3.7516 0.5021  -0.4505 -0.0488 1521 GLU A CD  
11605 O OE1 . GLU A 1521 ? 4.2931 3.4585 3.7849 0.4831  -0.4331 -0.0587 1521 GLU A OE1 
11606 O OE2 . GLU A 1521 ? 4.3285 3.4762 3.7192 0.4980  -0.4265 -0.0457 1521 GLU A OE2 
11607 N N   . GLY A 1522 ? 4.0432 3.3568 3.5976 0.5011  -0.4535 -0.0696 1522 GLY A N   
11608 C CA  . GLY A 1522 ? 3.9712 3.3522 3.5272 0.4818  -0.4118 -0.0785 1522 GLY A CA  
11609 C C   . GLY A 1522 ? 3.9574 3.3253 3.4429 0.4922  -0.4056 -0.0698 1522 GLY A C   
11610 O O   . GLY A 1522 ? 3.9693 3.3665 3.4344 0.4756  -0.3669 -0.0738 1522 GLY A O   
11611 N N   . ALA A 1523 ? 3.9201 3.2440 3.3693 0.5196  -0.4439 -0.0580 1523 ALA A N   
11612 C CA  . ALA A 1523 ? 3.8770 3.1844 3.2591 0.5339  -0.4451 -0.0488 1523 ALA A CA  
11613 C C   . ALA A 1523 ? 3.8880 3.0969 3.1806 0.5438  -0.4489 -0.0328 1523 ALA A C   
11614 O O   . ALA A 1523 ? 3.9190 3.0931 3.1544 0.5633  -0.4658 -0.0220 1523 ALA A O   
11615 C CB  . ALA A 1523 ? 3.8423 3.2277 3.2322 0.5169  -0.4046 -0.0591 1523 ALA A CB  
11616 N N   . ALA A 1524 ? 3.8440 3.0065 3.1230 0.5304  -0.4338 -0.0312 1524 ALA A N   
11617 C CA  . ALA A 1524 ? 3.8416 2.9074 3.0353 0.5379  -0.4367 -0.0163 1524 ALA A CA  
11618 C C   . ALA A 1524 ? 3.7726 2.7668 2.9362 0.5674  -0.4880 -0.0023 1524 ALA A C   
11619 O O   . ALA A 1524 ? 3.8651 2.7716 2.9578 0.5773  -0.4989 0.0113  1524 ALA A O   
11620 C CB  . ALA A 1524 ? 3.8837 2.9143 3.0765 0.5181  -0.4149 -0.0181 1524 ALA A CB  
11621 N N   . CYS A 1525 ? 3.5943 2.6266 2.8124 0.5808  -0.5195 -0.0059 1525 CYS A N   
11622 C CA  . CYS A 1525 ? 3.5121 2.4872 2.7118 0.6088  -0.5702 0.0062  1525 CYS A CA  
11623 C C   . CYS A 1525 ? 3.4485 2.4124 2.5922 0.6292  -0.5853 0.0157  1525 CYS A C   
11624 O O   . CYS A 1525 ? 3.5047 2.3853 2.5766 0.6459  -0.6058 0.0309  1525 CYS A O   
11625 C CB  . CYS A 1525 ? 3.4294 2.4491 2.7152 0.6128  -0.5973 -0.0024 1525 CYS A CB  
11626 S SG  . CYS A 1525 ? 4.1600 3.1318 3.4391 0.6468  -0.6606 0.0099  1525 CYS A SG  
11627 N N   . LYS A 1526 ? 3.3075 2.3528 2.4822 0.6275  -0.5752 0.0068  1526 LYS A N   
11628 C CA  . LYS A 1526 ? 3.2136 2.2577 2.3408 0.6462  -0.5876 0.0142  1526 LYS A CA  
11629 C C   . LYS A 1526 ? 3.2199 2.2326 2.2670 0.6418  -0.5565 0.0205  1526 LYS A C   
11630 O O   . LYS A 1526 ? 3.1757 2.2219 2.2002 0.6466  -0.5464 0.0198  1526 LYS A O   
11631 C CB  . LYS A 1526 ? 3.0750 2.2177 2.2606 0.6444  -0.5841 0.0017  1526 LYS A CB  
11632 C CG  . LYS A 1526 ? 2.9785 2.1509 2.2332 0.6540  -0.6209 -0.0028 1526 LYS A CG  
11633 C CD  . LYS A 1526 ? 2.8625 2.1394 2.1817 0.6442  -0.6073 -0.0183 1526 LYS A CD  
11634 C CE  . LYS A 1526 ? 2.7794 2.1001 2.1873 0.6369  -0.6209 -0.0294 1526 LYS A CE  
11635 N NZ  . LYS A 1526 ? 2.7736 2.0749 2.2062 0.6184  -0.6027 -0.0335 1526 LYS A NZ  
11636 N N   . CYS A 1527 ? 3.2837 2.2322 2.2883 0.6324  -0.5413 0.0262  1527 CYS A N   
11637 C CA  . CYS A 1527 ? 3.3470 2.2603 2.2743 0.6262  -0.5103 0.0320  1527 CYS A CA  
11638 C C   . CYS A 1527 ? 3.4624 2.2648 2.3201 0.6339  -0.5254 0.0470  1527 CYS A C   
11639 O O   . CYS A 1527 ? 3.5330 2.2797 2.3099 0.6411  -0.5204 0.0577  1527 CYS A O   
11640 C CB  . CYS A 1527 ? 3.3087 2.2796 2.2612 0.5960  -0.4576 0.0189  1527 CYS A CB  
11641 S SG  . CYS A 1527 ? 3.6591 2.6268 2.5346 0.5885  -0.4153 0.0214  1527 CYS A SG  
11642 N N   . VAL A 1528 ? 3.4994 2.2688 2.3881 0.6322  -0.5439 0.0476  1528 VAL A N   
11643 C CA  . VAL A 1528 ? 3.6373 2.2981 2.4643 0.6427  -0.5668 0.0624  1528 VAL A CA  
11644 C C   . VAL A 1528 ? 3.7214 2.3347 2.5047 0.6726  -0.6104 0.0761  1528 VAL A C   
11645 O O   . VAL A 1528 ? 3.8118 2.3311 2.5239 0.6857  -0.6307 0.0909  1528 VAL A O   
11646 C CB  . VAL A 1528 ? 3.7059 2.3447 2.5825 0.6375  -0.5828 0.0597  1528 VAL A CB  
11647 C CG1 . VAL A 1528 ? 3.7966 2.3200 2.6081 0.6504  -0.6106 0.0756  1528 VAL A CG1 
11648 C CG2 . VAL A 1528 ? 3.6772 2.3625 2.5939 0.6072  -0.5381 0.0463  1528 VAL A CG2 
11649 N N   . GLU A 1529 ? 3.7003 2.3797 2.5264 0.6828  -0.6246 0.0708  1529 GLU A N   
11650 C CA  . GLU A 1529 ? 3.7696 2.4200 2.5553 0.7093  -0.6598 0.0821  1529 GLU A CA  
11651 C C   . GLU A 1529 ? 3.7404 2.4368 2.4958 0.7082  -0.6328 0.0793  1529 GLU A C   
11652 O O   . GLU A 1529 ? 3.6711 2.4496 2.4768 0.7087  -0.6306 0.0696  1529 GLU A O   
11653 C CB  . GLU A 1529 ? 3.7698 2.4576 2.6246 0.7233  -0.6995 0.0787  1529 GLU A CB  
11654 C CG  . GLU A 1529 ? 3.7205 2.5165 2.6682 0.7063  -0.6789 0.0601  1529 GLU A CG  
11655 C CD  . GLU A 1529 ? 3.6928 2.5279 2.7025 0.7207  -0.7173 0.0568  1529 GLU A CD  
11656 O OE1 . GLU A 1529 ? 3.7355 2.5173 2.7135 0.7447  -0.7592 0.0693  1529 GLU A OE1 
11657 O OE2 . GLU A 1529 ? 3.6250 2.5433 2.7142 0.7076  -0.7055 0.0418  1529 GLU A OE2 
11658 N N   . ALA A 1530 ? 3.7849 2.4265 2.4572 0.7070  -0.6128 0.0878  1530 ALA A N   
11659 C CA  . ALA A 1530 ? 3.7528 2.4340 2.3918 0.7029  -0.5800 0.0845  1530 ALA A CA  
11660 C C   . ALA A 1530 ? 3.6643 2.4060 2.3260 0.7186  -0.5963 0.0816  1530 ALA A C   
11661 O O   . ALA A 1530 ? 3.5647 2.3901 2.2597 0.7079  -0.5675 0.0695  1530 ALA A O   
11662 C CB  . ALA A 1530 ? 3.8436 2.4356 2.3780 0.7084  -0.5722 0.0985  1530 ALA A CB  
11663 N N   . ASP A 1531 ? 3.6844 2.3827 2.3287 0.7437  -0.6433 0.0926  1531 ASP A N   
11664 C CA  . ASP A 1531 ? 3.6504 2.3804 2.2886 0.7620  -0.6612 0.0941  1531 ASP A CA  
11665 C C   . ASP A 1531 ? 3.7817 2.4258 2.3753 0.7881  -0.7120 0.1109  1531 ASP A C   
11666 O O   . ASP A 1531 ? 3.7566 2.4121 2.3537 0.8075  -0.7433 0.1145  1531 ASP A O   
11667 C CB  . ASP A 1531 ? 3.6008 2.3377 2.1782 0.7592  -0.6263 0.0946  1531 ASP A CB  
11668 C CG  . ASP A 1531 ? 3.5173 2.2612 2.0639 0.7821  -0.6478 0.1002  1531 ASP A CG  
11669 O OD1 . ASP A 1531 ? 3.4667 2.2166 2.0422 0.7992  -0.6888 0.1029  1531 ASP A OD1 
11670 O OD2 . ASP A 1531 ? 3.5034 2.2468 1.9963 0.7828  -0.6232 0.1016  1531 ASP A OD2 
11671 N N   . CYS A 1532 ? 3.9424 2.4999 2.4952 0.7876  -0.7205 0.1210  1532 CYS A N   
11672 C CA  . CYS A 1532 ? 4.1207 2.5804 2.6156 0.8108  -0.7654 0.1388  1532 CYS A CA  
11673 C C   . CYS A 1532 ? 4.2210 2.6928 2.7472 0.8334  -0.8141 0.1425  1532 CYS A C   
11674 O O   . CYS A 1532 ? 4.1244 2.6761 2.7307 0.8298  -0.8183 0.1306  1532 CYS A O   
11675 C CB  . CYS A 1532 ? 4.1618 2.5480 2.6465 0.8046  -0.7738 0.1446  1532 CYS A CB  
11676 S SG  . CYS A 1532 ? 3.5965 2.0350 2.1911 0.7919  -0.7818 0.1317  1532 CYS A SG  
11677 N N   . GLY A 1533 ? 2.9567 2.8941 2.7095 0.2479  -0.2000 -0.2584 1533 GLY A N   
11678 C CA  . GLY A 1533 ? 3.1111 3.0361 2.8469 0.2502  -0.2281 -0.2594 1533 GLY A CA  
11679 C C   . GLY A 1533 ? 3.2219 3.1575 2.9633 0.2305  -0.2474 -0.2764 1533 GLY A C   
11680 O O   . GLY A 1533 ? 3.2261 3.1836 2.9864 0.2090  -0.2401 -0.2894 1533 GLY A O   
11681 N N   . GLN A 1534 ? 3.3288 3.2473 3.0548 0.2392  -0.2724 -0.2759 1534 GLN A N   
11682 C CA  . GLN A 1534 ? 3.4137 3.3405 3.1462 0.2221  -0.2942 -0.2890 1534 GLN A CA  
11683 C C   . GLN A 1534 ? 3.3724 3.2501 3.0744 0.2511  -0.3138 -0.2951 1534 GLN A C   
11684 O O   . GLN A 1534 ? 3.3919 3.2453 3.0753 0.2761  -0.3228 -0.2850 1534 GLN A O   
11685 C CB  . GLN A 1534 ? 3.5555 3.5254 3.3128 0.1961  -0.3090 -0.2809 1534 GLN A CB  
11686 C CG  . GLN A 1534 ? 3.7144 3.6690 3.4598 0.2144  -0.3284 -0.2684 1534 GLN A CG  
11687 C CD  . GLN A 1534 ? 3.8397 3.7886 3.5779 0.2297  -0.3154 -0.2501 1534 GLN A CD  
11688 O OE1 . GLN A 1534 ? 3.8876 3.8232 3.6174 0.2411  -0.2928 -0.2474 1534 GLN A OE1 
11689 N NE2 . GLN A 1534 ? 3.8769 3.8360 3.6204 0.2302  -0.3296 -0.2369 1534 GLN A NE2 
11690 N N   . MET A 1535 ? 3.2884 3.1510 2.9863 0.2477  -0.3206 -0.3119 1535 MET A N   
11691 C CA  . MET A 1535 ? 3.1997 3.0177 2.8726 0.2720  -0.3421 -0.3193 1535 MET A CA  
11692 C C   . MET A 1535 ? 3.0623 2.8973 2.7525 0.2523  -0.3678 -0.3244 1535 MET A C   
11693 O O   . MET A 1535 ? 3.0434 2.8922 2.7483 0.2290  -0.3695 -0.3364 1535 MET A O   
11694 C CB  . MET A 1535 ? 3.2134 2.9939 2.8666 0.2867  -0.3335 -0.3339 1535 MET A CB  
11695 C CG  . MET A 1535 ? 3.1891 2.9971 2.8645 0.2580  -0.3153 -0.3442 1535 MET A CG  
11696 S SD  . MET A 1535 ? 3.1747 2.9633 2.8493 0.2463  -0.3286 -0.3653 1535 MET A SD  
11697 C CE  . MET A 1535 ? 1.8508 1.6830 1.5577 0.2100  -0.3034 -0.3737 1535 MET A CE  
11698 N N   . GLN A 1536 ? 2.9510 2.7858 2.6414 0.2619  -0.3875 -0.3148 1536 GLN A N   
11699 C CA  . GLN A 1536 ? 2.8329 2.6872 2.5445 0.2451  -0.4118 -0.3172 1536 GLN A CA  
11700 C C   . GLN A 1536 ? 2.8109 2.6382 2.5165 0.2445  -0.4226 -0.3350 1536 GLN A C   
11701 O O   . GLN A 1536 ? 2.8419 2.6255 2.5208 0.2664  -0.4177 -0.3440 1536 GLN A O   
11702 C CB  . GLN A 1536 ? 2.7726 2.6182 2.4817 0.2650  -0.4329 -0.3063 1536 GLN A CB  
11703 C CG  . GLN A 1536 ? 2.7083 2.5929 2.4347 0.2545  -0.4263 -0.2879 1536 GLN A CG  
11704 C CD  . GLN A 1536 ? 2.6371 2.5788 2.4022 0.2181  -0.4329 -0.2834 1536 GLN A CD  
11705 O OE1 . GLN A 1536 ? 2.6062 2.5564 2.3875 0.2138  -0.4556 -0.2850 1536 GLN A OE1 
11706 N NE2 . GLN A 1536 ? 2.6094 2.5911 2.3908 0.1932  -0.4132 -0.2772 1536 GLN A NE2 
11707 N N   . GLU A 1537 ? 2.7592 2.6127 2.4902 0.2192  -0.4365 -0.3393 1537 GLU A N   
11708 C CA  . GLU A 1537 ? 2.7328 2.5627 2.4620 0.2147  -0.4470 -0.3552 1537 GLU A CA  
11709 C C   . GLU A 1537 ? 2.7744 2.5484 2.4797 0.2489  -0.4680 -0.3608 1537 GLU A C   
11710 O O   . GLU A 1537 ? 2.7626 2.5301 2.4659 0.2685  -0.4834 -0.3518 1537 GLU A O   
11711 C CB  . GLU A 1537 ? 2.6540 2.5239 2.4168 0.1835  -0.4601 -0.3556 1537 GLU A CB  
11712 C CG  . GLU A 1537 ? 2.5760 2.4960 2.3615 0.1475  -0.4409 -0.3561 1537 GLU A CG  
11713 C CD  . GLU A 1537 ? 2.5391 2.4448 2.3197 0.1355  -0.4289 -0.3721 1537 GLU A CD  
11714 O OE1 . GLU A 1537 ? 2.5426 2.3987 2.2970 0.1581  -0.4277 -0.3808 1537 GLU A OE1 
11715 O OE2 . GLU A 1537 ? 2.5120 2.4570 2.3159 0.1034  -0.4208 -0.3761 1537 GLU A OE2 
11716 N N   . GLU A 1538 ? 2.8232 2.5580 2.5124 0.2556  -0.4691 -0.3757 1538 GLU A N   
11717 C CA  . GLU A 1538 ? 2.8801 2.5601 2.5479 0.2872  -0.4906 -0.3829 1538 GLU A CA  
11718 C C   . GLU A 1538 ? 2.9513 2.6411 2.6429 0.2838  -0.5193 -0.3799 1538 GLU A C   
11719 O O   . GLU A 1538 ? 2.9461 2.6799 2.6687 0.2532  -0.5209 -0.3762 1538 GLU A O   
11720 C CB  . GLU A 1538 ? 2.8277 2.4680 2.4790 0.2890  -0.4867 -0.3996 1538 GLU A CB  
11721 C CG  . GLU A 1538 ? 2.7726 2.3599 2.4099 0.3140  -0.5131 -0.4090 1538 GLU A CG  
11722 C CD  . GLU A 1538 ? 2.7393 2.2732 2.3377 0.3540  -0.5117 -0.4135 1538 GLU A CD  
11723 O OE1 . GLU A 1538 ? 2.7208 2.2579 2.3024 0.3657  -0.4913 -0.4075 1538 GLU A OE1 
11724 O OE2 . GLU A 1538 ? 2.7343 2.2219 2.3194 0.3745  -0.5315 -0.4232 1538 GLU A OE2 
11725 N N   . LEU A 1539 ? 3.0236 2.6736 2.7023 0.3160  -0.5416 -0.3815 1539 LEU A N   
11726 C CA  . LEU A 1539 ? 3.0690 2.7267 2.7727 0.3195  -0.5701 -0.3771 1539 LEU A CA  
11727 C C   . LEU A 1539 ? 3.0941 2.8068 2.8243 0.3066  -0.5691 -0.3598 1539 LEU A C   
11728 O O   . LEU A 1539 ? 3.0790 2.8214 2.8072 0.2935  -0.5466 -0.3520 1539 LEU A O   
11729 C CB  . LEU A 1539 ? 3.0898 2.7483 2.8154 0.2981  -0.5826 -0.3859 1539 LEU A CB  
11730 C CG  . LEU A 1539 ? 3.1195 2.8186 2.8646 0.2565  -0.5657 -0.3877 1539 LEU A CG  
11731 C CD1 . LEU A 1539 ? 3.1091 2.8710 2.8923 0.2313  -0.5691 -0.3742 1539 LEU A CD1 
11732 C CD2 . LEU A 1539 ? 3.1333 2.8040 2.8799 0.2462  -0.5729 -0.4018 1539 LEU A CD2 
11733 N N   . ASP A 1540 ? 3.1363 2.8632 2.8935 0.3104  -0.5930 -0.3532 1540 ASP A N   
11734 C CA  . ASP A 1540 ? 3.1540 2.9388 2.9417 0.2931  -0.5917 -0.3365 1540 ASP A CA  
11735 C C   . ASP A 1540 ? 3.2307 3.0400 3.0583 0.2897  -0.6175 -0.3301 1540 ASP A C   
11736 O O   . ASP A 1540 ? 3.2440 3.0200 3.0742 0.3140  -0.6411 -0.3352 1540 ASP A O   
11737 C CB  . ASP A 1540 ? 3.0841 2.8698 2.8557 0.3114  -0.5823 -0.3254 1540 ASP A CB  
11738 C CG  . ASP A 1540 ? 2.9724 2.7981 2.7450 0.2868  -0.5543 -0.3164 1540 ASP A CG  
11739 O OD1 . ASP A 1540 ? 2.9029 2.7504 2.6832 0.2583  -0.5402 -0.3214 1540 ASP A OD1 
11740 O OD2 . ASP A 1540 ? 2.9566 2.7914 2.7236 0.2963  -0.5468 -0.3043 1540 ASP A OD2 
11741 N N   . LEU A 1541 ? 3.2938 3.1632 3.1542 0.2600  -0.6122 -0.3184 1541 LEU A N   
11742 C CA  . LEU A 1541 ? 3.3658 3.2705 3.2703 0.2517  -0.6330 -0.3099 1541 LEU A CA  
11743 C C   . LEU A 1541 ? 3.4961 3.4169 3.4176 0.2695  -0.6455 -0.2959 1541 LEU A C   
11744 O O   . LEU A 1541 ? 3.5286 3.4558 3.4347 0.2743  -0.6319 -0.2881 1541 LEU A O   
11745 C CB  . LEU A 1541 ? 3.3135 3.2779 3.2462 0.2117  -0.6213 -0.3038 1541 LEU A CB  
11746 C CG  . LEU A 1541 ? 3.3100 3.3125 3.2361 0.1888  -0.5939 -0.2966 1541 LEU A CG  
11747 C CD1 . LEU A 1541 ? 3.2962 3.3398 3.2430 0.1878  -0.5946 -0.2783 1541 LEU A CD1 
11748 C CD2 . LEU A 1541 ? 3.2907 3.3318 3.2336 0.1526  -0.5826 -0.2996 1541 LEU A CD2 
11749 N N   . THR A 1542 ? 3.5905 3.5181 3.5459 0.2792  -0.6712 -0.2925 1542 THR A N   
11750 C CA  . THR A 1542 ? 3.6845 3.6323 3.6644 0.2948  -0.6852 -0.2792 1542 THR A CA  
11751 C C   . THR A 1542 ? 3.7275 3.7416 3.7325 0.2677  -0.6713 -0.2612 1542 THR A C   
11752 O O   . THR A 1542 ? 3.7325 3.7816 3.7439 0.2362  -0.6554 -0.2592 1542 THR A O   
11753 C CB  . THR A 1542 ? 3.6923 3.6362 3.7100 0.3106  -0.7160 -0.2796 1542 THR A CB  
11754 O OG1 . THR A 1542 ? 3.6710 3.6414 3.7174 0.2858  -0.7191 -0.2800 1542 THR A OG1 
11755 C CG2 . THR A 1542 ? 3.7358 3.6092 3.7263 0.3461  -0.7318 -0.2956 1542 THR A CG2 
11756 N N   . ILE A 1543 ? 3.7533 3.7841 3.7733 0.2801  -0.6779 -0.2485 1543 ILE A N   
11757 C CA  . ILE A 1543 ? 3.7516 3.8337 3.7853 0.2595  -0.6622 -0.2313 1543 ILE A CA  
11758 C C   . ILE A 1543 ? 3.7875 3.8429 3.7747 0.2647  -0.6386 -0.2327 1543 ILE A C   
11759 O O   . ILE A 1543 ? 3.7908 3.8624 3.7651 0.2410  -0.6159 -0.2325 1543 ILE A O   
11760 C CB  . ILE A 1543 ? 3.1526 3.2952 3.2158 0.2195  -0.6516 -0.2241 1543 ILE A CB  
11761 C CG1 . ILE A 1543 ? 3.1071 3.2801 3.2194 0.2145  -0.6737 -0.2205 1543 ILE A CG1 
11762 C CG2 . ILE A 1543 ? 3.1401 3.3314 3.2148 0.1993  -0.6350 -0.2069 1543 ILE A CG2 
11763 C CD1 . ILE A 1543 ? 3.0636 3.2953 3.2038 0.1777  -0.6643 -0.2137 1543 ILE A CD1 
11764 N N   . SER A 1544 ? 3.8011 3.8164 3.7650 0.2967  -0.6441 -0.2337 1544 SER A N   
11765 C CA  . SER A 1544 ? 3.8176 3.8003 3.7353 0.3071  -0.6227 -0.2356 1544 SER A CA  
11766 C C   . SER A 1544 ? 3.8104 3.7684 3.7127 0.3372  -0.6271 -0.2291 1544 SER A C   
11767 O O   . SER A 1544 ? 3.8227 3.7667 3.6951 0.3415  -0.6072 -0.2247 1544 SER A O   
11768 C CB  . SER A 1544 ? 3.8527 3.7836 3.7311 0.3183  -0.6167 -0.2545 1544 SER A CB  
11769 O OG  . SER A 1544 ? 3.8836 3.7586 3.7336 0.3573  -0.6285 -0.2629 1544 SER A OG  
11770 N N   . ALA A 1545 ? 3.7781 3.7294 3.7011 0.3592  -0.6526 -0.2286 1545 ALA A N   
11771 C CA  . ALA A 1545 ? 3.7546 3.6850 3.6646 0.3873  -0.6571 -0.2225 1545 ALA A CA  
11772 C C   . ALA A 1545 ? 3.6623 3.6337 3.5837 0.3676  -0.6397 -0.2027 1545 ALA A C   
11773 O O   . ALA A 1545 ? 3.7146 3.6659 3.6136 0.3853  -0.6328 -0.1964 1545 ALA A O   
11774 C CB  . ALA A 1545 ? 3.7626 3.6892 3.7029 0.4108  -0.6883 -0.2242 1545 ALA A CB  
11775 N N   . GLU A 1546 ? 3.5133 3.5410 3.4689 0.3311  -0.6327 -0.1930 1546 GLU A N   
11776 C CA  . GLU A 1546 ? 3.3994 3.4700 3.3684 0.3066  -0.6146 -0.1743 1546 GLU A CA  
11777 C C   . GLU A 1546 ? 3.3637 3.4256 3.2982 0.2919  -0.5843 -0.1747 1546 GLU A C   
11778 O O   . GLU A 1546 ? 3.3613 3.4277 3.2859 0.2887  -0.5679 -0.1620 1546 GLU A O   
11779 C CB  . GLU A 1546 ? 3.7826 3.9216 3.8076 0.2752  -0.6217 -0.1625 1546 GLU A CB  
11780 C CG  . GLU A 1546 ? 3.7349 3.9003 3.7706 0.2464  -0.6154 -0.1692 1546 GLU A CG  
11781 C CD  . GLU A 1546 ? 3.6400 3.8773 3.7271 0.2134  -0.6167 -0.1546 1546 GLU A CD  
11782 O OE1 . GLU A 1546 ? 3.6038 3.8740 3.7133 0.2055  -0.6142 -0.1375 1546 GLU A OE1 
11783 O OE2 . GLU A 1546 ? 3.6006 3.8619 3.7059 0.1951  -0.6196 -0.1599 1546 GLU A OE2 
11784 N N   . THR A 1547 ? 3.3145 3.3641 3.2332 0.2833  -0.5771 -0.1888 1547 THR A N   
11785 C CA  . THR A 1547 ? 3.2634 3.3060 3.1539 0.2701  -0.5491 -0.1911 1547 THR A CA  
11786 C C   . THR A 1547 ? 3.2599 3.2441 3.1020 0.3011  -0.5379 -0.1966 1547 THR A C   
11787 O O   . THR A 1547 ? 3.1630 3.1429 2.9855 0.2961  -0.5138 -0.1913 1547 THR A O   
11788 C CB  . THR A 1547 ? 3.2319 3.2804 3.1235 0.2513  -0.5456 -0.2055 1547 THR A CB  
11789 O OG1 . THR A 1547 ? 3.1812 3.2821 3.1169 0.2251  -0.5570 -0.2010 1547 THR A OG1 
11790 C CG2 . THR A 1547 ? 3.2362 3.2871 3.1078 0.2347  -0.5166 -0.2068 1547 THR A CG2 
11791 N N   . ARG A 1548 ? 3.3464 3.2863 3.1711 0.3340  -0.5558 -0.2071 1548 ARG A N   
11792 C CA  . ARG A 1548 ? 3.3946 3.2752 3.1720 0.3681  -0.5489 -0.2147 1548 ARG A CA  
11793 C C   . ARG A 1548 ? 3.3439 3.2146 3.1087 0.3857  -0.5421 -0.1999 1548 ARG A C   
11794 O O   . ARG A 1548 ? 3.3617 3.2097 3.0955 0.3942  -0.5201 -0.1964 1548 ARG A O   
11795 C CB  . ARG A 1548 ? 2.8501 2.6876 2.6151 0.3978  -0.5725 -0.2314 1548 ARG A CB  
11796 C CG  . ARG A 1548 ? 2.1169 1.9468 1.8826 0.3864  -0.5765 -0.2484 1548 ARG A CG  
11797 C CD  . ARG A 1548 ? 2.0380 1.8272 1.7614 0.3964  -0.5570 -0.2599 1548 ARG A CD  
11798 N NE  . ARG A 1548 ? 2.0578 1.8543 1.7655 0.3913  -0.5298 -0.2485 1548 ARG A NE  
11799 C CZ  . ARG A 1548 ? 2.1188 1.8796 1.7894 0.4078  -0.5107 -0.2530 1548 ARG A CZ  
11800 N NH1 . ARG A 1548 ? 2.1877 1.9037 1.8317 0.4297  -0.5160 -0.2690 1548 ARG A NH1 
11801 N NH2 . ARG A 1548 ? 2.0983 1.8680 1.7599 0.4031  -0.4865 -0.2409 1548 ARG A NH2 
11802 N N   . LYS A 1549 ? 3.2811 3.1690 3.0719 0.3914  -0.5608 -0.1906 1549 LYS A N   
11803 C CA  . LYS A 1549 ? 3.2768 3.1637 3.0629 0.4017  -0.5546 -0.1744 1549 LYS A CA  
11804 C C   . LYS A 1549 ? 3.3515 3.2669 3.1401 0.3735  -0.5266 -0.1595 1549 LYS A C   
11805 O O   . LYS A 1549 ? 3.3883 3.2745 3.1436 0.3857  -0.5062 -0.1561 1549 LYS A O   
11806 C CB  . LYS A 1549 ? 3.1998 3.1157 3.0261 0.4025  -0.5783 -0.1655 1549 LYS A CB  
11807 C CG  . LYS A 1549 ? 3.1983 3.1015 3.0164 0.4222  -0.5776 -0.1521 1549 LYS A CG  
11808 C CD  . LYS A 1549 ? 3.1537 3.1085 3.0223 0.4041  -0.5893 -0.1359 1549 LYS A CD  
11809 C CE  . LYS A 1549 ? 3.1303 3.0904 3.0296 0.4202  -0.6213 -0.1434 1549 LYS A CE  
11810 N NZ  . LYS A 1549 ? 3.0851 3.0902 3.0316 0.4093  -0.6317 -0.1263 1549 LYS A NZ  
11811 N N   . GLN A 1550 ? 3.4028 3.3745 3.2316 0.3371  -0.5257 -0.1510 1550 GLN A N   
11812 C CA  . GLN A 1550 ? 3.4770 3.4813 3.3151 0.3081  -0.5020 -0.1362 1550 GLN A CA  
11813 C C   . GLN A 1550 ? 3.5923 3.5704 3.3958 0.3094  -0.4748 -0.1402 1550 GLN A C   
11814 O O   . GLN A 1550 ? 3.5983 3.5811 3.3971 0.3017  -0.4545 -0.1266 1550 GLN A O   
11815 C CB  . GLN A 1550 ? 3.4394 3.5052 3.3213 0.2690  -0.5051 -0.1328 1550 GLN A CB  
11816 C CG  . GLN A 1550 ? 3.4112 3.5121 3.3355 0.2640  -0.5302 -0.1272 1550 GLN A CG  
11817 C CD  . GLN A 1550 ? 3.3908 3.5291 3.3434 0.2487  -0.5270 -0.1056 1550 GLN A CD  
11818 O OE1 . GLN A 1550 ? 3.3798 3.5452 3.3390 0.2229  -0.5077 -0.0946 1550 GLN A OE1 
11819 N NE2 . GLN A 1550 ? 3.3855 3.5261 3.3572 0.2641  -0.5464 -0.0994 1550 GLN A NE2 
11820 N N   . THR A 1551 ? 3.6932 3.6452 3.4758 0.3182  -0.4741 -0.1584 1551 THR A N   
11821 C CA  . THR A 1551 ? 3.7899 3.7195 3.5443 0.3200  -0.4487 -0.1632 1551 THR A CA  
11822 C C   . THR A 1551 ? 3.8738 3.7547 3.5908 0.3545  -0.4381 -0.1578 1551 THR A C   
11823 O O   . THR A 1551 ? 3.9014 3.7587 3.5936 0.3626  -0.4165 -0.1600 1551 THR A O   
11824 C CB  . THR A 1551 ? 3.8183 3.7303 3.5603 0.3222  -0.4513 -0.1842 1551 THR A CB  
11825 O OG1 . THR A 1551 ? 3.8465 3.7223 3.5740 0.3517  -0.4739 -0.1951 1551 THR A OG1 
11826 C CG2 . THR A 1551 ? 3.7824 3.7431 3.5590 0.2853  -0.4555 -0.1889 1551 THR A CG2 
11827 N N   . ALA A 1552 ? 3.9198 3.7868 3.6345 0.3755  -0.4535 -0.1506 1552 ALA A N   
11828 C CA  . ALA A 1552 ? 3.9879 3.8084 3.6670 0.4105  -0.4458 -0.1448 1552 ALA A CA  
11829 C C   . ALA A 1552 ? 3.9790 3.8112 3.6632 0.4023  -0.4282 -0.1226 1552 ALA A C   
11830 O O   . ALA A 1552 ? 4.0295 3.8615 3.7061 0.3931  -0.4032 -0.1167 1552 ALA A O   
11831 C CB  . ALA A 1552 ? 4.0212 3.8146 3.6916 0.4419  -0.4719 -0.1508 1552 ALA A CB  
11832 N N   . CYS A 1553 ? 3.8896 3.7326 3.5894 0.4049  -0.4413 -0.1101 1553 CYS A N   
11833 C CA  . CYS A 1553 ? 3.7906 3.6349 3.4906 0.4025  -0.4259 -0.0885 1553 CYS A CA  
11834 C C   . CYS A 1553 ? 3.6805 3.5664 3.4064 0.3637  -0.4062 -0.0753 1553 CYS A C   
11835 O O   . CYS A 1553 ? 3.7083 3.5915 3.4332 0.3611  -0.3908 -0.0571 1553 CYS A O   
11836 C CB  . CYS A 1553 ? 3.8370 3.6876 3.5528 0.4113  -0.4454 -0.0784 1553 CYS A CB  
11837 S SG  . CYS A 1553 ? 5.3577 5.2772 5.1307 0.3671  -0.4503 -0.0604 1553 CYS A SG  
11838 N N   . LYS A 1554 ? 3.5178 3.4412 3.2672 0.3342  -0.4069 -0.0841 1554 LYS A N   
11839 C CA  . LYS A 1554 ? 3.3208 3.2829 3.0931 0.2987  -0.3880 -0.0743 1554 LYS A CA  
11840 C C   . LYS A 1554 ? 3.1790 3.1083 2.9249 0.3115  -0.3605 -0.0654 1554 LYS A C   
11841 O O   . LYS A 1554 ? 3.2014 3.1027 2.9226 0.3263  -0.3484 -0.0766 1554 LYS A O   
11842 C CB  . LYS A 1554 ? 3.2816 3.2723 3.0683 0.2753  -0.3881 -0.0901 1554 LYS A CB  
11843 C CG  . LYS A 1554 ? 3.2319 3.2600 3.0394 0.2412  -0.3677 -0.0832 1554 LYS A CG  
11844 C CD  . LYS A 1554 ? 3.1699 3.2564 3.0205 0.2068  -0.3770 -0.0722 1554 LYS A CD  
11845 C CE  . LYS A 1554 ? 3.1311 3.2558 3.0026 0.1732  -0.3579 -0.0666 1554 LYS A CE  
11846 N NZ  . LYS A 1554 ? 3.1259 3.2451 2.9974 0.1699  -0.3394 -0.0463 1554 LYS A NZ  
11847 N N   . PRO A 1555 ? 3.0010 2.9342 2.7544 0.3056  -0.3505 -0.0444 1555 PRO A N   
11848 C CA  . PRO A 1555 ? 2.9011 2.7963 2.6296 0.3244  -0.3275 -0.0310 1555 PRO A CA  
11849 C C   . PRO A 1555 ? 2.7739 2.6493 2.4845 0.3307  -0.3034 -0.0376 1555 PRO A C   
11850 O O   . PRO A 1555 ? 2.7968 2.6287 2.4788 0.3590  -0.2880 -0.0312 1555 PRO A O   
11851 C CB  . PRO A 1555 ? 2.8912 2.8173 2.6483 0.2969  -0.3202 -0.0090 1555 PRO A CB  
11852 C CG  . PRO A 1555 ? 2.8877 2.8522 2.6749 0.2804  -0.3455 -0.0085 1555 PRO A CG  
11853 C CD  . PRO A 1555 ? 2.9166 2.8958 2.7083 0.2779  -0.3618 -0.0309 1555 PRO A CD  
11854 N N   . GLU A 1556 ? 2.6272 2.5348 2.3562 0.3056  -0.3000 -0.0496 1556 GLU A N   
11855 C CA  . GLU A 1556 ? 2.5269 2.4184 2.2424 0.3125  -0.2800 -0.0595 1556 GLU A CA  
11856 C C   . GLU A 1556 ? 2.4881 2.3366 2.1690 0.3475  -0.2859 -0.0761 1556 GLU A C   
11857 O O   . GLU A 1556 ? 2.5083 2.3417 2.1773 0.3562  -0.2708 -0.0860 1556 GLU A O   
11858 C CB  . GLU A 1556 ? 2.4643 2.4033 2.2099 0.2760  -0.2760 -0.0694 1556 GLU A CB  
11859 C CG  . GLU A 1556 ? 2.4064 2.3905 2.1791 0.2490  -0.2995 -0.0769 1556 GLU A CG  
11860 C CD  . GLU A 1556 ? 2.3532 2.3863 2.1619 0.2134  -0.2975 -0.0624 1556 GLU A CD  
11861 O OE1 . GLU A 1556 ? 2.3164 2.3952 2.1521 0.1841  -0.3054 -0.0698 1556 GLU A OE1 
11862 O OE2 . GLU A 1556 ? 2.3545 2.3797 2.1642 0.2151  -0.2875 -0.0432 1556 GLU A OE2 
11863 N N   . ILE A 1557 ? 2.4176 2.2481 2.0850 0.3671  -0.3082 -0.0792 1557 ILE A N   
11864 C CA  . ILE A 1557 ? 2.3519 2.1401 1.9860 0.4021  -0.3173 -0.0948 1557 ILE A CA  
11865 C C   . ILE A 1557 ? 2.3283 2.0667 1.9281 0.4422  -0.3126 -0.0846 1557 ILE A C   
11866 O O   . ILE A 1557 ? 2.3200 2.0464 1.9131 0.4577  -0.3309 -0.0809 1557 ILE A O   
11867 C CB  . ILE A 1557 ? 2.2969 2.0975 1.9401 0.3990  -0.3477 -0.1089 1557 ILE A CB  
11868 C CG1 . ILE A 1557 ? 2.2632 2.0980 1.9283 0.3698  -0.3510 -0.1246 1557 ILE A CG1 
11869 C CG2 . ILE A 1557 ? 2.3072 2.0583 1.9148 0.4406  -0.3605 -0.1191 1557 ILE A CG2 
11870 C CD1 . ILE A 1557 ? 2.2683 2.0846 1.9164 0.3763  -0.3338 -0.1382 1557 ILE A CD1 
11871 N N   . ALA A 1558 ? 2.3040 2.0150 1.8841 0.4593  -0.2875 -0.0802 1558 ALA A N   
11872 C CA  . ALA A 1558 ? 2.2869 1.9522 1.8357 0.4960  -0.2771 -0.0675 1558 ALA A CA  
11873 C C   . ALA A 1558 ? 2.2899 1.9142 1.8032 0.5340  -0.2882 -0.0827 1558 ALA A C   
11874 O O   . ALA A 1558 ? 2.3226 1.9045 1.8039 0.5699  -0.2766 -0.0776 1558 ALA A O   
11875 C CB  . ALA A 1558 ? 2.2788 1.9333 1.8251 0.4995  -0.2452 -0.0563 1558 ALA A CB  
11876 N N   . TYR A 1559 ? 2.2699 1.9069 1.7895 0.5262  -0.3105 -0.1013 1559 TYR A N   
11877 C CA  . TYR A 1559 ? 2.3090 1.9084 1.7975 0.5604  -0.3255 -0.1172 1559 TYR A CA  
11878 C C   . TYR A 1559 ? 2.2872 1.9062 1.7908 0.5439  -0.3479 -0.1374 1559 TYR A C   
11879 O O   . TYR A 1559 ? 2.2278 1.8873 1.7622 0.5077  -0.3476 -0.1408 1559 TYR A O   
11880 C CB  . TYR A 1559 ? 2.3580 1.9177 1.8136 0.5913  -0.3037 -0.1206 1559 TYR A CB  
11881 C CG  . TYR A 1559 ? 2.3682 1.9439 1.8356 0.5728  -0.2868 -0.1311 1559 TYR A CG  
11882 C CD1 . TYR A 1559 ? 2.3772 1.9481 1.8438 0.5761  -0.2565 -0.1215 1559 TYR A CD1 
11883 C CD2 . TYR A 1559 ? 2.3596 1.9543 1.8402 0.5534  -0.3013 -0.1506 1559 TYR A CD2 
11884 C CE1 . TYR A 1559 ? 2.3609 1.9484 1.8417 0.5597  -0.2413 -0.1320 1559 TYR A CE1 
11885 C CE2 . TYR A 1559 ? 2.3385 1.9485 1.8310 0.5359  -0.2861 -0.1606 1559 TYR A CE2 
11886 C CZ  . TYR A 1559 ? 2.3321 1.9398 1.8255 0.5388  -0.2564 -0.1517 1559 TYR A CZ  
11887 O OH  . TYR A 1559 ? 2.3042 1.9299 1.8133 0.5210  -0.2425 -0.1625 1559 TYR A OH  
11888 N N   . ALA A 1560 ? 2.3566 1.9457 1.8385 0.5716  -0.3679 -0.1507 1560 ALA A N   
11889 C CA  . ALA A 1560 ? 2.4104 2.0089 1.9024 0.5610  -0.3871 -0.1705 1560 ALA A CA  
11890 C C   . ALA A 1560 ? 2.5432 2.0909 1.9972 0.6037  -0.3987 -0.1840 1560 ALA A C   
11891 O O   . ALA A 1560 ? 2.5931 2.1198 2.0343 0.6295  -0.4160 -0.1822 1560 ALA A O   
11892 C CB  . ALA A 1560 ? 2.3570 1.9933 1.8845 0.5365  -0.4112 -0.1690 1560 ALA A CB  
11893 N N   . TYR A 1561 ? 2.5892 2.1171 2.0255 0.6119  -0.3881 -0.1972 1561 TYR A N   
11894 C CA  . TYR A 1561 ? 2.6385 2.1163 2.0359 0.6537  -0.3948 -0.2091 1561 TYR A CA  
11895 C C   . TYR A 1561 ? 2.5956 2.0588 1.9836 0.6545  -0.3945 -0.2294 1561 TYR A C   
11896 O O   . TYR A 1561 ? 2.5699 2.0422 1.9617 0.6405  -0.3719 -0.2308 1561 TYR A O   
11897 C CB  . TYR A 1561 ? 2.7496 2.1948 2.1148 0.6881  -0.3756 -0.1954 1561 TYR A CB  
11898 C CG  . TYR A 1561 ? 2.8379 2.2868 2.2014 0.6828  -0.3409 -0.1851 1561 TYR A CG  
11899 C CD1 . TYR A 1561 ? 2.8841 2.3292 2.2427 0.6918  -0.3224 -0.1639 1561 TYR A CD1 
11900 C CD2 . TYR A 1561 ? 2.8743 2.3285 2.2419 0.6710  -0.3265 -0.1963 1561 TYR A CD2 
11901 C CE1 . TYR A 1561 ? 2.9177 2.3642 2.2772 0.6901  -0.2911 -0.1540 1561 TYR A CE1 
11902 C CE2 . TYR A 1561 ? 2.9032 2.3618 2.2733 0.6685  -0.2950 -0.1870 1561 TYR A CE2 
11903 C CZ  . TYR A 1561 ? 2.9233 2.3777 2.2898 0.6789  -0.2776 -0.1658 1561 TYR A CZ  
11904 O OH  . TYR A 1561 ? 2.9312 2.3895 2.3035 0.6779  -0.2464 -0.1560 1561 TYR A OH  
11905 N N   . LYS A 1562 ? 2.5861 2.0265 1.9639 0.6711  -0.4208 -0.2449 1562 LYS A N   
11906 C CA  . LYS A 1562 ? 2.5908 2.0141 1.9610 0.6721  -0.4268 -0.2650 1562 LYS A CA  
11907 C C   . LYS A 1562 ? 2.7458 2.1276 2.0771 0.7057  -0.4091 -0.2695 1562 LYS A C   
11908 O O   . LYS A 1562 ? 2.8698 2.2198 2.1709 0.7431  -0.4078 -0.2636 1562 LYS A O   
11909 C CB  . LYS A 1562 ? 2.5050 1.9140 1.8776 0.6827  -0.4619 -0.2785 1562 LYS A CB  
11910 C CG  . LYS A 1562 ? 2.4094 1.8189 1.7937 0.6652  -0.4731 -0.2968 1562 LYS A CG  
11911 C CD  . LYS A 1562 ? 2.3785 1.7375 1.7263 0.6981  -0.4751 -0.3124 1562 LYS A CD  
11912 C CE  . LYS A 1562 ? 2.3334 1.6579 1.6653 0.7326  -0.5051 -0.3207 1562 LYS A CE  
11913 N NZ  . LYS A 1562 ? 2.2705 1.6065 1.6318 0.7147  -0.5333 -0.3317 1562 LYS A NZ  
11914 N N   . VAL A 1563 ? 2.7367 2.1209 2.0710 0.6915  -0.3954 -0.2797 1563 VAL A N   
11915 C CA  . VAL A 1563 ? 2.8022 2.1569 2.1083 0.7160  -0.3732 -0.2828 1563 VAL A CA  
11916 C C   . VAL A 1563 ? 2.8031 2.1571 2.1159 0.6994  -0.3719 -0.3006 1563 VAL A C   
11917 O O   . VAL A 1563 ? 2.7135 2.0910 2.0529 0.6675  -0.3862 -0.3091 1563 VAL A O   
11918 C CB  . VAL A 1563 ? 2.8738 2.2493 2.1886 0.7072  -0.3394 -0.2661 1563 VAL A CB  
11919 C CG1 . VAL A 1563 ? 2.9170 2.3052 2.2371 0.7090  -0.3385 -0.2462 1563 VAL A CG1 
11920 C CG2 . VAL A 1563 ? 2.8618 2.2799 2.2134 0.6622  -0.3261 -0.2693 1563 VAL A CG2 
11921 N N   . SER A 1564 ? 2.9103 2.2389 2.2006 0.7205  -0.3534 -0.3052 1564 SER A N   
11922 C CA  . SER A 1564 ? 2.9645 2.2902 2.2601 0.7064  -0.3488 -0.3213 1564 SER A CA  
11923 C C   . SER A 1564 ? 3.0256 2.3536 2.3185 0.7117  -0.3145 -0.3163 1564 SER A C   
11924 O O   . SER A 1564 ? 3.0586 2.3670 2.3285 0.7447  -0.2996 -0.3054 1564 SER A O   
11925 C CB  . SER A 1564 ? 2.9618 2.2415 2.2283 0.7350  -0.3705 -0.3379 1564 SER A CB  
11926 O OG  . SER A 1564 ? 2.9254 2.1968 2.1924 0.7264  -0.3611 -0.3516 1564 SER A OG  
11927 N N   . ILE A 1565 ? 3.0562 2.4089 2.3747 0.6798  -0.3019 -0.3240 1565 ILE A N   
11928 C CA  . ILE A 1565 ? 3.1441 2.5057 2.4693 0.6807  -0.2688 -0.3202 1565 ILE A CA  
11929 C C   . ILE A 1565 ? 3.2776 2.5967 2.5703 0.7176  -0.2626 -0.3283 1565 ILE A C   
11930 O O   . ILE A 1565 ? 3.2667 2.5684 2.5536 0.7142  -0.2748 -0.3453 1565 ILE A O   
11931 C CB  . ILE A 1565 ? 3.1151 2.5173 2.4799 0.6348  -0.2585 -0.3280 1565 ILE A CB  
11932 C CG1 . ILE A 1565 ? 3.1034 2.5501 2.5007 0.5982  -0.2639 -0.3200 1565 ILE A CG1 
11933 C CG2 . ILE A 1565 ? 3.1178 2.5319 2.4947 0.6365  -0.2241 -0.3242 1565 ILE A CG2 
11934 C CD1 . ILE A 1565 ? 3.1050 2.5531 2.5061 0.5826  -0.2969 -0.3278 1565 ILE A CD1 
11935 N N   . THR A 1566 ? 3.4164 2.7183 2.6884 0.7531  -0.2434 -0.3157 1566 THR A N   
11936 C CA  . THR A 1566 ? 3.5420 2.8084 2.7857 0.7890  -0.2326 -0.3212 1566 THR A CA  
11937 C C   . THR A 1566 ? 3.6614 2.9489 2.9275 0.7811  -0.1983 -0.3179 1566 THR A C   
11938 O O   . THR A 1566 ? 3.7028 2.9686 2.9542 0.8026  -0.1877 -0.3245 1566 THR A O   
11939 C CB  . THR A 1566 ? 3.5305 2.7600 2.7338 0.8396  -0.2337 -0.3104 1566 THR A CB  
11940 O OG1 . THR A 1566 ? 3.5048 2.7526 2.7179 0.8443  -0.2113 -0.2891 1566 THR A OG1 
11941 C CG2 . THR A 1566 ? 3.5246 2.7328 2.7077 0.8496  -0.2685 -0.3154 1566 THR A CG2 
11942 N N   . SER A 1567 ? 3.7244 3.0552 3.0282 0.7506  -0.1811 -0.3081 1567 SER A N   
11943 C CA  . SER A 1567 ? 3.7906 3.1456 3.1223 0.7423  -0.1485 -0.3049 1567 SER A CA  
11944 C C   . SER A 1567 ? 3.8336 3.2410 3.2143 0.6941  -0.1389 -0.3044 1567 SER A C   
11945 O O   . SER A 1567 ? 3.8429 3.2742 3.2414 0.6856  -0.1292 -0.2894 1567 SER A O   
11946 C CB  . SER A 1567 ? 3.8140 3.1576 3.1339 0.7808  -0.1232 -0.2858 1567 SER A CB  
11947 O OG  . SER A 1567 ? 3.7944 3.1648 3.1475 0.7730  -0.0914 -0.2818 1567 SER A OG  
11948 N N   . ILE A 1568 ? 3.8762 3.3005 3.2789 0.6628  -0.1414 -0.3208 1568 ILE A N   
11949 C CA  . ILE A 1568 ? 3.8985 3.3732 3.3495 0.6202  -0.1273 -0.3220 1568 ILE A CA  
11950 C C   . ILE A 1568 ? 3.9069 3.3890 3.3766 0.6144  -0.1077 -0.3328 1568 ILE A C   
11951 O O   . ILE A 1568 ? 3.8983 3.3824 3.3754 0.5906  -0.1185 -0.3499 1568 ILE A O   
11952 C CB  . ILE A 1568 ? 3.9064 3.4045 3.3736 0.5786  -0.1518 -0.3310 1568 ILE A CB  
11953 C CG1 . ILE A 1568 ? 3.8781 3.4291 3.3947 0.5360  -0.1361 -0.3332 1568 ILE A CG1 
11954 C CG2 . ILE A 1568 ? 3.9223 3.3928 3.3702 0.5753  -0.1767 -0.3495 1568 ILE A CG2 
11955 C CD1 . ILE A 1568 ? 3.8752 3.4517 3.4152 0.5412  -0.1082 -0.3163 1568 ILE A CD1 
11956 N N   . THR A 1569 ? 3.9104 3.3964 3.3894 0.6370  -0.0783 -0.3219 1569 THR A N   
11957 C CA  . THR A 1569 ? 3.8846 3.3726 3.3780 0.6420  -0.0574 -0.3295 1569 THR A CA  
11958 C C   . THR A 1569 ? 3.8387 3.3600 3.3697 0.5957  -0.0579 -0.3465 1569 THR A C   
11959 O O   . THR A 1569 ? 3.8084 3.3750 3.3828 0.5652  -0.0448 -0.3445 1569 THR A O   
11960 C CB  . THR A 1569 ? 3.8641 3.3668 3.3783 0.6648  -0.0229 -0.3129 1569 THR A CB  
11961 O OG1 . THR A 1569 ? 3.8401 3.3730 3.3788 0.6502  -0.0166 -0.2991 1569 THR A OG1 
11962 C CG2 . THR A 1569 ? 3.9006 3.3588 3.3718 0.7192  -0.0183 -0.3018 1569 THR A CG2 
11963 N N   . VAL A 1570 ? 3.8316 3.3288 3.3454 0.5913  -0.0734 -0.3631 1570 VAL A N   
11964 C CA  . VAL A 1570 ? 3.7866 3.3084 3.3312 0.5485  -0.0763 -0.3800 1570 VAL A CA  
11965 C C   . VAL A 1570 ? 3.7517 3.3178 3.3467 0.5312  -0.0446 -0.3789 1570 VAL A C   
11966 O O   . VAL A 1570 ? 3.7142 3.3220 3.3483 0.4905  -0.0424 -0.3849 1570 VAL A O   
11967 C CB  . VAL A 1570 ? 3.7902 3.2733 3.3094 0.5550  -0.0898 -0.3961 1570 VAL A CB  
11968 C CG1 . VAL A 1570 ? 3.7488 3.2563 3.3004 0.5088  -0.0931 -0.4128 1570 VAL A CG1 
11969 C CG2 . VAL A 1570 ? 3.8242 3.2619 3.2957 0.5755  -0.1219 -0.3981 1570 VAL A CG2 
11970 N N   . GLU A 1571 ? 3.7650 3.3229 3.3604 0.5637  -0.0200 -0.3710 1571 GLU A N   
11971 C CA  . GLU A 1571 ? 3.7359 3.3353 3.3822 0.5536  0.0120  -0.3684 1571 GLU A CA  
11972 C C   . GLU A 1571 ? 3.7372 3.3853 3.4249 0.5242  0.0190  -0.3619 1571 GLU A C   
11973 O O   . GLU A 1571 ? 3.7446 3.3899 3.4183 0.5316  0.0106  -0.3498 1571 GLU A O   
11974 C CB  . GLU A 1571 ? 3.7301 3.3141 3.3689 0.6006  0.0370  -0.3539 1571 GLU A CB  
11975 C CG  . GLU A 1571 ? 3.7385 3.2773 3.3389 0.6325  0.0336  -0.3597 1571 GLU A CG  
11976 C CD  . GLU A 1571 ? 3.7740 3.2615 3.3131 0.6665  0.0100  -0.3550 1571 GLU A CD  
11977 O OE1 . GLU A 1571 ? 3.7776 3.2650 3.3048 0.6622  -0.0053 -0.3479 1571 GLU A OE1 
11978 O OE2 . GLU A 1571 ? 3.8025 3.2505 3.3064 0.6979  0.0066  -0.3584 1571 GLU A OE2 
11979 N N   . ASN A 1572 ? 3.7360 3.4290 3.4756 0.4906  0.0340  -0.3705 1572 ASN A N   
11980 C CA  . ASN A 1572 ? 3.7481 3.4908 3.5320 0.4622  0.0424  -0.3661 1572 ASN A CA  
11981 C C   . ASN A 1572 ? 3.7896 3.5453 3.5940 0.4901  0.0689  -0.3466 1572 ASN A C   
11982 O O   . ASN A 1572 ? 3.7946 3.5332 3.5946 0.5252  0.0876  -0.3391 1572 ASN A O   
11983 C CB  . ASN A 1572 ? 3.7060 3.4931 3.5407 0.4193  0.0505  -0.3823 1572 ASN A CB  
11984 C CG  . ASN A 1572 ? 3.7056 3.4820 3.5239 0.3881  0.0243  -0.4005 1572 ASN A CG  
11985 O OD1 . ASN A 1572 ? 3.7274 3.4780 3.5078 0.3879  -0.0023 -0.4006 1572 ASN A OD1 
11986 N ND2 . ASN A 1572 ? 3.6774 3.4743 3.5271 0.3616  0.0320  -0.4157 1572 ASN A ND2 
11987 N N   . VAL A 1573 ? 3.8246 3.6100 3.6521 0.4749  0.0706  -0.3380 1573 VAL A N   
11988 C CA  . VAL A 1573 ? 3.8652 3.6618 3.7138 0.4993  0.0941  -0.3183 1573 VAL A CA  
11989 C C   . VAL A 1573 ? 3.9565 3.7066 3.7550 0.5426  0.0889  -0.3002 1573 VAL A C   
11990 O O   . VAL A 1573 ? 3.9872 3.7419 3.7957 0.5591  0.1018  -0.2823 1573 VAL A O   
11991 C CB  . VAL A 1573 ? 3.8308 3.6497 3.7247 0.5117  0.1267  -0.3170 1573 VAL A CB  
11992 C CG1 . VAL A 1573 ? 3.8239 3.6538 3.7430 0.5373  0.1505  -0.2957 1573 VAL A CG1 
11993 C CG2 . VAL A 1573 ? 3.7778 3.6459 3.7252 0.4678  0.1322  -0.3347 1573 VAL A CG2 
11994 N N   . PHE A 1574 ? 4.0050 3.7103 3.7509 0.5607  0.0697  -0.3052 1574 PHE A N   
11995 C CA  . PHE A 1574 ? 4.0689 3.7289 3.7642 0.6009  0.0613  -0.2903 1574 PHE A CA  
11996 C C   . PHE A 1574 ? 4.0212 3.6845 3.7056 0.5876  0.0436  -0.2816 1574 PHE A C   
11997 O O   . PHE A 1574 ? 3.9976 3.6872 3.6977 0.5475  0.0282  -0.2915 1574 PHE A O   
11998 C CB  . PHE A 1574 ? 4.1847 3.7978 3.8286 0.6208  0.0422  -0.3004 1574 PHE A CB  
11999 C CG  . PHE A 1574 ? 4.2894 3.8833 3.9274 0.6553  0.0619  -0.2997 1574 PHE A CG  
12000 C CD1 . PHE A 1574 ? 4.3012 3.9285 3.9877 0.6456  0.0881  -0.3034 1574 PHE A CD1 
12001 C CD2 . PHE A 1574 ? 4.3703 3.9140 3.9556 0.6976  0.0538  -0.2958 1574 PHE A CD2 
12002 C CE1 . PHE A 1574 ? 4.3359 3.9481 4.0195 0.6772  0.1068  -0.3020 1574 PHE A CE1 
12003 C CE2 . PHE A 1574 ? 4.4089 3.9361 3.9883 0.7298  0.0719  -0.2949 1574 PHE A CE2 
12004 C CZ  . PHE A 1574 ? 4.3854 3.9471 4.0143 0.7194  0.0988  -0.2976 1574 PHE A CZ  
12005 N N   . VAL A 1575 ? 3.9911 3.6282 3.6496 0.6211  0.0463  -0.2627 1575 VAL A N   
12006 C CA  . VAL A 1575 ? 3.9179 3.5603 3.5709 0.6093  0.0332  -0.2519 1575 VAL A CA  
12007 C C   . VAL A 1575 ? 3.8454 3.4574 3.4514 0.6098  -0.0003 -0.2564 1575 VAL A C   
12008 O O   . VAL A 1575 ? 3.8453 3.4348 3.4253 0.6127  -0.0166 -0.2711 1575 VAL A O   
12009 C CB  . VAL A 1575 ? 3.8221 3.4601 3.4825 0.6371  0.0546  -0.2276 1575 VAL A CB  
12010 C CG1 . VAL A 1575 ? 3.7798 3.4638 3.5013 0.6185  0.0807  -0.2241 1575 VAL A CG1 
12011 C CG2 . VAL A 1575 ? 3.8569 3.4525 3.4843 0.6893  0.0667  -0.2172 1575 VAL A CG2 
12012 N N   . LYS A 1576 ? 3.7519 3.3632 3.3495 0.6080  -0.0096 -0.2431 1576 LYS A N   
12013 C CA  . LYS A 1576 ? 3.6395 3.2465 3.2164 0.5891  -0.0411 -0.2482 1576 LYS A CA  
12014 C C   . LYS A 1576 ? 3.5970 3.1575 3.1221 0.6153  -0.0656 -0.2528 1576 LYS A C   
12015 O O   . LYS A 1576 ? 3.6243 3.1506 3.1225 0.6507  -0.0598 -0.2537 1576 LYS A O   
12016 C CB  . LYS A 1576 ? 3.5913 3.2171 3.1817 0.5764  -0.0415 -0.2318 1576 LYS A CB  
12017 C CG  . LYS A 1576 ? 3.5184 3.1972 3.1610 0.5357  -0.0303 -0.2339 1576 LYS A CG  
12018 C CD  . LYS A 1576 ? 3.4803 3.1753 3.1571 0.5436  0.0017  -0.2316 1576 LYS A CD  
12019 C CE  . LYS A 1576 ? 3.4138 3.1629 3.1444 0.5025  0.0110  -0.2378 1576 LYS A CE  
12020 N NZ  . LYS A 1576 ? 3.3773 3.1477 3.1183 0.4687  -0.0034 -0.2606 1576 LYS A NZ  
12021 N N   . TYR A 1577 ? 3.5183 3.0800 3.0325 0.5973  -0.0930 -0.2559 1577 TYR A N   
12022 C CA  . TYR A 1577 ? 3.4755 2.9989 2.9478 0.6161  -0.1206 -0.2628 1577 TYR A CA  
12023 C C   . TYR A 1577 ? 3.4975 2.9810 2.9317 0.6610  -0.1207 -0.2477 1577 TYR A C   
12024 O O   . TYR A 1577 ? 3.4930 2.9789 2.9329 0.6749  -0.1015 -0.2295 1577 TYR A O   
12025 C CB  . TYR A 1577 ? 3.4118 2.9523 2.8897 0.5847  -0.1490 -0.2680 1577 TYR A CB  
12026 C CG  . TYR A 1577 ? 3.3412 2.9221 2.8550 0.5386  -0.1527 -0.2818 1577 TYR A CG  
12027 C CD1 . TYR A 1577 ? 3.3015 2.9266 2.8499 0.5043  -0.1495 -0.2756 1577 TYR A CD1 
12028 C CD2 . TYR A 1577 ? 3.3239 2.8982 2.8368 0.5294  -0.1598 -0.3009 1577 TYR A CD2 
12029 C CE1 . TYR A 1577 ? 3.2591 2.9221 2.8396 0.4631  -0.1531 -0.2883 1577 TYR A CE1 
12030 C CE2 . TYR A 1577 ? 3.2807 2.8914 2.8262 0.4872  -0.1631 -0.3132 1577 TYR A CE2 
12031 C CZ  . TYR A 1577 ? 3.2426 2.8982 2.8214 0.4547  -0.1598 -0.3070 1577 TYR A CZ  
12032 O OH  . TYR A 1577 ? 3.1914 2.8842 2.8020 0.4137  -0.1632 -0.3192 1577 TYR A OH  
12033 N N   . LYS A 1578 ? 3.5150 2.9613 2.9113 0.6837  -0.1431 -0.2557 1578 LYS A N   
12034 C CA  . LYS A 1578 ? 3.5384 2.9461 2.8959 0.7249  -0.1497 -0.2442 1578 LYS A CA  
12035 C C   . LYS A 1578 ? 3.5673 2.9485 2.8971 0.7316  -0.1823 -0.2595 1578 LYS A C   
12036 O O   . LYS A 1578 ? 3.5664 2.9406 2.8943 0.7256  -0.1894 -0.2771 1578 LYS A O   
12037 C CB  . LYS A 1578 ? 3.5398 2.9190 2.8768 0.7680  -0.1260 -0.2371 1578 LYS A CB  
12038 C CG  . LYS A 1578 ? 3.4961 2.9007 2.8666 0.7582  -0.0946 -0.2358 1578 LYS A CG  
12039 C CD  . LYS A 1578 ? 3.4998 2.8916 2.8654 0.7945  -0.0662 -0.2157 1578 LYS A CD  
12040 C CE  . LYS A 1578 ? 3.5399 2.8847 2.8605 0.8448  -0.0663 -0.2158 1578 LYS A CE  
12041 N NZ  . LYS A 1578 ? 3.5576 2.8918 2.8767 0.8809  -0.0361 -0.1959 1578 LYS A NZ  
12042 N N   . ALA A 1579 ? 3.5959 2.9623 2.9066 0.7440  -0.2025 -0.2529 1579 ALA A N   
12043 C CA  . ALA A 1579 ? 3.6105 2.9558 2.9018 0.7482  -0.2356 -0.2674 1579 ALA A CA  
12044 C C   . ALA A 1579 ? 3.6280 2.9349 2.8811 0.7902  -0.2490 -0.2603 1579 ALA A C   
12045 O O   . ALA A 1579 ? 3.6899 2.9965 2.9386 0.8038  -0.2380 -0.2418 1579 ALA A O   
12046 C CB  . ALA A 1579 ? 3.5924 2.9731 2.9142 0.7049  -0.2550 -0.2714 1579 ALA A CB  
12047 N N   . THR A 1580 ? 3.5755 2.8493 2.8017 0.8112  -0.2727 -0.2752 1580 THR A N   
12048 C CA  . THR A 1580 ? 3.5649 2.8025 2.7556 0.8510  -0.2900 -0.2718 1580 THR A CA  
12049 C C   . THR A 1580 ? 3.5445 2.7947 2.7473 0.8349  -0.3194 -0.2719 1580 THR A C   
12050 O O   . THR A 1580 ? 3.5110 2.7737 2.7317 0.8094  -0.3401 -0.2854 1580 THR A O   
12051 C CB  . THR A 1580 ? 4.0450 3.2377 3.1993 0.8872  -0.3013 -0.2880 1580 THR A CB  
12052 O OG1 . THR A 1580 ? 4.0624 3.2438 3.2052 0.9062  -0.2726 -0.2857 1580 THR A OG1 
12053 C CG2 . THR A 1580 ? 4.0739 3.2312 3.1930 0.9285  -0.3207 -0.2855 1580 THR A CG2 
12054 N N   . LEU A 1581 ? 3.5493 2.7963 2.7439 0.8504  -0.3205 -0.2559 1581 LEU A N   
12055 C CA  . LEU A 1581 ? 3.5197 2.7834 2.7304 0.8349  -0.3451 -0.2526 1581 LEU A CA  
12056 C C   . LEU A 1581 ? 3.5957 2.8263 2.7830 0.8632  -0.3771 -0.2666 1581 LEU A C   
12057 O O   . LEU A 1581 ? 3.6555 2.8457 2.8054 0.9053  -0.3769 -0.2703 1581 LEU A O   
12058 C CB  . LEU A 1581 ? 3.4358 2.7072 2.6471 0.8412  -0.3324 -0.2295 1581 LEU A CB  
12059 C CG  . LEU A 1581 ? 3.2910 2.6066 2.5411 0.8007  -0.3368 -0.2185 1581 LEU A CG  
12060 C CD1 . LEU A 1581 ? 3.2466 2.5714 2.5008 0.8010  -0.3114 -0.1946 1581 LEU A CD1 
12061 C CD2 . LEU A 1581 ? 3.2461 2.5625 2.5010 0.8014  -0.3705 -0.2229 1581 LEU A CD2 
12062 N N   . LEU A 1582 ? 3.5903 2.8382 2.8009 0.8414  -0.4046 -0.2744 1582 LEU A N   
12063 C CA  . LEU A 1582 ? 3.6228 2.8412 2.8180 0.8661  -0.4371 -0.2896 1582 LEU A CA  
12064 C C   . LEU A 1582 ? 3.6511 2.8726 2.8518 0.8768  -0.4597 -0.2823 1582 LEU A C   
12065 O O   . LEU A 1582 ? 3.6526 2.8413 2.8307 0.9118  -0.4811 -0.2910 1582 LEU A O   
12066 C CB  . LEU A 1582 ? 3.5933 2.8215 2.8110 0.8395  -0.4554 -0.3076 1582 LEU A CB  
12067 C CG  . LEU A 1582 ? 3.5970 2.8072 2.8027 0.8392  -0.4448 -0.3222 1582 LEU A CG  
12068 C CD1 . LEU A 1582 ? 3.5783 2.8129 2.7944 0.8175  -0.4098 -0.3124 1582 LEU A CD1 
12069 C CD2 . LEU A 1582 ? 3.5776 2.7971 2.8081 0.8126  -0.4673 -0.3379 1582 LEU A CD2 
12070 N N   . ASP A 1583 ? 3.6661 2.9282 2.8990 0.8456  -0.4554 -0.2671 1583 ASP A N   
12071 C CA  . ASP A 1583 ? 3.6890 2.9639 2.9372 0.8470  -0.4755 -0.2588 1583 ASP A CA  
12072 C C   . ASP A 1583 ? 2.9867 2.3089 2.2688 0.8079  -0.4587 -0.2389 1583 ASP A C   
12073 O O   . ASP A 1583 ? 2.8943 2.2493 2.2044 0.7698  -0.4513 -0.2404 1583 ASP A O   
12074 C CB  . ASP A 1583 ? 3.7771 3.0555 3.0461 0.8416  -0.5112 -0.2753 1583 ASP A CB  
12075 C CG  . ASP A 1583 ? 3.4608 2.6890 2.6962 0.8848  -0.5312 -0.2943 1583 ASP A CG  
12076 O OD1 . ASP A 1583 ? 3.5187 2.7148 2.7207 0.9247  -0.5312 -0.2916 1583 ASP A OD1 
12077 O OD2 . ASP A 1583 ? 3.4178 2.6376 2.6602 0.8793  -0.5477 -0.3119 1583 ASP A OD2 
12078 N N   . ILE A 1584 ? 3.0653 2.3893 2.3436 0.8177  -0.4516 -0.2206 1584 ILE A N   
12079 C CA  . ILE A 1584 ? 3.0733 2.4384 2.3823 0.7829  -0.4359 -0.2005 1584 ILE A CA  
12080 C C   . ILE A 1584 ? 3.0320 2.4307 2.3770 0.7619  -0.4583 -0.1947 1584 ILE A C   
12081 O O   . ILE A 1584 ? 3.0621 2.4477 2.4010 0.7849  -0.4752 -0.1918 1584 ILE A O   
12082 C CB  . ILE A 1584 ? 2.4053 1.7549 1.6932 0.8015  -0.4111 -0.1799 1584 ILE A CB  
12083 C CG1 . ILE A 1584 ? 2.5089 1.8309 1.7666 0.8214  -0.3838 -0.1807 1584 ILE A CG1 
12084 C CG2 . ILE A 1584 ? 2.3057 1.6970 1.6280 0.7640  -0.3978 -0.1602 1584 ILE A CG2 
12085 C CD1 . ILE A 1584 ? 2.5684 1.8784 1.8114 0.8366  -0.3576 -0.1586 1584 ILE A CD1 
12086 N N   . TYR A 1585 ? 2.9897 2.4342 2.3744 0.7181  -0.4574 -0.1920 1585 TYR A N   
12087 C CA  . TYR A 1585 ? 3.0015 2.4829 2.4247 0.6960  -0.4769 -0.1853 1585 TYR A CA  
12088 C C   . TYR A 1585 ? 3.0700 2.5756 2.5078 0.6785  -0.4593 -0.1613 1585 TYR A C   
12089 O O   . TYR A 1585 ? 3.0923 2.6059 2.5422 0.6826  -0.4714 -0.1510 1585 TYR A O   
12090 C CB  . TYR A 1585 ? 2.9784 2.4976 2.4382 0.6591  -0.4875 -0.1951 1585 TYR A CB  
12091 C CG  . TYR A 1585 ? 3.0416 2.5364 2.4893 0.6725  -0.5033 -0.2181 1585 TYR A CG  
12092 C CD1 . TYR A 1585 ? 3.0936 2.5537 2.5240 0.7086  -0.5279 -0.2299 1585 TYR A CD1 
12093 C CD2 . TYR A 1585 ? 3.0444 2.5512 2.4999 0.6482  -0.4943 -0.2281 1585 TYR A CD2 
12094 C CE1 . TYR A 1585 ? 3.1161 2.5519 2.5366 0.7202  -0.5429 -0.2508 1585 TYR A CE1 
12095 C CE2 . TYR A 1585 ? 3.0679 2.5513 2.5136 0.6583  -0.5085 -0.2484 1585 TYR A CE2 
12096 C CZ  . TYR A 1585 ? 3.0994 2.5463 2.5274 0.6942  -0.5327 -0.2595 1585 TYR A CZ  
12097 O OH  . TYR A 1585 ? 3.1020 2.5239 2.5212 0.7034  -0.5466 -0.2795 1585 TYR A OH  
12098 N N   . LYS A 1586 ? 3.1307 2.6480 2.5694 0.6588  -0.4310 -0.1525 1586 LYS A N   
12099 C CA  . LYS A 1586 ? 3.1845 2.7181 2.6334 0.6443  -0.4107 -0.1295 1586 LYS A CA  
12100 C C   . LYS A 1586 ? 3.2713 2.7693 2.6849 0.6680  -0.3817 -0.1231 1586 LYS A C   
12101 O O   . LYS A 1586 ? 3.2802 2.7771 2.6889 0.6617  -0.3656 -0.1306 1586 LYS A O   
12102 C CB  . LYS A 1586 ? 3.1536 2.7409 2.6448 0.5946  -0.4032 -0.1234 1586 LYS A CB  
12103 C CG  . LYS A 1586 ? 3.2246 2.8553 2.7574 0.5678  -0.4245 -0.1176 1586 LYS A CG  
12104 C CD  . LYS A 1586 ? 2.0892 1.7747 1.6630 0.5189  -0.4168 -0.1126 1586 LYS A CD  
12105 C CE  . LYS A 1586 ? 2.0545 1.7611 1.6434 0.4980  -0.3963 -0.0893 1586 LYS A CE  
12106 N NZ  . LYS A 1586 ? 2.0121 1.7387 1.6243 0.4912  -0.4103 -0.0749 1586 LYS A NZ  
12107 N N   . THR A 1587 ? 3.3487 2.8181 2.7391 0.6962  -0.3750 -0.1091 1587 THR A N   
12108 C CA  . THR A 1587 ? 3.4402 2.8718 2.7956 0.7253  -0.3487 -0.1026 1587 THR A CA  
12109 C C   . THR A 1587 ? 3.4895 2.9422 2.8628 0.6986  -0.3189 -0.0884 1587 THR A C   
12110 O O   . THR A 1587 ? 3.4765 2.9498 2.8709 0.6780  -0.3116 -0.0699 1587 THR A O   
12111 C CB  . THR A 1587 ? 3.9320 3.3259 3.2572 0.7641  -0.3484 -0.0900 1587 THR A CB  
12112 O OG1 . THR A 1587 ? 3.9539 3.3272 3.2625 0.7917  -0.3767 -0.1048 1587 THR A OG1 
12113 C CG2 . THR A 1587 ? 3.9584 3.3136 3.2482 0.7961  -0.3206 -0.0831 1587 THR A CG2 
12114 N N   . GLY A 1588 ? 3.5527 3.0006 2.9195 0.6990  -0.3021 -0.0973 1588 GLY A N   
12115 C CA  . GLY A 1588 ? 3.6021 3.0673 2.9861 0.6785  -0.2731 -0.0854 1588 GLY A CA  
12116 C C   . GLY A 1588 ? 3.6832 3.1253 3.0540 0.6979  -0.2538 -0.0617 1588 GLY A C   
12117 O O   . GLY A 1588 ? 3.7093 3.1107 3.0455 0.7380  -0.2552 -0.0585 1588 GLY A O   
12118 N N   . GLU A 1589 ? 3.7262 3.1931 3.1243 0.6700  -0.2365 -0.0449 1589 GLU A N   
12119 C CA  . GLU A 1589 ? 3.8017 3.2462 3.1909 0.6855  -0.2156 -0.0206 1589 GLU A CA  
12120 C C   . GLU A 1589 ? 3.9181 3.3300 3.2851 0.7168  -0.1882 -0.0173 1589 GLU A C   
12121 O O   . GLU A 1589 ? 3.9000 3.3091 3.2770 0.7149  -0.1630 0.0006  1589 GLU A O   
12122 C CB  . GLU A 1589 ? 3.7400 3.2210 3.1679 0.6448  -0.2050 -0.0042 1589 GLU A CB  
12123 C CG  . GLU A 1589 ? 3.6806 3.2048 3.1395 0.6067  -0.2288 -0.0076 1589 GLU A CG  
12124 C CD  . GLU A 1589 ? 3.6252 3.1923 3.1250 0.5624  -0.2166 0.0028  1589 GLU A CD  
12125 O OE1 . GLU A 1589 ? 3.6031 3.1964 3.1214 0.5411  -0.2101 -0.0087 1589 GLU A OE1 
12126 O OE2 . GLU A 1589 ? 3.6026 3.1780 3.1171 0.5484  -0.2138 0.0222  1589 GLU A OE2 
12127 N N   . ALA A 1590 ? 4.0536 3.4411 3.3926 0.7463  -0.1930 -0.0342 1590 ALA A N   
12128 C CA  . ALA A 1590 ? 4.1902 3.5508 3.5110 0.7761  -0.1677 -0.0329 1590 ALA A CA  
12129 C C   . ALA A 1590 ? 4.3481 3.6635 3.6232 0.8255  -0.1745 -0.0411 1590 ALA A C   
12130 O O   . ALA A 1590 ? 4.3533 3.6596 3.6118 0.8351  -0.2013 -0.0522 1590 ALA A O   
12131 C CB  . ALA A 1590 ? 4.1682 3.5577 3.5138 0.7516  -0.1581 -0.0474 1590 ALA A CB  
12132 N N   . VAL A 1591 ? 4.4936 3.7823 3.7509 0.8573  -0.1500 -0.0356 1591 VAL A N   
12133 C CA  . VAL A 1591 ? 4.6553 3.8994 3.8677 0.9080  -0.1519 -0.0400 1591 VAL A CA  
12134 C C   . VAL A 1591 ? 4.7725 4.0128 3.9710 0.9161  -0.1665 -0.0666 1591 VAL A C   
12135 O O   . VAL A 1591 ? 4.7600 4.0177 3.9755 0.9015  -0.1551 -0.0768 1591 VAL A O   
12136 C CB  . VAL A 1591 ? 4.6829 3.8996 3.8822 0.9419  -0.1188 -0.0221 1591 VAL A CB  
12137 C CG1 . VAL A 1591 ? 4.7241 3.9002 3.8794 0.9926  -0.1194 -0.0304 1591 VAL A CG1 
12138 C CG2 . VAL A 1591 ? 4.6886 3.8931 3.8887 0.9468  -0.1080 0.0050  1591 VAL A CG2 
12139 N N   . ALA A 1592 ? 4.8982 4.1148 4.0667 0.9401  -0.1918 -0.0773 1592 ALA A N   
12140 C CA  . ALA A 1592 ? 5.0029 4.2081 4.1531 0.9528  -0.2103 -0.1023 1592 ALA A CA  
12141 C C   . ALA A 1592 ? 5.0665 4.2715 4.2118 0.9497  -0.2459 -0.1121 1592 ALA A C   
12142 O O   . ALA A 1592 ? 5.0452 4.2764 4.2163 0.9201  -0.2557 -0.1042 1592 ALA A O   
12143 C CB  . ALA A 1592 ? 4.9917 4.2284 4.1710 0.9182  -0.2063 -0.1174 1592 ALA A CB  
12144 N N   . GLU A 1593 ? 5.1448 4.3215 4.2596 0.9803  -0.2654 -0.1292 1593 GLU A N   
12145 C CA  . GLU A 1593 ? 5.1829 4.3591 4.2963 0.9799  -0.3004 -0.1400 1593 GLU A CA  
12146 C C   . GLU A 1593 ? 5.0917 4.2567 4.1942 0.9879  -0.3230 -0.1666 1593 GLU A C   
12147 O O   . GLU A 1593 ? 5.1037 4.2496 4.1869 1.0063  -0.3119 -0.1761 1593 GLU A O   
12148 C CB  . GLU A 1593 ? 5.3310 4.4773 4.4162 1.0168  -0.3068 -0.1281 1593 GLU A CB  
12149 C CG  . GLU A 1593 ? 5.4020 4.5620 4.5025 1.0049  -0.3382 -0.1309 1593 GLU A CG  
12150 C CD  . GLU A 1593 ? 5.4087 4.6177 4.5579 0.9513  -0.3400 -0.1235 1593 GLU A CD  
12151 O OE1 . GLU A 1593 ? 5.4067 4.6334 4.5732 0.9292  -0.3142 -0.1073 1593 GLU A OE1 
12152 O OE2 . GLU A 1593 ? 5.4070 4.6372 4.5786 0.9322  -0.3676 -0.1336 1593 GLU A OE2 
12153 N N   . LYS A 1594 ? 4.9733 4.1505 4.0905 0.9741  -0.3546 -0.1779 1594 LYS A N   
12154 C CA  . LYS A 1594 ? 4.8553 4.0308 3.9753 0.9692  -0.3777 -0.2025 1594 LYS A CA  
12155 C C   . LYS A 1594 ? 4.7538 3.8883 3.8348 1.0080  -0.3758 -0.2173 1594 LYS A C   
12156 O O   . LYS A 1594 ? 4.7970 3.8958 3.8437 1.0505  -0.3866 -0.2204 1594 LYS A O   
12157 C CB  . LYS A 1594 ? 4.8630 4.0468 3.9980 0.9640  -0.4137 -0.2107 1594 LYS A CB  
12158 C CG  . LYS A 1594 ? 4.9010 4.0633 4.0162 0.9976  -0.4257 -0.2022 1594 LYS A CG  
12159 C CD  . LYS A 1594 ? 4.8828 4.0739 4.0329 0.9754  -0.4534 -0.2023 1594 LYS A CD  
12160 C CE  . LYS A 1594 ? 4.9171 4.0829 4.0481 1.0132  -0.4753 -0.2037 1594 LYS A CE  
12161 N NZ  . LYS A 1594 ? 4.9464 4.0805 4.0553 1.0446  -0.4995 -0.2277 1594 LYS A NZ  
12162 N N   . ASP A 1595 ? 4.5935 3.7354 3.6820 0.9918  -0.3617 -0.2261 1595 ASP A N   
12163 C CA  . ASP A 1595 ? 4.4745 3.5843 3.5334 1.0200  -0.3573 -0.2407 1595 ASP A CA  
12164 C C   . ASP A 1595 ? 4.3837 3.5029 3.4476 1.0123  -0.3210 -0.2324 1595 ASP A C   
12165 O O   . ASP A 1595 ? 4.3817 3.4938 3.4414 1.0129  -0.3143 -0.2454 1595 ASP A O   
12166 C CB  . ASP A 1595 ? 4.4656 3.5293 3.4783 1.0755  -0.3659 -0.2428 1595 ASP A CB  
12167 C CG  . ASP A 1595 ? 4.4307 3.4749 3.4336 1.0896  -0.4035 -0.2635 1595 ASP A CG  
12168 O OD1 . ASP A 1595 ? 4.3917 3.4559 3.4232 1.0573  -0.4217 -0.2763 1595 ASP A OD1 
12169 O OD2 . ASP A 1595 ? 4.4484 3.4571 3.4162 1.1339  -0.4151 -0.2670 1595 ASP A OD2 
12170 N N   . SER A 1596 ? 4.3008 3.4365 3.3766 1.0047  -0.2977 -0.2105 1596 SER A N   
12171 C CA  . SER A 1596 ? 4.2268 3.3720 3.3112 1.0008  -0.2621 -0.2000 1596 SER A CA  
12172 C C   . SER A 1596 ? 4.1340 3.3174 3.2577 0.9537  -0.2553 -0.2084 1596 SER A C   
12173 O O   . SER A 1596 ? 4.1167 3.3254 3.2656 0.9186  -0.2753 -0.2167 1596 SER A O   
12174 C CB  . SER A 1596 ? 4.2133 3.3654 3.3036 1.0038  -0.2408 -0.1737 1596 SER A CB  
12175 O OG  . SER A 1596 ? 4.1661 3.3596 3.2973 0.9572  -0.2405 -0.1661 1596 SER A OG  
12176 N N   . GLU A 1597 ? 4.0639 3.2523 3.1944 0.9542  -0.2268 -0.2060 1597 GLU A N   
12177 C CA  . GLU A 1597 ? 3.9503 3.1777 3.1209 0.9103  -0.2154 -0.2114 1597 GLU A CA  
12178 C C   . GLU A 1597 ? 3.7579 3.0180 2.9602 0.8850  -0.1960 -0.1916 1597 GLU A C   
12179 O O   . GLU A 1597 ? 3.7788 3.0268 2.9711 0.9080  -0.1788 -0.1722 1597 GLU A O   
12180 C CB  . GLU A 1597 ? 4.0353 3.2555 3.2031 0.9217  -0.1938 -0.2190 1597 GLU A CB  
12181 C CG  . GLU A 1597 ? 4.0479 3.3103 3.2601 0.8791  -0.1760 -0.2217 1597 GLU A CG  
12182 C CD  . GLU A 1597 ? 4.0707 3.3289 3.2849 0.8933  -0.1495 -0.2247 1597 GLU A CD  
12183 O OE1 . GLU A 1597 ? 4.0874 3.3218 3.2802 0.9102  -0.1573 -0.2403 1597 GLU A OE1 
12184 O OE2 . GLU A 1597 ? 4.0624 3.3419 3.3020 0.8873  -0.1208 -0.2114 1597 GLU A OE2 
12185 N N   . ILE A 1598 ? 3.5679 2.8688 2.8087 0.8379  -0.1992 -0.1962 1598 ILE A N   
12186 C CA  . ILE A 1598 ? 3.4597 2.7942 2.7339 0.8111  -0.1804 -0.1795 1598 ILE A CA  
12187 C C   . ILE A 1598 ? 3.3498 2.7232 2.6620 0.7698  -0.1728 -0.1908 1598 ILE A C   
12188 O O   . ILE A 1598 ? 3.3186 2.7069 2.6414 0.7439  -0.1935 -0.2072 1598 ILE A O   
12189 C CB  . ILE A 1598 ? 3.4723 2.8186 2.7536 0.7962  -0.1973 -0.1683 1598 ILE A CB  
12190 C CG1 . ILE A 1598 ? 3.3430 2.7215 2.6580 0.7699  -0.1765 -0.1498 1598 ILE A CG1 
12191 C CG2 . ILE A 1598 ? 3.5786 2.9407 2.8698 0.7698  -0.2297 -0.1847 1598 ILE A CG2 
12192 C CD1 . ILE A 1598 ? 3.2873 2.6448 2.5914 0.8008  -0.1478 -0.1296 1598 ILE A CD1 
12193 N N   . THR A 1599 ? 3.3223 2.7110 2.6557 0.7663  -0.1426 -0.1819 1599 THR A N   
12194 C CA  . THR A 1599 ? 3.3205 2.7437 2.6897 0.7336  -0.1304 -0.1927 1599 THR A CA  
12195 C C   . THR A 1599 ? 3.3022 2.7702 2.7079 0.6843  -0.1404 -0.1941 1599 THR A C   
12196 O O   . THR A 1599 ? 3.3189 2.7905 2.7221 0.6766  -0.1565 -0.1863 1599 THR A O   
12197 C CB  . THR A 1599 ? 3.3497 2.7769 2.7343 0.7480  -0.0946 -0.1804 1599 THR A CB  
12198 O OG1 . THR A 1599 ? 3.3938 2.7864 2.7498 0.7881  -0.0859 -0.1845 1599 THR A OG1 
12199 C CG2 . THR A 1599 ? 3.3344 2.8055 2.7653 0.7100  -0.0800 -0.1873 1599 THR A CG2 
12200 N N   . PHE A 1600 ? 3.2729 2.7759 2.7130 0.6513  -0.1316 -0.2046 1600 PHE A N   
12201 C CA  . PHE A 1600 ? 3.2344 2.7840 2.7127 0.6052  -0.1357 -0.2042 1600 PHE A CA  
12202 C C   . PHE A 1600 ? 3.2238 2.8089 2.7421 0.5816  -0.1112 -0.2075 1600 PHE A C   
12203 O O   . PHE A 1600 ? 3.2154 2.8033 2.7395 0.5773  -0.1071 -0.2231 1600 PHE A O   
12204 C CB  . PHE A 1600 ? 3.1810 2.7419 2.6599 0.5794  -0.1667 -0.2201 1600 PHE A CB  
12205 C CG  . PHE A 1600 ? 3.1392 2.6814 2.5948 0.5912  -0.1922 -0.2144 1600 PHE A CG  
12206 C CD1 . PHE A 1600 ? 3.0991 2.6540 2.5632 0.5848  -0.1920 -0.1963 1600 PHE A CD1 
12207 C CD2 . PHE A 1600 ? 3.1319 2.6452 2.5602 0.6075  -0.2168 -0.2276 1600 PHE A CD2 
12208 C CE1 . PHE A 1600 ? 3.0927 2.6335 2.5396 0.5945  -0.2150 -0.1914 1600 PHE A CE1 
12209 C CE2 . PHE A 1600 ? 3.1228 2.6219 2.5347 0.6185  -0.2406 -0.2232 1600 PHE A CE2 
12210 C CZ  . PHE A 1600 ? 3.1081 2.6221 2.5300 0.6118  -0.2394 -0.2051 1600 PHE A CZ  
12211 N N   . ILE A 1601 ? 3.2253 2.8376 2.7726 0.5662  -0.0953 -0.1931 1601 ILE A N   
12212 C CA  . ILE A 1601 ? 3.2195 2.8638 2.8072 0.5499  -0.0694 -0.1934 1601 ILE A CA  
12213 C C   . ILE A 1601 ? 3.2007 2.8971 2.8297 0.5004  -0.0738 -0.2020 1601 ILE A C   
12214 O O   . ILE A 1601 ? 3.1814 2.8952 2.8157 0.4783  -0.0893 -0.1975 1601 ILE A O   
12215 C CB  . ILE A 1601 ? 2.9468 2.5832 2.5432 0.5726  -0.0427 -0.1709 1601 ILE A CB  
12216 C CG1 . ILE A 1601 ? 2.9430 2.5843 2.5404 0.5632  -0.0499 -0.1535 1601 ILE A CG1 
12217 C CG2 . ILE A 1601 ? 2.9809 2.5704 2.5423 0.6225  -0.0324 -0.1635 1601 ILE A CG2 
12218 C CD1 . ILE A 1601 ? 2.9535 2.5729 2.5479 0.5929  -0.0278 -0.1297 1601 ILE A CD1 
12219 N N   . LYS A 1602 ? 3.2166 2.9386 2.8755 0.4840  -0.0600 -0.2145 1602 LYS A N   
12220 C CA  . LYS A 1602 ? 3.2190 2.9927 2.9213 0.4398  -0.0586 -0.2224 1602 LYS A CA  
12221 C C   . LYS A 1602 ? 3.2986 3.0934 3.0317 0.4313  -0.0394 -0.2355 1602 LYS A C   
12222 O O   . LYS A 1602 ? 3.3071 3.0817 3.0251 0.4453  -0.0393 -0.2470 1602 LYS A O   
12223 C CB  . LYS A 1602 ? 3.1453 2.9371 2.8450 0.4076  -0.0877 -0.2341 1602 LYS A CB  
12224 C CG  . LYS A 1602 ? 3.1083 2.8661 2.7698 0.4214  -0.1115 -0.2448 1602 LYS A CG  
12225 C CD  . LYS A 1602 ? 3.0668 2.7982 2.7145 0.4436  -0.1024 -0.2561 1602 LYS A CD  
12226 C CE  . LYS A 1602 ? 2.9907 2.7533 2.6693 0.4136  -0.0969 -0.2741 1602 LYS A CE  
12227 N NZ  . LYS A 1602 ? 2.9768 2.7163 2.6478 0.4377  -0.0812 -0.2811 1602 LYS A NZ  
12228 N N   . LYS A 1603 ? 3.3676 3.2039 3.1454 0.4077  -0.0237 -0.2339 1603 LYS A N   
12229 C CA  . LYS A 1603 ? 3.4341 3.2965 3.2499 0.3988  -0.0031 -0.2447 1603 LYS A CA  
12230 C C   . LYS A 1603 ? 3.5258 3.4390 3.3776 0.3515  -0.0108 -0.2592 1603 LYS A C   
12231 O O   . LYS A 1603 ? 3.5299 3.4557 3.3752 0.3288  -0.0313 -0.2596 1603 LYS A O   
12232 C CB  . LYS A 1603 ? 3.3841 3.2489 3.2257 0.4201  0.0264  -0.2283 1603 LYS A CB  
12233 C CG  . LYS A 1603 ? 3.2927 3.1997 3.1899 0.4031  0.0485  -0.2363 1603 LYS A CG  
12234 C CD  . LYS A 1603 ? 3.2433 3.1351 3.1477 0.4333  0.0711  -0.2369 1603 LYS A CD  
12235 C CE  . LYS A 1603 ? 3.1632 3.0980 3.1291 0.4207  0.0956  -0.2398 1603 LYS A CE  
12236 N NZ  . LYS A 1603 ? 3.1487 3.0688 3.1264 0.4561  0.1212  -0.2338 1603 LYS A NZ  
12237 N N   . VAL A 1604 ? 3.6108 3.5542 3.5015 0.3373  0.0054  -0.2710 1604 VAL A N   
12238 C CA  . VAL A 1604 ? 3.6797 3.6744 3.6091 0.2937  0.0014  -0.2846 1604 VAL A CA  
12239 C C   . VAL A 1604 ? 3.7773 3.7743 3.6894 0.2694  -0.0238 -0.3020 1604 VAL A C   
12240 O O   . VAL A 1604 ? 3.8070 3.7663 3.6766 0.2845  -0.0414 -0.3018 1604 VAL A O   
12241 C CB  . VAL A 1604 ? 3.7405 3.7632 3.6894 0.2763  0.0000  -0.2725 1604 VAL A CB  
12242 C CG1 . VAL A 1604 ? 3.6996 3.7766 3.6869 0.2322  -0.0052 -0.2871 1604 VAL A CG1 
12243 C CG2 . VAL A 1604 ? 3.7439 3.7639 3.7144 0.2995  0.0256  -0.2552 1604 VAL A CG2 
12244 N N   . THR A 1605 ? 3.8351 3.8760 3.7817 0.2325  -0.0251 -0.3172 1605 THR A N   
12245 C CA  . THR A 1605 ? 3.9114 3.9584 3.8476 0.2065  -0.0476 -0.3335 1605 THR A CA  
12246 C C   . THR A 1605 ? 3.9955 4.0355 3.9048 0.1994  -0.0732 -0.3264 1605 THR A C   
12247 O O   . THR A 1605 ? 3.9884 4.0551 3.9127 0.1855  -0.0747 -0.3172 1605 THR A O   
12248 C CB  . THR A 1605 ? 3.9500 4.0504 3.9317 0.1667  -0.0434 -0.3495 1605 THR A CB  
12249 O OG1 . THR A 1605 ? 3.9320 4.0712 3.9394 0.1471  -0.0428 -0.3425 1605 THR A OG1 
12250 C CG2 . THR A 1605 ? 3.9298 4.0427 3.9451 0.1714  -0.0179 -0.3573 1605 THR A CG2 
12251 N N   . CYS A 1606 ? 4.0699 4.0747 3.9419 0.2092  -0.0932 -0.3308 1606 CYS A N   
12252 C CA  . CYS A 1606 ? 4.1086 4.1099 3.9600 0.2006  -0.1194 -0.3264 1606 CYS A CA  
12253 C C   . CYS A 1606 ? 4.0942 4.0835 3.9306 0.1888  -0.1406 -0.3420 1606 CYS A C   
12254 O O   . CYS A 1606 ? 4.1532 4.0980 3.9548 0.2126  -0.1522 -0.3431 1606 CYS A O   
12255 C CB  . CYS A 1606 ? 4.1652 4.1268 3.9816 0.2346  -0.1245 -0.3091 1606 CYS A CB  
12256 S SG  . CYS A 1606 ? 3.4028 3.3723 3.2068 0.2210  -0.1530 -0.3008 1606 CYS A SG  
12257 N N   . THR A 1607 ? 4.0113 4.0403 3.8750 0.1522  -0.1459 -0.3540 1607 THR A N   
12258 C CA  . THR A 1607 ? 3.9654 3.9876 3.8226 0.1364  -0.1630 -0.3699 1607 THR A CA  
12259 C C   . THR A 1607 ? 3.9544 3.9670 3.7913 0.1331  -0.1917 -0.3661 1607 THR A C   
12260 O O   . THR A 1607 ? 3.9540 3.9855 3.8012 0.1069  -0.2066 -0.3756 1607 THR A O   
12261 C CB  . THR A 1607 ? 4.2691 4.3401 4.1660 0.0974  -0.1566 -0.3841 1607 THR A CB  
12262 O OG1 . THR A 1607 ? 4.2551 4.3518 4.1829 0.0962  -0.1297 -0.3834 1607 THR A OG1 
12263 C CG2 . THR A 1607 ? 4.2622 4.3170 4.1544 0.0878  -0.1638 -0.4016 1607 THR A CG2 
12264 N N   . ASN A 1608 ? 3.9348 3.9190 3.7450 0.1601  -0.1995 -0.3519 1608 ASN A N   
12265 C CA  . ASN A 1608 ? 3.8862 3.8696 3.6851 0.1561  -0.2254 -0.3460 1608 ASN A CA  
12266 C C   . ASN A 1608 ? 3.8413 3.7742 3.6019 0.1916  -0.2400 -0.3386 1608 ASN A C   
12267 O O   . ASN A 1608 ? 3.8444 3.7795 3.5991 0.1947  -0.2554 -0.3277 1608 ASN A O   
12268 C CB  . ASN A 1608 ? 3.8817 3.9093 3.7037 0.1373  -0.2235 -0.3334 1608 ASN A CB  
12269 C CG  . ASN A 1608 ? 3.8460 3.9266 3.7067 0.1011  -0.2126 -0.3418 1608 ASN A CG  
12270 O OD1 . ASN A 1608 ? 3.8339 3.9396 3.7157 0.0961  -0.1929 -0.3365 1608 ASN A OD1 
12271 N ND2 . ASN A 1608 ? 3.8261 3.9232 3.6969 0.0766  -0.2256 -0.3550 1608 ASN A ND2 
12272 N N   . ALA A 1609 ? 3.7804 3.6698 3.5169 0.2180  -0.2354 -0.3449 1609 ALA A N   
12273 C CA  . ALA A 1609 ? 3.7271 3.5665 3.4261 0.2527  -0.2508 -0.3410 1609 ALA A CA  
12274 C C   . ALA A 1609 ? 3.6770 3.4745 3.3529 0.2826  -0.2376 -0.3463 1609 ALA A C   
12275 O O   . ALA A 1609 ? 3.6851 3.4847 3.3651 0.2947  -0.2134 -0.3400 1609 ALA A O   
12276 C CB  . ALA A 1609 ? 3.7313 3.5697 3.4215 0.2686  -0.2535 -0.3223 1609 ALA A CB  
12277 N N   . GLU A 1610 ? 3.6202 3.3795 3.2731 0.2959  -0.2534 -0.3573 1610 GLU A N   
12278 C CA  . GLU A 1610 ? 3.5787 3.2968 3.2078 0.3254  -0.2425 -0.3628 1610 GLU A CA  
12279 C C   . GLU A 1610 ? 3.5465 3.2129 3.1367 0.3596  -0.2633 -0.3631 1610 GLU A C   
12280 O O   . GLU A 1610 ? 3.5416 3.1905 3.1244 0.3552  -0.2858 -0.3737 1610 GLU A O   
12281 C CB  . GLU A 1610 ? 3.5678 3.2902 3.2115 0.3059  -0.2348 -0.3798 1610 GLU A CB  
12282 C CG  . GLU A 1610 ? 3.5533 3.3127 3.2291 0.2891  -0.2051 -0.3800 1610 GLU A CG  
12283 C CD  . GLU A 1610 ? 3.5809 3.3352 3.2514 0.3173  -0.1828 -0.3655 1610 GLU A CD  
12284 O OE1 . GLU A 1610 ? 3.6207 3.3324 3.2570 0.3549  -0.1854 -0.3595 1610 GLU A OE1 
12285 O OE2 . GLU A 1610 ? 3.5629 3.3555 3.2643 0.3026  -0.1627 -0.3599 1610 GLU A OE2 
12286 N N   . LEU A 1611 ? 3.5234 3.1650 3.0897 0.3948  -0.2559 -0.3515 1611 LEU A N   
12287 C CA  . LEU A 1611 ? 3.5209 3.1132 3.0494 0.4307  -0.2745 -0.3521 1611 LEU A CA  
12288 C C   . LEU A 1611 ? 3.5120 3.0668 3.0213 0.4472  -0.2721 -0.3664 1611 LEU A C   
12289 O O   . LEU A 1611 ? 3.5125 3.0687 3.0260 0.4518  -0.2474 -0.3676 1611 LEU A O   
12290 C CB  . LEU A 1611 ? 3.5318 3.1092 3.0401 0.4635  -0.2672 -0.3348 1611 LEU A CB  
12291 C CG  . LEU A 1611 ? 3.5216 3.1027 3.0317 0.4783  -0.2350 -0.3246 1611 LEU A CG  
12292 C CD1 . LEU A 1611 ? 3.5438 3.0828 3.0259 0.5122  -0.2261 -0.3312 1611 LEU A CD1 
12293 C CD2 . LEU A 1611 ? 3.5250 3.1079 3.0285 0.4948  -0.2304 -0.3046 1611 LEU A CD2 
12294 N N   . VAL A 1612 ? 3.4959 3.0188 2.9874 0.4550  -0.2979 -0.3771 1612 VAL A N   
12295 C CA  . VAL A 1612 ? 3.4828 2.9645 2.9529 0.4724  -0.2996 -0.3909 1612 VAL A CA  
12296 C C   . VAL A 1612 ? 3.5025 2.9395 2.9330 0.5214  -0.2982 -0.3858 1612 VAL A C   
12297 O O   . VAL A 1612 ? 3.5351 2.9507 2.9451 0.5439  -0.3183 -0.3812 1612 VAL A O   
12298 C CB  . VAL A 1612 ? 3.4695 2.9320 2.9376 0.4616  -0.3292 -0.4047 1612 VAL A CB  
12299 C CG1 . VAL A 1612 ? 3.4831 2.9056 2.9335 0.4738  -0.3286 -0.4195 1612 VAL A CG1 
12300 C CG2 . VAL A 1612 ? 3.4271 2.9339 2.9327 0.4155  -0.3339 -0.4076 1612 VAL A CG2 
12301 N N   . LYS A 1613 ? 3.4707 2.8951 2.8921 0.5385  -0.2745 -0.3866 1613 LYS A N   
12302 C CA  . LYS A 1613 ? 3.4626 2.8454 2.8461 0.5864  -0.2708 -0.3818 1613 LYS A CA  
12303 C C   . LYS A 1613 ? 3.4349 2.7699 2.7867 0.6097  -0.3005 -0.3929 1613 LYS A C   
12304 O O   . LYS A 1613 ? 3.4195 2.7441 2.7763 0.5930  -0.3146 -0.4078 1613 LYS A O   
12305 C CB  . LYS A 1613 ? 3.4707 2.8496 2.8543 0.5979  -0.2411 -0.3830 1613 LYS A CB  
12306 C CG  . LYS A 1613 ? 3.5180 2.8486 2.8604 0.6471  -0.2393 -0.3827 1613 LYS A CG  
12307 C CD  . LYS A 1613 ? 3.5504 2.8686 2.8692 0.6810  -0.2402 -0.3664 1613 LYS A CD  
12308 C CE  . LYS A 1613 ? 3.6000 2.8655 2.8732 0.7300  -0.2480 -0.3693 1613 LYS A CE  
12309 N NZ  . LYS A 1613 ? 3.6088 2.8638 2.8749 0.7513  -0.2207 -0.3689 1613 LYS A NZ  
12310 N N   . GLY A 1614 ? 3.4130 2.7187 2.7333 0.6484  -0.3102 -0.3857 1614 GLY A N   
12311 C CA  . GLY A 1614 ? 3.3851 2.6447 2.6753 0.6755  -0.3386 -0.3960 1614 GLY A CA  
12312 C C   . GLY A 1614 ? 3.3109 2.5769 2.6117 0.6619  -0.3697 -0.3975 1614 GLY A C   
12313 O O   . GLY A 1614 ? 3.3317 2.5624 2.6131 0.6832  -0.3962 -0.4059 1614 GLY A O   
12314 N N   . ARG A 1615 ? 3.2237 2.5363 2.5581 0.6267  -0.3664 -0.3893 1615 ARG A N   
12315 C CA  . ARG A 1615 ? 3.1724 2.4986 2.5213 0.6143  -0.3929 -0.3870 1615 ARG A CA  
12316 C C   . ARG A 1615 ? 3.1321 2.4758 2.4802 0.6254  -0.3894 -0.3686 1615 ARG A C   
12317 O O   . ARG A 1615 ? 3.1097 2.4697 2.4588 0.6272  -0.3630 -0.3565 1615 ARG A O   
12318 C CB  . ARG A 1615 ? 3.1543 2.5214 2.5425 0.5657  -0.3951 -0.3911 1615 ARG A CB  
12319 C CG  . ARG A 1615 ? 3.1761 2.5263 2.5691 0.5504  -0.4046 -0.4089 1615 ARG A CG  
12320 C CD  . ARG A 1615 ? 3.1738 2.5726 2.6068 0.5016  -0.3979 -0.4095 1615 ARG A CD  
12321 N NE  . ARG A 1615 ? 3.1872 2.5777 2.6329 0.4801  -0.4150 -0.4236 1615 ARG A NE  
12322 C CZ  . ARG A 1615 ? 3.1647 2.5941 2.6443 0.4401  -0.4177 -0.4245 1615 ARG A CZ  
12323 N NH1 . ARG A 1615 ? 3.1362 2.6155 2.6397 0.4178  -0.4051 -0.4127 1615 ARG A NH1 
12324 N NH2 . ARG A 1615 ? 3.1609 2.5784 2.6505 0.4230  -0.4331 -0.4368 1615 ARG A NH2 
12325 N N   . GLN A 1616 ? 3.1191 2.4590 2.4680 0.6327  -0.4161 -0.3665 1616 GLN A N   
12326 C CA  . GLN A 1616 ? 3.1004 2.4531 2.4486 0.6442  -0.4174 -0.3498 1616 GLN A CA  
12327 C C   . GLN A 1616 ? 3.1055 2.5100 2.4927 0.6055  -0.4199 -0.3401 1616 GLN A C   
12328 O O   . GLN A 1616 ? 3.0927 2.5068 2.4970 0.5952  -0.4452 -0.3426 1616 GLN A O   
12329 C CB  . GLN A 1616 ? 3.0623 2.3801 2.3894 0.6787  -0.4461 -0.3531 1616 GLN A CB  
12330 C CG  . GLN A 1616 ? 3.0388 2.3032 2.3244 0.7218  -0.4473 -0.3625 1616 GLN A CG  
12331 C CD  . GLN A 1616 ? 2.9975 2.2288 2.2665 0.7537  -0.4791 -0.3688 1616 GLN A CD  
12332 O OE1 . GLN A 1616 ? 2.9612 2.2107 2.2489 0.7480  -0.4977 -0.3627 1616 GLN A OE1 
12333 N NE2 . GLN A 1616 ? 3.0034 2.1872 2.2390 0.7881  -0.4856 -0.3811 1616 GLN A NE2 
12334 N N   . TYR A 1617 ? 3.1383 2.5764 2.5408 0.5858  -0.3936 -0.3284 1617 TYR A N   
12335 C CA  . TYR A 1617 ? 3.1458 2.6349 2.5846 0.5492  -0.3929 -0.3181 1617 TYR A CA  
12336 C C   . TYR A 1617 ? 3.0526 2.5480 2.4890 0.5627  -0.3964 -0.3006 1617 TYR A C   
12337 O O   . TYR A 1617 ? 3.0429 2.5167 2.4551 0.5912  -0.3825 -0.2914 1617 TYR A O   
12338 C CB  . TYR A 1617 ? 3.2599 2.7840 2.7201 0.5193  -0.3639 -0.3152 1617 TYR A CB  
12339 C CG  . TYR A 1617 ? 3.3689 2.8966 2.8402 0.4974  -0.3611 -0.3320 1617 TYR A CG  
12340 C CD1 . TYR A 1617 ? 3.4387 2.9319 2.8874 0.5171  -0.3509 -0.3426 1617 TYR A CD1 
12341 C CD2 . TYR A 1617 ? 3.3858 2.9519 2.8906 0.4571  -0.3683 -0.3368 1617 TYR A CD2 
12342 C CE1 . TYR A 1617 ? 3.4582 2.9543 2.9183 0.4960  -0.3481 -0.3575 1617 TYR A CE1 
12343 C CE2 . TYR A 1617 ? 3.4044 2.9727 2.9193 0.4367  -0.3658 -0.3518 1617 TYR A CE2 
12344 C CZ  . TYR A 1617 ? 3.4359 2.9689 2.9288 0.4555  -0.3556 -0.3622 1617 TYR A CZ  
12345 O OH  . TYR A 1617 ? 3.4243 2.9591 2.9286 0.4341  -0.3526 -0.3768 1617 TYR A OH  
12346 N N   . LEU A 1618 ? 2.9712 2.4961 2.4338 0.5425  -0.4150 -0.2958 1618 LEU A N   
12347 C CA  . LEU A 1618 ? 2.8985 2.4380 2.3667 0.5473  -0.4170 -0.2781 1618 LEU A CA  
12348 C C   . LEU A 1618 ? 2.8331 2.4153 2.3251 0.5170  -0.3929 -0.2645 1618 LEU A C   
12349 O O   . LEU A 1618 ? 2.7965 2.4116 2.3138 0.4830  -0.3862 -0.2694 1618 LEU A O   
12350 C CB  . LEU A 1618 ? 2.8247 2.3771 2.3127 0.5421  -0.4478 -0.2781 1618 LEU A CB  
12351 C CG  . LEU A 1618 ? 2.7081 2.3084 2.2380 0.5008  -0.4578 -0.2787 1618 LEU A CG  
12352 C CD1 . LEU A 1618 ? 2.6677 2.3132 2.2214 0.4743  -0.4414 -0.2612 1618 LEU A CD1 
12353 C CD2 . LEU A 1618 ? 2.6710 2.2695 2.2142 0.5088  -0.4903 -0.2815 1618 LEU A CD2 
12354 N N   . ILE A 1619 ? 2.8050 2.3857 2.2891 0.5300  -0.3804 -0.2476 1619 ILE A N   
12355 C CA  . ILE A 1619 ? 2.7563 2.3639 2.2545 0.5115  -0.3526 -0.2346 1619 ILE A CA  
12356 C C   . ILE A 1619 ? 2.7142 2.3441 2.2271 0.5037  -0.3549 -0.2154 1619 ILE A C   
12357 O O   . ILE A 1619 ? 2.7310 2.3398 2.2291 0.5277  -0.3692 -0.2098 1619 ILE A O   
12358 C CB  . ILE A 1619 ? 2.8820 2.4558 2.3513 0.5412  -0.3272 -0.2318 1619 ILE A CB  
12359 C CG1 . ILE A 1619 ? 2.6570 2.2303 2.1283 0.5323  -0.3132 -0.2467 1619 ILE A CG1 
12360 C CG2 . ILE A 1619 ? 2.8775 2.4657 2.3546 0.5382  -0.3039 -0.2111 1619 ILE A CG2 
12361 C CD1 . ILE A 1619 ? 2.6619 2.1933 2.1049 0.5585  -0.3249 -0.2641 1619 ILE A CD1 
12362 N N   . MET A 1620 ? 2.6742 2.3472 2.2173 0.4699  -0.3411 -0.2058 1620 MET A N   
12363 C CA  . MET A 1620 ? 2.6570 2.3559 2.2186 0.4569  -0.3428 -0.1872 1620 MET A CA  
12364 C C   . MET A 1620 ? 2.6232 2.3555 2.2076 0.4301  -0.3177 -0.1752 1620 MET A C   
12365 O O   . MET A 1620 ? 2.5491 2.3168 2.1590 0.3984  -0.3137 -0.1820 1620 MET A O   
12366 C CB  . MET A 1620 ? 2.6399 2.3689 2.2277 0.4362  -0.3706 -0.1897 1620 MET A CB  
12367 C CG  . MET A 1620 ? 2.6602 2.3590 2.2313 0.4661  -0.3965 -0.1932 1620 MET A CG  
12368 S SD  . MET A 1620 ? 3.0365 2.7730 2.6449 0.4447  -0.4284 -0.1936 1620 MET A SD  
12369 C CE  . MET A 1620 ? 3.3820 3.1369 3.0070 0.4191  -0.4346 -0.2133 1620 MET A CE  
12370 N N   . GLY A 1621 ? 2.6786 2.3985 2.2543 0.4437  -0.3014 -0.1575 1621 GLY A N   
12371 C CA  . GLY A 1621 ? 2.6813 2.4290 2.2793 0.4211  -0.2785 -0.1440 1621 GLY A CA  
12372 C C   . GLY A 1621 ? 2.6854 2.4109 2.2705 0.4413  -0.2639 -0.1229 1621 GLY A C   
12373 O O   . GLY A 1621 ? 2.6788 2.3718 2.2394 0.4701  -0.2739 -0.1176 1621 GLY A O   
12374 N N   . LYS A 1622 ? 2.7124 2.4547 2.3150 0.4264  -0.2406 -0.1106 1622 LYS A N   
12375 C CA  . LYS A 1622 ? 2.7898 2.5092 2.3822 0.4446  -0.2241 -0.0891 1622 LYS A CA  
12376 C C   . LYS A 1622 ? 2.9606 2.6270 2.5149 0.4901  -0.2133 -0.0888 1622 LYS A C   
12377 O O   . LYS A 1622 ? 2.9728 2.6200 2.5076 0.5076  -0.2208 -0.1056 1622 LYS A O   
12378 C CB  . LYS A 1622 ? 2.7141 2.4598 2.3350 0.4208  -0.2002 -0.0774 1622 LYS A CB  
12379 C CG  . LYS A 1622 ? 2.6396 2.4212 2.2864 0.3928  -0.1937 -0.0927 1622 LYS A CG  
12380 C CD  . LYS A 1622 ? 2.5643 2.3944 2.2401 0.3536  -0.2122 -0.0973 1622 LYS A CD  
12381 C CE  . LYS A 1622 ? 2.5203 2.3764 2.2102 0.3337  -0.2162 -0.1186 1622 LYS A CE  
12382 N NZ  . LYS A 1622 ? 2.4880 2.3743 2.1915 0.3106  -0.2426 -0.1265 1622 LYS A NZ  
12383 N N   . GLU A 1623 ? 3.1200 2.7619 2.6636 0.5097  -0.1955 -0.0694 1623 GLU A N   
12384 C CA  . GLU A 1623 ? 3.3022 2.8937 2.8088 0.5554  -0.1851 -0.0671 1623 GLU A CA  
12385 C C   . GLU A 1623 ? 3.4531 3.0393 2.9619 0.5640  -0.1607 -0.0730 1623 GLU A C   
12386 O O   . GLU A 1623 ? 3.4195 3.0405 2.9572 0.5345  -0.1547 -0.0822 1623 GLU A O   
12387 C CB  . GLU A 1623 ? 3.3157 2.8797 2.8083 0.5765  -0.1761 -0.0431 1623 GLU A CB  
12388 C CG  . GLU A 1623 ? 3.3126 2.8691 2.8150 0.5813  -0.1443 -0.0256 1623 GLU A CG  
12389 C CD  . GLU A 1623 ? 3.3371 2.8508 2.8139 0.6157  -0.1340 -0.0040 1623 GLU A CD  
12390 O OE1 . GLU A 1623 ? 3.3425 2.8460 2.8063 0.6212  -0.1515 0.0022  1623 GLU A OE1 
12391 O OE2 . GLU A 1623 ? 3.3493 2.8400 2.8209 0.6377  -0.1082 0.0072  1623 GLU A OE2 
12392 N N   . ALA A 1624 ? 3.6476 3.1912 3.1268 0.6053  -0.1468 -0.0679 1624 ALA A N   
12393 C CA  . ALA A 1624 ? 3.8151 3.3509 3.2971 0.6192  -0.1213 -0.0705 1624 ALA A CA  
12394 C C   . ALA A 1624 ? 3.9528 3.4871 3.4519 0.6219  -0.0933 -0.0481 1624 ALA A C   
12395 O O   . ALA A 1624 ? 3.9685 3.4849 3.4582 0.6325  -0.0916 -0.0287 1624 ALA A O   
12396 C CB  . ALA A 1624 ? 3.8691 3.3607 3.3111 0.6642  -0.1212 -0.0772 1624 ALA A CB  
12397 N N   . LEU A 1625 ? 4.0658 3.6183 3.5916 0.6127  -0.0715 -0.0506 1625 LEU A N   
12398 C CA  . LEU A 1625 ? 4.1732 3.7281 3.7227 0.6124  -0.0451 -0.0305 1625 LEU A CA  
12399 C C   . LEU A 1625 ? 4.2365 3.7467 3.7637 0.6598  -0.0230 -0.0155 1625 LEU A C   
12400 O O   . LEU A 1625 ? 4.2574 3.7545 3.7755 0.6838  -0.0123 -0.0244 1625 LEU A O   
12401 C CB  . LEU A 1625 ? 4.2049 3.8025 3.7988 0.5813  -0.0315 -0.0393 1625 LEU A CB  
12402 C CG  . LEU A 1625 ? 4.2421 3.8459 3.8438 0.5890  -0.0201 -0.0568 1625 LEU A CG  
12403 C CD1 . LEU A 1625 ? 4.2675 3.8496 3.8754 0.6216  0.0109  -0.0433 1625 LEU A CD1 
12404 C CD2 . LEU A 1625 ? 4.2124 3.8680 3.8548 0.5450  -0.0224 -0.0724 1625 LEU A CD2 
12405 N N   . GLN A 1626 ? 4.2588 3.7461 3.7783 0.6733  -0.0155 0.0081  1626 GLN A N   
12406 C CA  . GLN A 1626 ? 4.2869 3.7310 3.7862 0.7190  0.0063  0.0250  1626 GLN A CA  
12407 C C   . GLN A 1626 ? 4.2048 3.6573 3.7400 0.7201  0.0375  0.0372  1626 GLN A C   
12408 O O   . GLN A 1626 ? 4.1874 3.6552 3.7517 0.6975  0.0455  0.0513  1626 GLN A O   
12409 C CB  . GLN A 1626 ? 4.3662 3.7768 3.8393 0.7369  0.0013  0.0460  1626 GLN A CB  
12410 C CG  . GLN A 1626 ? 4.4303 3.8185 3.8615 0.7544  -0.0248 0.0372  1626 GLN A CG  
12411 C CD  . GLN A 1626 ? 4.4764 3.8295 3.8830 0.7763  -0.0260 0.0592  1626 GLN A CD  
12412 O OE1 . GLN A 1626 ? 4.4955 3.8229 3.9010 0.7990  -0.0028 0.0807  1626 GLN A OE1 
12413 N NE2 . GLN A 1626 ? 4.4868 3.8390 3.8760 0.7699  -0.0532 0.0542  1626 GLN A NE2 
12414 N N   . ILE A 1627 ? 4.1394 3.5830 3.6749 0.7462  0.0549  0.0315  1627 ILE A N   
12415 C CA  . ILE A 1627 ? 4.0640 3.5001 3.6250 0.7651  0.0869  0.0484  1627 ILE A CA  
12416 C C   . ILE A 1627 ? 4.0337 3.4166 3.5564 0.8152  0.0967  0.0684  1627 ILE A C   
12417 O O   . ILE A 1627 ? 4.0462 3.4071 3.5493 0.8523  0.1064  0.0654  1627 ILE A O   
12418 C CB  . ILE A 1627 ? 3.9656 3.4232 3.5525 0.7681  0.1024  0.0330  1627 ILE A CB  
12419 C CG1 . ILE A 1627 ? 3.9770 3.4257 3.5307 0.7826  0.0877  0.0115  1627 ILE A CG1 
12420 C CG2 . ILE A 1627 ? 3.9246 3.4350 3.5605 0.7201  0.1014  0.0205  1627 ILE A CG2 
12421 C CD1 . ILE A 1627 ? 3.9523 3.4358 3.5115 0.7412  0.0618  -0.0135 1627 ILE A CD1 
12422 N N   . LYS A 1628 ? 3.9775 3.3404 3.4900 0.8157  0.0940  0.0888  1628 LYS A N   
12423 C CA  . LYS A 1628 ? 3.9523 3.2643 3.4218 0.8592  0.0962  0.1062  1628 LYS A CA  
12424 C C   . LYS A 1628 ? 4.0609 3.3419 3.5159 0.9100  0.1195  0.1131  1628 LYS A C   
12425 O O   . LYS A 1628 ? 4.0982 3.3532 3.5115 0.9419  0.1109  0.1058  1628 LYS A O   
12426 C CB  . LYS A 1628 ? 3.8058 3.1012 3.2810 0.8541  0.1021  0.1332  1628 LYS A CB  
12427 C CG  . LYS A 1628 ? 3.7130 2.9556 3.1437 0.8982  0.1042  0.1516  1628 LYS A CG  
12428 C CD  . LYS A 1628 ? 3.6046 2.8299 3.0418 0.8908  0.1099  0.1787  1628 LYS A CD  
12429 C CE  . LYS A 1628 ? 3.5180 2.7351 2.9894 0.9004  0.1423  0.2004  1628 LYS A CE  
12430 N NZ  . LYS A 1628 ? 3.5079 2.6874 2.9595 0.9552  0.1641  0.2109  1628 LYS A NZ  
12431 N N   . TYR A 1629 ? 4.1238 3.4080 3.6145 0.9187  0.1487  0.1272  1629 TYR A N   
12432 C CA  . TYR A 1629 ? 4.2203 3.4764 3.7021 0.9687  0.1733  0.1370  1629 TYR A CA  
12433 C C   . TYR A 1629 ? 4.3036 3.5739 3.8375 0.9727  0.2052  0.1492  1629 TYR A C   
12434 O O   . TYR A 1629 ? 4.3008 3.5706 3.8632 0.9613  0.2171  0.1685  1629 TYR A O   
12435 C CB  . TYR A 1629 ? 4.2330 3.4365 3.6715 1.0103  0.1762  0.1594  1629 TYR A CB  
12436 C CG  . TYR A 1629 ? 4.2472 3.4199 3.6393 1.0572  0.1745  0.1533  1629 TYR A CG  
12437 C CD1 . TYR A 1629 ? 4.2472 3.4190 3.6014 1.0537  0.1455  0.1314  1629 TYR A CD1 
12438 C CD2 . TYR A 1629 ? 4.2611 3.4052 3.6479 1.1064  0.2016  0.1702  1629 TYR A CD2 
12439 C CE1 . TYR A 1629 ? 4.2740 3.4170 3.5854 1.0968  0.1430  0.1253  1629 TYR A CE1 
12440 C CE2 . TYR A 1629 ? 4.2880 3.4047 3.6315 1.1500  0.1999  0.1648  1629 TYR A CE2 
12441 C CZ  . TYR A 1629 ? 4.2947 3.4105 3.5998 1.1447  0.1703  0.1419  1629 TYR A CZ  
12442 O OH  . TYR A 1629 ? 4.3269 3.4149 3.5886 1.1885  0.1678  0.1358  1629 TYR A OH  
12443 N N   . ASN A 1630 ? 4.3911 3.6746 3.9393 0.9887  0.2184  0.1376  1630 ASN A N   
12444 C CA  . ASN A 1630 ? 4.4621 3.7478 4.0515 1.0120  0.2519  0.1520  1630 ASN A CA  
12445 C C   . ASN A 1630 ? 4.4829 3.7563 4.0542 1.0542  0.2629  0.1454  1630 ASN A C   
12446 O O   . ASN A 1630 ? 4.4554 3.7566 4.0637 1.0544  0.2783  0.1361  1630 ASN A O   
12447 C CB  . ASN A 1630 ? 4.4820 3.8166 4.1365 0.9718  0.2606  0.1446  1630 ASN A CB  
12448 C CG  . ASN A 1630 ? 4.5078 3.8862 4.1717 0.9328  0.2412  0.1123  1630 ASN A CG  
12449 O OD1 . ASN A 1630 ? 4.5373 3.9147 4.1769 0.9456  0.2340  0.0952  1630 ASN A OD1 
12450 N ND2 . ASN A 1630 ? 4.4868 3.9035 4.1872 0.8852  0.2333  0.1042  1630 ASN A ND2 
12451 N N   . PHE A 1631 ? 4.5157 3.7475 4.0299 1.0895  0.2543  0.1507  1631 PHE A N   
12452 C CA  . PHE A 1631 ? 4.5116 3.7243 3.9935 1.1323  0.2590  0.1442  1631 PHE A CA  
12453 C C   . PHE A 1631 ? 4.5043 3.7211 3.9461 1.1199  0.2284  0.1157  1631 PHE A C   
12454 O O   . PHE A 1631 ? 4.5247 3.7499 3.9625 1.1320  0.2303  0.0994  1631 PHE A O   
12455 C CB  . PHE A 1631 ? 4.4624 3.6929 3.9871 1.1529  0.2893  0.1468  1631 PHE A CB  
12456 C CG  . PHE A 1631 ? 4.4401 3.6404 3.9744 1.1993  0.3200  0.1785  1631 PHE A CG  
12457 C CD1 . PHE A 1631 ? 4.4664 3.6169 3.9497 1.2403  0.3195  0.1967  1631 PHE A CD1 
12458 C CD2 . PHE A 1631 ? 4.3961 3.6179 3.9918 1.2031  0.3492  0.1901  1631 PHE A CD2 
12459 C CE1 . PHE A 1631 ? 4.4720 3.5932 3.9636 1.2841  0.3480  0.2270  1631 PHE A CE1 
12460 C CE2 . PHE A 1631 ? 4.4003 3.5933 4.0072 1.2475  0.3777  0.2204  1631 PHE A CE2 
12461 C CZ  . PHE A 1631 ? 4.4408 3.5827 3.9946 1.2880  0.3773  0.2393  1631 PHE A CZ  
12462 N N   . SER A 1632 ? 4.4618 3.6733 3.8774 1.0949  0.2006  0.1104  1632 SER A N   
12463 C CA  . SER A 1632 ? 4.4330 3.6316 3.7991 1.0968  0.1705  0.0908  1632 SER A CA  
12464 C C   . SER A 1632 ? 4.3560 3.5905 3.7309 1.0562  0.1477  0.0595  1632 SER A C   
12465 O O   . SER A 1632 ? 4.3672 3.6161 3.7519 1.0606  0.1540  0.0442  1632 SER A O   
12466 C CB  . SER A 1632 ? 4.4763 3.6377 3.8004 1.1534  0.1782  0.0937  1632 SER A CB  
12467 O OG  . SER A 1632 ? 4.4978 3.6286 3.8194 1.1933  0.2037  0.1231  1632 SER A OG  
12468 N N   . PHE A 1633 ? 4.2639 3.5122 3.6359 1.0176  0.1215  0.0511  1633 PHE A N   
12469 C CA  . PHE A 1633 ? 4.1754 3.4461 3.5406 0.9865  0.0933  0.0224  1633 PHE A CA  
12470 C C   . PHE A 1633 ? 4.3984 3.6882 3.7670 0.9428  0.0656  0.0161  1633 PHE A C   
12471 O O   . PHE A 1633 ? 4.4058 3.6801 3.7634 0.9437  0.0603  0.0325  1633 PHE A O   
12472 C CB  . PHE A 1633 ? 4.0859 3.3904 3.4840 0.9693  0.1021  0.0034  1633 PHE A CB  
12473 C CG  . PHE A 1633 ? 4.0665 3.3546 3.4329 0.9954  0.0953  -0.0142 1633 PHE A CG  
12474 C CD1 . PHE A 1633 ? 4.0674 3.3437 3.3970 0.9908  0.0639  -0.0321 1633 PHE A CD1 
12475 C CD2 . PHE A 1633 ? 4.0624 3.3472 3.4381 1.0246  0.1201  -0.0126 1633 PHE A CD2 
12476 C CE1 . PHE A 1633 ? 4.0902 3.3494 3.3909 1.0145  0.0570  -0.0483 1633 PHE A CE1 
12477 C CE2 . PHE A 1633 ? 4.0839 3.3534 3.4305 1.0477  0.1138  -0.0285 1633 PHE A CE2 
12478 C CZ  . PHE A 1633 ? 4.1008 3.3564 3.4089 1.0425  0.0820  -0.0466 1633 PHE A CZ  
12479 N N   . ARG A 1634 ? 4.3722 3.6963 3.7579 0.9051  0.0491  -0.0073 1634 ARG A N   
12480 C CA  . ARG A 1634 ? 4.3680 3.7021 3.7407 0.8764  0.0157  -0.0208 1634 ARG A CA  
12481 C C   . ARG A 1634 ? 4.3203 3.6945 3.7282 0.8241  0.0047  -0.0219 1634 ARG A C   
12482 O O   . ARG A 1634 ? 4.2993 3.6805 3.7288 0.8130  0.0166  -0.0030 1634 ARG A O   
12483 C CB  . ARG A 1634 ? 4.3874 3.7230 3.7427 0.8762  -0.0026 -0.0477 1634 ARG A CB  
12484 C CG  . ARG A 1634 ? 4.4438 3.7356 3.7527 0.9267  -0.0034 -0.0495 1634 ARG A CG  
12485 C CD  . ARG A 1634 ? 4.4931 3.7511 3.7642 0.9504  -0.0183 -0.0377 1634 ARG A CD  
12486 N NE  . ARG A 1634 ? 4.5574 3.7725 3.7850 1.0035  -0.0145 -0.0357 1634 ARG A NE  
12487 C CZ  . ARG A 1634 ? 4.6167 3.7973 3.8056 1.0330  -0.0268 -0.0277 1634 ARG A CZ  
12488 N NH1 . ARG A 1634 ? 4.6188 3.8036 3.8090 1.0136  -0.0435 -0.0206 1634 ARG A NH1 
12489 N NH2 . ARG A 1634 ? 4.6680 3.8113 3.8178 1.0821  -0.0224 -0.0268 1634 ARG A NH2 
12490 N N   . TYR A 1635 ? 4.3046 3.7045 3.7181 0.7932  -0.0181 -0.0443 1635 TYR A N   
12491 C CA  . TYR A 1635 ? 4.2856 3.7138 3.7141 0.7520  -0.0402 -0.0477 1635 TYR A CA  
12492 C C   . TYR A 1635 ? 4.2422 3.7153 3.7020 0.7081  -0.0506 -0.0686 1635 TYR A C   
12493 O O   . TYR A 1635 ? 4.2101 3.7197 3.7087 0.6737  -0.0429 -0.0657 1635 TYR A O   
12494 C CB  . TYR A 1635 ? 4.3202 3.7246 3.7103 0.7654  -0.0694 -0.0536 1635 TYR A CB  
12495 C CG  . TYR A 1635 ? 4.3531 3.7284 3.7207 0.7871  -0.0716 -0.0327 1635 TYR A CG  
12496 C CD1 . TYR A 1635 ? 4.3975 3.7272 3.7273 0.8362  -0.0636 -0.0237 1635 TYR A CD1 
12497 C CD2 . TYR A 1635 ? 4.3402 3.7341 3.7242 0.7582  -0.0825 -0.0224 1635 TYR A CD2 
12498 C CE1 . TYR A 1635 ? 4.4233 3.7260 3.7323 0.8557  -0.0660 -0.0049 1635 TYR A CE1 
12499 C CE2 . TYR A 1635 ? 4.3632 3.7310 3.7283 0.7762  -0.0847 -0.0034 1635 TYR A CE2 
12500 C CZ  . TYR A 1635 ? 4.4043 3.7261 3.7318 0.8248  -0.0766 0.0052  1635 TYR A CZ  
12501 O OH  . TYR A 1635 ? 4.4227 3.7184 3.7315 0.8422  -0.0788 0.0241  1635 TYR A OH  
12502 N N   . ILE A 1636 ? 4.2403 3.7081 3.6817 0.7116  -0.0679 -0.0896 1636 ILE A N   
12503 C CA  . ILE A 1636 ? 4.2124 3.7097 3.6656 0.6749  -0.0931 -0.1088 1636 ILE A CA  
12504 C C   . ILE A 1636 ? 4.1829 3.7319 3.6807 0.6243  -0.0943 -0.1128 1636 ILE A C   
12505 O O   . ILE A 1636 ? 4.1594 3.7288 3.6868 0.6103  -0.0750 -0.1004 1636 ILE A O   
12506 C CB  . ILE A 1636 ? 4.2068 3.6920 3.6419 0.6854  -0.1037 -0.1314 1636 ILE A CB  
12507 C CG1 . ILE A 1636 ? 4.1889 3.6810 3.6161 0.6665  -0.1376 -0.1462 1636 ILE A CG1 
12508 C CG2 . ILE A 1636 ? 4.1818 3.6940 3.6480 0.6675  -0.0855 -0.1423 1636 ILE A CG2 
12509 C CD1 . ILE A 1636 ? 4.1906 3.6732 3.6044 0.6707  -0.1554 -0.1338 1636 ILE A CD1 
12510 N N   . TYR A 1637 ? 4.1858 3.7541 3.6873 0.5992  -0.1181 -0.1309 1637 TYR A N   
12511 C CA  . TYR A 1637 ? 4.1686 3.7795 3.6996 0.5551  -0.1322 -0.1335 1637 TYR A CA  
12512 C C   . TYR A 1637 ? 4.1303 3.7845 3.6998 0.5190  -0.1235 -0.1457 1637 TYR A C   
12513 O O   . TYR A 1637 ? 4.1547 3.8065 3.7270 0.5254  -0.1120 -0.1575 1637 TYR A O   
12514 C CB  . TYR A 1637 ? 4.1824 3.7877 3.6955 0.5518  -0.1648 -0.1452 1637 TYR A CB  
12515 C CG  . TYR A 1637 ? 4.1533 3.7994 3.6934 0.5117  -0.1821 -0.1452 1637 TYR A CG  
12516 C CD1 . TYR A 1637 ? 4.1269 3.8046 3.6871 0.4803  -0.1950 -0.1629 1637 TYR A CD1 
12517 C CD2 . TYR A 1637 ? 4.1436 3.7971 3.6901 0.5050  -0.1851 -0.1269 1637 TYR A CD2 
12518 C CE1 . TYR A 1637 ? 4.0926 3.8093 3.6783 0.4449  -0.2104 -0.1620 1637 TYR A CE1 
12519 C CE2 . TYR A 1637 ? 4.1095 3.8028 3.6826 0.4685  -0.2001 -0.1262 1637 TYR A CE2 
12520 C CZ  . TYR A 1637 ? 4.0837 3.8089 3.6761 0.4394  -0.2128 -0.1436 1637 TYR A CZ  
12521 O OH  . TYR A 1637 ? 4.0504 3.8168 3.6700 0.4045  -0.2274 -0.1419 1637 TYR A OH  
12522 N N   . PRO A 1638 ? 4.0490 3.7444 3.6495 0.4809  -0.1288 -0.1425 1638 PRO A N   
12523 C CA  . PRO A 1638 ? 3.9353 3.6780 3.5739 0.4412  -0.1256 -0.1542 1638 PRO A CA  
12524 C C   . PRO A 1638 ? 3.8090 3.5654 3.4485 0.4231  -0.1445 -0.1774 1638 PRO A C   
12525 O O   . PRO A 1638 ? 3.8475 3.6133 3.4995 0.4176  -0.1333 -0.1906 1638 PRO A O   
12526 C CB  . PRO A 1638 ? 3.9605 3.7359 3.6226 0.4115  -0.1314 -0.1416 1638 PRO A CB  
12527 C CG  . PRO A 1638 ? 4.0228 3.7681 3.6570 0.4329  -0.1438 -0.1270 1638 PRO A CG  
12528 C CD  . PRO A 1638 ? 4.0607 3.7580 3.6644 0.4774  -0.1296 -0.1218 1638 PRO A CD  
12529 N N   . LEU A 1639 ? 3.6797 3.4382 3.3093 0.4138  -0.1717 -0.1818 1639 LEU A N   
12530 C CA  . LEU A 1639 ? 3.5284 3.3018 3.1629 0.3938  -0.1908 -0.2020 1639 LEU A CA  
12531 C C   . LEU A 1639 ? 3.4431 3.2716 3.1173 0.3483  -0.1924 -0.2064 1639 LEU A C   
12532 O O   . LEU A 1639 ? 3.4490 3.2983 3.1414 0.3298  -0.1862 -0.2208 1639 LEU A O   
12533 C CB  . LEU A 1639 ? 3.3955 3.1468 3.0178 0.4097  -0.1824 -0.2177 1639 LEU A CB  
12534 C CG  . LEU A 1639 ? 3.2299 2.9765 2.8447 0.4017  -0.2030 -0.2381 1639 LEU A CG  
12535 C CD1 . LEU A 1639 ? 3.1898 2.9113 2.7791 0.4172  -0.2303 -0.2373 1639 LEU A CD1 
12536 C CD2 . LEU A 1639 ? 3.1880 2.9081 2.7891 0.4219  -0.1902 -0.2498 1639 LEU A CD2 
12537 N N   . ASP A 1640 ? 3.3310 3.1835 3.0189 0.3308  -0.2007 -0.1937 1640 ASP A N   
12538 C CA  . ASP A 1640 ? 3.1876 3.0939 2.9134 0.2898  -0.1999 -0.1938 1640 ASP A CA  
12539 C C   . ASP A 1640 ? 3.0153 2.9506 2.7532 0.2623  -0.2246 -0.2054 1640 ASP A C   
12540 O O   . ASP A 1640 ? 3.0149 2.9327 2.7380 0.2696  -0.2392 -0.2195 1640 ASP A O   
12541 C CB  . ASP A 1640 ? 3.2383 3.1582 2.9763 0.2836  -0.1932 -0.1725 1640 ASP A CB  
12542 C CG  . ASP A 1640 ? 3.3088 3.2219 3.0347 0.2876  -0.2152 -0.1624 1640 ASP A CG  
12543 O OD1 . ASP A 1640 ? 3.3556 3.2281 3.0504 0.3178  -0.2254 -0.1628 1640 ASP A OD1 
12544 O OD2 . ASP A 1640 ? 3.3116 3.2609 3.0606 0.2608  -0.2224 -0.1542 1640 ASP A OD2 
12545 N N   . SER A 1641 ? 2.8489 2.8285 2.6150 0.2313  -0.2286 -0.1987 1641 SER A N   
12546 C CA  . SER A 1641 ? 2.6974 2.7132 2.4819 0.2019  -0.2490 -0.2078 1641 SER A CA  
12547 C C   . SER A 1641 ? 2.5712 2.5870 2.3508 0.2035  -0.2747 -0.2006 1641 SER A C   
12548 O O   . SER A 1641 ? 2.5448 2.5848 2.3378 0.1846  -0.2931 -0.2089 1641 SER A O   
12549 C CB  . SER A 1641 ? 2.6544 2.7248 2.4759 0.1650  -0.2396 -0.2075 1641 SER A CB  
12550 O OG  . SER A 1641 ? 2.6365 2.7169 2.4690 0.1555  -0.2260 -0.2230 1641 SER A OG  
12551 N N   . LEU A 1642 ? 2.4441 2.4358 2.2082 0.2251  -0.2759 -0.1848 1642 LEU A N   
12552 C CA  . LEU A 1642 ? 2.3071 2.2893 2.0631 0.2348  -0.3009 -0.1806 1642 LEU A CA  
12553 C C   . LEU A 1642 ? 2.4650 2.3900 2.1834 0.2763  -0.3067 -0.1826 1642 LEU A C   
12554 O O   . LEU A 1642 ? 2.5946 2.5067 2.3049 0.2905  -0.3225 -0.1745 1642 LEU A O   
12555 C CB  . LEU A 1642 ? 1.9930 2.0044 1.7688 0.2199  -0.3055 -0.1615 1642 LEU A CB  
12556 C CG  . LEU A 1642 ? 1.7778 1.8320 1.5810 0.1937  -0.3277 -0.1627 1642 LEU A CG  
12557 C CD1 . LEU A 1642 ? 1.7505 1.7811 1.5412 0.2146  -0.3519 -0.1648 1642 LEU A CD1 
12558 C CD2 . LEU A 1642 ? 1.7197 1.8033 1.5400 0.1690  -0.3295 -0.1792 1642 LEU A CD2 
12559 N N   . THR A 1643 ? 2.4753 2.3677 2.1722 0.2959  -0.2940 -0.1933 1643 THR A N   
12560 C CA  . THR A 1643 ? 2.4914 2.3318 2.1528 0.3335  -0.3033 -0.2001 1643 THR A CA  
12561 C C   . THR A 1643 ? 2.4965 2.3386 2.1605 0.3262  -0.3259 -0.2175 1643 THR A C   
12562 O O   . THR A 1643 ? 2.4503 2.3186 2.1330 0.3004  -0.3238 -0.2288 1643 THR A O   
12563 C CB  . THR A 1643 ? 1.9318 1.7347 1.5684 0.3600  -0.2820 -0.2052 1643 THR A CB  
12564 O OG1 . THR A 1643 ? 1.9470 1.7407 1.5788 0.3731  -0.2605 -0.1881 1643 THR A OG1 
12565 C CG2 . THR A 1643 ? 1.9344 1.6875 1.5354 0.3966  -0.2955 -0.2135 1643 THR A CG2 
12566 N N   . TRP A 1644 ? 2.6209 2.4346 2.2673 0.3492  -0.3477 -0.2197 1644 TRP A N   
12567 C CA  . TRP A 1644 ? 2.7700 2.5862 2.4233 0.3418  -0.3714 -0.2343 1644 TRP A CA  
12568 C C   . TRP A 1644 ? 3.0287 2.8012 2.6548 0.3647  -0.3740 -0.2516 1644 TRP A C   
12569 O O   . TRP A 1644 ? 3.0355 2.7904 2.6564 0.3744  -0.3971 -0.2613 1644 TRP A O   
12570 C CB  . TRP A 1644 ? 2.7250 2.5445 2.3857 0.3483  -0.3973 -0.2276 1644 TRP A CB  
12571 C CG  . TRP A 1644 ? 2.6973 2.5329 2.3777 0.3332  -0.4210 -0.2388 1644 TRP A CG  
12572 C CD1 . TRP A 1644 ? 2.7009 2.5068 2.3710 0.3543  -0.4448 -0.2486 1644 TRP A CD1 
12573 C CD2 . TRP A 1644 ? 2.6796 2.5642 2.3946 0.2948  -0.4234 -0.2412 1644 TRP A CD2 
12574 N NE1 . TRP A 1644 ? 2.6872 2.5192 2.3844 0.3318  -0.4616 -0.2560 1644 TRP A NE1 
12575 C CE2 . TRP A 1644 ? 2.6671 2.5479 2.3912 0.2952  -0.4487 -0.2515 1644 TRP A CE2 
12576 C CE3 . TRP A 1644 ? 2.6715 2.6025 2.4111 0.2612  -0.4067 -0.2356 1644 TRP A CE3 
12577 C CZ2 . TRP A 1644 ? 2.6381 2.5599 2.3945 0.2636  -0.4572 -0.2555 1644 TRP A CZ2 
12578 C CZ3 . TRP A 1644 ? 2.6365 2.6094 2.4068 0.2295  -0.4156 -0.2406 1644 TRP A CZ3 
12579 C CH2 . TRP A 1644 ? 2.6207 2.5886 2.3988 0.2311  -0.4404 -0.2499 1644 TRP A CH2 
12580 N N   . ILE A 1645 ? 3.2840 3.0397 2.8953 0.3733  -0.3504 -0.2552 1645 ILE A N   
12581 C CA  . ILE A 1645 ? 3.5371 3.2516 3.1229 0.3950  -0.3508 -0.2710 1645 ILE A CA  
12582 C C   . ILE A 1645 ? 3.7435 3.4609 3.3395 0.3809  -0.3742 -0.2863 1645 ILE A C   
12583 O O   . ILE A 1645 ? 3.7341 3.4902 3.3590 0.3463  -0.3752 -0.2903 1645 ILE A O   
12584 C CB  . ILE A 1645 ? 1.9640 1.6768 1.5475 0.3928  -0.3217 -0.2757 1645 ILE A CB  
12585 C CG1 . ILE A 1645 ? 1.9246 1.6804 1.5409 0.3521  -0.3151 -0.2842 1645 ILE A CG1 
12586 C CG2 . ILE A 1645 ? 1.9802 1.6925 1.5590 0.4056  -0.2975 -0.2591 1645 ILE A CG2 
12587 C CD1 . ILE A 1645 ? 1.9315 1.6705 1.5424 0.3499  -0.3169 -0.3033 1645 ILE A CD1 
12588 N N   . GLU A 1646 ? 3.9508 3.6266 3.5235 0.4089  -0.3935 -0.2944 1646 GLU A N   
12589 C CA  . GLU A 1646 ? 4.1038 3.7782 3.6874 0.3999  -0.4193 -0.3064 1646 GLU A CA  
12590 C C   . GLU A 1646 ? 4.1114 3.7302 3.6637 0.4343  -0.4334 -0.3191 1646 GLU A C   
12591 O O   . GLU A 1646 ? 4.1354 3.7228 3.6634 0.4682  -0.4397 -0.3146 1646 GLU A O   
12592 C CB  . GLU A 1646 ? 4.2551 3.9573 3.8621 0.3907  -0.4401 -0.2962 1646 GLU A CB  
12593 C CG  . GLU A 1646 ? 4.3668 4.0767 3.9941 0.3774  -0.4657 -0.3060 1646 GLU A CG  
12594 C CD  . GLU A 1646 ? 4.4429 4.1704 4.0902 0.3798  -0.4885 -0.2960 1646 GLU A CD  
12595 O OE1 . GLU A 1646 ? 4.4923 4.1959 4.1226 0.4093  -0.4952 -0.2896 1646 GLU A OE1 
12596 O OE2 . GLU A 1646 ? 4.4405 4.2067 4.1217 0.3528  -0.4995 -0.2943 1646 GLU A OE2 
12597 N N   . TYR A 1647 ? 4.0907 3.6979 3.6444 0.4247  -0.4385 -0.3350 1647 TYR A N   
12598 C CA  . TYR A 1647 ? 4.1243 3.6784 3.6502 0.4533  -0.4512 -0.3490 1647 TYR A CA  
12599 C C   . TYR A 1647 ? 4.1704 3.7006 3.6885 0.4805  -0.4803 -0.3479 1647 TYR A C   
12600 O O   . TYR A 1647 ? 4.0634 3.6203 3.6088 0.4659  -0.4986 -0.3432 1647 TYR A O   
12601 C CB  . TYR A 1647 ? 4.1031 3.6579 3.6423 0.4292  -0.4558 -0.3645 1647 TYR A CB  
12602 C CG  . TYR A 1647 ? 4.1478 3.6500 3.6601 0.4514  -0.4614 -0.3805 1647 TYR A CG  
12603 C CD1 . TYR A 1647 ? 4.1992 3.6628 3.6763 0.4859  -0.4502 -0.3815 1647 TYR A CD1 
12604 C CD2 . TYR A 1647 ? 4.1513 3.6426 3.6742 0.4370  -0.4772 -0.3940 1647 TYR A CD2 
12605 C CE1 . TYR A 1647 ? 4.2396 3.6560 3.6925 0.5058  -0.4553 -0.3960 1647 TYR A CE1 
12606 C CE2 . TYR A 1647 ? 4.1901 3.6321 3.6892 0.4558  -0.4823 -0.4084 1647 TYR A CE2 
12607 C CZ  . TYR A 1647 ? 4.2320 3.6374 3.6961 0.4901  -0.4714 -0.4096 1647 TYR A CZ  
12608 O OH  . TYR A 1647 ? 4.2543 3.6112 3.6946 0.5090  -0.4763 -0.4238 1647 TYR A OH  
12609 N N   . TRP A 1648 ? 4.3136 3.7959 3.7962 0.5208  -0.4836 -0.3515 1648 TRP A N   
12610 C CA  . TRP A 1648 ? 4.3325 3.7837 3.8044 0.5518  -0.5124 -0.3546 1648 TRP A CA  
12611 C C   . TRP A 1648 ? 4.2363 3.6449 3.6943 0.5643  -0.5274 -0.3736 1648 TRP A C   
12612 O O   . TRP A 1648 ? 4.2424 3.6056 3.6656 0.5976  -0.5265 -0.3808 1648 TRP A O   
12613 C CB  . TRP A 1648 ? 3.4734 2.8987 2.9138 0.5906  -0.5071 -0.3460 1648 TRP A CB  
12614 C CG  . TRP A 1648 ? 3.0358 2.4415 2.4721 0.6204  -0.5360 -0.3452 1648 TRP A CG  
12615 C CD1 . TRP A 1648 ? 3.0437 2.4062 2.4638 0.6498  -0.5599 -0.3591 1648 TRP A CD1 
12616 C CD2 . TRP A 1648 ? 3.0521 2.4811 2.5021 0.6238  -0.5428 -0.3299 1648 TRP A CD2 
12617 N NE1 . TRP A 1648 ? 3.0557 2.4150 2.4804 0.6713  -0.5815 -0.3541 1648 TRP A NE1 
12618 C CE2 . TRP A 1648 ? 3.0676 2.4679 2.5110 0.6552  -0.5712 -0.3360 1648 TRP A CE2 
12619 C CE3 . TRP A 1648 ? 3.0639 2.5355 2.5331 0.6026  -0.5278 -0.3117 1648 TRP A CE3 
12620 C CZ2 . TRP A 1648 ? 3.0971 2.5118 2.5537 0.6655  -0.5847 -0.3246 1648 TRP A CZ2 
12621 C CZ3 . TRP A 1648 ? 3.0720 2.5561 2.5526 0.6121  -0.5409 -0.2999 1648 TRP A CZ3 
12622 C CH2 . TRP A 1648 ? 3.0870 2.5437 2.5619 0.6429  -0.5688 -0.3064 1648 TRP A CH2 
12623 N N   . PRO A 1649 ? 4.0984 3.5209 3.5837 0.5376  -0.5410 -0.3812 1649 PRO A N   
12624 C CA  . PRO A 1649 ? 4.0481 3.4299 3.5232 0.5454  -0.5547 -0.3988 1649 PRO A CA  
12625 C C   . PRO A 1649 ? 4.0637 3.4023 3.5218 0.5856  -0.5820 -0.4045 1649 PRO A C   
12626 O O   . PRO A 1649 ? 4.0001 3.3387 3.4807 0.5846  -0.6087 -0.4077 1649 PRO A O   
12627 C CB  . PRO A 1649 ? 3.9794 3.3918 3.4937 0.5087  -0.5667 -0.4013 1649 PRO A CB  
12628 C CG  . PRO A 1649 ? 3.9530 3.4253 3.4947 0.4780  -0.5521 -0.3862 1649 PRO A CG  
12629 C CD  . PRO A 1649 ? 4.0071 3.4817 3.5345 0.5016  -0.5469 -0.3733 1649 PRO A CD  
12630 N N   . ARG A 1650 ? 4.1492 3.4527 3.5697 0.6218  -0.5753 -0.4054 1650 ARG A N   
12631 C CA  . ARG A 1650 ? 4.2093 3.4655 3.6084 0.6632  -0.6001 -0.4141 1650 ARG A CA  
12632 C C   . ARG A 1650 ? 4.3471 3.5644 3.7407 0.6650  -0.6134 -0.4323 1650 ARG A C   
12633 O O   . ARG A 1650 ? 4.4083 3.5764 3.7743 0.7002  -0.6268 -0.4432 1650 ARG A O   
12634 C CB  . ARG A 1650 ? 4.1123 3.3402 3.4695 0.7009  -0.5864 -0.4110 1650 ARG A CB  
12635 C CG  . ARG A 1650 ? 3.9621 3.2053 3.3189 0.7186  -0.5898 -0.3964 1650 ARG A CG  
12636 C CD  . ARG A 1650 ? 3.8480 3.0462 3.1786 0.7665  -0.6125 -0.4035 1650 ARG A CD  
12637 N NE  . ARG A 1650 ? 3.7666 2.9220 3.0513 0.7986  -0.5985 -0.4098 1650 ARG A NE  
12638 C CZ  . ARG A 1650 ? 3.7061 2.8163 2.9602 0.8427  -0.6145 -0.4186 1650 ARG A CZ  
12639 N NH1 . ARG A 1650 ? 3.6743 2.7757 2.9404 0.8602  -0.6459 -0.4227 1650 ARG A NH1 
12640 N NH2 . ARG A 1650 ? 3.7063 2.7814 2.9197 0.8701  -0.5992 -0.4233 1650 ARG A NH2 
12641 N N   . ASP A 1651 ? 4.4103 3.6495 3.8301 0.6267  -0.6094 -0.4355 1651 ASP A N   
12642 C CA  . ASP A 1651 ? 4.5071 3.7121 3.9250 0.6216  -0.6190 -0.4516 1651 ASP A CA  
12643 C C   . ASP A 1651 ? 4.5924 3.7597 4.0143 0.6470  -0.6554 -0.4613 1651 ASP A C   
12644 O O   . ASP A 1651 ? 4.6120 3.7329 4.0186 0.6597  -0.6654 -0.4758 1651 ASP A O   
12645 C CB  . ASP A 1651 ? 4.5064 3.7482 3.9571 0.5736  -0.6095 -0.4511 1651 ASP A CB  
12646 C CG  . ASP A 1651 ? 4.5575 3.8164 3.9988 0.5523  -0.5747 -0.4500 1651 ASP A CG  
12647 O OD1 . ASP A 1651 ? 4.6068 3.8325 4.0157 0.5735  -0.5615 -0.4561 1651 ASP A OD1 
12648 O OD2 . ASP A 1651 ? 4.5474 3.8541 4.0159 0.5149  -0.5605 -0.4433 1651 ASP A OD2 
12649 N N   . THR A 1652 ? 4.6512 3.8394 4.0962 0.6542  -0.6749 -0.4531 1652 THR A N   
12650 C CA  . THR A 1652 ? 4.7124 3.8705 4.1668 0.6817  -0.7104 -0.4606 1652 THR A CA  
12651 C C   . THR A 1652 ? 4.7552 3.8810 4.2215 0.6748  -0.7285 -0.4747 1652 THR A C   
12652 O O   . THR A 1652 ? 4.7729 3.8641 4.2438 0.7013  -0.7576 -0.4835 1652 THR A O   
12653 C CB  . THR A 1652 ? 4.7489 3.8644 4.1654 0.7309  -0.7184 -0.4658 1652 THR A CB  
12654 O OG1 . THR A 1652 ? 4.7775 3.8440 4.1566 0.7462  -0.7106 -0.4795 1652 THR A OG1 
12655 C CG2 . THR A 1652 ? 4.7542 3.8970 4.1560 0.7382  -0.6984 -0.4513 1652 THR A CG2 
12656 N N   . THR A 1653 ? 4.7722 3.9103 4.2453 0.6391  -0.7109 -0.4766 1653 THR A N   
12657 C CA  . THR A 1653 ? 4.7986 3.9075 4.2816 0.6261  -0.7222 -0.4888 1653 THR A CA  
12658 C C   . THR A 1653 ? 4.8392 3.9489 4.3051 0.6000  -0.6918 -0.4928 1653 THR A C   
12659 O O   . THR A 1653 ? 4.8759 3.9493 4.3055 0.6185  -0.6804 -0.5009 1653 THR A O   
12660 C CB  . THR A 1653 ? 3.9730 3.0176 3.4406 0.6658  -0.7511 -0.5033 1653 THR A CB  
12661 O OG1 . THR A 1653 ? 3.9577 2.9878 3.4559 0.6528  -0.7728 -0.5095 1653 THR A OG1 
12662 C CG2 . THR A 1653 ? 4.0023 2.9975 3.4228 0.6871  -0.7388 -0.5152 1653 THR A CG2 
12663 N N   . CYS A 1654 ? 4.8415 3.9962 4.3356 0.5574  -0.6783 -0.4864 1654 CYS A N   
12664 C CA  . CYS A 1654 ? 4.8638 4.0316 4.3505 0.5279  -0.6483 -0.4885 1654 CYS A CA  
12665 C C   . CYS A 1654 ? 4.8181 4.0303 4.3447 0.4840  -0.6464 -0.4836 1654 CYS A C   
12666 O O   . CYS A 1654 ? 4.8068 4.0628 4.3599 0.4737  -0.6517 -0.4718 1654 CYS A O   
12667 C CB  . CYS A 1654 ? 4.8948 4.0937 4.3651 0.5291  -0.6197 -0.4786 1654 CYS A CB  
12668 S SG  . CYS A 1654 ? 5.0189 4.2974 4.5267 0.4922  -0.6067 -0.4608 1654 CYS A SG  
12669 N N   . SER A 1655 ? 4.7897 3.9922 4.3213 0.4579  -0.6385 -0.4922 1655 SER A N   
12670 C CA  . SER A 1655 ? 4.7375 3.9816 4.3061 0.4160  -0.6362 -0.4880 1655 SER A CA  
12671 C C   . SER A 1655 ? 4.6752 3.9497 4.2767 0.4162  -0.6585 -0.4773 1655 SER A C   
12672 O O   . SER A 1655 ? 4.6578 3.9872 4.2877 0.3866  -0.6509 -0.4674 1655 SER A O   
12673 C CB  . SER A 1655 ? 4.7460 4.0404 4.3188 0.3847  -0.6031 -0.4823 1655 SER A CB  
12674 O OG  . SER A 1655 ? 4.7632 4.0936 4.3336 0.3938  -0.5932 -0.4697 1655 SER A OG  
12675 N N   . SER A 1656 ? 4.6241 3.8632 4.2226 0.4507  -0.6858 -0.4796 1656 SER A N   
12676 C CA  . SER A 1656 ? 4.5296 3.7933 4.1584 0.4602  -0.7086 -0.4694 1656 SER A CA  
12677 C C   . SER A 1656 ? 4.4280 3.7545 4.0705 0.4482  -0.6950 -0.4534 1656 SER A C   
12678 O O   . SER A 1656 ? 4.3817 3.7578 4.0567 0.4168  -0.6911 -0.4445 1656 SER A O   
12679 C CB  . SER A 1656 ? 4.5026 3.7691 4.1700 0.4426  -0.7289 -0.4698 1656 SER A CB  
12680 O OG  . SER A 1656 ? 4.4895 3.7641 4.1846 0.4623  -0.7556 -0.4629 1656 SER A OG  
12681 N N   . CYS A 1657 ? 4.3797 3.7026 3.9971 0.4739  -0.6882 -0.4495 1657 CYS A N   
12682 C CA  . CYS A 1657 ? 4.2918 3.6674 3.9204 0.4672  -0.6773 -0.4338 1657 CYS A CA  
12683 C C   . CYS A 1657 ? 4.2101 3.5924 3.8621 0.4890  -0.7048 -0.4268 1657 CYS A C   
12684 O O   . CYS A 1657 ? 4.2108 3.5531 3.8656 0.5131  -0.7304 -0.4352 1657 CYS A O   
12685 C CB  . CYS A 1657 ? 4.3216 3.6893 3.9121 0.4839  -0.6543 -0.4318 1657 CYS A CB  
12686 S SG  . CYS A 1657 ? 4.9585 4.2965 4.5130 0.4773  -0.6258 -0.4438 1657 CYS A SG  
12687 N N   . GLN A 1658 ? 4.1334 3.5665 3.8047 0.4801  -0.6996 -0.4114 1658 GLN A N   
12688 C CA  . GLN A 1658 ? 4.0766 3.5210 3.7696 0.5019  -0.7220 -0.4031 1658 GLN A CA  
12689 C C   . GLN A 1658 ? 4.0127 3.5256 3.7449 0.4751  -0.7178 -0.3857 1658 GLN A C   
12690 O O   . GLN A 1658 ? 4.0057 3.5568 3.7475 0.4400  -0.6983 -0.3806 1658 GLN A O   
12691 C CB  . GLN A 1658 ? 4.0554 3.4659 3.7677 0.5223  -0.7551 -0.4119 1658 GLN A CB  
12692 C CG  . GLN A 1658 ? 4.0516 3.4489 3.7691 0.5603  -0.7781 -0.4099 1658 GLN A CG  
12693 C CD  . GLN A 1658 ? 4.0784 3.4431 3.7482 0.5907  -0.7679 -0.4137 1658 GLN A CD  
12694 O OE1 . GLN A 1658 ? 4.0768 3.4693 3.7341 0.5848  -0.7474 -0.4030 1658 GLN A OE1 
12695 N NE2 . GLN A 1658 ? 4.1049 3.4097 3.7481 0.6245  -0.7825 -0.4285 1658 GLN A NE2 
12696 N N   . ALA A 1659 ? 3.9631 3.4925 3.7193 0.4917  -0.7362 -0.3769 1659 ALA A N   
12697 C CA  . ALA A 1659 ? 3.8951 3.4896 3.6895 0.4684  -0.7329 -0.3594 1659 ALA A CA  
12698 C C   . ALA A 1659 ? 3.8860 3.5101 3.6608 0.4516  -0.7024 -0.3495 1659 ALA A C   
12699 O O   . ALA A 1659 ? 3.8634 3.5392 3.6641 0.4344  -0.6970 -0.3342 1659 ALA A O   
12700 C CB  . ALA A 1659 ? 3.8460 3.4752 3.6810 0.4365  -0.7381 -0.3568 1659 ALA A CB  
12701 N N   . PHE A 1660 ? 3.8929 3.4847 3.6244 0.4566  -0.6823 -0.3578 1660 PHE A N   
12702 C CA  . PHE A 1660 ? 3.8670 3.4766 3.5766 0.4491  -0.6540 -0.3491 1660 PHE A CA  
12703 C C   . PHE A 1660 ? 3.7758 3.3444 3.4483 0.4883  -0.6539 -0.3505 1660 PHE A C   
12704 O O   . PHE A 1660 ? 3.7704 3.3538 3.4311 0.4907  -0.6374 -0.3394 1660 PHE A O   
12705 C CB  . PHE A 1660 ? 3.9495 3.5602 3.6419 0.4246  -0.6279 -0.3553 1660 PHE A CB  
12706 C CG  . PHE A 1660 ? 4.0141 3.6393 3.6854 0.4200  -0.5987 -0.3469 1660 PHE A CG  
12707 C CD1 . PHE A 1660 ? 4.0148 3.6920 3.7084 0.3996  -0.5884 -0.3306 1660 PHE A CD1 
12708 C CD2 . PHE A 1660 ? 4.0561 3.6430 3.6876 0.4364  -0.5813 -0.3546 1660 PHE A CD2 
12709 C CE1 . PHE A 1660 ? 4.0289 3.7170 3.7052 0.3961  -0.5619 -0.3223 1660 PHE A CE1 
12710 C CE2 . PHE A 1660 ? 4.0692 3.6691 3.6848 0.4338  -0.5543 -0.3459 1660 PHE A CE2 
12711 C CZ  . PHE A 1660 ? 4.0540 3.7031 3.6920 0.4138  -0.5448 -0.3298 1660 PHE A CZ  
12712 N N   . LEU A 1661 ? 3.6887 3.2047 3.3430 0.5196  -0.6724 -0.3641 1661 LEU A N   
12713 C CA  . LEU A 1661 ? 3.6381 3.1139 3.2586 0.5606  -0.6766 -0.3665 1661 LEU A CA  
12714 C C   . LEU A 1661 ? 3.7216 3.2109 3.3663 0.5791  -0.6993 -0.3581 1661 LEU A C   
12715 O O   . LEU A 1661 ? 3.7353 3.2144 3.3603 0.6034  -0.6967 -0.3526 1661 LEU A O   
12716 C CB  . LEU A 1661 ? 3.5084 2.9221 3.0988 0.5875  -0.6872 -0.3852 1661 LEU A CB  
12717 C CG  . LEU A 1661 ? 3.4121 2.8018 2.9624 0.5864  -0.6600 -0.3914 1661 LEU A CG  
12718 C CD1 . LEU A 1661 ? 3.3901 2.7310 2.9249 0.5967  -0.6704 -0.4097 1661 LEU A CD1 
12719 C CD2 . LEU A 1661 ? 3.4101 2.7809 2.9238 0.6169  -0.6474 -0.3863 1661 LEU A CD2 
12720 N N   . ALA A 1662 ? 3.7965 3.3096 3.4857 0.5679  -0.7213 -0.3568 1662 ALA A N   
12721 C CA  . ALA A 1662 ? 3.8838 3.4155 3.6050 0.5832  -0.7439 -0.3488 1662 ALA A CA  
12722 C C   . ALA A 1662 ? 3.9559 3.5320 3.6847 0.5707  -0.7276 -0.3301 1662 ALA A C   
12723 O O   . ALA A 1662 ? 3.9722 3.5529 3.7098 0.5909  -0.7390 -0.3232 1662 ALA A O   
12724 C CB  . ALA A 1662 ? 3.8571 3.4156 3.6308 0.5677  -0.7658 -0.3481 1662 ALA A CB  
12725 N N   . ASN A 1663 ? 4.0099 3.6179 3.7363 0.5371  -0.7009 -0.3222 1663 ASN A N   
12726 C CA  . ASN A 1663 ? 4.0923 3.7448 3.8288 0.5195  -0.6834 -0.3037 1663 ASN A CA  
12727 C C   . ASN A 1663 ? 4.1634 3.7927 3.8547 0.5337  -0.6596 -0.3003 1663 ASN A C   
12728 O O   . ASN A 1663 ? 4.2524 3.8991 3.9456 0.5373  -0.6533 -0.2863 1663 ASN A O   
12729 C CB  . ASN A 1663 ? 4.2109 3.9162 3.9758 0.4743  -0.6688 -0.2959 1663 ASN A CB  
12730 C CG  . ASN A 1663 ? 4.3491 4.0827 4.1617 0.4593  -0.6907 -0.2965 1663 ASN A CG  
12731 O OD1 . ASN A 1663 ? 4.4034 4.1378 4.2422 0.4773  -0.7157 -0.2951 1663 ASN A OD1 
12732 N ND2 . ASN A 1663 ? 4.3832 4.1413 4.2094 0.4270  -0.6815 -0.2983 1663 ASN A ND2 
12733 N N   . LEU A 1664 ? 3.9276 3.5188 3.5803 0.5411  -0.6455 -0.3120 1664 LEU A N   
12734 C CA  . LEU A 1664 ? 3.8316 3.3976 3.4417 0.5585  -0.6228 -0.3091 1664 LEU A CA  
12735 C C   . LEU A 1664 ? 3.7995 3.3196 3.3823 0.6041  -0.6377 -0.3142 1664 LEU A C   
12736 O O   . LEU A 1664 ? 3.8201 3.3229 3.3724 0.6237  -0.6233 -0.3079 1664 LEU A O   
12737 C CB  . LEU A 1664 ? 3.8094 3.3541 3.3919 0.5508  -0.6019 -0.3194 1664 LEU A CB  
12738 C CG  . LEU A 1664 ? 3.7351 3.3216 3.3271 0.5162  -0.5732 -0.3079 1664 LEU A CG  
12739 C CD1 . LEU A 1664 ? 3.7283 3.2934 3.2931 0.5128  -0.5504 -0.3173 1664 LEU A CD1 
12740 C CD2 . LEU A 1664 ? 3.7213 3.3210 3.3081 0.5242  -0.5616 -0.2906 1664 LEU A CD2 
12741 N N   . ASP A 1665 ? 3.7283 3.2276 3.3224 0.6219  -0.6667 -0.3258 1665 ASP A N   
12742 C CA  . ASP A 1665 ? 3.6908 3.1534 3.2680 0.6646  -0.6859 -0.3307 1665 ASP A CA  
12743 C C   . ASP A 1665 ? 3.7334 3.2348 3.3473 0.6619  -0.6984 -0.3161 1665 ASP A C   
12744 O O   . ASP A 1665 ? 3.8485 3.3339 3.4495 0.6912  -0.7054 -0.3129 1665 ASP A O   
12745 C CB  . ASP A 1665 ? 3.5866 3.0104 3.1638 0.6853  -0.7126 -0.3497 1665 ASP A CB  
12746 C CG  . ASP A 1665 ? 3.5347 2.9007 3.0685 0.7323  -0.7206 -0.3611 1665 ASP A CG  
12747 O OD1 . ASP A 1665 ? 3.5268 2.8505 3.0327 0.7448  -0.7207 -0.3765 1665 ASP A OD1 
12748 O OD2 . ASP A 1665 ? 3.5156 2.8789 3.0432 0.7565  -0.7262 -0.3546 1665 ASP A OD2 
12749 N N   . GLU A 1666 ? 3.6810 3.2347 3.3412 0.6260  -0.7003 -0.3069 1666 GLU A N   
12750 C CA  . GLU A 1666 ? 3.7367 3.3367 3.4384 0.6162  -0.7092 -0.2909 1666 GLU A CA  
12751 C C   . GLU A 1666 ? 3.7530 3.3754 3.4430 0.6042  -0.6831 -0.2731 1666 GLU A C   
12752 O O   . GLU A 1666 ? 3.8277 3.4394 3.5057 0.6267  -0.6844 -0.2662 1666 GLU A O   
12753 C CB  . GLU A 1666 ? 3.8537 3.5038 3.6087 0.5811  -0.7180 -0.2864 1666 GLU A CB  
12754 C CG  . GLU A 1666 ? 4.0057 3.7123 3.8075 0.5642  -0.7229 -0.2679 1666 GLU A CG  
12755 C CD  . GLU A 1666 ? 4.2057 3.9040 4.0261 0.5959  -0.7492 -0.2678 1666 GLU A CD  
12756 O OE1 . GLU A 1666 ? 4.2448 3.9799 4.1184 0.5881  -0.7690 -0.2627 1666 GLU A OE1 
12757 O OE2 . GLU A 1666 ? 4.3211 3.9772 4.1044 0.6295  -0.7502 -0.2730 1666 GLU A OE2 
12758 N N   . PHE A 1667 ? 3.6016 3.2556 3.2972 0.5681  -0.6601 -0.2657 1667 PHE A N   
12759 C CA  . PHE A 1667 ? 3.3990 3.0648 3.0765 0.5569  -0.6314 -0.2515 1667 PHE A CA  
12760 C C   . PHE A 1667 ? 3.4180 3.0362 3.0504 0.5961  -0.6260 -0.2521 1667 PHE A C   
12761 O O   . PHE A 1667 ? 3.4435 3.0705 3.0751 0.6016  -0.6195 -0.2375 1667 PHE A O   
12762 C CB  . PHE A 1667 ? 3.0994 2.7710 2.7647 0.5306  -0.6076 -0.2555 1667 PHE A CB  
12763 C CG  . PHE A 1667 ? 2.7355 2.4143 2.3813 0.5205  -0.5766 -0.2430 1667 PHE A CG  
12764 C CD1 . PHE A 1667 ? 2.5224 2.2518 2.1965 0.4842  -0.5625 -0.2287 1667 PHE A CD1 
12765 C CD2 . PHE A 1667 ? 2.5919 2.2265 2.1921 0.5480  -0.5611 -0.2456 1667 PHE A CD2 
12766 C CE1 . PHE A 1667 ? 2.4301 2.1638 2.0882 0.4761  -0.5344 -0.2174 1667 PHE A CE1 
12767 C CE2 . PHE A 1667 ? 2.4843 2.1242 2.0693 0.5405  -0.5324 -0.2334 1667 PHE A CE2 
12768 C CZ  . PHE A 1667 ? 2.4255 2.1137 2.0397 0.5048  -0.5194 -0.2196 1667 PHE A CZ  
12769 N N   . ALA A 1668 ? 3.3918 2.9592 2.9878 0.6241  -0.6296 -0.2688 1668 ALA A N   
12770 C CA  . ALA A 1668 ? 3.3983 2.9177 2.9460 0.6622  -0.6212 -0.2709 1668 ALA A CA  
12771 C C   . ALA A 1668 ? 3.5287 3.0405 3.0764 0.6904  -0.6355 -0.2635 1668 ALA A C   
12772 O O   . ALA A 1668 ? 3.5292 3.0438 3.0635 0.6942  -0.6186 -0.2487 1668 ALA A O   
12773 C CB  . ALA A 1668 ? 3.3310 2.7996 2.8460 0.6880  -0.6285 -0.2917 1668 ALA A CB  
12774 N N   . GLU A 1669 ? 3.6795 3.1805 3.2430 0.7108  -0.6665 -0.2738 1669 GLU A N   
12775 C CA  . GLU A 1669 ? 3.8300 3.3255 3.3979 0.7381  -0.6827 -0.2686 1669 GLU A CA  
12776 C C   . GLU A 1669 ? 3.9039 3.4559 3.5194 0.7097  -0.6835 -0.2496 1669 GLU A C   
12777 O O   . GLU A 1669 ? 3.9164 3.4754 3.5499 0.7255  -0.7001 -0.2445 1669 GLU A O   
12778 C CB  . GLU A 1669 ? 3.8502 3.3196 3.4265 0.7684  -0.7168 -0.2862 1669 GLU A CB  
12779 C CG  . GLU A 1669 ? 3.8813 3.3196 3.4365 0.8117  -0.7298 -0.2882 1669 GLU A CG  
12780 C CD  . GLU A 1669 ? 3.9306 3.3153 3.4224 0.8433  -0.7136 -0.2949 1669 GLU A CD  
12781 O OE1 . GLU A 1669 ? 3.9395 3.3137 3.4071 0.8301  -0.6919 -0.2975 1669 GLU A OE1 
12782 O OE2 . GLU A 1669 ? 3.9597 3.3139 3.4269 0.8817  -0.7224 -0.2977 1669 GLU A OE2 
12783 N N   . ASP A 1670 ? 3.9560 3.5490 3.5928 0.6678  -0.6658 -0.2395 1670 ASP A N   
12784 C CA  . ASP A 1670 ? 3.9836 3.6344 3.6667 0.6356  -0.6637 -0.2207 1670 ASP A CA  
12785 C C   . ASP A 1670 ? 3.9753 3.6373 3.6428 0.6215  -0.6341 -0.2018 1670 ASP A C   
12786 O O   . ASP A 1670 ? 3.9548 3.6516 3.6509 0.6069  -0.6332 -0.1849 1670 ASP A O   
12787 C CB  . ASP A 1670 ? 4.0215 3.7160 3.7455 0.5971  -0.6667 -0.2216 1670 ASP A CB  
12788 C CG  . ASP A 1670 ? 4.0476 3.8047 3.8179 0.5608  -0.6610 -0.2015 1670 ASP A CG  
12789 O OD1 . ASP A 1670 ? 4.0325 3.8280 3.8516 0.5452  -0.6794 -0.2004 1670 ASP A OD1 
12790 O OD2 . ASP A 1670 ? 4.0725 3.8410 3.8321 0.5478  -0.6380 -0.1863 1670 ASP A OD2 
12791 N N   . ILE A 1671 ? 3.9758 3.6089 3.6007 0.6255  -0.6096 -0.2041 1671 ILE A N   
12792 C CA  . ILE A 1671 ? 3.9375 3.5810 3.5504 0.6101  -0.5797 -0.1865 1671 ILE A CA  
12793 C C   . ILE A 1671 ? 3.9545 3.5797 3.5501 0.6344  -0.5759 -0.1733 1671 ILE A C   
12794 O O   . ILE A 1671 ? 3.9166 3.5748 3.5385 0.6157  -0.5717 -0.1553 1671 ILE A O   
12795 C CB  . ILE A 1671 ? 3.9230 3.5387 3.4971 0.6121  -0.5545 -0.1927 1671 ILE A CB  
12796 C CG1 . ILE A 1671 ? 3.9044 3.5223 3.4637 0.6052  -0.5247 -0.1740 1671 ILE A CG1 
12797 C CG2 . ILE A 1671 ? 3.9550 3.5132 3.4860 0.6548  -0.5622 -0.2096 1671 ILE A CG2 
12798 C CD1 . ILE A 1671 ? 3.8491 3.5219 3.4495 0.5635  -0.5164 -0.1569 1671 ILE A CD1 
12799 N N   . PHE A 1672 ? 4.0100 3.5824 3.5610 0.6758  -0.5768 -0.1822 1672 PHE A N   
12800 C CA  . PHE A 1672 ? 4.0312 3.5783 3.5576 0.7039  -0.5715 -0.1710 1672 PHE A CA  
12801 C C   . PHE A 1672 ? 4.0290 3.6064 3.5939 0.6987  -0.5899 -0.1601 1672 PHE A C   
12802 O O   . PHE A 1672 ? 4.0633 3.6492 3.6303 0.6942  -0.5776 -0.1413 1672 PHE A O   
12803 C CB  . PHE A 1672 ? 4.0307 3.5193 3.5098 0.7530  -0.5795 -0.1866 1672 PHE A CB  
12804 C CG  . PHE A 1672 ? 3.9714 3.4512 3.4638 0.7726  -0.6141 -0.2052 1672 PHE A CG  
12805 C CD1 . PHE A 1672 ? 3.9430 3.4202 3.4472 0.7954  -0.6365 -0.2041 1672 PHE A CD1 
12806 C CD2 . PHE A 1672 ? 3.9424 3.4154 3.4370 0.7687  -0.6244 -0.2237 1672 PHE A CD2 
12807 C CE1 . PHE A 1672 ? 3.9186 3.3877 3.4385 0.8146  -0.6687 -0.2214 1672 PHE A CE1 
12808 C CE2 . PHE A 1672 ? 3.9175 3.3800 3.4262 0.7875  -0.6563 -0.2402 1672 PHE A CE2 
12809 C CZ  . PHE A 1672 ? 3.9089 3.3697 3.4309 0.8110  -0.6787 -0.2392 1672 PHE A CZ  
12810 N N   . LEU A 1673 ? 3.9796 3.5739 3.5779 0.6991  -0.6192 -0.1715 1673 LEU A N   
12811 C CA  . LEU A 1673 ? 3.9179 3.5417 3.5578 0.6977  -0.6400 -0.1636 1673 LEU A CA  
12812 C C   . LEU A 1673 ? 3.7544 3.4378 3.4412 0.6524  -0.6306 -0.1435 1673 LEU A C   
12813 O O   . LEU A 1673 ? 3.7485 3.4453 3.4460 0.6484  -0.6250 -0.1262 1673 LEU A O   
12814 C CB  . LEU A 1673 ? 3.9986 3.6213 3.6630 0.7147  -0.6745 -0.1820 1673 LEU A CB  
12815 C CG  . LEU A 1673 ? 4.0792 3.7048 3.7553 0.7047  -0.6856 -0.1991 1673 LEU A CG  
12816 C CD1 . LEU A 1673 ? 4.0549 3.7415 3.7875 0.6608  -0.6882 -0.1906 1673 LEU A CD1 
12817 C CD2 . LEU A 1673 ? 4.1276 3.7245 3.8055 0.7408  -0.7176 -0.2188 1673 LEU A CD2 
12818 N N   . ASN A 1674 ? 3.5928 3.3113 3.3070 0.6184  -0.6282 -0.1455 1674 ASN A N   
12819 C CA  . ASN A 1674 ? 3.3999 3.1752 3.1563 0.5751  -0.6179 -0.1270 1674 ASN A CA  
12820 C C   . ASN A 1674 ? 3.2407 3.0113 2.9725 0.5615  -0.5855 -0.1100 1674 ASN A C   
12821 O O   . ASN A 1674 ? 3.1884 3.0013 2.9506 0.5277  -0.5745 -0.0928 1674 ASN A O   
12822 C CB  . ASN A 1674 ? 3.3721 3.1860 3.1620 0.5434  -0.6228 -0.1334 1674 ASN A CB  
12823 C CG  . ASN A 1674 ? 3.3153 3.1732 3.1644 0.5338  -0.6501 -0.1326 1674 ASN A CG  
12824 O OD1 . ASN A 1674 ? 3.2823 3.1678 3.1628 0.5292  -0.6563 -0.1184 1674 ASN A OD1 
12825 N ND2 . ASN A 1674 ? 3.2966 3.1622 3.1637 0.5304  -0.6660 -0.1471 1674 ASN A ND2 
12826 N N   . GLY A 1675 ? 3.1335 2.8523 2.8118 0.5891  -0.5704 -0.1146 1675 GLY A N   
12827 C CA  . GLY A 1675 ? 2.9977 2.7053 2.6512 0.5822  -0.5397 -0.0986 1675 GLY A CA  
12828 C C   . GLY A 1675 ? 2.8172 2.5731 2.5022 0.5354  -0.5238 -0.0873 1675 GLY A C   
12829 O O   . GLY A 1675 ? 2.7762 2.5600 2.4838 0.5135  -0.5303 -0.0969 1675 GLY A O   
12830 N N   . CYS A 1676 ? 2.7107 2.4761 2.3979 0.5201  -0.5033 -0.0666 1676 CYS A N   
12831 C CA  . CYS A 1676 ? 2.5973 2.4085 2.3146 0.4760  -0.4879 -0.0549 1676 CYS A CA  
12832 C C   . CYS A 1676 ? 2.5281 2.3404 2.2449 0.4661  -0.4673 -0.0311 1676 CYS A C   
12833 O O   . CYS A 1676 ? 2.4712 2.3244 2.2266 0.4393  -0.4701 -0.0160 1676 CYS A O   
12834 C CB  . CYS A 1676 ? 2.6094 2.4140 2.3085 0.4667  -0.4714 -0.0662 1676 CYS A CB  
12835 S SG  . CYS A 1676 ? 3.6436 3.4971 3.3718 0.4169  -0.4479 -0.0524 1676 CYS A SG  
12836 O OXT . CYS A 1676 ? 2.5338 2.3051 2.2122 0.4855  -0.4473 -0.0262 1676 CYS A OXT 
12837 N N   . LEU B 40   ? 2.5229 1.9086 3.5514 -0.4158 0.0184  0.0458  40   LEU X N   
12838 C CA  . LEU B 40   ? 2.5593 1.9031 3.5569 -0.3880 0.0608  0.0633  40   LEU X CA  
12839 C C   . LEU B 40   ? 2.5777 1.9266 3.5173 -0.3902 0.0438  0.0913  40   LEU X C   
12840 O O   . LEU B 40   ? 2.6219 1.9222 3.5462 -0.3752 0.0724  0.1031  40   LEU X O   
12841 C CB  . LEU B 40   ? 2.5282 1.8874 3.5034 -0.3620 0.0862  0.0661  40   LEU X CB  
12842 C CG  . LEU B 40   ? 2.4921 1.8378 3.5288 -0.3559 0.1102  0.0377  40   LEU X CG  
12843 C CD1 . LEU B 40   ? 2.4978 1.8617 3.5116 -0.3305 0.1332  0.0410  40   LEU X CD1 
12844 C CD2 . LEU B 40   ? 2.4925 1.7647 3.5830 -0.3495 0.1503  0.0239  40   LEU X CD2 
12845 N N   . HIS B 41   ? 2.5947 2.0030 3.5020 -0.4083 -0.0022 0.1015  41   HIS X N   
12846 C CA  . HIS B 41   ? 2.6051 2.0258 3.4745 -0.4213 -0.0318 0.1221  41   HIS X CA  
12847 C C   . HIS B 41   ? 2.9334 2.3331 3.7466 -0.3977 -0.0117 0.1475  41   HIS X C   
12848 O O   . HIS B 41   ? 2.9575 2.2992 3.7752 -0.3776 0.0292  0.1486  41   HIS X O   
12849 C CB  . HIS B 41   ? 2.8771 2.2708 3.7925 -0.4463 -0.0490 0.1103  41   HIS X CB  
12850 C CG  . HIS B 41   ? 2.8781 2.2786 3.8540 -0.4649 -0.0632 0.0822  41   HIS X CG  
12851 N ND1 . HIS B 41   ? 2.8900 2.2482 3.9221 -0.4554 -0.0289 0.0585  41   HIS X ND1 
12852 C CD2 . HIS B 41   ? 2.8471 2.2896 3.8361 -0.4919 -0.1085 0.0736  41   HIS X CD2 
12853 C CE1 . HIS B 41   ? 2.8585 2.2342 3.9364 -0.4748 -0.0537 0.0354  41   HIS X CE1 
12854 N NE2 . HIS B 41   ? 2.8350 2.2608 3.8855 -0.4969 -0.1023 0.0445  41   HIS X NE2 
12855 N N   . ASP B 42   ? 2.9224 2.3694 3.6831 -0.4007 -0.0414 0.1670  42   ASP X N   
12856 C CA  . ASP B 42   ? 2.9321 2.3686 3.6363 -0.3808 -0.0329 0.1909  42   ASP X CA  
12857 C C   . ASP B 42   ? 2.8704 2.3742 3.5263 -0.3827 -0.0651 0.2055  42   ASP X C   
12858 O O   . ASP B 42   ? 2.8734 2.4221 3.5354 -0.3899 -0.0784 0.1972  42   ASP X O   
12859 C CB  . ASP B 42   ? 3.0054 2.3913 3.6953 -0.3449 0.0188  0.1941  42   ASP X CB  
12860 C CG  . ASP B 42   ? 3.0456 2.4033 3.6827 -0.3244 0.0304  0.2164  42   ASP X CG  
12861 O OD1 . ASP B 42   ? 3.0369 2.4356 3.6275 -0.3239 0.0025  0.2327  42   ASP X OD1 
12862 O OD2 . ASP B 42   ? 3.0760 2.3693 3.7183 -0.3082 0.0684  0.2168  42   ASP X OD2 
12863 N N   . ILE B 43   ? 2.7948 2.3062 3.4044 -0.3764 -0.0776 0.2258  43   ILE X N   
12864 C CA  . ILE B 43   ? 2.7292 2.3038 3.2959 -0.3776 -0.1070 0.2385  43   ILE X CA  
12865 C C   . ILE B 43   ? 2.7309 2.3080 3.2549 -0.3431 -0.0828 0.2472  43   ILE X C   
12866 O O   . ILE B 43   ? 2.6999 2.3290 3.2070 -0.3421 -0.0962 0.2474  43   ILE X O   
12867 C CB  . ILE B 43   ? 2.6997 2.2948 3.2424 -0.3929 -0.1422 0.2541  43   ILE X CB  
12868 C CG1 . ILE B 43   ? 2.6377 2.3041 3.1478 -0.4001 -0.1750 0.2631  43   ILE X CG1 
12869 C CG2 . ILE B 43   ? 2.7564 2.3043 3.2687 -0.3690 -0.1213 0.2679  43   ILE X CG2 
12870 C CD1 . ILE B 43   ? 2.5886 2.2828 3.0799 -0.4176 -0.2123 0.2772  43   ILE X CD1 
12871 N N   . ARG B 44   ? 2.7752 2.2953 3.2815 -0.3147 -0.0472 0.2541  44   ARG X N   
12872 C CA  . ARG B 44   ? 2.8282 2.3429 3.2921 -0.2793 -0.0235 0.2628  44   ARG X CA  
12873 C C   . ARG B 44   ? 2.8999 2.4304 3.3832 -0.2714 -0.0065 0.2489  44   ARG X C   
12874 O O   . ARG B 44   ? 2.9218 2.4925 3.3769 -0.2588 -0.0129 0.2525  44   ARG X O   
12875 C CB  . ARG B 44   ? 2.8127 2.2546 3.2548 -0.2506 0.0145  0.2720  44   ARG X CB  
12876 C CG  . ARG B 44   ? 2.7706 2.2136 3.1566 -0.2358 0.0013  0.2919  44   ARG X CG  
12877 C CD  . ARG B 44   ? 2.7480 2.1229 3.1258 -0.2255 0.0245  0.2989  44   ARG X CD  
12878 N NE  . ARG B 44   ? 2.6826 2.0456 3.1084 -0.2572 0.0134  0.2896  44   ARG X NE  
12879 C CZ  . ARG B 44   ? 2.6481 1.9761 3.0705 -0.2613 0.0134  0.2955  44   ARG X CZ  
12880 N NH1 . ARG B 44   ? 2.6581 1.9592 3.0286 -0.2356 0.0237  0.3113  44   ARG X NH1 
12881 N NH2 . ARG B 44   ? 2.6096 1.9294 3.0809 -0.2909 0.0020  0.2846  44   ARG X NH2 
12882 N N   . ASP B 45   ? 2.9520 2.4525 3.4864 -0.2792 0.0140  0.2317  45   ASP X N   
12883 C CA  . ASP B 45   ? 2.9985 2.5073 3.5589 -0.2710 0.0337  0.2160  45   ASP X CA  
12884 C C   . ASP B 45   ? 2.9865 2.5699 3.5544 -0.2914 -0.0002 0.2073  45   ASP X C   
12885 O O   . ASP B 45   ? 2.9892 2.6013 3.5456 -0.2772 0.0064  0.2040  45   ASP X O   
12886 C CB  . ASP B 45   ? 3.0271 2.4867 3.6468 -0.2772 0.0607  0.1974  45   ASP X CB  
12887 C CG  . ASP B 45   ? 3.0913 2.4733 3.7068 -0.2543 0.1033  0.2037  45   ASP X CG  
12888 O OD1 . ASP B 45   ? 3.1317 2.4957 3.6946 -0.2287 0.1160  0.2222  45   ASP X OD1 
12889 O OD2 . ASP B 45   ? 3.0996 2.4375 3.7645 -0.2617 0.1243  0.1894  45   ASP X OD2 
12890 N N   . LEU B 46   ? 2.9716 2.5848 3.5586 -0.3248 -0.0360 0.2033  46   LEU X N   
12891 C CA  . LEU B 46   ? 2.9600 2.6400 3.5543 -0.3471 -0.0681 0.1949  46   LEU X CA  
12892 C C   . LEU B 46   ? 2.9606 2.6952 3.5057 -0.3391 -0.0855 0.2080  46   LEU X C   
12893 O O   . LEU B 46   ? 2.9412 2.7320 3.4868 -0.3514 -0.1045 0.2011  46   LEU X O   
12894 C CB  . LEU B 46   ? 2.9433 2.6392 3.5611 -0.3837 -0.1044 0.1912  46   LEU X CB  
12895 C CG  . LEU B 46   ? 2.9475 2.5910 3.6146 -0.3953 -0.0948 0.1786  46   LEU X CG  
12896 C CD1 . LEU B 46   ? 2.9136 2.5849 3.6031 -0.4322 -0.1366 0.1725  46   LEU X CD1 
12897 C CD2 . LEU B 46   ? 2.9706 2.5806 3.6807 -0.3819 -0.0592 0.1580  46   LEU X CD2 
12898 N N   . HIS B 47   ? 2.9740 2.6915 3.4775 -0.3183 -0.0789 0.2259  47   HIS X N   
12899 C CA  . HIS B 47   ? 2.9602 2.7232 3.4181 -0.3061 -0.0927 0.2374  47   HIS X CA  
12900 C C   . HIS B 47   ? 2.9710 2.7245 3.4142 -0.2718 -0.0614 0.2346  47   HIS X C   
12901 O O   . HIS B 47   ? 2.9680 2.7630 3.3808 -0.2606 -0.0709 0.2391  47   HIS X O   
12902 C CB  . HIS B 47   ? 2.9602 2.7112 3.3801 -0.2995 -0.1048 0.2569  47   HIS X CB  
12903 C CG  . HIS B 47   ? 2.9444 2.7501 3.3244 -0.2945 -0.1285 0.2669  47   HIS X CG  
12904 N ND1 . HIS B 47   ? 2.9186 2.7511 3.2797 -0.3098 -0.1612 0.2790  47   HIS X ND1 
12905 C CD2 . HIS B 47   ? 2.9431 2.7827 3.3022 -0.2763 -0.1246 0.2652  47   HIS X CD2 
12906 C CE1 . HIS B 47   ? 2.9096 2.7898 3.2407 -0.3010 -0.1756 0.2840  47   HIS X CE1 
12907 N NE2 . HIS B 47   ? 2.9269 2.8124 3.2560 -0.2808 -0.1542 0.2755  47   HIS X NE2 
12908 N N   . ARG B 48   ? 2.9731 2.6708 3.4396 -0.2552 -0.0240 0.2268  48   ARG X N   
12909 C CA  . ARG B 48   ? 2.9814 2.6605 3.4365 -0.2215 0.0090  0.2246  48   ARG X CA  
12910 C C   . ARG B 48   ? 2.9176 2.6187 3.4126 -0.2259 0.0192  0.2038  48   ARG X C   
12911 O O   . ARG B 48   ? 2.9356 2.6554 3.4196 -0.2059 0.0306  0.2002  48   ARG X O   
12912 C CB  . ARG B 48   ? 3.0424 2.6408 3.4922 -0.1958 0.0484  0.2315  48   ARG X CB  
12913 C CG  . ARG B 48   ? 3.0762 2.6475 3.4864 -0.1895 0.0410  0.2510  48   ARG X CG  
12914 C CD  . ARG B 48   ? 3.1380 2.6265 3.5438 -0.1656 0.0829  0.2567  48   ARG X CD  
12915 N NE  . ARG B 48   ? 3.1499 2.6024 3.6127 -0.1779 0.1062  0.2406  48   ARG X NE  
12916 C CZ  . ARG B 48   ? 3.1948 2.5754 3.6680 -0.1600 0.1484  0.2404  48   ARG X CZ  
12917 N NH1 . ARG B 48   ? 3.1922 2.5455 3.7234 -0.1731 0.1672  0.2231  48   ARG X NH1 
12918 N NH2 . ARG B 48   ? 3.2394 2.5746 3.6649 -0.1286 0.1721  0.2569  48   ARG X NH2 
12919 N N   . TYR B 49   ? 2.8370 2.5352 3.3793 -0.2512 0.0142  0.1890  49   TYR X N   
12920 C CA  . TYR B 49   ? 2.7681 2.4848 3.3522 -0.2562 0.0228  0.1671  49   TYR X CA  
12921 C C   . TYR B 49   ? 2.6689 2.4645 3.2464 -0.2747 -0.0102 0.1607  49   TYR X C   
12922 O O   . TYR B 49   ? 2.6671 2.4896 3.2561 -0.2666 -0.0014 0.1477  49   TYR X O   
12923 C CB  . TYR B 49   ? 2.7640 2.4479 3.4028 -0.2755 0.0280  0.1515  49   TYR X CB  
12924 C CG  . TYR B 49   ? 2.7967 2.4010 3.4533 -0.2579 0.0671  0.1527  49   TYR X CG  
12925 C CD1 . TYR B 49   ? 2.8229 2.3915 3.5187 -0.2420 0.1042  0.1369  49   TYR X CD1 
12926 C CD2 . TYR B 49   ? 2.8004 2.3652 3.4368 -0.2579 0.0675  0.1687  49   TYR X CD2 
12927 C CE1 . TYR B 49   ? 2.8520 2.3465 3.5655 -0.2269 0.1423  0.1378  49   TYR X CE1 
12928 C CE2 . TYR B 49   ? 2.8320 2.3233 3.4840 -0.2426 0.1051  0.1694  49   TYR X CE2 
12929 C CZ  . TYR B 49   ? 2.8607 2.3166 3.5510 -0.2274 0.1431  0.1542  49   TYR X CZ  
12930 O OH  . TYR B 49   ? 2.8964 2.2779 3.6029 -0.2130 0.1829  0.1549  49   TYR X OH  
12931 N N   . TYR B 50   ? 2.5894 2.4213 3.1491 -0.3000 -0.0473 0.1696  50   TYR X N   
12932 C CA  . TYR B 50   ? 2.5116 2.4165 3.0644 -0.3216 -0.0791 0.1645  50   TYR X CA  
12933 C C   . TYR B 50   ? 2.4656 2.4140 2.9737 -0.3082 -0.0881 0.1757  50   TYR X C   
12934 O O   . TYR B 50   ? 2.4194 2.4295 2.9198 -0.3237 -0.1108 0.1714  50   TYR X O   
12935 C CB  . TYR B 50   ? 2.4993 2.4232 3.0591 -0.3579 -0.1150 0.1669  50   TYR X CB  
12936 C CG  . TYR B 50   ? 2.5132 2.4265 3.1216 -0.3774 -0.1172 0.1472  50   TYR X CG  
12937 C CD1 . TYR B 50   ? 2.5258 2.4545 3.1615 -0.3726 -0.1039 0.1266  50   TYR X CD1 
12938 C CD2 . TYR B 50   ? 2.5104 2.3996 3.1389 -0.4002 -0.1339 0.1475  50   TYR X CD2 
12939 C CE1 . TYR B 50   ? 2.5240 2.4437 3.2051 -0.3889 -0.1073 0.1066  50   TYR X CE1 
12940 C CE2 . TYR B 50   ? 2.5122 2.3915 3.1865 -0.4167 -0.1378 0.1275  50   TYR X CE2 
12941 C CZ  . TYR B 50   ? 2.5212 2.4157 3.2212 -0.4105 -0.1246 0.1069  50   TYR X CZ  
12942 O OH  . TYR B 50   ? 2.5245 2.4095 3.2707 -0.4254 -0.1298 0.0852  50   TYR X OH  
12943 N N   . SER B 51   ? 2.4786 2.3935 2.9573 -0.2793 -0.0703 0.1894  51   SER X N   
12944 C CA  . SER B 51   ? 2.4678 2.4172 2.9058 -0.2613 -0.0766 0.1984  51   SER X CA  
12945 C C   . SER B 51   ? 2.5010 2.4467 2.9427 -0.2323 -0.0481 0.1882  51   SER X C   
12946 O O   . SER B 51   ? 2.5156 2.4909 2.9297 -0.2147 -0.0505 0.1911  51   SER X O   
12947 C CB  . SER B 51   ? 2.4670 2.3841 2.8669 -0.2451 -0.0777 0.2189  51   SER X CB  
12948 O OG  . SER B 51   ? 2.4821 2.3250 2.8892 -0.2285 -0.0482 0.2229  51   SER X OG  
12949 N N   . SER B 52   ? 2.5041 2.4136 2.9835 -0.2279 -0.0218 0.1749  52   SER X N   
12950 C CA  . SER B 52   ? 2.5347 2.4270 3.0245 -0.1991 0.0104  0.1652  52   SER X CA  
12951 C C   . SER B 52   ? 2.5240 2.4813 3.0168 -0.1998 0.0013  0.1516  52   SER X C   
12952 O O   . SER B 52   ? 2.4559 2.4735 2.9442 -0.2248 -0.0293 0.1485  52   SER X O   
12953 C CB  . SER B 52   ? 2.5654 2.4093 3.1036 -0.2001 0.0374  0.1515  52   SER X CB  
12954 O OG  . SER B 52   ? 2.5457 2.4198 3.1197 -0.2336 0.0168  0.1369  52   SER X OG  
12955 N N   . GLU B 53   ? 2.5853 2.5281 3.0859 -0.1719 0.0292  0.1435  53   GLU X N   
12956 C CA  . GLU B 53   ? 2.6152 2.6143 3.1260 -0.1703 0.0257  0.1273  53   GLU X CA  
12957 C C   . GLU B 53   ? 2.6965 2.7093 3.2583 -0.1881 0.0303  0.1045  53   GLU X C   
12958 O O   . GLU B 53   ? 2.7195 2.6890 3.3141 -0.1744 0.0597  0.0947  53   GLU X O   
12959 C CB  . GLU B 53   ? 2.5603 2.5405 3.0560 -0.1313 0.0510  0.1284  53   GLU X CB  
12960 C CG  . GLU B 53   ? 2.4906 2.4886 2.9355 -0.1152 0.0363  0.1440  53   GLU X CG  
12961 C CD  . GLU B 53   ? 2.3886 2.4685 2.8242 -0.1373 0.0022  0.1384  53   GLU X CD  
12962 O OE1 . GLU B 53   ? 2.3457 2.4701 2.7945 -0.1341 0.0029  0.1226  53   GLU X OE1 
12963 O OE2 . GLU B 53   ? 2.3499 2.4493 2.7656 -0.1577 -0.0245 0.1497  53   GLU X OE2 
12964 N N   . SER B 54   ? 2.7715 2.8445 3.3391 -0.2185 0.0010  0.0957  54   SER X N   
12965 C CA  . SER B 54   ? 2.8763 2.9727 3.4868 -0.2364 -0.0003 0.0726  54   SER X CA  
12966 C C   . SER B 54   ? 3.0161 3.1470 3.6409 -0.2205 0.0130  0.0548  54   SER X C   
12967 O O   . SER B 54   ? 3.0210 3.1754 3.6185 -0.2030 0.0137  0.0600  54   SER X O   
12968 C CB  . SER B 54   ? 2.8371 2.9843 3.4417 -0.2740 -0.0373 0.0713  54   SER X CB  
12969 O OG  . SER B 54   ? 2.8285 3.0149 3.4630 -0.2883 -0.0423 0.0482  54   SER X OG  
12970 N N   . PHE B 55   ? 3.1643 3.2989 3.8339 -0.2265 0.0222  0.0323  55   PHE X N   
12971 C CA  . PHE B 55   ? 3.2967 3.4656 3.9864 -0.2137 0.0342  0.0123  55   PHE X CA  
12972 C C   . PHE B 55   ? 3.3602 3.5572 4.0902 -0.2364 0.0251  -0.0120 55   PHE X C   
12973 O O   . PHE B 55   ? 3.3655 3.5385 4.1145 -0.2548 0.0174  -0.0141 55   PHE X O   
12974 C CB  . PHE B 55   ? 3.3680 3.4834 4.0755 -0.1777 0.0727  0.0106  55   PHE X CB  
12975 C CG  . PHE B 55   ? 3.3923 3.5416 4.1165 -0.1602 0.0854  -0.0074 55   PHE X CG  
12976 C CD1 . PHE B 55   ? 3.3996 3.5825 4.0901 -0.1452 0.0805  -0.0011 55   PHE X CD1 
12977 C CD2 . PHE B 55   ? 3.3923 3.5390 4.1686 -0.1579 0.1022  -0.0319 55   PHE X CD2 
12978 C CE1 . PHE B 55   ? 3.4018 3.6158 4.1098 -0.1291 0.0917  -0.0188 55   PHE X CE1 
12979 C CE2 . PHE B 55   ? 3.3924 3.5707 4.1865 -0.1418 0.1137  -0.0492 55   PHE X CE2 
12980 C CZ  . PHE B 55   ? 3.3962 3.6081 4.1559 -0.1276 0.1085  -0.0425 55   PHE X CZ  
12981 N N   . GLU B 56   ? 3.4110 3.6587 4.1540 -0.2347 0.0250  -0.0313 56   GLU X N   
12982 C CA  . GLU B 56   ? 3.4510 3.7299 4.2293 -0.2541 0.0157  -0.0564 56   GLU X CA  
12983 C C   . GLU B 56   ? 3.4154 3.7153 4.2254 -0.2346 0.0361  -0.0796 56   GLU X C   
12984 O O   . GLU B 56   ? 3.4239 3.7450 4.2165 -0.2162 0.0441  -0.0768 56   GLU X O   
12985 C CB  . GLU B 56   ? 3.5208 3.8618 4.2701 -0.2863 -0.0203 -0.0551 56   GLU X CB  
12986 C CG  . GLU B 56   ? 3.5822 3.9511 4.3598 -0.3092 -0.0346 -0.0784 56   GLU X CG  
12987 C CD  . GLU B 56   ? 3.6315 4.0500 4.4279 -0.3024 -0.0277 -0.1032 56   GLU X CD  
12988 O OE1 . GLU B 56   ? 3.6437 4.0958 4.4192 -0.2903 -0.0231 -0.1001 56   GLU X OE1 
12989 O OE2 . GLU B 56   ? 3.6505 4.0750 4.4839 -0.3089 -0.0277 -0.1270 56   GLU X OE2 
12990 N N   . TYR B 57   ? 3.3547 3.6492 4.2133 -0.2383 0.0434  -0.1037 57   TYR X N   
12991 C CA  . TYR B 57   ? 3.2944 3.6036 4.1901 -0.2186 0.0646  -0.1271 57   TYR X CA  
12992 C C   . TYR B 57   ? 3.2159 3.5648 4.1465 -0.2368 0.0521  -0.1566 57   TYR X C   
12993 O O   . TYR B 57   ? 3.2219 3.5711 4.1550 -0.2614 0.0312  -0.1594 57   TYR X O   
12994 C CB  . TYR B 57   ? 3.2984 3.5376 4.2287 -0.1898 0.1014  -0.1270 57   TYR X CB  
12995 C CG  . TYR B 57   ? 3.2846 3.5298 4.2302 -0.1600 0.1267  -0.1365 57   TYR X CG  
12996 C CD1 . TYR B 57   ? 3.3043 3.4875 4.2596 -0.1299 0.1598  -0.1268 57   TYR X CD1 
12997 C CD2 . TYR B 57   ? 3.2555 3.5673 4.2045 -0.1619 0.1176  -0.1549 57   TYR X CD2 
12998 C CE1 . TYR B 57   ? 3.3080 3.4945 4.2769 -0.1022 0.1820  -0.1349 57   TYR X CE1 
12999 C CE2 . TYR B 57   ? 3.2543 3.5722 4.2194 -0.1347 0.1394  -0.1645 57   TYR X CE2 
13000 C CZ  . TYR B 57   ? 3.2803 3.5351 4.2555 -0.1047 0.1708  -0.1541 57   TYR X CZ  
13001 O OH  . TYR B 57   ? 3.2844 3.5436 4.2752 -0.0772 0.1916  -0.1631 57   TYR X OH  
13002 N N   . SER B 58   ? 3.1280 3.5099 4.0847 -0.2236 0.0641  -0.1789 58   SER X N   
13003 C CA  . SER B 58   ? 3.0174 3.4406 4.0073 -0.2370 0.0539  -0.2095 58   SER X CA  
13004 C C   . SER B 58   ? 2.9249 3.3546 3.9622 -0.2122 0.0799  -0.2343 58   SER X C   
13005 O O   . SER B 58   ? 2.9143 3.3193 3.9549 -0.1853 0.1047  -0.2265 58   SER X O   
13006 C CB  . SER B 58   ? 3.0029 3.4987 3.9527 -0.2620 0.0235  -0.2107 58   SER X CB  
13007 O OG  . SER B 58   ? 3.0019 3.5355 3.9262 -0.2500 0.0284  -0.2055 58   SER X OG  
13008 N N   . ASN B 59   ? 2.8441 3.3065 3.9172 -0.2210 0.0733  -0.2643 59   ASN X N   
13009 C CA  . ASN B 59   ? 2.7783 3.2479 3.9034 -0.1992 0.0964  -0.2911 59   ASN X CA  
13010 C C   . ASN B 59   ? 2.8098 3.2068 3.9838 -0.1767 0.1277  -0.2928 59   ASN X C   
13011 O O   . ASN B 59   ? 2.8240 3.2139 4.0410 -0.1536 0.1529  -0.3095 59   ASN X O   
13012 C CB  . ASN B 59   ? 2.6883 3.1956 3.7943 -0.1824 0.1055  -0.2888 59   ASN X CB  
13013 C CG  . ASN B 59   ? 2.5816 3.1630 3.6443 -0.2042 0.0779  -0.2899 59   ASN X CG  
13014 O OD1 . ASN B 59   ? 2.5389 3.1743 3.6159 -0.2033 0.0767  -0.3132 59   ASN X OD1 
13015 N ND2 . ASN B 59   ? 2.5469 3.1315 3.5579 -0.2242 0.0565  -0.2654 59   ASN X ND2 
13016 N N   . VAL B 60   ? 2.8339 3.1765 4.0020 -0.1838 0.1270  -0.2756 60   VAL X N   
13017 C CA  . VAL B 60   ? 2.8894 3.1585 4.1022 -0.1650 0.1579  -0.2756 60   VAL X CA  
13018 C C   . VAL B 60   ? 2.9497 3.2028 4.2245 -0.1733 0.1571  -0.3042 60   VAL X C   
13019 O O   . VAL B 60   ? 2.9420 3.1885 4.2111 -0.1960 0.1343  -0.3035 60   VAL X O   
13020 C CB  . VAL B 60   ? 2.5564 2.7676 3.7327 -0.1644 0.1629  -0.2415 60   VAL X CB  
13021 C CG1 . VAL B 60   ? 2.5696 2.7801 3.6977 -0.1460 0.1732  -0.2161 60   VAL X CG1 
13022 C CG2 . VAL B 60   ? 2.5399 2.7633 3.6821 -0.1959 0.1282  -0.2307 60   VAL X CG2 
13023 N N   . SER B 61   ? 3.0220 3.2686 4.3575 -0.1542 0.1811  -0.3301 61   SER X N   
13024 C CA  . SER B 61   ? 3.0943 3.3194 4.4976 -0.1572 0.1849  -0.3595 61   SER X CA  
13025 C C   . SER B 61   ? 3.1987 3.3480 4.6541 -0.1348 0.2248  -0.3596 61   SER X C   
13026 O O   . SER B 61   ? 3.2085 3.3392 4.6742 -0.1093 0.2555  -0.3546 61   SER X O   
13027 C CB  . SER B 61   ? 3.0749 3.3566 4.5166 -0.1557 0.1783  -0.3957 61   SER X CB  
13028 O OG  . SER B 61   ? 3.0736 3.3306 4.5877 -0.1535 0.1856  -0.4259 61   SER X OG  
13029 N N   . GLY B 62   ? 3.2965 3.4015 4.7861 -0.1443 0.2245  -0.3663 62   GLY X N   
13030 C CA  . GLY B 62   ? 3.4148 3.4450 4.9551 -0.1260 0.2630  -0.3668 62   GLY X CA  
13031 C C   . GLY B 62   ? 3.5067 3.5133 5.1225 -0.1322 0.2639  -0.3989 62   GLY X C   
13032 O O   . GLY B 62   ? 3.4774 3.5249 5.1034 -0.1510 0.2314  -0.4208 62   GLY X O   
13033 N N   . LYS B 63   ? 3.6197 3.5587 5.2880 -0.1161 0.3013  -0.4020 63   LYS X N   
13034 C CA  . LYS B 63   ? 3.7007 3.6122 5.4506 -0.1189 0.3071  -0.4350 63   LYS X CA  
13035 C C   . LYS B 63   ? 3.7622 3.5950 5.5334 -0.1192 0.3293  -0.4233 63   LYS X C   
13036 O O   . LYS B 63   ? 3.8167 3.5949 5.5943 -0.0997 0.3700  -0.4069 63   LYS X O   
13037 C CB  . LYS B 63   ? 3.7258 3.6418 5.5477 -0.0968 0.3346  -0.4656 63   LYS X CB  
13038 C CG  . LYS B 63   ? 3.7731 3.6528 5.5930 -0.0688 0.3789  -0.4470 63   LYS X CG  
13039 C CD  . LYS B 63   ? 3.8035 3.6905 5.6975 -0.0481 0.4039  -0.4785 63   LYS X CD  
13040 C CE  . LYS B 63   ? 3.8633 3.6987 5.7628 -0.0198 0.4518  -0.4599 63   LYS X CE  
13041 N NZ  . LYS B 63   ? 3.9090 3.6635 5.8070 -0.0178 0.4787  -0.4379 63   LYS X NZ  
13042 N N   . VAL B 64   ? 3.7534 3.5808 5.5373 -0.1414 0.3023  -0.4336 64   VAL X N   
13043 C CA  . VAL B 64   ? 3.7618 3.5236 5.5569 -0.1485 0.3129  -0.4223 64   VAL X CA  
13044 C C   . VAL B 64   ? 3.7396 3.4246 5.5885 -0.1276 0.3662  -0.4221 64   VAL X C   
13045 O O   . VAL B 64   ? 3.7492 3.4247 5.6628 -0.1097 0.3943  -0.4460 64   VAL X O   
13046 C CB  . VAL B 64   ? 3.7871 3.5556 5.6230 -0.1706 0.2795  -0.4506 64   VAL X CB  
13047 C CG1 . VAL B 64   ? 3.7981 3.5787 5.7205 -0.1613 0.2860  -0.4957 64   VAL X CG1 
13048 C CG2 . VAL B 64   ? 3.8118 3.5141 5.6648 -0.1789 0.2894  -0.4418 64   VAL X CG2 
13049 N N   . GLU B 65   ? 3.7025 3.3333 5.5223 -0.1305 0.3800  -0.3943 65   GLU X N   
13050 C CA  . GLU B 65   ? 3.6643 3.2155 5.5382 -0.1197 0.4238  -0.3968 65   GLU X CA  
13051 C C   . GLU B 65   ? 3.6060 3.1213 5.4510 -0.1383 0.4115  -0.3778 65   GLU X C   
13052 O O   . GLU B 65   ? 3.5965 3.1234 5.3613 -0.1454 0.3945  -0.3447 65   GLU X O   
13053 C CB  . GLU B 65   ? 3.6812 3.1862 5.5414 -0.0918 0.4748  -0.3737 65   GLU X CB  
13054 C CG  . GLU B 65   ? 3.6606 3.2015 5.4700 -0.0733 0.4803  -0.3565 65   GLU X CG  
13055 C CD  . GLU B 65   ? 3.6181 3.2276 5.3458 -0.0866 0.4353  -0.3387 65   GLU X CD  
13056 O OE1 . GLU B 65   ? 3.5853 3.2206 5.2871 -0.1117 0.3959  -0.3371 65   GLU X OE1 
13057 O OE2 . GLU B 65   ? 3.6187 3.2564 5.3101 -0.0712 0.4405  -0.3269 65   GLU X OE2 
13058 N N   . ASN B 66   ? 3.5485 3.0197 5.4604 -0.1457 0.4206  -0.3992 66   ASN X N   
13059 C CA  . ASN B 66   ? 3.4816 2.9138 5.3725 -0.1621 0.4129  -0.3825 66   ASN X CA  
13060 C C   . ASN B 66   ? 3.4787 2.8337 5.3637 -0.1468 0.4639  -0.3582 66   ASN X C   
13061 O O   . ASN B 66   ? 3.4855 2.7883 5.4398 -0.1339 0.5062  -0.3751 66   ASN X O   
13062 C CB  . ASN B 66   ? 3.4162 2.8455 5.3717 -0.1823 0.3868  -0.4164 66   ASN X CB  
13063 C CG  . ASN B 66   ? 3.3666 2.7986 5.4174 -0.1729 0.3993  -0.4608 66   ASN X CG  
13064 O OD1 . ASN B 66   ? 3.3491 2.8240 5.4062 -0.1616 0.3980  -0.4729 66   ASN X OD1 
13065 N ND2 . ASN B 66   ? 3.3497 2.7366 5.4782 -0.1779 0.4106  -0.4871 66   ASN X ND2 
13066 N N   . TYR B 67   ? 3.4628 2.8117 5.2632 -0.1479 0.4598  -0.3187 67   TYR X N   
13067 C CA  . TYR B 67   ? 3.4630 2.7404 5.2416 -0.1365 0.5009  -0.2917 67   TYR X CA  
13068 C C   . TYR B 67   ? 3.4325 2.6553 5.2687 -0.1498 0.5114  -0.3068 67   TYR X C   
13069 O O   . TYR B 67   ? 3.4787 2.6483 5.3831 -0.1380 0.5548  -0.3238 67   TYR X O   
13070 C CB  . TYR B 67   ? 3.4604 2.7519 5.1350 -0.1377 0.4839  -0.2494 67   TYR X CB  
13071 C CG  . TYR B 67   ? 3.4522 2.6966 5.0984 -0.1489 0.4859  -0.2283 67   TYR X CG  
13072 C CD1 . TYR B 67   ? 3.4753 2.6414 5.1343 -0.1341 0.5364  -0.2173 67   TYR X CD1 
13073 C CD2 . TYR B 67   ? 3.4020 2.6801 5.0076 -0.1741 0.4379  -0.2190 67   TYR X CD2 
13074 C CE1 . TYR B 67   ? 3.4594 2.5833 5.0930 -0.1442 0.5389  -0.1993 67   TYR X CE1 
13075 C CE2 . TYR B 67   ? 3.3860 2.6230 4.9679 -0.1843 0.4388  -0.2008 67   TYR X CE2 
13076 C CZ  . TYR B 67   ? 3.4063 2.5668 5.0026 -0.1692 0.4894  -0.1916 67   TYR X CZ  
13077 O OH  . TYR B 67   ? 3.3913 2.5108 4.9649 -0.1789 0.4916  -0.1746 67   TYR X OH  
13078 N N   . ASN B 68   ? 3.3596 2.5950 5.1710 -0.1744 0.4725  -0.3015 68   ASN X N   
13079 C CA  . ASN B 68   ? 3.3837 2.5815 5.2599 -0.1910 0.4709  -0.3243 68   ASN X CA  
13080 C C   . ASN B 68   ? 3.4397 2.6860 5.3543 -0.2141 0.4189  -0.3562 68   ASN X C   
13081 O O   . ASN B 68   ? 3.4946 2.7533 5.4800 -0.2103 0.4204  -0.3919 68   ASN X O   
13082 C CB  . ASN B 68   ? 3.3854 2.5334 5.2238 -0.1986 0.4802  -0.2973 68   ASN X CB  
13083 C CG  . ASN B 68   ? 3.4285 2.6208 5.1835 -0.2173 0.4300  -0.2709 68   ASN X CG  
13084 O OD1 . ASN B 68   ? 3.4273 2.6867 5.1564 -0.2279 0.3858  -0.2747 68   ASN X OD1 
13085 N ND2 . ASN B 68   ? 3.4540 2.6084 5.1677 -0.2215 0.4377  -0.2447 68   ASN X ND2 
13086 N N   . GLY B 69   ? 3.4338 2.7070 5.3004 -0.2368 0.3730  -0.3433 69   GLY X N   
13087 C CA  . GLY B 69   ? 3.3772 2.6835 5.2758 -0.2601 0.3239  -0.3704 69   GLY X CA  
13088 C C   . GLY B 69   ? 3.3325 2.6977 5.2577 -0.2603 0.2969  -0.3995 69   GLY X C   
13089 O O   . GLY B 69   ? 3.3215 2.6821 5.3242 -0.2646 0.2894  -0.4380 69   GLY X O   
13090 N N   . SER B 70   ? 3.2760 2.6961 5.1390 -0.2552 0.2825  -0.3827 70   SER X N   
13091 C CA  . SER B 70   ? 3.1865 2.6701 5.0596 -0.2591 0.2495  -0.4069 70   SER X CA  
13092 C C   . SER B 70   ? 3.1058 2.6346 4.9343 -0.2433 0.2575  -0.3940 70   SER X C   
13093 O O   . SER B 70   ? 3.0717 2.6483 4.9190 -0.2418 0.2404  -0.4174 70   SER X O   
13094 C CB  . SER B 70   ? 3.1656 2.6909 5.0013 -0.2866 0.1897  -0.4061 70   SER X CB  
13095 O OG  . SER B 70   ? 3.1541 2.6492 5.0456 -0.3011 0.1740  -0.4297 70   SER X OG  
13096 N N   . ASN B 71   ? 3.0557 2.5709 4.8246 -0.2314 0.2814  -0.3579 71   ASN X N   
13097 C CA  . ASN B 71   ? 2.9944 2.5593 4.7106 -0.2199 0.2797  -0.3434 71   ASN X CA  
13098 C C   . ASN B 71   ? 2.9882 2.5284 4.6442 -0.2029 0.3100  -0.3051 71   ASN X C   
13099 O O   . ASN B 71   ? 3.0203 2.5086 4.6607 -0.2029 0.3272  -0.2846 71   ASN X O   
13100 C CB  . ASN B 71   ? 2.9274 2.5621 4.5880 -0.2419 0.2243  -0.3387 71   ASN X CB  
13101 C CG  . ASN B 71   ? 2.8666 2.5632 4.5388 -0.2380 0.2093  -0.3618 71   ASN X CG  
13102 O OD1 . ASN B 71   ? 2.8613 2.5539 4.5747 -0.2170 0.2402  -0.3774 71   ASN X OD1 
13103 N ND2 . ASN B 71   ? 2.8289 2.5827 4.4643 -0.2586 0.1618  -0.3643 71   ASN X ND2 
13104 N N   . VAL B 72   ? 2.9564 2.5351 4.5796 -0.1880 0.3153  -0.2971 72   VAL X N   
13105 C CA  . VAL B 72   ? 2.9701 2.5386 4.5278 -0.1706 0.3362  -0.2618 72   VAL X CA  
13106 C C   . VAL B 72   ? 2.9666 2.5822 4.5176 -0.1541 0.3408  -0.2683 72   VAL X C   
13107 O O   . VAL B 72   ? 2.9342 2.5592 4.5482 -0.1464 0.3518  -0.2990 72   VAL X O   
13108 C CB  . VAL B 72   ? 3.0137 2.5005 4.5864 -0.1509 0.3877  -0.2479 72   VAL X CB  
13109 C CG1 . VAL B 72   ? 3.0525 2.5312 4.6024 -0.1213 0.4223  -0.2335 72   VAL X CG1 
13110 C CG2 . VAL B 72   ? 3.0287 2.4827 4.5500 -0.1616 0.3811  -0.2181 72   VAL X CG2 
13111 N N   . VAL B 73   ? 2.9994 2.6457 4.4770 -0.1484 0.3318  -0.2413 73   VAL X N   
13112 C CA  . VAL B 73   ? 3.0089 2.7074 4.4770 -0.1354 0.3306  -0.2482 73   VAL X CA  
13113 C C   . VAL B 73   ? 3.0098 2.6939 4.4235 -0.1115 0.3542  -0.2184 73   VAL X C   
13114 O O   . VAL B 73   ? 3.0302 2.6562 4.4204 -0.1019 0.3775  -0.1945 73   VAL X O   
13115 C CB  . VAL B 73   ? 2.2013 1.9827 3.6450 -0.1580 0.2808  -0.2593 73   VAL X CB  
13116 C CG1 . VAL B 73   ? 2.1736 1.9611 3.6294 -0.1874 0.2458  -0.2699 73   VAL X CG1 
13117 C CG2 . VAL B 73   ? 2.2007 2.0320 3.5687 -0.1564 0.2635  -0.2358 73   VAL X CG2 
13118 N N   . ARG B 74   ? 3.0045 2.7389 4.4009 -0.1007 0.3494  -0.2215 74   ARG X N   
13119 C CA  . ARG B 74   ? 3.0284 2.7561 4.3713 -0.0777 0.3661  -0.1953 74   ARG X CA  
13120 C C   . ARG B 74   ? 3.0364 2.8383 4.3563 -0.0746 0.3462  -0.2019 74   ARG X C   
13121 O O   . ARG B 74   ? 3.0213 2.8717 4.3794 -0.0840 0.3309  -0.2305 74   ARG X O   
13122 C CB  . ARG B 74   ? 3.0656 2.7238 4.4415 -0.0481 0.4181  -0.1930 74   ARG X CB  
13123 C CG  . ARG B 74   ? 3.0752 2.7461 4.5184 -0.0339 0.4379  -0.2235 74   ARG X CG  
13124 C CD  . ARG B 74   ? 3.1250 2.7203 4.6033 -0.0066 0.4908  -0.2201 74   ARG X CD  
13125 N NE  . ARG B 74   ? 3.1410 2.6730 4.6570 -0.0145 0.5098  -0.2227 74   ARG X NE  
13126 C CZ  . ARG B 74   ? 3.1352 2.6515 4.7342 -0.0194 0.5225  -0.2540 74   ARG X CZ  
13127 N NH1 . ARG B 74   ? 3.1188 2.6784 4.7708 -0.0168 0.5179  -0.2852 74   ARG X NH1 
13128 N NH2 . ARG B 74   ? 3.1448 2.6025 4.7760 -0.0267 0.5398  -0.2555 74   ARG X NH2 
13129 N N   . PHE B 75   ? 3.0649 2.8750 4.3227 -0.0609 0.3464  -0.1764 75   PHE X N   
13130 C CA  . PHE B 75   ? 3.0686 2.9468 4.3017 -0.0565 0.3294  -0.1809 75   PHE X CA  
13131 C C   . PHE B 75   ? 3.0304 2.8966 4.2104 -0.0309 0.3429  -0.1555 75   PHE X C   
13132 O O   . PHE B 75   ? 3.0408 2.8698 4.1717 -0.0265 0.3454  -0.1270 75   PHE X O   
13133 C CB  . PHE B 75   ? 3.1183 3.0667 4.3197 -0.0868 0.2825  -0.1837 75   PHE X CB  
13134 C CG  . PHE B 75   ? 3.1692 3.1736 4.4151 -0.0996 0.2665  -0.2176 75   PHE X CG  
13135 C CD1 . PHE B 75   ? 3.1903 3.2465 4.4399 -0.0890 0.2659  -0.2314 75   PHE X CD1 
13136 C CD2 . PHE B 75   ? 3.1872 3.1909 4.4726 -0.1210 0.2523  -0.2370 75   PHE X CD2 
13137 C CE1 . PHE B 75   ? 3.1855 3.2928 4.4754 -0.0998 0.2521  -0.2635 75   PHE X CE1 
13138 C CE2 . PHE B 75   ? 3.1827 3.2363 4.5071 -0.1310 0.2371  -0.2691 75   PHE X CE2 
13139 C CZ  . PHE B 75   ? 3.1790 3.2845 4.5049 -0.1204 0.2376  -0.2821 75   PHE X CZ  
13140 N N   . ASN B 76   ? 2.9708 2.8696 4.1621 -0.0135 0.3503  -0.1676 76   ASN X N   
13141 C CA  . ASN B 76   ? 2.9286 2.8214 4.0752 0.0130  0.3613  -0.1483 76   ASN X CA  
13142 C C   . ASN B 76   ? 2.8546 2.8203 3.9483 0.0015  0.3241  -0.1423 76   ASN X C   
13143 O O   . ASN B 76   ? 2.8185 2.8458 3.9273 -0.0006 0.3120  -0.1623 76   ASN X O   
13144 C CB  . ASN B 76   ? 2.9376 2.8214 4.1307 0.0397  0.3917  -0.1656 76   ASN X CB  
13145 C CG  . ASN B 76   ? 2.9579 2.8039 4.1120 0.0730  0.4139  -0.1430 76   ASN X CG  
13146 O OD1 . ASN B 76   ? 2.9431 2.8234 4.0439 0.0779  0.3945  -0.1300 76   ASN X OD1 
13147 N ND2 . ASN B 76   ? 2.9952 2.7695 4.1768 0.0966  0.4550  -0.1391 76   ASN X ND2 
13148 N N   . PRO B 77   ? 2.8121 2.7707 3.8454 -0.0063 0.3066  -0.1155 77   PRO X N   
13149 C CA  . PRO B 77   ? 2.7824 2.8044 3.7636 -0.0214 0.2699  -0.1069 77   PRO X CA  
13150 C C   . PRO B 77   ? 2.7944 2.8465 3.7433 0.0006  0.2685  -0.1018 77   PRO X C   
13151 O O   . PRO B 77   ? 2.7646 2.8771 3.6803 -0.0135 0.2385  -0.1003 77   PRO X O   
13152 C CB  . PRO B 77   ? 2.7743 2.7583 3.7087 -0.0301 0.2609  -0.0784 77   PRO X CB  
13153 C CG  . PRO B 77   ? 2.8102 2.7076 3.7556 -0.0057 0.2996  -0.0665 77   PRO X CG  
13154 C CD  . PRO B 77   ? 2.8196 2.7063 3.8375 -0.0053 0.3207  -0.0937 77   PRO X CD  
13155 N N   . LYS B 78   ? 2.8542 2.8643 3.8136 0.0337  0.2998  -0.0996 78   LYS X N   
13156 C CA  . LYS B 78   ? 2.8963 2.9240 3.8283 0.0599  0.3017  -0.0951 78   LYS X CA  
13157 C C   . LYS B 78   ? 3.0517 3.0127 3.9349 0.0891  0.3188  -0.0651 78   LYS X C   
13158 O O   . LYS B 78   ? 3.0838 3.0507 3.9413 0.1139  0.3204  -0.0598 78   LYS X O   
13159 C CB  . LYS B 78   ? 2.7777 2.8918 3.6831 0.0438  0.2653  -0.1021 78   LYS X CB  
13160 C CG  . LYS B 78   ? 2.7010 2.8286 3.5460 0.0289  0.2371  -0.0793 78   LYS X CG  
13161 C CD  . LYS B 78   ? 2.6914 2.7796 3.4852 0.0580  0.2437  -0.0542 78   LYS X CD  
13162 C CE  . LYS B 78   ? 2.6654 2.7332 3.4108 0.0452  0.2270  -0.0288 78   LYS X CE  
13163 N NZ  . LYS B 78   ? 2.6950 2.7062 3.3933 0.0766  0.2392  -0.0037 78   LYS X NZ  
13164 N N   . ASP B 79   ? 3.1651 3.0619 4.0369 0.0870  0.3318  -0.0470 79   ASP X N   
13165 C CA  . ASP B 79   ? 3.2874 3.1185 4.1070 0.1119  0.3465  -0.0172 79   ASP X CA  
13166 C C   . ASP B 79   ? 3.3962 3.1411 4.2337 0.1183  0.3812  -0.0073 79   ASP X C   
13167 O O   . ASP B 79   ? 3.4407 3.1189 4.2468 0.1455  0.4057  0.0135  79   ASP X O   
13168 C CB  . ASP B 79   ? 3.2721 3.1289 4.0308 0.0984  0.3128  0.0019  79   ASP X CB  
13169 C CG  . ASP B 79   ? 3.3138 3.1200 4.0116 0.1283  0.3208  0.0296  79   ASP X CG  
13170 O OD1 . ASP B 79   ? 3.3530 3.0814 4.0420 0.1427  0.3487  0.0456  79   ASP X OD1 
13171 O OD2 . ASP B 79   ? 3.3086 3.1525 3.9667 0.1373  0.2987  0.0348  79   ASP X OD2 
13172 N N   . GLN B 80   ? 3.4514 3.1972 4.3391 0.0935  0.3833  -0.0230 80   GLN X N   
13173 C CA  . GLN B 80   ? 3.5439 3.2126 4.4597 0.0964  0.4166  -0.0187 80   GLN X CA  
13174 C C   . GLN B 80   ? 3.5641 3.2479 4.5554 0.0749  0.4205  -0.0477 80   GLN X C   
13175 O O   . GLN B 80   ? 3.5362 3.2722 4.5663 0.0712  0.4131  -0.0725 80   GLN X O   
13176 C CB  . GLN B 80   ? 3.5711 3.2024 4.4418 0.0862  0.4090  0.0061  80   GLN X CB  
13177 C CG  . GLN B 80   ? 3.5339 3.2198 4.4004 0.0488  0.3687  0.0013  80   GLN X CG  
13178 C CD  . GLN B 80   ? 3.5224 3.2640 4.3297 0.0445  0.3323  0.0137  80   GLN X CD  
13179 O OE1 . GLN B 80   ? 3.4973 3.2780 4.2893 0.0166  0.2997  0.0157  80   GLN X OE1 
13180 N NE2 . GLN B 80   ? 3.5437 3.2878 4.3185 0.0725  0.3375  0.0218  80   GLN X NE2 
13181 N N   . ASN B 81   ? 3.6078 3.2454 4.6206 0.0614  0.4317  -0.0459 81   ASN X N   
13182 C CA  . ASN B 81   ? 3.6210 3.2683 4.7055 0.0406  0.4331  -0.0739 81   ASN X CA  
13183 C C   . ASN B 81   ? 3.6650 3.2905 4.7496 0.0148  0.4211  -0.0684 81   ASN X C   
13184 O O   . ASN B 81   ? 3.6994 3.2537 4.7862 0.0220  0.4484  -0.0560 81   ASN X O   
13185 C CB  . ASN B 81   ? 3.6230 3.2174 4.7678 0.0617  0.4782  -0.0875 81   ASN X CB  
13186 C CG  . ASN B 81   ? 3.5864 3.2224 4.7606 0.0767  0.4824  -0.1074 81   ASN X CG  
13187 O OD1 . ASN B 81   ? 3.5426 3.2333 4.7633 0.0608  0.4658  -0.1358 81   ASN X OD1 
13188 N ND2 . ASN B 81   ? 3.6104 3.2198 4.7574 0.1079  0.5041  -0.0930 81   ASN X ND2 
13189 N N   . HIS B 82   ? 3.6723 3.3588 4.7553 -0.0154 0.3808  -0.0783 82   HIS X N   
13190 C CA  . HIS B 82   ? 3.7028 3.3787 4.7753 -0.0415 0.3608  -0.0706 82   HIS X CA  
13191 C C   . HIS B 82   ? 3.6562 3.3048 4.7973 -0.0570 0.3701  -0.0928 82   HIS X C   
13192 O O   . HIS B 82   ? 3.6503 3.2709 4.8493 -0.0441 0.4008  -0.1114 82   HIS X O   
13193 C CB  . HIS B 82   ? 3.7483 3.4997 4.7844 -0.0674 0.3121  -0.0694 82   HIS X CB  
13194 C CG  . HIS B 82   ? 3.8235 3.5959 4.7878 -0.0573 0.2981  -0.0442 82   HIS X CG  
13195 N ND1 . HIS B 82   ? 3.8640 3.5973 4.7778 -0.0532 0.2982  -0.0159 82   HIS X ND1 
13196 C CD2 . HIS B 82   ? 3.8341 3.6635 4.7708 -0.0506 0.2826  -0.0449 82   HIS X CD2 
13197 C CE1 . HIS B 82   ? 3.8751 3.6400 4.7337 -0.0435 0.2827  -0.0004 82   HIS X CE1 
13198 N NE2 . HIS B 82   ? 3.8578 3.6810 4.7298 -0.0420 0.2732  -0.0176 82   HIS X NE2 
13199 N N   . GLN B 83   ? 3.6105 3.2680 4.7458 -0.0849 0.3423  -0.0912 83   GLN X N   
13200 C CA  . GLN B 83   ? 3.5774 3.2152 4.7748 -0.1031 0.3425  -0.1133 83   GLN X CA  
13201 C C   . GLN B 83   ? 3.5416 3.2290 4.7244 -0.1369 0.2945  -0.1168 83   GLN X C   
13202 O O   . GLN B 83   ? 3.5380 3.2543 4.6594 -0.1459 0.2681  -0.0955 83   GLN X O   
13203 C CB  . GLN B 83   ? 3.5729 3.1268 4.7831 -0.0954 0.3757  -0.1018 83   GLN X CB  
13204 C CG  . GLN B 83   ? 3.5362 3.0635 4.8186 -0.1115 0.3805  -0.1271 83   GLN X CG  
13205 C CD  . GLN B 83   ? 3.5496 2.9912 4.8515 -0.1008 0.4210  -0.1184 83   GLN X CD  
13206 O OE1 . GLN B 83   ? 3.5791 2.9815 4.8306 -0.0848 0.4403  -0.0901 83   GLN X OE1 
13207 N NE2 . GLN B 83   ? 3.5330 2.9443 4.9084 -0.1092 0.4343  -0.1436 83   GLN X NE2 
13208 N N   . LEU B 84   ? 3.5140 3.2098 4.7534 -0.1549 0.2830  -0.1441 84   LEU X N   
13209 C CA  . LEU B 84   ? 3.4644 3.2043 4.6926 -0.1868 0.2371  -0.1493 84   LEU X CA  
13210 C C   . LEU B 84   ? 3.3972 3.1066 4.6877 -0.2024 0.2347  -0.1720 84   LEU X C   
13211 O O   . LEU B 84   ? 3.4232 3.1221 4.7791 -0.1953 0.2520  -0.2002 84   LEU X O   
13212 C CB  . LEU B 84   ? 3.4666 3.2858 4.6854 -0.1950 0.2088  -0.1638 84   LEU X CB  
13213 C CG  . LEU B 84   ? 3.4588 3.3260 4.6749 -0.2270 0.1632  -0.1757 84   LEU X CG  
13214 C CD1 . LEU B 84   ? 3.4614 3.3278 4.6226 -0.2463 0.1363  -0.1486 84   LEU X CD1 
13215 C CD2 . LEU B 84   ? 3.4522 3.3945 4.6552 -0.2314 0.1422  -0.1890 84   LEU X CD2 
13216 N N   . PHE B 85   ? 3.3133 3.0088 4.5858 -0.2231 0.2125  -0.1605 85   PHE X N   
13217 C CA  . PHE B 85   ? 3.2247 2.8887 4.5542 -0.2387 0.2075  -0.1810 85   PHE X CA  
13218 C C   . PHE B 85   ? 3.1343 2.8511 4.4654 -0.2672 0.1583  -0.1966 85   PHE X C   
13219 O O   . PHE B 85   ? 3.1298 2.8692 4.4117 -0.2870 0.1249  -0.1785 85   PHE X O   
13220 C CB  . PHE B 85   ? 3.2375 2.8410 4.5549 -0.2417 0.2191  -0.1607 85   PHE X CB  
13221 C CG  . PHE B 85   ? 3.2829 2.8218 4.6096 -0.2142 0.2714  -0.1499 85   PHE X CG  
13222 C CD1 . PHE B 85   ? 3.3083 2.8512 4.5882 -0.1910 0.2911  -0.1291 85   PHE X CD1 
13223 C CD2 . PHE B 85   ? 3.3075 2.7802 4.6889 -0.2114 0.3009  -0.1606 85   PHE X CD2 
13224 C CE1 . PHE B 85   ? 3.3572 2.8376 4.6407 -0.1650 0.3388  -0.1179 85   PHE X CE1 
13225 C CE2 . PHE B 85   ? 3.3551 2.7656 4.7420 -0.1865 0.3510  -0.1496 85   PHE X CE2 
13226 C CZ  . PHE B 85   ? 3.3803 2.7938 4.7161 -0.1630 0.3697  -0.1275 85   PHE X CZ  
13227 N N   . LEU B 86   ? 3.0413 2.7766 4.4286 -0.2686 0.1543  -0.2304 86   LEU X N   
13228 C CA  . LEU B 86   ? 2.9335 2.7118 4.3283 -0.2936 0.1097  -0.2493 86   LEU X CA  
13229 C C   . LEU B 86   ? 2.8742 2.6063 4.3173 -0.3072 0.1028  -0.2633 86   LEU X C   
13230 O O   . LEU B 86   ? 2.8696 2.5543 4.3785 -0.2948 0.1336  -0.2826 86   LEU X O   
13231 C CB  . LEU B 86   ? 2.9029 2.7218 4.3360 -0.2864 0.1088  -0.2810 86   LEU X CB  
13232 C CG  . LEU B 86   ? 2.8615 2.7470 4.2753 -0.3067 0.0634  -0.2949 86   LEU X CG  
13233 C CD1 . LEU B 86   ? 2.8411 2.7693 4.1710 -0.3207 0.0366  -0.2639 86   LEU X CD1 
13234 C CD2 . LEU B 86   ? 2.8506 2.7739 4.2975 -0.2934 0.0718  -0.3230 86   LEU X CD2 
13235 N N   . LEU B 87   ? 2.8084 2.5527 4.2213 -0.3325 0.0633  -0.2540 87   LEU X N   
13236 C CA  . LEU B 87   ? 2.7608 2.4641 4.2194 -0.3469 0.0520  -0.2685 87   LEU X CA  
13237 C C   . LEU B 87   ? 2.7793 2.5137 4.2039 -0.3764 -0.0013 -0.2638 87   LEU X C   
13238 O O   . LEU B 87   ? 2.7856 2.4866 4.2225 -0.3907 -0.0148 -0.2618 87   LEU X O   
13239 C CB  . LEU B 87   ? 2.6741 2.3081 4.1457 -0.3377 0.0869  -0.2530 87   LEU X CB  
13240 C CG  . LEU B 87   ? 2.5843 2.2072 3.9867 -0.3341 0.0963  -0.2123 87   LEU X CG  
13241 C CD1 . LEU B 87   ? 2.5390 2.1689 3.9042 -0.3602 0.0565  -0.1959 87   LEU X CD1 
13242 C CD2 . LEU B 87   ? 2.5741 2.1279 4.0005 -0.3136 0.1468  -0.2047 87   LEU X CD2 
13243 N N   . GLY B 88   ? 2.8212 2.6190 4.2031 -0.3854 -0.0308 -0.2622 88   GLY X N   
13244 C CA  . GLY B 88   ? 2.8728 2.7037 4.2202 -0.4130 -0.0814 -0.2587 88   GLY X CA  
13245 C C   . GLY B 88   ? 2.9610 2.8031 4.3570 -0.4210 -0.1054 -0.2960 88   GLY X C   
13246 O O   . GLY B 88   ? 2.9751 2.8089 4.4281 -0.4044 -0.0831 -0.3243 88   GLY X O   
13247 N N   . LYS B 89   ? 3.0386 2.8986 4.4128 -0.4455 -0.1514 -0.2967 89   LYS X N   
13248 C CA  . LYS B 89   ? 3.1254 2.9965 4.5393 -0.4531 -0.1792 -0.3321 89   LYS X CA  
13249 C C   . LYS B 89   ? 3.2326 3.1548 4.6431 -0.4427 -0.1767 -0.3496 89   LYS X C   
13250 O O   . LYS B 89   ? 3.2432 3.1721 4.6991 -0.4402 -0.1877 -0.3846 89   LYS X O   
13251 C CB  . LYS B 89   ? 3.1086 2.9934 4.4862 -0.4812 -0.2311 -0.3252 89   LYS X CB  
13252 C CG  . LYS B 89   ? 3.1058 2.9969 4.5215 -0.4885 -0.2631 -0.3617 89   LYS X CG  
13253 C CD  . LYS B 89   ? 3.1181 2.9554 4.6247 -0.4763 -0.2441 -0.3940 89   LYS X CD  
13254 C CE  . LYS B 89   ? 3.1377 2.9825 4.6845 -0.4811 -0.2771 -0.4331 89   LYS X CE  
13255 N NZ  . LYS B 89   ? 3.1511 2.9421 4.7909 -0.4706 -0.2605 -0.4659 89   LYS X NZ  
13256 N N   . ASP B 90   ? 3.3038 3.2621 4.6615 -0.4363 -0.1626 -0.3264 90   ASP X N   
13257 C CA  . ASP B 90   ? 3.3551 3.3630 4.7073 -0.4249 -0.1553 -0.3403 90   ASP X CA  
13258 C C   . ASP B 90   ? 3.3593 3.3442 4.7710 -0.3964 -0.1087 -0.3581 90   ASP X C   
13259 O O   . ASP B 90   ? 3.3636 3.3834 4.7891 -0.3847 -0.1007 -0.3774 90   ASP X O   
13260 C CB  . ASP B 90   ? 3.3813 3.4386 4.6545 -0.4304 -0.1605 -0.3094 90   ASP X CB  
13261 C CG  . ASP B 90   ? 3.3930 3.4872 4.6081 -0.4583 -0.2073 -0.2980 90   ASP X CG  
13262 O OD1 . ASP B 90   ? 3.3964 3.4821 4.6302 -0.4722 -0.2377 -0.3161 90   ASP X OD1 
13263 O OD2 . ASP B 90   ? 3.3927 3.5236 4.5439 -0.4660 -0.2138 -0.2712 90   ASP X OD2 
13264 N N   . LYS B 91   ? 3.3475 3.2735 4.7938 -0.3852 -0.0773 -0.3513 91   LYS X N   
13265 C CA  . LYS B 91   ? 3.3417 3.2368 4.8473 -0.3584 -0.0305 -0.3668 91   LYS X CA  
13266 C C   . LYS B 91   ? 3.2789 3.1546 4.8695 -0.3530 -0.0290 -0.4102 91   LYS X C   
13267 O O   . LYS B 91   ? 3.2942 3.1706 4.9324 -0.3328 -0.0008 -0.4318 91   LYS X O   
13268 C CB  . LYS B 91   ? 3.3908 3.2260 4.9015 -0.3481 0.0051  -0.3439 91   LYS X CB  
13269 C CG  . LYS B 91   ? 3.4480 3.2479 5.0167 -0.3201 0.0561  -0.3576 91   LYS X CG  
13270 C CD  . LYS B 91   ? 3.4981 3.2236 5.1087 -0.3140 0.0865  -0.3545 91   LYS X CD  
13271 C CE  . LYS B 91   ? 3.5246 3.2181 5.2280 -0.3111 0.0941  -0.3951 91   LYS X CE  
13272 N NZ  . LYS B 91   ? 3.5241 3.2257 5.2398 -0.3350 0.0480  -0.4120 91   LYS X NZ  
13273 N N   . GLU B 92   ? 3.2017 3.0585 4.8141 -0.3703 -0.0594 -0.4236 92   GLU X N   
13274 C CA  . GLU B 92   ? 3.1121 2.9509 4.8062 -0.3662 -0.0635 -0.4670 92   GLU X CA  
13275 C C   . GLU B 92   ? 3.1021 2.9983 4.7974 -0.3635 -0.0830 -0.4930 92   GLU X C   
13276 O O   . GLU B 92   ? 3.0959 2.9874 4.8592 -0.3555 -0.0841 -0.5323 92   GLU X O   
13277 C CB  . GLU B 92   ? 3.0230 2.8328 4.7336 -0.3863 -0.0976 -0.4751 92   GLU X CB  
13278 C CG  . GLU B 92   ? 2.9501 2.7294 4.7550 -0.3800 -0.0974 -0.5206 92   GLU X CG  
13279 C CD  . GLU B 92   ? 2.9012 2.6428 4.7784 -0.3548 -0.0428 -0.5363 92   GLU X CD  
13280 O OE1 . GLU B 92   ? 2.8886 2.5933 4.7582 -0.3471 -0.0057 -0.5109 92   GLU X OE1 
13281 O OE2 . GLU B 92   ? 2.8857 2.6338 4.8272 -0.3423 -0.0369 -0.5742 92   GLU X OE2 
13282 N N   . GLN B 93   ? 3.0951 3.0458 4.7155 -0.3701 -0.0980 -0.4715 93   GLN X N   
13283 C CA  . GLN B 93   ? 3.0810 3.0906 4.6919 -0.3667 -0.1116 -0.4913 93   GLN X CA  
13284 C C   . GLN B 93   ? 3.1166 3.1460 4.7258 -0.3448 -0.0720 -0.4851 93   GLN X C   
13285 O O   . GLN B 93   ? 3.1176 3.1978 4.7182 -0.3399 -0.0773 -0.4996 93   GLN X O   
13286 C CB  . GLN B 93   ? 3.0370 3.0966 4.5661 -0.3904 -0.1562 -0.4741 93   GLN X CB  
13287 C CG  . GLN B 93   ? 2.9929 3.0309 4.5101 -0.4134 -0.1962 -0.4715 93   GLN X CG  
13288 C CD  . GLN B 93   ? 2.9507 3.0324 4.3802 -0.4371 -0.2349 -0.4464 93   GLN X CD  
13289 O OE1 . GLN B 93   ? 2.9324 3.0604 4.3088 -0.4370 -0.2302 -0.4295 93   GLN X OE1 
13290 N NE2 . GLN B 93   ? 2.9376 3.0039 4.3529 -0.4576 -0.2729 -0.4443 93   GLN X NE2 
13291 N N   . TYR B 94   ? 3.1449 3.1330 4.7619 -0.3313 -0.0327 -0.4641 94   TYR X N   
13292 C CA  . TYR B 94   ? 3.1793 3.1801 4.7880 -0.3100 0.0047  -0.4533 94   TYR X CA  
13293 C C   . TYR B 94   ? 3.1421 3.0812 4.8004 -0.2882 0.0544  -0.4499 94   TYR X C   
13294 O O   . TYR B 94   ? 3.1426 3.0714 4.7656 -0.2771 0.0807  -0.4209 94   TYR X O   
13295 C CB  . TYR B 94   ? 3.2578 3.2933 4.7768 -0.3181 -0.0041 -0.4144 94   TYR X CB  
13296 C CG  . TYR B 94   ? 3.3268 3.4342 4.8086 -0.3207 -0.0211 -0.4203 94   TYR X CG  
13297 C CD1 . TYR B 94   ? 3.3589 3.4888 4.8721 -0.2997 0.0037  -0.4391 94   TYR X CD1 
13298 C CD2 . TYR B 94   ? 3.3504 3.5026 4.7661 -0.3443 -0.0609 -0.4071 94   TYR X CD2 
13299 C CE1 . TYR B 94   ? 3.3668 3.5631 4.8476 -0.3023 -0.0109 -0.4460 94   TYR X CE1 
13300 C CE2 . TYR B 94   ? 3.3597 3.5769 4.7410 -0.3473 -0.0743 -0.4130 94   TYR X CE2 
13301 C CZ  . TYR B 94   ? 3.3625 3.6022 4.7770 -0.3263 -0.0493 -0.4330 94   TYR X CZ  
13302 O OH  . TYR B 94   ? 3.3549 3.6603 4.7368 -0.3296 -0.0619 -0.4403 94   TYR X OH  
13303 N N   . LYS B 95   ? 3.1029 2.9997 4.8420 -0.2818 0.0673  -0.4794 95   LYS X N   
13304 C CA  . LYS B 95   ? 3.0688 2.9084 4.8632 -0.2597 0.1182  -0.4813 95   LYS X CA  
13305 C C   . LYS B 95   ? 3.0535 2.9158 4.8799 -0.2364 0.1463  -0.4983 95   LYS X C   
13306 O O   . LYS B 95   ? 3.0864 2.9061 4.9593 -0.2157 0.1907  -0.5013 95   LYS X O   
13307 C CB  . LYS B 95   ? 3.0394 2.8264 4.9153 -0.2614 0.1237  -0.5095 95   LYS X CB  
13308 C CG  . LYS B 95   ? 3.0125 2.7571 4.8705 -0.2785 0.1120  -0.4905 95   LYS X CG  
13309 C CD  . LYS B 95   ? 2.9944 2.6795 4.9427 -0.2751 0.1299  -0.5189 95   LYS X CD  
13310 C CE  . LYS B 95   ? 2.9806 2.6211 4.9148 -0.2914 0.1215  -0.5007 95   LYS X CE  
13311 N NZ  . LYS B 95   ? 2.9788 2.5563 5.0030 -0.2862 0.1470  -0.5265 95   LYS X NZ  
13312 N N   . GLU B 96   ? 2.9965 2.9251 4.7982 -0.2401 0.1205  -0.5098 96   GLU X N   
13313 C CA  . GLU B 96   ? 2.9488 2.9079 4.7819 -0.2199 0.1411  -0.5298 96   GLU X CA  
13314 C C   . GLU B 96   ? 2.9353 2.9053 4.7181 -0.2055 0.1672  -0.4988 96   GLU X C   
13315 O O   . GLU B 96   ? 2.9468 2.8953 4.7681 -0.1819 0.2070  -0.5034 96   GLU X O   
13316 C CB  . GLU B 96   ? 2.9119 2.9387 4.7378 -0.2303 0.1020  -0.5561 96   GLU X CB  
13317 C CG  . GLU B 96   ? 2.8871 2.9653 4.6190 -0.2511 0.0648  -0.5303 96   GLU X CG  
13318 C CD  . GLU B 96   ? 2.8677 2.9962 4.5915 -0.2675 0.0203  -0.5557 96   GLU X CD  
13319 O OE1 . GLU B 96   ? 2.8670 2.9758 4.6447 -0.2712 0.0059  -0.5854 96   GLU X OE1 
13320 O OE2 . GLU B 96   ? 2.8545 3.0412 4.5175 -0.2764 -0.0001 -0.5464 96   GLU X OE2 
13321 N N   . GLY B 97   ? 2.9046 2.9076 4.6025 -0.2193 0.1438  -0.4680 97   GLY X N   
13322 C CA  . GLY B 97   ? 2.8827 2.9000 4.5275 -0.2071 0.1624  -0.4388 97   GLY X CA  
13323 C C   . GLY B 97   ? 2.8392 2.9195 4.4032 -0.2244 0.1271  -0.4205 97   GLY X C   
13324 O O   . GLY B 97   ? 2.8201 2.9352 4.3681 -0.2460 0.0887  -0.4312 97   GLY X O   
13325 N N   . LEU B 98   ? 2.8208 2.9139 4.3338 -0.2146 0.1404  -0.3931 98   LEU X N   
13326 C CA  . LEU B 98   ? 2.7882 2.9415 4.2268 -0.2290 0.1118  -0.3754 98   LEU X CA  
13327 C C   . LEU B 98   ? 2.7644 2.9795 4.2056 -0.2202 0.1119  -0.3941 98   LEU X C   
13328 O O   . LEU B 98   ? 2.7737 2.9811 4.2425 -0.1959 0.1435  -0.3992 98   LEU X O   
13329 C CB  . LEU B 98   ? 2.7885 2.9230 4.1667 -0.2242 0.1225  -0.3349 98   LEU X CB  
13330 C CG  . LEU B 98   ? 2.7881 2.8772 4.1366 -0.2373 0.1146  -0.3079 98   LEU X CG  
13331 C CD1 . LEU B 98   ? 2.7921 2.8867 4.0710 -0.2334 0.1170  -0.2712 98   LEU X CD1 
13332 C CD2 . LEU B 98   ? 2.7707 2.8796 4.1066 -0.2675 0.0726  -0.3139 98   LEU X CD2 
13333 N N   . GLN B 99   ? 2.7422 3.0175 4.1546 -0.2400 0.0769  -0.4043 99   GLN X N   
13334 C CA  . GLN B 99   ? 2.7326 3.0735 4.1285 -0.2358 0.0734  -0.4151 99   GLN X CA  
13335 C C   . GLN B 99   ? 2.7457 3.1193 4.0612 -0.2469 0.0592  -0.3825 99   GLN X C   
13336 O O   . GLN B 99   ? 2.7298 3.1193 3.9994 -0.2717 0.0284  -0.3694 99   GLN X O   
13337 C CB  . GLN B 99   ? 2.7076 3.0965 4.1208 -0.2497 0.0458  -0.4485 99   GLN X CB  
13338 C CG  . GLN B 99   ? 2.7014 3.0589 4.1929 -0.2429 0.0512  -0.4826 99   GLN X CG  
13339 C CD  . GLN B 99   ? 2.6988 3.0270 4.1892 -0.2635 0.0244  -0.4823 99   GLN X CD  
13340 O OE1 . GLN B 99   ? 2.6973 3.0291 4.1272 -0.2835 0.0015  -0.4558 99   GLN X OE1 
13341 N NE2 . GLN B 99   ? 2.6981 2.9975 4.2579 -0.2585 0.0264  -0.5130 99   GLN X NE2 
13342 N N   . GLY B 100  ? 2.7774 3.1608 4.0781 -0.2282 0.0812  -0.3705 100  GLY X N   
13343 C CA  . GLY B 100  ? 2.7851 3.1908 4.0164 -0.2337 0.0730  -0.3393 100  GLY X CA  
13344 C C   . GLY B 100  ? 2.7758 3.2013 3.9496 -0.2639 0.0375  -0.3206 100  GLY X C   
13345 O O   . GLY B 100  ? 2.7510 3.2366 3.8901 -0.2806 0.0143  -0.3244 100  GLY X O   
13346 N N   . GLN B 101  ? 2.7956 3.1695 3.9597 -0.2711 0.0342  -0.3004 101  GLN X N   
13347 C CA  . GLN B 101  ? 2.8177 3.2027 3.9275 -0.2985 0.0022  -0.2789 101  GLN X CA  
13348 C C   . GLN B 101  ? 2.8522 3.2336 3.9075 -0.2952 0.0056  -0.2440 101  GLN X C   
13349 O O   . GLN B 101  ? 2.8452 3.2139 3.9027 -0.2709 0.0321  -0.2365 101  GLN X O   
13350 C CB  . GLN B 101  ? 2.8289 3.1623 3.9605 -0.3104 -0.0077 -0.2785 101  GLN X CB  
13351 C CG  . GLN B 101  ? 2.8493 3.1900 4.0247 -0.3199 -0.0226 -0.3115 101  GLN X CG  
13352 C CD  . GLN B 101  ? 2.8853 3.1819 4.1359 -0.2977 0.0070  -0.3353 101  GLN X CD  
13353 O OE1 . GLN B 101  ? 2.9053 3.1708 4.1737 -0.2742 0.0410  -0.3278 101  GLN X OE1 
13354 N NE2 . GLN B 101  ? 2.8939 3.1860 4.1895 -0.3045 -0.0058 -0.3645 101  GLN X NE2 
13355 N N   . ASN B 102  ? 2.8988 3.2912 3.9057 -0.3192 -0.0222 -0.2233 102  ASN X N   
13356 C CA  . ASN B 102  ? 2.9454 3.3266 3.9038 -0.3180 -0.0221 -0.1899 102  ASN X CA  
13357 C C   . ASN B 102  ? 3.0667 3.3778 4.0334 -0.3155 -0.0146 -0.1729 102  ASN X C   
13358 O O   . ASN B 102  ? 3.0702 3.3616 4.0481 -0.3338 -0.0321 -0.1761 102  ASN X O   
13359 C CB  . ASN B 102  ? 2.8550 3.2872 3.7574 -0.3456 -0.0556 -0.1761 102  ASN X CB  
13360 C CG  . ASN B 102  ? 2.7691 3.2699 3.6536 -0.3462 -0.0589 -0.1868 102  ASN X CG  
13361 O OD1 . ASN B 102  ? 2.7287 3.2739 3.6075 -0.3653 -0.0787 -0.2023 102  ASN X OD1 
13362 N ND2 . ASN B 102  ? 2.7471 3.2561 3.6220 -0.3249 -0.0396 -0.1793 102  ASN X ND2 
13363 N N   . VAL B 103  ? 3.1819 3.4552 4.1419 -0.2926 0.0110  -0.1553 103  VAL X N   
13364 C CA  . VAL B 103  ? 3.3105 3.5160 4.2764 -0.2883 0.0219  -0.1388 103  VAL X CA  
13365 C C   . VAL B 103  ? 3.4313 3.6291 4.3422 -0.2857 0.0185  -0.1061 103  VAL X C   
13366 O O   . VAL B 103  ? 3.4472 3.6392 4.3420 -0.2620 0.0388  -0.0957 103  VAL X O   
13367 C CB  . VAL B 103  ? 3.4351 3.5835 4.4524 -0.2602 0.0619  -0.1494 103  VAL X CB  
13368 C CG1 . VAL B 103  ? 3.4519 3.5301 4.4670 -0.2546 0.0761  -0.1291 103  VAL X CG1 
13369 C CG2 . VAL B 103  ? 3.4356 3.5840 4.5149 -0.2635 0.0643  -0.1831 103  VAL X CG2 
13370 N N   . PHE B 104  ? 3.5427 3.7417 4.4250 -0.3100 -0.0090 -0.0907 104  PHE X N   
13371 C CA  . PHE B 104  ? 3.6526 3.8390 4.4868 -0.3096 -0.0147 -0.0601 104  PHE X CA  
13372 C C   . PHE B 104  ? 3.6739 3.7873 4.5221 -0.2861 0.0163  -0.0493 104  PHE X C   
13373 O O   . PHE B 104  ? 3.6796 3.7484 4.5367 -0.2947 0.0142  -0.0420 104  PHE X O   
13374 C CB  . PHE B 104  ? 3.7291 3.9256 4.5407 -0.3417 -0.0500 -0.0493 104  PHE X CB  
13375 C CG  . PHE B 104  ? 3.7914 3.9911 4.5516 -0.3458 -0.0628 -0.0200 104  PHE X CG  
13376 C CD1 . PHE B 104  ? 3.8022 4.0536 4.5231 -0.3446 -0.0716 -0.0113 104  PHE X CD1 
13377 C CD2 . PHE B 104  ? 3.8179 3.9699 4.5719 -0.3510 -0.0663 -0.0027 104  PHE X CD2 
13378 C CE1 . PHE B 104  ? 3.8066 4.0620 4.4836 -0.3477 -0.0842 0.0140  104  PHE X CE1 
13379 C CE2 . PHE B 104  ? 3.8215 3.9779 4.5300 -0.3543 -0.0791 0.0230  104  PHE X CE2 
13380 C CZ  . PHE B 104  ? 3.8134 4.0212 4.4839 -0.3523 -0.0883 0.0312  104  PHE X CZ  
13381 N N   . VAL B 105  ? 3.6729 3.7733 4.5230 -0.2563 0.0457  -0.0488 105  VAL X N   
13382 C CA  . VAL B 105  ? 3.6676 3.6963 4.5298 -0.2313 0.0797  -0.0392 105  VAL X CA  
13383 C C   . VAL B 105  ? 3.6194 3.6250 4.4293 -0.2241 0.0776  -0.0084 105  VAL X C   
13384 O O   . VAL B 105  ? 3.6397 3.6524 4.4174 -0.2029 0.0868  0.0032  105  VAL X O   
13385 C CB  . VAL B 105  ? 3.7066 3.7237 4.5954 -0.2007 0.1140  -0.0519 105  VAL X CB  
13386 C CG1 . VAL B 105  ? 3.7047 3.7814 4.5635 -0.1926 0.1057  -0.0519 105  VAL X CG1 
13387 C CG2 . VAL B 105  ? 3.7444 3.6873 4.6322 -0.1733 0.1496  -0.0367 105  VAL X CG2 
13388 N N   . VAL B 106  ? 3.5378 3.5166 4.3398 -0.2416 0.0638  0.0036  106  VAL X N   
13389 C CA  . VAL B 106  ? 3.4661 3.4122 4.2254 -0.2335 0.0651  0.0311  106  VAL X CA  
13390 C C   . VAL B 106  ? 3.4106 3.2769 4.1954 -0.2184 0.0976  0.0339  106  VAL X C   
13391 O O   . VAL B 106  ? 3.4030 3.2447 4.2353 -0.2294 0.1033  0.0179  106  VAL X O   
13392 C CB  . VAL B 106  ? 3.4460 3.4174 4.1770 -0.2635 0.0270  0.0441  106  VAL X CB  
13393 C CG1 . VAL B 106  ? 3.4188 3.4679 4.1330 -0.2828 -0.0037 0.0377  106  VAL X CG1 
13394 C CG2 . VAL B 106  ? 3.4374 3.3765 4.2042 -0.2845 0.0202  0.0363  106  VAL X CG2 
13395 N N   . GLN B 107  ? 3.3546 3.1795 4.1082 -0.1929 0.1194  0.0533  107  GLN X N   
13396 C CA  . GLN B 107  ? 3.3007 3.0470 4.0748 -0.1761 0.1554  0.0569  107  GLN X CA  
13397 C C   . GLN B 107  ? 3.2445 2.9559 4.0197 -0.1953 0.1451  0.0662  107  GLN X C   
13398 O O   . GLN B 107  ? 3.2297 2.9598 3.9640 -0.2077 0.1179  0.0834  107  GLN X O   
13399 C CB  . GLN B 107  ? 3.3034 3.0138 4.0399 -0.1403 0.1835  0.0746  107  GLN X CB  
13400 C CG  . GLN B 107  ? 3.2697 3.0053 3.9409 -0.1362 0.1609  0.0976  107  GLN X CG  
13401 C CD  . GLN B 107  ? 3.2745 2.9862 3.9095 -0.0989 0.1844  0.1104  107  GLN X CD  
13402 O OE1 . GLN B 107  ? 3.2822 2.9975 3.9350 -0.0804 0.2041  0.0989  107  GLN X OE1 
13403 N NE2 . GLN B 107  ? 3.2774 2.9637 3.8612 -0.0869 0.1815  0.1338  107  GLN X NE2 
13404 N N   . GLU B 108  ? 3.2004 2.8627 4.0260 -0.1983 0.1661  0.0531  108  GLU X N   
13405 C CA  . GLU B 108  ? 3.1446 2.7652 3.9786 -0.2137 0.1621  0.0595  108  GLU X CA  
13406 C C   . GLU B 108  ? 3.1606 2.7035 3.9873 -0.1879 0.2042  0.0728  108  GLU X C   
13407 O O   . GLU B 108  ? 3.1605 2.6690 3.9664 -0.1920 0.2028  0.0884  108  GLU X O   
13408 C CB  . GLU B 108  ? 3.0963 2.7138 3.9949 -0.2363 0.1554  0.0337  108  GLU X CB  
13409 C CG  . GLU B 108  ? 3.0301 2.7181 3.9423 -0.2571 0.1215  0.0158  108  GLU X CG  
13410 C CD  . GLU B 108  ? 2.9685 2.7000 3.8483 -0.2862 0.0753  0.0262  108  GLU X CD  
13411 O OE1 . GLU B 108  ? 2.9508 2.6528 3.8318 -0.3003 0.0654  0.0340  108  GLU X OE1 
13412 O OE2 . GLU B 108  ? 2.9393 2.7340 3.7938 -0.2952 0.0495  0.0261  108  GLU X OE2 
13413 N N   . LEU B 109  ? 3.1749 2.6907 4.0186 -0.1613 0.2416  0.0662  109  LEU X N   
13414 C CA  . LEU B 109  ? 3.2282 2.6707 4.0609 -0.1330 0.2856  0.0791  109  LEU X CA  
13415 C C   . LEU B 109  ? 3.3445 2.7896 4.1798 -0.1049 0.3116  0.0739  109  LEU X C   
13416 O O   . LEU B 109  ? 3.3383 2.8358 4.1985 -0.1113 0.2979  0.0557  109  LEU X O   
13417 C CB  . LEU B 109  ? 3.1898 2.5697 4.0750 -0.1393 0.3122  0.0682  109  LEU X CB  
13418 C CG  . LEU B 109  ? 3.1394 2.4903 4.0153 -0.1565 0.3012  0.0787  109  LEU X CG  
13419 C CD1 . LEU B 109  ? 3.1646 2.4572 4.1052 -0.1635 0.3289  0.0617  109  LEU X CD1 
13420 C CD2 . LEU B 109  ? 3.1559 2.4741 3.9631 -0.1373 0.3107  0.1090  109  LEU X CD2 
13421 N N   . ILE B 110  ? 3.4839 2.8714 4.2948 -0.0740 0.3494  0.0887  110  ILE X N   
13422 C CA  . ILE B 110  ? 3.6098 3.0004 4.4150 -0.0455 0.3711  0.0869  110  ILE X CA  
13423 C C   . ILE B 110  ? 3.7697 3.0800 4.5901 -0.0171 0.4253  0.0901  110  ILE X C   
13424 O O   . ILE B 110  ? 3.7927 3.0394 4.6108 -0.0148 0.4485  0.1001  110  ILE X O   
13425 C CB  . ILE B 110  ? 3.6239 3.0485 4.3570 -0.0302 0.3506  0.1073  110  ILE X CB  
13426 C CG1 . ILE B 110  ? 3.5592 3.0625 4.2760 -0.0585 0.2989  0.1054  110  ILE X CG1 
13427 C CG2 . ILE B 110  ? 3.6567 3.0918 4.3877 -0.0026 0.3680  0.1027  110  ILE X CG2 
13428 C CD1 . ILE B 110  ? 3.5502 3.0989 4.2117 -0.0447 0.2785  0.1175  110  ILE X CD1 
13429 N N   . ASP B 111  ? 3.8847 3.1989 4.7227 0.0037  0.4459  0.0808  111  ASP X N   
13430 C CA  . ASP B 111  ? 4.0309 3.2724 4.8735 0.0351  0.4972  0.0870  111  ASP X CA  
13431 C C   . ASP B 111  ? 4.1019 3.3427 4.8758 0.0662  0.4992  0.1086  111  ASP X C   
13432 O O   . ASP B 111  ? 4.0843 3.3915 4.8309 0.0636  0.4645  0.1086  111  ASP X O   
13433 C CB  . ASP B 111  ? 4.0674 3.3104 4.9862 0.0369  0.5202  0.0591  111  ASP X CB  
13434 C CG  . ASP B 111  ? 4.1472 3.3093 5.0825 0.0655  0.5766  0.0635  111  ASP X CG  
13435 O OD1 . ASP B 111  ? 4.1987 3.3473 5.0990 0.0951  0.5930  0.0758  111  ASP X OD1 
13436 O OD2 . ASP B 111  ? 4.1559 3.2673 5.1404 0.0583  0.6048  0.0540  111  ASP X OD2 
13437 N N   . PRO B 112  ? 4.1754 3.3402 4.9200 0.0960  0.5394  0.1268  112  PRO X N   
13438 C CA  . PRO B 112  ? 4.2112 3.3671 4.8871 0.1284  0.5415  0.1480  112  PRO X CA  
13439 C C   . PRO B 112  ? 4.1832 3.3952 4.8674 0.1401  0.5294  0.1359  112  PRO X C   
13440 O O   . PRO B 112  ? 4.1970 3.4334 4.8248 0.1566  0.5102  0.1490  112  PRO X O   
13441 C CB  . PRO B 112  ? 4.2817 3.3397 4.9473 0.1571  0.5961  0.1622  112  PRO X CB  
13442 C CG  . PRO B 112  ? 4.2759 3.3021 5.0204 0.1391  0.6243  0.1424  112  PRO X CG  
13443 C CD  . PRO B 112  ? 4.2191 3.2994 4.9866 0.1008  0.5837  0.1304  112  PRO X CD  
13444 N N   . ASN B 113  ? 4.1413 3.3741 4.8961 0.1318  0.5395  0.1099  113  ASN X N   
13445 C CA  . ASN B 113  ? 4.1024 3.3879 4.8715 0.1424  0.5303  0.0958  113  ASN X CA  
13446 C C   . ASN B 113  ? 3.9990 3.3795 4.7579 0.1198  0.4784  0.0864  113  ASN X C   
13447 O O   . ASN B 113  ? 3.9768 3.4098 4.7479 0.1248  0.4665  0.0728  113  ASN X O   
13448 C CB  . ASN B 113  ? 4.1216 3.3983 4.9720 0.1419  0.5589  0.0696  113  ASN X CB  
13449 C CG  . ASN B 113  ? 4.0890 3.4171 5.0012 0.1056  0.5356  0.0428  113  ASN X CG  
13450 O OD1 . ASN B 113  ? 4.0720 3.4403 5.0383 0.1006  0.5333  0.0173  113  ASN X OD1 
13451 N ND2 . ASN B 113  ? 4.0788 3.4051 4.9824 0.0808  0.5173  0.0481  113  ASN X ND2 
13452 N N   . GLY B 114  ? 3.9289 3.3302 4.6659 0.0946  0.4485  0.0936  114  GLY X N   
13453 C CA  . GLY B 114  ? 3.8368 3.3238 4.5616 0.0711  0.4005  0.0867  114  GLY X CA  
13454 C C   . GLY B 114  ? 3.7444 3.2761 4.5289 0.0363  0.3824  0.0617  114  GLY X C   
13455 O O   . GLY B 114  ? 3.7077 3.2999 4.4809 0.0106  0.3429  0.0587  114  GLY X O   
13456 N N   . ARG B 115  ? 3.7091 3.2102 4.5573 0.0359  0.4111  0.0432  115  ARG X N   
13457 C CA  . ARG B 115  ? 3.6366 3.1731 4.5439 0.0051  0.3950  0.0177  115  ARG X CA  
13458 C C   . ARG B 115  ? 3.6124 3.1359 4.5103 -0.0207 0.3768  0.0262  115  ARG X C   
13459 O O   . ARG B 115  ? 3.6243 3.0857 4.4994 -0.0123 0.3959  0.0448  115  ARG X O   
13460 C CB  . ARG B 115  ? 3.6358 3.1355 4.6161 0.0124  0.4315  -0.0044 115  ARG X CB  
13461 C CG  . ARG B 115  ? 3.6544 3.0794 4.6619 0.0092  0.4600  -0.0014 115  ARG X CG  
13462 C CD  . ARG B 115  ? 3.6649 3.0608 4.7521 0.0148  0.4941  -0.0270 115  ARG X CD  
13463 N NE  . ARG B 115  ? 3.7000 3.0103 4.8060 0.0231  0.5347  -0.0198 115  ARG X NE  
13464 C CZ  . ARG B 115  ? 3.7455 2.9916 4.8442 0.0531  0.5795  -0.0076 115  ARG X CZ  
13465 N NH1 . ARG B 115  ? 3.7638 3.0219 4.8376 0.0785  0.5874  -0.0015 115  ARG X NH1 
13466 N NH2 . ARG B 115  ? 3.7721 2.9409 4.8887 0.0578  0.6168  -0.0019 115  ARG X NH2 
13467 N N   . LEU B 116  ? 3.5872 3.1685 4.5025 -0.0519 0.3401  0.0121  116  LEU X N   
13468 C CA  . LEU B 116  ? 3.5830 3.1619 4.4842 -0.0779 0.3156  0.0208  116  LEU X CA  
13469 C C   . LEU B 116  ? 3.6038 3.2015 4.5651 -0.1067 0.3008  -0.0048 116  LEU X C   
13470 O O   . LEU B 116  ? 3.5853 3.2366 4.5751 -0.1163 0.2849  -0.0263 116  LEU X O   
13471 C CB  . LEU B 116  ? 3.5169 3.1516 4.3561 -0.0882 0.2755  0.0374  116  LEU X CB  
13472 C CG  . LEU B 116  ? 3.4335 3.1506 4.2716 -0.0972 0.2474  0.0236  116  LEU X CG  
13473 C CD1 . LEU B 116  ? 3.3771 3.1420 4.2376 -0.1338 0.2117  0.0091  116  LEU X CD1 
13474 C CD2 . LEU B 116  ? 3.4138 3.1638 4.1873 -0.0863 0.2298  0.0431  116  LEU X CD2 
13475 N N   . SER B 117  ? 3.6412 3.1931 4.6221 -0.1194 0.3062  -0.0034 117  SER X N   
13476 C CA  . SER B 117  ? 3.6409 3.2062 4.6755 -0.1474 0.2879  -0.0266 117  SER X CA  
13477 C C   . SER B 117  ? 3.6015 3.2304 4.6055 -0.1768 0.2364  -0.0231 117  SER X C   
13478 O O   . SER B 117  ? 3.6118 3.2550 4.5563 -0.1785 0.2185  0.0009  117  SER X O   
13479 C CB  . SER B 117  ? 3.6816 3.1755 4.7484 -0.1509 0.3108  -0.0267 117  SER X CB  
13480 O OG  . SER B 117  ? 3.7116 3.1741 4.7245 -0.1484 0.3106  0.0019  117  SER X OG  
13481 N N   . THR B 118  ? 3.5487 3.2144 4.5936 -0.1994 0.2129  -0.0474 118  THR X N   
13482 C CA  . THR B 118  ? 3.4943 3.2204 4.5137 -0.2285 0.1646  -0.0464 118  THR X CA  
13483 C C   . THR B 118  ? 3.4487 3.1836 4.5231 -0.2522 0.1460  -0.0735 118  THR X C   
13484 O O   . THR B 118  ? 3.4617 3.1707 4.5963 -0.2444 0.1688  -0.0970 118  THR X O   
13485 C CB  . THR B 118  ? 3.6872 3.4836 4.6718 -0.2258 0.1468  -0.0456 118  THR X CB  
13486 O OG1 . THR B 118  ? 3.6534 3.5062 4.6164 -0.2555 0.1021  -0.0459 118  THR X OG1 
13487 C CG2 . THR B 118  ? 3.6933 3.5067 4.7233 -0.2128 0.1646  -0.0719 118  THR X CG2 
13488 N N   . VAL B 119  ? 3.3967 3.1673 4.4516 -0.2806 0.1042  -0.0708 119  VAL X N   
13489 C CA  . VAL B 119  ? 3.3389 3.1150 4.4408 -0.3031 0.0827  -0.0953 119  VAL X CA  
13490 C C   . VAL B 119  ? 3.2861 3.1324 4.3622 -0.3273 0.0378  -0.0997 119  VAL X C   
13491 O O   . VAL B 119  ? 3.2707 3.1431 4.2951 -0.3423 0.0105  -0.0784 119  VAL X O   
13492 C CB  . VAL B 119  ? 3.3203 3.0444 4.4387 -0.3161 0.0793  -0.0902 119  VAL X CB  
13493 C CG1 . VAL B 119  ? 3.3053 3.0309 4.3609 -0.3237 0.0629  -0.0576 119  VAL X CG1 
13494 C CG2 . VAL B 119  ? 3.2991 3.0361 4.4573 -0.3416 0.0479  -0.1140 119  VAL X CG2 
13495 N N   . GLY B 120  ? 3.2469 3.1226 4.3600 -0.3307 0.0311  -0.1279 120  GLY X N   
13496 C CA  . GLY B 120  ? 3.1930 3.1333 4.2832 -0.3525 -0.0085 -0.1349 120  GLY X CA  
13497 C C   . GLY B 120  ? 3.1515 3.1464 4.1899 -0.3464 -0.0118 -0.1214 120  GLY X C   
13498 O O   . GLY B 120  ? 3.1826 3.1718 4.2194 -0.3214 0.0184  -0.1179 120  GLY X O   
13499 N N   . GLY B 121  ? 3.0914 3.1386 4.0883 -0.3694 -0.0487 -0.1142 121  GLY X N   
13500 C CA  . GLY B 121  ? 3.0536 3.1557 4.0001 -0.3675 -0.0553 -0.1013 121  GLY X CA  
13501 C C   . GLY B 121  ? 3.0326 3.1865 3.9915 -0.3643 -0.0558 -0.1246 121  GLY X C   
13502 O O   . GLY B 121  ? 3.0201 3.2230 3.9426 -0.3626 -0.0601 -0.1178 121  GLY X O   
13503 N N   . VAL B 122  ? 3.0162 3.1601 4.0285 -0.3634 -0.0518 -0.1537 122  VAL X N   
13504 C CA  . VAL B 122  ? 2.9714 3.1612 4.0018 -0.3584 -0.0504 -0.1791 122  VAL X CA  
13505 C C   . VAL B 122  ? 2.8750 3.1220 3.8779 -0.3854 -0.0890 -0.1865 122  VAL X C   
13506 O O   . VAL B 122  ? 2.8816 3.1207 3.8772 -0.4080 -0.1172 -0.1841 122  VAL X O   
13507 C CB  . VAL B 122  ? 2.9948 3.1514 4.0974 -0.3434 -0.0281 -0.2096 122  VAL X CB  
13508 C CG1 . VAL B 122  ? 2.9929 3.1966 4.1147 -0.3336 -0.0219 -0.2349 122  VAL X CG1 
13509 C CG2 . VAL B 122  ? 3.0167 3.1101 4.1452 -0.3186 0.0113  -0.2005 122  VAL X CG2 
13510 N N   . THR B 123  ? 2.7685 3.0717 3.7561 -0.3825 -0.0895 -0.1958 123  THR X N   
13511 C CA  . THR B 123  ? 2.6789 3.0404 3.6351 -0.4062 -0.1218 -0.2025 123  THR X CA  
13512 C C   . THR B 123  ? 2.6071 3.0095 3.5894 -0.3964 -0.1133 -0.2329 123  THR X C   
13513 O O   . THR B 123  ? 2.6185 3.0039 3.6428 -0.3713 -0.0830 -0.2466 123  THR X O   
13514 C CB  . THR B 123  ? 2.8975 3.2965 3.7869 -0.4199 -0.1371 -0.1736 123  THR X CB  
13515 O OG1 . THR B 123  ? 2.8894 3.3547 3.7550 -0.4277 -0.1470 -0.1841 123  THR X OG1 
13516 C CG2 . THR B 123  ? 2.9033 3.2815 3.7804 -0.3985 -0.1112 -0.1520 123  THR X CG2 
13517 N N   . LYS B 124  ? 2.5434 2.9983 3.5007 -0.4159 -0.1394 -0.2433 124  LYS X N   
13518 C CA  . LYS B 124  ? 2.4596 2.9515 3.4448 -0.4099 -0.1369 -0.2765 124  LYS X CA  
13519 C C   . LYS B 124  ? 2.4428 2.9621 3.4429 -0.3860 -0.1075 -0.2861 124  LYS X C   
13520 O O   . LYS B 124  ? 2.4630 2.9570 3.5180 -0.3631 -0.0821 -0.3049 124  LYS X O   
13521 C CB  . LYS B 124  ? 2.3807 2.9224 3.3276 -0.4367 -0.1714 -0.2835 124  LYS X CB  
13522 C CG  . LYS B 124  ? 2.2949 2.8809 3.1741 -0.4545 -0.1853 -0.2581 124  LYS X CG  
13523 C CD  . LYS B 124  ? 2.2368 2.8533 3.0770 -0.4841 -0.2212 -0.2602 124  LYS X CD  
13524 C CE  . LYS B 124  ? 2.2026 2.8615 3.0552 -0.4837 -0.2252 -0.2930 124  LYS X CE  
13525 N NZ  . LYS B 124  ? 2.1828 2.9013 3.0102 -0.4808 -0.2132 -0.2942 124  LYS X NZ  
13526 N N   . LYS B 125  ? 2.3879 2.9581 3.3421 -0.3912 -0.1108 -0.2745 125  LYS X N   
13527 C CA  . LYS B 125  ? 2.3560 2.9603 3.3228 -0.3708 -0.0876 -0.2865 125  LYS X CA  
13528 C C   . LYS B 125  ? 2.3543 2.9880 3.3599 -0.3672 -0.0873 -0.3241 125  LYS X C   
13529 O O   . LYS B 125  ? 2.3525 2.9509 3.4125 -0.3556 -0.0778 -0.3442 125  LYS X O   
13530 C CB  . LYS B 125  ? 2.3393 2.8967 3.3356 -0.3411 -0.0538 -0.2779 125  LYS X CB  
13531 C CG  . LYS B 125  ? 2.3190 2.9061 3.3300 -0.3178 -0.0295 -0.2894 125  LYS X CG  
13532 C CD  . LYS B 125  ? 2.2905 2.9190 3.2478 -0.3216 -0.0343 -0.2691 125  LYS X CD  
13533 C CE  . LYS B 125  ? 2.2662 2.9192 3.2406 -0.2966 -0.0104 -0.2802 125  LYS X CE  
13534 N NZ  . LYS B 125  ? 2.2472 2.9515 3.2471 -0.2986 -0.0123 -0.3135 125  LYS X NZ  
13535 N N   . ASN B 126  ? 2.3614 3.0598 3.3414 -0.3767 -0.0970 -0.3349 126  ASN X N   
13536 C CA  . ASN B 126  ? 2.3659 3.1074 3.2874 -0.3894 -0.1052 -0.3134 126  ASN X CA  
13537 C C   . ASN B 126  ? 2.4651 3.2002 3.3341 -0.4171 -0.1326 -0.2863 126  ASN X C   
13538 O O   . ASN B 126  ? 2.4918 3.2434 3.3410 -0.4400 -0.1583 -0.2925 126  ASN X O   
13539 C CB  . ASN B 126  ? 2.2828 3.0946 3.1936 -0.3950 -0.1088 -0.3353 126  ASN X CB  
13540 C CG  . ASN B 126  ? 2.1754 2.9990 3.1358 -0.3673 -0.0815 -0.3603 126  ASN X CG  
13541 O OD1 . ASN B 126  ? 2.1467 2.9352 3.1338 -0.3433 -0.0574 -0.3531 126  ASN X OD1 
13542 N ND2 . ASN B 126  ? 2.2063 3.0786 3.1784 -0.3702 -0.0851 -0.3898 126  ASN X ND2 
13543 N N   . ASN B 127  ? 2.5515 3.2617 3.3982 -0.4137 -0.1272 -0.2565 127  ASN X N   
13544 C CA  . ASN B 127  ? 2.6337 3.3337 3.4344 -0.4373 -0.1506 -0.2284 127  ASN X CA  
13545 C C   . ASN B 127  ? 2.6880 3.4453 3.4354 -0.4537 -0.1617 -0.2150 127  ASN X C   
13546 O O   . ASN B 127  ? 2.6731 3.4445 3.4100 -0.4408 -0.1469 -0.2043 127  ASN X O   
13547 C CB  . ASN B 127  ? 2.6959 3.3369 3.5023 -0.4244 -0.1388 -0.2043 127  ASN X CB  
13548 C CG  . ASN B 127  ? 2.7574 3.3745 3.5316 -0.4478 -0.1639 -0.1801 127  ASN X CG  
13549 O OD1 . ASN B 127  ? 2.7771 3.4185 3.5250 -0.4739 -0.1908 -0.1807 127  ASN X OD1 
13550 N ND2 . ASN B 127  ? 2.7844 3.3525 3.5599 -0.4381 -0.1550 -0.1587 127  ASN X ND2 
13551 N N   . LYS B 128  ? 2.7334 3.5221 3.4477 -0.4818 -0.1875 -0.2161 128  LYS X N   
13552 C CA  . LYS B 128  ? 2.7610 3.6048 3.4251 -0.5010 -0.1982 -0.2046 128  LYS X CA  
13553 C C   . LYS B 128  ? 2.8086 3.6417 3.4472 -0.4993 -0.1955 -0.1736 128  LYS X C   
13554 O O   . LYS B 128  ? 2.8212 3.6064 3.4581 -0.5008 -0.2021 -0.1540 128  LYS X O   
13555 C CB  . LYS B 128  ? 2.7200 3.5803 3.3479 -0.5332 -0.2284 -0.2028 128  LYS X CB  
13556 C CG  . LYS B 128  ? 2.6670 3.5281 3.3181 -0.5350 -0.2362 -0.2324 128  LYS X CG  
13557 C CD  . LYS B 128  ? 2.6160 3.4897 3.2240 -0.5663 -0.2676 -0.2278 128  LYS X CD  
13558 C CE  . LYS B 128  ? 2.5677 3.4931 3.1204 -0.5876 -0.2742 -0.2117 128  LYS X CE  
13559 N NZ  . LYS B 128  ? 2.5386 3.5193 3.0957 -0.5780 -0.2545 -0.2305 128  LYS X NZ  
13560 N N   . THR B 129  ? 2.2535 3.1796 2.5875 0.2243  -0.7174 -0.6905 129  THR X N   
13561 C CA  . THR B 129  ? 2.2497 3.1975 2.5798 0.2076  -0.6891 -0.6749 129  THR X CA  
13562 C C   . THR B 129  ? 2.2601 3.2321 2.5560 0.2033  -0.6589 -0.6724 129  THR X C   
13563 O O   . THR B 129  ? 2.2420 3.2403 2.5188 0.2003  -0.6391 -0.6731 129  THR X O   
13564 C CB  . THR B 129  ? 2.2567 3.2150 2.5853 0.2168  -0.6935 -0.6808 129  THR X CB  
13565 O OG1 . THR B 129  ? 2.2814 3.2086 2.6346 0.2247  -0.7227 -0.6854 129  THR X OG1 
13566 C CG2 . THR B 129  ? 2.2277 3.2072 2.5626 0.1963  -0.6686 -0.6627 129  THR X CG2 
13567 N N   . SER B 130  ? 2.2929 3.2557 2.5802 0.2032  -0.6553 -0.6700 130  SER X N   
13568 C CA  . SER B 130  ? 2.3140 3.2893 2.5680 0.1970  -0.6248 -0.6641 130  SER X CA  
13569 C C   . SER B 130  ? 2.3289 3.3122 2.5884 0.1699  -0.5953 -0.6442 130  SER X C   
13570 O O   . SER B 130  ? 2.3155 3.2905 2.6081 0.1558  -0.5997 -0.6313 130  SER X O   
13571 C CB  . SER B 130  ? 2.3083 3.2679 2.5539 0.2054  -0.6295 -0.6633 130  SER X CB  
13572 O OG  . SER B 130  ? 2.2888 3.2486 2.5134 0.1921  -0.5980 -0.6483 130  SER X OG  
13573 N N   . GLU B 131  ? 2.3507 3.3495 2.5763 0.1617  -0.5646 -0.6423 131  GLU X N   
13574 C CA  . GLU B 131  ? 2.3315 3.3405 2.5560 0.1352  -0.5339 -0.6272 131  GLU X CA  
13575 C C   . GLU B 131  ? 2.3389 3.3397 2.5276 0.1270  -0.5037 -0.6205 131  GLU X C   
13576 O O   . GLU B 131  ? 2.3590 3.3735 2.5116 0.1271  -0.4848 -0.6286 131  GLU X O   
13577 C CB  . GLU B 131  ? 2.3118 3.3544 2.5292 0.1296  -0.5237 -0.6345 131  GLU X CB  
13578 C CG  . GLU B 131  ? 2.2873 3.3480 2.4841 0.1038  -0.4854 -0.6266 131  GLU X CG  
13579 C CD  . GLU B 131  ? 2.2654 3.3685 2.4487 0.1006  -0.4746 -0.6383 131  GLU X CD  
13580 O OE1 . GLU B 131  ? 2.2506 3.3712 2.4566 0.1077  -0.4918 -0.6420 131  GLU X OE1 
13581 O OE2 . GLU B 131  ? 2.2621 3.3817 2.4110 0.0908  -0.4480 -0.6438 131  GLU X OE2 
13582 N N   . THR B 132  ? 2.3212 3.2992 2.5181 0.1205  -0.4982 -0.6058 132  THR X N   
13583 C CA  . THR B 132  ? 2.3209 3.2840 2.4805 0.1154  -0.4691 -0.5982 132  THR X CA  
13584 C C   . THR B 132  ? 2.2790 3.2435 2.4316 0.0868  -0.4347 -0.5849 132  THR X C   
13585 O O   . THR B 132  ? 2.2521 3.2206 2.4370 0.0720  -0.4359 -0.5747 132  THR X O   
13586 C CB  . THR B 132  ? 2.3405 3.2782 2.5021 0.1306  -0.4804 -0.5914 132  THR X CB  
13587 O OG1 . THR B 132  ? 2.3672 3.2863 2.4885 0.1271  -0.4494 -0.5821 132  THR X OG1 
13588 C CG2 . THR B 132  ? 2.3155 3.2478 2.5228 0.1225  -0.4944 -0.5794 132  THR X CG2 
13589 N N   . ASN B 133  ? 2.2654 3.2263 2.3738 0.0785  -0.4035 -0.5858 133  ASN X N   
13590 C CA  . ASN B 133  ? 2.2071 3.1638 2.3005 0.0508  -0.3677 -0.5754 133  ASN X CA  
13591 C C   . ASN B 133  ? 2.1736 3.0912 2.2445 0.0532  -0.3508 -0.5615 133  ASN X C   
13592 O O   . ASN B 133  ? 2.2328 3.1314 2.2587 0.0587  -0.3321 -0.5627 133  ASN X O   
13593 C CB  . ASN B 133  ? 2.1999 3.1760 2.2562 0.0372  -0.3417 -0.5864 133  ASN X CB  
13594 C CG  . ASN B 133  ? 2.1597 3.1443 2.2102 0.0043  -0.3095 -0.5808 133  ASN X CG  
13595 O OD1 . ASN B 133  ? 2.1212 3.1226 2.2061 -0.0076 -0.3153 -0.5760 133  ASN X OD1 
13596 N ND2 . ASN B 133  ? 2.1726 3.1446 2.1776 -0.0112 -0.2747 -0.5817 133  ASN X ND2 
13597 N N   . THR B 134  ? 2.0777 2.9836 2.1785 0.0503  -0.3569 -0.5478 134  THR X N   
13598 C CA  . THR B 134  ? 2.0151 2.8870 2.0999 0.0594  -0.3468 -0.5345 134  THR X CA  
13599 C C   . THR B 134  ? 1.9677 2.8175 2.0260 0.0379  -0.3076 -0.5225 134  THR X C   
13600 O O   . THR B 134  ? 1.9194 2.7814 1.9980 0.0148  -0.2973 -0.5179 134  THR X O   
13601 C CB  . THR B 134  ? 2.2823 3.1542 2.4129 0.0717  -0.3758 -0.5265 134  THR X CB  
13602 O OG1 . THR B 134  ? 2.3034 3.1479 2.4184 0.0782  -0.3614 -0.5125 134  THR X OG1 
13603 C CG2 . THR B 134  ? 2.2383 3.1306 2.4148 0.0521  -0.3831 -0.5216 134  THR X CG2 
13604 N N   . PRO B 135  ? 1.9680 2.7828 1.9788 0.0467  -0.2855 -0.5172 135  PRO X N   
13605 C CA  . PRO B 135  ? 1.9799 2.7634 1.9641 0.0311  -0.2500 -0.5044 135  PRO X CA  
13606 C C   . PRO B 135  ? 1.9344 2.7211 1.9611 0.0279  -0.2591 -0.4918 135  PRO X C   
13607 O O   . PRO B 135  ? 1.9135 2.7222 1.9861 0.0401  -0.2928 -0.4921 135  PRO X O   
13608 C CB  . PRO B 135  ? 2.0271 2.7703 1.9616 0.0543  -0.2379 -0.4988 135  PRO X CB  
13609 C CG  . PRO B 135  ? 2.0206 2.7806 1.9680 0.0841  -0.2739 -0.5075 135  PRO X CG  
13610 C CD  . PRO B 135  ? 1.9940 2.7942 1.9690 0.0719  -0.2904 -0.5227 135  PRO X CD  
13611 N N   . LEU B 136  ? 1.9199 2.6846 1.9309 0.0109  -0.2289 -0.4815 136  LEU X N   
13612 C CA  . LEU B 136  ? 1.8626 2.6374 1.9143 0.0016  -0.2332 -0.4709 136  LEU X CA  
13613 C C   . LEU B 136  ? 1.8956 2.6478 1.9203 -0.0229 -0.1939 -0.4645 136  LEU X C   
13614 O O   . LEU B 136  ? 1.8893 2.6554 1.9071 -0.0503 -0.1766 -0.4723 136  LEU X O   
13615 C CB  . LEU B 136  ? 1.7870 2.6065 1.8904 -0.0107 -0.2579 -0.4773 136  LEU X CB  
13616 C CG  . LEU B 136  ? 1.7248 2.5583 1.8552 -0.0353 -0.2470 -0.4696 136  LEU X CG  
13617 C CD1 . LEU B 136  ? 1.7107 2.5356 1.8674 -0.0248 -0.2551 -0.4545 136  LEU X CD1 
13618 C CD2 . LEU B 136  ? 1.6774 2.5528 1.8467 -0.0478 -0.2662 -0.4768 136  LEU X CD2 
13619 N N   . PHE B 137  ? 1.9365 2.6556 1.9454 -0.0126 -0.1797 -0.4513 137  PHE X N   
13620 C CA  . PHE B 137  ? 1.9820 2.6712 1.9582 -0.0338 -0.1403 -0.4461 137  PHE X CA  
13621 C C   . PHE B 137  ? 1.9604 2.6666 1.9765 -0.0460 -0.1413 -0.4373 137  PHE X C   
13622 O O   . PHE B 137  ? 1.9120 2.6484 1.9790 -0.0356 -0.1717 -0.4326 137  PHE X O   
13623 C CB  . PHE B 137  ? 2.0600 2.6926 1.9798 -0.0154 -0.1159 -0.4375 137  PHE X CB  
13624 C CG  . PHE B 137  ? 2.1227 2.7389 2.0057 0.0039  -0.1194 -0.4430 137  PHE X CG  
13625 C CD1 . PHE B 137  ? 2.0929 2.7447 1.9930 0.0024  -0.1417 -0.4565 137  PHE X CD1 
13626 C CD2 . PHE B 137  ? 2.1804 2.7447 2.0089 0.0247  -0.0995 -0.4345 137  PHE X CD2 
13627 C CE1 . PHE B 137  ? 2.1259 2.7650 1.9919 0.0204  -0.1447 -0.4619 137  PHE X CE1 
13628 C CE2 . PHE B 137  ? 2.2197 2.7695 2.0124 0.0428  -0.1019 -0.4387 137  PHE X CE2 
13629 C CZ  . PHE B 137  ? 2.1844 2.7731 1.9966 0.0400  -0.1246 -0.4528 137  PHE X CZ  
13630 N N   . VAL B 138  ? 1.9676 2.6539 1.9592 -0.0694 -0.1073 -0.4356 138  VAL X N   
13631 C CA  . VAL B 138  ? 1.9199 2.6214 1.9440 -0.0819 -0.1045 -0.4276 138  VAL X CA  
13632 C C   . VAL B 138  ? 1.9915 2.6488 1.9705 -0.0949 -0.0633 -0.4236 138  VAL X C   
13633 O O   . VAL B 138  ? 2.0272 2.6720 1.9725 -0.1218 -0.0351 -0.4333 138  VAL X O   
13634 C CB  . VAL B 138  ? 1.8435 2.5964 1.9093 -0.1071 -0.1167 -0.4352 138  VAL X CB  
13635 C CG1 . VAL B 138  ? 1.8348 2.5900 1.8999 -0.1343 -0.0910 -0.4332 138  VAL X CG1 
13636 C CG2 . VAL B 138  ? 1.7659 2.5569 1.8916 -0.0921 -0.1576 -0.4302 138  VAL X CG2 
13637 N N   . ASN B 139  ? 1.9958 2.6295 1.9732 -0.0747 -0.0600 -0.4100 139  ASN X N   
13638 C CA  . ASN B 139  ? 2.0345 2.6224 1.9705 -0.0818 -0.0226 -0.4048 139  ASN X CA  
13639 C C   . ASN B 139  ? 2.0086 2.6215 1.9840 -0.0911 -0.0237 -0.3974 139  ASN X C   
13640 O O   . ASN B 139  ? 1.9791 2.6175 1.9971 -0.0711 -0.0490 -0.3872 139  ASN X O   
13641 C CB  . ASN B 139  ? 2.0632 2.6004 1.9585 -0.0468 -0.0145 -0.3943 139  ASN X CB  
13642 C CG  . ASN B 139  ? 2.0853 2.6179 1.9654 -0.0251 -0.0316 -0.3976 139  ASN X CG  
13643 O OD1 . ASN B 139  ? 2.0674 2.6233 1.9784 0.0030  -0.0635 -0.3926 139  ASN X OD1 
13644 N ND2 . ASN B 139  ? 2.1230 2.6280 1.9557 -0.0394 -0.0105 -0.4071 139  ASN X ND2 
13645 N N   . LYS B 140  ? 2.0363 2.6454 1.9986 -0.1224 0.0033  -0.4031 140  LYS X N   
13646 C CA  . LYS B 140  ? 2.0174 2.6462 2.0104 -0.1300 0.0059  -0.3957 140  LYS X CA  
13647 C C   . LYS B 140  ? 2.0562 2.6304 2.0071 -0.1171 0.0354  -0.3874 140  LYS X C   
13648 O O   . LYS B 140  ? 2.0959 2.6187 1.9888 -0.1284 0.0697  -0.3934 140  LYS X O   
13649 C CB  . LYS B 140  ? 2.0084 2.6703 2.0149 -0.1687 0.0162  -0.4064 140  LYS X CB  
13650 C CG  . LYS B 140  ? 1.9563 2.6718 2.0011 -0.1787 -0.0121 -0.4146 140  LYS X CG  
13651 C CD  . LYS B 140  ? 1.9099 2.6728 1.9855 -0.2080 -0.0115 -0.4196 140  LYS X CD  
13652 C CE  . LYS B 140  ? 1.8573 2.6580 1.9907 -0.1982 -0.0369 -0.4057 140  LYS X CE  
13653 N NZ  . LYS B 140  ? 1.8230 2.6726 1.9861 -0.2236 -0.0398 -0.4097 140  LYS X NZ  
13654 N N   . VAL B 141  ? 2.0561 2.6405 2.0349 -0.0924 0.0221  -0.3736 141  VAL X N   
13655 C CA  . VAL B 141  ? 2.1350 2.6738 2.0786 -0.0770 0.0484  -0.3650 141  VAL X CA  
13656 C C   . VAL B 141  ? 2.1721 2.7219 2.1248 -0.1036 0.0681  -0.3668 141  VAL X C   
13657 O O   . VAL B 141  ? 2.1084 2.7142 2.1128 -0.1211 0.0506  -0.3675 141  VAL X O   
13658 C CB  . VAL B 141  ? 2.1457 2.6969 2.1157 -0.0367 0.0261  -0.3498 141  VAL X CB  
13659 C CG1 . VAL B 141  ? 2.2108 2.7019 2.1271 -0.0113 0.0547  -0.3416 141  VAL X CG1 
13660 C CG2 . VAL B 141  ? 2.1229 2.6933 2.1114 -0.0148 -0.0069 -0.3494 141  VAL X CG2 
13661 N N   . ASN B 142  ? 2.2599 2.7538 2.1595 -0.1058 0.1051  -0.3675 142  ASN X N   
13662 C CA  . ASN B 142  ? 2.2757 2.7739 2.1784 -0.1251 0.1256  -0.3687 142  ASN X CA  
13663 C C   . ASN B 142  ? 2.3557 2.7901 2.2079 -0.1012 0.1539  -0.3614 142  ASN X C   
13664 O O   . ASN B 142  ? 2.4180 2.8010 2.2184 -0.1184 0.1907  -0.3693 142  ASN X O   
13665 C CB  . ASN B 142  ? 2.2735 2.7715 2.1569 -0.1698 0.1477  -0.3862 142  ASN X CB  
13666 C CG  . ASN B 142  ? 2.2401 2.7598 2.1388 -0.1917 0.1618  -0.3887 142  ASN X CG  
13667 O OD1 . ASN B 142  ? 2.2807 2.7530 2.1370 -0.1948 0.1944  -0.3908 142  ASN X OD1 
13668 N ND2 . ASN B 142  ? 2.1662 2.7561 2.1237 -0.2064 0.1379  -0.3884 142  ASN X ND2 
13669 N N   . GLY B 143  ? 2.3556 2.7938 2.2224 -0.0605 0.1360  -0.3468 143  GLY X N   
13670 C CA  . GLY B 143  ? 2.4365 2.8155 2.2546 -0.0279 0.1584  -0.3378 143  GLY X CA  
13671 C C   . GLY B 143  ? 2.5312 2.8359 2.2776 -0.0208 0.1809  -0.3416 143  GLY X C   
13672 O O   . GLY B 143  ? 2.5407 2.8428 2.2834 0.0040  0.1628  -0.3367 143  GLY X O   
13673 N N   . GLU B 144  ? 2.6119 2.8557 2.3000 -0.0437 0.2210  -0.3508 144  GLU X N   
13674 C CA  . GLU B 144  ? 2.6979 2.8643 2.3123 -0.0421 0.2476  -0.3544 144  GLU X CA  
13675 C C   . GLU B 144  ? 2.6482 2.8313 2.2643 -0.0800 0.2448  -0.3694 144  GLU X C   
13676 O O   . GLU B 144  ? 2.6835 2.8176 2.2490 -0.0804 0.2594  -0.3725 144  GLU X O   
13677 C CB  . GLU B 144  ? 2.8186 2.9041 2.3644 -0.0491 0.2943  -0.3576 144  GLU X CB  
13678 C CG  . GLU B 144  ? 2.8889 2.9385 2.4127 -0.0012 0.3015  -0.3415 144  GLU X CG  
13679 C CD  . GLU B 144  ? 2.9255 2.9624 2.4370 0.0468  0.2833  -0.3271 144  GLU X CD  
13680 O OE1 . GLU B 144  ? 2.9494 2.9690 2.4387 0.0413  0.2808  -0.3306 144  GLU X OE1 
13681 O OE2 . GLU B 144  ? 2.9252 2.9732 2.4493 0.0902  0.2713  -0.3130 144  GLU X OE2 
13682 N N   . ASP B 145  ? 2.5555 2.8098 2.2295 -0.1106 0.2263  -0.3781 145  ASP X N   
13683 C CA  . ASP B 145  ? 2.5009 2.7824 2.1822 -0.1477 0.2231  -0.3937 145  ASP X CA  
13684 C C   . ASP B 145  ? 2.3882 2.7211 2.1132 -0.1324 0.1823  -0.3906 145  ASP X C   
13685 O O   . ASP B 145  ? 2.3318 2.7037 2.1040 -0.1036 0.1503  -0.3787 145  ASP X O   
13686 C CB  . ASP B 145  ? 2.4814 2.8110 2.1956 -0.1889 0.2271  -0.4060 145  ASP X CB  
13687 C CG  . ASP B 145  ? 2.5598 2.8346 2.2201 -0.2158 0.2723  -0.4164 145  ASP X CG  
13688 O OD1 . ASP B 145  ? 2.6452 2.8390 2.2392 -0.2057 0.3024  -0.4148 145  ASP X OD1 
13689 O OD2 . ASP B 145  ? 2.5309 2.8426 2.2137 -0.2472 0.2780  -0.4266 145  ASP X OD2 
13690 N N   . LEU B 146  ? 2.3469 2.6792 2.0544 -0.1524 0.1845  -0.4024 146  LEU X N   
13691 C CA  . LEU B 146  ? 2.2526 2.6327 1.9975 -0.1422 0.1481  -0.4031 146  LEU X CA  
13692 C C   . LEU B 146  ? 2.2164 2.6208 1.9583 -0.1794 0.1525  -0.4208 146  LEU X C   
13693 O O   . LEU B 146  ? 2.2343 2.5937 1.9209 -0.1933 0.1792  -0.4290 146  LEU X O   
13694 C CB  . LEU B 146  ? 2.2793 2.6192 1.9915 -0.1041 0.1424  -0.3936 146  LEU X CB  
13695 C CG  . LEU B 146  ? 2.2185 2.6073 1.9730 -0.0841 0.1004  -0.3922 146  LEU X CG  
13696 C CD1 . LEU B 146  ? 2.2612 2.6092 1.9647 -0.0721 0.1084  -0.3943 146  LEU X CD1 
13697 C CD2 . LEU B 146  ? 2.1463 2.6061 1.9569 -0.1113 0.0765  -0.4034 146  LEU X CD2 
13698 N N   . ASP B 147  ? 2.1654 2.6419 1.9664 -0.1944 0.1261  -0.4263 147  ASP X N   
13699 C CA  . ASP B 147  ? 2.1358 2.6502 1.9443 -0.2225 0.1218  -0.4424 147  ASP X CA  
13700 C C   . ASP B 147  ? 2.1550 2.7046 1.9964 -0.1989 0.0833  -0.4399 147  ASP X C   
13701 O O   . ASP B 147  ? 2.1104 2.7131 2.0104 -0.1898 0.0497  -0.4355 147  ASP X O   
13702 C CB  . ASP B 147  ? 2.0117 2.5821 1.8582 -0.2545 0.1203  -0.4512 147  ASP X CB  
13703 C CG  . ASP B 147  ? 1.9691 2.5068 1.7781 -0.2838 0.1606  -0.4587 147  ASP X CG  
13704 O OD1 . ASP B 147  ? 2.0010 2.4761 1.7484 -0.2924 0.1940  -0.4638 147  ASP X OD1 
13705 O OD2 . ASP B 147  ? 1.9112 2.4845 1.7511 -0.2985 0.1595  -0.4596 147  ASP X OD2 
13706 N N   . ALA B 148  ? 2.2198 2.7358 2.0203 -0.1890 0.0898  -0.4427 148  ALA X N   
13707 C CA  . ALA B 148  ? 2.2218 2.7620 2.0436 -0.1637 0.0562  -0.4413 148  ALA X CA  
13708 C C   . ALA B 148  ? 2.2329 2.8085 2.0560 -0.1852 0.0517  -0.4578 148  ALA X C   
13709 O O   . ALA B 148  ? 2.2916 2.8615 2.0845 -0.2185 0.0804  -0.4705 148  ALA X O   
13710 C CB  . ALA B 148  ? 2.2721 2.7552 2.0496 -0.1303 0.0620  -0.4313 148  ALA X CB  
13711 N N   . SER B 149  ? 2.1739 2.7867 2.0312 -0.1654 0.0157  -0.4585 149  SER X N   
13712 C CA  . SER B 149  ? 2.1307 2.7845 1.9957 -0.1794 0.0057  -0.4737 149  SER X CA  
13713 C C   . SER B 149  ? 2.0349 2.6988 1.9137 -0.1461 -0.0276 -0.4718 149  SER X C   
13714 O O   . SER B 149  ? 1.9852 2.6619 1.9031 -0.1207 -0.0576 -0.4620 149  SER X O   
13715 C CB  . SER B 149  ? 2.1151 2.8321 2.0321 -0.1994 -0.0100 -0.4800 149  SER X CB  
13716 O OG  . SER B 149  ? 2.1429 2.8543 2.0592 -0.2221 0.0128  -0.4779 149  SER X OG  
13717 N N   . ILE B 150  ? 1.9953 2.6541 1.8416 -0.1469 -0.0218 -0.4818 150  ILE X N   
13718 C CA  . ILE B 150  ? 1.8675 2.5442 1.7284 -0.1181 -0.0545 -0.4837 150  ILE X CA  
13719 C C   . ILE B 150  ? 1.7886 2.5303 1.6969 -0.1282 -0.0804 -0.4954 150  ILE X C   
13720 O O   . ILE B 150  ? 1.7890 2.5574 1.6967 -0.1588 -0.0645 -0.5060 150  ILE X O   
13721 C CB  . ILE B 150  ? 1.7039 2.3497 1.5085 -0.1131 -0.0373 -0.4893 150  ILE X CB  
13722 C CG1 . ILE B 150  ? 1.6298 2.3212 1.4384 -0.1316 -0.0406 -0.5072 150  ILE X CG1 
13723 C CG2 . ILE B 150  ? 1.8284 2.4127 1.5715 -0.1283 0.0079  -0.4847 150  ILE X CG2 
13724 C CD1 . ILE B 150  ? 1.4474 2.1815 1.2955 -0.1068 -0.0829 -0.5125 150  ILE X CD1 
13725 N N   . ASP B 151  ? 1.7285 2.4963 1.6763 -0.1026 -0.1196 -0.4945 151  ASP X N   
13726 C CA  . ASP B 151  ? 1.6773 2.5015 1.6695 -0.1094 -0.1444 -0.5040 151  ASP X CA  
13727 C C   . ASP B 151  ? 1.7380 2.5799 1.7497 -0.0812 -0.1807 -0.5092 151  ASP X C   
13728 O O   . ASP B 151  ? 1.7525 2.5736 1.7318 -0.0647 -0.1798 -0.5125 151  ASP X O   
13729 C CB  . ASP B 151  ? 1.5780 2.4240 1.6177 -0.1178 -0.1552 -0.4953 151  ASP X CB  
13730 C CG  . ASP B 151  ? 1.4760 2.3739 1.5416 -0.1395 -0.1593 -0.5052 151  ASP X CG  
13731 O OD1 . ASP B 151  ? 1.4660 2.3880 1.5178 -0.1452 -0.1580 -0.5197 151  ASP X OD1 
13732 O OD2 . ASP B 151  ? 1.4131 2.3299 1.5122 -0.1496 -0.1636 -0.4983 151  ASP X OD2 
13733 N N   . SER B 152  ? 1.8112 2.6898 1.8738 -0.0761 -0.2120 -0.5101 152  SER X N   
13734 C CA  . SER B 152  ? 1.9160 2.8132 1.9994 -0.0520 -0.2474 -0.5177 152  SER X CA  
13735 C C   . SER B 152  ? 2.0180 2.9397 2.1587 -0.0455 -0.2805 -0.5132 152  SER X C   
13736 O O   . SER B 152  ? 1.9936 2.9328 2.1589 -0.0635 -0.2760 -0.5077 152  SER X O   
13737 C CB  . SER B 152  ? 1.9216 2.8478 1.9872 -0.0583 -0.2442 -0.5351 152  SER X CB  
13738 O OG  . SER B 152  ? 1.9570 2.8595 1.9692 -0.0612 -0.2175 -0.5399 152  SER X OG  
13739 N N   . PHE B 153  ? 2.1477 3.0692 2.3072 -0.0201 -0.3131 -0.5160 153  PHE X N   
13740 C CA  . PHE B 153  ? 2.2554 3.1968 2.4658 -0.0130 -0.3467 -0.5145 153  PHE X CA  
13741 C C   . PHE B 153  ? 2.3160 3.2716 2.5316 0.0063  -0.3750 -0.5295 153  PHE X C   
13742 O O   . PHE B 153  ? 2.3327 3.2763 2.5215 0.0235  -0.3783 -0.5376 153  PHE X O   
13743 C CB  . PHE B 153  ? 2.3412 3.2650 2.5789 -0.0025 -0.3616 -0.5012 153  PHE X CB  
13744 C CG  . PHE B 153  ? 2.4050 3.3453 2.6943 0.0009  -0.3941 -0.4991 153  PHE X CG  
13745 C CD1 . PHE B 153  ? 2.4115 3.3607 2.7330 -0.0152 -0.3920 -0.4862 153  PHE X CD1 
13746 C CD2 . PHE B 153  ? 2.4463 3.3910 2.7496 0.0197  -0.4259 -0.5102 153  PHE X CD2 
13747 C CE1 . PHE B 153  ? 2.4186 3.3790 2.7847 -0.0136 -0.4200 -0.4830 153  PHE X CE1 
13748 C CE2 . PHE B 153  ? 2.4514 3.4048 2.7987 0.0212  -0.4543 -0.5084 153  PHE X CE2 
13749 C CZ  . PHE B 153  ? 2.4346 3.3949 2.8130 0.0041  -0.4509 -0.4942 153  PHE X CZ  
13750 N N   . LEU B 154  ? 2.3269 3.3069 2.5753 0.0047  -0.3949 -0.5329 154  LEU X N   
13751 C CA  . LEU B 154  ? 2.3479 3.3405 2.6014 0.0233  -0.4214 -0.5478 154  LEU X CA  
13752 C C   . LEU B 154  ? 2.3651 3.3478 2.6572 0.0391  -0.4575 -0.5461 154  LEU X C   
13753 O O   . LEU B 154  ? 2.3358 3.3255 2.6631 0.0322  -0.4702 -0.5392 154  LEU X O   
13754 C CB  . LEU B 154  ? 2.3186 3.3458 2.5737 0.0136  -0.4170 -0.5556 154  LEU X CB  
13755 C CG  . LEU B 154  ? 2.2960 3.3375 2.5135 -0.0057 -0.3805 -0.5597 154  LEU X CG  
13756 C CD1 . LEU B 154  ? 2.2639 3.3451 2.4909 -0.0215 -0.3726 -0.5630 154  LEU X CD1 
13757 C CD2 . LEU B 154  ? 2.3158 3.3555 2.4943 0.0064  -0.3750 -0.5740 154  LEU X CD2 
13758 N N   . ILE B 155  ? 2.4106 3.3767 2.6944 0.0594  -0.4733 -0.5525 155  ILE X N   
13759 C CA  . ILE B 155  ? 2.4459 3.4035 2.7625 0.0742  -0.5086 -0.5555 155  ILE X CA  
13760 C C   . ILE B 155  ? 2.4939 3.4615 2.8117 0.0890  -0.5312 -0.5727 155  ILE X C   
13761 O O   . ILE B 155  ? 2.5066 3.4778 2.7938 0.1034  -0.5308 -0.5867 155  ILE X O   
13762 C CB  . ILE B 155  ? 2.4271 3.3670 2.7336 0.0909  -0.5166 -0.5567 155  ILE X CB  
13763 C CG1 . ILE B 155  ? 2.4144 3.3430 2.7007 0.0818  -0.4868 -0.5423 155  ILE X CG1 
13764 C CG2 . ILE B 155  ? 2.4320 3.3658 2.7796 0.0982  -0.5494 -0.5569 155  ILE X CG2 
13765 C CD1 . ILE B 155  ? 2.4239 3.3372 2.6979 0.1009  -0.4932 -0.5416 155  ILE X CD1 
13766 N N   . GLN B 156  ? 2.5462 3.5166 2.8978 0.0863  -0.5504 -0.5713 156  GLN X N   
13767 C CA  . GLN B 156  ? 2.6251 3.6035 2.9770 0.1006  -0.5697 -0.5863 156  GLN X CA  
13768 C C   . GLN B 156  ? 2.6868 3.6459 3.0536 0.1202  -0.6046 -0.5983 156  GLN X C   
13769 O O   . GLN B 156  ? 2.6959 3.6530 3.0721 0.1310  -0.6249 -0.6081 156  GLN X O   
13770 C CB  . GLN B 156  ? 2.6319 3.6229 3.0049 0.0889  -0.5687 -0.5783 156  GLN X CB  
13771 C CG  . GLN B 156  ? 2.6584 3.6610 3.0259 0.1055  -0.5839 -0.5928 156  GLN X CG  
13772 C CD  . GLN B 156  ? 2.6744 3.6928 3.0043 0.1205  -0.5776 -0.6108 156  GLN X CD  
13773 O OE1 . GLN B 156  ? 2.6633 3.7012 2.9671 0.1099  -0.5497 -0.6101 156  GLN X OE1 
13774 N NE2 . GLN B 156  ? 2.6928 3.7022 3.0187 0.1443  -0.6028 -0.6275 156  GLN X NE2 
13775 N N   . LYS B 157  ? 2.7543 3.6997 3.1218 0.1258  -0.6114 -0.5985 157  LYS X N   
13776 C CA  . LYS B 157  ? 2.8195 3.7492 3.2030 0.1417  -0.6447 -0.6113 157  LYS X CA  
13777 C C   . LYS B 157  ? 2.8684 3.7944 3.2319 0.1572  -0.6489 -0.6195 157  LYS X C   
13778 O O   . LYS B 157  ? 2.8730 3.8043 3.2078 0.1566  -0.6248 -0.6135 157  LYS X O   
13779 C CB  . LYS B 157  ? 2.8229 3.7390 3.2515 0.1283  -0.6612 -0.6009 157  LYS X CB  
13780 C CG  . LYS B 157  ? 2.8231 3.7373 3.2715 0.1182  -0.6640 -0.5944 157  LYS X CG  
13781 C CD  . LYS B 157  ? 2.8493 3.7559 3.2898 0.1373  -0.6852 -0.6128 157  LYS X CD  
13782 C CE  . LYS B 157  ? 2.8474 3.7531 3.3008 0.1312  -0.6851 -0.6050 157  LYS X CE  
13783 N NZ  . LYS B 157  ? 2.8738 3.7711 3.3159 0.1533  -0.7046 -0.6228 157  LYS X NZ  
13784 N N   . GLU B 158  ? 2.9107 3.8264 3.2874 0.1714  -0.6795 -0.6337 158  GLU X N   
13785 C CA  . GLU B 158  ? 2.9518 3.8671 3.3123 0.1889  -0.6886 -0.6434 158  GLU X CA  
13786 C C   . GLU B 158  ? 2.9298 3.8434 3.3164 0.1803  -0.6922 -0.6315 158  GLU X C   
13787 O O   . GLU B 158  ? 2.9395 3.8578 3.3068 0.1877  -0.6805 -0.6265 158  GLU X O   
13788 C CB  . GLU B 158  ? 3.0256 3.9345 3.3865 0.2089  -0.7207 -0.6675 158  GLU X CB  
13789 C CG  . GLU B 158  ? 3.0874 3.9977 3.4409 0.2263  -0.7374 -0.6791 158  GLU X CG  
13790 C CD  . GLU B 158  ? 3.1365 4.0568 3.4434 0.2418  -0.7172 -0.6793 158  GLU X CD  
13791 O OE1 . GLU B 158  ? 3.1420 4.0675 3.4214 0.2380  -0.6911 -0.6733 158  GLU X OE1 
13792 O OE2 . GLU B 158  ? 3.1658 4.0896 3.4628 0.2574  -0.7272 -0.6854 158  GLU X OE2 
13793 N N   . GLU B 159  ? 2.8880 3.7953 3.3175 0.1652  -0.7078 -0.6267 159  GLU X N   
13794 C CA  . GLU B 159  ? 2.8375 3.7487 3.2976 0.1529  -0.7096 -0.6139 159  GLU X CA  
13795 C C   . GLU B 159  ? 2.7649 3.6750 3.2499 0.1278  -0.6942 -0.5938 159  GLU X C   
13796 O O   . GLU B 159  ? 2.7590 3.6605 3.2554 0.1198  -0.6992 -0.5943 159  GLU X O   
13797 C CB  . GLU B 159  ? 2.8606 3.7682 3.3526 0.1554  -0.7442 -0.6279 159  GLU X CB  
13798 C CG  . GLU B 159  ? 2.8452 3.7626 3.3757 0.1393  -0.7477 -0.6153 159  GLU X CG  
13799 C CD  . GLU B 159  ? 2.8569 3.7723 3.4217 0.1365  -0.7817 -0.6306 159  GLU X CD  
13800 O OE1 . GLU B 159  ? 2.8495 3.7677 3.4543 0.1154  -0.7870 -0.6211 159  GLU X OE1 
13801 O OE2 . GLU B 159  ? 2.8769 3.7884 3.4285 0.1541  -0.8026 -0.6530 159  GLU X OE2 
13802 N N   . ILE B 160  ? 2.6876 3.6064 3.1792 0.1170  -0.6754 -0.5760 160  ILE X N   
13803 C CA  . ILE B 160  ? 2.6044 3.5249 3.1140 0.0941  -0.6569 -0.5566 160  ILE X CA  
13804 C C   . ILE B 160  ? 2.5862 3.5152 3.1300 0.0803  -0.6564 -0.5417 160  ILE X C   
13805 O O   . ILE B 160  ? 2.5858 3.5239 3.1228 0.0888  -0.6513 -0.5389 160  ILE X O   
13806 C CB  . ILE B 160  ? 2.4944 3.4186 2.9671 0.0915  -0.6228 -0.5482 160  ILE X CB  
13807 C CG1 . ILE B 160  ? 2.4277 3.3563 2.9187 0.0679  -0.6044 -0.5297 160  ILE X CG1 
13808 C CG2 . ILE B 160  ? 2.4879 3.4139 2.9293 0.1028  -0.6049 -0.5452 160  ILE X CG2 
13809 C CD1 . ILE B 160  ? 2.4013 3.3355 2.8584 0.0621  -0.5729 -0.5249 160  ILE X CD1 
13810 N N   . SER B 161  ? 2.5759 3.5026 3.1555 0.0604  -0.6618 -0.5322 161  SER X N   
13811 C CA  . SER B 161  ? 2.5621 3.4994 3.1794 0.0443  -0.6629 -0.5182 161  SER X CA  
13812 C C   . SER B 161  ? 2.5444 3.4934 3.1512 0.0371  -0.6311 -0.4992 161  SER X C   
13813 O O   . SER B 161  ? 2.5400 3.4858 3.1271 0.0306  -0.6086 -0.4915 161  SER X O   
13814 C CB  . SER B 161  ? 2.5492 3.4774 3.2031 0.0242  -0.6750 -0.5121 161  SER X CB  
13815 O OG  . SER B 161  ? 2.5327 3.4536 3.1732 0.0178  -0.6593 -0.5043 161  SER X OG  
13816 N N   . LEU B 162  ? 2.5500 3.5138 3.1699 0.0386  -0.6295 -0.4927 162  LEU X N   
13817 C CA  . LEU B 162  ? 2.5345 3.5068 3.1436 0.0343  -0.5999 -0.4753 162  LEU X CA  
13818 C C   . LEU B 162  ? 2.5077 3.4829 3.1388 0.0096  -0.5854 -0.4581 162  LEU X C   
13819 O O   . LEU B 162  ? 2.4823 3.4592 3.0962 0.0040  -0.5571 -0.4457 162  LEU X O   
13820 C CB  . LEU B 162  ? 2.5448 3.5359 3.1674 0.0435  -0.6044 -0.4722 162  LEU X CB  
13821 C CG  . LEU B 162  ? 2.5453 3.5422 3.1494 0.0469  -0.5745 -0.4565 162  LEU X CG  
13822 C CD1 . LEU B 162  ? 2.5543 3.5303 3.1024 0.0598  -0.5501 -0.4584 162  LEU X CD1 
13823 C CD2 . LEU B 162  ? 2.5545 3.5737 3.1721 0.0613  -0.5835 -0.4558 162  LEU X CD2 
13824 N N   . LYS B 163  ? 2.5045 3.4786 3.1716 -0.0051 -0.6042 -0.4575 163  LYS X N   
13825 C CA  . LYS B 163  ? 2.4852 3.4604 3.1699 -0.0267 -0.5918 -0.4413 163  LYS X CA  
13826 C C   . LYS B 163  ? 2.4955 3.4613 3.1463 -0.0254 -0.5746 -0.4426 163  LYS X C   
13827 O O   . LYS B 163  ? 2.5063 3.4787 3.1441 -0.0342 -0.5481 -0.4308 163  LYS X O   
13828 C CB  . LYS B 163  ? 2.4722 3.4407 3.1955 -0.0404 -0.6161 -0.4414 163  LYS X CB  
13829 C CG  . LYS B 163  ? 2.4378 3.4016 3.1702 -0.0580 -0.6054 -0.4267 163  LYS X CG  
13830 C CD  . LYS B 163  ? 2.4342 3.3768 3.1844 -0.0626 -0.6295 -0.4323 163  LYS X CD  
13831 C CE  . LYS B 163  ? 2.4077 3.3467 3.1691 -0.0791 -0.6196 -0.4147 163  LYS X CE  
13832 N NZ  . LYS B 163  ? 2.3869 3.3433 3.1796 -0.0993 -0.6094 -0.3953 163  LYS X NZ  
13833 N N   . GLU B 164  ? 2.5053 3.4579 3.1417 -0.0143 -0.5900 -0.4583 164  GLU X N   
13834 C CA  . GLU B 164  ? 2.5103 3.4597 3.1151 -0.0113 -0.5763 -0.4624 164  GLU X CA  
13835 C C   . GLU B 164  ? 2.4252 3.3790 2.9895 -0.0043 -0.5497 -0.4638 164  GLU X C   
13836 O O   . GLU B 164  ? 2.3840 3.3432 2.9264 -0.0113 -0.5274 -0.4606 164  GLU X O   
13837 C CB  . GLU B 164  ? 2.6227 3.5591 3.2188 0.0034  -0.5995 -0.4809 164  GLU X CB  
13838 C CG  . GLU B 164  ? 2.7061 3.6458 3.2691 0.0090  -0.5864 -0.4873 164  GLU X CG  
13839 C CD  . GLU B 164  ? 2.7967 3.7264 3.3443 0.0287  -0.6072 -0.5079 164  GLU X CD  
13840 O OE1 . GLU B 164  ? 2.8385 3.7556 3.4010 0.0373  -0.6326 -0.5177 164  GLU X OE1 
13841 O OE2 . GLU B 164  ? 2.8191 3.7560 3.3396 0.0354  -0.5981 -0.5153 164  GLU X OE2 
13842 N N   . LEU B 165  ? 2.3922 3.3436 2.9450 0.0095  -0.5519 -0.4691 165  LEU X N   
13843 C CA  . LEU B 165  ? 2.3419 3.2906 2.8536 0.0171  -0.5259 -0.4689 165  LEU X CA  
13844 C C   . LEU B 165  ? 2.3328 3.2872 2.8456 0.0006  -0.4976 -0.4511 165  LEU X C   
13845 O O   . LEU B 165  ? 2.3301 3.2812 2.8100 -0.0044 -0.4701 -0.4493 165  LEU X O   
13846 C CB  . LEU B 165  ? 2.2947 3.2398 2.7969 0.0374  -0.5358 -0.4753 165  LEU X CB  
13847 C CG  . LEU B 165  ? 2.2412 3.1751 2.6920 0.0538  -0.5175 -0.4812 165  LEU X CG  
13848 C CD1 . LEU B 165  ? 2.2284 3.1573 2.6566 0.0659  -0.5292 -0.4993 165  LEU X CD1 
13849 C CD2 . LEU B 165  ? 2.2220 3.1554 2.6672 0.0723  -0.5214 -0.4798 165  LEU X CD2 
13850 N N   . ASP B 166  ? 2.3200 3.2839 2.8710 -0.0089 -0.5043 -0.4390 166  ASP X N   
13851 C CA  . ASP B 166  ? 2.3221 3.2933 2.8773 -0.0226 -0.4795 -0.4222 166  ASP X CA  
13852 C C   . ASP B 166  ? 2.3257 3.3040 2.8872 -0.0431 -0.4665 -0.4144 166  ASP X C   
13853 O O   . ASP B 166  ? 2.3141 3.2954 2.8606 -0.0537 -0.4390 -0.4056 166  ASP X O   
13854 C CB  . ASP B 166  ? 2.3317 3.3161 2.9272 -0.0250 -0.4920 -0.4125 166  ASP X CB  
13855 C CG  . ASP B 166  ? 2.3560 3.3461 2.9446 -0.0275 -0.4663 -0.3987 166  ASP X CG  
13856 O OD1 . ASP B 166  ? 2.3810 3.3590 2.9305 -0.0268 -0.4389 -0.3977 166  ASP X OD1 
13857 O OD2 . ASP B 166  ? 2.3618 3.3685 2.9833 -0.0303 -0.4729 -0.3895 166  ASP X OD2 
13858 N N   . PHE B 167  ? 2.3595 3.3398 2.9414 -0.0475 -0.4864 -0.4179 167  PHE X N   
13859 C CA  . PHE B 167  ? 2.3900 3.3795 2.9782 -0.0635 -0.4775 -0.4105 167  PHE X CA  
13860 C C   . PHE B 167  ? 2.3495 3.3418 2.8971 -0.0642 -0.4556 -0.4184 167  PHE X C   
13861 O O   . PHE B 167  ? 2.3605 3.3651 2.9022 -0.0792 -0.4338 -0.4105 167  PHE X O   
13862 C CB  . PHE B 167  ? 2.4582 3.4440 3.0740 -0.0639 -0.5053 -0.4126 167  PHE X CB  
13863 C CG  . PHE B 167  ? 2.5026 3.4985 3.1283 -0.0780 -0.4984 -0.4019 167  PHE X CG  
13864 C CD1 . PHE B 167  ? 2.5225 3.5227 3.1269 -0.0736 -0.4963 -0.4102 167  PHE X CD1 
13865 C CD2 . PHE B 167  ? 2.5135 3.5177 3.1692 -0.0943 -0.4944 -0.3836 167  PHE X CD2 
13866 C CE1 . PHE B 167  ? 2.5277 3.5406 3.1396 -0.0838 -0.4906 -0.4001 167  PHE X CE1 
13867 C CE2 . PHE B 167  ? 2.5205 3.5347 3.1830 -0.1054 -0.4881 -0.3728 167  PHE X CE2 
13868 C CZ  . PHE B 167  ? 2.5243 3.5429 3.1645 -0.0994 -0.4866 -0.3811 167  PHE X CZ  
13869 N N   . LYS B 168  ? 2.2902 3.2740 2.8103 -0.0490 -0.4611 -0.4347 168  LYS X N   
13870 C CA  . LYS B 168  ? 2.2068 3.1960 2.6877 -0.0505 -0.4406 -0.4442 168  LYS X CA  
13871 C C   . LYS B 168  ? 2.1579 3.1390 2.6048 -0.0543 -0.4097 -0.4423 168  LYS X C   
13872 O O   . LYS B 168  ? 2.1367 3.1252 2.5574 -0.0666 -0.3843 -0.4445 168  LYS X O   
13873 C CB  . LYS B 168  ? 2.1977 3.1831 2.6621 -0.0330 -0.4581 -0.4624 168  LYS X CB  
13874 C CG  . LYS B 168  ? 2.1704 3.1611 2.6593 -0.0288 -0.4842 -0.4659 168  LYS X CG  
13875 C CD  . LYS B 168  ? 2.1638 3.1496 2.6357 -0.0087 -0.5023 -0.4851 168  LYS X CD  
13876 C CE  . LYS B 168  ? 2.1514 3.1395 2.6422 -0.0033 -0.5247 -0.4883 168  LYS X CE  
13877 N NZ  . LYS B 168  ? 2.1631 3.1493 2.6341 0.0171  -0.5398 -0.5079 168  LYS X NZ  
13878 N N   . ILE B 169  ? 2.1197 3.0855 2.5663 -0.0437 -0.4118 -0.4386 169  ILE X N   
13879 C CA  . ILE B 169  ? 2.0713 3.0225 2.4858 -0.0440 -0.3833 -0.4341 169  ILE X CA  
13880 C C   . ILE B 169  ? 2.0684 3.0265 2.4896 -0.0638 -0.3594 -0.4204 169  ILE X C   
13881 O O   . ILE B 169  ? 2.0935 3.0395 2.4810 -0.0704 -0.3294 -0.4192 169  ILE X O   
13882 C CB  . ILE B 169  ? 1.9900 2.9277 2.4074 -0.0246 -0.3938 -0.4313 169  ILE X CB  
13883 C CG1 . ILE B 169  ? 1.9570 2.8835 2.3507 -0.0034 -0.4078 -0.4459 169  ILE X CG1 
13884 C CG2 . ILE B 169  ? 1.9828 2.9058 2.3753 -0.0255 -0.3643 -0.4214 169  ILE X CG2 
13885 C CD1 . ILE B 169  ? 1.9374 2.8547 2.2843 -0.0052 -0.3870 -0.4560 169  ILE X CD1 
13886 N N   . ARG B 170  ? 2.0451 3.0204 2.5082 -0.0734 -0.3722 -0.4103 170  ARG X N   
13887 C CA  . ARG B 170  ? 2.0502 3.0365 2.5231 -0.0920 -0.3519 -0.3972 170  ARG X CA  
13888 C C   . ARG B 170  ? 2.0069 3.0138 2.4816 -0.1094 -0.3450 -0.3985 170  ARG X C   
13889 O O   . ARG B 170  ? 1.9931 3.0080 2.4558 -0.1255 -0.3196 -0.3941 170  ARG X O   
13890 C CB  . ARG B 170  ? 2.0946 3.0894 2.6109 -0.0924 -0.3662 -0.3829 170  ARG X CB  
13891 C CG  . ARG B 170  ? 2.1756 3.1587 2.6927 -0.0745 -0.3728 -0.3816 170  ARG X CG  
13892 C CD  . ARG B 170  ? 2.2318 3.2284 2.7812 -0.0800 -0.3708 -0.3657 170  ARG X CD  
13893 N NE  . ARG B 170  ? 2.2843 3.2840 2.8550 -0.0641 -0.3909 -0.3649 170  ARG X NE  
13894 C CZ  . ARG B 170  ? 2.3017 3.3181 2.9023 -0.0656 -0.3923 -0.3529 170  ARG X CZ  
13895 N NH1 . ARG B 170  ? 2.3043 3.3326 2.9156 -0.0818 -0.3742 -0.3400 170  ARG X NH1 
13896 N NH2 . ARG B 170  ? 2.3027 3.3275 2.9225 -0.0509 -0.4117 -0.3545 170  ARG X NH2 
13897 N N   . GLN B 171  ? 1.9946 3.0109 2.4827 -0.1048 -0.3677 -0.4051 171  GLN X N   
13898 C CA  . GLN B 171  ? 1.9729 3.0118 2.4593 -0.1161 -0.3631 -0.4078 171  GLN X CA  
13899 C C   . GLN B 171  ? 1.9698 3.0129 2.4132 -0.1248 -0.3343 -0.4188 171  GLN X C   
13900 O O   . GLN B 171  ? 1.9456 3.0103 2.3830 -0.1416 -0.3163 -0.4178 171  GLN X O   
13901 C CB  . GLN B 171  ? 1.9561 2.9982 2.4534 -0.1032 -0.3914 -0.4165 171  GLN X CB  
13902 C CG  . GLN B 171  ? 1.9241 2.9925 2.4169 -0.1096 -0.3884 -0.4203 171  GLN X CG  
13903 C CD  . GLN B 171  ? 1.9011 2.9710 2.3845 -0.0928 -0.4076 -0.4357 171  GLN X CD  
13904 O OE1 . GLN B 171  ? 1.9014 2.9590 2.3622 -0.0817 -0.4089 -0.4487 171  GLN X OE1 
13905 N NE2 . GLN B 171  ? 1.8806 2.9652 2.3792 -0.0893 -0.4222 -0.4339 171  GLN X NE2 
13906 N N   . GLN B 172  ? 1.9929 3.0161 2.4060 -0.1140 -0.3299 -0.4298 172  GLN X N   
13907 C CA  . GLN B 172  ? 1.9867 3.0080 2.3553 -0.1228 -0.3020 -0.4414 172  GLN X CA  
13908 C C   . GLN B 172  ? 2.0250 3.0347 2.3737 -0.1390 -0.2690 -0.4347 172  GLN X C   
13909 O O   . GLN B 172  ? 2.0321 3.0542 2.3582 -0.1581 -0.2441 -0.4409 172  GLN X O   
13910 C CB  . GLN B 172  ? 1.9417 2.9413 2.2826 -0.1052 -0.3071 -0.4529 172  GLN X CB  
13911 C CG  . GLN B 172  ? 1.8736 2.8877 2.2205 -0.0922 -0.3318 -0.4652 172  GLN X CG  
13912 C CD  . GLN B 172  ? 1.8451 2.8534 2.1499 -0.0872 -0.3204 -0.4807 172  GLN X CD  
13913 O OE1 . GLN B 172  ? 1.8536 2.8338 2.1318 -0.0795 -0.3104 -0.4813 172  GLN X OE1 
13914 N NE2 . GLN B 172  ? 1.8225 2.8588 2.1197 -0.0910 -0.3209 -0.4930 172  GLN X NE2 
13915 N N   . LEU B 173  ? 2.0421 3.0294 2.3987 -0.1311 -0.2688 -0.4233 173  LEU X N   
13916 C CA  . LEU B 173  ? 2.0652 3.0384 2.4048 -0.1429 -0.2392 -0.4158 173  LEU X CA  
13917 C C   . LEU B 173  ? 2.0605 3.0617 2.4210 -0.1638 -0.2301 -0.4086 173  LEU X C   
13918 O O   . LEU B 173  ? 2.0844 3.0838 2.4209 -0.1814 -0.2005 -0.4104 173  LEU X O   
13919 C CB  . LEU B 173  ? 2.0746 3.0253 2.4243 -0.1259 -0.2453 -0.4043 173  LEU X CB  
13920 C CG  . LEU B 173  ? 2.1050 3.0285 2.4326 -0.1024 -0.2535 -0.4097 173  LEU X CG  
13921 C CD1 . LEU B 173  ? 2.1162 3.0314 2.4653 -0.0841 -0.2666 -0.3982 173  LEU X CD1 
13922 C CD2 . LEU B 173  ? 2.1430 3.0363 2.4135 -0.1058 -0.2216 -0.4173 173  LEU X CD2 
13923 N N   . VAL B 174  ? 2.0356 3.0611 2.4391 -0.1618 -0.2552 -0.4007 174  VAL X N   
13924 C CA  . VAL B 174  ? 1.9988 3.0531 2.4251 -0.1785 -0.2504 -0.3917 174  VAL X CA  
13925 C C   . VAL B 174  ? 1.9958 3.0764 2.4024 -0.1952 -0.2352 -0.4031 174  VAL X C   
13926 O O   . VAL B 174  ? 1.9815 3.0820 2.3890 -0.2127 -0.2179 -0.3993 174  VAL X O   
13927 C CB  . VAL B 174  ? 2.0627 3.1333 2.5357 -0.1715 -0.2820 -0.3809 174  VAL X CB  
13928 C CG1 . VAL B 174  ? 2.0551 3.1563 2.5466 -0.1876 -0.2761 -0.3714 174  VAL X CG1 
13929 C CG2 . VAL B 174  ? 2.0572 3.1111 2.5559 -0.1598 -0.2964 -0.3694 174  VAL X CG2 
13930 N N   . ASN B 175  ? 1.9657 3.0502 2.3549 -0.1894 -0.2419 -0.4177 175  ASN X N   
13931 C CA  . ASN B 175  ? 1.9330 3.0515 2.3080 -0.2027 -0.2323 -0.4300 175  ASN X CA  
13932 C C   . ASN B 175  ? 1.9114 3.0227 2.2403 -0.2158 -0.2035 -0.4464 175  ASN X C   
13933 O O   . ASN B 175  ? 1.9073 3.0513 2.2223 -0.2309 -0.1913 -0.4584 175  ASN X O   
13934 C CB  . ASN B 175  ? 1.9156 3.0522 2.3065 -0.1872 -0.2611 -0.4354 175  ASN X CB  
13935 C CG  . ASN B 175  ? 1.8845 3.0182 2.3173 -0.1743 -0.2900 -0.4200 175  ASN X CG  
13936 O OD1 . ASN B 175  ? 1.8811 3.0110 2.3267 -0.1570 -0.3163 -0.4228 175  ASN X OD1 
13937 N ND2 . ASN B 175  ? 1.8649 2.9992 2.3184 -0.1833 -0.2845 -0.4041 175  ASN X ND2 
13938 N N   . ASN B 176  ? 1.8802 2.9497 2.1844 -0.2101 -0.1922 -0.4469 176  ASN X N   
13939 C CA  . ASN B 176  ? 1.8645 2.9188 2.1213 -0.2216 -0.1649 -0.4617 176  ASN X CA  
13940 C C   . ASN B 176  ? 1.8309 2.8386 2.0563 -0.2260 -0.1376 -0.4574 176  ASN X C   
13941 O O   . ASN B 176  ? 1.8452 2.8359 2.0279 -0.2408 -0.1093 -0.4685 176  ASN X O   
13942 C CB  . ASN B 176  ? 1.8756 2.9264 2.1192 -0.2058 -0.1796 -0.4731 176  ASN X CB  
13943 C CG  . ASN B 176  ? 1.8514 2.9474 2.1188 -0.2006 -0.2032 -0.4799 176  ASN X CG  
13944 O OD1 . ASN B 176  ? 1.8526 2.9778 2.1019 -0.2115 -0.1935 -0.4949 176  ASN X OD1 
13945 N ND2 . ASN B 176  ? 1.8286 2.9303 2.1357 -0.1837 -0.2338 -0.4690 176  ASN X ND2 
13946 N N   . TYR B 177  ? 1.8072 2.7944 2.0521 -0.2135 -0.1449 -0.4416 177  TYR X N   
13947 C CA  . TYR B 177  ? 1.8220 2.7646 2.0364 -0.2131 -0.1197 -0.4365 177  TYR X CA  
13948 C C   . TYR B 177  ? 1.8696 2.8147 2.1025 -0.2200 -0.1106 -0.4236 177  TYR X C   
13949 O O   . TYR B 177  ? 1.9145 2.8244 2.1317 -0.2120 -0.0967 -0.4158 177  TYR X O   
13950 C CB  . TYR B 177  ? 1.7614 2.6679 1.9666 -0.1850 -0.1323 -0.4319 177  TYR X CB  
13951 C CG  . TYR B 177  ? 1.7156 2.6106 1.8871 -0.1813 -0.1300 -0.4458 177  TYR X CG  
13952 C CD1 . TYR B 177  ? 1.6686 2.5891 1.8607 -0.1698 -0.1591 -0.4522 177  TYR X CD1 
13953 C CD2 . TYR B 177  ? 1.7218 2.5804 1.8392 -0.1907 -0.0974 -0.4531 177  TYR X CD2 
13954 C CE1 . TYR B 177  ? 1.6570 2.5712 1.8182 -0.1662 -0.1566 -0.4655 177  TYR X CE1 
13955 C CE2 . TYR B 177  ? 1.7182 2.5685 1.8039 -0.1891 -0.0938 -0.4655 177  TYR X CE2 
13956 C CZ  . TYR B 177  ? 1.6760 2.5569 1.7848 -0.1764 -0.1238 -0.4717 177  TYR X CZ  
13957 O OH  . TYR B 177  ? 1.6664 2.5429 1.7444 -0.1740 -0.1204 -0.4842 177  TYR X OH  
13958 N N   . GLY B 178  ? 1.8841 2.8717 2.1483 -0.2334 -0.1178 -0.4212 178  GLY X N   
13959 C CA  . GLY B 178  ? 1.9268 2.9238 2.2097 -0.2418 -0.1091 -0.4093 178  GLY X CA  
13960 C C   . GLY B 178  ? 1.9838 2.9710 2.2990 -0.2209 -0.1278 -0.3917 178  GLY X C   
13961 O O   . GLY B 178  ? 1.9810 2.9525 2.2921 -0.2204 -0.1123 -0.3831 178  GLY X O   
13962 N N   . LEU B 179  ? 2.0350 3.0327 2.3817 -0.2039 -0.1607 -0.3874 179  LEU X N   
13963 C CA  . LEU B 179  ? 2.1072 3.1018 2.4883 -0.1865 -0.1806 -0.3725 179  LEU X CA  
13964 C C   . LEU B 179  ? 2.1593 3.1888 2.5856 -0.1950 -0.1932 -0.3594 179  LEU X C   
13965 O O   . LEU B 179  ? 2.1407 3.1984 2.5807 -0.2056 -0.2013 -0.3616 179  LEU X O   
13966 C CB  . LEU B 179  ? 2.0964 3.0821 2.4883 -0.1650 -0.2096 -0.3753 179  LEU X CB  
13967 C CG  . LEU B 179  ? 2.0694 3.0532 2.4950 -0.1471 -0.2306 -0.3627 179  LEU X CG  
13968 C CD1 . LEU B 179  ? 2.0908 3.0509 2.4964 -0.1388 -0.2095 -0.3562 179  LEU X CD1 
13969 C CD2 . LEU B 179  ? 2.0530 3.0299 2.4871 -0.1276 -0.2595 -0.3688 179  LEU X CD2 
13970 N N   . TYR B 180  ? 2.2470 3.2754 2.6951 -0.1889 -0.1942 -0.3453 180  TYR X N   
13971 C CA  . TYR B 180  ? 2.3103 3.3697 2.8013 -0.1968 -0.2043 -0.3305 180  TYR X CA  
13972 C C   . TYR B 180  ? 2.3781 3.4609 2.8628 -0.2187 -0.1844 -0.3303 180  TYR X C   
13973 O O   . TYR B 180  ? 2.3778 3.4905 2.8918 -0.2268 -0.1963 -0.3223 180  TYR X O   
13974 C CB  . TYR B 180  ? 2.3048 3.3794 2.8346 -0.1905 -0.2391 -0.3262 180  TYR X CB  
13975 C CG  . TYR B 180  ? 2.3284 3.3870 2.8726 -0.1707 -0.2604 -0.3250 180  TYR X CG  
13976 C CD1 . TYR B 180  ? 2.3440 3.3937 2.8903 -0.1607 -0.2534 -0.3179 180  TYR X CD1 
13977 C CD2 . TYR B 180  ? 2.3290 3.3840 2.8844 -0.1608 -0.2878 -0.3318 180  TYR X CD2 
13978 C CE1 . TYR B 180  ? 2.3471 3.3885 2.9070 -0.1420 -0.2734 -0.3178 180  TYR X CE1 
13979 C CE2 . TYR B 180  ? 2.3329 3.3766 2.9015 -0.1434 -0.3079 -0.3324 180  TYR X CE2 
13980 C CZ  . TYR B 180  ? 2.3366 3.3757 2.9081 -0.1344 -0.3008 -0.3255 180  TYR X CZ  
13981 O OH  . TYR B 180  ? 2.3326 3.3666 2.9176 -0.1166 -0.3214 -0.3272 180  TYR X OH  
13982 N N   . LYS B 181  ? 2.4478 3.5156 2.8924 -0.2282 -0.1535 -0.3394 181  LYS X N   
13983 C CA  . LYS B 181  ? 2.4900 3.5804 2.9234 -0.2503 -0.1321 -0.3430 181  LYS X CA  
13984 C C   . LYS B 181  ? 2.5120 3.5779 2.9111 -0.2566 -0.0986 -0.3462 181  LYS X C   
13985 O O   . LYS B 181  ? 2.5309 3.5704 2.8864 -0.2628 -0.0773 -0.3609 181  LYS X O   
13986 C CB  . LYS B 181  ? 2.5474 3.6500 2.9595 -0.2612 -0.1303 -0.3597 181  LYS X CB  
13987 C CG  . LYS B 181  ? 2.5988 3.7330 3.0003 -0.2846 -0.1105 -0.3659 181  LYS X CG  
13988 C CD  . LYS B 181  ? 2.6344 3.7883 3.0184 -0.2935 -0.1114 -0.3831 181  LYS X CD  
13989 C CE  . LYS B 181  ? 2.6465 3.8421 3.0250 -0.3158 -0.0954 -0.3895 181  LYS X CE  
13990 N NZ  . LYS B 181  ? 2.6492 3.8724 3.0132 -0.3234 -0.0973 -0.4067 181  LYS X NZ  
13991 N N   . GLY B 182  ? 2.4996 3.5731 2.9174 -0.2552 -0.0931 -0.3325 182  GLY X N   
13992 C CA  . GLY B 182  ? 2.5116 3.5588 2.8987 -0.2565 -0.0630 -0.3340 182  GLY X CA  
13993 C C   . GLY B 182  ? 2.4902 3.5043 2.8736 -0.2315 -0.0659 -0.3271 182  GLY X C   
13994 O O   . GLY B 182  ? 2.4521 3.4804 2.8738 -0.2165 -0.0904 -0.3145 182  GLY X O   
13995 N N   . THR B 183  ? 2.5236 3.4936 2.8593 -0.2270 -0.0402 -0.3354 183  THR X N   
13996 C CA  . THR B 183  ? 2.5402 3.4776 2.8659 -0.1998 -0.0411 -0.3291 183  THR X CA  
13997 C C   . THR B 183  ? 2.5730 3.5004 2.9040 -0.1822 -0.0664 -0.3311 183  THR X C   
13998 O O   . THR B 183  ? 2.6007 3.5033 2.9216 -0.1576 -0.0694 -0.3271 183  THR X O   
13999 C CB  . THR B 183  ? 2.4883 3.3733 2.7551 -0.1973 -0.0048 -0.3366 183  THR X CB  
14000 O OG1 . THR B 183  ? 2.4972 3.3662 2.7255 -0.2213 0.0153  -0.3536 183  THR X OG1 
14001 C CG2 . THR B 183  ? 2.4957 3.3855 2.7645 -0.1982 0.0144  -0.3289 183  THR X CG2 
14002 N N   . SER B 184  ? 2.5677 3.5158 2.9133 -0.1928 -0.0846 -0.3377 184  SER X N   
14003 C CA  . SER B 184  ? 2.5858 3.5261 2.9357 -0.1770 -0.1091 -0.3416 184  SER X CA  
14004 C C   . SER B 184  ? 2.5747 3.5456 2.9799 -0.1651 -0.1448 -0.3302 184  SER X C   
14005 O O   . SER B 184  ? 2.5454 3.5498 2.9852 -0.1775 -0.1610 -0.3268 184  SER X O   
14006 C CB  . SER B 184  ? 2.5810 3.5254 2.9140 -0.1922 -0.1099 -0.3565 184  SER X CB  
14007 O OG  . SER B 184  ? 2.6163 3.5271 2.8947 -0.2023 -0.0785 -0.3691 184  SER X OG  
14008 N N   . LYS B 185  ? 2.5963 3.5552 3.0079 -0.1410 -0.1567 -0.3248 185  LYS X N   
14009 C CA  . LYS B 185  ? 2.5802 3.5679 3.0439 -0.1314 -0.1891 -0.3153 185  LYS X CA  
14010 C C   . LYS B 185  ? 2.5422 3.5177 3.0063 -0.1033 -0.2017 -0.3133 185  LYS X C   
14011 O O   . LYS B 185  ? 2.5233 3.5191 3.0252 -0.0956 -0.2313 -0.3107 185  LYS X O   
14012 C CB  . LYS B 185  ? 2.6082 3.6295 3.1105 -0.1431 -0.1884 -0.3012 185  LYS X CB  
14013 C CG  . LYS B 185  ? 2.6598 3.6785 3.1600 -0.1296 -0.1739 -0.2919 185  LYS X CG  
14014 C CD  . LYS B 185  ? 2.6641 3.7198 3.2026 -0.1426 -0.1724 -0.2781 185  LYS X CD  
14015 C CE  . LYS B 185  ? 2.6877 3.7425 3.2036 -0.1631 -0.1444 -0.2800 185  LYS X CE  
14016 N NZ  . LYS B 185  ? 2.6761 3.7703 3.2305 -0.1767 -0.1452 -0.2663 185  LYS X NZ  
14017 N N   . TYR B 186  ? 2.5263 3.4690 2.9479 -0.0878 -0.1791 -0.3147 186  TYR X N   
14018 C CA  . TYR B 186  ? 2.4971 3.4284 2.9126 -0.0574 -0.1893 -0.3129 186  TYR X CA  
14019 C C   . TYR B 186  ? 2.4788 3.3713 2.8472 -0.0435 -0.1858 -0.3243 186  TYR X C   
14020 O O   . TYR B 186  ? 2.4910 3.3502 2.8127 -0.0527 -0.1597 -0.3312 186  TYR X O   
14021 C CB  . TYR B 186  ? 2.5121 3.4350 2.9136 -0.0423 -0.1682 -0.3036 186  TYR X CB  
14022 C CG  . TYR B 186  ? 2.4817 3.4412 2.9228 -0.0560 -0.1659 -0.2924 186  TYR X CG  
14023 C CD1 . TYR B 186  ? 2.5011 3.4481 2.9185 -0.0649 -0.1346 -0.2894 186  TYR X CD1 
14024 C CD2 . TYR B 186  ? 2.4488 3.4542 2.9495 -0.0610 -0.1943 -0.2853 186  TYR X CD2 
14025 C CE1 . TYR B 186  ? 2.4824 3.4649 2.9348 -0.0767 -0.1320 -0.2791 186  TYR X CE1 
14026 C CE2 . TYR B 186  ? 2.4314 3.4708 2.9672 -0.0742 -0.1911 -0.2740 186  TYR X CE2 
14027 C CZ  . TYR B 186  ? 2.4483 3.4776 2.9600 -0.0812 -0.1600 -0.2707 186  TYR X CZ  
14028 O OH  . TYR B 186  ? 2.4286 3.4937 2.9740 -0.0938 -0.1562 -0.2594 186  TYR X OH  
14029 N N   . GLY B 187  ? 2.4511 3.3488 2.8307 -0.0220 -0.2113 -0.3265 187  GLY X N   
14030 C CA  . GLY B 187  ? 2.4394 3.3029 2.7750 -0.0061 -0.2096 -0.3362 187  GLY X CA  
14031 C C   . GLY B 187  ? 2.3904 3.2700 2.7481 0.0142  -0.2437 -0.3403 187  GLY X C   
14032 O O   . GLY B 187  ? 2.3490 3.2664 2.7583 0.0147  -0.2696 -0.3364 187  GLY X O   
14033 N N   . LYS B 188  ? 2.3863 3.2375 2.7042 0.0296  -0.2430 -0.3489 188  LYS X N   
14034 C CA  . LYS B 188  ? 2.3899 3.2533 2.7206 0.0525  -0.2733 -0.3542 188  LYS X CA  
14035 C C   . LYS B 188  ? 2.3883 3.2322 2.6893 0.0533  -0.2783 -0.3676 188  LYS X C   
14036 O O   . LYS B 188  ? 2.4408 3.2458 2.6864 0.0581  -0.2535 -0.3703 188  LYS X O   
14037 C CB  . LYS B 188  ? 2.4224 3.2745 2.7305 0.0864  -0.2681 -0.3475 188  LYS X CB  
14038 C CG  . LYS B 188  ? 2.4139 3.2971 2.7589 0.0921  -0.2710 -0.3357 188  LYS X CG  
14039 C CD  . LYS B 188  ? 2.3823 3.3146 2.7854 0.0975  -0.3096 -0.3379 188  LYS X CD  
14040 C CE  . LYS B 188  ? 2.3634 3.3297 2.7983 0.1082  -0.3118 -0.3268 188  LYS X CE  
14041 N NZ  . LYS B 188  ? 2.3378 3.3130 2.7919 0.0832  -0.2940 -0.3173 188  LYS X NZ  
14042 N N   . ILE B 189  ? 2.3453 3.2147 2.6815 0.0485  -0.3096 -0.3762 189  ILE X N   
14043 C CA  . ILE B 189  ? 2.3325 3.1896 2.6452 0.0510  -0.3176 -0.3899 189  ILE X CA  
14044 C C   . ILE B 189  ? 2.3489 3.2013 2.6469 0.0827  -0.3351 -0.3951 189  ILE X C   
14045 O O   . ILE B 189  ? 2.3354 3.2161 2.6729 0.0924  -0.3662 -0.3978 189  ILE X O   
14046 C CB  . ILE B 189  ? 2.2795 3.1638 2.6342 0.0334  -0.3438 -0.3979 189  ILE X CB  
14047 C CG1 . ILE B 189  ? 2.2441 3.1466 2.6315 0.0063  -0.3367 -0.3896 189  ILE X CG1 
14048 C CG2 . ILE B 189  ? 2.2885 3.1593 2.6123 0.0303  -0.3420 -0.4116 189  ILE X CG2 
14049 C CD1 . ILE B 189  ? 2.2101 3.1380 2.6415 -0.0074 -0.3641 -0.3943 189  ILE X CD1 
14050 N N   . ILE B 190  ? 2.4071 3.2241 2.6475 0.0979  -0.3152 -0.3970 190  ILE X N   
14051 C CA  . ILE B 190  ? 2.4466 3.2588 2.6674 0.1302  -0.3305 -0.4016 190  ILE X CA  
14052 C C   . ILE B 190  ? 2.4739 3.2853 2.6828 0.1315  -0.3460 -0.4171 190  ILE X C   
14053 O O   . ILE B 190  ? 2.4949 3.2760 2.6533 0.1323  -0.3254 -0.4209 190  ILE X O   
14054 C CB  . ILE B 190  ? 1.5494 2.3233 1.7134 0.1547  -0.3020 -0.3917 190  ILE X CB  
14055 C CG1 . ILE B 190  ? 1.5822 2.3315 1.6970 0.1786  -0.3022 -0.3986 190  ILE X CG1 
14056 C CG2 . ILE B 190  ? 1.5584 2.2995 1.6916 0.1342  -0.2620 -0.3837 190  ILE X CG2 
14057 C CD1 . ILE B 190  ? 1.6296 2.3305 1.6782 0.2004  -0.2696 -0.3883 190  ILE X CD1 
14058 N N   . ILE B 191  ? 2.4710 3.3151 2.7259 0.1306  -0.3816 -0.4264 191  ILE X N   
14059 C CA  . ILE B 191  ? 2.5185 3.3645 2.7648 0.1357  -0.3998 -0.4422 191  ILE X CA  
14060 C C   . ILE B 191  ? 2.6071 3.4412 2.8169 0.1692  -0.4043 -0.4454 191  ILE X C   
14061 O O   . ILE B 191  ? 2.6317 3.4809 2.8569 0.1898  -0.4196 -0.4420 191  ILE X O   
14062 C CB  . ILE B 191  ? 1.8145 2.6939 2.1174 0.1295  -0.4386 -0.4522 191  ILE X CB  
14063 C CG1 . ILE B 191  ? 1.7286 2.6264 2.0797 0.1035  -0.4404 -0.4438 191  ILE X CG1 
14064 C CG2 . ILE B 191  ? 1.8395 2.7174 2.1318 0.1273  -0.4505 -0.4685 191  ILE X CG2 
14065 C CD1 . ILE B 191  ? 1.6592 2.5812 2.0607 0.0948  -0.4751 -0.4528 191  ILE X CD1 
14066 N N   . ASN B 192  ? 2.6628 3.4729 2.8238 0.1751  -0.3911 -0.4520 192  ASN X N   
14067 C CA  . ASN B 192  ? 2.7428 3.5444 2.8695 0.2077  -0.3991 -0.4565 192  ASN X CA  
14068 C C   . ASN B 192  ? 2.7766 3.6053 2.9291 0.2155  -0.4365 -0.4744 192  ASN X C   
14069 O O   . ASN B 192  ? 2.7438 3.5837 2.9189 0.1956  -0.4467 -0.4843 192  ASN X O   
14070 C CB  . ASN B 192  ? 2.7895 3.5491 2.8464 0.2121  -0.3644 -0.4532 192  ASN X CB  
14071 C CG  . ASN B 192  ? 2.8208 3.5472 2.8468 0.2100  -0.3282 -0.4361 192  ASN X CG  
14072 O OD1 . ASN B 192  ? 2.8289 3.5571 2.8609 0.2292  -0.3303 -0.4256 192  ASN X OD1 
14073 N ND2 . ASN B 192  ? 2.8351 3.5323 2.8273 0.1866  -0.2947 -0.4341 192  ASN X ND2 
14074 N N   . LEU B 193  ? 2.8395 3.6791 2.9880 0.2455  -0.4573 -0.4790 193  LEU X N   
14075 C CA  . LEU B 193  ? 2.8684 3.7338 3.0417 0.2544  -0.4944 -0.4975 193  LEU X CA  
14076 C C   . LEU B 193  ? 2.9551 3.8145 3.0847 0.2889  -0.4996 -0.5033 193  LEU X C   
14077 O O   . LEU B 193  ? 2.9730 3.8418 3.0994 0.2973  -0.5200 -0.5199 193  LEU X O   
14078 C CB  . LEU B 193  ? 2.8148 3.7156 3.0511 0.2508  -0.5256 -0.5002 193  LEU X CB  
14079 C CG  . LEU B 193  ? 2.7411 3.6508 3.0247 0.2169  -0.5257 -0.4957 193  LEU X CG  
14080 C CD1 . LEU B 193  ? 2.7048 3.6474 3.0459 0.2135  -0.5517 -0.4954 193  LEU X CD1 
14081 C CD2 . LEU B 193  ? 2.7183 3.6258 3.0099 0.1999  -0.5351 -0.5090 193  LEU X CD2 
14082 N N   . LYS B 194  ? 3.0210 3.8640 3.1152 0.3103  -0.4805 -0.4893 194  LYS X N   
14083 C CA  . LYS B 194  ? 3.1083 3.9389 3.1503 0.3448  -0.4782 -0.4905 194  LYS X CA  
14084 C C   . LYS B 194  ? 3.1462 3.9457 3.1428 0.3625  -0.4463 -0.4701 194  LYS X C   
14085 O O   . LYS B 194  ? 3.1073 3.9002 3.1186 0.3491  -0.4300 -0.4570 194  LYS X O   
14086 C CB  . LYS B 194  ? 3.1501 4.0198 3.2186 0.3693  -0.5186 -0.5047 194  LYS X CB  
14087 C CG  . LYS B 194  ? 3.1774 4.0825 3.2994 0.3700  -0.5386 -0.5017 194  LYS X CG  
14088 C CD  . LYS B 194  ? 3.2291 4.1757 3.3800 0.3882  -0.5798 -0.5200 194  LYS X CD  
14089 C CE  . LYS B 194  ? 3.2467 4.2340 3.4531 0.3862  -0.5996 -0.5183 194  LYS X CE  
14090 N NZ  . LYS B 194  ? 3.2888 4.2740 3.4714 0.4098  -0.5798 -0.4993 194  LYS X NZ  
14091 N N   . ASP B 195  ? 3.2240 4.0028 3.1633 0.3936  -0.4371 -0.4673 195  ASP X N   
14092 C CA  . ASP B 195  ? 3.2720 4.0087 3.1540 0.4126  -0.4024 -0.4475 195  ASP X CA  
14093 C C   . ASP B 195  ? 3.3418 4.0887 3.2489 0.4193  -0.3998 -0.4338 195  ASP X C   
14094 O O   . ASP B 195  ? 3.3970 4.1043 3.2657 0.4236  -0.3662 -0.4166 195  ASP X O   
14095 C CB  . ASP B 195  ? 3.2270 3.9530 3.0544 0.4541  -0.4042 -0.4469 195  ASP X CB  
14096 C CG  . ASP B 195  ? 3.1470 3.8368 2.9186 0.4486  -0.3828 -0.4500 195  ASP X CG  
14097 O OD1 . ASP B 195  ? 3.1247 3.7687 2.8590 0.4290  -0.3446 -0.4393 195  ASP X OD1 
14098 O OD2 . ASP B 195  ? 3.1189 3.8272 2.8833 0.4632  -0.4039 -0.4639 195  ASP X OD2 
14099 N N   . GLU B 196  ? 3.3470 4.1464 3.3182 0.4189  -0.4344 -0.4419 196  GLU X N   
14100 C CA  . GLU B 196  ? 3.4033 4.2234 3.3987 0.4322  -0.4366 -0.4305 196  GLU X CA  
14101 C C   . GLU B 196  ? 3.2783 4.1415 3.3512 0.4033  -0.4578 -0.4356 196  GLU X C   
14102 O O   . GLU B 196  ? 3.2639 4.1592 3.3680 0.4142  -0.4679 -0.4301 196  GLU X O   
14103 C CB  . GLU B 196  ? 3.5833 4.4311 3.5666 0.4778  -0.4573 -0.4320 196  GLU X CB  
14104 C CG  . GLU B 196  ? 3.6988 4.6050 3.7342 0.4800  -0.5037 -0.4533 196  GLU X CG  
14105 C CD  . GLU B 196  ? 3.8323 4.7298 3.8459 0.4799  -0.5151 -0.4696 196  GLU X CD  
14106 O OE1 . GLU B 196  ? 3.9077 4.7574 3.8687 0.4757  -0.4870 -0.4641 196  GLU X OE1 
14107 O OE2 . GLU B 196  ? 3.8590 4.7984 3.9080 0.4835  -0.5519 -0.4886 196  GLU X OE2 
14108 N N   . ASN B 197  ? 3.1661 4.0311 3.2692 0.3672  -0.4639 -0.4455 197  ASN X N   
14109 C CA  . ASN B 197  ? 3.0281 3.9307 3.2026 0.3398  -0.4844 -0.4497 197  ASN X CA  
14110 C C   . ASN B 197  ? 2.8904 3.7721 3.0759 0.3015  -0.4625 -0.4437 197  ASN X C   
14111 O O   . ASN B 197  ? 2.8937 3.7402 3.0413 0.2900  -0.4406 -0.4441 197  ASN X O   
14112 C CB  . ASN B 197  ? 3.0055 3.9448 3.2218 0.3358  -0.5254 -0.4707 197  ASN X CB  
14113 C CG  . ASN B 197  ? 2.9402 3.9201 3.2292 0.3128  -0.5491 -0.4743 197  ASN X CG  
14114 O OD1 . ASN B 197  ? 2.9042 3.8779 3.2193 0.2813  -0.5394 -0.4688 197  ASN X OD1 
14115 N ND2 . ASN B 197  ? 2.9263 3.9494 3.2479 0.3277  -0.5800 -0.4838 197  ASN X ND2 
14116 N N   . LYS B 198  ? 2.7541 3.6609 2.9914 0.2817  -0.4684 -0.4385 198  LYS X N   
14117 C CA  . LYS B 198  ? 2.6289 3.5234 2.8824 0.2458  -0.4507 -0.4329 198  LYS X CA  
14118 C C   . LYS B 198  ? 2.5531 3.4864 2.8754 0.2242  -0.4698 -0.4316 198  LYS X C   
14119 O O   . LYS B 198  ? 2.5559 3.5181 2.9041 0.2362  -0.4794 -0.4262 198  LYS X O   
14120 C CB  . LYS B 198  ? 2.5887 3.4435 2.7959 0.2458  -0.4085 -0.4167 198  LYS X CB  
14121 C CG  . LYS B 198  ? 2.5368 3.4017 2.7526 0.2595  -0.3988 -0.4018 198  LYS X CG  
14122 C CD  . LYS B 198  ? 2.5038 3.3288 2.6861 0.2460  -0.3574 -0.3882 198  LYS X CD  
14123 C CE  . LYS B 198  ? 2.4851 3.3079 2.6565 0.2685  -0.3418 -0.3731 198  LYS X CE  
14124 N NZ  . LYS B 198  ? 2.4800 3.2578 2.6132 0.2557  -0.3005 -0.3619 198  LYS X NZ  
14125 N N   . VAL B 199  ? 2.4930 3.4281 2.8436 0.1929  -0.4749 -0.4364 199  VAL X N   
14126 C CA  . VAL B 199  ? 2.4283 3.3931 2.8401 0.1683  -0.4890 -0.4333 199  VAL X CA  
14127 C C   . VAL B 199  ? 2.3832 3.3346 2.7958 0.1431  -0.4601 -0.4195 199  VAL X C   
14128 O O   . VAL B 199  ? 2.3868 3.3198 2.7870 0.1239  -0.4486 -0.4220 199  VAL X O   
14129 C CB  . VAL B 199  ? 2.4122 3.3896 2.8592 0.1522  -0.5189 -0.4483 199  VAL X CB  
14130 C CG1 . VAL B 199  ? 2.3822 3.3874 2.8906 0.1277  -0.5334 -0.4437 199  VAL X CG1 
14131 C CG2 . VAL B 199  ? 2.4350 3.4242 2.8786 0.1758  -0.5472 -0.4646 199  VAL X CG2 
14132 N N   . GLU B 200  ? 2.3319 3.2969 2.7602 0.1437  -0.4493 -0.4059 200  GLU X N   
14133 C CA  . GLU B 200  ? 2.2736 3.2266 2.6989 0.1230  -0.4201 -0.3928 200  GLU X CA  
14134 C C   . GLU B 200  ? 2.2186 3.1975 2.6997 0.0923  -0.4315 -0.3895 200  GLU X C   
14135 O O   . GLU B 200  ? 2.1786 3.1878 2.7061 0.0884  -0.4610 -0.3943 200  GLU X O   
14136 C CB  . GLU B 200  ? 2.2755 3.2259 2.6831 0.1412  -0.3989 -0.3792 200  GLU X CB  
14137 C CG  . GLU B 200  ? 2.3134 3.2289 2.6576 0.1718  -0.3810 -0.3787 200  GLU X CG  
14138 C CD  . GLU B 200  ? 2.3430 3.2447 2.6617 0.1874  -0.3533 -0.3640 200  GLU X CD  
14139 O OE1 . GLU B 200  ? 2.3245 3.2464 2.6757 0.1732  -0.3475 -0.3550 200  GLU X OE1 
14140 O OE2 . GLU B 200  ? 2.3901 3.2592 2.6543 0.2149  -0.3367 -0.3611 200  GLU X OE2 
14141 N N   . ILE B 201  ? 2.2051 3.1715 2.6799 0.0702  -0.4073 -0.3815 201  ILE X N   
14142 C CA  . ILE B 201  ? 2.1686 3.1573 2.6906 0.0422  -0.4133 -0.3753 201  ILE X CA  
14143 C C   . ILE B 201  ? 2.2068 3.1908 2.7205 0.0293  -0.3820 -0.3614 201  ILE X C   
14144 O O   . ILE B 201  ? 2.2160 3.1760 2.6970 0.0180  -0.3583 -0.3616 201  ILE X O   
14145 C CB  . ILE B 201  ? 2.0919 3.0736 2.6193 0.0229  -0.4221 -0.3837 201  ILE X CB  
14146 C CG1 . ILE B 201  ? 2.0635 3.0405 2.5847 0.0373  -0.4478 -0.4000 201  ILE X CG1 
14147 C CG2 . ILE B 201  ? 2.0502 3.0557 2.6292 -0.0017 -0.4341 -0.3767 201  ILE X CG2 
14148 C CD1 . ILE B 201  ? 2.0286 2.9968 2.5474 0.0234  -0.4544 -0.4093 201  ILE X CD1 
14149 N N   . ASP B 202  ? 2.2432 3.2528 2.7871 0.0302  -0.3819 -0.3503 202  ASP X N   
14150 C CA  . ASP B 202  ? 2.2985 3.3070 2.8383 0.0178  -0.3537 -0.3375 202  ASP X CA  
14151 C C   . ASP B 202  ? 2.3305 3.3394 2.8839 -0.0125 -0.3505 -0.3370 202  ASP X C   
14152 O O   . ASP B 202  ? 2.2968 3.3197 2.8828 -0.0242 -0.3750 -0.3415 202  ASP X O   
14153 C CB  . ASP B 202  ? 2.3024 3.3478 2.8826 0.0208  -0.3589 -0.3263 202  ASP X CB  
14154 C CG  . ASP B 202  ? 2.3281 3.3715 2.8991 0.0124  -0.3278 -0.3135 202  ASP X CG  
14155 O OD1 . ASP B 202  ? 2.3167 3.3944 2.9250 0.0088  -0.3305 -0.3035 202  ASP X OD1 
14156 O OD2 . ASP B 202  ? 2.3616 3.3704 2.8878 0.0086  -0.3004 -0.3142 202  ASP X OD2 
14157 N N   . LEU B 203  ? 2.4140 3.4062 2.9394 -0.0241 -0.3200 -0.3324 203  LEU X N   
14158 C CA  . LEU B 203  ? 2.4674 3.4639 3.0017 -0.0513 -0.3140 -0.3317 203  LEU X CA  
14159 C C   . LEU B 203  ? 2.5560 3.5795 3.1254 -0.0673 -0.3076 -0.3175 203  LEU X C   
14160 O O   . LEU B 203  ? 2.5436 3.5786 3.1294 -0.0892 -0.3064 -0.3141 203  LEU X O   
14161 C CB  . LEU B 203  ? 2.4454 3.4108 2.9266 -0.0570 -0.2847 -0.3381 203  LEU X CB  
14162 C CG  . LEU B 203  ? 2.4271 3.3661 2.8711 -0.0401 -0.2890 -0.3510 203  LEU X CG  
14163 C CD1 . LEU B 203  ? 2.4399 3.3464 2.8282 -0.0466 -0.2569 -0.3571 203  LEU X CD1 
14164 C CD2 . LEU B 203  ? 2.3941 3.3463 2.8622 -0.0438 -0.3189 -0.3602 203  LEU X CD2 
14165 N N   . GLY B 204  ? 2.6567 3.6926 3.2368 -0.0546 -0.3036 -0.3089 204  GLY X N   
14166 C CA  . GLY B 204  ? 2.7387 3.8028 3.3508 -0.0673 -0.2961 -0.2951 204  GLY X CA  
14167 C C   . GLY B 204  ? 2.8075 3.9063 3.4778 -0.0829 -0.3226 -0.2891 204  GLY X C   
14168 O O   . GLY B 204  ? 2.8056 3.9289 3.5039 -0.0979 -0.3166 -0.2768 204  GLY X O   
14169 N N   . ASP B 205  ? 2.8835 3.9824 3.5701 -0.0798 -0.3511 -0.2978 205  ASP X N   
14170 C CA  . ASP B 205  ? 2.9430 4.0676 3.6821 -0.0946 -0.3775 -0.2936 205  ASP X CA  
14171 C C   . ASP B 205  ? 2.9506 4.0621 3.6929 -0.0906 -0.4052 -0.3074 205  ASP X C   
14172 O O   . ASP B 205  ? 2.9723 4.0667 3.6865 -0.0707 -0.4094 -0.3194 205  ASP X O   
14173 C CB  . ASP B 205  ? 3.0058 4.1651 3.7817 -0.0891 -0.3858 -0.2860 205  ASP X CB  
14174 C CG  . ASP B 205  ? 3.0489 4.2344 3.8797 -0.1091 -0.4100 -0.2808 205  ASP X CG  
14175 O OD1 . ASP B 205  ? 3.0642 4.2406 3.9044 -0.1285 -0.4144 -0.2778 205  ASP X OD1 
14176 O OD2 . ASP B 205  ? 3.0648 4.2805 3.9285 -0.1054 -0.4240 -0.2795 205  ASP X OD2 
14177 N N   . LYS B 206  ? 2.9333 4.0506 3.7076 -0.1086 -0.4232 -0.3053 206  LYS X N   
14178 C CA  . LYS B 206  ? 2.9172 4.0212 3.6974 -0.1054 -0.4507 -0.3186 206  LYS X CA  
14179 C C   . LYS B 206  ? 2.8786 4.0038 3.7047 -0.1090 -0.4775 -0.3191 206  LYS X C   
14180 O O   . LYS B 206  ? 2.8918 4.0121 3.7426 -0.1218 -0.4981 -0.3213 206  LYS X O   
14181 C CB  . LYS B 206  ? 2.9232 4.0133 3.7018 -0.1207 -0.4529 -0.3177 206  LYS X CB  
14182 C CG  . LYS B 206  ? 2.9268 4.0075 3.6682 -0.1236 -0.4243 -0.3154 206  LYS X CG  
14183 C CD  . LYS B 206  ? 2.9269 4.0035 3.6705 -0.1382 -0.4260 -0.3126 206  LYS X CD  
14184 C CE  . LYS B 206  ? 2.9275 4.0039 3.6377 -0.1440 -0.3961 -0.3104 206  LYS X CE  
14185 N NZ  . LYS B 206  ? 2.9273 4.0032 3.6324 -0.1535 -0.3974 -0.3109 206  LYS X NZ  
14186 N N   . LEU B 207  ? 2.8200 3.9685 3.6561 -0.0976 -0.4766 -0.3176 207  LEU X N   
14187 C CA  . LEU B 207  ? 2.7546 3.9331 3.6371 -0.1032 -0.4996 -0.3183 207  LEU X CA  
14188 C C   . LEU B 207  ? 2.7129 3.8868 3.5960 -0.0889 -0.5275 -0.3375 207  LEU X C   
14189 O O   . LEU B 207  ? 2.7092 3.9119 3.6261 -0.0898 -0.5462 -0.3417 207  LEU X O   
14190 C CB  . LEU B 207  ? 2.7430 3.9575 3.6387 -0.0963 -0.4865 -0.3084 207  LEU X CB  
14191 C CG  . LEU B 207  ? 2.7322 3.9902 3.6811 -0.1072 -0.5041 -0.3056 207  LEU X CG  
14192 C CD1 . LEU B 207  ? 2.7288 3.9921 3.7153 -0.1402 -0.5077 -0.2938 207  LEU X CD1 
14193 C CD2 . LEU B 207  ? 2.7212 4.0152 3.6733 -0.0930 -0.4883 -0.2974 207  LEU X CD2 
14194 N N   . GLN B 208  ? 2.6653 3.8065 3.5115 -0.0764 -0.5301 -0.3499 208  GLN X N   
14195 C CA  . GLN B 208  ? 2.6214 3.7568 3.4609 -0.0595 -0.5545 -0.3691 208  GLN X CA  
14196 C C   . GLN B 208  ? 2.5960 3.7176 3.4583 -0.0737 -0.5817 -0.3795 208  GLN X C   
14197 O O   . GLN B 208  ? 2.5919 3.6879 3.4296 -0.0633 -0.5919 -0.3936 208  GLN X O   
14198 C CB  . GLN B 208  ? 2.6025 3.7115 3.3866 -0.0352 -0.5421 -0.3779 208  GLN X CB  
14199 C CG  . GLN B 208  ? 2.5918 3.6996 3.3639 -0.0127 -0.5640 -0.3965 208  GLN X CG  
14200 C CD  . GLN B 208  ? 2.5732 3.7133 3.3548 0.0051  -0.5683 -0.3968 208  GLN X CD  
14201 O OE1 . GLN B 208  ? 2.5623 3.7289 3.3788 0.0033  -0.5936 -0.4053 208  GLN X OE1 
14202 N NE2 . GLN B 208  ? 2.5756 3.7142 3.3251 0.0228  -0.5431 -0.3880 208  GLN X NE2 
14203 N N   . PHE B 209  ? 2.5770 3.7144 3.4849 -0.0974 -0.5928 -0.3725 209  PHE X N   
14204 C CA  . PHE B 209  ? 2.5802 3.6992 3.5098 -0.1129 -0.6172 -0.3809 209  PHE X CA  
14205 C C   . PHE B 209  ? 2.6442 3.7621 3.5749 -0.0997 -0.6453 -0.4040 209  PHE X C   
14206 O O   . PHE B 209  ? 2.6723 3.7602 3.5938 -0.0988 -0.6614 -0.4168 209  PHE X O   
14207 C CB  . PHE B 209  ? 2.5136 3.6501 3.4914 -0.1426 -0.6211 -0.3674 209  PHE X CB  
14208 C CG  . PHE B 209  ? 2.4416 3.6257 3.4498 -0.1449 -0.6198 -0.3628 209  PHE X CG  
14209 C CD1 . PHE B 209  ? 2.4270 3.6345 3.4660 -0.1484 -0.6447 -0.3766 209  PHE X CD1 
14210 C CD2 . PHE B 209  ? 2.3899 3.5977 3.3954 -0.1431 -0.5939 -0.3457 209  PHE X CD2 
14211 C CE1 . PHE B 209  ? 2.3962 3.6543 3.4640 -0.1494 -0.6439 -0.3731 209  PHE X CE1 
14212 C CE2 . PHE B 209  ? 2.3603 3.6149 3.3930 -0.1425 -0.5926 -0.3417 209  PHE X CE2 
14213 C CZ  . PHE B 209  ? 2.3684 3.6506 3.4330 -0.1453 -0.6178 -0.3552 209  PHE X CZ  
14214 N N   . GLU B 210  ? 2.6892 3.8414 3.6297 -0.0874 -0.6510 -0.4097 210  GLU X N   
14215 C CA  . GLU B 210  ? 2.7485 3.9109 3.6995 -0.0784 -0.6800 -0.4317 210  GLU X CA  
14216 C C   . GLU B 210  ? 2.7471 3.8906 3.6530 -0.0479 -0.6852 -0.4487 210  GLU X C   
14217 O O   . GLU B 210  ? 2.7794 3.9172 3.6882 -0.0428 -0.7107 -0.4689 210  GLU X O   
14218 C CB  . GLU B 210  ? 2.8051 4.0205 3.7901 -0.0789 -0.6869 -0.4321 210  GLU X CB  
14219 C CG  . GLU B 210  ? 2.8678 4.1060 3.8287 -0.0450 -0.6903 -0.4435 210  GLU X CG  
14220 C CD  . GLU B 210  ? 2.9072 4.1473 3.8327 -0.0233 -0.6599 -0.4284 210  GLU X CD  
14221 O OE1 . GLU B 210  ? 2.9062 4.1484 3.8391 -0.0370 -0.6379 -0.4092 210  GLU X OE1 
14222 O OE2 . GLU B 210  ? 2.9373 4.1749 3.8256 0.0076  -0.6577 -0.4360 210  GLU X OE2 
14223 N N   . ARG B 211  ? 2.6979 3.8314 3.5616 -0.0284 -0.6609 -0.4413 211  ARG X N   
14224 C CA  . ARG B 211  ? 2.6432 3.7560 3.4607 -0.0012 -0.6624 -0.4553 211  ARG X CA  
14225 C C   . ARG B 211  ? 2.6443 3.7171 3.4390 -0.0065 -0.6599 -0.4587 211  ARG X C   
14226 O O   . ARG B 211  ? 2.6346 3.6889 3.3952 0.0120  -0.6648 -0.4726 211  ARG X O   
14227 C CB  . ARG B 211  ? 2.5701 3.6879 3.3491 0.0227  -0.6371 -0.4469 211  ARG X CB  
14228 C CG  . ARG B 211  ? 2.5125 3.6122 3.2436 0.0517  -0.6387 -0.4608 211  ARG X CG  
14229 C CD  . ARG B 211  ? 2.4553 3.5638 3.1537 0.0775  -0.6188 -0.4533 211  ARG X CD  
14230 N NE  . ARG B 211  ? 2.3952 3.4949 3.0809 0.0696  -0.5860 -0.4336 211  ARG X NE  
14231 C CZ  . ARG B 211  ? 2.3660 3.4704 3.0273 0.0876  -0.5645 -0.4231 211  ARG X CZ  
14232 N NH1 . ARG B 211  ? 2.3739 3.4935 3.0207 0.1164  -0.5724 -0.4291 211  ARG X NH1 
14233 N NH2 . ARG B 211  ? 2.3459 3.4393 2.9957 0.0782  -0.5349 -0.4069 211  ARG X NH2 
14234 N N   . MET B 212  ? 2.6304 3.6930 3.4441 -0.0307 -0.6523 -0.4459 212  MET X N   
14235 C CA  . MET B 212  ? 2.6268 3.6566 3.4236 -0.0361 -0.6513 -0.4480 212  MET X CA  
14236 C C   . MET B 212  ? 2.6183 3.6309 3.4194 -0.0317 -0.6814 -0.4691 212  MET X C   
14237 O O   . MET B 212  ? 2.6522 3.6376 3.4394 -0.0321 -0.6854 -0.4743 212  MET X O   
14238 C CB  . MET B 212  ? 2.6105 3.6368 3.4315 -0.0622 -0.6410 -0.4297 212  MET X CB  
14239 C CG  . MET B 212  ? 2.5912 3.6248 3.3941 -0.0643 -0.6080 -0.4118 212  MET X CG  
14240 S SD  . MET B 212  ? 2.3048 3.3392 3.1327 -0.0929 -0.5940 -0.3893 212  MET X SD  
14241 C CE  . MET B 212  ? 1.0540 2.0935 1.8445 -0.0874 -0.5559 -0.3774 212  MET X CE  
14242 N N   . GLY B 213  ? 2.5874 3.6183 3.4076 -0.0267 -0.7027 -0.4819 213  GLY X N   
14243 C CA  . GLY B 213  ? 2.5810 3.5986 3.4030 -0.0202 -0.7320 -0.5051 213  GLY X CA  
14244 C C   . GLY B 213  ? 2.5800 3.5972 3.3612 0.0107  -0.7346 -0.5210 213  GLY X C   
14245 O O   . GLY B 213  ? 2.5897 3.5853 3.3535 0.0210  -0.7499 -0.5385 213  GLY X O   
14246 N N   . ASP B 214  ? 2.5706 3.6104 3.3348 0.0266  -0.7191 -0.5144 214  ASP X N   
14247 C CA  . ASP B 214  ? 2.5522 3.5902 3.2723 0.0569  -0.7165 -0.5254 214  ASP X CA  
14248 C C   . ASP B 214  ? 2.5842 3.5892 3.2681 0.0639  -0.7118 -0.5326 214  ASP X C   
14249 O O   . ASP B 214  ? 2.6100 3.5980 3.2949 0.0485  -0.6994 -0.5226 214  ASP X O   
14250 C CB  . ASP B 214  ? 2.4695 3.5220 3.1672 0.0696  -0.6888 -0.5093 214  ASP X CB  
14251 C CG  . ASP B 214  ? 2.3969 3.4578 3.0596 0.1019  -0.6912 -0.5194 214  ASP X CG  
14252 O OD1 . ASP B 214  ? 2.3753 3.4193 3.0078 0.1174  -0.6994 -0.5344 214  ASP X OD1 
14253 O OD2 . ASP B 214  ? 2.3634 3.4487 3.0268 0.1137  -0.6841 -0.5117 214  ASP X OD2 
14254 N N   . VAL B 215  ? 2.5475 3.5471 3.1999 0.0878  -0.7219 -0.5502 215  VAL X N   
14255 C CA  . VAL B 215  ? 2.5056 3.4799 3.1216 0.0972  -0.7171 -0.5586 215  VAL X CA  
14256 C C   . VAL B 215  ? 2.4790 3.4532 3.0442 0.1235  -0.7020 -0.5617 215  VAL X C   
14257 O O   . VAL B 215  ? 2.4681 3.4591 3.0262 0.1398  -0.7042 -0.5629 215  VAL X O   
14258 C CB  . VAL B 215  ? 2.9990 3.9589 3.6256 0.0983  -0.7479 -0.5805 215  VAL X CB  
14259 C CG1 . VAL B 215  ? 2.9917 3.9392 3.6581 0.0716  -0.7570 -0.5749 215  VAL X CG1 
14260 C CG2 . VAL B 215  ? 3.0207 3.9969 3.6551 0.1127  -0.7745 -0.5997 215  VAL X CG2 
14261 N N   . LEU B 216  ? 2.4544 3.4109 2.9836 0.1280  -0.6861 -0.5627 216  LEU X N   
14262 C CA  . LEU B 216  ? 2.4188 3.3711 2.8970 0.1481  -0.6655 -0.5622 216  LEU X CA  
14263 C C   . LEU B 216  ? 2.3957 3.3365 2.8393 0.1631  -0.6706 -0.5794 216  LEU X C   
14264 O O   . LEU B 216  ? 2.3819 3.3139 2.8307 0.1543  -0.6755 -0.5854 216  LEU X O   
14265 C CB  . LEU B 216  ? 2.3714 3.3171 2.8310 0.1365  -0.6286 -0.5419 216  LEU X CB  
14266 C CG  . LEU B 216  ? 2.3084 3.2654 2.7880 0.1283  -0.6160 -0.5236 216  LEU X CG  
14267 C CD1 . LEU B 216  ? 2.3096 3.2832 2.7924 0.1491  -0.6308 -0.5279 216  LEU X CD1 
14268 C CD2 . LEU B 216  ? 2.2591 3.2239 2.7886 0.1021  -0.6238 -0.5154 216  LEU X CD2 
14269 N N   . ASN B 217  ? 2.3845 3.3267 2.7912 0.1873  -0.6687 -0.5865 217  ASN X N   
14270 C CA  . ASN B 217  ? 2.3895 3.3237 2.7575 0.2036  -0.6694 -0.6015 217  ASN X CA  
14271 C C   . ASN B 217  ? 2.3841 3.3072 2.7143 0.1970  -0.6341 -0.5911 217  ASN X C   
14272 O O   . ASN B 217  ? 2.3666 3.2843 2.6694 0.1998  -0.6082 -0.5778 217  ASN X O   
14273 C CB  . ASN B 217  ? 2.4201 3.3610 2.7605 0.2324  -0.6790 -0.6115 217  ASN X CB  
14274 C CG  . ASN B 217  ? 2.4416 3.4005 2.8186 0.2378  -0.7094 -0.6195 217  ASN X CG  
14275 O OD1 . ASN B 217  ? 2.4430 3.4061 2.8657 0.2199  -0.7279 -0.6225 217  ASN X OD1 
14276 N ND2 . ASN B 217  ? 2.4586 3.4293 2.8147 0.2624  -0.7142 -0.6231 217  ASN X ND2 
14277 N N   . SER B 218  ? 2.4144 3.3345 2.7416 0.1887  -0.6329 -0.5981 218  SER X N   
14278 C CA  . SER B 218  ? 2.4484 3.3644 2.7448 0.1780  -0.6002 -0.5901 218  SER X CA  
14279 C C   . SER B 218  ? 2.5260 3.4347 2.7686 0.1925  -0.5771 -0.5891 218  SER X C   
14280 O O   . SER B 218  ? 2.5100 3.4096 2.7313 0.1831  -0.5464 -0.5741 218  SER X O   
14281 C CB  . SER B 218  ? 2.4165 3.3373 2.7152 0.1735  -0.6070 -0.6019 218  SER X CB  
14282 O OG  . SER B 218  ? 2.3758 3.2977 2.7186 0.1577  -0.6212 -0.5981 218  SER X OG  
14283 N N   . LYS B 219  ? 2.6233 3.5339 2.8422 0.2152  -0.5912 -0.6051 219  LYS X N   
14284 C CA  . LYS B 219  ? 2.7378 3.6401 2.9017 0.2297  -0.5693 -0.6047 219  LYS X CA  
14285 C C   . LYS B 219  ? 2.6697 3.5600 2.8153 0.2399  -0.5557 -0.5900 219  LYS X C   
14286 O O   . LYS B 219  ? 2.7221 3.5978 2.8189 0.2480  -0.5300 -0.5839 219  LYS X O   
14287 C CB  . LYS B 219  ? 2.9565 3.8661 3.1012 0.2539  -0.5904 -0.6255 219  LYS X CB  
14288 C CG  . LYS B 219  ? 3.2275 4.1479 3.3796 0.2493  -0.6005 -0.6409 219  LYS X CG  
14289 C CD  . LYS B 219  ? 3.2705 4.1978 3.3994 0.2754  -0.6194 -0.6616 219  LYS X CD  
14290 C CE  . LYS B 219  ? 3.3418 4.2715 3.4980 0.2918  -0.6562 -0.6728 219  LYS X CE  
14291 N NZ  . LYS B 219  ? 3.3784 4.3090 3.5852 0.2787  -0.6807 -0.6786 219  LYS X NZ  
14292 N N   . ASP B 220  ? 2.5694 3.4659 2.7527 0.2402  -0.5724 -0.5843 220  ASP X N   
14293 C CA  . ASP B 220  ? 2.5059 3.3961 2.6748 0.2541  -0.5628 -0.5711 220  ASP X CA  
14294 C C   . ASP B 220  ? 2.4533 3.3244 2.6033 0.2383  -0.5244 -0.5503 220  ASP X C   
14295 O O   . ASP B 220  ? 2.4917 3.3444 2.5991 0.2523  -0.5024 -0.5402 220  ASP X O   
14296 C CB  . ASP B 220  ? 2.4730 3.3827 2.6906 0.2584  -0.5927 -0.5726 220  ASP X CB  
14297 C CG  . ASP B 220  ? 2.4906 3.4162 2.7117 0.2825  -0.6267 -0.5923 220  ASP X CG  
14298 O OD1 . ASP B 220  ? 2.5232 3.4433 2.7023 0.3018  -0.6245 -0.6015 220  ASP X OD1 
14299 O OD2 . ASP B 220  ? 2.4771 3.4218 2.7427 0.2811  -0.6553 -0.5992 220  ASP X OD2 
14300 N N   . ILE B 221  ? 2.3590 3.2326 2.5382 0.2101  -0.5162 -0.5441 221  ILE X N   
14301 C CA  . ILE B 221  ? 2.2812 3.1395 2.4500 0.1921  -0.4823 -0.5257 221  ILE X CA  
14302 C C   . ILE B 221  ? 2.2410 3.0736 2.3492 0.1912  -0.4456 -0.5214 221  ILE X C   
14303 O O   . ILE B 221  ? 2.2647 3.0983 2.3570 0.1786  -0.4356 -0.5295 221  ILE X O   
14304 C CB  . ILE B 221  ? 1.7283 2.5970 1.9359 0.1613  -0.4798 -0.5220 221  ILE X CB  
14305 C CG1 . ILE B 221  ? 1.6681 2.5587 1.9333 0.1583  -0.5162 -0.5286 221  ILE X CG1 
14306 C CG2 . ILE B 221  ? 1.7485 2.6057 1.9544 0.1460  -0.4512 -0.5033 221  ILE X CG2 
14307 C CD1 . ILE B 221  ? 1.6023 2.5013 1.9044 0.1303  -0.5134 -0.5221 221  ILE X CD1 
14308 N N   . ARG B 222  ? 2.2045 3.0139 2.2782 0.2043  -0.4248 -0.5085 222  ARG X N   
14309 C CA  . ARG B 222  ? 2.1987 2.9759 2.2095 0.2043  -0.3883 -0.5032 222  ARG X CA  
14310 C C   . ARG B 222  ? 2.1719 2.9345 2.1738 0.1720  -0.3539 -0.4950 222  ARG X C   
14311 O O   . ARG B 222  ? 2.1451 2.8962 2.1110 0.1583  -0.3304 -0.4994 222  ARG X O   
14312 C CB  . ARG B 222  ? 2.2753 3.0280 2.2485 0.2329  -0.3781 -0.4916 222  ARG X CB  
14313 C CG  . ARG B 222  ? 2.3724 3.0823 2.2769 0.2327  -0.3371 -0.4830 222  ARG X CG  
14314 C CD  . ARG B 222  ? 2.4640 3.1488 2.3339 0.2647  -0.3295 -0.4697 222  ARG X CD  
14315 N NE  . ARG B 222  ? 2.5033 3.2136 2.3856 0.2969  -0.3648 -0.4782 222  ARG X NE  
14316 C CZ  . ARG B 222  ? 2.5501 3.2518 2.4084 0.3314  -0.3680 -0.4700 222  ARG X CZ  
14317 N NH1 . ARG B 222  ? 2.5875 3.2514 2.4064 0.3400  -0.3372 -0.4518 222  ARG X NH1 
14318 N NH2 . ARG B 222  ? 2.5568 3.2880 2.4291 0.3583  -0.4020 -0.4807 222  ARG X NH2 
14319 N N   . GLY B 223  ? 2.1289 2.8948 2.1632 0.1590  -0.3508 -0.4840 223  GLY X N   
14320 C CA  . GLY B 223  ? 2.0836 2.8400 2.1139 0.1280  -0.3209 -0.4775 223  GLY X CA  
14321 C C   . GLY B 223  ? 1.9613 2.7204 2.0244 0.1195  -0.3180 -0.4640 223  GLY X C   
14322 O O   . GLY B 223  ? 1.9752 2.7192 2.0290 0.1380  -0.3141 -0.4530 223  GLY X O   
14323 N N   . ILE B 224  ? 1.9109 2.6913 2.0112 0.0927  -0.3195 -0.4647 224  ILE X N   
14324 C CA  . ILE B 224  ? 1.8936 2.6783 2.0235 0.0797  -0.3126 -0.4518 224  ILE X CA  
14325 C C   . ILE B 224  ? 1.9878 2.7384 2.0760 0.0681  -0.2705 -0.4415 224  ILE X C   
14326 O O   . ILE B 224  ? 2.0158 2.7438 2.0582 0.0572  -0.2437 -0.4460 224  ILE X O   
14327 C CB  . ILE B 224  ? 1.6461 2.4627 1.8246 0.0537  -0.3243 -0.4545 224  ILE X CB  
14328 C CG1 . ILE B 224  ? 1.6067 2.4505 1.8213 0.0609  -0.3622 -0.4663 224  ILE X CG1 
14329 C CG2 . ILE B 224  ? 1.6265 2.4525 1.8416 0.0454  -0.3240 -0.4409 224  ILE X CG2 
14330 C CD1 . ILE B 224  ? 1.5513 2.4217 1.8152 0.0403  -0.3754 -0.4648 224  ILE X CD1 
14331 N N   . SER B 225  ? 2.0437 2.7916 2.1486 0.0690  -0.2646 -0.4285 225  SER X N   
14332 C CA  . SER B 225  ? 2.1284 2.8424 2.1968 0.0592  -0.2262 -0.4188 225  SER X CA  
14333 C C   . SER B 225  ? 2.1593 2.8903 2.2683 0.0503  -0.2270 -0.4077 225  SER X C   
14334 O O   . SER B 225  ? 2.1668 2.9098 2.3012 0.0706  -0.2442 -0.4000 225  SER X O   
14335 C CB  . SER B 225  ? 2.1778 2.8496 2.1924 0.0876  -0.2101 -0.4123 225  SER X CB  
14336 O OG  . SER B 225  ? 2.2039 2.8312 2.1594 0.0742  -0.1699 -0.4116 225  SER X OG  
14337 N N   . VAL B 226  ? 2.1580 2.8944 2.2739 0.0198  -0.2088 -0.4077 226  VAL X N   
14338 C CA  . VAL B 226  ? 2.1545 2.9075 2.3057 0.0085  -0.2062 -0.3974 226  VAL X CA  
14339 C C   . VAL B 226  ? 2.2220 2.9374 2.3323 0.0034  -0.1672 -0.3894 226  VAL X C   
14340 O O   . VAL B 226  ? 2.2337 2.9125 2.2912 -0.0048 -0.1383 -0.3942 226  VAL X O   
14341 C CB  . VAL B 226  ? 2.5609 3.3505 2.7522 -0.0210 -0.2147 -0.4020 226  VAL X CB  
14342 C CG1 . VAL B 226  ? 2.5339 3.3419 2.7612 -0.0320 -0.2120 -0.3902 226  VAL X CG1 
14343 C CG2 . VAL B 226  ? 2.5324 3.3533 2.7614 -0.0153 -0.2523 -0.4099 226  VAL X CG2 
14344 N N   . THR B 227  ? 2.2610 2.9850 2.3953 0.0076  -0.1660 -0.3778 227  THR X N   
14345 C CA  . THR B 227  ? 2.3306 3.0217 2.4314 0.0020  -0.1303 -0.3706 227  THR X CA  
14346 C C   . THR B 227  ? 2.3591 3.0837 2.5059 -0.0148 -0.1326 -0.3637 227  THR X C   
14347 O O   . THR B 227  ? 2.3492 3.1047 2.5404 -0.0016 -0.1555 -0.3556 227  THR X O   
14348 C CB  . THR B 227  ? 2.3256 2.9818 2.3925 0.0370  -0.1211 -0.3610 227  THR X CB  
14349 O OG1 . THR B 227  ? 2.3377 2.9672 2.3651 0.0555  -0.1230 -0.3661 227  THR X OG1 
14350 C CG2 . THR B 227  ? 2.3505 2.9621 2.3726 0.0318  -0.0807 -0.3551 227  THR X CG2 
14351 N N   . ILE B 228  ? 2.4029 3.1241 2.5391 -0.0449 -0.1089 -0.3677 228  ILE X N   
14352 C CA  . ILE B 228  ? 2.4136 3.1663 2.5883 -0.0633 -0.1078 -0.3616 228  ILE X CA  
14353 C C   . ILE B 228  ? 2.4704 3.1947 2.6181 -0.0622 -0.0762 -0.3542 228  ILE X C   
14354 O O   . ILE B 228  ? 2.5163 3.2008 2.6136 -0.0748 -0.0432 -0.3600 228  ILE X O   
14355 C CB  . ILE B 228  ? 2.4167 3.1943 2.6032 -0.0973 -0.1048 -0.3712 228  ILE X CB  
14356 C CG1 . ILE B 228  ? 2.3750 3.1992 2.6160 -0.0985 -0.1426 -0.3720 228  ILE X CG1 
14357 C CG2 . ILE B 228  ? 2.4256 3.2124 2.6181 -0.1188 -0.0834 -0.3672 228  ILE X CG2 
14358 C CD1 . ILE B 228  ? 2.3538 3.2114 2.6163 -0.1275 -0.1426 -0.3768 228  ILE X CD1 
14359 N N   . ASN B 229  ? 2.4692 3.2146 2.6504 -0.0475 -0.0863 -0.3419 229  ASN X N   
14360 C CA  . ASN B 229  ? 2.4915 3.2194 2.6560 -0.0456 -0.0595 -0.3343 229  ASN X CA  
14361 C C   . ASN B 229  ? 2.3741 3.1420 2.5788 -0.0707 -0.0585 -0.3308 229  ASN X C   
14362 O O   . ASN B 229  ? 2.3119 3.1265 2.5723 -0.0693 -0.0841 -0.3230 229  ASN X O   
14363 C CB  . ASN B 229  ? 2.5755 3.2946 2.7376 -0.0075 -0.0642 -0.3229 229  ASN X CB  
14364 C CG  . ASN B 229  ? 2.5760 3.3458 2.7970 0.0083  -0.1047 -0.3174 229  ASN X CG  
14365 O OD1 . ASN B 229  ? 2.5546 3.3485 2.8032 -0.0007 -0.1302 -0.3236 229  ASN X OD1 
14366 N ND2 . ASN B 229  ? 2.5887 3.3748 2.8275 0.0324  -0.1099 -0.3067 229  ASN X ND2 
14367 N N   . GLN B 230  ? 2.3321 3.0810 2.5067 -0.0948 -0.0281 -0.3370 230  GLN X N   
14368 C CA  . GLN B 230  ? 2.2386 3.0247 2.4447 -0.1200 -0.0245 -0.3352 230  GLN X CA  
14369 C C   . GLN B 230  ? 2.2372 3.0186 2.4416 -0.1111 -0.0065 -0.3254 230  GLN X C   
14370 O O   . GLN B 230  ? 2.2222 3.0110 2.4238 -0.1322 0.0128  -0.3273 230  GLN X O   
14371 C CB  . GLN B 230  ? 2.2005 2.9789 2.3791 -0.1532 -0.0035 -0.3496 230  GLN X CB  
14372 C CG  . GLN B 230  ? 2.1468 2.9238 2.3157 -0.1599 -0.0154 -0.3611 230  GLN X CG  
14373 C CD  . GLN B 230  ? 2.1067 2.8903 2.2561 -0.1941 0.0026  -0.3760 230  GLN X CD  
14374 O OE1 . GLN B 230  ? 2.1306 2.8769 2.2305 -0.2033 0.0251  -0.3878 230  GLN X OE1 
14375 N NE2 . GLN B 230  ? 2.0560 2.8889 2.2438 -0.2133 -0.0068 -0.3755 230  GLN X NE2 
14376 N N   . THR C 22   ? 3.5890 1.3444 1.4002 -0.0452 -0.2902 -0.1007 22   THR B N   
14377 C CA  . THR C 22   ? 3.5714 1.3079 1.3704 -0.0231 -0.2934 -0.1018 22   THR B CA  
14378 C C   . THR C 22   ? 3.4975 1.2811 1.3219 -0.0259 -0.3179 -0.1202 22   THR B C   
14379 O O   . THR C 22   ? 3.4375 1.2737 1.2966 -0.0431 -0.3294 -0.1297 22   THR B O   
14380 C CB  . THR C 22   ? 3.5598 1.2958 1.3780 -0.0035 -0.2732 -0.0846 22   THR B CB  
14381 O OG1 . THR C 22   ? 3.4995 1.2816 1.3614 -0.0149 -0.2646 -0.0773 22   THR B OG1 
14382 C CG2 . THR C 22   ? 3.6099 1.2732 1.3827 0.0111  -0.2520 -0.0674 22   THR B CG2 
14383 N N   . TYR C 23   ? 3.5023 1.2657 1.3087 -0.0093 -0.3255 -0.1248 23   TYR B N   
14384 C CA  . TYR C 23   ? 3.5145 1.3215 1.3464 -0.0094 -0.3467 -0.1401 23   TYR B CA  
14385 C C   . TYR C 23   ? 3.4747 1.3077 1.3379 0.0101  -0.3412 -0.1366 23   TYR B C   
14386 O O   . TYR C 23   ? 3.4638 1.2643 1.3141 0.0292  -0.3243 -0.1236 23   TYR B O   
14387 C CB  . TYR C 23   ? 3.6313 1.4036 1.4228 -0.0080 -0.3637 -0.1504 23   TYR B CB  
14388 C CG  . TYR C 23   ? 3.7751 1.4734 1.5129 0.0086  -0.3517 -0.1411 23   TYR B CG  
14389 C CD1 . TYR C 23   ? 3.8006 1.4744 1.5364 0.0285  -0.3290 -0.1254 23   TYR B CD1 
14390 C CD2 . TYR C 23   ? 3.8705 1.5219 1.5584 0.0040  -0.3633 -0.1476 23   TYR B CD2 
14391 C CE1 . TYR C 23   ? 3.8813 1.4854 1.5677 0.0440  -0.3173 -0.1165 23   TYR B CE1 
14392 C CE2 . TYR C 23   ? 3.9375 1.5186 1.5740 0.0185  -0.3520 -0.1395 23   TYR B CE2 
14393 C CZ  . TYR C 23   ? 3.9540 1.5112 1.5900 0.0389  -0.3286 -0.1241 23   TYR B CZ  
14394 O OH  . TYR C 23   ? 4.0175 1.5022 1.6014 0.0536  -0.3168 -0.1158 23   TYR B OH  
14395 N N   . VAL C 24   ? 3.4324 1.3234 1.3365 0.0052  -0.3555 -0.1482 24   VAL B N   
14396 C CA  . VAL C 24   ? 3.3687 1.2906 1.3044 0.0218  -0.3539 -0.1483 24   VAL B CA  
14397 C C   . VAL C 24   ? 3.3159 1.2625 1.2603 0.0214  -0.3758 -0.1641 24   VAL B C   
14398 O O   . VAL C 24   ? 3.2983 1.2753 1.2563 0.0029  -0.3919 -0.1752 24   VAL B O   
14399 C CB  . VAL C 24   ? 3.3403 1.3163 1.3263 0.0150  -0.3452 -0.1441 24   VAL B CB  
14400 C CG1 . VAL C 24   ? 3.3072 1.3291 1.3310 0.0248  -0.3508 -0.1506 24   VAL B CG1 
14401 C CG2 . VAL C 24   ? 3.3398 1.2910 1.3207 0.0224  -0.3215 -0.1249 24   VAL B CG2 
14402 N N   . ILE C 25   ? 3.3217 1.2545 1.2586 0.0426  -0.3760 -0.1641 25   ILE B N   
14403 C CA  . ILE C 25   ? 3.3708 1.3217 1.3134 0.0453  -0.3952 -0.1770 25   ILE B CA  
14404 C C   . ILE C 25   ? 3.3248 1.3007 1.2962 0.0655  -0.3888 -0.1754 25   ILE B C   
14405 O O   . ILE C 25   ? 3.3539 1.2945 1.3039 0.0870  -0.3809 -0.1694 25   ILE B O   
14406 C CB  . ILE C 25   ? 3.4984 1.3909 1.3880 0.0522  -0.4030 -0.1788 25   ILE B CB  
14407 C CG1 . ILE C 25   ? 3.5756 1.4388 1.4319 0.0317  -0.4091 -0.1803 25   ILE B CG1 
14408 C CG2 . ILE C 25   ? 3.5100 1.4210 1.4071 0.0580  -0.4217 -0.1902 25   ILE B CG2 
14409 C CD1 . ILE C 25   ? 3.6029 1.4898 1.4630 0.0137  -0.4338 -0.1939 25   ILE B CD1 
14410 N N   . SER C 26   ? 3.2531 1.2892 1.2729 0.0587  -0.3915 -0.1805 26   SER B N   
14411 C CA  . SER C 26   ? 3.1926 1.2540 1.2412 0.0762  -0.3830 -0.1779 26   SER B CA  
14412 C C   . SER C 26   ? 3.1171 1.1887 1.1691 0.0873  -0.3968 -0.1879 26   SER B C   
14413 O O   . SER C 26   ? 3.1279 1.2065 1.1751 0.0759  -0.4149 -0.1980 26   SER B O   
14414 C CB  . SER C 26   ? 3.1871 1.3062 1.2843 0.0637  -0.3783 -0.1785 26   SER B CB  
14415 O OG  . SER C 26   ? 3.2119 1.3226 1.3061 0.0514  -0.3669 -0.1693 26   SER B OG  
14416 N N   . ALA C 27   ? 3.0420 1.1144 1.1025 0.1095  -0.3883 -0.1844 27   ALA B N   
14417 C CA  . ALA C 27   ? 2.9797 1.0721 1.0529 0.1204  -0.3995 -0.1937 27   ALA B CA  
14418 C C   . ALA C 27   ? 2.9224 1.0206 1.0104 0.1446  -0.3865 -0.1884 27   ALA B C   
14419 O O   . ALA C 27   ? 2.8869 0.9576 0.9627 0.1562  -0.3700 -0.1763 27   ALA B O   
14420 C CB  . ALA C 27   ? 3.0401 1.0911 1.0728 0.1236  -0.4134 -0.1984 27   ALA B CB  
14421 N N   . PRO C 28   ? 2.8809 1.0149 0.9958 0.1521  -0.3937 -0.1967 28   PRO B N   
14422 C CA  . PRO C 28   ? 2.8851 1.0327 1.0192 0.1740  -0.3827 -0.1936 28   PRO B CA  
14423 C C   . PRO C 28   ? 2.9788 1.0725 1.0785 0.1974  -0.3711 -0.1833 28   PRO B C   
14424 O O   . PRO C 28   ? 3.0397 1.0828 1.0977 0.1985  -0.3736 -0.1804 28   PRO B O   
14425 C CB  . PRO C 28   ? 2.8427 1.0182 0.9935 0.1783  -0.3970 -0.2053 28   PRO B CB  
14426 C CG  . PRO C 28   ? 2.8203 1.0260 0.9862 0.1527  -0.4114 -0.2135 28   PRO B CG  
14427 C CD  . PRO C 28   ? 2.8600 1.0267 0.9913 0.1389  -0.4129 -0.2092 28   PRO B CD  
14428 N N   . LYS C 29   ? 2.9846 1.0884 1.1016 0.2158  -0.3579 -0.1773 29   LYS B N   
14429 C CA  . LYS C 29   ? 3.0390 1.0952 1.1280 0.2407  -0.3466 -0.1673 29   LYS B CA  
14430 C C   . LYS C 29   ? 3.0489 1.0854 1.1187 0.2567  -0.3579 -0.1755 29   LYS B C   
14431 O O   . LYS C 29   ? 3.0842 1.0667 1.1155 0.2723  -0.3546 -0.1702 29   LYS B O   
14432 C CB  . LYS C 29   ? 3.0071 1.0837 1.1231 0.2542  -0.3298 -0.1579 29   LYS B CB  
14433 C CG  . LYS C 29   ? 3.0330 1.0667 1.1272 0.2827  -0.3173 -0.1467 29   LYS B CG  
14434 C CD  . LYS C 29   ? 3.6743 1.6410 1.7210 0.2871  -0.3116 -0.1361 29   LYS B CD  
14435 C CE  . LYS C 29   ? 3.6111 1.5313 1.6261 0.3136  -0.3114 -0.1354 29   LYS B CE  
14436 N NZ  . LYS C 29   ? 3.6434 1.4945 1.6124 0.3226  -0.3017 -0.1229 29   LYS B NZ  
14437 N N   . ILE C 30   ? 3.0241 1.1034 1.1202 0.2519  -0.3710 -0.1880 30   ILE B N   
14438 C CA  . ILE C 30   ? 3.0230 1.0911 1.1063 0.2651  -0.3828 -0.1959 30   ILE B CA  
14439 C C   . ILE C 30   ? 3.0025 1.0960 1.0937 0.2446  -0.4030 -0.2076 30   ILE B C   
14440 O O   . ILE C 30   ? 2.9746 1.1075 1.0932 0.2239  -0.4062 -0.2108 30   ILE B O   
14441 C CB  . ILE C 30   ? 2.9003 0.9999 1.0143 0.2862  -0.3771 -0.1982 30   ILE B CB  
14442 C CG1 . ILE C 30   ? 2.9031 0.9791 1.0111 0.3073  -0.3577 -0.1859 30   ILE B CG1 
14443 C CG2 . ILE C 30   ? 2.9016 0.9919 1.0044 0.2993  -0.3897 -0.2063 30   ILE B CG2 
14444 C CD1 . ILE C 30   ? 2.9644 0.9727 1.0242 0.3238  -0.3541 -0.1786 30   ILE B CD1 
14445 N N   . PHE C 31   ? 2.9892 1.0591 1.0560 0.2495  -0.4169 -0.2132 31   PHE B N   
14446 C CA  . PHE C 31   ? 2.9498 1.0525 1.0325 0.2336  -0.4365 -0.2235 31   PHE B CA  
14447 C C   . PHE C 31   ? 2.9124 1.0504 1.0249 0.2483  -0.4403 -0.2295 31   PHE B C   
14448 O O   . PHE C 31   ? 2.8741 1.0053 0.9889 0.2723  -0.4294 -0.2269 31   PHE B O   
14449 C CB  . PHE C 31   ? 2.9753 1.0355 1.0145 0.2226  -0.4529 -0.2260 31   PHE B CB  
14450 C CG  . PHE C 31   ? 3.0142 1.0387 1.0223 0.2070  -0.4498 -0.2207 31   PHE B CG  
14451 C CD1 . PHE C 31   ? 3.0636 1.0206 1.0195 0.2156  -0.4444 -0.2144 31   PHE B CD1 
14452 C CD2 . PHE C 31   ? 2.9882 1.0448 1.0184 0.1837  -0.4517 -0.2219 31   PHE B CD2 
14453 C CE1 . PHE C 31   ? 3.0670 0.9902 0.9941 0.2015  -0.4401 -0.2089 31   PHE B CE1 
14454 C CE2 . PHE C 31   ? 3.0069 1.0309 1.0089 0.1697  -0.4483 -0.2169 31   PHE B CE2 
14455 C CZ  . PHE C 31   ? 3.0453 1.0029 0.9959 0.1786  -0.4422 -0.2103 31   PHE B CZ  
14456 N N   . ARG C 32   ? 2.9050 1.0813 1.0411 0.2334  -0.4559 -0.2372 32   ARG B N   
14457 C CA  . ARG C 32   ? 2.8670 1.0797 1.0332 0.2439  -0.4611 -0.2427 32   ARG B CA  
14458 C C   . ARG C 32   ? 2.8171 1.0301 0.9744 0.2309  -0.4836 -0.2481 32   ARG B C   
14459 O O   . ARG C 32   ? 2.8113 1.0265 0.9633 0.2075  -0.4953 -0.2493 32   ARG B O   
14460 C CB  . ARG C 32   ? 2.8689 1.1460 1.0902 0.2376  -0.4537 -0.2451 32   ARG B CB  
14461 C CG  . ARG C 32   ? 2.8812 1.1674 1.1187 0.2520  -0.4320 -0.2401 32   ARG B CG  
14462 C CD  . ARG C 32   ? 2.8540 1.2042 1.1451 0.2440  -0.4254 -0.2433 32   ARG B CD  
14463 N NE  . ARG C 32   ? 2.8135 1.1745 1.1210 0.2617  -0.4063 -0.2394 32   ARG B NE  
14464 C CZ  . ARG C 32   ? 2.7830 1.1581 1.1052 0.2555  -0.3923 -0.2348 32   ARG B CZ  
14465 N NH1 . ARG C 32   ? 2.7854 1.1683 1.1106 0.2319  -0.3943 -0.2340 32   ARG B NH1 
14466 N NH2 . ARG C 32   ? 2.7645 1.1464 1.0986 0.2728  -0.3764 -0.2307 32   ARG B NH2 
14467 N N   . VAL C 33   ? 2.7971 1.0078 0.9530 0.2466  -0.4895 -0.2507 33   VAL B N   
14468 C CA  . VAL C 33   ? 2.8174 1.0341 0.9706 0.2370  -0.5107 -0.2548 33   VAL B CA  
14469 C C   . VAL C 33   ? 2.8058 1.0874 1.0108 0.2204  -0.5171 -0.2581 33   VAL B C   
14470 O O   . VAL C 33   ? 2.7746 1.0989 1.0207 0.2262  -0.5039 -0.2587 33   VAL B O   
14471 C CB  . VAL C 33   ? 2.8221 1.0279 0.9695 0.2604  -0.5115 -0.2561 33   VAL B CB  
14472 C CG1 . VAL C 33   ? 2.8692 1.0651 1.0002 0.2515  -0.5345 -0.2587 33   VAL B CG1 
14473 C CG2 . VAL C 33   ? 2.8458 0.9942 0.9520 0.2811  -0.4979 -0.2517 33   VAL B CG2 
14474 N N   . GLY C 34   ? 2.8710 1.1591 1.0735 0.1993  -0.5369 -0.2596 34   GLY B N   
14475 C CA  . GLY C 34   ? 2.8959 1.2433 1.1469 0.1822  -0.5434 -0.2615 34   GLY B CA  
14476 C C   . GLY C 34   ? 2.9279 1.2982 1.2002 0.1697  -0.5313 -0.2609 34   GLY B C   
14477 O O   . GLY C 34   ? 2.9079 1.3286 1.2236 0.1571  -0.5316 -0.2622 34   GLY B O   
14478 N N   . ALA C 35   ? 2.9655 1.2978 1.2073 0.1732  -0.5198 -0.2583 35   ALA B N   
14479 C CA  . ALA C 35   ? 2.9793 1.3306 1.2393 0.1623  -0.5073 -0.2570 35   ALA B CA  
14480 C C   . ALA C 35   ? 3.0431 1.3741 1.2795 0.1390  -0.5176 -0.2563 35   ALA B C   
14481 O O   . ALA C 35   ? 3.0562 1.3346 1.2447 0.1388  -0.5232 -0.2544 35   ALA B O   
14482 C CB  . ALA C 35   ? 2.9759 1.3054 1.2247 0.1804  -0.4863 -0.2530 35   ALA B CB  
14483 N N   . SER C 36   ? 3.0718 1.4442 1.3419 0.1195  -0.5192 -0.2579 36   SER B N   
14484 C CA  . SER C 36   ? 3.1111 1.4723 1.3662 0.0964  -0.5271 -0.2575 36   SER B CA  
14485 C C   . SER C 36   ? 3.1272 1.4617 1.3633 0.0995  -0.5097 -0.2536 36   SER B C   
14486 O O   . SER C 36   ? 3.1088 1.4734 1.3746 0.0963  -0.4963 -0.2528 36   SER B O   
14487 C CB  . SER C 36   ? 3.0648 1.4817 1.3668 0.0772  -0.5310 -0.2600 36   SER B CB  
14488 O OG  . SER C 36   ? 3.0182 1.4797 1.3625 0.0857  -0.5288 -0.2618 36   SER B OG  
14489 N N   . GLU C 37   ? 3.1745 1.4517 1.3609 0.1055  -0.5093 -0.2503 37   GLU B N   
14490 C CA  . GLU C 37   ? 3.2064 1.4560 1.3749 0.1109  -0.4913 -0.2445 37   GLU B CA  
14491 C C   . GLU C 37   ? 3.1940 1.4424 1.3579 0.0879  -0.4921 -0.2434 37   GLU B C   
14492 O O   . GLU C 37   ? 3.2151 1.4332 1.3465 0.0750  -0.5043 -0.2439 37   GLU B O   
14493 C CB  . GLU C 37   ? 3.3023 1.4905 1.4222 0.1298  -0.4865 -0.2399 37   GLU B CB  
14494 C CG  . GLU C 37   ? 3.3566 1.5462 1.4824 0.1545  -0.4839 -0.2408 37   GLU B CG  
14495 C CD  . GLU C 37   ? 3.3788 1.6037 1.5428 0.1687  -0.4658 -0.2389 37   GLU B CD  
14496 O OE1 . GLU C 37   ? 3.3633 1.6374 1.5684 0.1569  -0.4624 -0.2410 37   GLU B OE1 
14497 O OE2 . GLU C 37   ? 3.3988 1.6008 1.5507 0.1917  -0.4547 -0.2352 37   GLU B OE2 
14498 N N   . ASN C 38   ? 3.1461 1.4284 1.3429 0.0826  -0.4789 -0.2419 38   ASN B N   
14499 C CA  . ASN C 38   ? 3.1192 1.4064 1.3178 0.0617  -0.4773 -0.2407 38   ASN B CA  
14500 C C   . ASN C 38   ? 3.1332 1.3693 1.2918 0.0645  -0.4660 -0.2330 38   ASN B C   
14501 O O   . ASN C 38   ? 3.1295 1.3487 1.2820 0.0816  -0.4496 -0.2264 38   ASN B O   
14502 C CB  . ASN C 38   ? 3.0611 1.4006 1.3079 0.0555  -0.4663 -0.2413 38   ASN B CB  
14503 C CG  . ASN C 38   ? 3.0281 1.4163 1.3119 0.0390  -0.4793 -0.2483 38   ASN B CG  
14504 O OD1 . ASN C 38   ? 3.0183 1.4193 1.3107 0.0426  -0.4916 -0.2523 38   ASN B OD1 
14505 N ND2 . ASN C 38   ? 2.9944 1.4101 1.3011 0.0206  -0.4763 -0.2491 38   ASN B ND2 
14506 N N   . ILE C 39   ? 3.1306 1.3431 1.2631 0.0472  -0.4745 -0.2333 39   ILE B N   
14507 C CA  . ILE C 39   ? 3.1182 1.2791 1.2096 0.0474  -0.4646 -0.2258 39   ILE B CA  
14508 C C   . ILE C 39   ? 3.1103 1.2777 1.2023 0.0231  -0.4674 -0.2262 39   ILE B C   
14509 O O   . ILE C 39   ? 3.1115 1.2690 1.1860 0.0082  -0.4837 -0.2309 39   ILE B O   
14510 C CB  . ILE C 39   ? 3.1617 1.2652 1.2009 0.0540  -0.4737 -0.2255 39   ILE B CB  
14511 C CG1 . ILE C 39   ? 3.1300 1.2332 1.1704 0.0738  -0.4785 -0.2282 39   ILE B CG1 
14512 C CG2 . ILE C 39   ? 3.1875 1.2339 1.1846 0.0603  -0.4585 -0.2159 39   ILE B CG2 
14513 C CD1 . ILE C 39   ? 3.0719 1.1777 1.1260 0.0974  -0.4599 -0.2226 39   ILE B CD1 
14514 N N   . VAL C 40   ? 3.1125 1.2968 1.2245 0.0187  -0.4521 -0.2211 40   VAL B N   
14515 C CA  . VAL C 40   ? 3.1576 1.3443 1.2680 -0.0032 -0.4525 -0.2205 40   VAL B CA  
14516 C C   . VAL C 40   ? 3.2414 1.3673 1.3014 -0.0024 -0.4466 -0.2134 40   VAL B C   
14517 O O   . VAL C 40   ? 3.2486 1.3343 1.2824 0.0160  -0.4344 -0.2056 40   VAL B O   
14518 C CB  . VAL C 40   ? 3.1851 1.4121 1.3348 -0.0116 -0.4386 -0.2172 40   VAL B CB  
14519 C CG1 . VAL C 40   ? 3.1449 1.4260 1.3423 -0.0079 -0.4384 -0.2220 40   VAL B CG1 
14520 C CG2 . VAL C 40   ? 3.1811 1.3780 1.3153 -0.0019 -0.4175 -0.2045 40   VAL B CG2 
14521 N N   . ILE C 41   ? 3.3080 1.4271 1.3548 -0.0227 -0.4548 -0.2160 41   ILE B N   
14522 C CA  . ILE C 41   ? 3.3851 1.4517 1.3883 -0.0263 -0.4472 -0.2091 41   ILE B CA  
14523 C C   . ILE C 41   ? 3.3460 1.4371 1.3677 -0.0475 -0.4449 -0.2092 41   ILE B C   
14524 O O   . ILE C 41   ? 3.3048 1.4381 1.3552 -0.0636 -0.4580 -0.2175 41   ILE B O   
14525 C CB  . ILE C 41   ? 3.4854 1.5106 1.4439 -0.0315 -0.4630 -0.2136 41   ILE B CB  
14526 C CG1 . ILE C 41   ? 3.5583 1.5347 1.4754 -0.0401 -0.4544 -0.2071 41   ILE B CG1 
14527 C CG2 . ILE C 41   ? 3.4987 1.5626 1.4781 -0.0497 -0.4859 -0.2246 41   ILE B CG2 
14528 C CD1 . ILE C 41   ? 3.6224 1.5579 1.4933 -0.0500 -0.4704 -0.2118 41   ILE B CD1 
14529 N N   . GLN C 42   ? 3.3822 1.4453 1.3872 -0.0473 -0.4276 -0.1990 42   GLN B N   
14530 C CA  . GLN C 42   ? 3.4408 1.5275 1.4659 -0.0652 -0.4215 -0.1970 42   GLN B CA  
14531 C C   . GLN C 42   ? 3.5230 1.5560 1.5099 -0.0609 -0.4044 -0.1847 42   GLN B C   
14532 O O   . GLN C 42   ? 3.5284 1.5253 1.4935 -0.0412 -0.3933 -0.1765 42   GLN B O   
14533 C CB  . GLN C 42   ? 3.4186 1.5559 1.4935 -0.0628 -0.4115 -0.1948 42   GLN B CB  
14534 C CG  . GLN C 42   ? 3.4252 1.5617 1.5082 -0.0669 -0.3920 -0.1831 42   GLN B CG  
14535 C CD  . GLN C 42   ? 3.4106 1.5622 1.5172 -0.0514 -0.3770 -0.1747 42   GLN B CD  
14536 O OE1 . GLN C 42   ? 3.4158 1.5679 1.5312 -0.0529 -0.3607 -0.1633 42   GLN B OE1 
14537 N NE2 . GLN C 42   ? 3.3824 1.5460 1.4991 -0.0364 -0.3823 -0.1795 42   GLN B NE2 
14538 N N   . VAL C 43   ? 3.5759 1.6020 1.5540 -0.0784 -0.4018 -0.1830 43   VAL B N   
14539 C CA  . VAL C 43   ? 3.6061 1.5759 1.5432 -0.0752 -0.3859 -0.1712 43   VAL B CA  
14540 C C   . VAL C 43   ? 3.6510 1.6281 1.5940 -0.0943 -0.3783 -0.1673 43   VAL B C   
14541 O O   . VAL C 43   ? 3.6472 1.6676 1.6186 -0.1123 -0.3895 -0.1762 43   VAL B O   
14542 C CB  . VAL C 43   ? 3.5648 1.4785 1.4479 -0.0715 -0.3949 -0.1744 43   VAL B CB  
14543 C CG1 . VAL C 43   ? 3.5580 1.4822 1.4342 -0.0931 -0.4156 -0.1865 43   VAL B CG1 
14544 C CG2 . VAL C 43   ? 3.5693 1.4203 1.4089 -0.0639 -0.3753 -0.1608 43   VAL B CG2 
14545 N N   . TYR C 44   ? 3.7157 1.6505 1.6331 -0.0896 -0.3583 -0.1532 44   TYR B N   
14546 C CA  . TYR C 44   ? 3.7928 1.7299 1.7144 -0.1056 -0.3471 -0.1465 44   TYR B CA  
14547 C C   . TYR C 44   ? 4.0631 1.9578 1.9403 -0.1186 -0.3509 -0.1492 44   TYR B C   
14548 O O   . TYR C 44   ? 4.0271 1.9086 1.8971 -0.1284 -0.3377 -0.1410 44   TYR B O   
14549 C CB  . TYR C 44   ? 3.9056 1.8276 1.8323 -0.0940 -0.3212 -0.1273 44   TYR B CB  
14550 C CG  . TYR C 44   ? 4.0458 1.9861 1.9924 -0.1101 -0.3085 -0.1189 44   TYR B CG  
14551 C CD1 . TYR C 44   ? 4.0595 2.0613 2.0570 -0.1214 -0.3108 -0.1217 44   TYR B CD1 
14552 C CD2 . TYR C 44   ? 4.1495 2.0448 2.0637 -0.1141 -0.2935 -0.1077 44   TYR B CD2 
14553 C CE1 . TYR C 44   ? 4.0768 2.0956 2.0926 -0.1365 -0.2996 -0.1139 44   TYR B CE1 
14554 C CE2 . TYR C 44   ? 4.1679 2.0811 2.1016 -0.1288 -0.2815 -0.0995 44   TYR B CE2 
14555 C CZ  . TYR C 44   ? 4.1248 2.1003 2.1096 -0.1399 -0.2852 -0.1027 44   TYR B CZ  
14556 O OH  . TYR C 44   ? 4.1079 2.1014 2.1122 -0.1549 -0.2737 -0.0945 44   TYR B OH  
14557 N N   . GLY C 45   ? 4.1386 2.0125 1.9865 -0.1194 -0.3691 -0.1602 45   GLY B N   
14558 C CA  . GLY C 45   ? 4.2009 2.0330 2.0037 -0.1319 -0.3746 -0.1634 45   GLY B CA  
14559 C C   . GLY C 45   ? 4.1824 2.0461 2.0041 -0.1557 -0.3795 -0.1685 45   GLY B C   
14560 O O   . GLY C 45   ? 4.1139 2.0367 1.9812 -0.1654 -0.3904 -0.1766 45   GLY B O   
14561 N N   . TYR C 46   ? 4.2660 2.0887 2.0516 -0.1648 -0.3706 -0.1636 46   TYR B N   
14562 C CA  . TYR C 46   ? 4.3020 2.1467 2.0980 -0.1875 -0.3748 -0.1684 46   TYR B CA  
14563 C C   . TYR C 46   ? 4.2934 2.1720 2.1010 -0.2031 -0.4034 -0.1855 46   TYR B C   
14564 O O   . TYR C 46   ? 4.3368 2.2357 2.1575 -0.1968 -0.4196 -0.1933 46   TYR B O   
14565 C CB  . TYR C 46   ? 4.3973 2.1820 2.1428 -0.1929 -0.3610 -0.1608 46   TYR B CB  
14566 C CG  . TYR C 46   ? 4.5000 2.2183 2.1868 -0.1820 -0.3623 -0.1597 46   TYR B CG  
14567 C CD1 . TYR C 46   ? 4.5506 2.2537 2.2076 -0.1915 -0.3853 -0.1723 46   TYR B CD1 
14568 C CD2 . TYR C 46   ? 4.5382 2.2086 2.1997 -0.1624 -0.3409 -0.1456 46   TYR B CD2 
14569 C CE1 . TYR C 46   ? 4.6200 2.2610 2.2217 -0.1825 -0.3869 -0.1713 46   TYR B CE1 
14570 C CE2 . TYR C 46   ? 4.6059 2.2137 2.2128 -0.1523 -0.3416 -0.1447 46   TYR B CE2 
14571 C CZ  . TYR C 46   ? 4.6501 2.2430 2.2263 -0.1628 -0.3647 -0.1580 46   TYR B CZ  
14572 O OH  . TYR C 46   ? 4.7182 2.2473 2.2383 -0.1538 -0.3656 -0.1571 46   TYR B OH  
14573 N N   . THR C 47   ? 4.2308 2.1148 2.0339 -0.2232 -0.4089 -0.1903 47   THR B N   
14574 C CA  . THR C 47   ? 4.1665 2.0895 1.9883 -0.2406 -0.4345 -0.2048 47   THR B CA  
14575 C C   . THR C 47   ? 4.1606 2.0620 1.9522 -0.2396 -0.4569 -0.2133 47   THR B C   
14576 O O   . THR C 47   ? 4.1356 2.0779 1.9550 -0.2448 -0.4781 -0.2232 47   THR B O   
14577 C CB  . THR C 47   ? 4.8191 2.7385 2.6300 -0.2616 -0.4347 -0.2070 47   THR B CB  
14578 O OG1 . THR C 47   ? 4.7861 2.7201 2.6205 -0.2635 -0.4126 -0.1977 47   THR B OG1 
14579 C CG2 . THR C 47   ? 4.8020 2.7698 2.6416 -0.2793 -0.4601 -0.2208 47   THR B CG2 
14580 N N   . GLU C 48   ? 4.1891 2.0248 1.9233 -0.2334 -0.4515 -0.2085 48   GLU B N   
14581 C CA  . GLU C 48   ? 4.2024 2.0103 1.9007 -0.2346 -0.4722 -0.2155 48   GLU B CA  
14582 C C   . GLU C 48   ? 4.1296 1.9690 1.8567 -0.2218 -0.4849 -0.2199 48   GLU B C   
14583 O O   . GLU C 48   ? 4.1215 1.9421 1.8427 -0.2019 -0.4730 -0.2135 48   GLU B O   
14584 C CB  . GLU C 48   ? 4.2794 2.0085 1.9124 -0.2257 -0.4593 -0.2077 48   GLU B CB  
14585 C CG  . GLU C 48   ? 4.3317 2.0235 1.9186 -0.2307 -0.4804 -0.2143 48   GLU B CG  
14586 C CD  . GLU C 48   ? 4.3512 2.0344 1.9150 -0.2548 -0.4941 -0.2206 48   GLU B CD  
14587 O OE1 . GLU C 48   ? 4.3328 2.0295 1.9095 -0.2658 -0.4836 -0.2189 48   GLU B OE1 
14588 O OE2 . GLU C 48   ? 4.3919 2.0544 1.9242 -0.2632 -0.5156 -0.2268 48   GLU B OE2 
14589 N N   . ALA C 49   ? 4.0534 1.9399 1.8115 -0.2325 -0.5085 -0.2301 49   ALA B N   
14590 C CA  . ALA C 49   ? 3.9977 1.9086 1.7769 -0.2216 -0.5224 -0.2343 49   ALA B CA  
14591 C C   . ALA C 49   ? 4.0103 1.8607 1.7376 -0.2071 -0.5211 -0.2306 49   ALA B C   
14592 O O   . ALA C 49   ? 4.0786 1.8702 1.7531 -0.2093 -0.5134 -0.2263 49   ALA B O   
14593 C CB  . ALA C 49   ? 3.9731 1.9227 1.7734 -0.2378 -0.5503 -0.2444 49   ALA B CB  
14594 N N   . PHE C 50   ? 3.9767 1.8396 1.7179 -0.1921 -0.5276 -0.2320 50   PHE B N   
14595 C CA  . PHE C 50   ? 4.0282 1.8347 1.7203 -0.1789 -0.5289 -0.2295 50   PHE B CA  
14596 C C   . PHE C 50   ? 3.9413 1.7684 1.6533 -0.1635 -0.5390 -0.2322 50   PHE B C   
14597 O O   . PHE C 50   ? 3.8782 1.7410 1.6315 -0.1496 -0.5290 -0.2304 50   PHE B O   
14598 C CB  . PHE C 50   ? 4.1448 1.8942 1.7991 -0.1655 -0.5019 -0.2187 50   PHE B CB  
14599 C CG  . PHE C 50   ? 4.2276 1.9954 1.9143 -0.1447 -0.4819 -0.2116 50   PHE B CG  
14600 C CD1 . PHE C 50   ? 4.2826 2.0189 1.9505 -0.1227 -0.4747 -0.2070 50   PHE B CD1 
14601 C CD2 . PHE C 50   ? 4.2274 2.0429 1.9626 -0.1476 -0.4702 -0.2091 50   PHE B CD2 
14602 C CE1 . PHE C 50   ? 4.2815 2.0343 1.9788 -0.1037 -0.4566 -0.1998 50   PHE B CE1 
14603 C CE2 . PHE C 50   ? 4.2193 2.0509 1.9830 -0.1297 -0.4522 -0.2016 50   PHE B CE2 
14604 C CZ  . PHE C 50   ? 4.2412 2.0417 1.9862 -0.1076 -0.4455 -0.1969 50   PHE B CZ  
14605 N N   . ASP C 51   ? 3.9510 1.7537 1.6319 -0.1664 -0.5586 -0.2361 51   ASP B N   
14606 C CA  . ASP C 51   ? 3.9174 1.7394 1.6155 -0.1541 -0.5708 -0.2391 51   ASP B CA  
14607 C C   . ASP C 51   ? 3.8979 1.7054 1.5976 -0.1275 -0.5516 -0.2333 51   ASP B C   
14608 O O   . ASP C 51   ? 3.9270 1.6894 1.5963 -0.1179 -0.5305 -0.2258 51   ASP B O   
14609 C CB  . ASP C 51   ? 3.9500 1.7349 1.6032 -0.1616 -0.5928 -0.2421 51   ASP B CB  
14610 C CG  . ASP C 51   ? 3.8973 1.7269 1.5770 -0.1812 -0.6204 -0.2487 51   ASP B CG  
14611 O OD1 . ASP C 51   ? 3.8309 1.7180 1.5621 -0.1894 -0.6220 -0.2515 51   ASP B OD1 
14612 O OD2 . ASP C 51   ? 3.9332 1.7391 1.5818 -0.1887 -0.6406 -0.2505 51   ASP B OD2 
14613 N N   . ALA C 52   ? 3.8462 1.6918 1.5814 -0.1160 -0.5592 -0.2363 52   ALA B N   
14614 C CA  . ALA C 52   ? 3.7773 1.6208 1.5236 -0.0904 -0.5437 -0.2320 52   ALA B CA  
14615 C C   . ALA C 52   ? 3.7579 1.6200 1.5175 -0.0810 -0.5599 -0.2365 52   ALA B C   
14616 O O   . ALA C 52   ? 3.7168 1.6379 1.5251 -0.0858 -0.5713 -0.2415 52   ALA B O   
14617 C CB  . ALA C 52   ? 3.6953 1.5878 1.4945 -0.0851 -0.5269 -0.2294 52   ALA B CB  
14618 N N   . THR C 53   ? 3.7740 1.5852 1.4906 -0.0676 -0.5601 -0.2344 53   THR B N   
14619 C CA  . THR C 53   ? 3.7580 1.5813 1.4834 -0.0566 -0.5735 -0.2377 53   THR B CA  
14620 C C   . THR C 53   ? 3.6947 1.5026 1.4205 -0.0284 -0.5553 -0.2331 53   THR B C   
14621 O O   . THR C 53   ? 3.7221 1.4780 1.4110 -0.0174 -0.5375 -0.2266 53   THR B O   
14622 C CB  . THR C 53   ? 3.8504 1.6278 1.5241 -0.0657 -0.5934 -0.2398 53   THR B CB  
14623 O OG1 . THR C 53   ? 3.8631 1.6765 1.5552 -0.0885 -0.6176 -0.2450 53   THR B OG1 
14624 C CG2 . THR C 53   ? 3.8624 1.6252 1.5265 -0.0465 -0.5976 -0.2399 53   THR B CG2 
14625 N N   . ILE C 54   ? 3.6313 1.4835 1.3987 -0.0164 -0.5593 -0.2359 54   ILE B N   
14626 C CA  . ILE C 54   ? 3.5876 1.4301 1.3593 0.0105  -0.5426 -0.2319 54   ILE B CA  
14627 C C   . ILE C 54   ? 3.5717 1.4145 1.3399 0.0199  -0.5580 -0.2358 54   ILE B C   
14628 O O   . ILE C 54   ? 3.5248 1.3848 1.2965 0.0047  -0.5803 -0.2408 54   ILE B O   
14629 C CB  . ILE C 54   ? 3.5598 1.4610 1.3912 0.0182  -0.5290 -0.2310 54   ILE B CB  
14630 C CG1 . ILE C 54   ? 3.5509 1.4607 1.3923 0.0057  -0.5161 -0.2274 54   ILE B CG1 
14631 C CG2 . ILE C 54   ? 3.5456 1.4351 1.3800 0.0461  -0.5116 -0.2260 54   ILE B CG2 
14632 C CD1 . ILE C 54   ? 3.4912 1.4617 1.3918 0.0090  -0.5051 -0.2270 54   ILE B CD1 
14633 N N   . SER C 55   ? 3.5919 1.4160 1.3540 0.0449  -0.5461 -0.2328 55   SER B N   
14634 C CA  . SER C 55   ? 3.6428 1.4662 1.4021 0.0561  -0.5589 -0.2362 55   SER B CA  
14635 C C   . SER C 55   ? 3.6653 1.4648 1.4170 0.0855  -0.5418 -0.2320 55   SER B C   
14636 O O   . SER C 55   ? 3.6518 1.4258 1.3928 0.0969  -0.5204 -0.2254 55   SER B O   
14637 C CB  . SER C 55   ? 3.7112 1.4873 1.4178 0.0428  -0.5777 -0.2379 55   SER B CB  
14638 O OG  . SER C 55   ? 3.7629 1.4868 1.4232 0.0325  -0.5701 -0.2341 55   SER B OG  
14639 N N   . ILE C 56   ? 3.7316 1.5395 1.4896 0.0975  -0.5518 -0.2354 56   ILE B N   
14640 C CA  . ILE C 56   ? 3.8225 1.6179 1.5819 0.1263  -0.5376 -0.2326 56   ILE B CA  
14641 C C   . ILE C 56   ? 3.9247 1.6576 1.6296 0.1365  -0.5435 -0.2321 56   ILE B C   
14642 O O   . ILE C 56   ? 3.9223 1.6604 1.6219 0.1298  -0.5640 -0.2370 56   ILE B O   
14643 C CB  . ILE C 56   ? 3.8313 1.6931 1.6486 0.1346  -0.5423 -0.2372 56   ILE B CB  
14644 C CG1 . ILE C 56   ? 3.8626 1.7544 1.6923 0.1155  -0.5685 -0.2433 56   ILE B CG1 
14645 C CG2 . ILE C 56   ? 3.8290 1.7443 1.6985 0.1342  -0.5277 -0.2359 56   ILE B CG2 
14646 C CD1 . ILE C 56   ? 3.8331 1.8004 1.7281 0.1160  -0.5728 -0.2471 56   ILE B CD1 
14647 N N   . LYS C 57   ? 4.0233 1.6984 1.6897 0.1532  -0.5250 -0.2255 57   LYS B N   
14648 C CA  . LYS C 57   ? 4.1165 1.7208 1.7225 0.1616  -0.5277 -0.2241 57   LYS B CA  
14649 C C   . LYS C 57   ? 4.1498 1.7214 1.7443 0.1930  -0.5087 -0.2187 57   LYS B C   
14650 O O   . LYS C 57   ? 4.1392 1.7161 1.7514 0.2062  -0.4876 -0.2122 57   LYS B O   
14651 C CB  . LYS C 57   ? 4.1729 1.7174 1.7226 0.1441  -0.5271 -0.2208 57   LYS B CB  
14652 C CG  . LYS C 57   ? 4.1703 1.7375 1.7216 0.1130  -0.5495 -0.2265 57   LYS B CG  
14653 C CD  . LYS C 57   ? 4.2110 1.7222 1.7092 0.0952  -0.5469 -0.2232 57   LYS B CD  
14654 C CE  . LYS C 57   ? 4.2108 1.7498 1.7153 0.0646  -0.5697 -0.2286 57   LYS B CE  
14655 N NZ  . LYS C 57   ? 4.2681 1.7463 1.7125 0.0464  -0.5713 -0.2266 57   LYS B NZ  
14656 N N   . SER C 58   ? 4.1885 1.7235 1.7507 0.2038  -0.5167 -0.2208 58   SER B N   
14657 C CA  . SER C 58   ? 4.1809 1.7089 1.7497 0.2341  -0.5065 -0.2193 58   SER B CA  
14658 C C   . SER C 58   ? 4.2156 1.6735 1.7410 0.2559  -0.4845 -0.2103 58   SER B C   
14659 O O   . SER C 58   ? 4.2744 1.6649 1.7412 0.2547  -0.4864 -0.2089 58   SER B O   
14660 C CB  . SER C 58   ? 4.2242 1.7533 1.7845 0.2350  -0.5278 -0.2263 58   SER B CB  
14661 O OG  . SER C 58   ? 4.2964 1.7716 1.7995 0.2171  -0.5419 -0.2274 58   SER B OG  
14662 N N   . TYR C 59   ? 4.1571 1.6307 1.7117 0.2763  -0.4638 -0.2040 59   TYR B N   
14663 C CA  . TYR C 59   ? 4.1798 1.5921 1.7005 0.2972  -0.4403 -0.1930 59   TYR B CA  
14664 C C   . TYR C 59   ? 4.6168 1.9495 2.0699 0.2866  -0.4355 -0.1876 59   TYR B C   
14665 O O   . TYR C 59   ? 4.6430 1.9788 2.0896 0.2623  -0.4396 -0.1879 59   TYR B O   
14666 C CB  . TYR C 59   ? 4.1435 1.5469 1.6688 0.3284  -0.4335 -0.1921 59   TYR B CB  
14667 C CG  . TYR C 59   ? 4.1087 1.4896 1.6365 0.3508  -0.4064 -0.1793 59   TYR B CG  
14668 C CD1 . TYR C 59   ? 4.0828 1.4713 1.6228 0.3415  -0.3919 -0.1707 59   TYR B CD1 
14669 C CD2 . TYR C 59   ? 4.0963 1.4497 1.6159 0.3807  -0.3953 -0.1751 59   TYR B CD2 
14670 C CE1 . TYR C 59   ? 4.0620 1.4309 1.6057 0.3606  -0.3676 -0.1571 59   TYR B CE1 
14671 C CE2 . TYR C 59   ? 4.0754 1.4089 1.5989 0.4009  -0.3708 -0.1618 59   TYR B CE2 
14672 C CZ  . TYR C 59   ? 4.0595 1.4010 1.5952 0.3903  -0.3571 -0.1523 59   TYR B CZ  
14673 O OH  . TYR C 59   ? 4.0413 1.3636 1.5819 0.4095  -0.3331 -0.1373 59   TYR B OH  
14674 N N   . PRO C 60   ? 4.6315 1.8920 2.0338 0.3041  -0.4261 -0.1826 60   PRO B N   
14675 C CA  . PRO C 60   ? 4.6551 1.8435 1.9986 0.2934  -0.4162 -0.1754 60   PRO B CA  
14676 C C   . PRO C 60   ? 4.6378 1.7976 1.9370 0.2662  -0.4369 -0.1829 60   PRO B C   
14677 O O   . PRO C 60   ? 4.6743 1.7821 1.9290 0.2536  -0.4292 -0.1777 60   PRO B O   
14678 C CB  . PRO C 60   ? 4.6978 1.8165 2.0019 0.3215  -0.3973 -0.1665 60   PRO B CB  
14679 C CG  . PRO C 60   ? 4.6517 1.8149 2.0029 0.3478  -0.3951 -0.1679 60   PRO B CG  
14680 C CD  . PRO C 60   ? 4.6222 1.8578 2.0155 0.3334  -0.4203 -0.1814 60   PRO B CD  
14681 N N   . ASP C 61   ? 4.5913 1.7837 1.9021 0.2573  -0.4622 -0.1941 61   ASP B N   
14682 C CA  . ASP C 61   ? 4.6029 1.7763 1.8774 0.2298  -0.4844 -0.2007 61   ASP B CA  
14683 C C   . ASP C 61   ? 4.5370 1.7821 1.8573 0.2047  -0.5006 -0.2067 61   ASP B C   
14684 O O   . ASP C 61   ? 4.4840 1.7965 1.8566 0.2056  -0.5135 -0.2130 61   ASP B O   
14685 C CB  . ASP C 61   ? 4.6331 1.7955 1.8901 0.2344  -0.5038 -0.2078 61   ASP B CB  
14686 C CG  . ASP C 61   ? 4.5787 1.8247 1.9017 0.2389  -0.5187 -0.2152 61   ASP B CG  
14687 O OD1 . ASP C 61   ? 4.5915 1.8681 1.9234 0.2193  -0.5438 -0.2225 61   ASP B OD1 
14688 O OD2 . ASP C 61   ? 4.5224 1.8038 1.8891 0.2616  -0.5050 -0.2131 61   ASP B OD2 
14689 N N   . LYS C 62   ? 4.5612 1.7919 1.8625 0.1822  -0.4996 -0.2047 62   LYS B N   
14690 C CA  . LYS C 62   ? 4.5125 1.8085 1.8553 0.1577  -0.5151 -0.2103 62   LYS B CA  
14691 C C   . LYS C 62   ? 4.5470 1.8549 1.8797 0.1367  -0.5459 -0.2189 62   LYS B C   
14692 O O   . LYS C 62   ? 4.5790 1.8991 1.9082 0.1100  -0.5595 -0.2216 62   LYS B O   
14693 C CB  . LYS C 62   ? 4.4940 1.7759 1.8252 0.1413  -0.5029 -0.2051 62   LYS B CB  
14694 C CG  . LYS C 62   ? 4.3808 1.6998 1.7590 0.1537  -0.4806 -0.1985 62   LYS B CG  
14695 C CD  . LYS C 62   ? 4.3477 1.6242 1.6979 0.1482  -0.4595 -0.1889 62   LYS B CD  
14696 C CE  . LYS C 62   ? 4.2532 1.5547 1.6437 0.1669  -0.4353 -0.1798 62   LYS B CE  
14697 N NZ  . LYS C 62   ? 4.2476 1.5080 1.6143 0.1646  -0.4121 -0.1681 62   LYS B NZ  
14698 N N   . LYS C 63   ? 4.5190 1.8242 1.8482 0.1488  -0.5570 -0.2225 63   LYS B N   
14699 C CA  . LYS C 63   ? 4.5193 1.8344 1.8391 0.1305  -0.5865 -0.2289 63   LYS B CA  
14700 C C   . LYS C 63   ? 4.4370 1.8425 1.8265 0.1214  -0.6038 -0.2344 63   LYS B C   
14701 O O   . LYS C 63   ? 4.4334 1.8652 1.8318 0.0953  -0.6209 -0.2368 63   LYS B O   
14702 C CB  . LYS C 63   ? 4.5678 1.8372 1.8501 0.1456  -0.5918 -0.2298 63   LYS B CB  
14703 C CG  . LYS C 63   ? 4.6708 1.8429 1.8748 0.1498  -0.5789 -0.2248 63   LYS B CG  
14704 C CD  . LYS C 63   ? 4.7589 1.8907 1.9137 0.1194  -0.5882 -0.2244 63   LYS B CD  
14705 C CE  . LYS C 63   ? 4.8077 1.9404 1.9429 0.0971  -0.6199 -0.2298 63   LYS B CE  
14706 N NZ  . LYS C 63   ? 4.8572 1.9680 1.9579 0.0654  -0.6310 -0.2298 63   LYS B NZ  
14707 N N   . PHE C 64   ? 4.3507 1.8028 1.7892 0.1427  -0.5989 -0.2358 64   PHE B N   
14708 C CA  . PHE C 64   ? 4.2585 1.7952 1.7642 0.1354  -0.6123 -0.2402 64   PHE B CA  
14709 C C   . PHE C 64   ? 4.2094 1.7899 1.7543 0.1250  -0.6028 -0.2393 64   PHE B C   
14710 O O   . PHE C 64   ? 4.2081 1.7788 1.7571 0.1384  -0.5795 -0.2351 64   PHE B O   
14711 C CB  . PHE C 64   ? 4.1604 1.7339 1.7075 0.1616  -0.6069 -0.2418 64   PHE B CB  
14712 C CG  . PHE C 64   ? 4.1198 1.7104 1.6728 0.1592  -0.6297 -0.2456 64   PHE B CG  
14713 C CD1 . PHE C 64   ? 4.1258 1.6711 1.6435 0.1764  -0.6303 -0.2456 64   PHE B CD1 
14714 C CD2 . PHE C 64   ? 4.0710 1.7234 1.6664 0.1399  -0.6502 -0.2485 64   PHE B CD2 
14715 C CE1 . PHE C 64   ? 4.1039 1.6664 1.6285 0.1737  -0.6514 -0.2485 64   PHE B CE1 
14716 C CE2 . PHE C 64   ? 4.0502 1.7200 1.6536 0.1373  -0.6709 -0.2504 64   PHE B CE2 
14717 C CZ  . PHE C 64   ? 4.0721 1.6974 1.6401 0.1539  -0.6718 -0.2504 64   PHE B CZ  
14718 N N   . SER C 65   ? 4.2032 1.8307 1.7765 0.1008  -0.6209 -0.2424 65   SER B N   
14719 C CA  . SER C 65   ? 4.1779 1.8572 1.7971 0.0906  -0.6139 -0.2425 65   SER B CA  
14720 C C   . SER C 65   ? 4.1219 1.8800 1.8034 0.0816  -0.6300 -0.2466 65   SER B C   
14721 O O   . SER C 65   ? 4.1501 1.9248 1.8336 0.0584  -0.6518 -0.2484 65   SER B O   
14722 C CB  . SER C 65   ? 4.2475 1.8971 1.8333 0.0669  -0.6156 -0.2410 65   SER B CB  
14723 O OG  . SER C 65   ? 4.2576 1.9562 1.8741 0.0420  -0.6345 -0.2442 65   SER B OG  
14724 N N   . TYR C 66   ? 4.0294 1.8351 1.7619 0.1001  -0.6183 -0.2473 66   TYR B N   
14725 C CA  . TYR C 66   ? 3.9130 1.7884 1.7032 0.0977  -0.6305 -0.2505 66   TYR B CA  
14726 C C   . TYR C 66   ? 3.9062 1.8265 1.7277 0.0716  -0.6410 -0.2517 66   TYR B C   
14727 O O   . TYR C 66   ? 3.8906 1.8391 1.7278 0.0554  -0.6627 -0.2529 66   TYR B O   
14728 C CB  . TYR C 66   ? 3.7642 1.6765 1.5990 0.1230  -0.6118 -0.2508 66   TYR B CB  
14729 C CG  . TYR C 66   ? 3.6952 1.5556 1.4952 0.1496  -0.5957 -0.2483 66   TYR B CG  
14730 C CD1 . TYR C 66   ? 3.6558 1.5068 1.4495 0.1667  -0.6011 -0.2497 66   TYR B CD1 
14731 C CD2 . TYR C 66   ? 3.6614 1.4811 1.4347 0.1576  -0.5752 -0.2439 66   TYR B CD2 
14732 C CE1 . TYR C 66   ? 3.6349 1.4369 1.3965 0.1917  -0.5863 -0.2473 66   TYR B CE1 
14733 C CE2 . TYR C 66   ? 3.6488 1.4197 1.3909 0.1823  -0.5600 -0.2403 66   TYR B CE2 
14734 C CZ  . TYR C 66   ? 3.6228 1.3845 1.3588 0.1996  -0.5656 -0.2424 66   TYR B CZ  
14735 O OH  . TYR C 66   ? 3.5943 1.3070 1.2999 0.2248  -0.5504 -0.2388 66   TYR B OH  
14736 N N   . SER C 67   ? 3.8951 1.8191 1.7236 0.0671  -0.6260 -0.2506 67   SER B N   
14737 C CA  . SER C 67   ? 3.8602 1.8210 1.7140 0.0426  -0.6342 -0.2518 67   SER B CA  
14738 C C   . SER C 67   ? 3.8379 1.7743 1.6730 0.0364  -0.6187 -0.2497 67   SER B C   
14739 O O   . SER C 67   ? 3.8374 1.7302 1.6426 0.0516  -0.6004 -0.2463 67   SER B O   
14740 C CB  . SER C 67   ? 3.7950 1.8336 1.7199 0.0431  -0.6339 -0.2539 67   SER B CB  
14741 O OG  . SER C 67   ? 3.7462 1.8022 1.6979 0.0652  -0.6114 -0.2534 67   SER B OG  
14742 N N   . SER C 68   ? 3.8311 1.7975 1.6862 0.0140  -0.6261 -0.2510 68   SER B N   
14743 C CA  . SER C 68   ? 3.8767 1.8189 1.7100 0.0022  -0.6165 -0.2492 68   SER B CA  
14744 C C   . SER C 68   ? 3.8780 1.8754 1.7555 -0.0181 -0.6223 -0.2515 68   SER B C   
14745 O O   . SER C 68   ? 3.8009 1.8561 1.7293 -0.0199 -0.6294 -0.2538 68   SER B O   
14746 C CB  . SER C 68   ? 3.9687 1.8451 1.7358 -0.0098 -0.6271 -0.2480 68   SER B CB  
14747 O OG  . SER C 68   ? 4.0097 1.8942 1.7721 -0.0251 -0.6537 -0.2503 68   SER B OG  
14748 N N   . GLY C 69   ? 3.9591 1.9380 1.8174 -0.0333 -0.6185 -0.2505 69   GLY B N   
14749 C CA  . GLY C 69   ? 3.9946 2.0217 1.8913 -0.0530 -0.6239 -0.2528 69   GLY B CA  
14750 C C   . GLY C 69   ? 4.0434 2.0407 1.9091 -0.0705 -0.6218 -0.2518 69   GLY B C   
14751 O O   . GLY C 69   ? 4.0655 2.0267 1.9056 -0.0630 -0.6027 -0.2482 69   GLY B O   
14752 N N   . HIS C 70   ? 4.0843 2.0975 1.9536 -0.0937 -0.6412 -0.2543 70   HIS B N   
14753 C CA  . HIS C 70   ? 4.1375 2.1253 1.9781 -0.1126 -0.6420 -0.2540 70   HIS B CA  
14754 C C   . HIS C 70   ? 4.0547 2.0934 1.9433 -0.1220 -0.6340 -0.2555 70   HIS B C   
14755 O O   . HIS C 70   ? 4.0128 2.0904 1.9297 -0.1398 -0.6494 -0.2584 70   HIS B O   
14756 C CB  . HIS C 70   ? 4.2637 2.2383 2.0788 -0.1335 -0.6690 -0.2556 70   HIS B CB  
14757 C CG  . HIS C 70   ? 4.4194 2.3352 2.1752 -0.1467 -0.6696 -0.2543 70   HIS B CG  
14758 N ND1 . HIS C 70   ? 4.5068 2.3534 2.2015 -0.1381 -0.6635 -0.2516 70   HIS B ND1 
14759 C CD2 . HIS C 70   ? 4.4723 2.3873 2.2199 -0.1682 -0.6753 -0.2554 70   HIS B CD2 
14760 C CE1 . HIS C 70   ? 4.5755 2.3804 2.2261 -0.1539 -0.6645 -0.2509 70   HIS B CE1 
14761 N NE2 . HIS C 70   ? 4.5577 2.4037 2.2396 -0.1723 -0.6719 -0.2533 70   HIS B NE2 
14762 N N   . VAL C 71   ? 4.0235 2.0608 1.9208 -0.1104 -0.6099 -0.2529 71   VAL B N   
14763 C CA  . VAL C 71   ? 3.9582 2.0443 1.9027 -0.1172 -0.6000 -0.2538 71   VAL B CA  
14764 C C   . VAL C 71   ? 3.9876 2.0475 1.9090 -0.1275 -0.5879 -0.2513 71   VAL B C   
14765 O O   . VAL C 71   ? 3.9765 2.0072 1.8804 -0.1156 -0.5670 -0.2460 71   VAL B O   
14766 C CB  . VAL C 71   ? 3.8865 2.0035 1.8697 -0.0973 -0.5826 -0.2523 71   VAL B CB  
14767 C CG1 . VAL C 71   ? 3.8532 1.9898 1.8537 -0.0858 -0.5936 -0.2544 71   VAL B CG1 
14768 C CG2 . VAL C 71   ? 3.8838 1.9557 1.8363 -0.0799 -0.5601 -0.2459 71   VAL B CG2 
14769 N N   . HIS C 72   ? 4.0352 2.1069 1.9581 -0.1499 -0.6011 -0.2545 72   HIS B N   
14770 C CA  . HIS C 72   ? 4.1182 2.1582 2.0108 -0.1619 -0.5932 -0.2525 72   HIS B CA  
14771 C C   . HIS C 72   ? 4.0709 2.1478 2.0017 -0.1676 -0.5783 -0.2520 72   HIS B C   
14772 O O   . HIS C 72   ? 4.0463 2.1670 2.0116 -0.1834 -0.5884 -0.2564 72   HIS B O   
14773 C CB  . HIS C 72   ? 4.2297 2.2571 2.0976 -0.1841 -0.6155 -0.2560 72   HIS B CB  
14774 C CG  . HIS C 72   ? 4.3254 2.3373 2.1762 -0.1998 -0.6090 -0.2554 72   HIS B CG  
14775 N ND1 . HIS C 72   ? 4.4083 2.3573 2.2030 -0.1993 -0.5982 -0.2513 72   HIS B ND1 
14776 C CD2 . HIS C 72   ? 4.3295 2.3801 2.2125 -0.2160 -0.6108 -0.2583 72   HIS B CD2 
14777 C CE1 . HIS C 72   ? 4.4276 2.3783 2.2209 -0.2148 -0.5936 -0.2515 72   HIS B CE1 
14778 N NE2 . HIS C 72   ? 4.3803 2.3926 2.2268 -0.2250 -0.6016 -0.2560 72   HIS B NE2 
14779 N N   . LEU C 73   ? 4.0850 2.1429 2.0090 -0.1554 -0.5546 -0.2458 73   LEU B N   
14780 C CA  . LEU C 73   ? 4.0674 2.1561 2.0239 -0.1615 -0.5396 -0.2440 73   LEU B CA  
14781 C C   . LEU C 73   ? 4.1552 2.2277 2.0910 -0.1815 -0.5414 -0.2445 73   LEU B C   
14782 O O   . LEU C 73   ? 4.1829 2.2204 2.0785 -0.1909 -0.5546 -0.2464 73   LEU B O   
14783 C CB  . LEU C 73   ? 4.0209 2.0927 1.9757 -0.1431 -0.5140 -0.2353 73   LEU B CB  
14784 C CG  . LEU C 73   ? 4.0348 2.0417 1.9362 -0.1272 -0.5070 -0.2294 73   LEU B CG  
14785 C CD1 . LEU C 73   ? 4.0182 1.9977 1.9084 -0.1160 -0.4804 -0.2185 73   LEU B CD1 
14786 C CD2 . LEU C 73   ? 4.0226 2.0342 1.9294 -0.1104 -0.5148 -0.2318 73   LEU B CD2 
14787 N N   . SER C 74   ? 4.1866 2.2851 2.1499 -0.1883 -0.5281 -0.2425 74   SER B N   
14788 C CA  . SER C 74   ? 4.2516 2.3426 2.2031 -0.2071 -0.5278 -0.2431 74   SER B CA  
14789 C C   . SER C 74   ? 4.2627 2.3906 2.2546 -0.2100 -0.5107 -0.2400 74   SER B C   
14790 O O   . SER C 74   ? 4.2558 2.4131 2.2817 -0.1985 -0.5015 -0.2380 74   SER B O   
14791 C CB  . SER C 74   ? 4.2472 2.3626 2.2080 -0.2264 -0.5529 -0.2518 74   SER B CB  
14792 O OG  . SER C 74   ? 4.1771 2.3566 2.1959 -0.2308 -0.5593 -0.2567 74   SER B OG  
14793 N N   . SER C 75   ? 4.2944 2.4209 2.2825 -0.2256 -0.5065 -0.2395 75   SER B N   
14794 C CA  . SER C 75   ? 4.3079 2.4727 2.3361 -0.2314 -0.4923 -0.2370 75   SER B CA  
14795 C C   . SER C 75   ? 4.2561 2.4860 2.3401 -0.2387 -0.5036 -0.2449 75   SER B C   
14796 O O   . SER C 75   ? 4.2086 2.4756 2.3308 -0.2423 -0.4928 -0.2436 75   SER B O   
14797 C CB  . SER C 75   ? 4.3710 2.5213 2.3832 -0.2478 -0.4870 -0.2356 75   SER B CB  
14798 O OG  . SER C 75   ? 4.4275 2.5319 2.4072 -0.2398 -0.4655 -0.2245 75   SER B OG  
14799 N N   . GLU C 76   ? 4.2703 2.5126 2.3580 -0.2413 -0.5250 -0.2524 76   GLU B N   
14800 C CA  . GLU C 76   ? 4.1995 2.5002 2.3379 -0.2480 -0.5369 -0.2593 76   GLU B CA  
14801 C C   . GLU C 76   ? 4.0813 2.4051 2.2479 -0.2311 -0.5302 -0.2580 76   GLU B C   
14802 O O   . GLU C 76   ? 4.0528 2.4245 2.2658 -0.2336 -0.5273 -0.2604 76   GLU B O   
14803 C CB  . GLU C 76   ? 4.2494 2.5515 2.3791 -0.2583 -0.5627 -0.2659 76   GLU B CB  
14804 C CG  . GLU C 76   ? 4.2191 2.5761 2.3979 -0.2626 -0.5761 -0.2716 76   GLU B CG  
14805 C CD  . GLU C 76   ? 4.2443 2.5971 2.4109 -0.2702 -0.6016 -0.2753 76   GLU B CD  
14806 O OE1 . GLU C 76   ? 4.2903 2.5952 2.4083 -0.2676 -0.6082 -0.2734 76   GLU B OE1 
14807 O OE2 . GLU C 76   ? 4.2164 2.6129 2.4217 -0.2790 -0.6147 -0.2793 76   GLU B OE2 
14808 N N   . ASN C 77   ? 4.0026 2.2903 2.1390 -0.2141 -0.5278 -0.2542 77   ASN B N   
14809 C CA  . ASN C 77   ? 3.8582 2.1583 2.0127 -0.1954 -0.5201 -0.2520 77   ASN B CA  
14810 C C   . ASN C 77   ? 3.7122 1.9906 1.8570 -0.1829 -0.4958 -0.2427 77   ASN B C   
14811 O O   . ASN C 77   ? 3.6469 1.9121 1.7861 -0.1642 -0.4875 -0.2384 77   ASN B O   
14812 C CB  . ASN C 77   ? 3.9681 2.2396 2.0938 -0.1840 -0.5329 -0.2532 77   ASN B CB  
14813 C CG  . ASN C 77   ? 4.0216 2.3233 2.1786 -0.1695 -0.5336 -0.2546 77   ASN B CG  
14814 O OD1 . ASN C 77   ? 4.0186 2.3554 2.2132 -0.1651 -0.5212 -0.2536 77   ASN B OD1 
14815 N ND2 . ASN C 77   ? 4.0674 2.3547 2.2078 -0.1625 -0.5478 -0.2566 77   ASN B ND2 
14816 N N   . LYS C 78   ? 3.6257 1.8999 1.7684 -0.1934 -0.4846 -0.2387 78   LYS B N   
14817 C CA  . LYS C 78   ? 3.5047 1.7547 1.6357 -0.1837 -0.4616 -0.2277 78   LYS B CA  
14818 C C   . LYS C 78   ? 3.4809 1.6787 1.5706 -0.1640 -0.4553 -0.2211 78   LYS B C   
14819 O O   . LYS C 78   ? 3.4453 1.6292 1.5329 -0.1499 -0.4372 -0.2114 78   LYS B O   
14820 C CB  . LYS C 78   ? 3.3835 1.6761 1.5595 -0.1801 -0.4489 -0.2248 78   LYS B CB  
14821 C CG  . LYS C 78   ? 3.2036 1.5451 1.4195 -0.1994 -0.4529 -0.2306 78   LYS B CG  
14822 C CD  . LYS C 78   ? 3.1154 1.4411 1.3149 -0.2148 -0.4500 -0.2286 78   LYS B CD  
14823 C CE  . LYS C 78   ? 2.9959 1.3705 1.2358 -0.2337 -0.4538 -0.2346 78   LYS B CE  
14824 N NZ  . LYS C 78   ? 2.9913 1.3538 1.2149 -0.2507 -0.4583 -0.2365 78   LYS B NZ  
14825 N N   . PHE C 79   ? 3.4778 1.6462 1.5342 -0.1635 -0.4708 -0.2259 79   PHE B N   
14826 C CA  . PHE C 79   ? 3.4948 1.6101 1.5079 -0.1461 -0.4667 -0.2207 79   PHE B CA  
14827 C C   . PHE C 79   ? 3.5028 1.6347 1.5383 -0.1264 -0.4600 -0.2184 79   PHE B C   
14828 O O   . PHE C 79   ? 3.5114 1.6245 1.5412 -0.1124 -0.4410 -0.2085 79   PHE B O   
14829 C CB  . PHE C 79   ? 3.5187 1.5841 1.4950 -0.1433 -0.4478 -0.2098 79   PHE B CB  
14830 C CG  . PHE C 79   ? 3.5744 1.6133 1.5191 -0.1611 -0.4539 -0.2120 79   PHE B CG  
14831 C CD1 . PHE C 79   ? 3.5685 1.6159 1.5225 -0.1745 -0.4432 -0.2081 79   PHE B CD1 
14832 C CD2 . PHE C 79   ? 3.6340 1.6400 1.5399 -0.1651 -0.4708 -0.2177 79   PHE B CD2 
14833 C CE1 . PHE C 79   ? 3.5948 1.6186 1.5202 -0.1906 -0.4483 -0.2103 79   PHE B CE1 
14834 C CE2 . PHE C 79   ? 3.6637 1.6449 1.5395 -0.1819 -0.4764 -0.2196 79   PHE B CE2 
14835 C CZ  . PHE C 79   ? 3.6474 1.6378 1.5333 -0.1943 -0.4648 -0.2162 79   PHE B CZ  
14836 N N   . GLN C 80   ? 3.5181 1.6865 1.5807 -0.1259 -0.4753 -0.2269 80   GLN B N   
14837 C CA  . GLN C 80   ? 3.5111 1.7018 1.5990 -0.1083 -0.4713 -0.2266 80   GLN B CA  
14838 C C   . GLN C 80   ? 3.5064 1.7190 1.6061 -0.1089 -0.4922 -0.2358 80   GLN B C   
14839 O O   . GLN C 80   ? 3.5072 1.7446 1.6207 -0.1262 -0.5080 -0.2426 80   GLN B O   
14840 C CB  . GLN C 80   ? 3.4914 1.7316 1.6282 -0.1111 -0.4594 -0.2251 80   GLN B CB  
14841 C CG  . GLN C 80   ? 3.5044 1.7336 1.6382 -0.1155 -0.4406 -0.2157 80   GLN B CG  
14842 C CD  . GLN C 80   ? 3.4633 1.7314 1.6384 -0.1122 -0.4264 -0.2116 80   GLN B CD  
14843 O OE1 . GLN C 80   ? 3.4357 1.7510 1.6496 -0.1168 -0.4324 -0.2184 80   GLN B OE1 
14844 N NE2 . GLN C 80   ? 3.4634 1.7108 1.6298 -0.1047 -0.4072 -0.1994 80   GLN B NE2 
14845 N N   . ASN C 81   ? 3.4971 1.7021 1.5933 -0.0902 -0.4925 -0.2354 81   ASN B N   
14846 C CA  . ASN C 81   ? 3.5066 1.7290 1.6116 -0.0904 -0.5124 -0.2427 81   ASN B CA  
14847 C C   . ASN C 81   ? 3.4543 1.6778 1.5655 -0.0681 -0.5090 -0.2418 81   ASN B C   
14848 O O   . ASN C 81   ? 3.4156 1.6225 1.5208 -0.0513 -0.4917 -0.2356 81   ASN B O   
14849 C CB  . ASN C 81   ? 3.6081 1.7910 1.6691 -0.1002 -0.5295 -0.2450 81   ASN B CB  
14850 C CG  . ASN C 81   ? 3.6387 1.8563 1.7210 -0.1178 -0.5521 -0.2523 81   ASN B CG  
14851 O OD1 . ASN C 81   ? 3.6111 1.8727 1.7330 -0.1157 -0.5587 -0.2559 81   ASN B OD1 
14852 N ND2 . ASN C 81   ? 3.6907 1.8879 1.7468 -0.1354 -0.5636 -0.2539 81   ASN B ND2 
14853 N N   . SER C 82   ? 3.4414 1.6849 1.5653 -0.0677 -0.5256 -0.2475 82   SER B N   
14854 C CA  . SER C 82   ? 3.4438 1.6956 1.5799 -0.0474 -0.5223 -0.2473 82   SER B CA  
14855 C C   . SER C 82   ? 3.4859 1.7263 1.6061 -0.0444 -0.5414 -0.2508 82   SER B C   
14856 O O   . SER C 82   ? 3.5264 1.7730 1.6439 -0.0612 -0.5600 -0.2544 82   SER B O   
14857 C CB  . SER C 82   ? 3.3941 1.7056 1.5866 -0.0471 -0.5157 -0.2496 82   SER B CB  
14858 O OG  . SER C 82   ? 3.3840 1.6939 1.5839 -0.0300 -0.4953 -0.2444 82   SER B OG  
14859 N N   . ALA C 83   ? 3.4907 1.7144 1.6007 -0.0233 -0.5372 -0.2492 83   ALA B N   
14860 C CA  . ALA C 83   ? 3.5244 1.7329 1.6159 -0.0194 -0.5548 -0.2516 83   ALA B CA  
14861 C C   . ALA C 83   ? 3.4990 1.7272 1.6134 0.0016  -0.5503 -0.2521 83   ALA B C   
14862 O O   . ALA C 83   ? 3.5235 1.7456 1.6408 0.0194  -0.5320 -0.2487 83   ALA B O   
14863 C CB  . ALA C 83   ? 3.5628 1.7030 1.5918 -0.0167 -0.5570 -0.2486 83   ALA B CB  
14864 N N   . ILE C 84   ? 3.4815 1.7345 1.6133 -0.0009 -0.5671 -0.2556 84   ILE B N   
14865 C CA  . ILE C 84   ? 3.4345 1.7021 1.5837 0.0191  -0.5646 -0.2561 84   ILE B CA  
14866 C C   . ILE C 84   ? 3.4657 1.6846 1.5695 0.0301  -0.5743 -0.2552 84   ILE B C   
14867 O O   . ILE C 84   ? 3.4733 1.6979 1.5762 0.0241  -0.5935 -0.2570 84   ILE B O   
14868 C CB  . ILE C 84   ? 4.1418 2.4720 2.3454 0.0129  -0.5733 -0.2593 84   ILE B CB  
14869 C CG1 . ILE C 84   ? 4.1585 2.4955 2.3595 -0.0081 -0.5977 -0.2606 84   ILE B CG1 
14870 C CG2 . ILE C 84   ? 4.0936 2.4694 2.3420 0.0074  -0.5588 -0.2600 84   ILE B CG2 
14871 C CD1 . ILE C 84   ? 4.1204 2.5110 2.3696 -0.0113 -0.6076 -0.2617 84   ILE B CD1 
14872 N N   . LEU C 85   ? 3.4707 1.6405 1.5367 0.0456  -0.5606 -0.2516 85   LEU B N   
14873 C CA  . LEU C 85   ? 3.4561 1.5792 1.4816 0.0611  -0.5647 -0.2505 85   LEU B CA  
14874 C C   . LEU C 85   ? 3.3659 1.5248 1.4266 0.0777  -0.5644 -0.2525 85   LEU B C   
14875 O O   . LEU C 85   ? 3.3126 1.5279 1.4245 0.0754  -0.5611 -0.2544 85   LEU B O   
14876 C CB  . LEU C 85   ? 3.4764 1.5465 1.4640 0.0772  -0.5455 -0.2451 85   LEU B CB  
14877 C CG  . LEU C 85   ? 3.5071 1.5428 1.4622 0.0613  -0.5423 -0.2421 85   LEU B CG  
14878 C CD1 . LEU C 85   ? 3.5461 1.5749 1.4824 0.0387  -0.5656 -0.2459 85   LEU B CD1 
14879 C CD2 . LEU C 85   ? 3.4607 1.5337 1.4518 0.0526  -0.5294 -0.2408 85   LEU B CD2 
14880 N N   . THR C 86   ? 3.3149 1.4413 1.3489 0.0947  -0.5668 -0.2520 86   THR B N   
14881 C CA  . THR C 86   ? 3.2536 1.4149 1.3220 0.1115  -0.5654 -0.2538 86   THR B CA  
14882 C C   . THR C 86   ? 3.2446 1.3674 1.2794 0.1272  -0.5727 -0.2538 86   THR B C   
14883 O O   . THR C 86   ? 3.2736 1.3849 1.2904 0.1168  -0.5929 -0.2550 86   THR B O   
14884 C CB  . THR C 86   ? 3.0220 1.2489 1.1436 0.0966  -0.5772 -0.2570 86   THR B CB  
14885 O OG1 . THR C 86   ? 2.9815 1.2527 1.1486 0.1125  -0.5654 -0.2580 86   THR B OG1 
14886 C CG2 . THR C 86   ? 3.0518 1.2759 1.1623 0.0846  -0.6023 -0.2580 86   THR B CG2 
14887 N N   . ILE C 87   ? 3.2416 1.3437 1.2677 0.1522  -0.5558 -0.2517 87   ILE B N   
14888 C CA  . ILE C 87   ? 3.2700 1.3351 1.2661 0.1708  -0.5590 -0.2516 87   ILE B CA  
14889 C C   . ILE C 87   ? 3.4118 1.5234 1.4478 0.1790  -0.5666 -0.2550 87   ILE B C   
14890 O O   . ILE C 87   ? 3.4415 1.5883 1.5151 0.1945  -0.5526 -0.2555 87   ILE B O   
14891 C CB  . ILE C 87   ? 3.0957 1.1286 1.0758 0.1961  -0.5368 -0.2476 87   ILE B CB  
14892 C CG1 . ILE C 87   ? 3.0636 1.0594 1.0148 0.1894  -0.5246 -0.2425 87   ILE B CG1 
14893 C CG2 . ILE C 87   ? 3.0602 1.0472 1.0031 0.2149  -0.5401 -0.2474 87   ILE B CG2 
14894 C CD1 . ILE C 87   ? 3.0515 1.0037 0.9777 0.2133  -0.5044 -0.2363 87   ILE B CD1 
14895 N N   . GLN C 88   ? 3.5590 1.6713 1.5874 0.1683  -0.5883 -0.2567 88   GLN B N   
14896 C CA  . GLN C 88   ? 3.6431 1.7961 1.7071 0.1765  -0.5959 -0.2587 88   GLN B CA  
14897 C C   . GLN C 88   ? 3.7513 1.8659 1.7868 0.2015  -0.5920 -0.2587 88   GLN B C   
14898 O O   . GLN C 88   ? 3.8096 1.8703 1.8029 0.2129  -0.5812 -0.2568 88   GLN B O   
14899 C CB  . GLN C 88   ? 3.6524 1.8227 1.7214 0.1538  -0.6214 -0.2588 88   GLN B CB  
14900 C CG  . GLN C 88   ? 3.6628 1.8603 1.7505 0.1279  -0.6276 -0.2584 88   GLN B CG  
14901 C CD  . GLN C 88   ? 3.6387 1.8946 1.7743 0.1144  -0.6425 -0.2580 88   GLN B CD  
14902 O OE1 . GLN C 88   ? 3.6601 1.9334 1.8053 0.0908  -0.6549 -0.2569 88   GLN B OE1 
14903 N NE2 . GLN C 88   ? 3.6013 1.8885 1.7687 0.1298  -0.6409 -0.2582 88   GLN B NE2 
14904 N N   . PRO C 89   ? 3.8338 1.9769 1.8941 0.2107  -0.5997 -0.2603 89   PRO B N   
14905 C CA  . PRO C 89   ? 3.8759 1.9855 1.9099 0.2315  -0.6016 -0.2607 89   PRO B CA  
14906 C C   . PRO C 89   ? 3.8979 1.9399 1.8668 0.2250  -0.6170 -0.2597 89   PRO B C   
14907 O O   . PRO C 89   ? 3.8730 1.9148 1.8317 0.2038  -0.6388 -0.2591 89   PRO B O   
14908 C CB  . PRO C 89   ? 3.8529 2.0206 1.9367 0.2342  -0.6100 -0.2621 89   PRO B CB  
14909 C CG  . PRO C 89   ? 3.7926 2.0223 1.9334 0.2290  -0.5982 -0.2627 89   PRO B CG  
14910 C CD  . PRO C 89   ? 3.7858 2.0024 1.9111 0.2073  -0.5992 -0.2615 89   PRO B CD  
14911 N N   . LYS C 90   ? 4.0039 1.9881 1.9292 0.2438  -0.6051 -0.2587 90   LYS B N   
14912 C CA  . LYS C 90   ? 4.1071 2.0211 1.9674 0.2411  -0.6155 -0.2577 90   LYS B CA  
14913 C C   . LYS C 90   ? 4.2730 2.1557 2.1144 0.2694  -0.6084 -0.2582 90   LYS B C   
14914 O O   . LYS C 90   ? 4.2627 2.1523 2.1065 0.2724  -0.6222 -0.2599 90   LYS B O   
14915 C CB  . LYS C 90   ? 4.0124 1.8726 1.8272 0.2336  -0.6061 -0.2548 90   LYS B CB  
14916 C CG  . LYS C 90   ? 3.8816 1.7673 1.7106 0.2061  -0.6125 -0.2544 90   LYS B CG  
14917 C CD  . LYS C 90   ? 3.8129 1.7060 1.6346 0.1811  -0.6398 -0.2553 90   LYS B CD  
14918 C CE  . LYS C 90   ? 3.7538 1.6868 1.6036 0.1555  -0.6461 -0.2552 90   LYS B CE  
14919 N NZ  . LYS C 90   ? 3.8043 1.7044 1.6129 0.1290  -0.6665 -0.2541 90   LYS B NZ  
14920 N N   . GLN C 91   ? 4.4560 2.3048 2.2797 0.2902  -0.5866 -0.2561 91   GLN B N   
14921 C CA  . GLN C 91   ? 4.6704 2.4916 2.4801 0.3196  -0.5773 -0.2563 91   GLN B CA  
14922 C C   . GLN C 91   ? 4.8169 2.7014 2.6858 0.3371  -0.5724 -0.2592 91   GLN B C   
14923 O O   . GLN C 91   ? 4.7862 2.7081 2.6942 0.3463  -0.5557 -0.2586 91   GLN B O   
14924 C CB  . GLN C 91   ? 4.7202 2.4897 2.4982 0.3373  -0.5545 -0.2516 91   GLN B CB  
14925 C CG  . GLN C 91   ? 4.8315 2.5208 2.5390 0.3299  -0.5573 -0.2485 91   GLN B CG  
14926 C CD  . GLN C 91   ? 4.9088 2.5725 2.5839 0.3206  -0.5798 -0.2517 91   GLN B CD  
14927 O OE1 . GLN C 91   ? 4.9394 2.6160 2.6119 0.2937  -0.5995 -0.2532 91   GLN B OE1 
14928 N NE2 . GLN C 91   ? 4.9344 2.5613 2.5844 0.3423  -0.5776 -0.2521 91   GLN B NE2 
14929 N N   . LEU C 92   ? 5.0064 2.9018 2.8807 0.3411  -0.5868 -0.2620 92   LEU B N   
14930 C CA  . LEU C 92   ? 5.1438 3.0958 3.0713 0.3586  -0.5825 -0.2648 92   LEU B CA  
14931 C C   . LEU C 92   ? 5.2680 3.1912 3.1806 0.3904  -0.5730 -0.2658 92   LEU B C   
14932 O O   . LEU C 92   ? 5.2335 3.2014 3.1890 0.4072  -0.5674 -0.2681 92   LEU B O   
14933 C CB  . LEU C 92   ? 5.1783 3.1784 3.1371 0.3411  -0.6044 -0.2664 92   LEU B CB  
14934 C CG  . LEU C 92   ? 5.2008 3.2533 3.1974 0.3138  -0.6126 -0.2656 92   LEU B CG  
14935 C CD1 . LEU C 92   ? 5.2097 3.2974 3.2282 0.2978  -0.6358 -0.2651 92   LEU B CD1 
14936 C CD2 . LEU C 92   ? 5.1524 3.2614 3.2046 0.3217  -0.5935 -0.2664 92   LEU B CD2 
14937 N N   . PRO C 93   ? 5.4351 3.2832 3.2872 0.3991  -0.5704 -0.2638 93   PRO B N   
14938 C CA  . PRO C 93   ? 5.5006 3.3227 3.3394 0.4285  -0.5639 -0.2650 93   PRO B CA  
14939 C C   . PRO C 93   ? 5.5277 3.3746 3.4012 0.4558  -0.5403 -0.2643 93   PRO B C   
14940 O O   . PRO C 93   ? 5.5478 3.3687 3.4075 0.4627  -0.5230 -0.2599 93   PRO B O   
14941 C CB  . PRO C 93   ? 5.5593 3.2926 3.3251 0.4305  -0.5625 -0.2619 93   PRO B CB  
14942 C CG  . PRO C 93   ? 5.5861 3.3030 3.3264 0.3983  -0.5745 -0.2602 93   PRO B CG  
14943 C CD  . PRO C 93   ? 5.5200 3.3039 3.3151 0.3855  -0.5704 -0.2603 93   PRO B CD  
14944 N N   . GLY C 94   ? 5.5223 3.4192 3.4405 0.4708  -0.5394 -0.2679 94   GLY B N   
14945 C CA  . GLY C 94   ? 5.5117 3.4309 3.4610 0.4979  -0.5180 -0.2675 94   GLY B CA  
14946 C C   . GLY C 94   ? 5.5733 3.4249 3.4772 0.5236  -0.5061 -0.2646 94   GLY B C   
14947 O O   . GLY C 94   ? 5.6185 3.4266 3.4849 0.5294  -0.5158 -0.2660 94   GLY B O   
14948 N N   . GLY C 95   ? 5.5743 3.4164 3.4817 0.5387  -0.4850 -0.2597 95   GLY B N   
14949 C CA  . GLY C 95   ? 5.6116 3.3886 3.4775 0.5632  -0.4716 -0.2549 95   GLY B CA  
14950 C C   . GLY C 95   ? 5.6636 3.3805 3.4814 0.5516  -0.4663 -0.2479 95   GLY B C   
14951 O O   . GLY C 95   ? 5.6603 3.3566 3.4731 0.5643  -0.4472 -0.2405 95   GLY B O   
14952 N N   . GLN C 96   ? 5.7047 3.3927 3.4868 0.5272  -0.4828 -0.2493 96   GLN B N   
14953 C CA  . GLN C 96   ? 5.7302 3.3670 3.4701 0.5131  -0.4777 -0.2429 96   GLN B CA  
14954 C C   . GLN C 96   ? 5.7245 3.4060 3.5048 0.5069  -0.4648 -0.2391 96   GLN B C   
14955 O O   . GLN C 96   ? 5.7072 3.4572 3.5378 0.4964  -0.4704 -0.2436 96   GLN B O   
14956 C CB  . GLN C 96   ? 5.7253 3.3457 3.4353 0.4817  -0.4989 -0.2458 96   GLN B CB  
14957 C CG  . GLN C 96   ? 5.7271 3.3089 3.4038 0.4634  -0.4931 -0.2397 96   GLN B CG  
14958 C CD  . GLN C 96   ? 5.7684 3.3211 3.4054 0.4347  -0.5132 -0.2421 96   GLN B CD  
14959 O OE1 . GLN C 96   ? 5.7701 3.3355 3.4069 0.4261  -0.5332 -0.2478 96   GLN B OE1 
14960 N NE2 . GLN C 96   ? 5.8069 3.3203 3.4099 0.4192  -0.5081 -0.2370 96   GLN B NE2 
14961 N N   . ASN C 97   ? 5.7303 3.3735 3.4902 0.5142  -0.4466 -0.2301 97   ASN B N   
14962 C CA  . ASN C 97   ? 5.6829 3.3621 3.4748 0.5044  -0.4353 -0.2254 97   ASN B CA  
14963 C C   . ASN C 97   ? 5.6249 3.3021 3.4021 0.4710  -0.4473 -0.2265 97   ASN B C   
14964 O O   . ASN C 97   ? 5.6734 3.3036 3.4147 0.4632  -0.4400 -0.2196 97   ASN B O   
14965 C CB  . ASN C 97   ? 5.7370 3.3750 3.5122 0.5234  -0.4120 -0.2137 97   ASN B CB  
14966 C CG  . ASN C 97   ? 5.7506 3.3843 3.5360 0.5576  -0.4005 -0.2120 97   ASN B CG  
14967 O OD1 . ASN C 97   ? 5.7274 3.4070 3.5473 0.5666  -0.4068 -0.2197 97   ASN B OD1 
14968 N ND2 . ASN C 97   ? 5.7802 3.3588 3.5363 0.5769  -0.3832 -0.2013 97   ASN B ND2 
14969 N N   . PRO C 98   ? 5.5074 3.2362 3.3133 0.4511  -0.4655 -0.2346 98   PRO B N   
14970 C CA  . PRO C 98   ? 5.4293 3.1498 3.2149 0.4199  -0.4807 -0.2363 98   PRO B CA  
14971 C C   . PRO C 98   ? 5.2301 2.9790 3.0399 0.4049  -0.4712 -0.2324 98   PRO B C   
14972 O O   . PRO C 98   ? 5.2029 2.9828 3.0478 0.4179  -0.4554 -0.2292 98   PRO B O   
14973 C CB  . PRO C 98   ? 5.4602 3.2359 3.2794 0.4072  -0.5015 -0.2449 98   PRO B CB  
14974 C CG  . PRO C 98   ? 5.4392 3.2607 3.3042 0.4316  -0.4937 -0.2476 98   PRO B CG  
14975 C CD  . PRO C 98   ? 5.4397 3.2438 3.3053 0.4539  -0.4696 -0.2408 98   PRO B CD  
14976 N N   . VAL C 99   ? 5.0617 2.7997 2.8526 0.3780  -0.4806 -0.2323 99   VAL B N   
14977 C CA  . VAL C 99   ? 4.8437 2.6271 2.6696 0.3596  -0.4771 -0.2314 99   VAL B CA  
14978 C C   . VAL C 99   ? 4.5999 2.3689 2.4266 0.3693  -0.4536 -0.2221 99   VAL B C   
14979 O O   . VAL C 99   ? 4.6008 2.3828 2.4363 0.3513  -0.4498 -0.2192 99   VAL B O   
14980 C CB  . VAL C 99   ? 4.8289 2.6919 2.7176 0.3584  -0.4828 -0.2378 99   VAL B CB  
14981 C CG1 . VAL C 99   ? 4.8235 2.7360 2.7517 0.3412  -0.4775 -0.2370 99   VAL B CG1 
14982 C CG2 . VAL C 99   ? 4.8494 2.7293 2.7400 0.3463  -0.5065 -0.2451 99   VAL B CG2 
14983 N N   . SER C 100  ? 4.3588 2.1009 2.1770 0.3973  -0.4380 -0.2166 100  SER B N   
14984 C CA  . SER C 100  ? 4.1096 1.8390 1.9309 0.4074  -0.4158 -0.2059 100  SER B CA  
14985 C C   . SER C 100  ? 3.9739 1.6545 1.7542 0.3908  -0.4123 -0.1992 100  SER B C   
14986 O O   . SER C 100  ? 4.0487 1.6634 1.7773 0.3961  -0.4114 -0.1959 100  SER B O   
14987 C CB  . SER C 100  ? 4.0571 1.7501 1.8637 0.4400  -0.4014 -0.1998 100  SER B CB  
14988 O OG  . SER C 100  ? 4.0210 1.7190 1.8282 0.4527  -0.4128 -0.2081 100  SER B OG  
14989 N N   . TYR C 101  ? 3.7461 1.4576 1.5483 0.3705  -0.4099 -0.1973 101  TYR B N   
14990 C CA  . TYR C 101  ? 3.6020 1.2722 1.3690 0.3533  -0.4060 -0.1910 101  TYR B CA  
14991 C C   . TYR C 101  ? 3.5425 1.2064 1.2874 0.3267  -0.4265 -0.1989 101  TYR B C   
14992 O O   . TYR C 101  ? 3.5468 1.1942 1.2704 0.3271  -0.4416 -0.2056 101  TYR B O   
14993 C CB  . TYR C 101  ? 3.5920 1.1854 1.3092 0.3717  -0.3907 -0.1803 101  TYR B CB  
14994 C CG  . TYR C 101  ? 3.5432 1.1352 1.2775 0.3917  -0.3676 -0.1678 101  TYR B CG  
14995 C CD1 . TYR C 101  ? 3.5641 1.1303 1.2859 0.3856  -0.3519 -0.1553 101  TYR B CD1 
14996 C CD2 . TYR C 101  ? 3.4857 1.1034 1.2499 0.4160  -0.3616 -0.1677 101  TYR B CD2 
14997 C CE1 . TYR C 101  ? 3.5522 1.1176 1.2905 0.4025  -0.3314 -0.1421 101  TYR B CE1 
14998 C CE2 . TYR C 101  ? 3.4756 1.0918 1.2552 0.4335  -0.3410 -0.1550 101  TYR B CE2 
14999 C CZ  . TYR C 101  ? 3.5135 1.1031 1.2800 0.4263  -0.3262 -0.1417 101  TYR B CZ  
15000 O OH  . TYR C 101  ? 3.5002 1.0875 1.2820 0.4417  -0.3061 -0.1270 101  TYR B OH  
15001 N N   . VAL C 102  ? 3.4796 1.1567 1.2298 0.3031  -0.4272 -0.1976 102  VAL B N   
15002 C CA  . VAL C 102  ? 3.4760 1.1407 1.2008 0.2769  -0.4449 -0.2033 102  VAL B CA  
15003 C C   . VAL C 102  ? 3.5207 1.1647 1.2296 0.2610  -0.4349 -0.1962 102  VAL B C   
15004 O O   . VAL C 102  ? 3.4928 1.1318 1.2106 0.2706  -0.4147 -0.1864 102  VAL B O   
15005 C CB  . VAL C 102  ? 3.3869 1.1187 1.1538 0.2575  -0.4644 -0.2136 102  VAL B CB  
15006 C CG1 . VAL C 102  ? 3.3276 1.0982 1.1272 0.2731  -0.4711 -0.2197 102  VAL B CG1 
15007 C CG2 . VAL C 102  ? 3.3418 1.1229 1.1501 0.2429  -0.4576 -0.2119 102  VAL B CG2 
15008 N N   . TYR C 103  ? 3.5775 1.2119 1.2647 0.2359  -0.4497 -0.2009 103  TYR B N   
15009 C CA  . TYR C 103  ? 3.6324 1.2395 1.2962 0.2188  -0.4422 -0.1950 103  TYR B CA  
15010 C C   . TYR C 103  ? 3.5781 1.2380 1.2731 0.1909  -0.4554 -0.2013 103  TYR B C   
15011 O O   . TYR C 103  ? 3.5421 1.2215 1.2395 0.1756  -0.4772 -0.2103 103  TYR B O   
15012 C CB  . TYR C 103  ? 3.8617 1.3880 1.4555 0.2160  -0.4433 -0.1923 103  TYR B CB  
15013 C CG  . TYR C 103  ? 3.9844 1.4477 1.5435 0.2398  -0.4202 -0.1805 103  TYR B CG  
15014 C CD1 . TYR C 103  ? 4.0205 1.4712 1.5791 0.2670  -0.4152 -0.1794 103  TYR B CD1 
15015 C CD2 . TYR C 103  ? 4.0536 1.4701 1.5815 0.2355  -0.4028 -0.1698 103  TYR B CD2 
15016 C CE1 . TYR C 103  ? 4.0896 1.4828 1.6180 0.2894  -0.3939 -0.1678 103  TYR B CE1 
15017 C CE2 . TYR C 103  ? 4.1238 1.4824 1.6218 0.2576  -0.3807 -0.1574 103  TYR B CE2 
15018 C CZ  . TYR C 103  ? 4.1440 1.4912 1.6427 0.2847  -0.3766 -0.1565 103  TYR B CZ  
15019 O OH  . TYR C 103  ? 4.1876 1.4782 1.6586 0.3077  -0.3549 -0.1437 103  TYR B OH  
15020 N N   . LEU C 104  ? 3.5945 1.2787 1.3157 0.1849  -0.4418 -0.1958 104  LEU B N   
15021 C CA  . LEU C 104  ? 3.5923 1.3211 1.3409 0.1587  -0.4506 -0.2002 104  LEU B CA  
15022 C C   . LEU C 104  ? 3.6340 1.3116 1.3349 0.1424  -0.4502 -0.1969 104  LEU B C   
15023 O O   . LEU C 104  ? 3.6433 1.2665 1.3087 0.1523  -0.4331 -0.1873 104  LEU B O   
15024 C CB  . LEU C 104  ? 3.5173 1.2934 1.3142 0.1597  -0.4352 -0.1953 104  LEU B CB  
15025 C CG  . LEU C 104  ? 3.4549 1.2891 1.2922 0.1354  -0.4428 -0.2004 104  LEU B CG  
15026 C CD1 . LEU C 104  ? 3.4243 1.3081 1.2915 0.1255  -0.4646 -0.2121 104  LEU B CD1 
15027 C CD2 . LEU C 104  ? 3.3893 1.2616 1.2685 0.1396  -0.4255 -0.1942 104  LEU B CD2 
15028 N N   . GLU C 105  ? 3.6900 1.3842 1.3900 0.1175  -0.4685 -0.2043 105  GLU B N   
15029 C CA  . GLU C 105  ? 3.7846 1.4319 1.4389 0.1001  -0.4694 -0.2021 105  GLU B CA  
15030 C C   . GLU C 105  ? 3.7761 1.4669 1.4568 0.0736  -0.4792 -0.2067 105  GLU B C   
15031 O O   . GLU C 105  ? 3.7457 1.4938 1.4671 0.0642  -0.4949 -0.2146 105  GLU B O   
15032 C CB  . GLU C 105  ? 3.8743 1.4712 1.4761 0.0969  -0.4851 -0.2063 105  GLU B CB  
15033 C CG  . GLU C 105  ? 3.9532 1.4825 1.4946 0.0848  -0.4806 -0.2019 105  GLU B CG  
15034 C CD  . GLU C 105  ? 4.0327 1.5018 1.5166 0.0871  -0.4915 -0.2041 105  GLU B CD  
15035 O OE1 . GLU C 105  ? 4.0507 1.5344 1.5318 0.0727  -0.5160 -0.2124 105  GLU B OE1 
15036 O OE2 . GLU C 105  ? 4.0758 1.4821 1.5172 0.1030  -0.4754 -0.1968 105  GLU B OE2 
15037 N N   . VAL C 106  ? 3.8076 1.4695 1.4646 0.0617  -0.4692 -0.2013 106  VAL B N   
15038 C CA  . VAL C 106  ? 3.8049 1.4995 1.4796 0.0360  -0.4781 -0.2054 106  VAL B CA  
15039 C C   . VAL C 106  ? 3.8791 1.5144 1.4962 0.0211  -0.4801 -0.2038 106  VAL B C   
15040 O O   . VAL C 106  ? 3.9224 1.4939 1.4925 0.0321  -0.4665 -0.1966 106  VAL B O   
15041 C CB  . VAL C 106  ? 3.7695 1.5000 1.4842 0.0354  -0.4604 -0.1997 106  VAL B CB  
15042 C CG1 . VAL C 106  ? 3.7769 1.5355 1.5056 0.0087  -0.4685 -0.2037 106  VAL B CG1 
15043 C CG2 . VAL C 106  ? 3.7102 1.4988 1.4800 0.0483  -0.4589 -0.2017 106  VAL B CG2 
15044 N N   . VAL C 107  ? 3.8895 1.5448 1.5097 -0.0039 -0.4965 -0.2102 107  VAL B N   
15045 C CA  . VAL C 107  ? 3.9461 1.5476 1.5105 -0.0204 -0.5023 -0.2102 107  VAL B CA  
15046 C C   . VAL C 107  ? 3.9300 1.5600 1.5118 -0.0442 -0.5048 -0.2121 107  VAL B C   
15047 O O   . VAL C 107  ? 3.8644 1.5598 1.4991 -0.0525 -0.5133 -0.2171 107  VAL B O   
15048 C CB  . VAL C 107  ? 4.0598 1.6459 1.5966 -0.0279 -0.5282 -0.2178 107  VAL B CB  
15049 C CG1 . VAL C 107  ? 4.1297 1.6472 1.5988 -0.0419 -0.5317 -0.2165 107  VAL B CG1 
15050 C CG2 . VAL C 107  ? 4.0550 1.6307 1.5893 -0.0044 -0.5286 -0.2176 107  VAL B CG2 
15051 N N   . SER C 108  ? 3.9771 1.5576 1.5145 -0.0548 -0.4965 -0.2079 108  SER B N   
15052 C CA  . SER C 108  ? 4.0227 1.6250 1.5717 -0.0775 -0.4986 -0.2096 108  SER B CA  
15053 C C   . SER C 108  ? 4.1532 1.6893 1.6378 -0.0910 -0.4977 -0.2076 108  SER B C   
15054 O O   . SER C 108  ? 4.2210 1.7021 1.6549 -0.0867 -0.5024 -0.2074 108  SER B O   
15055 C CB  . SER C 108  ? 3.9670 1.5973 1.5536 -0.0720 -0.4758 -0.2024 108  SER B CB  
15056 O OG  . SER C 108  ? 3.9855 1.5650 1.5439 -0.0537 -0.4507 -0.1908 108  SER B OG  
15057 N N   . LYS C 109  ? 4.2325 1.7728 1.7179 -0.1079 -0.4917 -0.2063 109  LYS B N   
15058 C CA  . LYS C 109  ? 4.3597 1.8333 1.7832 -0.1191 -0.4849 -0.2026 109  LYS B CA  
15059 C C   . LYS C 109  ? 4.4278 1.8551 1.8293 -0.1044 -0.4525 -0.1896 109  LYS B C   
15060 O O   . LYS C 109  ? 4.4908 1.8475 1.8325 -0.1049 -0.4423 -0.1844 109  LYS B O   
15061 C CB  . LYS C 109  ? 4.3636 1.8587 1.7920 -0.1463 -0.4958 -0.2079 109  LYS B CB  
15062 C CG  . LYS C 109  ? 4.3393 1.8976 1.8274 -0.1523 -0.4876 -0.2074 109  LYS B CG  
15063 C CD  . LYS C 109  ? 4.3007 1.8524 1.8029 -0.1359 -0.4566 -0.1955 109  LYS B CD  
15064 C CE  . LYS C 109  ? 4.2304 1.8369 1.7833 -0.1456 -0.4486 -0.1944 109  LYS B CE  
15065 N NZ  . LYS C 109  ? 4.2567 1.8303 1.7814 -0.1585 -0.4342 -0.1888 109  LYS B NZ  
15066 N N   . HIS C 110  ? 4.4214 1.8882 1.8716 -0.0917 -0.4362 -0.1836 110  HIS B N   
15067 C CA  . HIS C 110  ? 4.4589 1.8952 1.9008 -0.0810 -0.4054 -0.1694 110  HIS B CA  
15068 C C   . HIS C 110  ? 4.4182 1.8233 1.8517 -0.0531 -0.3874 -0.1593 110  HIS B C   
15069 O O   . HIS C 110  ? 4.4507 1.8037 1.8538 -0.0438 -0.3630 -0.1464 110  HIS B O   
15070 C CB  . HIS C 110  ? 4.4901 1.9851 1.9877 -0.0879 -0.3963 -0.1665 110  HIS B CB  
15071 C CG  . HIS C 110  ? 4.5879 2.0556 2.0811 -0.0778 -0.3653 -0.1504 110  HIS B CG  
15072 N ND1 . HIS C 110  ? 4.5860 2.0964 2.1296 -0.0682 -0.3513 -0.1425 110  HIS B ND1 
15073 C CD2 . HIS C 110  ? 4.6795 2.0793 2.1230 -0.0755 -0.3451 -0.1394 110  HIS B CD2 
15074 C CE1 . HIS C 110  ? 4.6216 2.0937 2.1486 -0.0609 -0.3244 -0.1267 110  HIS B CE1 
15075 N NE2 . HIS C 110  ? 4.6779 2.0825 2.1449 -0.0647 -0.3195 -0.1244 110  HIS B NE2 
15076 N N   . PHE C 111  ? 4.3366 1.7742 1.7985 -0.0395 -0.3985 -0.1644 111  PHE B N   
15077 C CA  . PHE C 111  ? 4.2734 1.6794 1.7240 -0.0126 -0.3845 -0.1563 111  PHE B CA  
15078 C C   . PHE C 111  ? 4.1440 1.5671 1.6019 -0.0035 -0.4052 -0.1663 111  PHE B C   
15079 O O   . PHE C 111  ? 4.0810 1.5482 1.5610 -0.0173 -0.4294 -0.1784 111  PHE B O   
15080 C CB  . PHE C 111  ? 4.2568 1.6932 1.7522 0.0020  -0.3626 -0.1447 111  PHE B CB  
15081 C CG  . PHE C 111  ? 4.3056 1.6879 1.7753 0.0273  -0.3391 -0.1304 111  PHE B CG  
15082 C CD1 . PHE C 111  ? 4.3520 1.6819 1.7904 0.0290  -0.3143 -0.1157 111  PHE B CD1 
15083 C CD2 . PHE C 111  ? 4.2932 1.6775 1.7714 0.0496  -0.3412 -0.1309 111  PHE B CD2 
15084 C CE1 . PHE C 111  ? 4.3795 1.6593 1.7957 0.0525  -0.2923 -0.1014 111  PHE B CE1 
15085 C CE2 . PHE C 111  ? 4.3130 1.6477 1.7685 0.0733  -0.3199 -0.1174 111  PHE B CE2 
15086 C CZ  . PHE C 111  ? 4.3568 1.6392 1.7817 0.0749  -0.2955 -0.1024 111  PHE B CZ  
15087 N N   . SER C 112  ? 4.0824 1.4694 1.5215 0.0201  -0.3953 -0.1606 112  SER B N   
15088 C CA  . SER C 112  ? 3.9942 1.4075 1.4529 0.0328  -0.4104 -0.1681 112  SER B CA  
15089 C C   . SER C 112  ? 3.9713 1.3763 1.4431 0.0613  -0.3903 -0.1580 112  SER B C   
15090 O O   . SER C 112  ? 4.0090 1.3562 1.4463 0.0734  -0.3685 -0.1457 112  SER B O   
15091 C CB  . SER C 112  ? 3.9956 1.3641 1.4036 0.0288  -0.4282 -0.1754 112  SER B CB  
15092 O OG  . SER C 112  ? 3.9385 1.3563 1.3779 0.0280  -0.4519 -0.1865 112  SER B OG  
15093 N N   . LYS C 113  ? 3.8970 1.3606 1.4201 0.0714  -0.3972 -0.1625 113  LYS B N   
15094 C CA  . LYS C 113  ? 3.8225 1.2895 1.3662 0.0981  -0.3806 -0.1539 113  LYS B CA  
15095 C C   . LYS C 113  ? 3.7290 1.2445 1.3101 0.1092  -0.3952 -0.1630 113  LYS B C   
15096 O O   . LYS C 113  ? 3.6775 1.2452 1.2891 0.0951  -0.4152 -0.1745 113  LYS B O   
15097 C CB  . LYS C 113  ? 3.8097 1.3044 1.3899 0.0989  -0.3604 -0.1427 113  LYS B CB  
15098 C CG  . LYS C 113  ? 3.8267 1.3159 1.4223 0.1261  -0.3410 -0.1308 113  LYS B CG  
15099 C CD  . LYS C 113  ? 3.9067 1.3219 1.4571 0.1390  -0.3171 -0.1146 113  LYS B CD  
15100 C CE  . LYS C 113  ? 3.8939 1.3095 1.4658 0.1652  -0.2978 -0.1011 113  LYS B CE  
15101 N NZ  . LYS C 113  ? 3.9202 1.2818 1.4668 0.1741  -0.2705 -0.0812 113  LYS B NZ  
15102 N N   . SER C 114  ? 3.7276 1.2251 1.3073 0.1352  -0.3837 -0.1569 114  SER B N   
15103 C CA  . SER C 114  ? 3.7574 1.2892 1.3640 0.1491  -0.3954 -0.1647 114  SER B CA  
15104 C C   . SER C 114  ? 3.7455 1.2839 1.3764 0.1756  -0.3761 -0.1548 114  SER B C   
15105 O O   . SER C 114  ? 3.7284 1.2509 1.3598 0.1803  -0.3551 -0.1416 114  SER B O   
15106 C CB  . SER C 114  ? 3.8355 1.3225 1.3962 0.1526  -0.4100 -0.1714 114  SER B CB  
15107 O OG  . SER C 114  ? 3.9105 1.3233 1.4100 0.1483  -0.4023 -0.1656 114  SER B OG  
15108 N N   . LYS C 115  ? 3.7335 1.2961 1.3855 0.1923  -0.3829 -0.1603 115  LYS B N   
15109 C CA  . LYS C 115  ? 3.6986 1.2739 1.3777 0.2166  -0.3662 -0.1517 115  LYS B CA  
15110 C C   . LYS C 115  ? 3.6751 1.2504 1.3561 0.2386  -0.3724 -0.1569 115  LYS B C   
15111 O O   . LYS C 115  ? 3.6523 1.2545 1.3425 0.2323  -0.3925 -0.1696 115  LYS B O   
15112 C CB  . LYS C 115  ? 3.6349 1.2821 1.3742 0.2087  -0.3637 -0.1519 115  LYS B CB  
15113 C CG  . LYS C 115  ? 3.5714 1.2368 1.3418 0.2311  -0.3469 -0.1424 115  LYS B CG  
15114 C CD  . LYS C 115  ? 3.5429 1.1830 1.3081 0.2343  -0.3235 -0.1247 115  LYS B CD  
15115 C CE  . LYS C 115  ? 3.4637 1.1389 1.2708 0.2501  -0.3100 -0.1159 115  LYS B CE  
15116 N NZ  . LYS C 115  ? 3.4521 1.0980 1.2526 0.2559  -0.2869 -0.0960 115  LYS B NZ  
15117 N N   . ARG C 116  ? 3.7080 1.2537 1.3816 0.2643  -0.3548 -0.1463 116  ARG B N   
15118 C CA  . ARG C 116  ? 3.7486 1.3018 1.4329 0.2883  -0.3573 -0.1499 116  ARG B CA  
15119 C C   . ARG C 116  ? 3.7106 1.3299 1.4546 0.2956  -0.3523 -0.1493 116  ARG B C   
15120 O O   . ARG C 116  ? 3.7161 1.3389 1.4758 0.3015  -0.3343 -0.1369 116  ARG B O   
15121 C CB  . ARG C 116  ? 3.8335 1.3173 1.4771 0.3135  -0.3407 -0.1384 116  ARG B CB  
15122 C CG  . ARG C 116  ? 3.8628 1.3534 1.5201 0.3416  -0.3394 -0.1398 116  ARG B CG  
15123 C CD  . ARG C 116  ? 3.8932 1.3917 1.5766 0.3614  -0.3176 -0.1255 116  ARG B CD  
15124 N NE  . ARG C 116  ? 3.9667 1.4166 1.6255 0.3911  -0.3064 -0.1181 116  ARG B NE  
15125 C CZ  . ARG C 116  ? 3.9755 1.4352 1.6586 0.4140  -0.2916 -0.1082 116  ARG B CZ  
15126 N NH1 . ARG C 116  ? 3.9386 1.4557 1.6709 0.4100  -0.2866 -0.1046 116  ARG B NH1 
15127 N NH2 . ARG C 116  ? 4.0060 1.4180 1.6640 0.4408  -0.2823 -0.1018 116  ARG B NH2 
15128 N N   . MET C 117  ? 3.6571 1.3282 1.4342 0.2951  -0.3674 -0.1616 117  MET B N   
15129 C CA  . MET C 117  ? 3.5703 1.3069 1.4041 0.2979  -0.3631 -0.1622 117  MET B CA  
15130 C C   . MET C 117  ? 3.5043 1.2825 1.3665 0.3074  -0.3756 -0.1738 117  MET B C   
15131 O O   . MET C 117  ? 3.4708 1.2701 1.3366 0.2933  -0.3947 -0.1855 117  MET B O   
15132 C CB  . MET C 117  ? 3.5606 1.3410 1.4224 0.2708  -0.3666 -0.1643 117  MET B CB  
15133 C CG  . MET C 117  ? 3.5865 1.3788 1.4409 0.2474  -0.3882 -0.1768 117  MET B CG  
15134 S SD  . MET C 117  ? 3.5808 1.4345 1.4775 0.2183  -0.3925 -0.1805 117  MET B SD  
15135 C CE  . MET C 117  ? 3.0973 0.9251 0.9870 0.2204  -0.3679 -0.1635 117  MET B CE  
15136 N N   . PRO C 118  ? 3.4576 1.2488 1.3414 0.3310  -0.3645 -0.1697 118  PRO B N   
15137 C CA  . PRO C 118  ? 3.4002 1.2239 1.3080 0.3454  -0.3726 -0.1789 118  PRO B CA  
15138 C C   . PRO C 118  ? 3.3455 1.2350 1.2941 0.3271  -0.3881 -0.1913 118  PRO B C   
15139 O O   . PRO C 118  ? 3.3017 1.2252 1.2736 0.3065  -0.3884 -0.1916 118  PRO B O   
15140 C CB  . PRO C 118  ? 3.3685 1.2039 1.3003 0.3678  -0.3542 -0.1698 118  PRO B CB  
15141 C CG  . PRO C 118  ? 3.4094 1.1886 1.3081 0.3742  -0.3377 -0.1545 118  PRO B CG  
15142 C CD  . PRO C 118  ? 3.4538 1.2231 1.3365 0.3468  -0.3423 -0.1542 118  PRO B CD  
15143 N N   . ILE C 119  ? 3.3331 1.2395 1.2903 0.3352  -0.4004 -0.2007 119  ILE B N   
15144 C CA  . ILE C 119  ? 3.2858 1.2533 1.2823 0.3202  -0.4150 -0.2116 119  ILE B CA  
15145 C C   . ILE C 119  ? 3.2373 1.2400 1.2650 0.3391  -0.4154 -0.2169 119  ILE B C   
15146 O O   . ILE C 119  ? 3.2261 1.2007 1.2390 0.3640  -0.4078 -0.2137 119  ILE B O   
15147 C CB  . ILE C 119  ? 3.2841 1.2392 1.2575 0.3013  -0.4362 -0.2188 119  ILE B CB  
15148 C CG1 . ILE C 119  ? 3.2669 1.1963 1.2177 0.3167  -0.4463 -0.2232 119  ILE B CG1 
15149 C CG2 . ILE C 119  ? 3.3282 1.2359 1.2601 0.2855  -0.4359 -0.2137 119  ILE B CG2 
15150 C CD1 . ILE C 119  ? 3.2893 1.2145 1.2232 0.2967  -0.4687 -0.2299 119  ILE B CD1 
15151 N N   . THR C 120  ? 3.2138 1.2773 1.2847 0.3275  -0.4237 -0.2246 120  THR B N   
15152 C CA  . THR C 120  ? 3.2014 1.3049 1.3079 0.3441  -0.4215 -0.2291 120  THR B CA  
15153 C C   . THR C 120  ? 3.1870 1.3383 1.3240 0.3321  -0.4376 -0.2386 120  THR B C   
15154 O O   . THR C 120  ? 3.1863 1.3500 1.3251 0.3079  -0.4508 -0.2417 120  THR B O   
15155 C CB  . THR C 120  ? 3.1873 1.3260 1.3300 0.3511  -0.4034 -0.2249 120  THR B CB  
15156 O OG1 . THR C 120  ? 3.2199 1.3195 1.3383 0.3552  -0.3893 -0.2142 120  THR B OG1 
15157 C CG2 . THR C 120  ? 2.6944 0.8549 0.8607 0.3769  -0.3965 -0.2272 120  THR B CG2 
15158 N N   . TYR C 121  ? 3.4895 1.5310 1.5590 -0.0502 -0.6098 -0.2916 121  TYR B N   
15159 C CA  . TYR C 121  ? 3.4829 1.5789 1.5544 -0.0573 -0.6301 -0.2835 121  TYR B CA  
15160 C C   . TYR C 121  ? 3.3553 1.5037 1.4744 -0.0481 -0.6319 -0.2607 121  TYR B C   
15161 O O   . TYR C 121  ? 3.3474 1.5449 1.4754 -0.0509 -0.6465 -0.2505 121  TYR B O   
15162 C CB  . TYR C 121  ? 3.5697 1.6709 1.6071 -0.0411 -0.6281 -0.2860 121  TYR B CB  
15163 C CG  . TYR C 121  ? 3.6793 1.7313 1.6641 -0.0463 -0.6248 -0.3085 121  TYR B CG  
15164 C CD1 . TYR C 121  ? 3.7357 1.7792 1.6937 -0.0739 -0.6426 -0.3250 121  TYR B CD1 
15165 C CD2 . TYR C 121  ? 3.6989 1.7140 1.6611 -0.0234 -0.6036 -0.3137 121  TYR B CD2 
15166 C CE1 . TYR C 121  ? 3.8116 1.8108 1.7207 -0.0787 -0.6390 -0.3470 121  TYR B CE1 
15167 C CE2 . TYR C 121  ? 3.7657 1.7363 1.6793 -0.0274 -0.5994 -0.3343 121  TYR B CE2 
15168 C CZ  . TYR C 121  ? 3.8369 1.7996 1.7233 -0.0551 -0.6170 -0.3514 121  TYR B CZ  
15169 O OH  . TYR C 121  ? 3.9390 1.8570 1.7752 -0.0594 -0.6123 -0.3737 121  TYR B OH  
15170 N N   . ASP C 122  ? 3.2433 1.3821 1.3929 -0.0361 -0.6163 -0.2527 122  ASP B N   
15171 C CA  . ASP C 122  ? 3.1165 1.3025 1.3127 -0.0294 -0.6172 -0.2328 122  ASP B CA  
15172 C C   . ASP C 122  ? 3.0353 1.2443 1.2561 -0.0544 -0.6334 -0.2278 122  ASP B C   
15173 O O   . ASP C 122  ? 3.0530 1.2374 1.2870 -0.0632 -0.6285 -0.2298 122  ASP B O   
15174 C CB  . ASP C 122  ? 3.1113 1.2768 1.3298 -0.0109 -0.5960 -0.2279 122  ASP B CB  
15175 C CG  . ASP C 122  ? 3.1003 1.2918 1.3353 0.0166  -0.5841 -0.2165 122  ASP B CG  
15176 O OD1 . ASP C 122  ? 3.1081 1.2687 1.3394 0.0360  -0.5651 -0.2195 122  ASP B OD1 
15177 O OD2 . ASP C 122  ? 3.0811 1.3237 1.3349 0.0188  -0.5933 -0.2043 122  ASP B OD2 
15178 N N   . ASN C 123  ? 2.9558 1.2127 1.1861 -0.0652 -0.6519 -0.2197 123  ASN B N   
15179 C CA  . ASN C 123  ? 2.9292 1.2110 1.1886 -0.0873 -0.6661 -0.2125 123  ASN B CA  
15180 C C   . ASN C 123  ? 2.8931 1.2347 1.1922 -0.0797 -0.6700 -0.1917 123  ASN B C   
15181 O O   . ASN C 123  ? 2.8633 1.2425 1.1604 -0.0770 -0.6799 -0.1853 123  ASN B O   
15182 C CB  . ASN C 123  ? 2.9413 1.2223 1.1786 -0.1151 -0.6874 -0.2240 123  ASN B CB  
15183 C CG  . ASN C 123  ? 2.9222 1.2322 1.1930 -0.1380 -0.7025 -0.2152 123  ASN B CG  
15184 O OD1 . ASN C 123  ? 2.9500 1.2498 1.2096 -0.1631 -0.7172 -0.2261 123  ASN B OD1 
15185 N ND2 . ASN C 123  ? 2.8767 1.2234 1.1890 -0.1295 -0.6986 -0.1961 123  ASN B ND2 
15186 N N   . GLY C 124  ? 2.8936 1.2435 1.2287 -0.0762 -0.6616 -0.1809 124  GLY B N   
15187 C CA  . GLY C 124  ? 2.8463 1.2506 1.2223 -0.0704 -0.6636 -0.1618 124  GLY B CA  
15188 C C   . GLY C 124  ? 2.6643 1.0842 1.0555 -0.0416 -0.6467 -0.1535 124  GLY B C   
15189 O O   . GLY C 124  ? 2.6655 1.0505 1.0442 -0.0254 -0.6303 -0.1604 124  GLY B O   
15190 N N   . PHE C 125  ? 2.6268 1.0997 1.0463 -0.0358 -0.6507 -0.1387 125  PHE B N   
15191 C CA  . PHE C 125  ? 2.5796 1.0752 1.0241 -0.0110 -0.6351 -0.1294 125  PHE B CA  
15192 C C   . PHE C 125  ? 2.5556 1.1024 1.0157 -0.0042 -0.6409 -0.1176 125  PHE B C   
15193 O O   . PHE C 125  ? 2.5505 1.1339 1.0280 -0.0193 -0.6555 -0.1083 125  PHE B O   
15194 C CB  . PHE C 125  ? 2.5459 1.0586 1.0275 -0.0122 -0.6299 -0.1197 125  PHE B CB  
15195 C CG  . PHE C 125  ? 2.5644 1.0340 1.0389 -0.0192 -0.6239 -0.1270 125  PHE B CG  
15196 C CD1 . PHE C 125  ? 2.5851 1.0500 1.0640 -0.0431 -0.6356 -0.1261 125  PHE B CD1 
15197 C CD2 . PHE C 125  ? 2.5604 0.9951 1.0272 -0.0014 -0.6060 -0.1334 125  PHE B CD2 
15198 C CE1 . PHE C 125  ? 2.6021 1.0280 1.0776 -0.0490 -0.6289 -0.1312 125  PHE B CE1 
15199 C CE2 . PHE C 125  ? 2.5775 0.9736 1.0398 -0.0072 -0.5999 -0.1384 125  PHE B CE2 
15200 C CZ  . PHE C 125  ? 2.5984 0.9901 1.0655 -0.0310 -0.6110 -0.1370 125  PHE B CZ  
15201 N N   . LEU C 126  ? 2.5393 1.0902 0.9971 0.0189  -0.6287 -0.1168 126  LEU B N   
15202 C CA  . LEU C 126  ? 2.5118 1.1133 0.9910 0.0278  -0.6311 -0.1035 126  LEU B CA  
15203 C C   . LEU C 126  ? 2.4659 1.0968 0.9872 0.0463  -0.6155 -0.0936 126  LEU B C   
15204 O O   . LEU C 126  ? 2.4921 1.1019 1.0150 0.0654  -0.5978 -0.0988 126  LEU B O   
15205 C CB  . LEU C 126  ? 2.5315 1.1263 0.9825 0.0398  -0.6298 -0.1067 126  LEU B CB  
15206 C CG  . LEU C 126  ? 2.5776 1.1697 0.9931 0.0238  -0.6484 -0.1112 126  LEU B CG  
15207 C CD1 . LEU C 126  ? 2.5856 1.2075 1.0130 -0.0025 -0.6701 -0.1050 126  LEU B CD1 
15208 C CD2 . LEU C 126  ? 2.6255 1.1592 0.9946 0.0196  -0.6468 -0.1300 126  LEU B CD2 
15209 N N   . PHE C 127  ? 2.4300 1.1094 0.9859 0.0404  -0.6218 -0.0801 127  PHE B N   
15210 C CA  . PHE C 127  ? 2.3812 1.0905 0.9781 0.0550  -0.6078 -0.0719 127  PHE B CA  
15211 C C   . PHE C 127  ? 2.3534 1.1091 0.9757 0.0671  -0.6050 -0.0598 127  PHE B C   
15212 O O   . PHE C 127  ? 2.3485 1.1421 0.9876 0.0549  -0.6174 -0.0485 127  PHE B O   
15213 C CB  . PHE C 127  ? 2.3744 1.1038 0.9960 0.0388  -0.6146 -0.0651 127  PHE B CB  
15214 C CG  . PHE C 127  ? 2.3939 1.0850 1.0055 0.0332  -0.6104 -0.0736 127  PHE B CG  
15215 C CD1 . PHE C 127  ? 2.3895 1.0482 0.9931 0.0505  -0.5938 -0.0828 127  PHE B CD1 
15216 C CD2 . PHE C 127  ? 2.3951 1.0845 1.0087 0.0110  -0.6225 -0.0711 127  PHE B CD2 
15217 C CE1 . PHE C 127  ? 2.3847 1.0107 0.9812 0.0458  -0.5898 -0.0886 127  PHE B CE1 
15218 C CE2 . PHE C 127  ? 2.4058 1.0618 1.0128 0.0064  -0.6178 -0.0769 127  PHE B CE2 
15219 C CZ  . PHE C 127  ? 2.4006 1.0253 0.9988 0.0239  -0.6016 -0.0853 127  PHE B CZ  
15220 N N   . ILE C 128  ? 2.3341 1.0884 0.9631 0.0911  -0.5880 -0.0612 128  ILE B N   
15221 C CA  . ILE C 128  ? 2.3121 1.1073 0.9639 0.1037  -0.5841 -0.0495 128  ILE B CA  
15222 C C   . ILE C 128  ? 2.2636 1.1014 0.9650 0.1141  -0.5724 -0.0402 128  ILE B C   
15223 O O   . ILE C 128  ? 2.2371 1.0713 0.9560 0.1333  -0.5537 -0.0446 128  ILE B O   
15224 C CB  . ILE C 128  ? 2.3198 1.0946 0.9542 0.1245  -0.5720 -0.0540 128  ILE B CB  
15225 C CG1 . ILE C 128  ? 2.3621 1.0812 0.9488 0.1202  -0.5748 -0.0687 128  ILE B CG1 
15226 C CG2 . ILE C 128  ? 2.3239 1.1313 0.9610 0.1268  -0.5786 -0.0417 128  ILE B CG2 
15227 C CD1 . ILE C 128  ? 2.3719 1.0686 0.9398 0.1409  -0.5620 -0.0730 128  ILE B CD1 
15228 N N   . HIS C 129  ? 2.2529 1.1325 0.9777 0.1013  -0.5831 -0.0276 129  HIS B N   
15229 C CA  . HIS C 129  ? 2.2529 1.1736 1.0243 0.1076  -0.5732 -0.0192 129  HIS B CA  
15230 C C   . HIS C 129  ? 2.2591 1.2180 1.0605 0.1236  -0.5637 -0.0080 129  HIS B C   
15231 O O   . HIS C 129  ? 2.2744 1.2712 1.0932 0.1158  -0.5729 0.0062  129  HIS B O   
15232 C CB  . HIS C 129  ? 2.2140 1.1585 0.9980 0.0850  -0.5882 -0.0110 129  HIS B CB  
15233 C CG  . HIS C 129  ? 2.1709 1.1564 1.0000 0.0893  -0.5785 -0.0029 129  HIS B CG  
15234 N ND1 . HIS C 129  ? 2.1664 1.1779 1.0129 0.0717  -0.5887 0.0060  129  HIS B ND1 
15235 C CD2 . HIS C 129  ? 2.1348 1.1401 0.9956 0.1089  -0.5592 -0.0030 129  HIS B CD2 
15236 C CE1 . HIS C 129  ? 2.1298 1.1750 1.0150 0.0806  -0.5757 0.0111  129  HIS B CE1 
15237 N NE2 . HIS C 129  ? 2.1103 1.1526 1.0050 0.1028  -0.5579 0.0051  129  HIS B NE2 
15238 N N   . THR C 130  ? 2.2485 1.1972 1.0579 0.1463  -0.5446 -0.0138 130  THR B N   
15239 C CA  . THR C 130  ? 2.2272 1.2113 1.0705 0.1629  -0.5325 -0.0034 130  THR B CA  
15240 C C   . THR C 130  ? 2.2070 1.2284 1.0948 0.1622  -0.5250 0.0012  130  THR B C   
15241 O O   . THR C 130  ? 2.2229 1.2331 1.1116 0.1574  -0.5228 -0.0076 130  THR B O   
15242 C CB  . THR C 130  ? 2.2186 1.1797 1.0607 0.1871  -0.5130 -0.0118 130  THR B CB  
15243 O OG1 . THR C 130  ? 2.1730 1.1707 1.0613 0.2039  -0.4961 -0.0041 130  THR B OG1 
15244 C CG2 . THR C 130  ? 2.2242 1.1486 1.0557 0.1907  -0.5044 -0.0287 130  THR B CG2 
15245 N N   . ASP C 131  ? 2.1686 1.2350 1.0932 0.1666  -0.5209 0.0154  131  ASP B N   
15246 C CA  . ASP C 131  ? 2.1504 1.2531 1.1157 0.1636  -0.5148 0.0198  131  ASP B CA  
15247 C C   . ASP C 131  ? 2.1577 1.2555 1.1452 0.1803  -0.4931 0.0070  131  ASP B C   
15248 O O   . ASP C 131  ? 2.1617 1.2602 1.1549 0.1738  -0.4922 0.0006  131  ASP B O   
15249 C CB  . ASP C 131  ? 2.1122 1.2643 1.1142 0.1641  -0.5145 0.0384  131  ASP B CB  
15250 C CG  . ASP C 131  ? 2.0852 1.2519 1.1175 0.1877  -0.4936 0.0409  131  ASP B CG  
15251 O OD1 . ASP C 131  ? 2.0848 1.2204 1.0980 0.2015  -0.4857 0.0318  131  ASP B OD1 
15252 O OD2 . ASP C 131  ? 2.0692 1.2776 1.1456 0.1926  -0.4843 0.0520  131  ASP B OD2 
15253 N N   . LYS C 132  ? 2.1603 1.2534 1.1603 0.2018  -0.4759 0.0033  132  LYS B N   
15254 C CA  . LYS C 132  ? 2.1509 1.2360 1.1698 0.2176  -0.4560 -0.0111 132  LYS B CA  
15255 C C   . LYS C 132  ? 2.2184 1.2641 1.2163 0.2340  -0.4467 -0.0214 132  LYS B C   
15256 O O   . LYS C 132  ? 2.2962 1.3250 1.2673 0.2341  -0.4544 -0.0162 132  LYS B O   
15257 C CB  . LYS C 132  ? 2.0604 1.1897 1.1333 0.2279  -0.4390 -0.0066 132  LYS B CB  
15258 C CG  . LYS C 132  ? 2.0112 1.1546 1.1117 0.2473  -0.4232 -0.0007 132  LYS B CG  
15259 C CD  . LYS C 132  ? 1.9066 1.1012 1.0570 0.2480  -0.4150 0.0112  132  LYS B CD  
15260 C CE  . LYS C 132  ? 1.8901 1.1025 1.0757 0.2681  -0.3966 0.0186  132  LYS B CE  
15261 N NZ  . LYS C 132  ? 1.8905 1.1449 1.1018 0.2616  -0.4016 0.0398  132  LYS B NZ  
15262 N N   . PRO C 133  ? 2.1510 1.1811 1.1588 0.2473  -0.4310 -0.0362 133  PRO B N   
15263 C CA  . PRO C 133  ? 2.1105 1.0961 1.0886 0.2581  -0.4269 -0.0454 133  PRO B CA  
15264 C C   . PRO C 133  ? 2.0421 1.0347 1.0515 0.2821  -0.4051 -0.0471 133  PRO B C   
15265 O O   . PRO C 133  ? 2.0799 1.0383 1.0754 0.2948  -0.3963 -0.0572 133  PRO B O   
15266 C CB  . PRO C 133  ? 2.0668 1.0282 1.0347 0.2562  -0.4248 -0.0607 133  PRO B CB  
15267 C CG  . PRO C 133  ? 2.1467 1.1494 1.1585 0.2569  -0.4155 -0.0623 133  PRO B CG  
15268 C CD  . PRO C 133  ? 2.1391 1.1857 1.1799 0.2541  -0.4165 -0.0464 133  PRO B CD  
15269 N N   . VAL C 134  ? 2.0033 1.0378 1.0561 0.2887  -0.3953 -0.0378 134  VAL B N   
15270 C CA  . VAL C 134  ? 1.9378 0.9772 1.0206 0.3116  -0.3744 -0.0377 134  VAL B CA  
15271 C C   . VAL C 134  ? 2.0088 1.0896 1.1252 0.3153  -0.3702 -0.0196 134  VAL B C   
15272 O O   . VAL C 134  ? 1.9614 1.0797 1.1062 0.3068  -0.3717 -0.0131 134  VAL B O   
15273 C CB  . VAL C 134  ? 1.9044 0.9453 1.0207 0.3253  -0.3543 -0.0540 134  VAL B CB  
15274 C CG1 . VAL C 134  ? 1.8795 0.9445 1.0439 0.3448  -0.3326 -0.0501 134  VAL B CG1 
15275 C CG2 . VAL C 134  ? 1.9173 0.9119 1.0055 0.3327  -0.3512 -0.0686 134  VAL B CG2 
15276 N N   . TYR C 135  ? 1.9802 1.0542 1.0943 0.3290  -0.3640 -0.0108 135  TYR B N   
15277 C CA  . TYR C 135  ? 1.9984 1.1099 1.1426 0.3346  -0.3597 0.0092  135  TYR B CA  
15278 C C   . TYR C 135  ? 1.9173 1.0354 1.1001 0.3598  -0.3346 0.0116  135  TYR B C   
15279 O O   . TYR C 135  ? 1.9062 0.9930 1.0823 0.3745  -0.3225 0.0002  135  TYR B O   
15280 C CB  . TYR C 135  ? 1.9580 1.0648 1.0625 0.3245  -0.3798 0.0241  135  TYR B CB  
15281 C CG  . TYR C 135  ? 1.9777 1.0797 1.0480 0.2991  -0.4044 0.0227  135  TYR B CG  
15282 C CD1 . TYR C 135  ? 1.9730 1.1134 1.0593 0.2840  -0.4162 0.0365  135  TYR B CD1 
15283 C CD2 . TYR C 135  ? 2.0006 1.0593 1.0255 0.2902  -0.4148 0.0077  135  TYR B CD2 
15284 C CE1 . TYR C 135  ? 1.9911 1.1270 1.0489 0.2607  -0.4381 0.0354  135  TYR B CE1 
15285 C CE2 . TYR C 135  ? 2.0190 1.0725 1.0156 0.2671  -0.4361 0.0066  135  TYR B CE2 
15286 C CZ  . TYR C 135  ? 2.0143 1.1063 1.0273 0.2523  -0.4478 0.0203  135  TYR B CZ  
15287 O OH  . TYR C 135  ? 2.0332 1.1194 1.0198 0.2290  -0.4687 0.0192  135  TYR B OH  
15288 N N   . THR C 136  ? 1.9079 1.0680 1.1329 0.3646  -0.3267 0.0280  136  THR B N   
15289 C CA  . THR C 136  ? 1.9024 1.0755 1.1717 0.3879  -0.3019 0.0339  136  THR B CA  
15290 C C   . THR C 136  ? 1.9192 1.1126 1.1872 0.3910  -0.3070 0.0595  136  THR B C   
15291 O O   . THR C 136  ? 1.9182 1.1337 1.1742 0.3746  -0.3257 0.0732  136  THR B O   
15292 C CB  . THR C 136  ? 1.8792 1.0894 1.2097 0.3920  -0.2843 0.0315  136  THR B CB  
15293 O OG1 . THR C 136  ? 1.8983 1.1310 1.2252 0.3707  -0.3003 0.0336  136  THR B OG1 
15294 C CG2 . THR C 136  ? 1.8631 1.0543 1.2121 0.4030  -0.2663 0.0073  136  THR B CG2 
15295 N N   . PRO C 137  ? 1.8834 1.0708 1.1650 0.4125  -0.2904 0.0667  137  PRO B N   
15296 C CA  . PRO C 137  ? 1.8986 1.1059 1.1791 0.4183  -0.2935 0.0922  137  PRO B CA  
15297 C C   . PRO C 137  ? 1.8952 1.1473 1.1918 0.4032  -0.3067 0.1108  137  PRO B C   
15298 O O   . PRO C 137  ? 1.8651 1.1492 1.2127 0.4037  -0.2948 0.1124  137  PRO B O   
15299 C CB  . PRO C 137  ? 1.8745 1.0933 1.2095 0.4446  -0.2629 0.0976  137  PRO B CB  
15300 C CG  . PRO C 137  ? 1.8648 1.0465 1.1993 0.4541  -0.2491 0.0721  137  PRO B CG  
15301 C CD  . PRO C 137  ? 1.8896 1.0561 1.1962 0.4336  -0.2654 0.0523  137  PRO B CD  
15302 N N   . ASP C 138  ? 1.9272 1.1801 1.1799 0.3895  -0.3311 0.1235  138  ASP B N   
15303 C CA  . ASP C 138  ? 1.9302 1.2265 1.1950 0.3772  -0.3452 0.1462  138  ASP B CA  
15304 C C   . ASP C 138  ? 1.9311 1.2375 1.1843 0.3513  -0.3657 0.1412  138  ASP B C   
15305 O O   . ASP C 138  ? 1.9692 1.3098 1.2294 0.3393  -0.3795 0.1596  138  ASP B O   
15306 C CB  . ASP C 138  ? 1.9945 1.3345 1.3278 0.3934  -0.3225 0.1648  138  ASP B CB  
15307 C CG  . ASP C 138  ? 2.0620 1.4045 1.4018 0.4152  -0.3099 0.1821  138  ASP B CG  
15308 O OD1 . ASP C 138  ? 2.1462 1.4759 1.4365 0.4113  -0.3274 0.1900  138  ASP B OD1 
15309 O OD2 . ASP C 138  ? 2.0635 1.4204 1.4573 0.4362  -0.2823 0.1875  138  ASP B OD2 
15310 N N   . GLN C 139  ? 2.0362 1.3143 1.2731 0.3430  -0.3675 0.1175  139  GLN B N   
15311 C CA  . GLN C 139  ? 2.0239 1.3081 1.2462 0.3184  -0.3873 0.1126  139  GLN B CA  
15312 C C   . GLN C 139  ? 2.0717 1.3401 1.2362 0.3019  -0.4153 0.1179  139  GLN B C   
15313 O O   . GLN C 139  ? 2.1014 1.3463 1.2335 0.3102  -0.4173 0.1190  139  GLN B O   
15314 C CB  . GLN C 139  ? 2.0335 1.2896 1.2478 0.3139  -0.3833 0.0867  139  GLN B CB  
15315 C CG  . GLN C 139  ? 2.0021 1.2611 1.2630 0.3319  -0.3549 0.0736  139  GLN B CG  
15316 C CD  . GLN C 139  ? 1.9982 1.2540 1.2632 0.3207  -0.3555 0.0555  139  GLN B CD  
15317 O OE1 . GLN C 139  ? 1.9746 1.2012 1.2305 0.3265  -0.3475 0.0350  139  GLN B OE1 
15318 N NE2 . GLN C 139  ? 2.0050 1.2922 1.2836 0.3046  -0.3655 0.0639  139  GLN B NE2 
15319 N N   . SER C 140  ? 2.0823 1.3637 1.2341 0.2786  -0.4366 0.1211  140  SER B N   
15320 C CA  . SER C 140  ? 2.1132 1.3768 1.2098 0.2610  -0.4636 0.1225  140  SER B CA  
15321 C C   . SER C 140  ? 2.1132 1.3418 1.1746 0.2440  -0.4759 0.1020  140  SER B C   
15322 O O   . SER C 140  ? 2.0718 1.3148 1.1494 0.2306  -0.4804 0.0997  140  SER B O   
15323 C CB  . SER C 140  ? 2.1307 1.4365 1.2359 0.2468  -0.4817 0.1453  140  SER B CB  
15324 O OG  . SER C 140  ? 2.1356 1.4542 1.2350 0.2577  -0.4825 0.1624  140  SER B OG  
15325 N N   . VAL C 141  ? 2.1203 1.3030 1.1344 0.2454  -0.4802 0.0879  141  VAL B N   
15326 C CA  . VAL C 141  ? 2.1167 1.2618 1.0957 0.2308  -0.4905 0.0688  141  VAL B CA  
15327 C C   . VAL C 141  ? 2.1215 1.2762 1.0794 0.2038  -0.5170 0.0740  141  VAL B C   
15328 O O   . VAL C 141  ? 2.1814 1.3352 1.1091 0.1951  -0.5340 0.0813  141  VAL B O   
15329 C CB  . VAL C 141  ? 2.1048 1.1987 1.0348 0.2369  -0.4911 0.0552  141  VAL B CB  
15330 C CG1 . VAL C 141  ? 2.1193 1.1753 1.0169 0.2222  -0.5005 0.0368  141  VAL B CG1 
15331 C CG2 . VAL C 141  ? 2.0860 1.1676 1.0350 0.2642  -0.4651 0.0505  141  VAL B CG2 
15332 N N   . LYS C 142  ? 2.1286 1.2937 1.1028 0.1905  -0.5206 0.0704  142  LYS B N   
15333 C CA  . LYS C 142  ? 2.1704 1.3375 1.1224 0.1643  -0.5453 0.0729  142  LYS B CA  
15334 C C   . LYS C 142  ? 2.2563 1.3706 1.1565 0.1554  -0.5549 0.0546  142  LYS B C   
15335 O O   . LYS C 142  ? 2.2817 1.3649 1.1758 0.1665  -0.5410 0.0395  142  LYS B O   
15336 C CB  . LYS C 142  ? 2.1495 1.3452 1.1367 0.1536  -0.5449 0.0763  142  LYS B CB  
15337 C CG  . LYS C 142  ? 2.1390 1.3890 1.1728 0.1554  -0.5418 0.0972  142  LYS B CG  
15338 C CD  . LYS C 142  ? 2.1479 1.4237 1.1979 0.1344  -0.5546 0.1045  142  LYS B CD  
15339 C CE  . LYS C 142  ? 2.1477 1.4769 1.2388 0.1330  -0.5561 0.1279  142  LYS B CE  
15340 N NZ  . LYS C 142  ? 2.1102 1.4665 1.2512 0.1547  -0.5298 0.1334  142  LYS B NZ  
15341 N N   . VAL C 143  ? 2.2868 1.3907 1.1509 0.1357  -0.5780 0.0554  143  VAL B N   
15342 C CA  . VAL C 143  ? 2.3051 1.3582 1.1216 0.1256  -0.5868 0.0377  143  VAL B CA  
15343 C C   . VAL C 143  ? 2.3091 1.3582 1.1000 0.0975  -0.6126 0.0376  143  VAL B C   
15344 O O   . VAL C 143  ? 2.3173 1.3965 1.1109 0.0862  -0.6283 0.0509  143  VAL B O   
15345 C CB  . VAL C 143  ? 2.2297 1.2458 1.0103 0.1405  -0.5802 0.0289  143  VAL B CB  
15346 C CG1 . VAL C 143  ? 2.2207 1.2657 1.0187 0.1579  -0.5721 0.0436  143  VAL B CG1 
15347 C CG2 . VAL C 143  ? 2.2786 1.2602 1.0059 0.1231  -0.5998 0.0196  143  VAL B CG2 
15348 N N   . ARG C 144  ? 2.2850 1.2980 1.0542 0.0864  -0.6163 0.0231  144  ARG B N   
15349 C CA  . ARG C 144  ? 2.3194 1.3172 1.0589 0.0609  -0.6389 0.0190  144  ARG B CA  
15350 C C   . ARG C 144  ? 2.3328 1.2738 1.0352 0.0580  -0.6369 -0.0006 144  ARG B C   
15351 O O   . ARG C 144  ? 2.2984 1.2158 1.0014 0.0756  -0.6185 -0.0095 144  ARG B O   
15352 C CB  . ARG C 144  ? 2.3187 1.3496 1.0878 0.0424  -0.6493 0.0292  144  ARG B CB  
15353 C CG  . ARG C 144  ? 2.3111 1.3501 1.1135 0.0488  -0.6339 0.0284  144  ARG B CG  
15354 C CD  . ARG C 144  ? 2.3320 1.3874 1.1497 0.0269  -0.6463 0.0342  144  ARG B CD  
15355 N NE  . ARG C 144  ? 2.3120 1.3905 1.1685 0.0353  -0.6308 0.0382  144  ARG B NE  
15356 C CZ  . ARG C 144  ? 2.3083 1.4325 1.2056 0.0433  -0.6229 0.0518  144  ARG B CZ  
15357 N NH1 . ARG C 144  ? 2.3143 1.4666 1.2201 0.0440  -0.6295 0.0645  144  ARG B NH1 
15358 N NH2 . ARG C 144  ? 2.2872 1.4296 1.2168 0.0508  -0.6080 0.0529  144  ARG B NH2 
15359 N N   . VAL C 145  ? 2.3751 1.2946 1.0469 0.0357  -0.6555 -0.0073 145  VAL B N   
15360 C CA  . VAL C 145  ? 2.3802 1.2449 1.0157 0.0309  -0.6548 -0.0252 145  VAL B CA  
15361 C C   . VAL C 145  ? 2.3934 1.2532 1.0300 0.0063  -0.6686 -0.0270 145  VAL B C   
15362 O O   . VAL C 145  ? 2.4105 1.2915 1.0472 -0.0128 -0.6875 -0.0205 145  VAL B O   
15363 C CB  . VAL C 145  ? 2.4255 1.2605 1.0140 0.0280  -0.6638 -0.0346 145  VAL B CB  
15364 C CG1 . VAL C 145  ? 2.4592 1.2416 1.0138 0.0159  -0.6670 -0.0521 145  VAL B CG1 
15365 C CG2 . VAL C 145  ? 2.4179 1.2452 0.9988 0.0539  -0.6474 -0.0355 145  VAL B CG2 
15366 N N   . TYR C 146  ? 2.4015 1.2361 1.0419 0.0072  -0.6588 -0.0346 146  TYR B N   
15367 C CA  . TYR C 146  ? 2.4369 1.2546 1.0723 -0.0150 -0.6696 -0.0386 146  TYR B CA  
15368 C C   . TYR C 146  ? 2.5119 1.2737 1.1032 -0.0197 -0.6713 -0.0559 146  TYR B C   
15369 O O   . TYR C 146  ? 2.5107 1.2409 1.0889 -0.0028 -0.6557 -0.0651 146  TYR B O   
15370 C CB  . TYR C 146  ? 2.3712 1.1948 1.0360 -0.0111 -0.6575 -0.0354 146  TYR B CB  
15371 C CG  . TYR C 146  ? 2.4007 1.2761 1.1082 -0.0010 -0.6503 -0.0208 146  TYR B CG  
15372 C CD1 . TYR C 146  ? 2.4065 1.3251 1.1366 -0.0139 -0.6632 -0.0067 146  TYR B CD1 
15373 C CD2 . TYR C 146  ? 2.3719 1.2535 1.0985 0.0215  -0.6301 -0.0216 146  TYR B CD2 
15374 C CE1 . TYR C 146  ? 2.3664 1.3322 1.1373 -0.0041 -0.6550 0.0067  146  TYR B CE1 
15375 C CE2 . TYR C 146  ? 2.3253 1.2538 1.0920 0.0307  -0.6221 -0.0098 146  TYR B CE2 
15376 C CZ  . TYR C 146  ? 2.3170 1.2868 1.1056 0.0181  -0.6340 0.0045  146  TYR B CZ  
15377 O OH  . TYR C 146  ? 2.2682 1.2834 1.0975 0.0275  -0.6247 0.0160  146  TYR B OH  
15378 N N   . SER C 147  ? 2.5653 1.3149 1.1346 -0.0426 -0.6899 -0.0608 147  SER B N   
15379 C CA  . SER C 147  ? 2.6424 1.3386 1.1687 -0.0488 -0.6919 -0.0786 147  SER B CA  
15380 C C   . SER C 147  ? 2.6796 1.3547 1.2018 -0.0738 -0.7030 -0.0843 147  SER B C   
15381 O O   . SER C 147  ? 2.6932 1.3957 1.2302 -0.0933 -0.7193 -0.0769 147  SER B O   
15382 C CB  . SER C 147  ? 2.6973 1.3913 1.1904 -0.0497 -0.7023 -0.0836 147  SER B CB  
15383 O OG  . SER C 147  ? 2.7458 1.4557 1.2322 -0.0747 -0.7252 -0.0826 147  SER B OG  
15384 N N   . LEU C 148  ? 2.6960 1.3222 1.2004 -0.0729 -0.6934 -0.0969 148  LEU B N   
15385 C CA  . LEU C 148  ? 2.7423 1.3430 1.2443 -0.0947 -0.7004 -0.1027 148  LEU B CA  
15386 C C   . LEU C 148  ? 2.8158 1.3607 1.2748 -0.1000 -0.7002 -0.1223 148  LEU B C   
15387 O O   . LEU C 148  ? 2.9022 1.4243 1.3372 -0.0827 -0.6895 -0.1303 148  LEU B O   
15388 C CB  . LEU C 148  ? 2.6618 1.2584 1.1906 -0.0875 -0.6860 -0.0966 148  LEU B CB  
15389 C CG  . LEU C 148  ? 2.6180 1.2640 1.1899 -0.0917 -0.6889 -0.0787 148  LEU B CG  
15390 C CD1 . LEU C 148  ? 2.5949 1.2908 1.1813 -0.0899 -0.6980 -0.0678 148  LEU B CD1 
15391 C CD2 . LEU C 148  ? 2.5948 1.2452 1.1890 -0.0729 -0.6701 -0.0728 148  LEU B CD2 
15392 N N   . ASN C 149  ? 2.8340 1.3569 1.2847 -0.1241 -0.7113 -0.1302 149  ASN B N   
15393 C CA  . ASN C 149  ? 2.8531 1.3196 1.2659 -0.1318 -0.7099 -0.1501 149  ASN B CA  
15394 C C   . ASN C 149  ? 2.8111 1.2397 1.2329 -0.1329 -0.6966 -0.1531 149  ASN B C   
15395 O O   . ASN C 149  ? 2.7780 1.2272 1.2349 -0.1346 -0.6937 -0.1398 149  ASN B O   
15396 C CB  . ASN C 149  ? 2.9264 1.3930 1.3256 -0.1599 -0.7315 -0.1583 149  ASN B CB  
15397 C CG  . ASN C 149  ? 2.9615 1.4449 1.3949 -0.1803 -0.7401 -0.1493 149  ASN B CG  
15398 O OD1 . ASN C 149  ? 2.9340 1.4526 1.4045 -0.1737 -0.7359 -0.1317 149  ASN B OD1 
15399 N ND2 . ASN C 149  ? 3.0284 1.4864 1.4506 -0.2051 -0.7513 -0.1617 149  ASN B ND2 
15400 N N   . ASP C 150  ? 2.8610 1.2351 1.2514 -0.1328 -0.6887 -0.1700 150  ASP B N   
15401 C CA  . ASP C 150  ? 2.8440 1.1773 1.2404 -0.1347 -0.6758 -0.1735 150  ASP B CA  
15402 C C   . ASP C 150  ? 2.8366 1.1913 1.2726 -0.1468 -0.6785 -0.1593 150  ASP B C   
15403 O O   . ASP C 150  ? 2.7931 1.1309 1.2447 -0.1401 -0.6647 -0.1543 150  ASP B O   
15404 C CB  . ASP C 150  ? 2.9589 1.2377 1.3210 -0.1504 -0.6777 -0.1945 150  ASP B CB  
15405 C CG  . ASP C 150  ? 3.1624 1.4506 1.5198 -0.1801 -0.6999 -0.2014 150  ASP B CG  
15406 O OD1 . ASP C 150  ? 3.1672 1.4303 1.5315 -0.1997 -0.7020 -0.2071 150  ASP B OD1 
15407 O OD2 . ASP C 150  ? 3.1791 1.4997 1.5266 -0.1840 -0.7149 -0.2011 150  ASP B OD2 
15408 N N   . ASP C 151  ? 2.8419 1.2344 1.2946 -0.1645 -0.6962 -0.1522 151  ASP B N   
15409 C CA  . ASP C 151  ? 2.8695 1.2814 1.3587 -0.1789 -0.7003 -0.1391 151  ASP B CA  
15410 C C   . ASP C 151  ? 2.8341 1.3032 1.3578 -0.1686 -0.7006 -0.1187 151  ASP B C   
15411 O O   . ASP C 151  ? 2.8227 1.3203 1.3769 -0.1818 -0.7080 -0.1063 151  ASP B O   
15412 C CB  . ASP C 151  ? 2.9600 1.3723 1.4471 -0.2087 -0.7201 -0.1458 151  ASP B CB  
15413 C CG  . ASP C 151  ? 2.9953 1.3891 1.5053 -0.2263 -0.7186 -0.1429 151  ASP B CG  
15414 O OD1 . ASP C 151  ? 3.0305 1.4263 1.5450 -0.2514 -0.7341 -0.1474 151  ASP B OD1 
15415 O OD2 . ASP C 151  ? 2.9938 1.3717 1.5181 -0.2152 -0.7019 -0.1359 151  ASP B OD2 
15416 N N   . LEU C 152  ? 2.8165 1.3022 1.3365 -0.1451 -0.6918 -0.1156 152  LEU B N   
15417 C CA  . LEU C 152  ? 2.8082 1.3468 1.3610 -0.1328 -0.6892 -0.0978 152  LEU B CA  
15418 C C   . LEU C 152  ? 2.8369 1.4215 1.4130 -0.1503 -0.7068 -0.0863 152  LEU B C   
15419 O O   . LEU C 152  ? 2.7926 1.4135 1.4038 -0.1491 -0.7047 -0.0703 152  LEU B O   
15420 C CB  . LEU C 152  ? 2.7876 1.3276 1.3662 -0.1220 -0.6736 -0.0876 152  LEU B CB  
15421 C CG  . LEU C 152  ? 2.7959 1.2982 1.3597 -0.1023 -0.6548 -0.0953 152  LEU B CG  
15422 C CD1 . LEU C 152  ? 2.7920 1.2853 1.3293 -0.0859 -0.6511 -0.1054 152  LEU B CD1 
15423 C CD2 . LEU C 152  ? 2.8525 1.3024 1.4007 -0.1146 -0.6523 -0.1051 152  LEU B CD2 
15424 N N   . LYS C 153  ? 2.8891 1.4724 1.4463 -0.1669 -0.7240 -0.0945 153  LYS B N   
15425 C CA  . LYS C 153  ? 2.9038 1.5328 1.4813 -0.1827 -0.7421 -0.0839 153  LYS B CA  
15426 C C   . LYS C 153  ? 2.8971 1.5502 1.4585 -0.1755 -0.7504 -0.0849 153  LYS B C   
15427 O O   . LYS C 153  ? 2.8900 1.5170 1.4189 -0.1633 -0.7447 -0.0970 153  LYS B O   
15428 C CB  . LYS C 153  ? 2.9537 1.5669 1.5299 -0.2121 -0.7576 -0.0903 153  LYS B CB  
15429 C CG  . LYS C 153  ? 2.9526 1.5745 1.5652 -0.2230 -0.7552 -0.0778 153  LYS B CG  
15430 C CD  . LYS C 153  ? 3.0101 1.6060 1.6197 -0.2512 -0.7676 -0.0872 153  LYS B CD  
15431 C CE  . LYS C 153  ? 3.0189 1.6173 1.6646 -0.2600 -0.7619 -0.0743 153  LYS B CE  
15432 N NZ  . LYS C 153  ? 2.9951 1.5777 1.6478 -0.2397 -0.7398 -0.0682 153  LYS B NZ  
15433 N N   . PRO C 154  ? 2.9409 1.6447 1.5263 -0.1828 -0.7634 -0.0710 154  PRO B N   
15434 C CA  . PRO C 154  ? 2.9513 1.6888 1.5318 -0.1732 -0.7693 -0.0659 154  PRO B CA  
15435 C C   . PRO C 154  ? 3.0449 1.7506 1.5812 -0.1631 -0.7670 -0.0817 154  PRO B C   
15436 O O   . PRO C 154  ? 3.0309 1.7482 1.5645 -0.1408 -0.7565 -0.0779 154  PRO B O   
15437 C CB  . PRO C 154  ? 2.9790 1.7480 1.5709 -0.1978 -0.7927 -0.0601 154  PRO B CB  
15438 C CG  . PRO C 154  ? 2.9602 1.7356 1.5859 -0.2117 -0.7929 -0.0513 154  PRO B CG  
15439 C CD  . PRO C 154  ? 2.9430 1.6743 1.5624 -0.2028 -0.7743 -0.0589 154  PRO B CD  
15440 N N   . ALA C 155  ? 3.1208 1.7871 1.6242 -0.1793 -0.7759 -0.0993 155  ALA B N   
15441 C CA  . ALA C 155  ? 3.1934 1.8242 1.6515 -0.1708 -0.7727 -0.1161 155  ALA B CA  
15442 C C   . ALA C 155  ? 3.2442 1.9050 1.6853 -0.1687 -0.7855 -0.1139 155  ALA B C   
15443 O O   . ALA C 155  ? 3.2596 1.9077 1.6744 -0.1505 -0.7769 -0.1192 155  ALA B O   
15444 C CB  . ALA C 155  ? 3.1468 1.7529 1.6004 -0.1436 -0.7485 -0.1177 155  ALA B CB  
15445 N N   . LYS C 156  ? 3.2685 1.9696 1.7253 -0.1869 -0.8058 -0.1051 156  LYS B N   
15446 C CA  . LYS C 156  ? 3.2696 2.0090 1.7181 -0.1838 -0.8181 -0.0979 156  LYS B CA  
15447 C C   . LYS C 156  ? 3.2683 1.9750 1.6652 -0.1782 -0.8183 -0.1152 156  LYS B C   
15448 O O   . LYS C 156  ? 3.3060 1.9694 1.6718 -0.1922 -0.8223 -0.1352 156  LYS B O   
15449 C CB  . LYS C 156  ? 3.3135 2.0895 1.7776 -0.2099 -0.8431 -0.0915 156  LYS B CB  
15450 C CG  . LYS C 156  ? 3.2918 2.1074 1.8086 -0.2141 -0.8432 -0.0714 156  LYS B CG  
15451 C CD  . LYS C 156  ? 3.3419 2.1658 1.8719 -0.2451 -0.8637 -0.0728 156  LYS B CD  
15452 C CE  . LYS C 156  ? 3.3343 2.1689 1.9088 -0.2491 -0.8562 -0.0601 156  LYS B CE  
15453 N NZ  . LYS C 156  ? 3.3862 2.2142 1.9713 -0.2789 -0.8720 -0.0649 156  LYS B NZ  
15454 N N   . ARG C 157  ? 3.2253 1.9530 1.6146 -0.1573 -0.8127 -0.1073 157  ARG B N   
15455 C CA  . ARG C 157  ? 3.2243 1.9245 1.5657 -0.1478 -0.8102 -0.1209 157  ARG B CA  
15456 C C   . ARG C 157  ? 3.2407 1.9825 1.5902 -0.1264 -0.8064 -0.1039 157  ARG B C   
15457 O O   . ARG C 157  ? 3.2102 1.9933 1.6022 -0.1180 -0.8023 -0.0842 157  ARG B O   
15458 C CB  . ARG C 157  ? 3.1592 1.8036 1.4826 -0.1324 -0.7875 -0.1345 157  ARG B CB  
15459 C CG  . ARG C 157  ? 3.1184 1.7172 1.4341 -0.1509 -0.7878 -0.1509 157  ARG B CG  
15460 C CD  . ARG C 157  ? 3.0602 1.6123 1.3707 -0.1336 -0.7636 -0.1586 157  ARG B CD  
15461 N NE  . ARG C 157  ? 3.0624 1.5720 1.3677 -0.1518 -0.7637 -0.1727 157  ARG B NE  
15462 C CZ  . ARG C 157  ? 3.0523 1.5138 1.3490 -0.1426 -0.7453 -0.1824 157  ARG B CZ  
15463 N NH1 . ARG C 157  ? 3.0270 1.4768 1.3187 -0.1155 -0.7259 -0.1802 157  ARG B NH1 
15464 N NH2 . ARG C 157  ? 3.0715 1.4970 1.3665 -0.1604 -0.7460 -0.1936 157  ARG B NH2 
15465 N N   . GLU C 158  ? 3.2852 2.0171 1.5954 -0.1169 -0.8066 -0.1106 158  GLU B N   
15466 C CA  . GLU C 158  ? 3.2878 2.0542 1.6082 -0.0922 -0.7977 -0.0934 158  GLU B CA  
15467 C C   . GLU C 158  ? 3.2408 1.9730 1.5511 -0.0637 -0.7710 -0.0978 158  GLU B C   
15468 O O   . GLU C 158  ? 3.2867 1.9710 1.5554 -0.0615 -0.7652 -0.1162 158  GLU B O   
15469 C CB  . GLU C 158  ? 3.3830 2.1773 1.6760 -0.0975 -0.8160 -0.0904 158  GLU B CB  
15470 C CG  . GLU C 158  ? 3.4434 2.2881 1.7604 -0.1196 -0.8405 -0.0780 158  GLU B CG  
15471 C CD  . GLU C 158  ? 3.5185 2.4019 1.8170 -0.1192 -0.8560 -0.0687 158  GLU B CD  
15472 O OE1 . GLU C 158  ? 3.5058 2.4132 1.8136 -0.0946 -0.8439 -0.0527 158  GLU B OE1 
15473 O OE2 . GLU C 158  ? 3.5794 2.4704 1.8555 -0.1433 -0.8801 -0.0770 158  GLU B OE2 
15474 N N   . THR C 159  ? 3.1343 1.8919 1.4843 -0.0425 -0.7547 -0.0812 159  THR B N   
15475 C CA  . THR C 159  ? 3.0422 1.7715 1.3944 -0.0159 -0.7283 -0.0840 159  THR B CA  
15476 C C   . THR C 159  ? 2.9082 1.6641 1.2664 0.0099  -0.7172 -0.0701 159  THR B C   
15477 O O   . THR C 159  ? 2.8795 1.6853 1.2565 0.0095  -0.7268 -0.0529 159  THR B O   
15478 C CB  . THR C 159  ? 3.0358 1.7692 1.4325 -0.0113 -0.7154 -0.0783 159  THR B CB  
15479 O OG1 . THR C 159  ? 3.0699 1.7832 1.4657 -0.0353 -0.7256 -0.0881 159  THR B OG1 
15480 C CG2 . THR C 159  ? 3.0346 1.7349 1.4316 0.0138  -0.6895 -0.0841 159  THR B CG2 
15481 N N   . VAL C 160  ? 2.8246 1.5479 1.1699 0.0327  -0.6960 -0.0764 160  VAL B N   
15482 C CA  . VAL C 160  ? 2.7623 1.5068 1.1121 0.0579  -0.6839 -0.0638 160  VAL B CA  
15483 C C   . VAL C 160  ? 2.7213 1.4483 1.0908 0.0856  -0.6563 -0.0631 160  VAL B C   
15484 O O   . VAL C 160  ? 2.7233 1.4010 1.0669 0.0936  -0.6438 -0.0782 160  VAL B O   
15485 C CB  . VAL C 160  ? 2.7956 1.5226 1.0939 0.0591  -0.6899 -0.0713 160  VAL B CB  
15486 C CG1 . VAL C 160  ? 2.7929 1.4992 1.0838 0.0892  -0.6657 -0.0707 160  VAL B CG1 
15487 C CG2 . VAL C 160  ? 2.8136 1.5919 1.1124 0.0515  -0.7088 -0.0559 160  VAL B CG2 
15488 N N   . LEU C 161  ? 2.6879 1.4564 1.1043 0.1004  -0.6463 -0.0454 161  LEU B N   
15489 C CA  . LEU C 161  ? 2.6681 1.4258 1.1093 0.1268  -0.6200 -0.0442 161  LEU B CA  
15490 C C   . LEU C 161  ? 2.6569 1.4292 1.0984 0.1512  -0.6075 -0.0331 161  LEU B C   
15491 O O   . LEU C 161  ? 2.6897 1.4877 1.1162 0.1484  -0.6195 -0.0231 161  LEU B O   
15492 C CB  . LEU C 161  ? 2.5945 1.3800 1.0901 0.1287  -0.6123 -0.0362 161  LEU B CB  
15493 C CG  . LEU C 161  ? 2.5572 1.3934 1.0814 0.1118  -0.6292 -0.0217 161  LEU B CG  
15494 C CD1 . LEU C 161  ? 2.5538 1.4345 1.0937 0.1234  -0.6293 -0.0027 161  LEU B CD1 
15495 C CD2 . LEU C 161  ? 2.5008 1.3535 1.0708 0.1116  -0.6209 -0.0185 161  LEU B CD2 
15496 N N   . THR C 162  ? 2.6181 1.3752 1.0789 0.1752  -0.5832 -0.0343 162  THR B N   
15497 C CA  . THR C 162  ? 2.5928 1.3477 1.0479 0.2004  -0.5672 -0.0279 162  THR B CA  
15498 C C   . THR C 162  ? 2.5552 1.3077 1.0524 0.2247  -0.5408 -0.0262 162  THR B C   
15499 O O   . THR C 162  ? 2.5607 1.2696 1.0463 0.2341  -0.5268 -0.0401 162  THR B O   
15500 C CB  . THR C 162  ? 2.9531 1.6574 1.3483 0.2007  -0.5679 -0.0432 162  THR B CB  
15501 O OG1 . THR C 162  ? 2.9411 1.6231 1.3380 0.2285  -0.5435 -0.0437 162  THR B OG1 
15502 C CG2 . THR C 162  ? 2.9375 1.5952 1.3050 0.1809  -0.5757 -0.0645 162  THR B CG2 
15503 N N   . PHE C 163  ? 2.5110 1.3108 1.0582 0.2344  -0.5338 -0.0096 163  PHE B N   
15504 C CA  . PHE C 163  ? 2.4644 1.2689 1.0572 0.2572  -0.5086 -0.0075 163  PHE B CA  
15505 C C   . PHE C 163  ? 2.4809 1.2546 1.0624 0.2823  -0.4878 -0.0112 163  PHE B C   
15506 O O   . PHE C 163  ? 2.5233 1.2978 1.0809 0.2907  -0.4880 -0.0036 163  PHE B O   
15507 C CB  . PHE C 163  ? 2.4146 1.2768 1.0581 0.2649  -0.5044 0.0131  163  PHE B CB  
15508 C CG  . PHE C 163  ? 2.3876 1.2855 1.0475 0.2426  -0.5231 0.0200  163  PHE B CG  
15509 C CD1 . PHE C 163  ? 2.4311 1.3356 1.0569 0.2211  -0.5480 0.0226  163  PHE B CD1 
15510 C CD2 . PHE C 163  ? 2.3352 1.2608 1.0454 0.2430  -0.5155 0.0236  163  PHE B CD2 
15511 C CE1 . PHE C 163  ? 2.4387 1.3763 1.0821 0.2007  -0.5649 0.0296  163  PHE B CE1 
15512 C CE2 . PHE C 163  ? 2.3286 1.2870 1.0552 0.2231  -0.5316 0.0308  163  PHE B CE2 
15513 C CZ  . PHE C 163  ? 2.3910 1.3556 1.0855 0.2020  -0.5563 0.0344  163  PHE B CZ  
15514 N N   . ILE C 164  ? 2.4578 1.2075 1.0592 0.2955  -0.4689 -0.0215 164  ILE B N   
15515 C CA  . ILE C 164  ? 2.5110 1.2277 1.1011 0.3183  -0.4494 -0.0260 164  ILE B CA  
15516 C C   . ILE C 164  ? 2.4968 1.2268 1.1404 0.3413  -0.4249 -0.0224 164  ILE B C   
15517 O O   . ILE C 164  ? 2.4765 1.1995 1.1450 0.3408  -0.4179 -0.0324 164  ILE B O   
15518 C CB  . ILE C 164  ? 2.5772 1.2371 1.1296 0.3128  -0.4492 -0.0460 164  ILE B CB  
15519 C CG1 . ILE C 164  ? 2.6565 1.2999 1.1572 0.2873  -0.4735 -0.0527 164  ILE B CG1 
15520 C CG2 . ILE C 164  ? 2.6077 1.2335 1.1471 0.3365  -0.4289 -0.0494 164  ILE B CG2 
15521 C CD1 . ILE C 164  ? 2.6977 1.2817 1.1586 0.2810  -0.4728 -0.0725 164  ILE B CD1 
15522 N N   . ASP C 165  ? 2.5425 1.2916 1.2041 0.3619  -0.4112 -0.0084 165  ASP B N   
15523 C CA  . ASP C 165  ? 2.5449 1.3132 1.2643 0.3833  -0.3876 -0.0036 165  ASP B CA  
15524 C C   . ASP C 165  ? 2.4826 1.2098 1.2070 0.3944  -0.3709 -0.0210 165  ASP B C   
15525 O O   . ASP C 165  ? 2.4655 1.1474 1.1472 0.3906  -0.3742 -0.0337 165  ASP B O   
15526 C CB  . ASP C 165  ? 2.6672 1.4594 1.4040 0.4050  -0.3741 0.0155  165  ASP B CB  
15527 C CG  . ASP C 165  ? 2.8082 1.5599 1.5197 0.4250  -0.3583 0.0117  165  ASP B CG  
15528 O OD1 . ASP C 165  ? 2.8684 1.5721 1.5452 0.4212  -0.3590 -0.0060 165  ASP B OD1 
15529 O OD2 . ASP C 165  ? 2.8460 1.6150 1.5742 0.4451  -0.3444 0.0276  165  ASP B OD2 
15530 N N   . PRO C 166  ? 2.4566 1.2007 1.2351 0.4083  -0.3526 -0.0218 166  PRO B N   
15531 C CA  . PRO C 166  ? 2.4512 1.1640 1.2435 0.4181  -0.3372 -0.0382 166  PRO B CA  
15532 C C   . PRO C 166  ? 2.4497 1.1199 1.2188 0.4364  -0.3228 -0.0424 166  PRO B C   
15533 O O   . PRO C 166  ? 2.4288 1.0751 1.2147 0.4484  -0.3073 -0.0539 166  PRO B O   
15534 C CB  . PRO C 166  ? 2.4262 1.1758 1.2853 0.4321  -0.3192 -0.0341 166  PRO B CB  
15535 C CG  . PRO C 166  ? 2.4277 1.2270 1.3057 0.4214  -0.3303 -0.0188 166  PRO B CG  
15536 C CD  . PRO C 166  ? 2.4560 1.2531 1.2883 0.4143  -0.3459 -0.0070 166  PRO B CD  
15537 N N   . GLU C 167  ? 2.4842 1.1458 1.2161 0.4392  -0.3273 -0.0332 167  GLU B N   
15538 C CA  . GLU C 167  ? 2.5283 1.1486 1.2371 0.4570  -0.3126 -0.0370 167  GLU B CA  
15539 C C   . GLU C 167  ? 2.5835 1.1664 1.2254 0.4421  -0.3291 -0.0445 167  GLU B C   
15540 O O   . GLU C 167  ? 2.6304 1.1704 1.2432 0.4520  -0.3199 -0.0516 167  GLU B O   
15541 C CB  . GLU C 167  ? 2.5682 1.2085 1.2955 0.4796  -0.2970 -0.0191 167  GLU B CB  
15542 C CG  . GLU C 167  ? 2.5661 1.2237 1.3582 0.5017  -0.2718 -0.0161 167  GLU B CG  
15543 C CD  . GLU C 167  ? 2.6162 1.2906 1.4259 0.5251  -0.2549 0.0029  167  GLU B CD  
15544 O OE1 . GLU C 167  ? 2.6504 1.2910 1.4344 0.5399  -0.2440 0.0029  167  GLU B OE1 
15545 O OE2 . GLU C 167  ? 2.6116 1.3329 1.4615 0.5290  -0.2519 0.0188  167  GLU B OE2 
15546 N N   . GLY C 168  ? 2.5831 1.1819 1.2017 0.4178  -0.3531 -0.0436 168  GLY B N   
15547 C CA  . GLY C 168  ? 2.6426 1.2046 1.2008 0.4001  -0.3696 -0.0544 168  GLY B CA  
15548 C C   . GLY C 168  ? 2.7146 1.2806 1.2309 0.3987  -0.3791 -0.0449 168  GLY B C   
15549 O O   . GLY C 168  ? 2.7690 1.2962 1.2324 0.3924  -0.3852 -0.0544 168  GLY B O   
15550 N N   . SER C 169  ? 2.7260 1.3392 1.2661 0.4051  -0.3797 -0.0259 169  SER B N   
15551 C CA  . SER C 169  ? 2.7986 1.4264 1.2991 0.3971  -0.3957 -0.0159 169  SER B CA  
15552 C C   . SER C 169  ? 2.7642 1.4323 1.2723 0.3729  -0.4194 -0.0102 169  SER B C   
15553 O O   . SER C 169  ? 2.7089 1.4098 1.2661 0.3714  -0.4175 -0.0047 169  SER B O   
15554 C CB  . SER C 169  ? 2.8554 1.5073 1.3695 0.4212  -0.3811 0.0040  169  SER B CB  
15555 O OG  . SER C 169  ? 2.9219 1.5771 1.3853 0.4145  -0.3960 0.0103  169  SER B OG  
15556 N N   . GLU C 170  ? 2.7872 1.4522 1.2465 0.3534  -0.4418 -0.0124 170  GLU B N   
15557 C CA  . GLU C 170  ? 2.7884 1.4920 1.2529 0.3298  -0.4656 -0.0062 170  GLU B CA  
15558 C C   . GLU C 170  ? 2.6937 1.4546 1.2041 0.3419  -0.4605 0.0179  170  GLU B C   
15559 O O   . GLU C 170  ? 2.6521 1.4186 1.1820 0.3672  -0.4401 0.0287  170  GLU B O   
15560 C CB  . GLU C 170  ? 2.9249 1.6184 1.3290 0.3101  -0.4889 -0.0111 170  GLU B CB  
15561 C CG  . GLU C 170  ? 3.0373 1.6712 1.3923 0.2976  -0.4933 -0.0354 170  GLU B CG  
15562 C CD  . GLU C 170  ? 3.1668 1.7937 1.4645 0.2763  -0.5170 -0.0418 170  GLU B CD  
15563 O OE1 . GLU C 170  ? 3.2206 1.8651 1.4954 0.2835  -0.5202 -0.0310 170  GLU B OE1 
15564 O OE2 . GLU C 170  ? 3.1993 1.8041 1.4761 0.2525  -0.5321 -0.0575 170  GLU B OE2 
15565 N N   . VAL C 171  ? 2.6607 1.4641 1.1907 0.3247  -0.4777 0.0273  171  VAL B N   
15566 C CA  . VAL C 171  ? 2.6442 1.5035 1.2183 0.3353  -0.4734 0.0517  171  VAL B CA  
15567 C C   . VAL C 171  ? 2.5885 1.4888 1.1583 0.3123  -0.4997 0.0624  171  VAL B C   
15568 O O   . VAL C 171  ? 2.5818 1.5296 1.1776 0.3183  -0.5007 0.0845  171  VAL B O   
15569 C CB  . VAL C 171  ? 2.6393 1.5176 1.2804 0.3490  -0.4528 0.0556  171  VAL B CB  
15570 C CG1 . VAL C 171  ? 2.6296 1.5682 1.3181 0.3555  -0.4507 0.0808  171  VAL B CG1 
15571 C CG2 . VAL C 171  ? 2.6456 1.4917 1.2989 0.3753  -0.4249 0.0490  171  VAL B CG2 
15572 N N   . ASP C 172  ? 2.5772 1.4597 1.1161 0.2860  -0.5208 0.0475  172  ASP B N   
15573 C CA  . ASP C 172  ? 2.6005 1.5204 1.1360 0.2623  -0.5469 0.0563  172  ASP B CA  
15574 C C   . ASP C 172  ? 2.6472 1.5314 1.1317 0.2359  -0.5682 0.0357  172  ASP B C   
15575 O O   . ASP C 172  ? 2.6666 1.4991 1.1157 0.2378  -0.5622 0.0169  172  ASP B O   
15576 C CB  . ASP C 172  ? 2.5784 1.5389 1.1743 0.2580  -0.5452 0.0665  172  ASP B CB  
15577 C CG  . ASP C 172  ? 2.6124 1.6254 1.2196 0.2414  -0.5669 0.0845  172  ASP B CG  
15578 O OD1 . ASP C 172  ? 2.5822 1.6389 1.2435 0.2475  -0.5597 0.1016  172  ASP B OD1 
15579 O OD2 . ASP C 172  ? 2.6667 1.6775 1.2309 0.2220  -0.5906 0.0813  172  ASP B OD2 
15580 N N   . MET C 173  ? 2.6636 1.5752 1.1464 0.2113  -0.5924 0.0394  173  MET B N   
15581 C CA  . MET C 173  ? 2.6915 1.5728 1.1315 0.1848  -0.6129 0.0206  173  MET B CA  
15582 C C   . MET C 173  ? 2.6618 1.5883 1.1166 0.1620  -0.6369 0.0316  173  MET B C   
15583 O O   . MET C 173  ? 2.6594 1.6355 1.1404 0.1679  -0.6394 0.0535  173  MET B O   
15584 C CB  . MET C 173  ? 2.7711 1.6215 1.1492 0.1848  -0.6189 0.0107  173  MET B CB  
15585 C CG  . MET C 173  ? 2.8315 1.6267 1.1653 0.1670  -0.6266 -0.0157 173  MET B CG  
15586 S SD  . MET C 173  ? 3.0882 1.8306 1.3545 0.1759  -0.6207 -0.0320 173  MET B SD  
15587 C CE  . MET C 173  ? 2.9645 1.7126 1.2587 0.2153  -0.5893 -0.0167 173  MET B CE  
15588 N N   . VAL C 174  ? 2.6444 1.5545 1.0859 0.1363  -0.6534 0.0176  174  VAL B N   
15589 C CA  . VAL C 174  ? 2.6516 1.5995 1.0997 0.1114  -0.6791 0.0257  174  VAL B CA  
15590 C C   . VAL C 174  ? 2.6779 1.5974 1.1080 0.0836  -0.6949 0.0070  174  VAL B C   
15591 O O   . VAL C 174  ? 2.6891 1.5786 1.1306 0.0840  -0.6837 -0.0045 174  VAL B O   
15592 C CB  . VAL C 174  ? 2.6704 1.6753 1.1806 0.1165  -0.6754 0.0491  174  VAL B CB  
15593 C CG1 . VAL C 174  ? 2.6205 1.6169 1.1726 0.1353  -0.6492 0.0485  174  VAL B CG1 
15594 C CG2 . VAL C 174  ? 2.6713 1.7033 1.1949 0.0882  -0.6989 0.0524  174  VAL B CG2 
15595 N N   . GLU C 175  ? 2.6797 1.6089 1.0820 0.0597  -0.7207 0.0041  175  GLU B N   
15596 C CA  . GLU C 175  ? 2.6960 1.6035 1.0850 0.0316  -0.7374 -0.0118 175  GLU B CA  
15597 C C   . GLU C 175  ? 2.6574 1.6132 1.0889 0.0149  -0.7520 0.0033  175  GLU B C   
15598 O O   . GLU C 175  ? 2.6018 1.6066 1.0673 0.0248  -0.7504 0.0253  175  GLU B O   
15599 C CB  . GLU C 175  ? 2.8146 1.6988 1.1453 0.0150  -0.7560 -0.0275 175  GLU B CB  
15600 C CG  . GLU C 175  ? 2.8784 1.7856 1.1842 0.0273  -0.7594 -0.0172 175  GLU B CG  
15601 C CD  . GLU C 175  ? 2.9453 1.8095 1.1858 0.0237  -0.7640 -0.0379 175  GLU B CD  
15602 O OE1 . GLU C 175  ? 2.9796 1.8222 1.1890 -0.0019 -0.7823 -0.0561 175  GLU B OE1 
15603 O OE2 . GLU C 175  ? 2.9550 1.8071 1.1763 0.0469  -0.7484 -0.0358 175  GLU B OE2 
15604 N N   . GLU C 176  ? 2.6862 1.6282 1.1185 -0.0093 -0.7646 -0.0074 176  GLU B N   
15605 C CA  . GLU C 176  ? 2.7096 1.6947 1.1811 -0.0274 -0.7794 0.0060  176  GLU B CA  
15606 C C   . GLU C 176  ? 2.7801 1.7374 1.2371 -0.0559 -0.7947 -0.0108 176  GLU B C   
15607 O O   . GLU C 176  ? 2.8014 1.7060 1.2293 -0.0577 -0.7881 -0.0312 176  GLU B O   
15608 C CB  . GLU C 176  ? 2.6280 1.6394 1.1563 -0.0121 -0.7609 0.0215  176  GLU B CB  
15609 C CG  . GLU C 176  ? 2.8073 1.8789 1.3823 -0.0217 -0.7720 0.0438  176  GLU B CG  
15610 C CD  . GLU C 176  ? 2.9553 2.0750 1.5579 -0.0015 -0.7644 0.0673  176  GLU B CD  
15611 O OE1 . GLU C 176  ? 2.9781 2.1025 1.5526 0.0059  -0.7688 0.0703  176  GLU B OE1 
15612 O OE2 . GLU C 176  ? 2.9061 2.0603 1.5595 0.0069  -0.7535 0.0834  176  GLU B OE2 
15613 N N   . ILE C 177  ? 2.8426 1.8351 1.3216 -0.0778 -0.8146 -0.0018 177  ILE B N   
15614 C CA  . ILE C 177  ? 2.9217 1.8925 1.3875 -0.1071 -0.8321 -0.0166 177  ILE B CA  
15615 C C   . ILE C 177  ? 2.9227 1.8846 1.4239 -0.1121 -0.8230 -0.0163 177  ILE B C   
15616 O O   . ILE C 177  ? 2.8688 1.8631 1.4143 -0.1007 -0.8121 0.0009  177  ILE B O   
15617 C CB  . ILE C 177  ? 2.9565 1.9686 1.4244 -0.1309 -0.8609 -0.0085 177  ILE B CB  
15618 C CG1 . ILE C 177  ? 2.9083 1.9745 1.4340 -0.1342 -0.8640 0.0154  177  ILE B CG1 
15619 C CG2 . ILE C 177  ? 2.9859 2.0169 1.4234 -0.1233 -0.8693 -0.0044 177  ILE B CG2 
15620 C CD1 . ILE C 177  ? 2.8872 1.9460 1.4389 -0.1543 -0.8685 0.0121  177  ILE B CD1 
15621 N N   . ASP C 178  ? 3.0052 1.9244 1.4876 -0.1292 -0.8270 -0.0349 178  ASP B N   
15622 C CA  . ASP C 178  ? 3.0194 1.9255 1.5315 -0.1331 -0.8171 -0.0351 178  ASP B CA  
15623 C C   . ASP C 178  ? 3.0743 2.0007 1.6101 -0.1606 -0.8356 -0.0305 178  ASP B C   
15624 O O   . ASP C 178  ? 3.1207 2.0150 1.6387 -0.1811 -0.8450 -0.0458 178  ASP B O   
15625 C CB  . ASP C 178  ? 3.0114 1.8549 1.4945 -0.1300 -0.8039 -0.0562 178  ASP B CB  
15626 C CG  . ASP C 178  ? 2.9256 1.7596 1.4406 -0.1225 -0.7865 -0.0528 178  ASP B CG  
15627 O OD1 . ASP C 178  ? 2.9132 1.7005 1.4101 -0.1146 -0.7721 -0.0665 178  ASP B OD1 
15628 O OD2 . ASP C 178  ? 2.8620 1.7364 1.4199 -0.1243 -0.7870 -0.0360 178  ASP B OD2 
15629 N N   . HIS C 179  ? 3.0586 2.0377 1.6374 -0.1606 -0.8391 -0.0090 179  HIS B N   
15630 C CA  . HIS C 179  ? 3.0899 2.0942 1.6955 -0.1857 -0.8567 -0.0015 179  HIS B CA  
15631 C C   . HIS C 179  ? 3.0274 2.0108 1.6550 -0.1917 -0.8469 -0.0042 179  HIS B C   
15632 O O   . HIS C 179  ? 3.0366 2.0147 1.6701 -0.2158 -0.8606 -0.0079 179  HIS B O   
15633 C CB  . HIS C 179  ? 3.1330 2.2012 1.7792 -0.1829 -0.8626 0.0237  179  HIS B CB  
15634 C CG  . HIS C 179  ? 3.2325 2.3309 1.8903 -0.2103 -0.8889 0.0298  179  HIS B CG  
15635 N ND1 . HIS C 179  ? 3.2926 2.4214 1.9381 -0.2168 -0.9079 0.0354  179  HIS B ND1 
15636 C CD2 . HIS C 179  ? 3.2772 2.3807 1.9586 -0.2329 -0.8995 0.0316  179  HIS B CD2 
15637 C CE1 . HIS C 179  ? 3.3305 2.4823 1.9921 -0.2428 -0.9297 0.0397  179  HIS B CE1 
15638 N NE2 . HIS C 179  ? 3.3191 2.4554 2.0033 -0.2529 -0.9248 0.0375  179  HIS B NE2 
15639 N N   . ILE C 180  ? 2.9747 1.9470 1.6152 -0.1701 -0.8233 -0.0021 180  ILE B N   
15640 C CA  . ILE C 180  ? 2.9310 1.8870 1.5926 -0.1746 -0.8137 -0.0028 180  ILE B CA  
15641 C C   . ILE C 180  ? 2.8548 1.7649 1.5004 -0.1575 -0.7919 -0.0153 180  ILE B C   
15642 O O   . ILE C 180  ? 2.8070 1.6900 1.4557 -0.1655 -0.7874 -0.0213 180  ILE B O   
15643 C CB  . ILE C 180  ? 2.6745 1.6800 1.3887 -0.1738 -0.8105 0.0191  180  ILE B CB  
15644 C CG1 . ILE C 180  ? 2.6160 1.6518 1.3504 -0.1474 -0.7940 0.0315  180  ILE B CG1 
15645 C CG2 . ILE C 180  ? 2.6946 1.7391 1.4265 -0.1955 -0.8334 0.0306  180  ILE B CG2 
15646 C CD1 . ILE C 180  ? 2.5604 1.6448 1.3454 -0.1477 -0.7909 0.0520  180  ILE B CD1 
15647 N N   . GLY C 181  ? 2.8266 1.7283 1.4561 -0.1342 -0.7786 -0.0187 181  GLY B N   
15648 C CA  . GLY C 181  ? 2.7826 1.6424 1.3972 -0.1174 -0.7585 -0.0303 181  GLY B CA  
15649 C C   . GLY C 181  ? 2.7096 1.5929 1.3458 -0.0901 -0.7397 -0.0205 181  GLY B C   
15650 O O   . GLY C 181  ? 2.7052 1.5603 1.3311 -0.0717 -0.7219 -0.0287 181  GLY B O   
15651 N N   . ILE C 182  ? 2.6470 1.5825 1.3156 -0.0883 -0.7436 -0.0029 182  ILE B N   
15652 C CA  . ILE C 182  ? 2.5778 1.5423 1.2725 -0.0638 -0.7265 0.0077  182  ILE B CA  
15653 C C   . ILE C 182  ? 2.5888 1.5741 1.2736 -0.0550 -0.7313 0.0136  182  ILE B C   
15654 O O   . ILE C 182  ? 2.5655 1.5983 1.2809 -0.0518 -0.7333 0.0306  182  ILE B O   
15655 C CB  . ILE C 182  ? 2.5363 1.5469 1.2802 -0.0657 -0.7236 0.0249  182  ILE B CB  
15656 C CG1 . ILE C 182  ? 2.5381 1.5323 1.2898 -0.0798 -0.7241 0.0215  182  ILE B CG1 
15657 C CG2 . ILE C 182  ? 2.4815 1.5137 1.2528 -0.0395 -0.7018 0.0316  182  ILE B CG2 
15658 C CD1 . ILE C 182  ? 2.5239 1.5606 1.3154 -0.0931 -0.7310 0.0379  182  ILE B CD1 
15659 N N   . ILE C 183  ? 2.5907 1.5407 1.2328 -0.0513 -0.7328 0.0002  183  ILE B N   
15660 C CA  . ILE C 183  ? 2.5791 1.5440 1.2071 -0.0399 -0.7348 0.0050  183  ILE B CA  
15661 C C   . ILE C 183  ? 2.5314 1.5337 1.1969 -0.0163 -0.7178 0.0206  183  ILE B C   
15662 O O   . ILE C 183  ? 2.5149 1.5034 1.1921 0.0025  -0.6967 0.0166  183  ILE B O   
15663 C CB  . ILE C 183  ? 2.5889 1.5044 1.1718 -0.0294 -0.7274 -0.0125 183  ILE B CB  
15664 C CG1 . ILE C 183  ? 2.6409 1.5178 1.1841 -0.0525 -0.7436 -0.0294 183  ILE B CG1 
15665 C CG2 . ILE C 183  ? 2.6142 1.5457 1.1843 -0.0143 -0.7261 -0.0060 183  ILE B CG2 
15666 C CD1 . ILE C 183  ? 2.6693 1.4951 1.1659 -0.0432 -0.7360 -0.0475 183  ILE B CD1 
15667 N N   . SER C 184  ? 2.4954 1.5451 1.1808 -0.0174 -0.7266 0.0380  184  SER B N   
15668 C CA  . SER C 184  ? 2.4590 1.5486 1.1857 0.0034  -0.7107 0.0547  184  SER B CA  
15669 C C   . SER C 184  ? 2.5479 1.6497 1.2638 0.0210  -0.7067 0.0620  184  SER B C   
15670 O O   . SER C 184  ? 2.5774 1.7114 1.2925 0.0139  -0.7221 0.0749  184  SER B O   
15671 C CB  . SER C 184  ? 2.4129 1.5533 1.1833 -0.0089 -0.7194 0.0732  184  SER B CB  
15672 O OG  . SER C 184  ? 2.4213 1.5505 1.1909 -0.0317 -0.7313 0.0673  184  SER B OG  
15673 N N   . PHE C 185  ? 2.5450 1.6225 1.2546 0.0444  -0.6857 0.0548  185  PHE B N   
15674 C CA  . PHE C 185  ? 2.5305 1.6126 1.2278 0.0634  -0.6787 0.0605  185  PHE B CA  
15675 C C   . PHE C 185  ? 2.4772 1.6084 1.2231 0.0809  -0.6657 0.0817  185  PHE B C   
15676 O O   . PHE C 185  ? 2.4182 1.5763 1.2079 0.0805  -0.6588 0.0897  185  PHE B O   
15677 C CB  . PHE C 185  ? 2.5482 1.5824 1.2216 0.0819  -0.6600 0.0442  185  PHE B CB  
15678 C CG  . PHE C 185  ? 2.5946 1.5776 1.2161 0.0689  -0.6700 0.0239  185  PHE B CG  
15679 C CD1 . PHE C 185  ? 2.6316 1.5976 1.2089 0.0685  -0.6787 0.0191  185  PHE B CD1 
15680 C CD2 . PHE C 185  ? 2.5928 1.5447 1.2104 0.0579  -0.6694 0.0099  185  PHE B CD2 
15681 C CE1 . PHE C 185  ? 2.6888 1.6062 1.2189 0.0568  -0.6863 -0.0008 185  PHE B CE1 
15682 C CE2 . PHE C 185  ? 2.6522 1.5558 1.2248 0.0465  -0.6768 -0.0085 185  PHE B CE2 
15683 C CZ  . PHE C 185  ? 2.7005 1.5859 1.2292 0.0456  -0.6850 -0.0147 185  PHE B CZ  
15684 N N   . PRO C 186  ? 2.5161 1.6580 1.2552 0.0974  -0.6604 0.0908  186  PRO B N   
15685 C CA  . PRO C 186  ? 2.5078 1.6990 1.2944 0.1129  -0.6492 0.1132  186  PRO B CA  
15686 C C   . PRO C 186  ? 2.5071 1.6864 1.3189 0.1398  -0.6192 0.1094  186  PRO B C   
15687 O O   . PRO C 186  ? 2.5322 1.6697 1.3137 0.1514  -0.6095 0.0950  186  PRO B O   
15688 C CB  . PRO C 186  ? 2.5576 1.7632 1.3188 0.1167  -0.6596 0.1244  186  PRO B CB  
15689 C CG  . PRO C 186  ? 2.6040 1.7568 1.3019 0.1108  -0.6680 0.1030  186  PRO B CG  
15690 C CD  . PRO C 186  ? 2.5712 1.6802 1.2621 0.1056  -0.6608 0.0815  186  PRO B CD  
15691 N N   . ASP C 187  ? 2.4557 1.6714 1.3229 0.1490  -0.6048 0.1220  187  ASP B N   
15692 C CA  . ASP C 187  ? 2.4228 1.6339 1.3226 0.1738  -0.5757 0.1189  187  ASP B CA  
15693 C C   . ASP C 187  ? 2.3963 1.5915 1.2801 0.1966  -0.5626 0.1200  187  ASP B C   
15694 O O   . ASP C 187  ? 2.3991 1.6104 1.2670 0.1978  -0.5722 0.1333  187  ASP B O   
15695 C CB  . ASP C 187  ? 2.4052 1.6665 1.3684 0.1800  -0.5636 0.1360  187  ASP B CB  
15696 C CG  . ASP C 187  ? 2.4236 1.6968 1.4062 0.1613  -0.5708 0.1330  187  ASP B CG  
15697 O OD1 . ASP C 187  ? 2.4631 1.7167 1.4125 0.1398  -0.5907 0.1240  187  ASP B OD1 
15698 O OD2 . ASP C 187  ? 2.4019 1.7046 1.4342 0.1683  -0.5557 0.1398  187  ASP B OD2 
15699 N N   . PHE C 188  ? 2.3569 1.5215 1.2451 0.2144  -0.5408 0.1060  188  PHE B N   
15700 C CA  . PHE C 188  ? 2.3338 1.4768 1.2080 0.2370  -0.5256 0.1045  188  PHE B CA  
15701 C C   . PHE C 188  ? 2.2973 1.4618 1.2271 0.2611  -0.4977 0.1119  188  PHE B C   
15702 O O   . PHE C 188  ? 2.2753 1.4249 1.2258 0.2681  -0.4819 0.0985  188  PHE B O   
15703 C CB  . PHE C 188  ? 2.3020 1.3867 1.1337 0.2368  -0.5236 0.0804  188  PHE B CB  
15704 C CG  . PHE C 188  ? 2.3006 1.3582 1.1210 0.2611  -0.5048 0.0764  188  PHE B CG  
15705 C CD1 . PHE C 188  ? 2.2617 1.3063 1.1121 0.2804  -0.4798 0.0680  188  PHE B CD1 
15706 C CD2 . PHE C 188  ? 2.3366 1.3800 1.1147 0.2641  -0.5121 0.0797  188  PHE B CD2 
15707 C CE1 . PHE C 188  ? 2.2716 1.2894 1.1132 0.3028  -0.4620 0.0641  188  PHE B CE1 
15708 C CE2 . PHE C 188  ? 2.3530 1.3697 1.1203 0.2871  -0.4938 0.0763  188  PHE B CE2 
15709 C CZ  . PHE C 188  ? 2.3118 1.3154 1.1124 0.3064  -0.4684 0.0688  188  PHE B CZ  
15710 N N   . LYS C 189  ? 2.2921 1.4931 1.2474 0.2736  -0.4917 0.1337  189  LYS B N   
15711 C CA  . LYS C 189  ? 2.2543 1.4824 1.2693 0.2954  -0.4653 0.1438  189  LYS B CA  
15712 C C   . LYS C 189  ? 2.2052 1.3998 1.2196 0.3196  -0.4417 0.1329  189  LYS B C   
15713 O O   . LYS C 189  ? 2.2540 1.4320 1.2391 0.3303  -0.4407 0.1366  189  LYS B O   
15714 C CB  . LYS C 189  ? 2.2563 1.5339 1.2974 0.3006  -0.4672 0.1727  189  LYS B CB  
15715 C CG  . LYS C 189  ? 2.2740 1.5696 1.3606 0.3289  -0.4393 0.1860  189  LYS B CG  
15716 C CD  . LYS C 189  ? 2.2601 1.5894 1.4144 0.3341  -0.4213 0.1912  189  LYS B CD  
15717 C CE  . LYS C 189  ? 2.2587 1.6199 1.4622 0.3582  -0.3986 0.2128  189  LYS B CE  
15718 N NZ  . LYS C 189  ? 2.2826 1.6156 1.4620 0.3781  -0.3878 0.2120  189  LYS B NZ  
15719 N N   . ILE C 190  ? 2.1692 1.3546 1.2162 0.3281  -0.4226 0.1192  190  ILE B N   
15720 C CA  . ILE C 190  ? 2.1489 1.3070 1.2052 0.3516  -0.3985 0.1093  190  ILE B CA  
15721 C C   . ILE C 190  ? 2.2107 1.3976 1.3038 0.3742  -0.3803 0.1305  190  ILE B C   
15722 O O   . ILE C 190  ? 2.2376 1.4687 1.3798 0.3767  -0.3735 0.1466  190  ILE B O   
15723 C CB  . ILE C 190  ? 2.1269 1.2798 1.2187 0.3545  -0.3827 0.0920  190  ILE B CB  
15724 C CG1 . ILE C 190  ? 2.0186 1.1616 1.0861 0.3294  -0.4025 0.0790  190  ILE B CG1 
15725 C CG2 . ILE C 190  ? 2.0067 1.1212 1.0971 0.3742  -0.3624 0.0759  190  ILE B CG2 
15726 C CD1 . ILE C 190  ? 2.0394 1.1290 1.0592 0.3241  -0.4084 0.0568  190  ILE B CD1 
15727 N N   . PRO C 191  ? 2.2069 1.3689 1.2770 0.3911  -0.3719 0.1318  191  PRO B N   
15728 C CA  . PRO C 191  ? 2.2329 1.4164 1.3334 0.4148  -0.3532 0.1522  191  PRO B CA  
15729 C C   . PRO C 191  ? 2.1984 1.4123 1.3743 0.4311  -0.3262 0.1581  191  PRO B C   
15730 O O   . PRO C 191  ? 2.1817 1.3864 1.3830 0.4306  -0.3155 0.1400  191  PRO B O   
15731 C CB  . PRO C 191  ? 2.2048 1.3414 1.2722 0.4306  -0.3427 0.1408  191  PRO B CB  
15732 C CG  . PRO C 191  ? 2.2423 1.3426 1.2435 0.4103  -0.3669 0.1249  191  PRO B CG  
15733 C CD  . PRO C 191  ? 2.2344 1.3442 1.2436 0.3872  -0.3808 0.1142  191  PRO B CD  
15734 N N   . SER C 192  ? 2.2354 1.4858 1.4467 0.4458  -0.3150 0.1836  192  SER B N   
15735 C CA  . SER C 192  ? 2.1656 1.4463 1.4517 0.4628  -0.2874 0.1917  192  SER B CA  
15736 C C   . SER C 192  ? 2.0944 1.3418 1.4000 0.4800  -0.2626 0.1706  192  SER B C   
15737 O O   . SER C 192  ? 2.0122 1.2698 1.3676 0.4840  -0.2454 0.1605  192  SER B O   
15738 C CB  . SER C 192  ? 2.2060 1.5217 1.5194 0.4800  -0.2771 0.2232  192  SER B CB  
15739 O OG  . SER C 192  ? 2.2485 1.5857 1.5262 0.4658  -0.3032 0.2420  192  SER B OG  
15740 N N   . ASN C 193  ? 2.1261 1.3339 1.3910 0.4896  -0.2613 0.1638  193  ASN B N   
15741 C CA  . ASN C 193  ? 2.1248 1.2959 1.3997 0.5057  -0.2403 0.1441  193  ASN B CA  
15742 C C   . ASN C 193  ? 2.1944 1.3144 1.3987 0.4989  -0.2552 0.1280  193  ASN B C   
15743 O O   . ASN C 193  ? 2.2174 1.3173 1.3945 0.5121  -0.2513 0.1349  193  ASN B O   
15744 C CB  . ASN C 193  ? 2.1417 1.3233 1.4586 0.5343  -0.2126 0.1606  193  ASN B CB  
15745 C CG  . ASN C 193  ? 2.1638 1.3006 1.4702 0.5515  -0.1962 0.1451  193  ASN B CG  
15746 O OD1 . ASN C 193  ? 2.1614 1.2626 1.4438 0.5436  -0.2008 0.1198  193  ASN B OD1 
15747 N ND2 . ASN C 193  ? 2.1808 1.3194 1.5062 0.5756  -0.1765 0.1614  193  ASN B ND2 
15748 N N   . PRO C 194  ? 2.1868 1.2861 1.3619 0.4785  -0.2718 0.1071  194  PRO B N   
15749 C CA  . PRO C 194  ? 2.2097 1.2644 1.3161 0.4665  -0.2903 0.0928  194  PRO B CA  
15750 C C   . PRO C 194  ? 2.1978 1.2063 1.2941 0.4819  -0.2743 0.0755  194  PRO B C   
15751 O O   . PRO C 194  ? 2.1326 1.1429 1.2760 0.5019  -0.2489 0.0732  194  PRO B O   
15752 C CB  . PRO C 194  ? 2.2280 1.2830 1.3237 0.4415  -0.3085 0.0780  194  PRO B CB  
15753 C CG  . PRO C 194  ? 2.2108 1.3152 1.3626 0.4388  -0.3032 0.0886  194  PRO B CG  
15754 C CD  . PRO C 194  ? 2.1895 1.3101 1.3969 0.4647  -0.2740 0.0975  194  PRO B CD  
15755 N N   . ARG C 195  ? 2.2588 1.2261 1.2938 0.4717  -0.2897 0.0635  195  ARG B N   
15756 C CA  . ARG C 195  ? 2.3134 1.2310 1.3277 0.4813  -0.2795 0.0451  195  ARG B CA  
15757 C C   . ARG C 195  ? 2.2939 1.2005 1.3176 0.4685  -0.2829 0.0235  195  ARG B C   
15758 O O   . ARG C 195  ? 2.3132 1.2093 1.2998 0.4463  -0.3046 0.0155  195  ARG B O   
15759 C CB  . ARG C 195  ? 2.3903 1.2716 1.3328 0.4729  -0.2968 0.0429  195  ARG B CB  
15760 C CG  . ARG C 195  ? 2.4568 1.3001 1.3799 0.4938  -0.2808 0.0410  195  ARG B CG  
15761 C CD  . ARG C 195  ? 2.5317 1.3930 1.4445 0.5058  -0.2787 0.0640  195  ARG B CD  
15762 N NE  . ARG C 195  ? 2.6201 1.4402 1.4739 0.5095  -0.2822 0.0605  195  ARG B NE  
15763 C CZ  . ARG C 195  ? 2.6567 1.4562 1.5116 0.5335  -0.2616 0.0648  195  ARG B CZ  
15764 N NH1 . ARG C 195  ? 2.6164 1.4327 1.5307 0.5562  -0.2358 0.0730  195  ARG B NH1 
15765 N NH2 . ARG C 195  ? 2.7195 1.4810 1.5164 0.5345  -0.2663 0.0605  195  ARG B NH2 
15766 N N   . TYR C 196  ? 2.2390 1.1492 1.3126 0.4821  -0.2615 0.0142  196  TYR B N   
15767 C CA  . TYR C 196  ? 2.1906 1.1067 1.2844 0.4702  -0.2639 -0.0023 196  TYR B CA  
15768 C C   . TYR C 196  ? 2.1448 1.0148 1.2006 0.4637  -0.2703 -0.0228 196  TYR B C   
15769 O O   . TYR C 196  ? 2.1653 1.0017 1.2146 0.4791  -0.2570 -0.0300 196  TYR B O   
15770 C CB  . TYR C 196  ? 2.1709 1.1091 1.3326 0.4872  -0.2384 -0.0062 196  TYR B CB  
15771 C CG  . TYR C 196  ? 2.1557 1.1455 1.3656 0.4901  -0.2317 0.0117  196  TYR B CG  
15772 C CD1 . TYR C 196  ? 2.1438 1.1662 1.3587 0.4707  -0.2470 0.0161  196  TYR B CD1 
15773 C CD2 . TYR C 196  ? 2.1429 1.1487 1.3960 0.5128  -0.2087 0.0247  196  TYR B CD2 
15774 C CE1 . TYR C 196  ? 2.1125 1.1815 1.3731 0.4735  -0.2400 0.0330  196  TYR B CE1 
15775 C CE2 . TYR C 196  ? 2.1061 1.1586 1.4058 0.5159  -0.2014 0.0420  196  TYR B CE2 
15776 C CZ  . TYR C 196  ? 2.0945 1.1784 1.3975 0.4961  -0.2171 0.0458  196  TYR B CZ  
15777 O OH  . TYR C 196  ? 2.0602 1.1906 1.4111 0.4990  -0.2092 0.0635  196  TYR B OH  
15778 N N   . GLY C 197  ? 2.1475 1.0159 1.1800 0.4412  -0.2896 -0.0311 197  GLY B N   
15779 C CA  . GLY C 197  ? 2.1532 0.9800 1.1534 0.4342  -0.2954 -0.0497 197  GLY B CA  
15780 C C   . GLY C 197  ? 2.1957 1.0089 1.1469 0.4088  -0.3213 -0.0529 197  GLY B C   
15781 O O   . GLY C 197  ? 2.1906 1.0334 1.1420 0.3921  -0.3364 -0.0449 197  GLY B O   
15782 N N   . MET C 198  ? 2.1899 0.9570 1.1003 0.4058  -0.3258 -0.0646 198  MET B N   
15783 C CA  . MET C 198  ? 2.2209 0.9712 1.0897 0.3822  -0.3477 -0.0702 198  MET B CA  
15784 C C   . MET C 198  ? 2.2114 0.9580 1.0357 0.3688  -0.3666 -0.0598 198  MET B C   
15785 O O   . MET C 198  ? 2.1653 0.8772 0.9506 0.3729  -0.3674 -0.0612 198  MET B O   
15786 C CB  . MET C 198  ? 2.2914 0.9938 1.1376 0.3844  -0.3438 -0.0867 198  MET B CB  
15787 C CG  . MET C 198  ? 2.6234 1.3067 1.4369 0.3616  -0.3622 -0.0952 198  MET B CG  
15788 S SD  . MET C 198  ? 2.7694 1.4975 1.6031 0.3398  -0.3778 -0.0912 198  MET B SD  
15789 C CE  . MET C 198  ? 2.0517 0.8248 0.9528 0.3567  -0.3578 -0.0899 198  MET B CE  
15790 N N   . TRP C 199  ? 2.1740 0.9567 1.0040 0.3524  -0.3819 -0.0500 199  TRP B N   
15791 C CA  . TRP C 199  ? 2.2286 1.0101 1.0168 0.3368  -0.4024 -0.0416 199  TRP B CA  
15792 C C   . TRP C 199  ? 2.2512 0.9974 0.9939 0.3161  -0.4197 -0.0535 199  TRP B C   
15793 O O   . TRP C 199  ? 2.2863 1.0189 1.0356 0.3115  -0.4179 -0.0649 199  TRP B O   
15794 C CB  . TRP C 199  ? 2.2328 1.0672 1.0464 0.3275  -0.4121 -0.0252 199  TRP B CB  
15795 C CG  . TRP C 199  ? 2.2575 1.1195 1.1039 0.3480  -0.3965 -0.0109 199  TRP B CG  
15796 C CD1 . TRP C 199  ? 2.2537 1.1253 1.1462 0.3690  -0.3727 -0.0121 199  TRP B CD1 
15797 C CD2 . TRP C 199  ? 2.2970 1.1798 1.1332 0.3504  -0.4024 0.0069  199  TRP B CD2 
15798 N NE1 . TRP C 199  ? 2.2728 1.1692 1.1869 0.3848  -0.3623 0.0046  199  TRP B NE1 
15799 C CE2 . TRP C 199  ? 2.2862 1.1907 1.1658 0.3741  -0.3804 0.0173  199  TRP B CE2 
15800 C CE3 . TRP C 199  ? 2.3158 1.2027 1.1119 0.3347  -0.4243 0.0152  199  TRP B CE3 
15801 C CZ2 . TRP C 199  ? 2.2789 1.2094 1.1630 0.3832  -0.3792 0.0374  199  TRP B CZ2 
15802 C CZ3 . TRP C 199  ? 2.3171 1.2307 1.1158 0.3433  -0.4243 0.0340  199  TRP B CZ3 
15803 C CH2 . TRP C 199  ? 2.3045 1.2398 1.1468 0.3676  -0.4017 0.0458  199  TRP B CH2 
15804 N N   . THR C 200  ? 2.2572 0.9887 0.9547 0.3038  -0.4359 -0.0511 200  THR B N   
15805 C CA  . THR C 200  ? 2.2690 0.9669 0.9256 0.2834  -0.4518 -0.0625 200  THR B CA  
15806 C C   . THR C 200  ? 2.2970 1.0130 0.9289 0.2635  -0.4743 -0.0541 200  THR B C   
15807 O O   . THR C 200  ? 2.3323 1.0567 0.9492 0.2688  -0.4767 -0.0453 200  THR B O   
15808 C CB  . THR C 200  ? 2.3025 0.9452 0.9172 0.2911  -0.4454 -0.0741 200  THR B CB  
15809 O OG1 . THR C 200  ? 2.2791 0.9077 0.9176 0.3149  -0.4221 -0.0786 200  THR B OG1 
15810 C CG2 . THR C 200  ? 2.3271 0.9334 0.9099 0.2723  -0.4569 -0.0873 200  THR B CG2 
15811 N N   . ILE C 201  ? 2.3005 1.0248 0.9292 0.2405  -0.4912 -0.0559 201  ILE B N   
15812 C CA  . ILE C 201  ? 2.3335 1.0681 0.9337 0.2197  -0.5141 -0.0506 201  ILE B CA  
15813 C C   . ILE C 201  ? 2.4086 1.0971 0.9631 0.2019  -0.5261 -0.0656 201  ILE B C   
15814 O O   . ILE C 201  ? 2.4475 1.1267 1.0087 0.1898  -0.5296 -0.0723 201  ILE B O   
15815 C CB  . ILE C 201  ? 2.3123 1.0952 0.9437 0.2039  -0.5270 -0.0392 201  ILE B CB  
15816 C CG1 . ILE C 201  ? 2.2761 1.1082 0.9536 0.2187  -0.5168 -0.0229 201  ILE B CG1 
15817 C CG2 . ILE C 201  ? 2.3693 1.1600 0.9705 0.1818  -0.5512 -0.0350 201  ILE B CG2 
15818 C CD1 . ILE C 201  ? 2.2699 1.1489 0.9663 0.2012  -0.5337 -0.0088 201  ILE B CD1 
15819 N N   . LYS C 202  ? 2.4693 1.1294 0.9781 0.1999  -0.5320 -0.0707 202  LYS B N   
15820 C CA  . LYS C 202  ? 2.5488 1.1667 1.0148 0.1806  -0.5443 -0.0852 202  LYS B CA  
15821 C C   . LYS C 202  ? 2.5178 1.1565 0.9669 0.1549  -0.5697 -0.0815 202  LYS B C   
15822 O O   . LYS C 202  ? 2.5146 1.1951 0.9748 0.1546  -0.5776 -0.0676 202  LYS B O   
15823 C CB  . LYS C 202  ? 2.6239 1.1937 1.0471 0.1913  -0.5356 -0.0962 202  LYS B CB  
15824 C CG  . LYS C 202  ? 2.6740 1.2131 1.1086 0.2141  -0.5115 -0.1028 202  LYS B CG  
15825 C CD  . LYS C 202  ? 2.7763 1.2684 1.1664 0.2237  -0.5037 -0.1125 202  LYS B CD  
15826 C CE  . LYS C 202  ? 2.7935 1.2694 1.2012 0.2522  -0.4783 -0.1128 202  LYS B CE  
15827 N NZ  . LYS C 202  ? 2.8431 1.3063 1.2226 0.2677  -0.4707 -0.1104 202  LYS B NZ  
15828 N N   . ALA C 203  ? 2.5405 1.1509 0.9647 0.1332  -0.5823 -0.0933 203  ALA B N   
15829 C CA  . ALA C 203  ? 2.5822 1.2089 0.9893 0.1075  -0.6068 -0.0918 203  ALA B CA  
15830 C C   . ALA C 203  ? 2.6506 1.2286 1.0122 0.0893  -0.6165 -0.1098 203  ALA B C   
15831 O O   . ALA C 203  ? 2.6329 1.1750 0.9929 0.0866  -0.6092 -0.1204 203  ALA B O   
15832 C CB  . ALA C 203  ? 2.5125 1.1797 0.9599 0.0938  -0.6162 -0.0814 203  ALA B CB  
15833 N N   . LYS C 204  ? 2.7323 1.3106 1.0581 0.0767  -0.6327 -0.1130 204  LYS B N   
15834 C CA  . LYS C 204  ? 2.8238 1.3565 1.1035 0.0586  -0.6422 -0.1318 204  LYS B CA  
15835 C C   . LYS C 204  ? 2.8379 1.3931 1.1056 0.0310  -0.6686 -0.1319 204  LYS B C   
15836 O O   . LYS C 204  ? 2.7911 1.3961 1.0756 0.0288  -0.6799 -0.1170 204  LYS B O   
15837 C CB  . LYS C 204  ? 2.9211 1.4193 1.1574 0.0726  -0.6329 -0.1414 204  LYS B CB  
15838 C CG  . LYS C 204  ? 2.9932 1.5292 1.2273 0.0864  -0.6344 -0.1276 204  LYS B CG  
15839 C CD  . LYS C 204  ? 3.0788 1.5816 1.2784 0.1066  -0.6191 -0.1342 204  LYS B CD  
15840 C CE  . LYS C 204  ? 3.0961 1.6374 1.3130 0.1302  -0.6102 -0.1158 204  LYS B CE  
15841 N NZ  . LYS C 204  ? 3.1598 1.6727 1.3332 0.1448  -0.6011 -0.1218 204  LYS B NZ  
15842 N N   . TYR C 205  ? 2.9017 1.4208 1.1428 0.0095  -0.6782 -0.1485 205  TYR B N   
15843 C CA  . TYR C 205  ? 2.9970 1.5367 1.2302 -0.0183 -0.7035 -0.1500 205  TYR B CA  
15844 C C   . TYR C 205  ? 3.1395 1.6844 1.3310 -0.0193 -0.7142 -0.1540 205  TYR B C   
15845 O O   . TYR C 205  ? 3.2074 1.7111 1.3591 -0.0114 -0.7054 -0.1680 205  TYR B O   
15846 C CB  . TYR C 205  ? 3.0172 1.5176 1.2406 -0.0413 -0.7092 -0.1663 205  TYR B CB  
15847 C CG  . TYR C 205  ? 2.9860 1.5074 1.2560 -0.0501 -0.7106 -0.1561 205  TYR B CG  
15848 C CD1 . TYR C 205  ? 2.9602 1.4511 1.2463 -0.0446 -0.6947 -0.1597 205  TYR B CD1 
15849 C CD2 . TYR C 205  ? 2.9719 1.5461 1.2713 -0.0628 -0.7272 -0.1414 205  TYR B CD2 
15850 C CE1 . TYR C 205  ? 2.9245 1.4372 1.2525 -0.0519 -0.6957 -0.1492 205  TYR B CE1 
15851 C CE2 . TYR C 205  ? 2.9352 1.5298 1.2773 -0.0701 -0.7276 -0.1312 205  TYR B CE2 
15852 C CZ  . TYR C 205  ? 2.9039 1.4678 1.2589 -0.0645 -0.7118 -0.1353 205  TYR B CZ  
15853 O OH  . TYR C 205  ? 2.8531 1.4393 1.2486 -0.0714 -0.7122 -0.1246 205  TYR B OH  
15854 N N   . LYS C 206  ? 3.1657 1.7621 1.3661 -0.0278 -0.7324 -0.1410 206  LYS B N   
15855 C CA  . LYS C 206  ? 3.2344 1.8415 1.3959 -0.0265 -0.7424 -0.1423 206  LYS B CA  
15856 C C   . LYS C 206  ? 3.2986 1.8555 1.4075 -0.0426 -0.7489 -0.1681 206  LYS B C   
15857 O O   . LYS C 206  ? 3.3278 1.8489 1.3995 -0.0290 -0.7366 -0.1789 206  LYS B O   
15858 C CB  . LYS C 206  ? 3.2384 1.9058 1.4144 -0.0403 -0.7659 -0.1270 206  LYS B CB  
15859 C CG  . LYS C 206  ? 3.2920 1.9760 1.4285 -0.0366 -0.7758 -0.1257 206  LYS B CG  
15860 C CD  . LYS C 206  ? 3.2956 2.0455 1.4525 -0.0455 -0.7966 -0.1059 206  LYS B CD  
15861 C CE  . LYS C 206  ? 3.3403 2.1001 1.4962 -0.0799 -0.8232 -0.1142 206  LYS B CE  
15862 N NZ  . LYS C 206  ? 3.3593 2.1773 1.5183 -0.0907 -0.8469 -0.0995 206  LYS B NZ  
15863 N N   . GLU C 207  ? 3.3319 1.8852 1.4400 -0.0716 -0.7671 -0.1780 207  GLU B N   
15864 C CA  . GLU C 207  ? 3.4057 1.9113 1.4693 -0.0907 -0.7740 -0.2041 207  GLU B CA  
15865 C C   . GLU C 207  ? 3.3666 1.8089 1.4184 -0.0807 -0.7510 -0.2192 207  GLU B C   
15866 O O   . GLU C 207  ? 3.3377 1.7721 1.4047 -0.0550 -0.7295 -0.2107 207  GLU B O   
15867 C CB  . GLU C 207  ? 3.4558 1.9745 1.5321 -0.1236 -0.7969 -0.2094 207  GLU B CB  
15868 C CG  . GLU C 207  ? 3.5016 2.0720 1.5712 -0.1377 -0.8228 -0.2019 207  GLU B CG  
15869 C CD  . GLU C 207  ? 3.5814 2.1309 1.5920 -0.1493 -0.8348 -0.2229 207  GLU B CD  
15870 O OE1 . GLU C 207  ? 3.6075 2.1138 1.5811 -0.1351 -0.8188 -0.2363 207  GLU B OE1 
15871 O OE2 . GLU C 207  ? 3.6149 2.1916 1.6163 -0.1728 -0.8601 -0.2267 207  GLU B OE2 
15872 N N   . ASP C 208  ? 3.3766 1.7740 1.4021 -0.1008 -0.7552 -0.2419 208  ASP B N   
15873 C CA  . ASP C 208  ? 3.3207 1.6564 1.3340 -0.0928 -0.7339 -0.2564 208  ASP B CA  
15874 C C   . ASP C 208  ? 3.2438 1.5809 1.3066 -0.0880 -0.7226 -0.2449 208  ASP B C   
15875 O O   . ASP C 208  ? 3.2202 1.5989 1.3207 -0.0983 -0.7344 -0.2309 208  ASP B O   
15876 C CB  . ASP C 208  ? 3.3392 1.6328 1.3203 -0.1190 -0.7430 -0.2818 208  ASP B CB  
15877 C CG  . ASP C 208  ? 3.3084 1.6357 1.2996 -0.1483 -0.7699 -0.2824 208  ASP B CG  
15878 O OD1 . ASP C 208  ? 3.2342 1.5791 1.2690 -0.1583 -0.7740 -0.2720 208  ASP B OD1 
15879 O OD2 . ASP C 208  ? 3.3546 1.6928 1.3104 -0.1607 -0.7870 -0.2923 208  ASP B OD2 
15880 N N   . PHE C 209  ? 3.1953 1.4860 1.2565 -0.0737 -0.7002 -0.2513 209  PHE B N   
15881 C CA  . PHE C 209  ? 3.1011 1.3912 1.2061 -0.0628 -0.6853 -0.2398 209  PHE B CA  
15882 C C   . PHE C 209  ? 3.0769 1.3709 1.1915 -0.0296 -0.6642 -0.2287 209  PHE B C   
15883 O O   . PHE C 209  ? 3.0613 1.3963 1.1828 -0.0168 -0.6668 -0.2153 209  PHE B O   
15884 C CB  . PHE C 209  ? 3.0227 1.3640 1.1728 -0.0749 -0.6992 -0.2231 209  PHE B CB  
15885 C CG  . PHE C 209  ? 3.0124 1.3458 1.1664 -0.1058 -0.7152 -0.2318 209  PHE B CG  
15886 C CD1 . PHE C 209  ? 2.9837 1.3658 1.1659 -0.1226 -0.7345 -0.2199 209  PHE B CD1 
15887 C CD2 . PHE C 209  ? 2.9891 1.2669 1.1219 -0.1178 -0.7099 -0.2511 209  PHE B CD2 
15888 C CE1 . PHE C 209  ? 2.9580 1.3336 1.1475 -0.1510 -0.7486 -0.2272 209  PHE B CE1 
15889 C CE2 . PHE C 209  ? 3.0135 1.2841 1.1541 -0.1463 -0.7235 -0.2587 209  PHE B CE2 
15890 C CZ  . PHE C 209  ? 2.9973 1.3170 1.1665 -0.1629 -0.7431 -0.2467 209  PHE B CZ  
15891 N N   . SER C 210  ? 3.0562 1.3083 1.1737 -0.0159 -0.6432 -0.2338 210  SER B N   
15892 C CA  . SER C 210  ? 3.0272 1.2769 1.1534 0.0152  -0.6221 -0.2258 210  SER B CA  
15893 C C   . SER C 210  ? 2.9527 1.2403 1.1318 0.0279  -0.6152 -0.2071 210  SER B C   
15894 O O   . SER C 210  ? 2.9037 1.1973 1.0978 0.0533  -0.5985 -0.1992 210  SER B O   
15895 C CB  . SER C 210  ? 3.0511 1.2388 1.1561 0.0251  -0.6023 -0.2398 210  SER B CB  
15896 O OG  . SER C 210  ? 3.0366 1.2231 1.1508 0.0548  -0.5825 -0.2322 210  SER B OG  
15897 N N   . THR C 211  ? 2.9403 1.2535 1.1480 0.0098  -0.6278 -0.2007 211  THR B N   
15898 C CA  . THR C 211  ? 2.8875 1.2317 1.1438 0.0181  -0.6214 -0.1856 211  THR B CA  
15899 C C   . THR C 211  ? 2.8316 1.2193 1.1108 0.0401  -0.6150 -0.1705 211  THR B C   
15900 O O   . THR C 211  ? 2.8217 1.2406 1.0933 0.0389  -0.6258 -0.1646 211  THR B O   
15901 C CB  . THR C 211  ? 2.8798 1.2492 1.1601 -0.0067 -0.6382 -0.1802 211  THR B CB  
15902 O OG1 . THR C 211  ? 2.9140 1.3036 1.1761 -0.0260 -0.6597 -0.1822 211  THR B OG1 
15903 C CG2 . THR C 211  ? 2.8861 1.2115 1.1617 -0.0201 -0.6349 -0.1910 211  THR B CG2 
15904 N N   . THR C 212  ? 2.8125 1.2028 1.1215 0.0596  -0.5974 -0.1642 212  THR B N   
15905 C CA  . THR C 212  ? 2.7777 1.1997 1.1098 0.0839  -0.5859 -0.1525 212  THR B CA  
15906 C C   . THR C 212  ? 2.7382 1.2016 1.1204 0.0883  -0.5826 -0.1392 212  THR B C   
15907 O O   . THR C 212  ? 2.7582 1.2104 1.1587 0.0872  -0.5761 -0.1407 212  THR B O   
15908 C CB  . THR C 212  ? 2.7775 1.1618 1.1017 0.1076  -0.5635 -0.1591 212  THR B CB  
15909 O OG1 . THR C 212  ? 2.8339 1.1676 1.1116 0.1026  -0.5630 -0.1742 212  THR B OG1 
15910 C CG2 . THR C 212  ? 2.7432 1.1555 1.0845 0.1327  -0.5516 -0.1489 212  THR B CG2 
15911 N N   . GLY C 213  ? 2.7056 1.2181 1.1105 0.0940  -0.5864 -0.1259 213  GLY B N   
15912 C CA  . GLY C 213  ? 2.6454 1.1963 1.0981 0.1037  -0.5786 -0.1143 213  GLY B CA  
15913 C C   . GLY C 213  ? 2.6321 1.1904 1.0999 0.1320  -0.5595 -0.1104 213  GLY B C   
15914 O O   . GLY C 213  ? 2.6513 1.2051 1.0991 0.1424  -0.5569 -0.1102 213  GLY B O   
15915 N N   . THR C 214  ? 2.5616 1.1323 1.0656 0.1448  -0.5456 -0.1075 214  THR B N   
15916 C CA  . THR C 214  ? 2.5181 1.1035 1.0451 0.1705  -0.5278 -0.1029 214  THR B CA  
15917 C C   . THR C 214  ? 2.4126 1.0391 0.9884 0.1748  -0.5222 -0.0949 214  THR B C   
15918 O O   . THR C 214  ? 2.3971 1.0269 0.9848 0.1628  -0.5266 -0.0961 214  THR B O   
15919 C CB  . THR C 214  ? 2.5504 1.0896 1.0626 0.1885  -0.5099 -0.1140 214  THR B CB  
15920 O OG1 . THR C 214  ? 2.6027 1.1130 1.0736 0.1911  -0.5113 -0.1187 214  THR B OG1 
15921 C CG2 . THR C 214  ? 2.4975 1.0556 1.0478 0.2137  -0.4899 -0.1100 214  THR B CG2 
15922 N N   . ALA C 215  ? 2.3595 1.0185 0.9640 0.1919  -0.5118 -0.0865 215  ALA B N   
15923 C CA  . ALA C 215  ? 2.2692 0.9699 0.9215 0.1972  -0.5049 -0.0795 215  ALA B CA  
15924 C C   . ALA C 215  ? 2.2557 0.9654 0.9323 0.2236  -0.4847 -0.0778 215  ALA B C   
15925 O O   . ALA C 215  ? 2.2626 0.9477 0.9172 0.2355  -0.4783 -0.0802 215  ALA B O   
15926 C CB  . ALA C 215  ? 2.2641 1.0102 0.9316 0.1823  -0.5200 -0.0663 215  ALA B CB  
15927 N N   . TYR C 216  ? 2.2015 0.9448 0.9232 0.2331  -0.4735 -0.0743 216  TYR B N   
15928 C CA  . TYR C 216  ? 2.2615 1.0192 1.0109 0.2568  -0.4550 -0.0710 216  TYR B CA  
15929 C C   . TYR C 216  ? 2.1402 0.9510 0.9377 0.2595  -0.4506 -0.0609 216  TYR B C   
15930 O O   . TYR C 216  ? 2.1299 0.9643 0.9401 0.2440  -0.4603 -0.0581 216  TYR B O   
15931 C CB  . TYR C 216  ? 2.2952 1.0235 1.0517 0.2748  -0.4363 -0.0833 216  TYR B CB  
15932 C CG  . TYR C 216  ? 2.4216 1.0952 1.1342 0.2728  -0.4383 -0.0940 216  TYR B CG  
15933 C CD1 . TYR C 216  ? 2.4643 1.1066 1.1645 0.2914  -0.4244 -0.0987 216  TYR B CD1 
15934 C CD2 . TYR C 216  ? 2.4873 1.1400 1.1730 0.2526  -0.4528 -0.0991 216  TYR B CD2 
15935 C CE1 . TYR C 216  ? 2.5359 1.1268 1.1963 0.2896  -0.4251 -0.1086 216  TYR B CE1 
15936 C CE2 . TYR C 216  ? 2.5642 1.1663 1.2118 0.2505  -0.4535 -0.1089 216  TYR B CE2 
15937 C CZ  . TYR C 216  ? 2.5908 1.1618 1.2252 0.2689  -0.4396 -0.1138 216  TYR B CZ  
15938 O OH  . TYR C 216  ? 2.6518 1.1714 1.2487 0.2665  -0.4394 -0.1236 216  TYR B OH  
15939 N N   . PHE C 217  ? 2.1220 0.9506 0.9460 0.2791  -0.4353 -0.0549 217  PHE B N   
15940 C CA  . PHE C 217  ? 2.0818 0.9556 0.9590 0.2882  -0.4233 -0.0483 217  PHE B CA  
15941 C C   . PHE C 217  ? 2.1148 0.9857 1.0167 0.3144  -0.4004 -0.0496 217  PHE B C   
15942 O O   . PHE C 217  ? 2.1340 0.9760 1.0112 0.3247  -0.3964 -0.0502 217  PHE B O   
15943 C CB  . PHE C 217  ? 2.0790 0.9972 0.9709 0.2768  -0.4350 -0.0314 217  PHE B CB  
15944 C CG  . PHE C 217  ? 2.0997 1.0235 0.9773 0.2813  -0.4391 -0.0184 217  PHE B CG  
15945 C CD1 . PHE C 217  ? 2.0948 1.0563 1.0112 0.2950  -0.4277 -0.0043 217  PHE B CD1 
15946 C CD2 . PHE C 217  ? 2.1416 1.0357 0.9682 0.2715  -0.4544 -0.0193 217  PHE B CD2 
15947 C CE1 . PHE C 217  ? 2.1126 1.0834 1.0168 0.2999  -0.4316 0.0102  217  PHE B CE1 
15948 C CE2 . PHE C 217  ? 2.1818 1.0847 0.9939 0.2758  -0.4589 -0.0068 217  PHE B CE2 
15949 C CZ  . PHE C 217  ? 2.1581 1.1006 1.0093 0.2903  -0.4477 0.0089  217  PHE B CZ  
15950 N N   . GLU C 218  ? 2.1097 1.0087 1.0606 0.3253  -0.3844 -0.0514 218  GLU B N   
15951 C CA  . GLU C 218  ? 2.1523 1.0498 1.1329 0.3500  -0.3614 -0.0535 218  GLU B CA  
15952 C C   . GLU C 218  ? 2.1209 1.0642 1.1452 0.3583  -0.3523 -0.0384 218  GLU B C   
15953 O O   . GLU C 218  ? 2.0698 1.0505 1.1242 0.3503  -0.3540 -0.0342 218  GLU B O   
15954 C CB  . GLU C 218  ? 2.2222 1.1096 1.2260 0.3589  -0.3469 -0.0707 218  GLU B CB  
15955 C CG  . GLU C 218  ? 2.3086 1.1789 1.3317 0.3837  -0.3246 -0.0763 218  GLU B CG  
15956 C CD  . GLU C 218  ? 2.3848 1.2418 1.4266 0.3912  -0.3124 -0.0947 218  GLU B CD  
15957 O OE1 . GLU C 218  ? 2.4041 1.2629 1.4810 0.4111  -0.2917 -0.0995 218  GLU B OE1 
15958 O OE2 . GLU C 218  ? 2.4149 1.2609 1.4378 0.3775  -0.3234 -0.1038 218  GLU B OE2 
15959 N N   . VAL C 219  ? 2.1234 1.0636 1.1504 0.3745  -0.3424 -0.0291 219  VAL B N   
15960 C CA  . VAL C 219  ? 2.0672 1.0483 1.1383 0.3856  -0.3308 -0.0135 219  VAL B CA  
15961 C C   . VAL C 219  ? 2.0602 1.0415 1.1763 0.4073  -0.3043 -0.0225 219  VAL B C   
15962 O O   . VAL C 219  ? 2.0642 1.0145 1.1716 0.4231  -0.2926 -0.0279 219  VAL B O   
15963 C CB  . VAL C 219  ? 2.0661 1.0458 1.1159 0.3921  -0.3342 0.0036  219  VAL B CB  
15964 C CG1 . VAL C 219  ? 2.0045 1.0082 1.1036 0.4157  -0.3105 0.0150  219  VAL B CG1 
15965 C CG2 . VAL C 219  ? 2.0179 1.0211 1.0456 0.3715  -0.3582 0.0181  219  VAL B CG2 
15966 N N   . LYS C 220  ? 2.0504 1.0662 1.2149 0.4074  -0.2948 -0.0251 220  LYS B N   
15967 C CA  . LYS C 220  ? 1.9991 1.0225 1.2148 0.4271  -0.2687 -0.0339 220  LYS B CA  
15968 C C   . LYS C 220  ? 1.9792 1.0468 1.2483 0.4369  -0.2543 -0.0181 220  LYS B C   
15969 O O   . LYS C 220  ? 1.8571 0.9564 1.1305 0.4251  -0.2652 -0.0032 220  LYS B O   
15970 C CB  . LYS C 220  ? 1.9862 1.0087 1.2158 0.4213  -0.2659 -0.0549 220  LYS B CB  
15971 C CG  . LYS C 220  ? 2.0146 0.9923 1.1993 0.4158  -0.2754 -0.0705 220  LYS B CG  
15972 C CD  . LYS C 220  ? 2.0461 1.0325 1.2322 0.4011  -0.2830 -0.0842 220  LYS B CD  
15973 C CE  . LYS C 220  ? 2.0753 1.0219 1.2336 0.4008  -0.2854 -0.1018 220  LYS B CE  
15974 N NZ  . LYS C 220  ? 2.0508 0.9970 1.2467 0.4161  -0.2653 -0.1189 220  LYS B NZ  
15975 N N   . GLU C 221  ? 2.0192 1.0875 1.3301 0.4588  -0.2292 -0.0212 221  GLU B N   
15976 C CA  . GLU C 221  ? 2.1362 1.2415 1.5023 0.4724  -0.2108 -0.0060 221  GLU B CA  
15977 C C   . GLU C 221  ? 2.0819 1.2219 1.5055 0.4722  -0.1965 -0.0150 221  GLU B C   
15978 O O   . GLU C 221  ? 2.0464 1.1793 1.5009 0.4829  -0.1786 -0.0334 221  GLU B O   
15979 C CB  . GLU C 221  ? 2.2714 1.3594 1.6569 0.4975  -0.1888 -0.0036 221  GLU B CB  
15980 C CG  . GLU C 221  ? 2.3684 1.4931 1.8218 0.5139  -0.1644 0.0084  221  GLU B CG  
15981 C CD  . GLU C 221  ? 2.4532 1.5614 1.9436 0.5372  -0.1374 -0.0016 221  GLU B CD  
15982 O OE1 . GLU C 221  ? 2.4870 1.5553 1.9480 0.5401  -0.1389 -0.0177 221  GLU B OE1 
15983 O OE2 . GLU C 221  ? 2.4608 1.5958 2.0110 0.5525  -0.1144 0.0069  221  GLU B OE2 
15984 N N   . TYR C 222  ? 2.0599 1.2380 1.4996 0.4606  -0.2034 -0.0018 222  TYR B N   
15985 C CA  . TYR C 222  ? 2.0087 1.2197 1.4982 0.4580  -0.1914 -0.0107 222  TYR B CA  
15986 C C   . TYR C 222  ? 2.0036 1.2321 1.5594 0.4799  -0.1603 -0.0108 222  TYR B C   
15987 O O   . TYR C 222  ? 2.0120 1.2488 1.5856 0.4933  -0.1506 0.0088  222  TYR B O   
15988 C CB  . TYR C 222  ? 1.9880 1.2355 1.4804 0.4409  -0.2053 0.0051  222  TYR B CB  
15989 C CG  . TYR C 222  ? 1.9480 1.2302 1.4951 0.4405  -0.1896 -0.0031 222  TYR B CG  
15990 C CD1 . TYR C 222  ? 1.9322 1.2207 1.4695 0.4241  -0.1992 -0.0177 222  TYR B CD1 
15991 C CD2 . TYR C 222  ? 1.9370 1.2446 1.5467 0.4573  -0.1634 0.0028  222  TYR B CD2 
15992 C CE1 . TYR C 222  ? 1.9098 1.2302 1.4963 0.4241  -0.1837 -0.0267 222  TYR B CE1 
15993 C CE2 . TYR C 222  ? 1.9136 1.2515 1.5741 0.4572  -0.1473 -0.0067 222  TYR B CE2 
15994 C CZ  . TYR C 222  ? 1.8972 1.2416 1.5449 0.4405  -0.1576 -0.0219 222  TYR B CZ  
15995 O OH  . TYR C 222  ? 1.8758 1.2514 1.5738 0.4407  -0.1405 -0.0320 222  TYR B OH  
15996 N N   . VAL C 223  ? 1.9682 1.2033 1.5608 0.4831  -0.1447 -0.0328 223  VAL B N   
15997 C CA  . VAL C 223  ? 1.9203 1.1741 1.5816 0.5018  -0.1140 -0.0369 223  VAL B CA  
15998 C C   . VAL C 223  ? 1.9002 1.1881 1.6016 0.4936  -0.1061 -0.0485 223  VAL B C   
15999 O O   . VAL C 223  ? 1.8954 1.1796 1.5748 0.4796  -0.1176 -0.0663 223  VAL B O   
16000 C CB  . VAL C 223  ? 1.8820 1.1065 1.5547 0.5162  -0.0984 -0.0599 223  VAL B CB  
16001 C CG1 . VAL C 223  ? 1.8365 1.0805 1.5831 0.5361  -0.0660 -0.0613 223  VAL B CG1 
16002 C CG2 . VAL C 223  ? 1.9128 1.0942 1.5358 0.5222  -0.1080 -0.0559 223  VAL B CG2 
16003 N N   . LEU C 224  ? 1.9061 1.2272 1.6681 0.5034  -0.0848 -0.0386 224  LEU B N   
16004 C CA  . LEU C 224  ? 1.8981 1.2535 1.7052 0.4977  -0.0730 -0.0495 224  LEU B CA  
16005 C C   . LEU C 224  ? 1.9491 1.2939 1.7803 0.5041  -0.0569 -0.0822 224  LEU B C   
16006 O O   . LEU C 224  ? 1.9326 1.2599 1.7873 0.5217  -0.0392 -0.0899 224  LEU B O   
16007 C CB  . LEU C 224  ? 1.8775 1.2690 1.7465 0.5082  -0.0520 -0.0294 224  LEU B CB  
16008 C CG  . LEU C 224  ? 1.8611 1.2927 1.7538 0.4947  -0.0531 -0.0235 224  LEU B CG  
16009 C CD1 . LEU C 224  ? 1.8592 1.3058 1.7979 0.4961  -0.0325 -0.0509 224  LEU B CD1 
16010 C CD2 . LEU C 224  ? 1.8810 1.3085 1.7122 0.4720  -0.0853 -0.0194 224  LEU B CD2 
16011 N N   . PRO C 225  ? 2.2812 1.6258 1.5348 0.8153  -0.7686 -0.5250 225  PRO B N   
16012 C CA  . PRO C 225  ? 2.2718 1.5823 1.5319 0.7819  -0.7312 -0.4891 225  PRO B CA  
16013 C C   . PRO C 225  ? 2.2275 1.5255 1.5274 0.7863  -0.7385 -0.4793 225  PRO B C   
16014 O O   . PRO C 225  ? 2.2049 1.5353 1.5578 0.7937  -0.7583 -0.5202 225  PRO B O   
16015 C CB  . PRO C 225  ? 2.2153 1.5526 1.5177 0.7359  -0.7053 -0.5287 225  PRO B CB  
16016 C CG  . PRO C 225  ? 2.2328 1.6205 1.5579 0.7458  -0.7299 -0.5864 225  PRO B CG  
16017 C CD  . PRO C 225  ? 2.2793 1.6760 1.5980 0.7935  -0.7737 -0.5894 225  PRO B CD  
16018 N N   . HIS C 226  ? 2.2687 1.5192 1.5467 0.7822  -0.7227 -0.4255 226  HIS B N   
16019 C CA  . HIS C 226  ? 2.3146 1.5442 1.6261 0.7855  -0.7295 -0.4135 226  HIS B CA  
16020 C C   . HIS C 226  ? 2.2395 1.4657 1.5962 0.7413  -0.7055 -0.4326 226  HIS B C   
16021 O O   . HIS C 226  ? 2.2001 1.4279 1.5998 0.7406  -0.7128 -0.4538 226  HIS B O   
16022 C CB  . HIS C 226  ? 2.4216 1.5988 1.6932 0.8039  -0.7277 -0.3459 226  HIS B CB  
16023 C CG  . HIS C 226  ? 2.5390 1.7125 1.7711 0.8552  -0.7552 -0.3261 226  HIS B CG  
16024 N ND1 . HIS C 226  ? 2.6167 1.7662 1.7830 0.8758  -0.7478 -0.2813 226  HIS B ND1 
16025 C CD2 . HIS C 226  ? 2.5874 1.7763 1.8337 0.8920  -0.7894 -0.3439 226  HIS B CD2 
16026 C CE1 . HIS C 226  ? 2.6754 1.8232 1.8112 0.9234  -0.7765 -0.2722 226  HIS B CE1 
16027 N NE2 . HIS C 226  ? 2.6595 1.8318 1.8444 0.9338  -0.8039 -0.3095 226  HIS B NE2 
16028 N N   . PHE C 227  ? 2.2180 1.4363 1.5607 0.7059  -0.6761 -0.4240 227  PHE B N   
16029 C CA  . PHE C 227  ? 2.1698 1.3791 1.5426 0.6638  -0.6522 -0.4377 227  PHE B CA  
16030 C C   . PHE C 227  ? 2.1688 1.3825 1.5239 0.6317  -0.6242 -0.4362 227  PHE B C   
16031 O O   . PHE C 227  ? 2.2234 1.4213 1.5372 0.6369  -0.6170 -0.3988 227  PHE B O   
16032 C CB  . PHE C 227  ? 2.1176 1.2738 1.4867 0.6555  -0.6490 -0.3942 227  PHE B CB  
16033 C CG  . PHE C 227  ? 2.0588 1.1791 1.3871 0.6623  -0.6439 -0.3316 227  PHE B CG  
16034 C CD1 . PHE C 227  ? 2.0088 1.1155 1.3186 0.6332  -0.6183 -0.3073 227  PHE B CD1 
16035 C CD2 . PHE C 227  ? 2.0739 1.1737 1.3850 0.6996  -0.6631 -0.2952 227  PHE B CD2 
16036 C CE1 . PHE C 227  ? 2.0301 1.1057 1.3094 0.6411  -0.6108 -0.2481 227  PHE B CE1 
16037 C CE2 . PHE C 227  ? 2.0807 1.1473 1.3581 0.7074  -0.6541 -0.2349 227  PHE B CE2 
16038 C CZ  . PHE C 227  ? 2.0614 1.1169 1.3250 0.6784  -0.6275 -0.2114 227  PHE B CZ  
16039 N N   . SER C 228  ? 2.1252 1.3576 1.5116 0.5994  -0.6058 -0.4746 228  SER B N   
16040 C CA  . SER C 228  ? 2.1336 1.3743 1.5089 0.5690  -0.5791 -0.4793 228  SER B CA  
16041 C C   . SER C 228  ? 2.0992 1.2949 1.4418 0.5475  -0.5594 -0.4251 228  SER B C   
16042 O O   . SER C 228  ? 2.0722 1.2373 1.4233 0.5264  -0.5520 -0.4110 228  SER B O   
16043 C CB  . SER C 228  ? 2.1682 1.4351 1.5870 0.5402  -0.5618 -0.5298 228  SER B CB  
16044 O OG  . SER C 228  ? 2.1869 1.4571 1.5970 0.5077  -0.5332 -0.5324 228  SER B OG  
16045 N N   . VAL C 229  ? 2.0632 1.2530 1.3689 0.5545  -0.5521 -0.3945 229  VAL B N   
16046 C CA  . VAL C 229  ? 2.0194 1.1741 1.3043 0.5316  -0.5297 -0.3464 229  VAL B CA  
16047 C C   . VAL C 229  ? 1.9503 1.1222 1.2337 0.5022  -0.5032 -0.3660 229  VAL B C   
16048 O O   . VAL C 229  ? 1.9498 1.1491 1.2214 0.5131  -0.5020 -0.3888 229  VAL B O   
16049 C CB  . VAL C 229  ? 1.7320 0.8607 0.9795 0.5588  -0.5328 -0.2891 229  VAL B CB  
16050 C CG1 . VAL C 229  ? 1.6493 0.7584 0.8783 0.5374  -0.5046 -0.2501 229  VAL B CG1 
16051 C CG2 . VAL C 229  ? 1.6830 0.7784 0.9397 0.5716  -0.5492 -0.2542 229  VAL B CG2 
16052 N N   . SER C 230  ? 1.9369 1.0910 1.2326 0.4653  -0.4841 -0.3599 230  SER B N   
16053 C CA  . SER C 230  ? 1.8990 1.0614 1.1934 0.4342  -0.4560 -0.3702 230  SER B CA  
16054 C C   . SER C 230  ? 1.8841 1.0126 1.1578 0.4199  -0.4395 -0.3142 230  SER B C   
16055 O O   . SER C 230  ? 1.8972 0.9922 1.1700 0.4208  -0.4479 -0.2721 230  SER B O   
16056 C CB  . SER C 230  ? 1.8663 1.0334 1.1882 0.4024  -0.4440 -0.4061 230  SER B CB  
16057 O OG  . SER C 230  ? 1.8369 0.9640 1.1568 0.3843  -0.4442 -0.3780 230  SER B OG  
16058 N N   . ILE C 231  ? 1.8504 0.9865 1.1134 0.4048  -0.4158 -0.3136 231  ILE B N   
16059 C CA  . ILE C 231  ? 1.8512 0.9577 1.1011 0.3908  -0.3980 -0.2604 231  ILE B CA  
16060 C C   . ILE C 231  ? 1.9212 1.0333 1.1744 0.3585  -0.3702 -0.2722 231  ILE B C   
16061 O O   . ILE C 231  ? 1.9428 1.0794 1.1897 0.3610  -0.3583 -0.3012 231  ILE B O   
16062 C CB  . ILE C 231  ? 1.8317 0.9299 1.0527 0.4226  -0.3974 -0.2204 231  ILE B CB  
16063 C CG1 . ILE C 231  ? 1.8092 0.8909 1.0194 0.4082  -0.3692 -0.1803 231  ILE B CG1 
16064 C CG2 . ILE C 231  ? 1.8357 0.9636 1.0365 0.4518  -0.4059 -0.2576 231  ILE B CG2 
16065 C CD1 . ILE C 231  ? 1.8457 0.9180 1.0239 0.4415  -0.3629 -0.1430 231  ILE B CD1 
16066 N N   . GLU C 232  ? 1.9792 1.0662 1.2422 0.3283  -0.3620 -0.2504 232  GLU B N   
16067 C CA  . GLU C 232  ? 2.0176 1.1052 1.2845 0.2952  -0.3367 -0.2608 232  GLU B CA  
16068 C C   . GLU C 232  ? 2.0061 1.0635 1.2692 0.2790  -0.3237 -0.2039 232  GLU B C   
16069 O O   . GLU C 232  ? 1.9861 1.0148 1.2555 0.2756  -0.3375 -0.1645 232  GLU B O   
16070 C CB  . GLU C 232  ? 2.0927 1.1792 1.3734 0.2720  -0.3383 -0.2966 232  GLU B CB  
16071 C CG  . GLU C 232  ? 2.1932 1.3039 1.4871 0.2902  -0.3554 -0.3435 232  GLU B CG  
16072 C CD  . GLU C 232  ? 2.2771 1.3691 1.5784 0.2779  -0.3652 -0.3586 232  GLU B CD  
16073 O OE1 . GLU C 232  ? 2.3060 1.3725 1.5997 0.2495  -0.3539 -0.3502 232  GLU B OE1 
16074 O OE2 . GLU C 232  ? 2.3112 1.4125 1.6232 0.2986  -0.3847 -0.3803 232  GLU B OE2 
16075 N N   . PRO C 233  ? 2.0138 1.0774 1.2712 0.2686  -0.2977 -0.2000 233  PRO B N   
16076 C CA  . PRO C 233  ? 2.0365 1.0777 1.2933 0.2609  -0.2826 -0.1446 233  PRO B CA  
16077 C C   . PRO C 233  ? 2.0413 1.0666 1.3079 0.2237  -0.2715 -0.1391 233  PRO B C   
16078 O O   . PRO C 233  ? 2.0572 1.0952 1.3235 0.2073  -0.2637 -0.1837 233  PRO B O   
16079 C CB  . PRO C 233  ? 2.0586 1.1175 1.2992 0.2753  -0.2600 -0.1534 233  PRO B CB  
16080 C CG  . PRO C 233  ? 2.0252 1.1171 1.2638 0.2800  -0.2645 -0.2220 233  PRO B CG  
16081 C CD  . PRO C 233  ? 2.0096 1.1024 1.2656 0.2645  -0.2806 -0.2481 233  PRO B CD  
16082 N N   . GLU C 234  ? 2.0002 0.9987 1.2769 0.2111  -0.2701 -0.0858 234  GLU B N   
16083 C CA  . GLU C 234  ? 1.9646 0.9442 1.2464 0.1771  -0.2661 -0.0800 234  GLU B CA  
16084 C C   . GLU C 234  ? 1.9001 0.8962 1.1735 0.1613  -0.2382 -0.1166 234  GLU B C   
16085 O O   . GLU C 234  ? 1.9271 0.9224 1.1949 0.1430  -0.2375 -0.1510 234  GLU B O   
16086 C CB  . GLU C 234  ? 2.0015 0.9539 1.3014 0.1658  -0.2678 -0.0164 234  GLU B CB  
16087 C CG  . GLU C 234  ? 2.1247 1.0500 1.4245 0.1338  -0.2814 -0.0139 234  GLU B CG  
16088 C CD  . GLU C 234  ? 2.1791 1.0773 1.5025 0.1186  -0.2897 0.0461  234  GLU B CD  
16089 O OE1 . GLU C 234  ? 2.1987 1.0963 1.5474 0.1340  -0.2899 0.0918  234  GLU B OE1 
16090 O OE2 . GLU C 234  ? 2.1878 1.0643 1.5047 0.0919  -0.2963 0.0477  234  GLU B OE2 
16091 N N   . TYR C 235  ? 1.8303 0.8391 1.1024 0.1692  -0.2137 -0.1098 235  TYR B N   
16092 C CA  . TYR C 235  ? 1.7893 0.8154 1.0572 0.1569  -0.1878 -0.1493 235  TYR B CA  
16093 C C   . TYR C 235  ? 1.7460 0.7950 1.0055 0.1827  -0.1764 -0.1677 235  TYR B C   
16094 O O   . TYR C 235  ? 1.7577 0.8072 1.0089 0.2103  -0.1869 -0.1479 235  TYR B O   
16095 C CB  . TYR C 235  ? 1.8003 0.8089 1.0730 0.1314  -0.1647 -0.1221 235  TYR B CB  
16096 C CG  . TYR C 235  ? 1.8379 0.8154 1.1152 0.1083  -0.1774 -0.0858 235  TYR B CG  
16097 C CD1 . TYR C 235  ? 1.8924 0.8563 1.1675 0.0811  -0.1605 -0.0826 235  TYR B CD1 
16098 C CD2 . TYR C 235  ? 1.8666 0.8260 1.1507 0.1138  -0.2071 -0.0533 235  TYR B CD2 
16099 C CE1 . TYR C 235  ? 1.9410 0.8737 1.2154 0.0607  -0.1758 -0.0497 235  TYR B CE1 
16100 C CE2 . TYR C 235  ? 1.9098 0.8382 1.1983 0.0918  -0.2235 -0.0218 235  TYR B CE2 
16101 C CZ  . TYR C 235  ? 1.9523 0.8672 1.2334 0.0658  -0.2090 -0.0207 235  TYR B CZ  
16102 O OH  . TYR C 235  ? 1.9832 0.8651 1.2633 0.0450  -0.2288 0.0093  235  TYR B OH  
16103 N N   . ASN C 236  ? 1.7175 0.7820 0.9774 0.1737  -0.1545 -0.2038 236  ASN B N   
16104 C CA  . ASN C 236  ? 1.7058 0.7910 0.9552 0.1965  -0.1486 -0.2331 236  ASN B CA  
16105 C C   . ASN C 236  ? 1.6777 0.7507 0.9126 0.2083  -0.1264 -0.2020 236  ASN B C   
16106 O O   . ASN C 236  ? 1.7428 0.8259 0.9588 0.2316  -0.1234 -0.2228 236  ASN B O   
16107 C CB  . ASN C 236  ? 1.7568 0.8654 1.0200 0.1816  -0.1386 -0.2925 236  ASN B CB  
16108 C CG  . ASN C 236  ? 1.8371 0.9683 1.1126 0.1866  -0.1616 -0.3350 236  ASN B CG  
16109 O OD1 . ASN C 236  ? 1.8523 0.9784 1.1233 0.1992  -0.1856 -0.3203 236  ASN B OD1 
16110 N ND2 . ASN C 236  ? 1.8772 1.0336 1.1734 0.1769  -0.1538 -0.3878 236  ASN B ND2 
16111 N N   . PHE C 237  ? 1.5761 0.6262 0.8190 0.1930  -0.1104 -0.1540 237  PHE B N   
16112 C CA  . PHE C 237  ? 1.5800 0.6160 0.8125 0.2080  -0.0884 -0.1158 237  PHE B CA  
16113 C C   . PHE C 237  ? 1.5392 0.5536 0.7884 0.2026  -0.0919 -0.0523 237  PHE B C   
16114 O O   . PHE C 237  ? 1.4801 0.4882 0.7459 0.1812  -0.1080 -0.0450 237  PHE B O   
16115 C CB  . PHE C 237  ? 1.4327 0.4640 0.6696 0.1904  -0.0569 -0.1249 237  PHE B CB  
16116 C CG  . PHE C 237  ? 1.4340 0.4854 0.6704 0.1822  -0.0532 -0.1891 237  PHE B CG  
16117 C CD1 . PHE C 237  ? 1.4594 0.5097 0.6874 0.1857  -0.0298 -0.2084 237  PHE B CD1 
16118 C CD2 . PHE C 237  ? 1.4335 0.5035 0.6826 0.1698  -0.0712 -0.2300 237  PHE B CD2 
16119 C CE1 . PHE C 237  ? 1.5243 0.5929 0.7610 0.1756  -0.0272 -0.2674 237  PHE B CE1 
16120 C CE2 . PHE C 237  ? 1.5208 0.6117 0.7806 0.1608  -0.0656 -0.2875 237  PHE B CE2 
16121 C CZ  . PHE C 237  ? 1.5188 0.6094 0.7747 0.1628  -0.0449 -0.3059 237  PHE B CZ  
16122 N N   . ILE C 238  ? 1.5796 0.5813 0.8251 0.2226  -0.0765 -0.0063 238  ILE B N   
16123 C CA  . ILE C 238  ? 1.5925 0.5750 0.8663 0.2148  -0.0755 0.0580  238  ILE B CA  
16124 C C   . ILE C 238  ? 1.6599 0.6301 0.9492 0.2008  -0.0438 0.0865  238  ILE B C   
16125 O O   . ILE C 238  ? 1.6951 0.6653 0.9667 0.2139  -0.0158 0.0766  238  ILE B O   
16126 C CB  . ILE C 238  ? 1.5124 0.4889 0.7841 0.2451  -0.0816 0.0977  238  ILE B CB  
16127 C CG1 . ILE C 238  ? 1.4630 0.4539 0.7094 0.2644  -0.1074 0.0574  238  ILE B CG1 
16128 C CG2 . ILE C 238  ? 1.5587 0.5206 0.8704 0.2309  -0.0974 0.1506  238  ILE B CG2 
16129 C CD1 . ILE C 238  ? 1.4767 0.4591 0.7291 0.2869  -0.1241 0.0977  238  ILE B CD1 
16130 N N   . GLY C 239  ? 1.7095 0.6673 1.0307 0.1740  -0.0511 0.1196  239  GLY B N   
16131 C CA  . GLY C 239  ? 1.7409 0.6878 1.0800 0.1532  -0.0278 0.1397  239  GLY B CA  
16132 C C   . GLY C 239  ? 1.7773 0.7081 1.1577 0.1434  -0.0378 0.2056  239  GLY B C   
16133 O O   . GLY C 239  ? 1.7743 0.7019 1.1684 0.1445  -0.0678 0.2242  239  GLY B O   
16134 N N   . TYR C 240  ? 1.8016 0.7220 1.2065 0.1344  -0.0147 0.2420  240  TYR B N   
16135 C CA  . TYR C 240  ? 1.8336 0.7431 1.2865 0.1350  -0.0204 0.3114  240  TYR B CA  
16136 C C   . TYR C 240  ? 1.8467 0.7488 1.3162 0.1156  -0.0648 0.3199  240  TYR B C   
16137 O O   . TYR C 240  ? 1.8213 0.7183 1.3264 0.1217  -0.0815 0.3649  240  TYR B O   
16138 C CB  . TYR C 240  ? 1.8273 0.7263 1.3118 0.1217  0.0029  0.3489  240  TYR B CB  
16139 C CG  . TYR C 240  ? 1.7750 0.6643 1.2605 0.0870  -0.0154 0.3367  240  TYR B CG  
16140 C CD1 . TYR C 240  ? 1.7223 0.5986 1.2412 0.0673  -0.0488 0.3742  240  TYR B CD1 
16141 C CD2 . TYR C 240  ? 1.7788 0.6696 1.2293 0.0745  -0.0007 0.2864  240  TYR B CD2 
16142 C CE1 . TYR C 240  ? 1.7032 0.5657 1.2107 0.0383  -0.0662 0.3612  240  TYR B CE1 
16143 C CE2 . TYR C 240  ? 1.7698 0.6487 1.2145 0.0452  -0.0136 0.2761  240  TYR B CE2 
16144 C CZ  . TYR C 240  ? 1.7399 0.6035 1.2078 0.0281  -0.0462 0.3128  240  TYR B CZ  
16145 O OH  . TYR C 240  ? 1.7764 0.6237 1.2259 0.0011  -0.0578 0.2993  240  TYR B OH  
16146 N N   . LYS C 241  ? 1.9089 0.8085 1.3517 0.0927  -0.0821 0.2755  241  LYS B N   
16147 C CA  . LYS C 241  ? 1.9799 0.8656 1.4281 0.0721  -0.1243 0.2777  241  LYS B CA  
16148 C C   . LYS C 241  ? 2.0350 0.9219 1.4950 0.0889  -0.1511 0.2907  241  LYS B C   
16149 O O   . LYS C 241  ? 2.0558 0.9297 1.5571 0.0838  -0.1746 0.3390  241  LYS B O   
16150 C CB  . LYS C 241  ? 1.7783 0.6615 1.1840 0.0523  -0.1322 0.2189  241  LYS B CB  
16151 C CG  . LYS C 241  ? 1.5793 0.4456 0.9818 0.0243  -0.1256 0.2245  241  LYS B CG  
16152 C CD  . LYS C 241  ? 1.7527 0.6176 1.1109 0.0083  -0.1218 0.1654  241  LYS B CD  
16153 C CE  . LYS C 241  ? 2.1653 1.0085 1.5139 -0.0184 -0.1143 0.1740  241  LYS B CE  
16154 N NZ  . LYS C 241  ? 2.1514 1.0016 1.4985 -0.0218 -0.0710 0.1631  241  LYS B NZ  
16155 N N   . ASN C 242  ? 2.0569 0.9590 1.4849 0.1087  -0.1491 0.2490  242  ASN B N   
16156 C CA  . ASN C 242  ? 2.0466 0.9503 1.4838 0.1299  -0.1685 0.2630  242  ASN B CA  
16157 C C   . ASN C 242  ? 2.0907 1.0064 1.5267 0.1634  -0.1383 0.2817  242  ASN B C   
16158 O O   . ASN C 242  ? 2.0761 1.0045 1.4793 0.1760  -0.1116 0.2487  242  ASN B O   
16159 C CB  . ASN C 242  ? 1.9783 0.8864 1.3828 0.1312  -0.1941 0.2096  242  ASN B CB  
16160 C CG  . ASN C 242  ? 1.9092 0.8261 1.2774 0.1166  -0.1851 0.1492  242  ASN B CG  
16161 O OD1 . ASN C 242  ? 1.8964 0.8113 1.2459 0.1083  -0.2064 0.1112  242  ASN B OD1 
16162 N ND2 . ASN C 242  ? 1.8642 0.7896 1.2251 0.1137  -0.1517 0.1405  242  ASN B ND2 
16163 N N   . PHE C 243  ? 2.1605 1.0693 1.6325 0.1778  -0.1427 0.3357  243  PHE B N   
16164 C CA  . PHE C 243  ? 2.2450 1.1586 1.7194 0.2102  -0.1094 0.3680  243  PHE B CA  
16165 C C   . PHE C 243  ? 2.3214 1.2238 1.8528 0.2138  -0.1213 0.4333  243  PHE B C   
16166 O O   . PHE C 243  ? 2.3218 1.2239 1.8668 0.2411  -0.0968 0.4739  243  PHE B O   
16167 C CB  . PHE C 243  ? 2.2678 1.1822 1.7460 0.2095  -0.0697 0.3825  243  PHE B CB  
16168 C CG  . PHE C 243  ? 2.3117 1.2261 1.7855 0.2453  -0.0309 0.4153  243  PHE B CG  
16169 C CD1 . PHE C 243  ? 2.3313 1.2521 1.7452 0.2738  -0.0125 0.3754  243  PHE B CD1 
16170 C CD2 . PHE C 243  ? 2.3224 1.2288 1.8511 0.2514  -0.0125 0.4854  243  PHE B CD2 
16171 C CE1 . PHE C 243  ? 2.3544 1.2693 1.7525 0.3088  0.0236  0.4036  243  PHE B CE1 
16172 C CE2 . PHE C 243  ? 2.3463 1.2497 1.8659 0.2866  0.0282  0.5157  243  PHE B CE2 
16173 C CZ  . PHE C 243  ? 2.3626 1.2680 1.8115 0.3159  0.0466  0.4741  243  PHE B CZ  
16174 N N   . LYS C 244  ? 2.3921 1.2830 1.9582 0.1854  -0.1585 0.4446  244  LYS B N   
16175 C CA  . LYS C 244  ? 2.4821 1.3616 2.0986 0.1869  -0.1838 0.4906  244  LYS B CA  
16176 C C   . LYS C 244  ? 2.5087 1.3829 2.0962 0.1834  -0.2224 0.4470  244  LYS B C   
16177 O O   . LYS C 244  ? 2.5731 1.4357 2.1927 0.1860  -0.2481 0.4727  244  LYS B O   
16178 C CB  . LYS C 244  ? 2.5227 1.4003 2.2102 0.1573  -0.1998 0.5355  244  LYS B CB  
16179 C CG  . LYS C 244  ? 2.5512 1.4569 2.2912 0.1635  -0.1581 0.5810  244  LYS B CG  
16180 C CD  . LYS C 244  ? 2.5579 1.4844 2.3960 0.1409  -0.1778 0.6302  244  LYS B CD  
16181 C CE  . LYS C 244  ? 2.5495 1.5043 2.4479 0.1454  -0.1368 0.6755  244  LYS B CE  
16182 N NZ  . LYS C 244  ? 2.5343 1.4886 2.4260 0.1243  -0.1333 0.6642  244  LYS B NZ  
16183 N N   . ASN C 245  ? 2.4402 1.3229 1.9703 0.1786  -0.2244 0.3814  245  ASN B N   
16184 C CA  . ASN C 245  ? 2.4362 1.3169 1.9359 0.1803  -0.2549 0.3355  245  ASN B CA  
16185 C C   . ASN C 245  ? 2.3485 1.2466 1.7894 0.1829  -0.2460 0.2635  245  ASN B C   
16186 O O   . ASN C 245  ? 2.3660 1.2722 1.7905 0.1717  -0.2236 0.2439  245  ASN B O   
16187 C CB  . ASN C 245  ? 2.4453 1.3022 1.9688 0.1513  -0.2977 0.3406  245  ASN B CB  
16188 C CG  . ASN C 245  ? 2.4968 1.3473 2.0022 0.1213  -0.3012 0.3151  245  ASN B CG  
16189 O OD1 . ASN C 245  ? 2.4984 1.3612 1.9919 0.1186  -0.2700 0.3098  245  ASN B OD1 
16190 N ND2 . ASN C 245  ? 2.5354 1.3633 2.0345 0.0996  -0.3385 0.2985  245  ASN B ND2 
16191 N N   . PHE C 246  ? 2.2580 1.1611 1.6738 0.1972  -0.2644 0.2263  246  PHE B N   
16192 C CA  . PHE C 246  ? 2.0616 0.9854 1.4318 0.2053  -0.2588 0.1595  246  PHE B CA  
16193 C C   . PHE C 246  ? 1.9799 0.9016 1.3395 0.2128  -0.2904 0.1283  246  PHE B C   
16194 O O   . PHE C 246  ? 1.9632 0.8913 1.3168 0.2418  -0.2934 0.1326  246  PHE B O   
16195 C CB  . PHE C 246  ? 1.9376 0.8800 1.2854 0.2381  -0.2311 0.1570  246  PHE B CB  
16196 C CG  . PHE C 246  ? 1.7950 0.7598 1.1062 0.2404  -0.2167 0.0960  246  PHE B CG  
16197 C CD1 . PHE C 246  ? 1.7085 0.6769 1.0175 0.2181  -0.1966 0.0803  246  PHE B CD1 
16198 C CD2 . PHE C 246  ? 1.7531 0.7352 1.0362 0.2656  -0.2239 0.0563  246  PHE B CD2 
16199 C CE1 . PHE C 246  ? 1.6620 0.6504 0.9456 0.2192  -0.1836 0.0257  246  PHE B CE1 
16200 C CE2 . PHE C 246  ? 1.7088 0.7126 0.9675 0.2666  -0.2135 0.0010  246  PHE B CE2 
16201 C CZ  . PHE C 246  ? 1.6686 0.6754 0.9296 0.2427  -0.1928 -0.0142 246  PHE B CZ  
16202 N N   . GLU C 247  ? 1.9588 0.8697 1.3126 0.1893  -0.3119 0.0970  247  GLU B N   
16203 C CA  . GLU C 247  ? 1.9643 0.8659 1.3130 0.1946  -0.3438 0.0723  247  GLU B CA  
16204 C C   . GLU C 247  ? 2.0311 0.9617 1.3527 0.2198  -0.3386 0.0197  247  GLU B C   
16205 O O   . GLU C 247  ? 2.0443 0.9899 1.3471 0.2108  -0.3322 -0.0322 247  GLU B O   
16206 C CB  . GLU C 247  ? 2.5430 1.4189 1.8860 0.1630  -0.3655 0.0535  247  GLU B CB  
16207 C CG  . GLU C 247  ? 2.3185 1.1583 1.6769 0.1568  -0.4068 0.0702  247  GLU B CG  
16208 C CD  . GLU C 247  ? 1.7304 0.5339 1.0822 0.1230  -0.4285 0.0709  247  GLU B CD  
16209 O OE1 . GLU C 247  ? 1.6408 0.4471 0.9761 0.1044  -0.4106 0.0614  247  GLU B OE1 
16210 O OE2 . GLU C 247  ? 1.5393 0.3084 0.8999 0.1157  -0.4643 0.0814  247  GLU B OE2 
16211 N N   . ILE C 248  ? 1.9980 0.9366 1.3197 0.2519  -0.3407 0.0350  248  ILE B N   
16212 C CA  . ILE C 248  ? 1.9276 0.8919 1.2261 0.2788  -0.3426 -0.0096 248  ILE B CA  
16213 C C   . ILE C 248  ? 1.9055 0.8609 1.2081 0.2843  -0.3734 -0.0307 248  ILE B C   
16214 O O   . ILE C 248  ? 1.9224 0.8575 1.2404 0.2959  -0.3909 0.0056  248  ILE B O   
16215 C CB  . ILE C 248  ? 1.9199 0.8913 1.2082 0.3155  -0.3334 0.0191  248  ILE B CB  
16216 C CG1 . ILE C 248  ? 1.9107 0.8827 1.1961 0.3156  -0.3013 0.0530  248  ILE B CG1 
16217 C CG2 . ILE C 248  ? 1.9233 0.9222 1.1836 0.3424  -0.3375 -0.0306 248  ILE B CG2 
16218 C CD1 . ILE C 248  ? 1.9252 0.9050 1.1837 0.3542  -0.2869 0.0666  248  ILE B CD1 
16219 N N   . THR C 249  ? 1.8766 0.8459 1.1689 0.2767  -0.3782 -0.0878 249  THR B N   
16220 C CA  . THR C 249  ? 1.8976 0.8569 1.1937 0.2821  -0.4053 -0.1124 249  THR B CA  
16221 C C   . THR C 249  ? 1.9215 0.9097 1.2106 0.3147  -0.4130 -0.1490 249  THR B C   
16222 O O   . THR C 249  ? 1.8910 0.9112 1.1730 0.3168  -0.4013 -0.1956 249  THR B O   
16223 C CB  . THR C 249  ? 1.9680 0.9191 1.2584 0.2537  -0.4060 -0.1522 249  THR B CB  
16224 O OG1 . THR C 249  ? 1.9531 0.8956 1.2398 0.2249  -0.3873 -0.1376 249  THR B OG1 
16225 C CG2 . THR C 249  ? 1.9732 0.8888 1.2681 0.2496  -0.4355 -0.1497 249  THR B CG2 
16226 N N   . ILE C 250  ? 1.9540 0.9308 1.2485 0.3398  -0.4340 -0.1289 250  ILE B N   
16227 C CA  . ILE C 250  ? 1.9866 0.9889 1.2745 0.3722  -0.4450 -0.1614 250  ILE B CA  
16228 C C   . ILE C 250  ? 2.0332 1.0264 1.3332 0.3743  -0.4684 -0.1914 250  ILE B C   
16229 O O   . ILE C 250  ? 2.0401 0.9972 1.3504 0.3636  -0.4832 -0.1676 250  ILE B O   
16230 C CB  . ILE C 250  ? 1.9866 0.9855 1.2651 0.4054  -0.4481 -0.1200 250  ILE B CB  
16231 C CG1 . ILE C 250  ? 2.0197 0.9829 1.3158 0.4112  -0.4683 -0.0786 250  ILE B CG1 
16232 C CG2 . ILE C 250  ? 1.9543 0.9490 1.2239 0.3999  -0.4229 -0.0790 250  ILE B CG2 
16233 C CD1 . ILE C 250  ? 2.0527 1.0068 1.3417 0.4405  -0.4644 -0.0268 250  ILE B CD1 
16234 N N   . LYS C 251  ? 2.0980 1.1226 1.3997 0.3883  -0.4725 -0.2438 251  LYS B N   
16235 C CA  . LYS C 251  ? 2.2015 1.2193 1.5167 0.3888  -0.4888 -0.2784 251  LYS B CA  
16236 C C   . LYS C 251  ? 2.2958 1.3410 1.6198 0.4252  -0.5062 -0.3074 251  LYS B C   
16237 O O   . LYS C 251  ? 2.3073 1.3942 1.6358 0.4348  -0.5003 -0.3468 251  LYS B O   
16238 C CB  . LYS C 251  ? 2.2037 1.2296 1.5214 0.3595  -0.4717 -0.3218 251  LYS B CB  
16239 C CG  . LYS C 251  ? 2.2147 1.2169 1.5203 0.3245  -0.4545 -0.2979 251  LYS B CG  
16240 C CD  . LYS C 251  ? 2.2311 1.2304 1.5327 0.2977  -0.4392 -0.3378 251  LYS B CD  
16241 C CE  . LYS C 251  ? 2.2240 1.2695 1.5348 0.2953  -0.4148 -0.3818 251  LYS B CE  
16242 N NZ  . LYS C 251  ? 2.2152 1.2555 1.5202 0.2665  -0.3913 -0.4103 251  LYS B NZ  
16243 N N   . ALA C 252  ? 2.3659 1.3865 1.6959 0.4448  -0.5293 -0.2878 252  ALA B N   
16244 C CA  . ALA C 252  ? 2.3997 1.4401 1.7362 0.4834  -0.5490 -0.3028 252  ALA B CA  
16245 C C   . ALA C 252  ? 2.4183 1.4585 1.7773 0.4889  -0.5628 -0.3437 252  ALA B C   
16246 O O   . ALA C 252  ? 2.4390 1.4425 1.8022 0.4720  -0.5665 -0.3398 252  ALA B O   
16247 C CB  . ALA C 252  ? 2.4309 1.4446 1.7576 0.5082  -0.5628 -0.2468 252  ALA B CB  
16248 N N   . ARG C 253  ? 2.4269 1.5061 1.8006 0.5147  -0.5720 -0.3821 253  ARG B N   
16249 C CA  . ARG C 253  ? 2.4374 1.5245 1.8390 0.5202  -0.5794 -0.4265 253  ARG B CA  
16250 C C   . ARG C 253  ? 2.3854 1.5163 1.8087 0.5565  -0.5968 -0.4576 253  ARG B C   
16251 O O   . ARG C 253  ? 2.3735 1.5443 1.7952 0.5646  -0.5948 -0.4720 253  ARG B O   
16252 C CB  . ARG C 253  ? 2.5122 1.6132 1.9230 0.4878  -0.5536 -0.4660 253  ARG B CB  
16253 C CG  . ARG C 253  ? 2.5852 1.7369 2.0034 0.4843  -0.5387 -0.4924 253  ARG B CG  
16254 C CD  . ARG C 253  ? 2.6731 1.8500 2.1196 0.4659  -0.5178 -0.5445 253  ARG B CD  
16255 N NE  . ARG C 253  ? 2.7759 1.9501 2.2491 0.4809  -0.5272 -0.5725 253  ARG B NE  
16256 C CZ  . ARG C 253  ? 2.8448 1.9755 2.3081 0.4685  -0.5224 -0.5711 253  ARG B CZ  
16257 N NH1 . ARG C 253  ? 2.8673 1.9542 2.2956 0.4399  -0.5121 -0.5428 253  ARG B NH1 
16258 N NH2 . ARG C 253  ? 2.8709 1.9998 2.3586 0.4856  -0.5293 -0.5988 253  ARG B NH2 
16259 N N   . TYR C 254  ? 2.3135 1.4359 1.7580 0.5784  -0.6154 -0.4696 254  TYR B N   
16260 C CA  . TYR C 254  ? 2.2261 1.3897 1.6976 0.6143  -0.6355 -0.4996 254  TYR B CA  
16261 C C   . TYR C 254  ? 2.1436 1.3552 1.6560 0.6053  -0.6227 -0.5599 254  TYR B C   
16262 O O   . TYR C 254  ? 2.0994 1.3045 1.6187 0.5744  -0.5974 -0.5794 254  TYR B O   
16263 C CB  . TYR C 254  ? 2.2338 1.3707 1.7175 0.6427  -0.6593 -0.4888 254  TYR B CB  
16264 C CG  . TYR C 254  ? 2.2532 1.3371 1.7065 0.6481  -0.6692 -0.4284 254  TYR B CG  
16265 C CD1 . TYR C 254  ? 2.2807 1.3131 1.7368 0.6372  -0.6717 -0.4128 254  TYR B CD1 
16266 C CD2 . TYR C 254  ? 2.2651 1.3486 1.6879 0.6641  -0.6749 -0.3871 254  TYR B CD2 
16267 C CE1 . TYR C 254  ? 2.3042 1.2892 1.7430 0.6403  -0.6813 -0.3571 254  TYR B CE1 
16268 C CE2 . TYR C 254  ? 2.2894 1.3257 1.6921 0.6689  -0.6800 -0.3291 254  TYR B CE2 
16269 C CZ  . TYR C 254  ? 2.3031 1.2918 1.7185 0.6559  -0.6839 -0.3140 254  TYR B CZ  
16270 O OH  . TYR C 254  ? 2.3267 1.2693 1.7321 0.6589  -0.6895 -0.2557 254  TYR B OH  
16271 N N   . PHE C 255  ? 2.1356 1.3951 1.6760 0.6327  -0.6403 -0.5881 255  PHE B N   
16272 C CA  . PHE C 255  ? 2.1474 1.4591 1.7367 0.6244  -0.6289 -0.6433 255  PHE B CA  
16273 C C   . PHE C 255  ? 2.2267 1.5348 1.8568 0.6227  -0.6192 -0.6738 255  PHE B C   
16274 O O   . PHE C 255  ? 2.1903 1.5356 1.8657 0.6114  -0.6009 -0.7177 255  PHE B O   
16275 C CB  . PHE C 255  ? 2.1340 1.4959 1.7478 0.6576  -0.6581 -0.6645 255  PHE B CB  
16276 C CG  . PHE C 255  ? 2.1085 1.4805 1.6830 0.6593  -0.6644 -0.6477 255  PHE B CG  
16277 C CD1 . PHE C 255  ? 2.0756 1.4968 1.6759 0.6527  -0.6635 -0.6856 255  PHE B CD1 
16278 C CD2 . PHE C 255  ? 2.1214 1.4520 1.6350 0.6677  -0.6699 -0.5940 255  PHE B CD2 
16279 C CE1 . PHE C 255  ? 2.0741 1.4992 1.6331 0.6553  -0.6693 -0.6725 255  PHE B CE1 
16280 C CE2 . PHE C 255  ? 2.1134 1.4497 1.5862 0.6714  -0.6718 -0.5786 255  PHE B CE2 
16281 C CZ  . PHE C 255  ? 2.1002 1.4820 1.5922 0.6656  -0.6721 -0.6190 255  PHE B CZ  
16282 N N   . TYR C 256  ? 2.3735 1.6361 1.9897 0.6359  -0.6308 -0.6505 256  TYR B N   
16283 C CA  . TYR C 256  ? 2.5127 1.7617 2.1601 0.6390  -0.6228 -0.6773 256  TYR B CA  
16284 C C   . TYR C 256  ? 2.6778 1.8805 2.2983 0.6028  -0.5924 -0.6758 256  TYR B C   
16285 O O   . TYR C 256  ? 2.7728 1.9326 2.3880 0.6058  -0.5924 -0.6760 256  TYR B O   
16286 C CB  . TYR C 256  ? 2.4745 1.7001 2.1285 0.6762  -0.6533 -0.6615 256  TYR B CB  
16287 C CG  . TYR C 256  ? 2.4424 1.6215 2.0492 0.6870  -0.6748 -0.6040 256  TYR B CG  
16288 C CD1 . TYR C 256  ? 2.4499 1.5642 2.0322 0.6777  -0.6746 -0.5762 256  TYR B CD1 
16289 C CD2 . TYR C 256  ? 2.4142 1.6121 2.0030 0.7088  -0.6961 -0.5780 256  TYR B CD2 
16290 C CE1 . TYR C 256  ? 2.4437 1.5169 1.9940 0.6874  -0.6928 -0.5219 256  TYR B CE1 
16291 C CE2 . TYR C 256  ? 2.4109 1.5661 1.9601 0.7208  -0.7110 -0.5231 256  TYR B CE2 
16292 C CZ  . TYR C 256  ? 2.4141 1.5090 1.9491 0.7092  -0.7085 -0.4944 256  TYR B CZ  
16293 O OH  . TYR C 256  ? 2.4107 1.4647 1.9160 0.7200  -0.7214 -0.4379 256  TYR B OH  
16294 N N   . ASN C 257  ? 2.7507 1.9601 2.3519 0.5697  -0.5680 -0.6752 257  ASN B N   
16295 C CA  . ASN C 257  ? 2.8307 1.9983 2.3998 0.5337  -0.5395 -0.6727 257  ASN B CA  
16296 C C   . ASN C 257  ? 2.8115 1.9071 2.3356 0.5271  -0.5513 -0.6345 257  ASN B C   
16297 O O   . ASN C 257  ? 2.8218 1.8762 2.3283 0.5116  -0.5377 -0.6448 257  ASN B O   
16298 C CB  . ASN C 257  ? 2.9723 2.1556 2.5732 0.5249  -0.5088 -0.7217 257  ASN B CB  
16299 C CG  . ASN C 257  ? 3.1210 2.3032 2.7575 0.5553  -0.5188 -0.7460 257  ASN B CG  
16300 O OD1 . ASN C 257  ? 3.1609 2.3887 2.8452 0.5848  -0.5374 -0.7612 257  ASN B OD1 
16301 N ND2 . ASN C 257  ? 3.1939 2.3223 2.8061 0.5491  -0.5073 -0.7510 257  ASN B ND2 
16302 N N   . LYS C 258  ? 2.7983 1.8774 2.3034 0.5388  -0.5765 -0.5899 258  LYS B N   
16303 C CA  . LYS C 258  ? 2.7933 1.8076 2.2691 0.5356  -0.5925 -0.5515 258  LYS B CA  
16304 C C   . LYS C 258  ? 2.7314 1.7327 2.1816 0.5300  -0.6027 -0.4976 258  LYS B C   
16305 O O   . LYS C 258  ? 2.7251 1.7441 2.1809 0.5568  -0.6202 -0.4759 258  LYS B O   
16306 C CB  . LYS C 258  ? 2.8887 1.8887 2.3861 0.5703  -0.6171 -0.5543 258  LYS B CB  
16307 C CG  . LYS C 258  ? 2.9675 1.9229 2.4623 0.5651  -0.6119 -0.5782 258  LYS B CG  
16308 C CD  . LYS C 258  ? 3.0219 1.9118 2.4731 0.5343  -0.6132 -0.5472 258  LYS B CD  
16309 C CE  . LYS C 258  ? 3.0894 1.9248 2.5244 0.5269  -0.6094 -0.5720 258  LYS B CE  
16310 N NZ  . LYS C 258  ? 3.1132 1.8891 2.5037 0.4932  -0.6123 -0.5456 258  LYS B NZ  
16311 N N   . VAL C 259  ? 2.6440 1.6122 2.0653 0.4967  -0.5912 -0.4745 259  VAL B N   
16312 C CA  . VAL C 259  ? 2.5718 1.5340 1.9741 0.4875  -0.5928 -0.4249 259  VAL B CA  
16313 C C   . VAL C 259  ? 2.5249 1.4614 1.9279 0.5113  -0.6181 -0.3774 259  VAL B C   
16314 O O   . VAL C 259  ? 2.5401 1.4425 1.9522 0.5241  -0.6366 -0.3740 259  VAL B O   
16315 C CB  . VAL C 259  ? 2.5010 1.4266 1.8776 0.4475  -0.5797 -0.4055 259  VAL B CB  
16316 C CG1 . VAL C 259  ? 2.4907 1.4284 1.8614 0.4241  -0.5537 -0.4515 259  VAL B CG1 
16317 C CG2 . VAL C 259  ? 2.5367 1.3980 1.9049 0.4406  -0.6007 -0.3758 259  VAL B CG2 
16318 N N   . VAL C 260  ? 2.4992 1.4504 1.8920 0.5181  -0.6165 -0.3404 260  VAL B N   
16319 C CA  . VAL C 260  ? 2.5277 1.4503 1.9182 0.5367  -0.6334 -0.2860 260  VAL B CA  
16320 C C   . VAL C 260  ? 2.5743 1.4375 1.9667 0.5128  -0.6416 -0.2568 260  VAL B C   
16321 O O   . VAL C 260  ? 2.5711 1.4195 1.9549 0.4795  -0.6311 -0.2686 260  VAL B O   
16322 C CB  . VAL C 260  ? 2.4828 1.4224 1.8551 0.5389  -0.6210 -0.2482 260  VAL B CB  
16323 C CG1 . VAL C 260  ? 2.5087 1.4129 1.8804 0.5544  -0.6319 -0.1848 260  VAL B CG1 
16324 C CG2 . VAL C 260  ? 2.4634 1.4568 1.8294 0.5642  -0.6184 -0.2781 260  VAL B CG2 
16325 N N   . THR C 261  ? 2.6434 1.4704 2.0474 0.5294  -0.6617 -0.2195 261  THR B N   
16326 C CA  . THR C 261  ? 2.6996 1.4687 2.1109 0.5051  -0.6732 -0.1878 261  THR B CA  
16327 C C   . THR C 261  ? 2.7282 1.4842 2.1445 0.4997  -0.6696 -0.1221 261  THR B C   
16328 O O   . THR C 261  ? 2.7226 1.4909 2.1293 0.4770  -0.6520 -0.1090 261  THR B O   
16329 C CB  . THR C 261  ? 2.7708 1.4982 2.1994 0.5205  -0.6984 -0.1914 261  THR B CB  
16330 O OG1 . THR C 261  ? 2.7910 1.5230 2.2150 0.5202  -0.6978 -0.2523 261  THR B OG1 
16331 C CG2 . THR C 261  ? 2.7996 1.4657 2.2391 0.4952  -0.7142 -0.1544 261  THR B CG2 
16332 N N   . GLU C 262  ? 2.7771 1.5078 2.2115 0.5211  -0.6838 -0.0787 262  GLU B N   
16333 C CA  . GLU C 262  ? 2.8271 1.5515 2.2691 0.5219  -0.6743 -0.0146 262  GLU B CA  
16334 C C   . GLU C 262  ? 2.8082 1.5813 2.2245 0.5507  -0.6558 -0.0151 262  GLU B C   
16335 O O   . GLU C 262  ? 2.7867 1.5878 2.1906 0.5781  -0.6613 -0.0523 262  GLU B O   
16336 C CB  . GLU C 262  ? 2.9575 1.6376 2.4299 0.5364  -0.6923 0.0347  262  GLU B CB  
16337 C CG  . GLU C 262  ? 3.0521 1.7238 2.5396 0.5385  -0.6783 0.1064  262  GLU B CG  
16338 C CD  . GLU C 262  ? 3.1753 1.8057 2.6969 0.5566  -0.6931 0.1562  262  GLU B CD  
16339 O OE1 . GLU C 262  ? 3.2235 1.8610 2.7415 0.5866  -0.6794 0.2005  262  GLU B OE1 
16340 O OE2 . GLU C 262  ? 3.2285 1.8163 2.7784 0.5417  -0.7178 0.1510  262  GLU B OE2 
16341 N N   . ALA C 263  ? 2.8010 1.5831 2.2096 0.5450  -0.6349 0.0251  263  ALA B N   
16342 C CA  . ALA C 263  ? 2.8130 1.6332 2.1901 0.5728  -0.6174 0.0284  263  ALA B CA  
16343 C C   . ALA C 263  ? 2.7741 1.5833 2.1521 0.5691  -0.5958 0.0915  263  ALA B C   
16344 O O   . ALA C 263  ? 2.7885 1.5730 2.1939 0.5376  -0.5926 0.1204  263  ALA B O   
16345 C CB  . ALA C 263  ? 2.8035 1.6670 2.1582 0.5618  -0.6063 -0.0289 263  ALA B CB  
16346 N N   . ASP C 264  ? 2.7509 1.5761 2.0989 0.6030  -0.5817 0.1141  264  ASP B N   
16347 C CA  . ASP C 264  ? 2.7554 1.5722 2.0996 0.6039  -0.5545 0.1733  264  ASP B CA  
16348 C C   . ASP C 264  ? 2.7150 1.5681 2.0216 0.5996  -0.5308 0.1486  264  ASP B C   
16349 O O   . ASP C 264  ? 2.6898 1.5712 1.9561 0.6262  -0.5320 0.1141  264  ASP B O   
16350 C CB  . ASP C 264  ? 2.8533 1.6526 2.1852 0.6468  -0.5505 0.2248  264  ASP B CB  
16351 C CG  . ASP C 264  ? 2.9578 1.7209 2.3298 0.6381  -0.5353 0.3016  264  ASP B CG  
16352 O OD1 . ASP C 264  ? 2.9580 1.7190 2.3559 0.6034  -0.5216 0.3175  264  ASP B OD1 
16353 O OD2 . ASP C 264  ? 3.0323 1.7694 2.4140 0.6657  -0.5371 0.3470  264  ASP B OD2 
16354 N N   . VAL C 265  ? 2.7122 1.5633 2.0343 0.5659  -0.5119 0.1645  265  VAL B N   
16355 C CA  . VAL C 265  ? 2.6398 1.5209 1.9313 0.5579  -0.4880 0.1422  265  VAL B CA  
16356 C C   . VAL C 265  ? 2.6907 1.5665 1.9662 0.5717  -0.4557 0.1964  265  VAL B C   
16357 O O   . VAL C 265  ? 2.7166 1.5673 2.0277 0.5598  -0.4447 0.2533  265  VAL B O   
16358 C CB  . VAL C 265  ? 2.5105 1.3949 1.8245 0.5116  -0.4839 0.1213  265  VAL B CB  
16359 C CG1 . VAL C 265  ? 2.4503 1.3657 1.7316 0.5089  -0.4602 0.0950  265  VAL B CG1 
16360 C CG2 . VAL C 265  ? 2.4709 1.3553 1.7994 0.4929  -0.5101 0.0691  265  VAL B CG2 
16361 N N   . TYR C 266  ? 2.7032 1.6020 1.9276 0.5951  -0.4400 0.1771  266  TYR B N   
16362 C CA  . TYR C 266  ? 2.7523 1.6438 1.9512 0.6125  -0.4055 0.2247  266  TYR B CA  
16363 C C   . TYR C 266  ? 2.6918 1.6075 1.8586 0.6030  -0.3839 0.1931  266  TYR B C   
16364 O O   . TYR C 266  ? 2.6949 1.6299 1.8105 0.6273  -0.3860 0.1543  266  TYR B O   
16365 C CB  . TYR C 266  ? 2.8990 1.7808 2.0517 0.6641  -0.4034 0.2483  266  TYR B CB  
16366 C CG  . TYR C 266  ? 3.0540 1.9036 2.2384 0.6778  -0.4099 0.3042  266  TYR B CG  
16367 C CD1 . TYR C 266  ? 3.0973 1.9394 2.3182 0.6689  -0.4440 0.2867  266  TYR B CD1 
16368 C CD2 . TYR C 266  ? 3.1489 1.9735 2.3272 0.7015  -0.3801 0.3747  266  TYR B CD2 
16369 C CE1 . TYR C 266  ? 3.1757 1.9857 2.4283 0.6814  -0.4507 0.3372  266  TYR B CE1 
16370 C CE2 . TYR C 266  ? 3.2277 2.0221 2.4408 0.7139  -0.3844 0.4279  266  TYR B CE2 
16371 C CZ  . TYR C 266  ? 3.2323 2.0191 2.4832 0.7031  -0.4212 0.4084  266  TYR B CZ  
16372 O OH  . TYR C 266  ? 3.2774 2.0314 2.5661 0.7147  -0.4262 0.4608  266  TYR B OH  
16373 N N   . ILE C 267  ? 2.5944 1.5067 1.7922 0.5687  -0.3644 0.2118  267  ILE B N   
16374 C CA  . ILE C 267  ? 2.4913 1.4226 1.6659 0.5560  -0.3421 0.1855  267  ILE B CA  
16375 C C   . ILE C 267  ? 2.5141 1.4329 1.6714 0.5701  -0.3025 0.2366  267  ILE B C   
16376 O O   . ILE C 267  ? 2.5377 1.4365 1.7360 0.5598  -0.2865 0.2959  267  ILE B O   
16377 C CB  . ILE C 267  ? 2.3884 1.3253 1.6047 0.5084  -0.3457 0.1666  267  ILE B CB  
16378 C CG1 . ILE C 267  ? 2.3152 1.2592 1.5494 0.4939  -0.3807 0.1196  267  ILE B CG1 
16379 C CG2 . ILE C 267  ? 2.3607 1.3183 1.5525 0.4966  -0.3247 0.1325  267  ILE B CG2 
16380 C CD1 . ILE C 267  ? 2.2575 1.1968 1.5295 0.4484  -0.3866 0.1083  267  ILE B CD1 
16381 N N   . THR C 268  ? 2.5132 1.4431 1.6119 0.5935  -0.2870 0.2118  268  THR B N   
16382 C CA  . THR C 268  ? 2.5471 1.4626 1.6162 0.6131  -0.2464 0.2541  268  THR B CA  
16383 C C   . THR C 268  ? 2.5178 1.4503 1.5662 0.5965  -0.2306 0.2130  268  THR B C   
16384 O O   . THR C 268  ? 2.5296 1.4839 1.5513 0.5958  -0.2500 0.1486  268  THR B O   
16385 C CB  . THR C 268  ? 2.6201 1.5239 1.6182 0.6669  -0.2413 0.2631  268  THR B CB  
16386 O OG1 . THR C 268  ? 2.6439 1.5694 1.6004 0.6793  -0.2724 0.1939  268  THR B OG1 
16387 C CG2 . THR C 268  ? 2.6673 1.5480 1.6827 0.6887  -0.2468 0.3176  268  THR B CG2 
16388 N N   . PHE C 269  ? 2.5023 1.4248 1.5674 0.5839  -0.1951 0.2508  269  PHE B N   
16389 C CA  . PHE C 269  ? 2.4322 1.3667 1.4833 0.5661  -0.1766 0.2173  269  PHE B CA  
16390 C C   . PHE C 269  ? 2.3851 1.3064 1.3736 0.6003  -0.1426 0.2275  269  PHE B C   
16391 O O   . PHE C 269  ? 2.4397 1.3407 1.3919 0.6395  -0.1288 0.2661  269  PHE B O   
16392 C CB  . PHE C 269  ? 2.4186 1.3507 1.5330 0.5253  -0.1617 0.2473  269  PHE B CB  
16393 C CG  . PHE C 269  ? 2.3812 1.3172 1.5527 0.4927  -0.1931 0.2452  269  PHE B CG  
16394 C CD1 . PHE C 269  ? 2.3811 1.2991 1.6047 0.4857  -0.1947 0.3053  269  PHE B CD1 
16395 C CD2 . PHE C 269  ? 2.3536 1.3094 1.5267 0.4702  -0.2209 0.1823  269  PHE B CD2 
16396 C CE1 . PHE C 269  ? 2.3597 1.2762 1.6302 0.4562  -0.2266 0.3000  269  PHE B CE1 
16397 C CE2 . PHE C 269  ? 2.3319 1.2862 1.5485 0.4426  -0.2483 0.1782  269  PHE B CE2 
16398 C CZ  . PHE C 269  ? 2.3410 1.2740 1.6033 0.4355  -0.2530 0.2356  269  PHE B CZ  
16399 N N   . GLY C 270  ? 2.2924 1.2221 1.2671 0.5857  -0.1270 0.1943  270  GLY B N   
16400 C CA  . GLY C 270  ? 2.2997 1.2130 1.2112 0.6167  -0.0942 0.1982  270  GLY B CA  
16401 C C   . GLY C 270  ? 2.2495 1.1717 1.1567 0.5940  -0.0797 0.1577  270  GLY B C   
16402 O O   . GLY C 270  ? 2.2375 1.1836 1.1739 0.5606  -0.1024 0.1082  270  GLY B O   
16403 N N   . ILE C 271  ? 2.1830 1.0840 1.0545 0.6127  -0.0395 0.1796  271  ILE B N   
16404 C CA  . ILE C 271  ? 2.0715 0.9754 0.9377 0.5938  -0.0214 0.1454  271  ILE B CA  
16405 C C   . ILE C 271  ? 2.1284 1.0362 0.9269 0.6133  -0.0401 0.0767  271  ILE B C   
16406 O O   . ILE C 271  ? 2.1593 1.0715 0.9225 0.6376  -0.0702 0.0556  271  ILE B O   
16407 C CB  . ILE C 271  ? 2.0304 0.9075 0.8866 0.6080  0.0296  0.1962  271  ILE B CB  
16408 C CG1 . ILE C 271  ? 1.9726 0.8431 0.8912 0.6021  0.0453  0.2743  271  ILE B CG1 
16409 C CG2 . ILE C 271  ? 1.9875 0.8691 0.8639 0.5776  0.0477  0.1704  271  ILE B CG2 
16410 C CD1 . ILE C 271  ? 1.8676 0.7602 0.8720 0.5522  0.0215  0.2769  271  ILE B CD1 
16411 N N   . ARG C 272  ? 2.1798 1.0852 0.9625 0.6030  -0.0244 0.0414  272  ARG B N   
16412 C CA  . ARG C 272  ? 2.2967 1.2083 1.0264 0.6155  -0.0482 -0.0305 272  ARG B CA  
16413 C C   . ARG C 272  ? 2.4073 1.3108 1.1280 0.6012  -0.0249 -0.0617 272  ARG B C   
16414 O O   . ARG C 272  ? 2.3592 1.2754 1.1397 0.5607  -0.0136 -0.0635 272  ARG B O   
16415 C CB  . ARG C 272  ? 2.2301 1.1791 0.9993 0.5909  -0.0951 -0.0819 272  ARG B CB  
16416 C CG  . ARG C 272  ? 2.2400 1.2009 0.9656 0.6066  -0.1289 -0.1537 272  ARG B CG  
16417 C CD  . ARG C 272  ? 2.1984 1.1892 0.9534 0.6023  -0.1730 -0.1773 272  ARG B CD  
16418 N NE  . ARG C 272  ? 2.2127 1.2284 0.9622 0.6008  -0.2091 -0.2522 272  ARG B NE  
16419 C CZ  . ARG C 272  ? 2.2223 1.2603 0.9756 0.6131  -0.2509 -0.2800 272  ARG B CZ  
16420 N NH1 . ARG C 272  ? 2.2204 1.2547 0.9769 0.6287  -0.2602 -0.2386 272  ARG B NH1 
16421 N NH2 . ARG C 272  ? 2.2232 1.2866 0.9814 0.6106  -0.2837 -0.3480 272  ARG B NH2 
16422 N N   . GLU C 273  ? 2.5556 1.4348 1.1980 0.6355  -0.0187 -0.0871 273  GLU B N   
16423 C CA  . GLU C 273  ? 2.6553 1.5227 1.2849 0.6243  0.0010  -0.1221 273  GLU B CA  
16424 C C   . GLU C 273  ? 2.6152 1.5173 1.2924 0.5849  -0.0308 -0.1903 273  GLU B C   
16425 O O   . GLU C 273  ? 2.5867 1.4953 1.3126 0.5488  -0.0127 -0.1983 273  GLU B O   
16426 C CB  . GLU C 273  ? 2.8332 1.6631 1.3603 0.6718  0.0079  -0.1421 273  GLU B CB  
16427 C CG  . GLU C 273  ? 2.9400 1.7266 1.4266 0.6998  0.0636  -0.0832 273  GLU B CG  
16428 C CD  . GLU C 273  ? 2.9200 1.7097 1.4809 0.6631  0.1030  -0.0471 273  GLU B CD  
16429 O OE1 . GLU C 273  ? 2.8917 1.6914 1.4849 0.6302  0.1023  -0.0883 273  GLU B OE1 
16430 O OE2 . GLU C 273  ? 2.9226 1.7049 1.5131 0.6674  0.1341  0.0242  273  GLU B OE2 
16431 N N   . ASP C 274  ? 2.6272 1.5517 1.2935 0.5928  -0.0770 -0.2371 274  ASP B N   
16432 C CA  . ASP C 274  ? 2.6061 1.5636 1.3146 0.5615  -0.1071 -0.3066 274  ASP B CA  
16433 C C   . ASP C 274  ? 2.5890 1.5797 1.3136 0.5654  -0.1560 -0.3373 274  ASP B C   
16434 O O   . ASP C 274  ? 2.5801 1.5703 1.2936 0.5859  -0.1667 -0.3010 274  ASP B O   
16435 C CB  . ASP C 274  ? 2.6577 1.5984 1.3215 0.5710  -0.1085 -0.3620 274  ASP B CB  
16436 C CG  . ASP C 274  ? 3.1407 2.0513 1.7031 0.6259  -0.1250 -0.3736 274  ASP B CG  
16437 O OD1 . ASP C 274  ? 3.1746 2.0915 1.7118 0.6346  -0.1617 -0.4380 274  ASP B OD1 
16438 O OD2 . ASP C 274  ? 3.1838 2.0626 1.6910 0.6608  -0.1013 -0.3186 274  ASP B OD2 
16439 N N   . LEU C 275  ? 2.6109 1.6305 1.3670 0.5456  -0.1848 -0.4036 275  LEU B N   
16440 C CA  . LEU C 275  ? 2.6466 1.6990 1.4196 0.5524  -0.2321 -0.4387 275  LEU B CA  
16441 C C   . LEU C 275  ? 2.7995 1.8506 1.5179 0.5849  -0.2704 -0.4944 275  LEU B C   
16442 O O   . LEU C 275  ? 2.7976 1.8820 1.5440 0.5845  -0.3123 -0.5380 275  LEU B O   
16443 C CB  . LEU C 275  ? 2.5247 1.6181 1.3892 0.5060  -0.2403 -0.4658 275  LEU B CB  
16444 C CG  . LEU C 275  ? 2.4248 1.5181 1.3341 0.4799  -0.2151 -0.4107 275  LEU B CG  
16445 C CD1 . LEU C 275  ? 2.3562 1.4822 1.3422 0.4358  -0.2181 -0.4418 275  LEU B CD1 
16446 C CD2 . LEU C 275  ? 2.4112 1.5012 1.3064 0.5038  -0.2298 -0.3679 275  LEU B CD2 
16447 N N   . LYS C 276  ? 2.9449 1.9563 1.5859 0.6136  -0.2567 -0.4935 276  LYS B N   
16448 C CA  . LYS C 276  ? 3.0812 2.0794 1.6479 0.6543  -0.2946 -0.5349 276  LYS B CA  
16449 C C   . LYS C 276  ? 3.2714 2.2279 1.7432 0.7058  -0.2832 -0.4821 276  LYS B C   
16450 O O   . LYS C 276  ? 3.3918 2.3228 1.7779 0.7478  -0.3063 -0.5030 276  LYS B O   
16451 C CB  . LYS C 276  ? 3.0538 2.0345 1.5978 0.6491  -0.2934 -0.5872 276  LYS B CB  
16452 C CG  . LYS C 276  ? 3.0643 2.0301 1.5320 0.6889  -0.3404 -0.6387 276  LYS B CG  
16453 C CD  . LYS C 276  ? 3.0192 1.9685 1.4757 0.6785  -0.3445 -0.6973 276  LYS B CD  
16454 C CE  . LYS C 276  ? 2.9919 1.8831 1.3759 0.6944  -0.2949 -0.6669 276  LYS B CE  
16455 N NZ  . LYS C 276  ? 3.0651 1.9064 1.3207 0.7533  -0.3060 -0.6620 276  LYS B NZ  
16456 N N   . ASP C 277  ? 3.3166 2.2648 1.8058 0.7019  -0.2472 -0.4125 277  ASP B N   
16457 C CA  . ASP C 277  ? 3.4769 2.3863 1.8923 0.7458  -0.2252 -0.3505 277  ASP B CA  
16458 C C   . ASP C 277  ? 3.5025 2.4297 1.9269 0.7626  -0.2552 -0.3287 277  ASP B C   
16459 O O   . ASP C 277  ? 3.4530 2.4028 1.9492 0.7362  -0.2490 -0.2968 277  ASP B O   
16460 C CB  . ASP C 277  ? 3.5320 2.4214 1.9724 0.7299  -0.1658 -0.2848 277  ASP B CB  
16461 C CG  . ASP C 277  ? 3.6802 2.5307 2.0581 0.7728  -0.1350 -0.2138 277  ASP B CG  
16462 O OD1 . ASP C 277  ? 3.7963 2.6273 2.0955 0.8186  -0.1552 -0.2149 277  ASP B OD1 
16463 O OD2 . ASP C 277  ? 3.6806 2.5195 2.0911 0.7606  -0.0897 -0.1546 277  ASP B OD2 
16464 N N   . ASP C 278  ? 3.5881 2.5024 1.9369 0.8074  -0.2895 -0.3471 278  ASP B N   
16465 C CA  . ASP C 278  ? 3.5710 2.4967 1.9180 0.8301  -0.3187 -0.3259 278  ASP B CA  
16466 C C   . ASP C 278  ? 3.5350 2.4370 1.8788 0.8423  -0.2786 -0.2410 278  ASP B C   
16467 O O   . ASP C 278  ? 3.5123 2.4252 1.8780 0.8505  -0.2950 -0.2139 278  ASP B O   
16468 C CB  . ASP C 278  ? 4.0697 2.9797 2.3246 0.8808  -0.3630 -0.3595 278  ASP B CB  
16469 C CG  . ASP C 278  ? 4.1463 3.0010 2.2847 0.9211  -0.3420 -0.3572 278  ASP B CG  
16470 O OD1 . ASP C 278  ? 4.1353 2.9588 2.2565 0.9197  -0.2866 -0.3124 278  ASP B OD1 
16471 O OD2 . ASP C 278  ? 4.2131 3.0537 2.2749 0.9560  -0.3825 -0.4007 278  ASP B OD2 
16472 N N   . GLN C 279  ? 3.4944 2.3644 1.8182 0.8424  -0.2258 -0.1993 279  GLN B N   
16473 C CA  . GLN C 279  ? 3.4540 2.2973 1.7715 0.8588  -0.1840 -0.1162 279  GLN B CA  
16474 C C   . GLN C 279  ? 3.2632 2.1126 1.6598 0.8171  -0.1410 -0.0761 279  GLN B C   
16475 O O   . GLN C 279  ? 3.1997 2.0526 1.6183 0.7895  -0.1240 -0.1005 279  GLN B O   
16476 C CB  . GLN C 279  ? 3.6123 2.4019 1.8165 0.9133  -0.1547 -0.0865 279  GLN B CB  
16477 C CG  . GLN C 279  ? 3.6712 2.4341 1.8737 0.9337  -0.1100 0.0030  279  GLN B CG  
16478 C CD  . GLN C 279  ? 3.6942 2.4710 1.9216 0.9440  -0.1378 0.0307  279  GLN B CD  
16479 O OE1 . GLN C 279  ? 3.6332 2.4279 1.9470 0.9152  -0.1283 0.0718  279  GLN B OE1 
16480 N NE2 . GLN C 279  ? 3.7765 2.5427 1.9272 0.9859  -0.1743 0.0075  279  GLN B NE2 
16481 N N   . LYS C 280  ? 3.1808 2.0286 1.6194 0.8144  -0.1242 -0.0114 280  LYS B N   
16482 C CA  . LYS C 280  ? 3.0470 1.9041 1.5704 0.7734  -0.0931 0.0286  280  LYS B CA  
16483 C C   . LYS C 280  ? 3.0439 1.8812 1.5830 0.7898  -0.0655 0.1117  280  LYS B C   
16484 O O   . LYS C 280  ? 3.0784 1.9184 1.6194 0.8054  -0.0883 0.1295  280  LYS B O   
16485 C CB  . LYS C 280  ? 2.9043 1.8050 1.5146 0.7238  -0.1268 -0.0095 280  LYS B CB  
16486 C CG  . LYS C 280  ? 2.8298 1.7510 1.4598 0.7287  -0.1705 -0.0190 280  LYS B CG  
16487 C CD  . LYS C 280  ? 2.8079 1.7528 1.4132 0.7360  -0.2180 -0.0955 280  LYS B CD  
16488 C CE  . LYS C 280  ? 2.7761 1.7391 1.4037 0.7444  -0.2581 -0.0977 280  LYS B CE  
16489 N NZ  . LYS C 280  ? 2.7722 1.7639 1.3921 0.7503  -0.3072 -0.1693 280  LYS B NZ  
16490 N N   . GLU C 281  ? 3.0215 1.8389 1.5767 0.7863  -0.0155 0.1635  281  GLU B N   
16491 C CA  . GLU C 281  ? 3.0379 1.8354 1.6149 0.8022  0.0169  0.2464  281  GLU B CA  
16492 C C   . GLU C 281  ? 2.8959 1.7183 1.5720 0.7655  -0.0035 0.2728  281  GLU B C   
16493 O O   . GLU C 281  ? 2.7932 1.6289 1.5456 0.7245  0.0075  0.2879  281  GLU B O   
16494 C CB  . GLU C 281  ? 3.1619 1.9367 1.7454 0.8033  0.0754  0.2916  281  GLU B CB  
16495 C CG  . GLU C 281  ? 3.3614 2.1098 1.8515 0.8322  0.0964  0.2565  281  GLU B CG  
16496 C CD  . GLU C 281  ? 3.5899 2.3101 1.9653 0.8888  0.0844  0.2411  281  GLU B CD  
16497 O OE1 . GLU C 281  ? 3.6524 2.3708 2.0197 0.9101  0.0678  0.2682  281  GLU B OE1 
16498 O OE2 . GLU C 281  ? 3.6999 2.3969 1.9903 0.9130  0.0904  0.2011  281  GLU B OE2 
16499 N N   . MET C 282  ? 2.8901 1.7155 1.5629 0.7811  -0.0339 0.2791  282  MET B N   
16500 C CA  . MET C 282  ? 2.8341 1.6762 1.5956 0.7498  -0.0537 0.3054  282  MET B CA  
16501 C C   . MET C 282  ? 2.8401 1.6685 1.6648 0.7377  -0.0135 0.3825  282  MET B C   
16502 O O   . MET C 282  ? 2.8704 1.6806 1.6761 0.7506  0.0312  0.4124  282  MET B O   
16503 C CB  . MET C 282  ? 2.8648 1.7026 1.6071 0.7774  -0.0835 0.3135  282  MET B CB  
16504 C CG  . MET C 282  ? 2.8711 1.7293 1.5740 0.7844  -0.1324 0.2392  282  MET B CG  
16505 S SD  . MET C 282  ? 2.8737 1.7749 1.6498 0.7258  -0.1687 0.1727  282  MET B SD  
16506 C CE  . MET C 282  ? 2.3349 1.2389 1.0699 0.7188  -0.1475 0.1267  282  MET B CE  
16507 N N   . MET C 283  ? 2.8371 1.6733 1.7401 0.7132  -0.0302 0.4145  283  MET B N   
16508 C CA  . MET C 283  ? 2.9087 1.7362 1.8878 0.6953  0.0006  0.4848  283  MET B CA  
16509 C C   . MET C 283  ? 3.0283 1.8505 2.0634 0.6933  -0.0179 0.5295  283  MET B C   
16510 O O   . MET C 283  ? 3.0188 1.8557 2.0796 0.6723  -0.0626 0.4961  283  MET B O   
16511 C CB  . MET C 283  ? 2.8178 1.6654 1.8623 0.6431  -0.0042 0.4664  283  MET B CB  
16512 C CG  . MET C 283  ? 2.9949 1.8477 1.9975 0.6382  0.0148  0.4225  283  MET B CG  
16513 S SD  . MET C 283  ? 2.1317 1.0093 1.2018 0.5764  0.0002  0.3882  283  MET B SD  
16514 C CE  . MET C 283  ? 2.0618 0.9631 1.1374 0.5550  -0.0599 0.3239  283  MET B CE  
16515 N N   . GLN C 284  ? 3.1760 1.9757 2.2323 0.7155  0.0182  0.6053  284  GLN B N   
16516 C CA  . GLN C 284  ? 3.2598 2.0506 2.3808 0.7127  0.0063  0.6573  284  GLN B CA  
16517 C C   . GLN C 284  ? 3.2548 2.0625 2.4721 0.6583  -0.0274 0.6524  284  GLN B C   
16518 O O   . GLN C 284  ? 3.2258 2.0513 2.4605 0.6236  -0.0364 0.6155  284  GLN B O   
16519 C CB  . GLN C 284  ? 3.3122 2.0797 2.4626 0.7357  0.0595  0.7443  284  GLN B CB  
16520 C CG  . GLN C 284  ? 3.2693 2.0436 2.4871 0.7071  0.0906  0.7758  284  GLN B CG  
16521 C CD  . GLN C 284  ? 3.2811 2.0555 2.4292 0.7202  0.1219  0.7441  284  GLN B CD  
16522 O OE1 . GLN C 284  ? 3.2554 2.0452 2.3594 0.7063  0.0960  0.6722  284  GLN B OE1 
16523 N NE2 . GLN C 284  ? 3.3248 2.0805 2.4659 0.7472  0.1798  0.7984  284  GLN B NE2 
16524 N N   . THR C 285  ? 3.2818 2.0802 2.5600 0.6517  -0.0458 0.6912  285  THR B N   
16525 C CA  . THR C 285  ? 3.2516 2.0585 2.6199 0.6024  -0.0787 0.6926  285  THR B CA  
16526 C C   . THR C 285  ? 3.1970 2.0262 2.5391 0.5732  -0.1154 0.6101  285  THR B C   
16527 O O   . THR C 285  ? 3.1341 1.9748 2.5128 0.5355  -0.1200 0.5962  285  THR B O   
16528 C CB  . THR C 285  ? 3.2623 2.0784 2.7133 0.5758  -0.0463 0.7440  285  THR B CB  
16529 O OG1 . THR C 285  ? 3.3166 2.1258 2.7672 0.6101  0.0075  0.8038  285  THR B OG1 
16530 C CG2 . THR C 285  ? 3.2422 2.0739 2.7998 0.5298  -0.0764 0.7594  285  THR B CG2 
16531 N N   . ALA C 286  ? 3.1943 2.0293 2.4706 0.5937  -0.1388 0.5569  286  ALA B N   
16532 C CA  . ALA C 286  ? 3.1260 1.9817 2.3870 0.5688  -0.1773 0.4807  286  ALA B CA  
16533 C C   . ALA C 286  ? 3.0817 1.9318 2.3837 0.5547  -0.2201 0.4751  286  ALA B C   
16534 O O   . ALA C 286  ? 3.0676 1.9101 2.3438 0.5838  -0.2344 0.4735  286  ALA B O   
16535 C CB  . ALA C 286  ? 3.1503 2.0180 2.3239 0.5989  -0.1793 0.4242  286  ALA B CB  
16536 N N   . MET C 287  ? 3.0420 1.8931 2.4045 0.5108  -0.2409 0.4715  287  MET B N   
16537 C CA  . MET C 287  ? 3.0044 1.8425 2.4144 0.4926  -0.2799 0.4733  287  MET B CA  
16538 C C   . MET C 287  ? 3.0322 1.8685 2.4069 0.5194  -0.3052 0.4433  287  MET B C   
16539 O O   . MET C 287  ? 3.0267 1.8817 2.3430 0.5351  -0.3113 0.3877  287  MET B O   
16540 C CB  . MET C 287  ? 2.9231 1.7678 2.3599 0.4466  -0.3065 0.4332  287  MET B CB  
16541 C CG  . MET C 287  ? 2.8781 1.7124 2.3805 0.4136  -0.3010 0.4784  287  MET B CG  
16542 S SD  . MET C 287  ? 3.3599 2.1983 2.8719 0.3646  -0.3320 0.4252  287  MET B SD  
16543 C CE  . MET C 287  ? 2.8785 1.7472 2.3253 0.3703  -0.3027 0.3730  287  MET B CE  
16544 N N   . GLN C 288  ? 3.0791 1.8924 2.4960 0.5238  -0.3212 0.4819  288  GLN B N   
16545 C CA  . GLN C 288  ? 3.1594 1.9661 2.5552 0.5470  -0.3484 0.4601  288  GLN B CA  
16546 C C   . GLN C 288  ? 3.1507 1.9453 2.5925 0.5152  -0.3900 0.4376  288  GLN B C   
16547 O O   . GLN C 288  ? 3.1253 1.9055 2.6256 0.4812  -0.3982 0.4628  288  GLN B O   
16548 C CB  . GLN C 288  ? 3.2678 2.0524 2.6649 0.5858  -0.3309 0.5227  288  GLN B CB  
16549 C CG  . GLN C 288  ? 3.3420 2.1038 2.8155 0.5723  -0.3133 0.6011  288  GLN B CG  
16550 C CD  . GLN C 288  ? 3.4639 2.2065 2.9347 0.6132  -0.2843 0.6661  288  GLN B CD  
16551 O OE1 . GLN C 288  ? 3.5264 2.2602 2.9505 0.6497  -0.2925 0.6582  288  GLN B OE1 
16552 N NE2 . GLN C 288  ? 3.4963 2.2454 3.0228 0.6016  -0.2459 0.7234  288  GLN B NE2 
16553 N N   . ASN C 289  ? 3.1930 1.9926 2.6059 0.5277  -0.4172 0.3880  289  ASN B N   
16554 C CA  . ASN C 289  ? 3.2239 2.0062 2.6715 0.5066  -0.4557 0.3660  289  ASN B CA  
16555 C C   . ASN C 289  ? 3.1235 1.8980 2.6104 0.4585  -0.4688 0.3566  289  ASN B C   
16556 O O   . ASN C 289  ? 3.0841 1.8401 2.6223 0.4386  -0.4648 0.4073  289  ASN B O   
16557 C CB  . ASN C 289  ? 3.3402 2.0891 2.8286 0.5218  -0.4659 0.4198  289  ASN B CB  
16558 C CG  . ASN C 289  ? 3.4436 2.1931 2.8944 0.5715  -0.4465 0.4477  289  ASN B CG  
16559 O OD1 . ASN C 289  ? 3.4748 2.2491 2.8628 0.5967  -0.4338 0.4170  289  ASN B OD1 
16560 N ND2 . ASN C 289  ? 3.4931 2.2127 2.9816 0.5862  -0.4451 0.5069  289  ASN B ND2 
16561 N N   . THR C 290  ? 3.0854 1.8740 2.5479 0.4408  -0.4843 0.2918  290  THR B N   
16562 C CA  . THR C 290  ? 3.0497 1.8186 2.5408 0.4017  -0.5104 0.2735  290  THR B CA  
16563 C C   . THR C 290  ? 3.0069 1.7770 2.4732 0.4128  -0.5346 0.2165  290  THR B C   
16564 O O   . THR C 290  ? 3.0230 1.8058 2.4660 0.3973  -0.5408 0.1600  290  THR B O   
16565 C CB  . THR C 290  ? 2.6345 1.4177 2.1172 0.3685  -0.4985 0.2529  290  THR B CB  
16566 O OG1 . THR C 290  ? 2.6290 1.3996 2.1550 0.3514  -0.4870 0.3126  290  THR B OG1 
16567 C CG2 . THR C 290  ? 2.6201 1.3883 2.1000 0.3380  -0.5263 0.2059  290  THR B CG2 
16568 N N   . MET C 291  ? 2.9607 1.7182 2.4332 0.4429  -0.5449 0.2345  291  MET B N   
16569 C CA  . MET C 291  ? 2.9151 1.6741 2.3687 0.4615  -0.5666 0.1876  291  MET B CA  
16570 C C   . MET C 291  ? 2.8308 1.6013 2.2658 0.4380  -0.5767 0.1201  291  MET B C   
16571 O O   . MET C 291  ? 2.8214 1.5667 2.2738 0.4050  -0.5911 0.1140  291  MET B O   
16572 C CB  . MET C 291  ? 2.9724 1.6890 2.4645 0.4648  -0.5939 0.2140  291  MET B CB  
16573 C CG  . MET C 291  ? 3.0127 1.7100 2.5353 0.4845  -0.5845 0.2868  291  MET B CG  
16574 S SD  . MET C 291  ? 3.3527 1.9977 2.9247 0.4836  -0.6209 0.3063  291  MET B SD  
16575 C CE  . MET C 291  ? 3.2912 1.9108 2.8855 0.4312  -0.6477 0.2762  291  MET B CE  
16576 N N   . LEU C 292  ? 2.7572 1.5643 2.1568 0.4558  -0.5694 0.0703  292  LEU B N   
16577 C CA  . LEU C 292  ? 2.6704 1.4907 2.0561 0.4392  -0.5758 0.0051  292  LEU B CA  
16578 C C   . LEU C 292  ? 2.6250 1.4055 2.0305 0.4292  -0.6045 -0.0050 292  LEU B C   
16579 O O   . LEU C 292  ? 2.6492 1.4054 2.0731 0.4483  -0.6215 0.0206  292  LEU B O   
16580 C CB  . LEU C 292  ? 2.6683 1.5300 2.0288 0.4685  -0.5721 -0.0422 292  LEU B CB  
16581 C CG  . LEU C 292  ? 2.6354 1.5284 1.9822 0.4541  -0.5645 -0.1076 292  LEU B CG  
16582 C CD1 . LEU C 292  ? 2.6423 1.5128 1.9993 0.4377  -0.5808 -0.1433 292  LEU B CD1 
16583 C CD2 . LEU C 292  ? 2.6023 1.5081 1.9390 0.4265  -0.5396 -0.1039 292  LEU B CD2 
16584 N N   . ILE C 293  ? 2.5441 1.3141 1.9427 0.4003  -0.6092 -0.0422 293  ILE B N   
16585 C CA  . ILE C 293  ? 2.5065 1.2313 1.9164 0.3891  -0.6363 -0.0526 293  ILE B CA  
16586 C C   . ILE C 293  ? 2.4633 1.1922 1.8481 0.3739  -0.6339 -0.1151 293  ILE B C   
16587 O O   . ILE C 293  ? 2.4556 1.1857 1.8248 0.3458  -0.6220 -0.1258 293  ILE B O   
16588 C CB  . ILE C 293  ? 2.4919 1.1733 1.9272 0.3615  -0.6499 -0.0031 293  ILE B CB  
16589 C CG1 . ILE C 293  ? 2.4828 1.1451 1.9545 0.3813  -0.6602 0.0548  293  ILE B CG1 
16590 C CG2 . ILE C 293  ? 2.5283 1.1644 1.9569 0.3357  -0.6742 -0.0308 293  ILE B CG2 
16591 C CD1 . ILE C 293  ? 2.4741 1.0981 1.9860 0.3555  -0.6734 0.1102  293  ILE B CD1 
16592 N N   . ASN C 294  ? 2.4580 1.1897 1.8396 0.3946  -0.6428 -0.1554 294  ASN B N   
16593 C CA  . ASN C 294  ? 2.4622 1.2002 1.8230 0.3858  -0.6356 -0.2161 294  ASN B CA  
16594 C C   . ASN C 294  ? 2.3515 1.1426 1.6976 0.3806  -0.6052 -0.2487 294  ASN B C   
16595 O O   . ASN C 294  ? 2.3375 1.1291 1.6657 0.3614  -0.5921 -0.2868 294  ASN B O   
16596 C CB  . ASN C 294  ? 2.5691 1.2532 1.9154 0.3547  -0.6487 -0.2208 294  ASN B CB  
16597 C CG  . ASN C 294  ? 2.6594 1.3374 1.9817 0.3526  -0.6426 -0.2814 294  ASN B CG  
16598 O OD1 . ASN C 294  ? 2.6816 1.3697 1.9791 0.3322  -0.6221 -0.3070 294  ASN B OD1 
16599 N ND2 . ASN C 294  ? 2.7024 1.3641 2.0326 0.3756  -0.6573 -0.3042 294  ASN B ND2 
16600 N N   . GLY C 295  ? 2.2821 1.1151 1.6343 0.3991  -0.5938 -0.2341 295  GLY B N   
16601 C CA  . GLY C 295  ? 2.2245 1.1094 1.5688 0.4000  -0.5695 -0.2695 295  GLY B CA  
16602 C C   . GLY C 295  ? 2.1893 1.0835 1.5228 0.3768  -0.5488 -0.2453 295  GLY B C   
16603 O O   . GLY C 295  ? 2.1573 1.0904 1.4845 0.3727  -0.5270 -0.2721 295  GLY B O   
16604 N N   . ILE C 296  ? 2.1777 1.0360 1.5142 0.3616  -0.5560 -0.1943 296  ILE B N   
16605 C CA  . ILE C 296  ? 2.1130 0.9754 1.4445 0.3398  -0.5374 -0.1636 296  ILE B CA  
16606 C C   . ILE C 296  ? 2.1544 0.9944 1.5034 0.3428  -0.5443 -0.0968 296  ILE B C   
16607 O O   . ILE C 296  ? 2.1953 1.0016 1.5621 0.3488  -0.5674 -0.0705 296  ILE B O   
16608 C CB  . ILE C 296  ? 1.9926 0.8322 1.3108 0.3022  -0.5319 -0.1765 296  ILE B CB  
16609 C CG1 . ILE C 296  ? 1.9684 0.8191 1.2711 0.2987  -0.5243 -0.2394 296  ILE B CG1 
16610 C CG2 . ILE C 296  ? 1.9089 0.7647 1.2224 0.2838  -0.5077 -0.1554 296  ILE B CG2 
16611 C CD1 . ILE C 296  ? 1.9275 0.8165 1.2203 0.2876  -0.4934 -0.2683 296  ILE B CD1 
16612 N N   . ALA C 297  ? 2.1409 1.0003 1.4875 0.3396  -0.5220 -0.0698 297  ALA B N   
16613 C CA  . ALA C 297  ? 2.1365 0.9758 1.5035 0.3338  -0.5198 -0.0050 297  ALA B CA  
16614 C C   . ALA C 297  ? 2.1384 0.9976 1.4958 0.3163  -0.4915 0.0007  297  ALA B C   
16615 O O   . ALA C 297  ? 2.1434 1.0332 1.4785 0.3151  -0.4745 -0.0430 297  ALA B O   
16616 C CB  . ALA C 297  ? 2.1186 0.9624 1.4937 0.3685  -0.5191 0.0320  297  ALA B CB  
16617 N N   . GLN C 298  ? 2.1516 0.9931 1.5313 0.3024  -0.4867 0.0549  298  GLN B N   
16618 C CA  . GLN C 298  ? 2.1300 0.9830 1.5061 0.2823  -0.4620 0.0653  298  GLN B CA  
16619 C C   . GLN C 298  ? 2.1074 0.9511 1.5140 0.2869  -0.4515 0.1341  298  GLN B C   
16620 O O   . GLN C 298  ? 2.1217 0.9407 1.5598 0.2920  -0.4692 0.1740  298  GLN B O   
16621 C CB  . GLN C 298  ? 2.1833 1.0141 1.5583 0.2451  -0.4732 0.0499  298  GLN B CB  
16622 C CG  . GLN C 298  ? 2.2512 1.1015 1.5922 0.2351  -0.4611 -0.0131 298  GLN B CG  
16623 C CD  . GLN C 298  ? 2.3269 1.1681 1.6600 0.2016  -0.4497 -0.0123 298  GLN B CD  
16624 O OE1 . GLN C 298  ? 2.3673 1.1913 1.7214 0.1868  -0.4516 0.0350  298  GLN B OE1 
16625 N NE2 . GLN C 298  ? 2.3439 1.1972 1.6497 0.1906  -0.4370 -0.0631 298  GLN B NE2 
16626 N N   . VAL C 299  ? 2.0721 0.9348 1.4724 0.2864  -0.4207 0.1490  299  VAL B N   
16627 C CA  . VAL C 299  ? 2.0895 0.9414 1.5248 0.2839  -0.4071 0.2151  299  VAL B CA  
16628 C C   . VAL C 299  ? 2.1214 0.9900 1.5447 0.2693  -0.3787 0.2095  299  VAL B C   
16629 O O   . VAL C 299  ? 2.1766 1.0696 1.5620 0.2756  -0.3635 0.1625  299  VAL B O   
16630 C CB  . VAL C 299  ? 2.0965 0.9553 1.5315 0.3211  -0.3894 0.2511  299  VAL B CB  
16631 C CG1 . VAL C 299  ? 2.1199 0.9546 1.5839 0.3332  -0.4145 0.2801  299  VAL B CG1 
16632 C CG2 . VAL C 299  ? 2.1064 0.9946 1.4886 0.3484  -0.3739 0.2049  299  VAL B CG2 
16633 N N   . THR C 300  ? 2.0870 0.9424 1.5468 0.2493  -0.3729 0.2566  300  THR B N   
16634 C CA  . THR C 300  ? 2.0685 0.9378 1.5225 0.2386  -0.3422 0.2616  300  THR B CA  
16635 C C   . THR C 300  ? 2.1101 0.9876 1.5759 0.2646  -0.3092 0.3102  300  THR B C   
16636 O O   . THR C 300  ? 2.1124 0.9779 1.6094 0.2802  -0.3123 0.3577  300  THR B O   
16637 C CB  . THR C 300  ? 2.5458 1.3971 2.0275 0.2004  -0.3545 0.2780  300  THR B CB  
16638 O OG1 . THR C 300  ? 2.5645 1.3890 2.0973 0.1907  -0.3830 0.3252  300  THR B OG1 
16639 C CG2 . THR C 300  ? 2.5462 1.3937 1.9926 0.1784  -0.3713 0.2186  300  THR B CG2 
16640 N N   . PHE C 301  ? 2.1879 1.0834 1.6269 0.2707  -0.2758 0.2975  301  PHE B N   
16641 C CA  . PHE C 301  ? 2.2954 1.1972 1.7262 0.3025  -0.2415 0.3311  301  PHE B CA  
16642 C C   . PHE C 301  ? 2.4102 1.3105 1.8683 0.2902  -0.2114 0.3708  301  PHE B C   
16643 O O   . PHE C 301  ? 2.4568 1.3674 1.8935 0.2777  -0.1953 0.3412  301  PHE B O   
16644 C CB  . PHE C 301  ? 2.2703 1.1921 1.6383 0.3278  -0.2303 0.2763  301  PHE B CB  
16645 C CG  . PHE C 301  ? 2.2405 1.1663 1.5803 0.3601  -0.1929 0.2969  301  PHE B CG  
16646 C CD1 . PHE C 301  ? 2.2368 1.1498 1.5860 0.3889  -0.1798 0.3513  301  PHE B CD1 
16647 C CD2 . PHE C 301  ? 2.2209 1.1606 1.5214 0.3630  -0.1697 0.2594  301  PHE B CD2 
16648 C CE1 . PHE C 301  ? 2.2543 1.1664 1.5673 0.4217  -0.1426 0.3688  301  PHE B CE1 
16649 C CE2 . PHE C 301  ? 2.2217 1.1597 1.4880 0.3941  -0.1359 0.2744  301  PHE B CE2 
16650 C CZ  . PHE C 301  ? 2.2477 1.1710 1.5164 0.4246  -0.1217 0.3291  301  PHE B CZ  
16651 N N   . ASP C 302  ? 2.4505 1.3379 1.9627 0.2926  -0.2042 0.4389  302  ASP B N   
16652 C CA  . ASP C 302  ? 2.4661 1.3526 2.0147 0.2840  -0.1743 0.4841  302  ASP B CA  
16653 C C   . ASP C 302  ? 2.4577 1.3528 1.9648 0.3184  -0.1277 0.4871  302  ASP B C   
16654 O O   . ASP C 302  ? 2.4481 1.3374 1.9566 0.3501  -0.1075 0.5263  302  ASP B O   
16655 C CB  . ASP C 302  ? 2.5361 1.4079 2.1659 0.2761  -0.1826 0.5572  302  ASP B CB  
16656 C CG  . ASP C 302  ? 2.6071 1.4992 2.2927 0.2577  -0.1550 0.5934  302  ASP B CG  
16657 O OD1 . ASP C 302  ? 2.6333 1.5391 2.3992 0.2330  -0.1708 0.6287  302  ASP B OD1 
16658 O OD2 . ASP C 302  ? 2.6310 1.5247 2.2851 0.2685  -0.1194 0.5881  302  ASP B OD2 
16659 N N   . SER C 303  ? 2.4461 1.3518 1.9129 0.3126  -0.1110 0.4442  303  SER B N   
16660 C CA  . SER C 303  ? 2.4601 1.3704 1.8773 0.3434  -0.0713 0.4343  303  SER B CA  
16661 C C   . SER C 303  ? 2.4655 1.3664 1.9168 0.3577  -0.0296 0.5016  303  SER B C   
16662 O O   . SER C 303  ? 2.5123 1.4078 1.9277 0.3942  0.0042  0.5158  303  SER B O   
16663 C CB  . SER C 303  ? 2.4019 1.3239 1.7792 0.3281  -0.0664 0.3722  303  SER B CB  
16664 O OG  . SER C 303  ? 2.3471 1.2790 1.7032 0.3138  -0.1018 0.3142  303  SER B OG  
16665 N N   . GLU C 304  ? 2.4211 1.3185 1.9413 0.3300  -0.0322 0.5436  304  GLU B N   
16666 C CA  . GLU C 304  ? 2.3863 1.2778 1.9513 0.3403  0.0080  0.6080  304  GLU B CA  
16667 C C   . GLU C 304  ? 2.3464 1.2363 1.9287 0.3727  0.0271  0.6568  304  GLU B C   
16668 O O   . GLU C 304  ? 2.3349 1.2147 1.8843 0.4087  0.0706  0.6779  304  GLU B O   
16669 C CB  . GLU C 304  ? 2.3727 1.2819 2.0246 0.2991  -0.0070 0.6349  304  GLU B CB  
16670 C CG  . GLU C 304  ? 2.3944 1.3190 2.0918 0.2986  0.0359  0.6724  304  GLU B CG  
16671 C CD  . GLU C 304  ? 2.3953 1.3470 2.1912 0.2615  0.0151  0.7033  304  GLU B CD  
16672 O OE1 . GLU C 304  ? 2.4083 1.3637 2.2367 0.2419  -0.0292 0.7030  304  GLU B OE1 
16673 O OE2 . GLU C 304  ? 2.3857 1.3521 2.2256 0.2534  0.0403  0.7278  304  GLU B OE2 
16674 N N   . THR C 305  ? 2.3499 1.2513 1.9844 0.3585  -0.0047 0.6721  305  THR B N   
16675 C CA  . THR C 305  ? 2.3846 1.2872 2.0368 0.3855  0.0069  0.7107  305  THR B CA  
16676 C C   . THR C 305  ? 2.4578 1.3343 2.0096 0.4329  0.0239  0.6912  305  THR B C   
16677 O O   . THR C 305  ? 2.4430 1.3106 1.9687 0.4692  0.0699  0.7219  305  THR B O   
16678 C CB  . THR C 305  ? 2.3648 1.2691 2.0516 0.3646  -0.0446 0.7027  305  THR B CB  
16679 O OG1 . THR C 305  ? 2.3317 1.2543 2.1056 0.3206  -0.0695 0.7182  305  THR B OG1 
16680 C CG2 . THR C 305  ? 2.3826 1.2849 2.0872 0.3922  -0.0346 0.7415  305  THR B CG2 
16681 N N   . ALA C 306  ? 2.5326 1.4052 2.0294 0.4301  -0.0138 0.6323  306  ALA B N   
16682 C CA  . ALA C 306  ? 2.6506 1.5214 2.0662 0.4662  -0.0131 0.5964  306  ALA B CA  
16683 C C   . ALA C 306  ? 2.8196 1.6889 2.1577 0.4968  0.0249  0.5717  306  ALA B C   
16684 O O   . ALA C 306  ? 2.8221 1.6934 2.0865 0.5188  0.0147  0.5221  306  ALA B O   
16685 C CB  . ALA C 306  ? 2.6318 1.5136 2.0228 0.4480  -0.0618 0.5301  306  ALA B CB  
16686 N N   . VAL C 307  ? 2.9347 1.7988 2.2889 0.4992  0.0670  0.6047  307  VAL B N   
16687 C CA  . VAL C 307  ? 3.1673 2.0239 2.4455 0.5292  0.1041  0.5815  307  VAL B CA  
16688 C C   . VAL C 307  ? 3.3864 2.2263 2.6874 0.5532  0.1593  0.6518  307  VAL B C   
16689 O O   . VAL C 307  ? 3.4412 2.2630 2.6777 0.5969  0.1945  0.6618  307  VAL B O   
16690 C CB  . VAL C 307  ? 2.3523 1.2213 1.6121 0.5016  0.0989  0.5219  307  VAL B CB  
16691 C CG1 . VAL C 307  ? 2.3934 1.2492 1.5919 0.5296  0.1424  0.5108  307  VAL B CG1 
16692 C CG2 . VAL C 307  ? 2.3294 1.2140 1.5518 0.4878  0.0540  0.4471  307  VAL B CG2 
16693 N N   . LYS C 308  ? 3.6066 2.4514 3.0005 0.5255  0.1660  0.7017  308  LYS B N   
16694 C CA  . LYS C 308  ? 3.8545 2.6881 3.2860 0.5427  0.2203  0.7677  308  LYS B CA  
16695 C C   . LYS C 308  ? 4.1400 2.9523 3.5243 0.5954  0.2584  0.8048  308  LYS B C   
16696 O O   . LYS C 308  ? 4.2198 3.0168 3.5101 0.6302  0.2847  0.7763  308  LYS B O   
16697 C CB  . LYS C 308  ? 3.8079 2.6764 3.3701 0.5034  0.2154  0.8123  308  LYS B CB  
16698 C CG  . LYS C 308  ? 3.7297 2.6163 3.3342 0.4573  0.1940  0.7860  308  LYS B CG  
16699 C CD  . LYS C 308  ? 3.6771 2.6023 3.4104 0.4265  0.1989  0.8352  308  LYS B CD  
16700 C CE  . LYS C 308  ? 3.6433 2.5888 3.4494 0.4094  0.1635  0.8586  308  LYS B CE  
16701 N NZ  . LYS C 308  ? 3.6069 2.5881 3.5432 0.3804  0.1625  0.9082  308  LYS B NZ  
16702 N N   . GLU C 309  ? 4.3154 3.1369 3.7654 0.5986  0.2619  0.8582  309  GLU B N   
16703 C CA  . GLU C 309  ? 4.5030 3.3016 3.9142 0.6495  0.3041  0.9033  309  GLU B CA  
16704 C C   . GLU C 309  ? 4.4440 3.2186 3.7344 0.6837  0.2834  0.8566  309  GLU B C   
16705 O O   . GLU C 309  ? 4.6592 3.4099 3.8847 0.7316  0.3170  0.8792  309  GLU B O   
16706 C CB  . GLU C 309  ? 4.7667 3.5927 4.2856 0.6392  0.3084  0.9603  309  GLU B CB  
16707 C CG  . GLU C 309  ? 5.1428 3.9440 4.6256 0.6916  0.3521  1.0110  309  GLU B CG  
16708 C CD  . GLU C 309  ? 5.3841 4.1690 4.8592 0.7269  0.4272  1.0613  309  GLU B CD  
16709 O OE1 . GLU C 309  ? 5.4307 4.2353 4.9687 0.7043  0.4470  1.0712  309  GLU B OE1 
16710 O OE2 . GLU C 309  ? 5.4938 4.2435 4.8976 0.7792  0.4675  1.0926  309  GLU B OE2 
16711 N N   . LEU C 310  ? 4.2060 2.9975 3.4699 0.6574  0.2302  0.7844  310  LEU B N   
16712 C CA  . LEU C 310  ? 4.0956 2.8819 3.2647 0.6826  0.2037  0.7310  310  LEU B CA  
16713 C C   . LEU C 310  ? 3.9139 2.6939 2.9808 0.7021  0.2148  0.6689  310  LEU B C   
16714 O O   . LEU C 310  ? 3.9026 2.6819 2.8922 0.7191  0.1870  0.6144  310  LEU B O   
16715 C CB  . LEU C 310  ? 4.0841 2.8913 3.2843 0.6479  0.1397  0.6894  310  LEU B CB  
16716 C CG  . LEU C 310  ? 4.0483 2.8621 3.3591 0.6162  0.1189  0.7391  310  LEU B CG  
16717 C CD1 . LEU C 310  ? 4.0150 2.8382 3.3292 0.5993  0.0603  0.6995  310  LEU B CD1 
16718 C CD2 . LEU C 310  ? 4.0903 2.8867 3.4450 0.6425  0.1583  0.8251  310  LEU B CD2 
16719 N N   . SER C 311  ? 3.7429 2.5172 2.8131 0.6997  0.2541  0.6773  311  SER B N   
16720 C CA  . SER C 311  ? 3.6246 2.3869 2.6008 0.7196  0.2696  0.6232  311  SER B CA  
16721 C C   . SER C 311  ? 3.5339 2.2884 2.5383 0.7134  0.3177  0.6484  311  SER B C   
16722 O O   . SER C 311  ? 3.4856 2.2477 2.5846 0.6931  0.3353  0.7066  311  SER B O   
16723 C CB  . SER C 311  ? 3.5063 2.2908 2.4553 0.6919  0.2170  0.5359  311  SER B CB  
16724 O OG  . SER C 311  ? 3.4866 2.2714 2.3758 0.7133  0.1810  0.5009  311  SER B OG  
16725 N N   . TYR C 312  ? 3.5422 2.2807 2.4678 0.7311  0.3375  0.6048  312  TYR B N   
16726 C CA  . TYR C 312  ? 3.5286 2.2583 2.4769 0.7245  0.3816  0.6203  312  TYR B CA  
16727 C C   . TYR C 312  ? 2.9124 1.6717 1.9533 0.6666  0.3586  0.6085  312  TYR B C   
16728 O O   . TYR C 312  ? 2.8791 1.6338 1.9480 0.6565  0.3907  0.6203  312  TYR B O   
16729 C CB  . TYR C 312  ? 3.6073 2.3104 2.4461 0.7534  0.4003  0.5652  312  TYR B CB  
16730 C CG  . TYR C 312  ? 3.7241 2.3843 2.4845 0.8121  0.4573  0.6010  312  TYR B CG  
16731 C CD1 . TYR C 312  ? 3.8157 2.4471 2.4493 0.8535  0.4532  0.5540  312  TYR B CD1 
16732 C CD2 . TYR C 312  ? 3.7475 2.3944 2.5597 0.8272  0.5156  0.6811  312  TYR B CD2 
16733 C CE1 . TYR C 312  ? 3.9160 2.5021 2.4657 0.9098  0.5064  0.5853  312  TYR B CE1 
16734 C CE2 . TYR C 312  ? 3.8418 2.4462 2.5776 0.8834  0.5732  0.7145  312  TYR B CE2 
16735 C CZ  . TYR C 312  ? 3.9213 2.4934 2.5208 0.9252  0.5686  0.6659  312  TYR B CZ  
16736 O OH  . TYR C 312  ? 4.0205 2.5449 2.5329 0.9835  0.6259  0.6978  312  TYR B OH  
16737 N N   . TYR C 313  ? 2.8428 1.6294 1.9267 0.6309  0.3044  0.5854  313  TYR B N   
16738 C CA  . TYR C 313  ? 2.7264 1.5373 1.8771 0.5781  0.2765  0.5626  313  TYR B CA  
16739 C C   . TYR C 313  ? 2.7198 1.5448 1.9839 0.5460  0.2695  0.6242  313  TYR B C   
16740 O O   . TYR C 313  ? 2.7175 1.5551 2.0210 0.5293  0.2310  0.6330  313  TYR B O   
16741 C CB  . TYR C 313  ? 2.5810 1.4110 1.7022 0.5564  0.2217  0.4885  313  TYR B CB  
16742 C CG  . TYR C 313  ? 2.5273 1.3476 1.5465 0.5862  0.2161  0.4266  313  TYR B CG  
16743 C CD1 . TYR C 313  ? 2.5339 1.3564 1.5090 0.6068  0.1853  0.4058  313  TYR B CD1 
16744 C CD2 . TYR C 313  ? 2.5134 1.3211 1.4823 0.5934  0.2384  0.3874  313  TYR B CD2 
16745 C CE1 . TYR C 313  ? 2.5687 1.3828 1.4512 0.6350  0.1742  0.3479  313  TYR B CE1 
16746 C CE2 . TYR C 313  ? 2.5470 1.3445 1.4236 0.6199  0.2273  0.3271  313  TYR B CE2 
16747 C CZ  . TYR C 313  ? 2.5737 1.3752 1.4069 0.6410  0.1937  0.3074  313  TYR B CZ  
16748 O OH  . TYR C 313  ? 2.6079 1.3997 1.3509 0.6684  0.1772  0.2478  313  TYR B OH  
16749 N N   . SER C 314  ? 2.7226 1.5442 2.0389 0.5369  0.3044  0.6634  314  SER B N   
16750 C CA  . SER C 314  ? 2.6718 1.5041 2.0996 0.5105  0.3029  0.7282  314  SER B CA  
16751 C C   . SER C 314  ? 2.5369 1.3841 2.0155 0.4630  0.2803  0.7089  314  SER B C   
16752 O O   . SER C 314  ? 2.4633 1.3256 2.0214 0.4297  0.2496  0.7345  314  SER B O   
16753 C CB  . SER C 314  ? 2.7751 1.5919 2.2336 0.5411  0.3641  0.7992  314  SER B CB  
16754 O OG  . SER C 314  ? 2.8542 1.6538 2.2483 0.5623  0.4051  0.7730  314  SER B OG  
16755 N N   . LEU C 315  ? 2.4903 1.3326 1.9228 0.4604  0.2963  0.6639  315  LEU B N   
16756 C CA  . LEU C 315  ? 2.4308 1.2849 1.8922 0.4170  0.2719  0.6334  315  LEU B CA  
16757 C C   . LEU C 315  ? 2.3067 1.1693 1.7031 0.4043  0.2334  0.5516  315  LEU B C   
16758 O O   . LEU C 315  ? 2.3230 1.1776 1.6415 0.4325  0.2425  0.5105  315  LEU B O   
16759 C CB  . LEU C 315  ? 2.5139 1.3567 1.9765 0.4196  0.3158  0.6384  315  LEU B CB  
16760 C CG  . LEU C 315  ? 2.5854 1.4246 2.1308 0.4190  0.3517  0.7123  315  LEU B CG  
16761 C CD1 . LEU C 315  ? 2.6245 1.4416 2.1318 0.4520  0.4124  0.7174  315  LEU B CD1 
16762 C CD2 . LEU C 315  ? 2.5233 1.3786 2.1426 0.3722  0.3250  0.7202  315  LEU B CD2 
16763 N N   . GLU C 316  ? 2.1826 1.0598 1.6104 0.3638  0.1906  0.5288  316  GLU B N   
16764 C CA  . GLU C 316  ? 2.1108 0.9981 1.4880 0.3490  0.1574  0.4528  316  GLU B CA  
16765 C C   . GLU C 316  ? 2.0531 0.9348 1.3849 0.3503  0.1823  0.4056  316  GLU B C   
16766 O O   . GLU C 316  ? 2.0377 0.9220 1.3090 0.3602  0.1738  0.3456  316  GLU B O   
16767 C CB  . GLU C 316  ? 2.1015 1.0004 1.5218 0.3059  0.1148  0.4433  316  GLU B CB  
16768 C CG  . GLU C 316  ? 2.1597 1.0703 1.5350 0.2915  0.0826  0.3685  316  GLU B CG  
16769 C CD  . GLU C 316  ? 2.2281 1.1411 1.5934 0.2645  0.0883  0.3245  316  GLU B CD  
16770 O OE1 . GLU C 316  ? 2.2470 1.1538 1.6521 0.2434  0.1004  0.3536  316  GLU B OE1 
16771 O OE2 . GLU C 316  ? 2.2500 1.1715 1.5708 0.2640  0.0798  0.2609  316  GLU B OE2 
16772 N N   . ASP C 317  ? 2.0422 0.9159 1.4098 0.3394  0.2112  0.4346  317  ASP B N   
16773 C CA  . ASP C 317  ? 2.0888 0.9490 1.4224 0.3486  0.2480  0.4097  317  ASP B CA  
16774 C C   . ASP C 317  ? 2.1623 1.0134 1.4134 0.3851  0.2571  0.3664  317  ASP B C   
16775 O O   . ASP C 317  ? 2.1407 0.9976 1.3477 0.3782  0.2388  0.2988  317  ASP B O   
16776 C CB  . ASP C 317  ? 2.1514 0.9975 1.5301 0.3618  0.2921  0.4786  317  ASP B CB  
16777 C CG  . ASP C 317  ? 2.2717 1.1038 1.6464 0.3560  0.3266  0.4654  317  ASP B CG  
16778 O OD1 . ASP C 317  ? 2.3321 1.1579 1.6504 0.3567  0.3293  0.4028  317  ASP B OD1 
16779 O OD2 . ASP C 317  ? 2.2824 1.1091 1.7158 0.3516  0.3516  0.5202  317  ASP B OD2 
16780 N N   . LEU C 318  ? 2.2615 1.0977 1.4956 0.4245  0.2854  0.4089  318  LEU B N   
16781 C CA  . LEU C 318  ? 2.3346 1.1570 1.4881 0.4680  0.2932  0.3868  318  LEU B CA  
16782 C C   . LEU C 318  ? 2.2947 1.1345 1.4167 0.4653  0.2446  0.3404  318  LEU B C   
16783 O O   . LEU C 318  ? 2.2824 1.1239 1.4028 0.4834  0.2328  0.3681  318  LEU B O   
16784 C CB  . LEU C 318  ? 2.3998 1.2088 1.5643 0.5030  0.3228  0.4588  318  LEU B CB  
16785 C CG  . LEU C 318  ? 2.4859 1.2710 1.6603 0.5293  0.3822  0.5131  318  LEU B CG  
16786 C CD1 . LEU C 318  ? 2.5229 1.3070 1.7422 0.5491  0.3984  0.5902  318  LEU B CD1 
16787 C CD2 . LEU C 318  ? 2.5878 1.3434 1.6639 0.5691  0.4119  0.4763  318  LEU B CD2 
16788 N N   . ASN C 319  ? 2.2463 1.0980 1.3456 0.4445  0.2186  0.2710  319  ASN B N   
16789 C CA  . ASN C 319  ? 2.1468 1.0183 1.2290 0.4387  0.1726  0.2279  319  ASN B CA  
16790 C C   . ASN C 319  ? 2.0509 0.9402 1.1415 0.4029  0.1490  0.1642  319  ASN B C   
16791 O O   . ASN C 319  ? 2.0087 0.9121 1.1519 0.3671  0.1322  0.1709  319  ASN B O   
16792 C CB  . ASN C 319  ? 2.1118 0.9954 1.2494 0.4258  0.1495  0.2742  319  ASN B CB  
16793 C CG  . ASN C 319  ? 2.1876 1.0808 1.2944 0.4423  0.1148  0.2521  319  ASN B CG  
16794 O OD1 . ASN C 319  ? 2.2427 1.1366 1.2888 0.4614  0.1045  0.1993  319  ASN B OD1 
16795 N ND2 . ASN C 319  ? 2.1881 1.0871 1.3374 0.4361  0.0946  0.2916  319  ASN B ND2 
16796 N N   . ASN C 320  ? 2.0286 0.9152 1.0686 0.4122  0.1484  0.1034  320  ASN B N   
16797 C CA  . ASN C 320  ? 1.9938 0.9007 1.0454 0.3801  0.1238  0.0397  320  ASN B CA  
16798 C C   . ASN C 320  ? 2.0336 0.9514 1.0365 0.3990  0.0939  -0.0197 320  ASN B C   
16799 O O   . ASN C 320  ? 2.0330 0.9603 1.0275 0.3862  0.0833  -0.0813 320  ASN B O   
16800 C CB  . ASN C 320  ? 2.0079 0.9050 1.0703 0.3601  0.1506  0.0205  320  ASN B CB  
16801 C CG  . ASN C 320  ? 2.0189 0.9128 1.1418 0.3316  0.1689  0.0724  320  ASN B CG  
16802 O OD1 . ASN C 320  ? 1.9876 0.8936 1.1481 0.2942  0.1590  0.0565  320  ASN B OD1 
16803 N ND2 . ASN C 320  ? 2.0541 0.9314 1.1882 0.3504  0.1953  0.1375  320  ASN B ND2 
16804 N N   . LYS C 321  ? 2.0652 0.9807 1.0412 0.4300  0.0808  0.0039  321  LYS B N   
16805 C CA  . LYS C 321  ? 2.1096 1.0348 1.0402 0.4550  0.0474  -0.0364 321  LYS B CA  
16806 C C   . LYS C 321  ? 2.0286 0.9790 0.9963 0.4396  0.0108  -0.0352 321  LYS B C   
16807 O O   . LYS C 321  ? 1.9873 0.9479 1.0114 0.4054  0.0083  -0.0168 321  LYS B O   
16808 C CB  . LYS C 321  ? 2.2441 1.1431 1.1140 0.5044  0.0625  -0.0022 321  LYS B CB  
16809 C CG  . LYS C 321  ? 2.3126 1.1946 1.2096 0.5119  0.0952  0.0801  321  LYS B CG  
16810 C CD  . LYS C 321  ? 2.4653 1.3136 1.2936 0.5627  0.1264  0.1099  321  LYS B CD  
16811 C CE  . LYS C 321  ? 2.5106 1.3331 1.3467 0.5671  0.1799  0.1521  321  LYS B CE  
16812 N NZ  . LYS C 321  ? 2.6067 1.3927 1.3659 0.6201  0.2127  0.1762  321  LYS B NZ  
16813 N N   . TYR C 322  ? 2.0252 0.9824 0.9584 0.4666  -0.0180 -0.0529 322  TYR B N   
16814 C CA  . TYR C 322  ? 1.9760 0.9586 0.9415 0.4521  -0.0564 -0.0688 322  TYR B CA  
16815 C C   . TYR C 322  ? 2.0029 0.9795 0.9858 0.4624  -0.0639 -0.0115 322  TYR B C   
16816 O O   . TYR C 322  ? 2.0620 1.0162 1.0215 0.4912  -0.0431 0.0387  322  TYR B O   
16817 C CB  . TYR C 322  ? 1.9694 0.9701 0.9020 0.4679  -0.0904 -0.1344 322  TYR B CB  
16818 C CG  . TYR C 322  ? 1.9618 0.9771 0.9077 0.4429  -0.0907 -0.1943 322  TYR B CG  
16819 C CD1 . TYR C 322  ? 1.9164 0.9632 0.8996 0.4186  -0.1185 -0.2447 322  TYR B CD1 
16820 C CD2 . TYR C 322  ? 2.0321 1.0280 0.9582 0.4427  -0.0594 -0.1980 322  TYR B CD2 
16821 C CE1 . TYR C 322  ? 1.9524 1.0129 0.9559 0.3943  -0.1153 -0.2968 322  TYR B CE1 
16822 C CE2 . TYR C 322  ? 2.0614 1.0681 1.0047 0.4183  -0.0578 -0.2513 322  TYR B CE2 
16823 C CZ  . TYR C 322  ? 2.0421 1.0819 1.0262 0.3934  -0.0856 -0.3000 322  TYR B CZ  
16824 O OH  . TYR C 322  ? 2.0702 1.1206 1.0781 0.3684  -0.0808 -0.3504 322  TYR B OH  
16825 N N   . LEU C 323  ? 1.9745 0.9690 1.0006 0.4386  -0.0920 -0.0185 323  LEU B N   
16826 C CA  . LEU C 323  ? 1.9982 0.9874 1.0411 0.4487  -0.1076 0.0251  323  LEU B CA  
16827 C C   . LEU C 323  ? 2.0507 1.0573 1.0779 0.4632  -0.1469 -0.0164 323  LEU B C   
16828 O O   . LEU C 323  ? 2.0293 1.0584 1.0776 0.4404  -0.1681 -0.0662 323  LEU B O   
16829 C CB  . LEU C 323  ? 1.9522 0.9414 1.0582 0.4103  -0.1100 0.0559  323  LEU B CB  
16830 C CG  . LEU C 323  ? 1.9469 0.9261 1.0785 0.4173  -0.1257 0.1051  323  LEU B CG  
16831 C CD1 . LEU C 323  ? 1.9285 0.9220 1.0571 0.4212  -0.1647 0.0680  323  LEU B CD1 
16832 C CD2 . LEU C 323  ? 2.0002 0.9598 1.1029 0.4569  -0.1034 0.1539  323  LEU B CD2 
16833 N N   . TYR C 324  ? 2.1290 1.1247 1.1208 0.5021  -0.1547 0.0057  324  TYR B N   
16834 C CA  . TYR C 324  ? 2.2005 1.2109 1.1725 0.5225  -0.1923 -0.0312 324  TYR B CA  
16835 C C   . TYR C 324  ? 2.1841 1.1920 1.1907 0.5206  -0.2134 0.0006  324  TYR B C   
16836 O O   . TYR C 324  ? 2.1909 1.1764 1.2023 0.5342  -0.1997 0.0626  324  TYR B O   
16837 C CB  . TYR C 324  ? 2.3164 1.3138 1.2147 0.5715  -0.1915 -0.0346 324  TYR B CB  
16838 C CG  . TYR C 324  ? 2.4116 1.4174 1.2854 0.6012  -0.2293 -0.0547 324  TYR B CG  
16839 C CD1 . TYR C 324  ? 2.4606 1.4878 1.3088 0.6118  -0.2586 -0.1212 324  TYR B CD1 
16840 C CD2 . TYR C 324  ? 2.4381 1.4298 1.3174 0.6199  -0.2364 -0.0061 324  TYR B CD2 
16841 C CE1 . TYR C 324  ? 2.4946 1.5304 1.3223 0.6410  -0.2953 -0.1391 324  TYR B CE1 
16842 C CE2 . TYR C 324  ? 2.4766 1.4744 1.3324 0.6492  -0.2711 -0.0236 324  TYR B CE2 
16843 C CZ  . TYR C 324  ? 2.4899 1.5103 1.3192 0.6600  -0.3007 -0.0900 324  TYR B CZ  
16844 O OH  . TYR C 324  ? 2.5036 1.5314 1.3126 0.6898  -0.3367 -0.1076 324  TYR B OH  
16845 N N   . ILE C 325  ? 2.1511 1.1809 1.1836 0.5052  -0.2457 -0.0424 325  ILE B N   
16846 C CA  . ILE C 325  ? 2.0840 1.1098 1.1496 0.5016  -0.2690 -0.0214 325  ILE B CA  
16847 C C   . ILE C 325  ? 2.0943 1.1359 1.1410 0.5270  -0.3028 -0.0607 325  ILE B C   
16848 O O   . ILE C 325  ? 2.0942 1.1609 1.1318 0.5263  -0.3165 -0.1205 325  ILE B O   
16849 C CB  . ILE C 325  ? 2.0281 1.0610 1.1478 0.4568  -0.2772 -0.0343 325  ILE B CB  
16850 C CG1 . ILE C 325  ? 1.9949 1.0265 1.1294 0.4251  -0.2490 -0.0312 325  ILE B CG1 
16851 C CG2 . ILE C 325  ? 1.9950 1.0075 1.1487 0.4511  -0.2892 0.0136  325  ILE B CG2 
16852 C CD1 . ILE C 325  ? 1.9523 0.9845 1.1307 0.3834  -0.2564 -0.0385 325  ILE B CD1 
16853 N N   . ALA C 326  ? 2.1181 1.1448 1.1649 0.5490  -0.3168 -0.0255 326  ALA B N   
16854 C CA  . ALA C 326  ? 2.1201 1.1577 1.1490 0.5781  -0.3497 -0.0537 326  ALA B CA  
16855 C C   . ALA C 326  ? 2.1329 1.1517 1.1881 0.5848  -0.3644 -0.0122 326  ALA B C   
16856 O O   . ALA C 326  ? 2.1292 1.1207 1.1774 0.6016  -0.3495 0.0488  326  ALA B O   
16857 C CB  . ALA C 326  ? 2.1645 1.1983 1.1262 0.6222  -0.3483 -0.0579 326  ALA B CB  
16858 N N   . VAL C 327  ? 2.1179 1.1504 1.2067 0.5710  -0.3922 -0.0463 327  VAL B N   
16859 C CA  . VAL C 327  ? 2.1129 1.1267 1.2323 0.5718  -0.4093 -0.0167 327  VAL B CA  
16860 C C   . VAL C 327  ? 2.1972 1.2145 1.2907 0.6134  -0.4349 -0.0272 327  VAL B C   
16861 O O   . VAL C 327  ? 2.2182 1.2608 1.2841 0.6309  -0.4478 -0.0750 327  VAL B O   
16862 C CB  . VAL C 327  ? 2.0555 1.0787 1.2205 0.5348  -0.4242 -0.0523 327  VAL B CB  
16863 C CG1 . VAL C 327  ? 2.0426 1.0381 1.2418 0.5298  -0.4408 -0.0183 327  VAL B CG1 
16864 C CG2 . VAL C 327  ? 1.9775 1.0046 1.1574 0.4957  -0.4012 -0.0587 327  VAL B CG2 
16865 N N   . THR C 328  ? 2.2309 1.2221 1.3366 0.6287  -0.4438 0.0178  328  THR B N   
16866 C CA  . THR C 328  ? 2.2921 1.2840 1.3876 0.6626  -0.4735 0.0071  328  THR B CA  
16867 C C   . THR C 328  ? 2.2699 1.2437 1.4166 0.6472  -0.4919 0.0203  328  THR B C   
16868 O O   . THR C 328  ? 2.2363 1.1786 1.4058 0.6404  -0.4825 0.0763  328  THR B O   
16869 C CB  . THR C 328  ? 2.3581 1.3303 1.4020 0.7103  -0.4671 0.0507  328  THR B CB  
16870 O OG1 . THR C 328  ? 2.4193 1.4015 1.4091 0.7248  -0.4493 0.0386  328  THR B OG1 
16871 C CG2 . THR C 328  ? 2.3854 1.3627 1.4154 0.7457  -0.5010 0.0309  328  THR B CG2 
16872 N N   . VAL C 329  ? 2.3035 1.2969 1.4707 0.6416  -0.5177 -0.0330 329  VAL B N   
16873 C CA  . VAL C 329  ? 2.3154 1.2919 1.5274 0.6249  -0.5360 -0.0343 329  VAL B CA  
16874 C C   . VAL C 329  ? 2.4507 1.4228 1.6589 0.6623  -0.5625 -0.0362 329  VAL B C   
16875 O O   . VAL C 329  ? 2.4961 1.4976 1.7007 0.6767  -0.5813 -0.0877 329  VAL B O   
16876 C CB  . VAL C 329  ? 2.2189 1.2197 1.4557 0.5949  -0.5432 -0.0970 329  VAL B CB  
16877 C CG1 . VAL C 329  ? 2.1596 1.1349 1.4348 0.5769  -0.5596 -0.0975 329  VAL B CG1 
16878 C CG2 . VAL C 329  ? 2.1752 1.1880 1.4093 0.5611  -0.5175 -0.1071 329  VAL B CG2 
16879 N N   . ILE C 330  ? 2.5241 1.4603 1.7381 0.6785  -0.5643 0.0204  330  ILE B N   
16880 C CA  . ILE C 330  ? 2.6289 1.5561 1.8403 0.7157  -0.5893 0.0240  330  ILE B CA  
16881 C C   . ILE C 330  ? 2.7093 1.6161 1.9696 0.6996  -0.6102 0.0142  330  ILE B C   
16882 O O   . ILE C 330  ? 2.6729 1.5447 1.9646 0.6767  -0.6061 0.0516  330  ILE B O   
16883 C CB  . ILE C 330  ? 2.8118 1.7119 1.9914 0.7537  -0.5791 0.0893  330  ILE B CB  
16884 C CG1 . ILE C 330  ? 2.8093 1.6727 2.0170 0.7330  -0.5563 0.1556  330  ILE B CG1 
16885 C CG2 . ILE C 330  ? 2.8258 1.7463 1.9426 0.7809  -0.5658 0.0840  330  ILE B CG2 
16886 C CD1 . ILE C 330  ? 2.8596 1.6990 2.0350 0.7691  -0.5357 0.2221  330  ILE B CD1 
16887 N N   . GLU C 331  ? 2.8341 1.7621 2.1023 0.7118  -0.6335 -0.0380 331  GLU B N   
16888 C CA  . GLU C 331  ? 2.9466 1.8570 2.2561 0.6962  -0.6510 -0.0585 331  GLU B CA  
16889 C C   . GLU C 331  ? 3.0869 1.9512 2.4137 0.7120  -0.6621 -0.0068 331  GLU B C   
16890 O O   . GLU C 331  ? 3.1349 1.9940 2.4423 0.7516  -0.6688 0.0204  331  GLU B O   
16891 C CB  . GLU C 331  ? 2.9511 1.8956 2.2678 0.7129  -0.6709 -0.1209 331  GLU B CB  
16892 C CG  . GLU C 331  ? 2.9667 1.8867 2.3198 0.7107  -0.6897 -0.1350 331  GLU B CG  
16893 C CD  . GLU C 331  ? 2.9835 1.9319 2.3447 0.7439  -0.7116 -0.1772 331  GLU B CD  
16894 O OE1 . GLU C 331  ? 2.9765 1.9686 2.3194 0.7598  -0.7126 -0.2044 331  GLU B OE1 
16895 O OE2 . GLU C 331  ? 3.0043 1.9310 2.3919 0.7547  -0.7289 -0.1836 331  GLU B OE2 
16896 N N   . SER C 332  ? 3.1694 1.9979 2.5317 0.6812  -0.6655 0.0060  332  SER B N   
16897 C CA  . SER C 332  ? 3.2982 2.0779 2.6861 0.6891  -0.6752 0.0585  332  SER B CA  
16898 C C   . SER C 332  ? 3.4075 2.1754 2.8072 0.7203  -0.7009 0.0435  332  SER B C   
16899 O O   . SER C 332  ? 3.4419 2.1832 2.8452 0.7482  -0.7065 0.0894  332  SER B O   
16900 C CB  . SER C 332  ? 3.3101 2.0530 2.7340 0.6451  -0.6765 0.0721  332  SER B CB  
16901 O OG  . SER C 332  ? 3.3637 2.0591 2.8191 0.6506  -0.6859 0.1266  332  SER B OG  
16902 N N   . THR C 333  ? 3.4690 2.2553 2.8769 0.7161  -0.7145 -0.0190 333  THR B N   
16903 C CA  . THR C 333  ? 3.5542 2.3312 2.9778 0.7455  -0.7384 -0.0381 333  THR B CA  
16904 C C   . THR C 333  ? 3.5947 2.3984 2.9928 0.7952  -0.7463 -0.0329 333  THR B C   
16905 O O   . THR C 333  ? 3.6443 2.4200 3.0415 0.8245  -0.7541 0.0121  333  THR B O   
16906 C CB  . THR C 333  ? 3.5530 2.3444 2.9939 0.7301  -0.7466 -0.1071 333  THR B CB  
16907 O OG1 . THR C 333  ? 3.5648 2.3945 3.0040 0.7658  -0.7592 -0.1454 333  THR B OG1 
16908 C CG2 . THR C 333  ? 3.5102 2.3272 2.9407 0.6915  -0.7268 -0.1377 333  THR B CG2 
16909 N N   . GLY C 334  ? 3.5692 2.4252 2.9466 0.8047  -0.7455 -0.0781 334  GLY B N   
16910 C CA  . GLY C 334  ? 3.5819 2.4646 2.9325 0.8517  -0.7592 -0.0805 334  GLY B CA  
16911 C C   . GLY C 334  ? 3.5655 2.4403 2.8693 0.8744  -0.7468 -0.0252 334  GLY B C   
16912 O O   . GLY C 334  ? 3.6514 2.5264 2.9282 0.9188  -0.7602 -0.0078 334  GLY B O   
16913 N N   . GLY C 335  ? 3.4528 2.3187 2.7448 0.8458  -0.7202 0.0034  335  GLY B N   
16914 C CA  . GLY C 335  ? 3.3851 2.2438 2.6307 0.8656  -0.7016 0.0541  335  GLY B CA  
16915 C C   . GLY C 335  ? 3.3049 2.2080 2.5031 0.8782  -0.6980 0.0202  335  GLY B C   
16916 O O   . GLY C 335  ? 3.3664 2.2650 2.5133 0.9032  -0.6852 0.0539  335  GLY B O   
16917 N N   . PHE C 336  ? 3.1212 2.0649 2.3368 0.8613  -0.7085 -0.0468 336  PHE B N   
16918 C CA  . PHE C 336  ? 2.9967 1.9844 2.1784 0.8688  -0.7090 -0.0871 336  PHE B CA  
16919 C C   . PHE C 336  ? 2.8875 1.8693 2.0353 0.8515  -0.6772 -0.0585 336  PHE B C   
16920 O O   . PHE C 336  ? 2.8876 1.8323 2.0286 0.8485  -0.6570 0.0013  336  PHE B O   
16921 C CB  . PHE C 336  ? 2.8803 1.9083 2.1025 0.8404  -0.7160 -0.1576 336  PHE B CB  
16922 C CG  . PHE C 336  ? 2.8031 1.8562 2.0523 0.8656  -0.7480 -0.2013 336  PHE B CG  
16923 C CD1 . PHE C 336  ? 2.7374 1.7909 2.0411 0.8465  -0.7539 -0.2324 336  PHE B CD1 
16924 C CD2 . PHE C 336  ? 2.8149 1.8904 2.0344 0.9089  -0.7724 -0.2127 336  PHE B CD2 
16925 C CE1 . PHE C 336  ? 2.7258 1.8039 2.0605 0.8701  -0.7802 -0.2725 336  PHE B CE1 
16926 C CE2 . PHE C 336  ? 2.8105 1.9121 2.0627 0.9318  -0.8031 -0.2526 336  PHE B CE2 
16927 C CZ  . PHE C 336  ? 2.7716 1.8757 2.0847 0.9122  -0.8053 -0.2819 336  PHE B CZ  
16928 N N   . SER C 337  ? 2.7847 1.8035 1.9162 0.8403  -0.6722 -0.1017 337  SER B N   
16929 C CA  . SER C 337  ? 2.7065 1.7226 1.8152 0.8165  -0.6401 -0.0844 337  SER B CA  
16930 C C   . SER C 337  ? 2.6594 1.7186 1.7650 0.7988  -0.6386 -0.1441 337  SER B C   
16931 O O   . SER C 337  ? 2.6810 1.7724 1.7760 0.8208  -0.6624 -0.1888 337  SER B O   
16932 C CB  . SER C 337  ? 2.6966 1.6867 1.7442 0.8493  -0.6243 -0.0286 337  SER B CB  
16933 O OG  . SER C 337  ? 2.6271 1.6181 1.6533 0.8282  -0.5926 -0.0183 337  SER B OG  
16934 N N   . GLU C 338  ? 2.6218 1.6806 1.7397 0.7588  -0.6110 -0.1425 338  GLU B N   
16935 C CA  . GLU C 338  ? 2.5938 1.6896 1.7175 0.7354  -0.6049 -0.1962 338  GLU B CA  
16936 C C   . GLU C 338  ? 2.5486 1.6325 1.6502 0.7131  -0.5704 -0.1699 338  GLU B C   
16937 O O   . GLU C 338  ? 2.5189 1.5736 1.6350 0.6919  -0.5502 -0.1250 338  GLU B O   
16938 C CB  . GLU C 338  ? 2.5948 1.7084 1.7776 0.7013  -0.6096 -0.2395 338  GLU B CB  
16939 C CG  . GLU C 338  ? 2.6314 1.7923 1.8303 0.6927  -0.6163 -0.3065 338  GLU B CG  
16940 C CD  . GLU C 338  ? 2.7254 1.9109 1.8980 0.7349  -0.6444 -0.3301 338  GLU B CD  
16941 O OE1 . GLU C 338  ? 2.7554 1.9356 1.9284 0.7678  -0.6706 -0.3226 338  GLU B OE1 
16942 O OE2 . GLU C 338  ? 2.7604 1.9685 1.9111 0.7355  -0.6420 -0.3565 338  GLU B OE2 
16943 N N   . GLU C 339  ? 2.5626 1.6686 1.6311 0.7192  -0.5656 -0.1980 339  GLU B N   
16944 C CA  . GLU C 339  ? 2.5557 1.6527 1.5996 0.7019  -0.5325 -0.1792 339  GLU B CA  
16945 C C   . GLU C 339  ? 2.4454 1.5746 1.5172 0.6660  -0.5252 -0.2340 339  GLU B C   
16946 O O   . GLU C 339  ? 2.3863 1.5496 1.4827 0.6657  -0.5474 -0.2901 339  GLU B O   
16947 C CB  . GLU C 339  ? 2.7161 1.8032 1.6884 0.7419  -0.5295 -0.1633 339  GLU B CB  
16948 C CG  . GLU C 339  ? 2.8680 1.9141 1.8062 0.7723  -0.5185 -0.0926 339  GLU B CG  
16949 C CD  . GLU C 339  ? 3.0483 2.0869 1.9154 0.8266  -0.5355 -0.0895 339  GLU B CD  
16950 O OE1 . GLU C 339  ? 3.1144 2.1693 1.9397 0.8390  -0.5428 -0.1286 339  GLU B OE1 
16951 O OE2 . GLU C 339  ? 3.1258 2.1395 1.9773 0.8574  -0.5430 -0.0478 339  GLU B OE2 
16952 N N   . ALA C 340  ? 2.3959 1.5142 1.4682 0.6365  -0.4928 -0.2150 340  ALA B N   
16953 C CA  . ALA C 340  ? 2.3658 1.5079 1.4600 0.6011  -0.4784 -0.2574 340  ALA B CA  
16954 C C   . ALA C 340  ? 2.3235 1.4468 1.3917 0.5892  -0.4438 -0.2246 340  ALA B C   
16955 O O   . ALA C 340  ? 2.3414 1.4332 1.3993 0.5931  -0.4274 -0.1654 340  ALA B O   
16956 C CB  . ALA C 340  ? 2.3358 1.4829 1.4858 0.5629  -0.4768 -0.2725 340  ALA B CB  
16957 N N   . GLU C 341  ? 2.3108 1.4530 1.3747 0.5740  -0.4318 -0.2619 341  GLU B N   
16958 C CA  . GLU C 341  ? 2.3256 1.4499 1.3669 0.5623  -0.3970 -0.2340 341  GLU B CA  
16959 C C   . GLU C 341  ? 2.0016 1.1431 1.0717 0.5220  -0.3781 -0.2697 341  GLU B C   
16960 O O   . GLU C 341  ? 2.0010 1.1734 1.0975 0.5101  -0.3919 -0.3263 341  GLU B O   
16961 C CB  . GLU C 341  ? 2.4071 1.5208 1.3820 0.6020  -0.3951 -0.2278 341  GLU B CB  
16962 C CG  . GLU C 341  ? 2.4584 1.6011 1.4168 0.6188  -0.4229 -0.2927 341  GLU B CG  
16963 C CD  . GLU C 341  ? 2.5342 1.6633 1.4262 0.6442  -0.4137 -0.2974 341  GLU B CD  
16964 O OE1 . GLU C 341  ? 2.5584 1.6552 1.4147 0.6520  -0.3821 -0.2479 341  GLU B OE1 
16965 O OE2 . GLU C 341  ? 2.5697 1.7196 1.4467 0.6570  -0.4388 -0.3512 341  GLU B OE2 
16966 N N   . ILE C 342  ? 1.9709 1.0926 1.0404 0.5013  -0.3456 -0.2346 342  ILE B N   
16967 C CA  . ILE C 342  ? 1.9138 1.0462 0.9970 0.4708  -0.3239 -0.2628 342  ILE B CA  
16968 C C   . ILE C 342  ? 1.9706 1.0889 1.0059 0.4898  -0.3036 -0.2515 342  ILE B C   
16969 O O   . ILE C 342  ? 2.0085 1.0984 1.0202 0.5025  -0.2834 -0.1959 342  ILE B O   
16970 C CB  . ILE C 342  ? 1.8250 0.9431 0.9422 0.4327  -0.3015 -0.2317 342  ILE B CB  
16971 C CG1 . ILE C 342  ? 1.8047 0.9328 0.9637 0.4106  -0.3191 -0.2501 342  ILE B CG1 
16972 C CG2 . ILE C 342  ? 1.7473 0.8705 0.8703 0.4068  -0.2750 -0.2514 342  ILE B CG2 
16973 C CD1 . ILE C 342  ? 1.7922 0.8963 0.9756 0.3805  -0.3066 -0.2085 342  ILE B CD1 
16974 N N   . PRO C 343  ? 1.9933 1.1297 1.0171 0.4908  -0.3072 -0.3041 343  PRO B N   
16975 C CA  . PRO C 343  ? 2.0220 1.1417 0.9875 0.5178  -0.2956 -0.3023 343  PRO B CA  
16976 C C   . PRO C 343  ? 2.0352 1.1264 0.9933 0.5056  -0.2539 -0.2526 343  PRO B C   
16977 O O   . PRO C 343  ? 2.0805 1.1433 0.9960 0.5331  -0.2375 -0.2059 343  PRO B O   
16978 C CB  . PRO C 343  ? 2.0143 1.1597 0.9915 0.5049  -0.3048 -0.3714 343  PRO B CB  
16979 C CG  . PRO C 343  ? 1.9744 1.1533 1.0177 0.4751  -0.3209 -0.4071 343  PRO B CG  
16980 C CD  . PRO C 343  ? 1.9420 1.1083 1.0121 0.4577  -0.3101 -0.3596 343  PRO B CD  
16981 N N   . GLY C 344  ? 2.0356 1.1343 1.0383 0.4644  -0.2355 -0.2613 344  GLY B N   
16982 C CA  . GLY C 344  ? 2.0378 1.1131 1.0443 0.4481  -0.1972 -0.2176 344  GLY B CA  
16983 C C   . GLY C 344  ? 1.8751 0.9598 0.9375 0.4012  -0.1860 -0.2227 344  GLY B C   
16984 O O   . GLY C 344  ? 1.8667 0.9762 0.9599 0.3813  -0.2027 -0.2681 344  GLY B O   
16985 N N   . ILE C 345  ? 1.7988 0.8626 0.8731 0.3855  -0.1567 -0.1749 345  ILE B N   
16986 C CA  . ILE C 345  ? 1.7385 0.8034 0.8584 0.3440  -0.1460 -0.1671 345  ILE B CA  
16987 C C   . ILE C 345  ? 1.7456 0.7898 0.8581 0.3401  -0.1096 -0.1352 345  ILE B C   
16988 O O   . ILE C 345  ? 1.7871 0.8106 0.8895 0.3574  -0.0954 -0.0802 345  ILE B O   
16989 C CB  . ILE C 345  ? 1.6937 0.7475 0.8390 0.3366  -0.1578 -0.1189 345  ILE B CB  
16990 C CG1 . ILE C 345  ? 1.5848 0.6555 0.7422 0.3368  -0.1921 -0.1494 345  ILE B CG1 
16991 C CG2 . ILE C 345  ? 1.6960 0.7401 0.8768 0.2992  -0.1444 -0.0959 345  ILE B CG2 
16992 C CD1 . ILE C 345  ? 1.4967 0.5529 0.6812 0.3233  -0.2044 -0.1099 345  ILE B CD1 
16993 N N   . LYS C 346  ? 1.6822 0.7311 0.8021 0.3196  -0.0923 -0.1678 346  LYS B N   
16994 C CA  . LYS C 346  ? 1.5833 0.6111 0.6914 0.3212  -0.0567 -0.1425 346  LYS B CA  
16995 C C   . LYS C 346  ? 1.5353 0.5456 0.6747 0.3042  -0.0393 -0.0776 346  LYS B C   
16996 O O   . LYS C 346  ? 1.6462 0.6620 0.8206 0.2749  -0.0500 -0.0733 346  LYS B O   
16997 C CB  . LYS C 346  ? 1.5671 0.6027 0.6837 0.2994  -0.0436 -0.1924 346  LYS B CB  
16998 C CG  . LYS C 346  ? 1.6419 0.6546 0.7370 0.3080  -0.0091 -0.1802 346  LYS B CG  
16999 C CD  . LYS C 346  ? 1.6897 0.7074 0.8030 0.2810  0.0053  -0.2260 346  LYS B CD  
17000 C CE  . LYS C 346  ? 1.7413 0.7776 0.8401 0.2894  -0.0158 -0.2974 346  LYS B CE  
17001 N NZ  . LYS C 346  ? 1.7662 0.7961 0.8726 0.2736  0.0050  -0.3341 346  LYS B NZ  
17002 N N   . TYR C 347  ? 1.6132 0.6016 0.7413 0.3231  -0.0137 -0.0265 347  TYR B N   
17003 C CA  . TYR C 347  ? 1.6204 0.5945 0.7886 0.3042  0.0041  0.0333  347  TYR B CA  
17004 C C   . TYR C 347  ? 1.6173 0.5864 0.7977 0.2803  0.0303  0.0199  347  TYR B C   
17005 O O   . TYR C 347  ? 1.6214 0.5893 0.7732 0.2896  0.0446  -0.0182 347  TYR B O   
17006 C CB  . TYR C 347  ? 1.6245 0.5786 0.7866 0.3337  0.0259  0.0974  347  TYR B CB  
17007 C CG  . TYR C 347  ? 1.6613 0.6145 0.8400 0.3449  0.0050  0.1389  347  TYR B CG  
17008 C CD1 . TYR C 347  ? 1.6499 0.5992 0.8835 0.3210  -0.0030 0.1858  347  TYR B CD1 
17009 C CD2 . TYR C 347  ? 1.7110 0.6649 0.8506 0.3802  -0.0085 0.1318  347  TYR B CD2 
17010 C CE1 . TYR C 347  ? 1.6649 0.6110 0.9190 0.3299  -0.0239 0.2233  347  TYR B CE1 
17011 C CE2 . TYR C 347  ? 1.7141 0.6649 0.8717 0.3906  -0.0264 0.1712  347  TYR B CE2 
17012 C CZ  . TYR C 347  ? 1.7069 0.6538 0.9243 0.3645  -0.0339 0.2163  347  TYR B CZ  
17013 O OH  . TYR C 347  ? 1.7272 0.6690 0.9684 0.3723  -0.0539 0.2538  347  TYR B OH  
17014 N N   . VAL C 348  ? 1.6432 0.6071 0.8651 0.2501  0.0354  0.0507  348  VAL B N   
17015 C CA  . VAL C 348  ? 1.6977 0.6542 0.9317 0.2283  0.0620  0.0428  348  VAL B CA  
17016 C C   . VAL C 348  ? 1.7025 0.6422 0.9739 0.2164  0.0810  0.1070  348  VAL B C   
17017 O O   . VAL C 348  ? 1.7119 0.6508 1.0152 0.2003  0.0620  0.1413  348  VAL B O   
17018 C CB  . VAL C 348  ? 1.7619 0.7322 1.0071 0.1948  0.0488  -0.0076 348  VAL B CB  
17019 C CG1 . VAL C 348  ? 1.7530 0.7113 1.0181 0.1691  0.0763  -0.0012 348  VAL B CG1 
17020 C CG2 . VAL C 348  ? 1.7827 0.7705 1.0009 0.2050  0.0391  -0.0748 348  VAL B CG2 
17021 N N   . LEU C 349  ? 1.7104 0.6356 0.9796 0.2242  0.1169  0.1221  349  LEU B N   
17022 C CA  . LEU C 349  ? 1.7170 0.6285 1.0287 0.2105  0.1353  0.1796  349  LEU B CA  
17023 C C   . LEU C 349  ? 1.6308 0.5435 0.9666 0.1703  0.1267  0.1664  349  LEU B C   
17024 O O   . LEU C 349  ? 1.5974 0.5073 0.9663 0.1505  0.1095  0.2021  349  LEU B O   
17025 C CB  . LEU C 349  ? 1.7899 0.6838 1.0921 0.2307  0.1790  0.1960  349  LEU B CB  
17026 C CG  . LEU C 349  ? 1.8012 0.6809 1.1482 0.2328  0.2044  0.2683  349  LEU B CG  
17027 C CD1 . LEU C 349  ? 1.8031 0.6723 1.1722 0.2094  0.2265  0.2690  349  LEU B CD1 
17028 C CD2 . LEU C 349  ? 1.7784 0.6648 1.1720 0.2230  0.1773  0.3209  349  LEU B CD2 
17029 N N   . SER C 350  ? 1.3158 0.8443 0.7935 0.2836  0.1244  0.1227  350  SER B N   
17030 C CA  . SER C 350  ? 1.2882 0.8254 0.7718 0.2822  0.1328  0.1143  350  SER B CA  
17031 C C   . SER C 350  ? 1.2951 0.8458 0.7723 0.2837  0.1283  0.0870  350  SER B C   
17032 O O   . SER C 350  ? 1.3407 0.8954 0.8069 0.2816  0.1351  0.0746  350  SER B O   
17033 C CB  . SER C 350  ? 1.2929 0.8275 0.7733 0.2773  0.1617  0.1229  350  SER B CB  
17034 O OG  . SER C 350  ? 1.2955 0.8383 0.7771 0.2748  0.1722  0.1115  350  SER B OG  
17035 N N   . PRO C 351  ? 1.2626 0.8219 0.7467 0.2874  0.1173  0.0774  351  PRO B N   
17036 C CA  . PRO C 351  ? 1.2582 0.8338 0.7385 0.2911  0.1098  0.0524  351  PRO B CA  
17037 C C   . PRO C 351  ? 1.2810 0.8704 0.7574 0.2841  0.1316  0.0397  351  PRO B C   
17038 O O   . PRO C 351  ? 1.3147 0.9224 0.7912 0.2861  0.1269  0.0199  351  PRO B O   
17039 C CB  . PRO C 351  ? 1.2416 0.8206 0.7285 0.2988  0.0926  0.0475  351  PRO B CB  
17040 C CG  . PRO C 351  ? 1.2246 0.7851 0.7186 0.2980  0.0853  0.0713  351  PRO B CG  
17041 C CD  . PRO C 351  ? 1.2264 0.7821 0.7210 0.2897  0.1086  0.0875  351  PRO B CD  
17042 N N   . TYR C 352  ? 1.2667 0.8481 0.7406 0.2763  0.1543  0.0508  352  TYR B N   
17043 C CA  . TYR C 352  ? 1.2837 0.8729 0.7515 0.2677  0.1741  0.0390  352  TYR B CA  
17044 C C   . TYR C 352  ? 1.2944 0.8700 0.7493 0.2627  0.1853  0.0426  352  TYR B C   
17045 O O   . TYR C 352  ? 1.2658 0.8271 0.7177 0.2662  0.1819  0.0576  352  TYR B O   
17046 C CB  . TYR C 352  ? 1.3396 0.9278 0.8105 0.2628  0.1927  0.0456  352  TYR B CB  
17047 C CG  . TYR C 352  ? 1.3475 0.9457 0.8274 0.2684  0.1834  0.0453  352  TYR B CG  
17048 C CD1 . TYR C 352  ? 1.3487 0.9682 0.8304 0.2689  0.1818  0.0276  352  TYR B CD1 
17049 C CD2 . TYR C 352  ? 1.3604 0.9474 0.8464 0.2731  0.1764  0.0632  352  TYR B CD2 
17050 C CE1 . TYR C 352  ? 1.3560 0.9834 0.8417 0.2755  0.1737  0.0266  352  TYR B CE1 
17051 C CE2 . TYR C 352  ? 1.3704 0.9638 0.8609 0.2784  0.1663  0.0620  352  TYR B CE2 
17052 C CZ  . TYR C 352  ? 1.3750 0.9874 0.8634 0.2803  0.1653  0.0433  352  TYR B CZ  
17053 O OH  . TYR C 352  ? 1.3934 1.0108 0.8824 0.2872  0.1555  0.0416  352  TYR B OH  
17054 N N   . LYS C 353  ? 1.3482 0.9279 0.7949 0.2542  0.1984  0.0292  353  LYS B N   
17055 C CA  . LYS C 353  ? 1.3825 0.9457 0.8123 0.2489  0.2112  0.0306  353  LYS B CA  
17056 C C   . LYS C 353  ? 1.3196 0.8790 0.7425 0.2376  0.2322  0.0229  353  LYS B C   
17057 O O   . LYS C 353  ? 1.2521 0.8285 0.6782 0.2302  0.2310  0.0054  353  LYS B O   
17058 C CB  . LYS C 353  ? 1.4741 1.0429 0.8955 0.2505  0.1958  0.0182  353  LYS B CB  
17059 C CG  . LYS C 353  ? 1.5544 1.1500 0.9884 0.2537  0.1765  0.0010  353  LYS B CG  
17060 C CD  . LYS C 353  ? 1.6242 1.2234 1.0548 0.2619  0.1538  -0.0036 353  LYS B CD  
17061 C CE  . LYS C 353  ? 1.6739 1.2827 1.0947 0.2562  0.1510  -0.0211 353  LYS B CE  
17062 N NZ  . LYS C 353  ? 1.7087 1.3181 1.1238 0.2650  0.1293  -0.0231 353  LYS B NZ  
17063 N N   . LEU C 354  ? 1.3200 0.8571 0.7347 0.2365  0.2513  0.0371  354  LEU B N   
17064 C CA  . LEU C 354  ? 1.3379 0.8627 0.7429 0.2265  0.2722  0.0328  354  LEU B CA  
17065 C C   . LEU C 354  ? 1.3336 0.8449 0.7175 0.2199  0.2767  0.0209  354  LEU B C   
17066 O O   . LEU C 354  ? 1.3553 0.8560 0.7265 0.2258  0.2726  0.0248  354  LEU B O   
17067 C CB  . LEU C 354  ? 1.3599 0.8626 0.7617 0.2305  0.2908  0.0530  354  LEU B CB  
17068 C CG  . LEU C 354  ? 1.3459 0.8512 0.7636 0.2399  0.2885  0.0737  354  LEU B CG  
17069 C CD1 . LEU C 354  ? 1.3468 0.8707 0.7791 0.2372  0.2828  0.0685  354  LEU B CD1 
17070 C CD2 . LEU C 354  ? 1.3064 0.8167 0.7298 0.2487  0.2715  0.0827  354  LEU B CD2 
17071 N N   . ASN C 355  ? 1.3085 0.8180 0.6871 0.2072  0.2859  0.0077  355  ASN B N   
17072 C CA  . ASN C 355  ? 1.3773 0.8682 0.7332 0.1992  0.2916  -0.0035 355  ASN B CA  
17073 C C   . ASN C 355  ? 1.3498 0.8302 0.7017 0.1851  0.3068  -0.0103 355  ASN B C   
17074 O O   . ASN C 355  ? 1.3059 0.8092 0.6744 0.1762  0.3037  -0.0183 355  ASN B O   
17075 C CB  . ASN C 355  ? 1.4703 0.9810 0.8258 0.1957  0.2719  -0.0211 355  ASN B CB  
17076 C CG  . ASN C 355  ? 1.5322 1.0776 0.9105 0.1888  0.2617  -0.0338 355  ASN B CG  
17077 O OD1 . ASN C 355  ? 1.5390 1.1076 0.9358 0.1977  0.2493  -0.0309 355  ASN B OD1 
17078 N ND2 . ASN C 355  ? 1.5581 1.1079 0.9349 0.1728  0.2661  -0.0481 355  ASN B ND2 
17079 N N   . LEU C 356  ? 1.3606 0.8054 0.6896 0.1835  0.3237  -0.0066 356  LEU B N   
17080 C CA  . LEU C 356  ? 1.3687 0.7949 0.6903 0.1700  0.3391  -0.0115 356  LEU B CA  
17081 C C   . LEU C 356  ? 1.4257 0.8710 0.7522 0.1525  0.3283  -0.0323 356  LEU B C   
17082 O O   . LEU C 356  ? 1.4192 0.8820 0.7459 0.1527  0.3113  -0.0434 356  LEU B O   
17083 C CB  . LEU C 356  ? 1.4292 0.8116 0.7196 0.1729  0.3545  -0.0087 356  LEU B CB  
17084 C CG  . LEU C 356  ? 1.4222 0.7879 0.7098 0.1909  0.3678  0.0135  356  LEU B CG  
17085 C CD1 . LEU C 356  ? 1.4518 0.7725 0.7076 0.1948  0.3868  0.0154  356  LEU B CD1 
17086 C CD2 . LEU C 356  ? 1.4087 0.7861 0.7193 0.1916  0.3739  0.0264  356  LEU B CD2 
17087 N N   . VAL C 357  ? 1.4546 0.8982 0.7863 0.1371  0.3375  -0.0365 357  VAL B N   
17088 C CA  . VAL C 357  ? 1.3865 0.8539 0.7284 0.1184  0.3280  -0.0545 357  VAL B CA  
17089 C C   . VAL C 357  ? 1.5430 0.9806 0.8695 0.0993  0.3402  -0.0610 357  VAL B C   
17090 O O   . VAL C 357  ? 1.4859 0.9099 0.8147 0.0942  0.3556  -0.0517 357  VAL B O   
17091 C CB  . VAL C 357  ? 1.3564 0.8646 0.7286 0.1154  0.3246  -0.0532 357  VAL B CB  
17092 C CG1 . VAL C 357  ? 1.3679 0.8949 0.7500 0.0933  0.3221  -0.0679 357  VAL B CG1 
17093 C CG2 . VAL C 357  ? 1.3243 0.8662 0.7126 0.1304  0.3071  -0.0535 357  VAL B CG2 
17094 N N   . ALA C 358  ? 1.5774 1.0034 0.8873 0.0880  0.3322  -0.0769 358  ALA B N   
17095 C CA  . ALA C 358  ? 1.6437 1.0340 0.9347 0.0690  0.3418  -0.0842 358  ALA B CA  
17096 C C   . ALA C 358  ? 1.6148 0.9634 0.8915 0.0751  0.3645  -0.0685 358  ALA B C   
17097 O O   . ALA C 358  ? 1.5840 0.9245 0.8670 0.0617  0.3755  -0.0646 358  ALA B O   
17098 C CB  . ALA C 358  ? 1.6362 1.0563 0.9496 0.0446  0.3357  -0.0951 358  ALA B CB  
17099 N N   . THR C 359  ? 1.6460 0.9707 0.9047 0.0962  0.3710  -0.0583 359  THR B N   
17100 C CA  . THR C 359  ? 1.6745 0.9563 0.9154 0.1056  0.3919  -0.0441 359  THR B CA  
17101 C C   . THR C 359  ? 1.6517 0.8904 0.8554 0.1180  0.3981  -0.0460 359  THR B C   
17102 O O   . THR C 359  ? 1.6105 0.8516 0.8113 0.1387  0.4002  -0.0347 359  THR B O   
17103 C CB  . THR C 359  ? 1.6734 0.9732 0.9353 0.1226  0.3989  -0.0229 359  THR B CB  
17104 O OG1 . THR C 359  ? 1.6681 0.9906 0.9367 0.1395  0.3879  -0.0185 359  THR B OG1 
17105 C CG2 . THR C 359  ? 1.6493 0.9847 0.9414 0.1111  0.3959  -0.0211 359  THR B CG2 
17106 N N   . PRO C 360  ? 1.6791 0.8778 0.8541 0.1048  0.4015  -0.0598 360  PRO B N   
17107 C CA  . PRO C 360  ? 1.7098 0.8617 0.8424 0.1119  0.4063  -0.0679 360  PRO B CA  
17108 C C   . PRO C 360  ? 1.7159 0.8449 0.8357 0.1378  0.4244  -0.0497 360  PRO B C   
17109 O O   . PRO C 360  ? 1.6617 0.7907 0.7976 0.1436  0.4373  -0.0332 360  PRO B O   
17110 C CB  . PRO C 360  ? 1.7744 0.8845 0.8882 0.0920  0.4127  -0.0784 360  PRO B CB  
17111 C CG  . PRO C 360  ? 1.7529 0.9012 0.8999 0.0679  0.4014  -0.0840 360  PRO B CG  
17112 C CD  . PRO C 360  ? 1.7004 0.8989 0.8850 0.0787  0.4001  -0.0687 360  PRO B CD  
17113 N N   . LEU C 361  ? 1.7459 0.8568 0.8372 0.1531  0.4255  -0.0520 361  LEU B N   
17114 C CA  . LEU C 361  ? 1.8058 0.9064 0.8908 0.1796  0.4418  -0.0324 361  LEU B CA  
17115 C C   . LEU C 361  ? 1.9500 0.9931 0.9967 0.1909  0.4626  -0.0315 361  LEU B C   
17116 O O   . LEU C 361  ? 1.9725 1.0027 1.0022 0.2139  0.4748  -0.0210 361  LEU B O   
17117 C CB  . LEU C 361  ? 1.7532 0.8788 0.8373 0.1934  0.4322  -0.0293 361  LEU B CB  
17118 C CG  . LEU C 361  ? 1.7006 0.8769 0.8293 0.1968  0.4240  -0.0137 361  LEU B CG  
17119 C CD1 . LEU C 361  ? 1.6017 0.8175 0.7568 0.1774  0.4019  -0.0267 361  LEU B CD1 
17120 C CD2 . LEU C 361  ? 1.7192 0.9096 0.8465 0.2168  0.4232  -0.0004 361  LEU B CD2 
17121 N N   . PHE C 362  ? 2.0688 1.0778 1.1031 0.1749  0.4669  -0.0417 362  PHE B N   
17122 C CA  . PHE C 362  ? 2.1860 1.1341 1.1816 0.1835  0.4849  -0.0439 362  PHE B CA  
17123 C C   . PHE C 362  ? 2.0879 1.0211 1.0982 0.1751  0.4954  -0.0350 362  PHE B C   
17124 O O   . PHE C 362  ? 2.0483 0.9978 1.0794 0.1508  0.4851  -0.0411 362  PHE B O   
17125 C CB  . PHE C 362  ? 2.3964 1.3057 1.3517 0.1684  0.4756  -0.0702 362  PHE B CB  
17126 C CG  . PHE C 362  ? 2.5302 1.4521 1.4669 0.1749  0.4634  -0.0806 362  PHE B CG  
17127 C CD1 . PHE C 362  ? 2.5836 1.5206 1.5189 0.1533  0.4404  -0.1007 362  PHE B CD1 
17128 C CD2 . PHE C 362  ? 2.6050 1.5261 1.5270 0.2031  0.4749  -0.0685 362  PHE B CD2 
17129 C CE1 . PHE C 362  ? 2.6337 1.5811 1.5500 0.1603  0.4286  -0.1093 362  PHE B CE1 
17130 C CE2 . PHE C 362  ? 2.6454 1.5774 1.5484 0.2095  0.4643  -0.0761 362  PHE B CE2 
17131 C CZ  . PHE C 362  ? 2.6623 1.6062 1.5612 0.1884  0.4407  -0.0968 362  PHE B CZ  
17132 N N   . LEU C 363  ? 2.0463 0.9500 1.0464 0.1957  0.5164  -0.0196 363  LEU B N   
17133 C CA  . LEU C 363  ? 1.9564 0.8389 0.9651 0.1894  0.5272  -0.0104 363  LEU B CA  
17134 C C   . LEU C 363  ? 1.9949 0.8088 0.9614 0.1827  0.5351  -0.0247 363  LEU B C   
17135 O O   . LEU C 363  ? 2.0034 0.7767 0.9318 0.2007  0.5451  -0.0298 363  LEU B O   
17136 C CB  . LEU C 363  ? 1.9101 0.8034 0.9378 0.2146  0.5438  0.0166  363  LEU B CB  
17137 C CG  . LEU C 363  ? 1.8545 0.7630 0.8789 0.2424  0.5504  0.0275  363  LEU B CG  
17138 C CD1 . LEU C 363  ? 1.9070 0.7590 0.8883 0.2624  0.5692  0.0251  363  LEU B CD1 
17139 C CD2 . LEU C 363  ? 1.7929 0.7414 0.8566 0.2568  0.5554  0.0540  363  LEU B CD2 
17140 N N   . LYS C 364  ? 2.0086 0.8103 0.9812 0.1559  0.5295  -0.0316 364  LYS B N   
17141 C CA  . LYS C 364  ? 2.1311 0.8652 1.0711 0.1490  0.5392  -0.0382 364  LYS B CA  
17142 C C   . LYS C 364  ? 2.1747 0.9002 1.1275 0.1679  0.5586  -0.0133 364  LYS B C   
17143 O O   . LYS C 364  ? 2.1162 0.8923 1.1095 0.1692  0.5574  0.0040  364  LYS B O   
17144 C CB  . LYS C 364  ? 2.1630 0.8967 1.1132 0.1116  0.5256  -0.0503 364  LYS B CB  
17145 C CG  . LYS C 364  ? 2.2014 0.9613 1.1524 0.0904  0.5031  -0.0721 364  LYS B CG  
17146 C CD  . LYS C 364  ? 2.1630 1.0006 1.1549 0.0932  0.4910  -0.0662 364  LYS B CD  
17147 C CE  . LYS C 364  ? 2.1825 1.0472 1.1779 0.0703  0.4673  -0.0879 364  LYS B CE  
17148 N NZ  . LYS C 364  ? 2.2657 1.0752 1.2127 0.0634  0.4616  -0.1105 364  LYS B NZ  
17149 N N   . PRO C 365  ? 2.2719 0.9341 1.1897 0.1844  0.5758  -0.0110 365  PRO B N   
17150 C CA  . PRO C 365  ? 2.2885 0.9444 1.2195 0.2048  0.5938  0.0139  365  PRO B CA  
17151 C C   . PRO C 365  ? 2.3413 0.9721 1.2785 0.1844  0.5959  0.0193  365  PRO B C   
17152 O O   . PRO C 365  ? 2.4172 1.0167 1.3381 0.1571  0.5874  0.0027  365  PRO B O   
17153 C CB  . PRO C 365  ? 2.3403 0.9412 1.2292 0.2353  0.6117  0.0130  365  PRO B CB  
17154 C CG  . PRO C 365  ? 2.3564 0.9372 1.2094 0.2307  0.6026  -0.0124 365  PRO B CG  
17155 C CD  . PRO C 365  ? 2.3347 0.9326 1.1990 0.1922  0.5805  -0.0295 365  PRO B CD  
17156 N N   . GLY C 366  ? 2.3477 0.9929 1.3091 0.1971  0.6066  0.0437  366  GLY B N   
17157 C CA  . GLY C 366  ? 2.4216 1.0554 1.3948 0.1771  0.6075  0.0524  366  GLY B CA  
17158 C C   . GLY C 366  ? 2.3402 1.0335 1.3505 0.1480  0.5909  0.0504  366  GLY B C   
17159 O O   . GLY C 366  ? 2.3852 1.0935 1.4176 0.1364  0.5922  0.0644  366  GLY B O   
17160 N N   . ILE C 367  ? 2.2544 0.9824 1.2709 0.1369  0.5755  0.0333  367  ILE B N   
17161 C CA  . ILE C 367  ? 2.1949 0.9831 1.2478 0.1137  0.5605  0.0318  367  ILE B CA  
17162 C C   . ILE C 367  ? 2.1042 0.9538 1.1903 0.1331  0.5585  0.0471  367  ILE B C   
17163 O O   . ILE C 367  ? 2.1204 0.9720 1.2000 0.1588  0.5630  0.0514  367  ILE B O   
17164 C CB  . ILE C 367  ? 2.1811 0.9762 1.2263 0.0900  0.5434  0.0063  367  ILE B CB  
17165 C CG1 . ILE C 367  ? 2.2281 0.9733 1.2529 0.0619  0.5425  -0.0048 367  ILE B CG1 
17166 C CG2 . ILE C 367  ? 2.1276 0.9952 1.2125 0.0759  0.5281  0.0050  367  ILE B CG2 
17167 C CD1 . ILE C 367  ? 2.2452 0.9814 1.2532 0.0410  0.5265  -0.0309 367  ILE B CD1 
17168 N N   . PRO C 368  ? 2.0168 0.9153 1.1378 0.1215  0.5522  0.0566  368  PRO B N   
17169 C CA  . PRO C 368  ? 1.9130 0.8645 1.0630 0.1402  0.5488  0.0708  368  PRO B CA  
17170 C C   . PRO C 368  ? 1.8824 0.8779 1.0445 0.1354  0.5315  0.0558  368  PRO B C   
17171 O O   . PRO C 368  ? 1.8651 0.8771 1.0332 0.1113  0.5197  0.0403  368  PRO B O   
17172 C CB  . PRO C 368  ? 1.8802 0.8606 1.0567 0.1287  0.5484  0.0843  368  PRO B CB  
17173 C CG  . PRO C 368  ? 1.9247 0.8713 1.0878 0.1013  0.5512  0.0764  368  PRO B CG  
17174 C CD  . PRO C 368  ? 1.9804 0.8926 1.1165 0.0918  0.5468  0.0543  368  PRO B CD  
17175 N N   . TYR C 369  ? 1.8470 0.8613 1.0131 0.1579  0.5300  0.0610  369  TYR B N   
17176 C CA  . TYR C 369  ? 1.7995 0.8506 0.9737 0.1562  0.5138  0.0481  369  TYR B CA  
17177 C C   . TYR C 369  ? 1.7675 0.8794 0.9796 0.1514  0.5007  0.0538  369  TYR B C   
17178 O O   . TYR C 369  ? 1.7798 0.9102 1.0101 0.1654  0.5043  0.0725  369  TYR B O   
17179 C CB  . TYR C 369  ? 1.8627 0.9057 1.0238 0.1822  0.5189  0.0533  369  TYR B CB  
17180 C CG  . TYR C 369  ? 1.8895 0.9623 1.0527 0.1826  0.5033  0.0412  369  TYR B CG  
17181 C CD1 . TYR C 369  ? 1.9173 0.9895 1.0692 0.1627  0.4902  0.0182  369  TYR B CD1 
17182 C CD2 . TYR C 369  ? 1.8675 0.9683 1.0439 0.2025  0.5012  0.0536  369  TYR B CD2 
17183 C CE1 . TYR C 369  ? 1.9242 1.0229 1.0772 0.1641  0.4753  0.0080  369  TYR B CE1 
17184 C CE2 . TYR C 369  ? 1.8886 1.0143 1.0659 0.2030  0.4869  0.0441  369  TYR B CE2 
17185 C CZ  . TYR C 369  ? 1.9217 1.0458 1.0864 0.1846  0.4740  0.0213  369  TYR B CZ  
17186 O OH  . TYR C 369  ? 1.9482 1.0966 1.1128 0.1865  0.4591  0.0127  369  TYR B OH  
17187 N N   . PRO C 370  ? 1.6086 0.7501 0.8316 0.1317  0.4853  0.0375  370  PRO B N   
17188 C CA  . PRO C 370  ? 1.5590 0.7580 0.8134 0.1253  0.4699  0.0355  370  PRO B CA  
17189 C C   . PRO C 370  ? 1.6277 0.8579 0.8907 0.1385  0.4559  0.0322  370  PRO B C   
17190 O O   . PRO C 370  ? 1.6279 0.8405 0.8709 0.1408  0.4531  0.0214  370  PRO B O   
17191 C CB  . PRO C 370  ? 1.5738 0.7787 0.8280 0.0984  0.4614  0.0162  370  PRO B CB  
17192 C CG  . PRO C 370  ? 1.6307 0.7790 0.8562 0.0883  0.4736  0.0121  370  PRO B CG  
17193 C CD  . PRO C 370  ? 1.6523 0.7629 0.8535 0.1108  0.4839  0.0184  370  PRO B CD  
17194 N N   . ILE C 371  ? 1.4806 0.7541 0.7702 0.1460  0.4461  0.0401  371  ILE B N   
17195 C CA  . ILE C 371  ? 1.4538 0.7520 0.7501 0.1584  0.4324  0.0382  371  ILE B CA  
17196 C C   . ILE C 371  ? 1.4413 0.7900 0.7652 0.1549  0.4148  0.0340  371  ILE B C   
17197 O O   . ILE C 371  ? 1.4227 0.7915 0.7611 0.1692  0.4086  0.0456  371  ILE B O   
17198 C CB  . ILE C 371  ? 1.4429 0.7352 0.7410 0.1825  0.4389  0.0591  371  ILE B CB  
17199 C CG1 . ILE C 371  ? 1.4820 0.7292 0.7530 0.1932  0.4560  0.0645  371  ILE B CG1 
17200 C CG2 . ILE C 371  ? 1.4149 0.7348 0.7227 0.1928  0.4235  0.0591  371  ILE B CG2 
17201 C CD1 . ILE C 371  ? 1.4689 0.7187 0.7475 0.2161  0.4625  0.0866  371  ILE B CD1 
17202 N N   . LYS C 372  ? 1.4095 0.7797 0.7414 0.1371  0.4061  0.0180  372  LYS B N   
17203 C CA  . LYS C 372  ? 1.3719 0.7914 0.7296 0.1366  0.3899  0.0132  372  LYS B CA  
17204 C C   . LYS C 372  ? 1.3493 0.7884 0.7120 0.1499  0.3730  0.0102  372  LYS B C   
17205 O O   . LYS C 372  ? 1.4004 0.8455 0.7578 0.1442  0.3626  -0.0048 372  LYS B O   
17206 C CB  . LYS C 372  ? 1.3769 0.8183 0.7424 0.1159  0.3836  -0.0045 372  LYS B CB  
17207 C CG  . LYS C 372  ? 1.4162 0.8260 0.7666 0.0968  0.3964  -0.0094 372  LYS B CG  
17208 C CD  . LYS C 372  ? 1.6192 1.0498 0.9764 0.0751  0.3864  -0.0289 372  LYS B CD  
17209 C CE  . LYS C 372  ? 1.9091 1.2973 1.2440 0.0559  0.3950  -0.0365 372  LYS B CE  
17210 N NZ  . LYS C 372  ? 1.9099 1.3058 1.2562 0.0314  0.4012  -0.0383 372  LYS B NZ  
17211 N N   . VAL C 373  ? 1.3253 0.7741 0.6981 0.1666  0.3688  0.0245  373  VAL B N   
17212 C CA  . VAL C 373  ? 1.3907 0.8596 0.7705 0.1777  0.3507  0.0224  373  VAL B CA  
17213 C C   . VAL C 373  ? 1.3347 0.8449 0.7348 0.1749  0.3338  0.0112  373  VAL B C   
17214 O O   . VAL C 373  ? 1.3663 0.8919 0.7762 0.1661  0.3379  0.0079  373  VAL B O   
17215 C CB  . VAL C 373  ? 1.2914 0.7539 0.6751 0.1952  0.3510  0.0424  373  VAL B CB  
17216 C CG1 . VAL C 373  ? 1.3149 0.7417 0.6839 0.1990  0.3718  0.0561  373  VAL B CG1 
17217 C CG2 . VAL C 373  ? 1.2651 0.7513 0.6693 0.2007  0.3438  0.0510  373  VAL B CG2 
17218 N N   . GLN C 374  ? 1.2788 0.8073 0.6846 0.1829  0.3154  0.0056  374  GLN B N   
17219 C CA  . GLN C 374  ? 1.2879 0.8543 0.7111 0.1813  0.3002  -0.0071 374  GLN B CA  
17220 C C   . GLN C 374  ? 1.3643 0.9463 0.7963 0.1966  0.2804  -0.0051 374  GLN B C   
17221 O O   . GLN C 374  ? 1.4433 1.0199 0.8680 0.2011  0.2702  -0.0079 374  GLN B O   
17222 C CB  . GLN C 374  ? 1.2835 0.8606 0.7041 0.1676  0.2961  -0.0263 374  GLN B CB  
17223 C CG  . GLN C 374  ? 1.3153 0.9299 0.7510 0.1714  0.2757  -0.0400 374  GLN B CG  
17224 C CD  . GLN C 374  ? 1.3940 1.0238 0.8309 0.1561  0.2715  -0.0583 374  GLN B CD  
17225 O OE1 . GLN C 374  ? 1.4219 1.0465 0.8487 0.1561  0.2609  -0.0665 374  GLN B OE1 
17226 N NE2 . GLN C 374  ? 1.4080 1.0572 0.8573 0.1422  0.2796  -0.0639 374  GLN B NE2 
17227 N N   . VAL C 375  ? 1.3462 0.9451 0.7920 0.2047  0.2741  0.0001  375  VAL B N   
17228 C CA  . VAL C 375  ? 1.3042 0.9100 0.7565 0.2193  0.2549  0.0044  375  VAL B CA  
17229 C C   . VAL C 375  ? 1.3370 0.9712 0.7977 0.2227  0.2360  -0.0128 375  VAL B C   
17230 O O   . VAL C 375  ? 1.3381 0.9969 0.8069 0.2167  0.2374  -0.0258 375  VAL B O   
17231 C CB  . VAL C 375  ? 1.2174 0.8255 0.6782 0.2279  0.2529  0.0169  375  VAL B CB  
17232 C CG1 . VAL C 375  ? 1.1779 0.7913 0.6447 0.2411  0.2303  0.0190  375  VAL B CG1 
17233 C CG2 . VAL C 375  ? 1.2015 0.7835 0.6568 0.2275  0.2693  0.0367  375  VAL B CG2 
17234 N N   . LYS C 376  ? 1.3572 0.9884 0.8166 0.2328  0.2185  -0.0118 376  LYS B N   
17235 C CA  . LYS C 376  ? 1.3232 0.9778 0.7893 0.2389  0.1983  -0.0271 376  LYS B CA  
17236 C C   . LYS C 376  ? 1.2575 0.9064 0.7262 0.2537  0.1790  -0.0193 376  LYS B C   
17237 O O   . LYS C 376  ? 1.2030 0.8287 0.6668 0.2565  0.1807  -0.0020 376  LYS B O   
17238 C CB  . LYS C 376  ? 1.3729 1.0260 0.8297 0.2326  0.1954  -0.0370 376  LYS B CB  
17239 C CG  . LYS C 376  ? 1.4078 1.0830 0.8695 0.2194  0.2017  -0.0539 376  LYS B CG  
17240 C CD  . LYS C 376  ? 1.4301 1.0932 0.8772 0.2095  0.2033  -0.0606 376  LYS B CD  
17241 C CE  . LYS C 376  ? 1.4348 1.1210 0.8895 0.1944  0.2069  -0.0769 376  LYS B CE  
17242 N NZ  . LYS C 376  ? 1.4846 1.1434 0.9196 0.1806  0.2185  -0.0777 376  LYS B NZ  
17243 N N   . ASP C 377  ? 1.2825 0.9524 0.7595 0.2632  0.1606  -0.0314 377  ASP B N   
17244 C CA  . ASP C 377  ? 1.3360 0.9972 0.8144 0.2771  0.1398  -0.0252 377  ASP B CA  
17245 C C   . ASP C 377  ? 1.4111 1.0675 0.8839 0.2815  0.1240  -0.0283 377  ASP B C   
17246 O O   . ASP C 377  ? 1.4268 1.0940 0.8963 0.2763  0.1252  -0.0398 377  ASP B O   
17247 C CB  . ASP C 377  ? 1.3436 1.0254 0.8309 0.2884  0.1265  -0.0368 377  ASP B CB  
17248 C CG  . ASP C 377  ? 1.3805 1.0943 0.8745 0.2886  0.1246  -0.0573 377  ASP B CG  
17249 O OD1 . ASP C 377  ? 1.3993 1.1197 0.8922 0.2761  0.1365  -0.0619 377  ASP B OD1 
17250 O OD2 . ASP C 377  ? 1.4060 1.1383 0.9063 0.3012  0.1112  -0.0687 377  ASP B OD2 
17251 N N   . SER C 378  ? 1.4582 1.0981 0.9299 0.2910  0.1076  -0.0175 378  SER B N   
17252 C CA  . SER C 378  ? 1.5165 1.1486 0.9820 0.2970  0.0900  -0.0173 378  SER B CA  
17253 C C   . SER C 378  ? 1.1994 0.8567 0.6676 0.3021  0.0778  -0.0391 378  SER B C   
17254 O O   . SER C 378  ? 1.2003 0.8537 0.6631 0.3085  0.0612  -0.0410 378  SER B O   
17255 C CB  . SER C 378  ? 1.5409 1.1537 1.0082 0.3065  0.0712  -0.0035 378  SER B CB  
17256 O OG  . SER C 378  ? 1.5307 1.1443 1.0061 0.3103  0.0696  -0.0016 378  SER B OG  
17257 N N   . LEU C 379  ? 1.2163 0.9007 0.6935 0.2988  0.0868  -0.0541 379  LEU B N   
17258 C CA  . LEU C 379  ? 1.2867 1.0011 0.7706 0.3023  0.0779  -0.0739 379  LEU B CA  
17259 C C   . LEU C 379  ? 1.3825 1.1143 0.8687 0.2864  0.0963  -0.0822 379  LEU B C   
17260 O O   . LEU C 379  ? 1.4253 1.1896 0.9228 0.2862  0.0934  -0.0984 379  LEU B O   
17261 C CB  . LEU C 379  ? 1.2596 0.9978 0.7560 0.3160  0.0677  -0.0861 379  LEU B CB  
17262 C CG  . LEU C 379  ? 1.2972 1.0312 0.7924 0.3343  0.0405  -0.0904 379  LEU B CG  
17263 C CD1 . LEU C 379  ? 1.2887 1.0309 0.7898 0.3513  0.0292  -0.0981 379  LEU B CD1 
17264 C CD2 . LEU C 379  ? 1.3120 1.0670 0.8099 0.3359  0.0309  -0.1035 379  LEU B CD2 
17265 N N   . ASP C 380  ? 1.4151 1.1257 0.8914 0.2731  0.1150  -0.0710 380  ASP B N   
17266 C CA  . ASP C 380  ? 1.4931 1.2127 0.9686 0.2564  0.1322  -0.0781 380  ASP B CA  
17267 C C   . ASP C 380  ? 1.5011 1.2550 0.9936 0.2509  0.1404  -0.0906 380  ASP B C   
17268 O O   . ASP C 380  ? 1.5136 1.2847 1.0100 0.2386  0.1454  -0.1014 380  ASP B O   
17269 C CB  . ASP C 380  ? 1.5802 1.3010 1.0466 0.2519  0.1238  -0.0866 380  ASP B CB  
17270 C CG  . ASP C 380  ? 1.6843 1.3690 1.1289 0.2521  0.1247  -0.0729 380  ASP B CG  
17271 O OD1 . ASP C 380  ? 1.6909 1.3536 1.1228 0.2414  0.1435  -0.0652 380  ASP B OD1 
17272 O OD2 . ASP C 380  ? 1.7542 1.4329 1.1940 0.2636  0.1067  -0.0697 380  ASP B OD2 
17273 N N   . GLN C 381  ? 1.5224 1.2871 1.0245 0.2594  0.1411  -0.0893 381  GLN B N   
17274 C CA  . GLN C 381  ? 1.5313 1.3219 1.0454 0.2510  0.1565  -0.0953 381  GLN B CA  
17275 C C   . GLN C 381  ? 1.4882 1.2534 0.9939 0.2408  0.1774  -0.0804 381  GLN B C   
17276 O O   . GLN C 381  ? 1.4764 1.2095 0.9709 0.2448  0.1777  -0.0657 381  GLN B O   
17277 C CB  . GLN C 381  ? 1.5631 1.3830 1.0901 0.2656  0.1491  -0.1033 381  GLN B CB  
17278 C CG  . GLN C 381  ? 1.6416 1.4878 1.1780 0.2800  0.1282  -0.1179 381  GLN B CG  
17279 C CD  . GLN C 381  ? 1.7173 1.5435 1.2463 0.3004  0.1081  -0.1139 381  GLN B CD  
17280 O OE1 . GLN C 381  ? 1.7470 1.5918 1.2825 0.3177  0.0953  -0.1236 381  GLN B OE1 
17281 N NE2 . GLN C 381  ? 1.7354 1.5227 1.2504 0.2984  0.1055  -0.0991 381  GLN B NE2 
17282 N N   . LEU C 382  ? 1.4360 1.2162 0.9480 0.2276  0.1949  -0.0832 382  LEU B N   
17283 C CA  . LEU C 382  ? 1.3830 1.1397 0.8870 0.2184  0.2147  -0.0693 382  LEU B CA  
17284 C C   . LEU C 382  ? 1.3808 1.1372 0.8862 0.2316  0.2128  -0.0614 382  LEU B C   
17285 O O   . LEU C 382  ? 1.4342 1.2172 0.9486 0.2425  0.2030  -0.0705 382  LEU B O   
17286 C CB  . LEU C 382  ? 1.3706 1.1435 0.8809 0.1999  0.2319  -0.0748 382  LEU B CB  
17287 C CG  . LEU C 382  ? 1.3875 1.1419 0.8882 0.1850  0.2358  -0.0777 382  LEU B CG  
17288 C CD1 . LEU C 382  ? 1.4094 1.1748 0.9157 0.1635  0.2513  -0.0827 382  LEU B CD1 
17289 C CD2 . LEU C 382  ? 1.3810 1.0898 0.8622 0.1869  0.2426  -0.0624 382  LEU B CD2 
17290 N N   . VAL C 383  ? 1.3494 1.0758 0.8453 0.2319  0.2208  -0.0447 383  VAL B N   
17291 C CA  . VAL C 383  ? 1.3111 1.0372 0.8075 0.2430  0.2182  -0.0371 383  VAL B CA  
17292 C C   . VAL C 383  ? 1.3332 1.0435 0.8242 0.2343  0.2386  -0.0230 383  VAL B C   
17293 O O   . VAL C 383  ? 1.3387 1.0210 0.8221 0.2282  0.2484  -0.0105 383  VAL B O   
17294 C CB  . VAL C 383  ? 1.2496 0.9580 0.7427 0.2578  0.1984  -0.0300 383  VAL B CB  
17295 C CG1 . VAL C 383  ? 1.2768 0.9754 0.7673 0.2576  0.1885  -0.0324 383  VAL B CG1 
17296 C CG2 . VAL C 383  ? 1.1822 0.8636 0.6696 0.2588  0.2043  -0.0100 383  VAL B CG2 
17297 N N   . GLY C 384  ? 1.3490 1.0788 0.8431 0.2345  0.2457  -0.0253 384  GLY B N   
17298 C CA  . GLY C 384  ? 1.3660 1.0838 0.8546 0.2261  0.2652  -0.0124 384  GLY B CA  
17299 C C   . GLY C 384  ? 1.3905 1.0939 0.8733 0.2376  0.2602  0.0011  384  GLY B C   
17300 O O   . GLY C 384  ? 1.4135 1.1198 0.8971 0.2518  0.2411  -0.0016 384  GLY B O   
17301 N N   . GLY C 385  ? 1.4025 1.0890 0.8793 0.2313  0.2764  0.0160  385  GLY B N   
17302 C CA  . GLY C 385  ? 1.4029 1.0774 0.8745 0.2406  0.2727  0.0301  385  GLY B CA  
17303 C C   . GLY C 385  ? 1.3894 1.0395 0.8616 0.2478  0.2607  0.0427  385  GLY B C   
17304 O O   . GLY C 385  ? 1.4079 1.0529 0.8792 0.2578  0.2481  0.0507  385  GLY B O   
17305 N N   . VAL C 386  ? 1.3575 0.9932 0.8309 0.2427  0.2638  0.0446  386  VAL B N   
17306 C CA  . VAL C 386  ? 1.3238 0.9376 0.7986 0.2482  0.2569  0.0599  386  VAL B CA  
17307 C C   . VAL C 386  ? 1.2748 0.8673 0.7456 0.2424  0.2773  0.0769  386  VAL B C   
17308 O O   . VAL C 386  ? 1.2858 0.8727 0.7510 0.2323  0.2952  0.0737  386  VAL B O   
17309 C CB  . VAL C 386  ? 1.2131 0.8231 0.6897 0.2492  0.2467  0.0539  386  VAL B CB  
17310 C CG1 . VAL C 386  ? 1.2022 0.8009 0.6836 0.2586  0.2298  0.0669  386  VAL B CG1 
17311 C CG2 . VAL C 386  ? 1.2090 0.8424 0.6878 0.2506  0.2346  0.0323  386  VAL B CG2 
17312 N N   . PRO C 387  ? 1.2285 0.8087 0.7026 0.2490  0.2741  0.0955  387  PRO B N   
17313 C CA  . PRO C 387  ? 1.2746 0.8345 0.7454 0.2457  0.2940  0.1119  387  PRO B CA  
17314 C C   . PRO C 387  ? 1.3297 0.8742 0.7996 0.2452  0.2990  0.1156  387  PRO B C   
17315 O O   . PRO C 387  ? 1.3368 0.8843 0.8121 0.2502  0.2837  0.1152  387  PRO B O   
17316 C CB  . PRO C 387  ? 1.2564 0.8131 0.7338 0.2541  0.2862  0.1308  387  PRO B CB  
17317 C CG  . PRO C 387  ? 1.1983 0.7706 0.6805 0.2609  0.2602  0.1226  387  PRO B CG  
17318 C CD  . PRO C 387  ? 1.1856 0.7672 0.6669 0.2591  0.2528  0.1035  387  PRO B CD  
17319 N N   . VAL C 388  ? 1.3369 0.8630 0.7981 0.2398  0.3201  0.1196  388  VAL B N   
17320 C CA  . VAL C 388  ? 1.3360 0.8454 0.7912 0.2402  0.3272  0.1216  388  VAL B CA  
17321 C C   . VAL C 388  ? 1.3619 0.8470 0.8122 0.2435  0.3475  0.1397  388  VAL B C   
17322 O O   . VAL C 388  ? 1.3931 0.8640 0.8329 0.2371  0.3644  0.1375  388  VAL B O   
17323 C CB  . VAL C 388  ? 1.3488 0.8580 0.7925 0.2295  0.3317  0.1002  388  VAL B CB  
17324 C CG1 . VAL C 388  ? 1.3759 0.8578 0.8045 0.2268  0.3494  0.1022  388  VAL B CG1 
17325 C CG2 . VAL C 388  ? 1.3290 0.8576 0.7773 0.2307  0.3111  0.0856  388  VAL B CG2 
17326 N N   . THR C 389  ? 1.3575 0.8377 0.8159 0.2535  0.3463  0.1582  389  THR B N   
17327 C CA  . THR C 389  ? 1.3922 0.8508 0.8465 0.2592  0.3669  0.1754  389  THR B CA  
17328 C C   . THR C 389  ? 1.4507 0.8867 0.8865 0.2583  0.3829  0.1687  389  THR B C   
17329 O O   . THR C 389  ? 1.4857 0.9249 0.9153 0.2560  0.3753  0.1567  389  THR B O   
17330 C CB  . THR C 389  ? 1.5309 0.9951 1.0035 0.2710  0.3629  0.2010  389  THR B CB  
17331 O OG1 . THR C 389  ? 1.5048 0.9888 0.9915 0.2722  0.3396  0.2015  389  THR B OG1 
17332 C CG2 . THR C 389  ? 1.5312 0.9964 1.0114 0.2738  0.3662  0.2148  389  THR B CG2 
17333 N N   . LEU C 390  ? 1.4023 0.8137 0.8269 0.2610  0.4041  0.1761  390  LEU B N   
17334 C CA  . LEU C 390  ? 1.3883 0.7738 0.7908 0.2606  0.4189  0.1680  390  LEU B CA  
17335 C C   . LEU C 390  ? 1.4519 0.8169 0.8507 0.2746  0.4379  0.1874  390  LEU B C   
17336 O O   . LEU C 390  ? 1.5399 0.8828 0.9295 0.2755  0.4536  0.1913  390  LEU B O   
17337 C CB  . LEU C 390  ? 1.3544 0.7230 0.7395 0.2468  0.4272  0.1502  390  LEU B CB  
17338 C CG  . LEU C 390  ? 1.4179 0.7505 0.7771 0.2481  0.4451  0.1449  390  LEU B CG  
17339 C CD1 . LEU C 390  ? 1.4609 0.7967 0.8090 0.2434  0.4359  0.1279  390  LEU B CD1 
17340 C CD2 . LEU C 390  ? 1.3957 0.7018 0.7385 0.2369  0.4579  0.1362  390  LEU B CD2 
17341 N N   . ASN C 391  ? 1.4323 0.8049 0.8388 0.2861  0.4369  0.2006  391  ASN B N   
17342 C CA  . ASN C 391  ? 1.4923 0.8490 0.8962 0.3015  0.4564  0.2192  391  ASN B CA  
17343 C C   . ASN C 391  ? 1.5576 0.8836 0.9303 0.3036  0.4723  0.2067  391  ASN B C   
17344 O O   . ASN C 391  ? 1.5857 0.9132 0.9463 0.2980  0.4645  0.1918  391  ASN B O   
17345 C CB  . ASN C 391  ? 1.5220 0.9024 0.9481 0.3123  0.4498  0.2397  391  ASN B CB  
17346 C CG  . ASN C 391  ? 1.5352 0.9395 0.9916 0.3141  0.4380  0.2580  391  ASN B CG  
17347 O OD1 . ASN C 391  ? 1.5014 0.9235 0.9687 0.3044  0.4178  0.2510  391  ASN B OD1 
17348 N ND2 . ASN C 391  ? 1.5656 0.9714 1.0356 0.3276  0.4499  0.2820  391  ASN B ND2 
17349 N N   . ALA C 392  ? 1.6083 0.9047 0.9662 0.3126  0.4938  0.2126  392  ALA B N   
17350 C CA  . ALA C 392  ? 1.6265 0.8872 0.9494 0.3148  0.5089  0.1984  392  ALA B CA  
17351 C C   . ALA C 392  ? 1.6264 0.8659 0.9407 0.3356  0.5318  0.2149  392  ALA B C   
17352 O O   . ALA C 392  ? 1.6193 0.8671 0.9537 0.3458  0.5377  0.2355  392  ALA B O   
17353 C CB  . ALA C 392  ? 1.6531 0.8868 0.9553 0.2990  0.5108  0.1776  392  ALA B CB  
17354 N N   . GLN C 393  ? 1.6676 0.8797 0.9509 0.3429  0.5446  0.2055  393  GLN B N   
17355 C CA  . GLN C 393  ? 1.7525 0.9504 1.0285 0.3668  0.5669  0.2226  393  GLN B CA  
17356 C C   . GLN C 393  ? 1.8167 0.9662 1.0469 0.3734  0.5843  0.2061  393  GLN B C   
17357 O O   . GLN C 393  ? 1.8072 0.9426 1.0114 0.3620  0.5773  0.1836  393  GLN B O   
17358 C CB  . GLN C 393  ? 1.7498 0.9852 1.0490 0.3784  0.5638  0.2424  393  GLN B CB  
17359 C CG  . GLN C 393  ? 1.7637 0.9969 1.0652 0.4039  0.5864  0.2649  393  GLN B CG  
17360 C CD  . GLN C 393  ? 1.8007 0.9992 1.0599 0.4163  0.6050  0.2533  393  GLN B CD  
17361 O OE1 . GLN C 393  ? 1.8297 1.0072 1.0765 0.4370  0.6278  0.2627  393  GLN B OE1 
17362 N NE2 . GLN C 393  ? 1.8013 0.9927 1.0361 0.4046  0.5949  0.2322  393  GLN B NE2 
17363 N N   . THR C 394  ? 1.8568 0.9803 1.0769 0.3926  0.6063  0.2175  394  THR B N   
17364 C CA  . THR C 394  ? 1.9499 1.0178 1.1271 0.3954  0.6209  0.2003  394  THR B CA  
17365 C C   . THR C 394  ? 2.1002 1.1415 1.2577 0.4249  0.6473  0.2117  394  THR B C   
17366 O O   . THR C 394  ? 2.1316 1.1929 1.3154 0.4432  0.6576  0.2372  394  THR B O   
17367 C CB  . THR C 394  ? 1.8890 0.9371 1.0689 0.3804  0.6174  0.1948  394  THR B CB  
17368 O OG1 . THR C 394  ? 1.8616 0.9083 1.0327 0.3534  0.5995  0.1709  394  THR B OG1 
17369 C CG2 . THR C 394  ? 1.9404 0.9314 1.0878 0.3929  0.6385  0.1920  394  THR B CG2 
17370 N N   . ILE C 395  ? 2.1837 1.1804 1.2944 0.4303  0.6579  0.1927  395  ILE B N   
17371 C CA  . ILE C 395  ? 2.2710 1.2336 1.3572 0.4593  0.6844  0.2003  395  ILE B CA  
17372 C C   . ILE C 395  ? 2.3900 1.2852 1.4312 0.4567  0.6926  0.1789  395  ILE B C   
17373 O O   . ILE C 395  ? 2.4248 1.2968 1.4433 0.4330  0.6790  0.1537  395  ILE B O   
17374 C CB  . ILE C 395  ? 2.2744 1.2434 1.3415 0.4793  0.6963  0.2028  395  ILE B CB  
17375 C CG1 . ILE C 395  ? 2.2973 1.2293 1.3149 0.4682  0.6907  0.1719  395  ILE B CG1 
17376 C CG2 . ILE C 395  ? 2.2281 1.2614 1.3381 0.4792  0.6868  0.2238  395  ILE B CG2 
17377 C CD1 . ILE C 395  ? 2.3554 1.2486 1.3265 0.4952  0.7140  0.1670  395  ILE B CD1 
17378 N N   . ASP C 396  ? 2.4524 1.3168 1.4824 0.4816  0.7146  0.1901  396  ASP B N   
17379 C CA  . ASP C 396  ? 2.5156 1.3122 1.5062 0.4828  0.7242  0.1749  396  ASP B CA  
17380 C C   . ASP C 396  ? 2.5722 1.3243 1.5078 0.4914  0.7325  0.1523  396  ASP B C   
17381 O O   . ASP C 396  ? 2.5715 1.3473 1.5019 0.5037  0.7364  0.1544  396  ASP B O   
17382 C CB  . ASP C 396  ? 2.5799 1.3633 1.5797 0.5114  0.7452  0.1976  396  ASP B CB  
17383 C CG  . ASP C 396  ? 2.6816 1.4211 1.6733 0.5005  0.7443  0.1934  396  ASP B CG  
17384 O OD1 . ASP C 396  ? 2.7526 1.4592 1.7347 0.5245  0.7626  0.2047  396  ASP B OD1 
17385 O OD2 . ASP C 396  ? 2.6877 1.4264 1.6832 0.4680  0.7252  0.1795  396  ASP B OD2 
17386 N N   . VAL C 397  ? 2.6423 1.3285 1.5350 0.4848  0.7347  0.1307  397  VAL B N   
17387 C CA  . VAL C 397  ? 2.7422 1.3774 1.5771 0.5005  0.7466  0.1113  397  VAL B CA  
17388 C C   . VAL C 397  ? 2.7773 1.4056 1.6061 0.5431  0.7752  0.1309  397  VAL B C   
17389 O O   . VAL C 397  ? 2.8083 1.4197 1.6011 0.5657  0.7894  0.1245  397  VAL B O   
17390 C CB  . VAL C 397  ? 2.7932 1.3532 1.5813 0.4840  0.7420  0.0837  397  VAL B CB  
17391 C CG1 . VAL C 397  ? 2.8340 1.3460 1.6122 0.5021  0.7594  0.0930  397  VAL B CG1 
17392 C CG2 . VAL C 397  ? 2.8624 1.3804 1.5913 0.4899  0.7439  0.0575  397  VAL B CG2 
17393 N N   . ASN C 398  ? 2.7674 1.4127 1.6331 0.5542  0.7832  0.1557  398  ASN B N   
17394 C CA  . ASN C 398  ? 2.8021 1.4517 1.6744 0.5940  0.8090  0.1789  398  ASN B CA  
17395 C C   . ASN C 398  ? 2.7275 1.4481 1.6352 0.6082  0.8135  0.2009  398  ASN B C   
17396 O O   . ASN C 398  ? 2.7077 1.4495 1.6332 0.6396  0.8334  0.2250  398  ASN B O   
17397 C CB  . ASN C 398  ? 2.8144 1.4660 1.7204 0.5968  0.8112  0.1994  398  ASN B CB  
17398 C CG  . ASN C 398  ? 2.8976 1.5096 1.7842 0.6356  0.8380  0.2102  398  ASN B CG  
17399 O OD1 . ASN C 398  ? 2.9797 1.5511 1.8200 0.6590  0.8551  0.1979  398  ASN B OD1 
17400 N ND2 . ASN C 398  ? 2.8832 1.5060 1.8037 0.6438  0.8417  0.2332  398  ASN B ND2 
17401 N N   . GLN C 399  ? 2.7202 1.4788 1.6400 0.5844  0.7942  0.1937  399  GLN B N   
17402 C CA  . GLN C 399  ? 2.7025 1.5266 1.6547 0.5932  0.7954  0.2137  399  GLN B CA  
17403 C C   . GLN C 399  ? 2.6584 1.5446 1.6769 0.5956  0.7923  0.2471  399  GLN B C   
17404 O O   . GLN C 399  ? 2.6301 1.5654 1.6769 0.6119  0.8006  0.2702  399  GLN B O   
17405 C CB  . GLN C 399  ? 2.7638 1.5748 1.6815 0.6275  0.8210  0.2159  399  GLN B CB  
17406 C CG  . GLN C 399  ? 2.8265 1.5976 1.6858 0.6197  0.8166  0.1846  399  GLN B CG  
17407 C CD  . GLN C 399  ? 2.7922 1.6034 1.6683 0.5886  0.7902  0.1772  399  GLN B CD  
17408 O OE1 . GLN C 399  ? 2.7696 1.6281 1.6626 0.5945  0.7910  0.1912  399  GLN B OE1 
17409 N NE2 . GLN C 399  ? 2.7834 1.5760 1.6553 0.5556  0.7667  0.1558  399  GLN B NE2 
17410 N N   . GLU C 400  ? 2.6509 1.5344 1.6928 0.5780  0.7796  0.2492  400  GLU B N   
17411 C CA  . GLU C 400  ? 2.5764 1.5144 1.6782 0.5749  0.7712  0.2771  400  GLU B CA  
17412 C C   . GLU C 400  ? 2.4916 1.4667 1.6200 0.5400  0.7419  0.2707  400  GLU B C   
17413 O O   . GLU C 400  ? 2.4838 1.4315 1.5863 0.5164  0.7285  0.2445  400  GLU B O   
17414 C CB  . GLU C 400  ? 2.6345 1.5419 1.7400 0.5792  0.7762  0.2832  400  GLU B CB  
17415 C CG  . GLU C 400  ? 2.6652 1.6117 1.8160 0.6012  0.7854  0.3175  400  GLU B CG  
17416 C CD  . GLU C 400  ? 2.7659 1.6680 1.9051 0.6172  0.7988  0.3227  400  GLU B CD  
17417 O OE1 . GLU C 400  ? 2.8050 1.7035 1.9446 0.6516  0.8214  0.3395  400  GLU B OE1 
17418 O OE2 . GLU C 400  ? 2.8052 1.6757 1.9345 0.5960  0.7871  0.3106  400  GLU B OE2 
17419 N N   . THR C 401  ? 2.3938 1.4304 1.5732 0.5366  0.7311  0.2937  401  THR B N   
17420 C CA  . THR C 401  ? 2.2843 1.3541 1.4882 0.5056  0.7028  0.2874  401  THR B CA  
17421 C C   . THR C 401  ? 2.2034 1.2836 1.4371 0.4923  0.6902  0.2956  401  THR B C   
17422 O O   . THR C 401  ? 2.2392 1.3037 1.4779 0.5062  0.7019  0.3083  401  THR B O   
17423 C CB  . THR C 401  ? 2.2388 1.3698 1.4813 0.5044  0.6923  0.3058  401  THR B CB  
17424 O OG1 . THR C 401  ? 2.2066 1.3739 1.4942 0.5166  0.6950  0.3365  401  THR B OG1 
17425 C CG2 . THR C 401  ? 2.2713 1.4053 1.4927 0.5193  0.7051  0.3053  401  THR B CG2 
17426 N N   . SER C 402  ? 2.1002 1.2099 1.3542 0.4666  0.6657  0.2893  402  SER B N   
17427 C CA  . SER C 402  ? 2.0129 1.1388 1.2950 0.4517  0.6506  0.2959  402  SER B CA  
17428 C C   . SER C 402  ? 1.8834 1.0562 1.1945 0.4315  0.6249  0.2952  402  SER B C   
17429 O O   . SER C 402  ? 1.8424 1.0133 1.1382 0.4144  0.6128  0.2740  402  SER B O   
17430 C CB  . SER C 402  ? 2.0439 1.1228 1.2965 0.4364  0.6502  0.2749  402  SER B CB  
17431 O OG  . SER C 402  ? 2.0688 1.1274 1.2905 0.4199  0.6436  0.2469  402  SER B OG  
17432 N N   . ASP C 403  ? 1.8247 1.0391 1.1772 0.4343  0.6157  0.3185  403  ASP B N   
17433 C CA  . ASP C 403  ? 1.7682 1.0220 1.1467 0.4158  0.5901  0.3176  403  ASP B CA  
17434 C C   . ASP C 403  ? 1.7256 0.9799 1.1122 0.3984  0.5753  0.3116  403  ASP B C   
17435 O O   . ASP C 403  ? 1.7143 0.9908 1.1293 0.4008  0.5683  0.3301  403  ASP B O   
17436 C CB  . ASP C 403  ? 1.7992 1.0989 1.2174 0.4257  0.5846  0.3448  403  ASP B CB  
17437 C CG  . ASP C 403  ? 1.8427 1.1590 1.2590 0.4275  0.5834  0.3440  403  ASP B CG  
17438 O OD1 . ASP C 403  ? 1.8044 1.1260 1.2130 0.4097  0.5660  0.3259  403  ASP B OD1 
17439 O OD2 . ASP C 403  ? 1.8896 1.2150 1.3129 0.4477  0.6005  0.3629  403  ASP B OD2 
17440 N N   . LEU C 404  ? 1.6919 0.9230 1.0530 0.3806  0.5702  0.2857  404  LEU B N   
17441 C CA  . LEU C 404  ? 1.6431 0.8751 1.0077 0.3620  0.5571  0.2766  404  LEU B CA  
17442 C C   . LEU C 404  ? 1.6357 0.9098 1.0360 0.3573  0.5377  0.2909  404  LEU B C   
17443 O O   . LEU C 404  ? 1.6360 0.9436 1.0608 0.3624  0.5275  0.3036  404  LEU B O   
17444 C CB  . LEU C 404  ? 1.5800 0.8029 0.9236 0.3415  0.5472  0.2479  404  LEU B CB  
17445 C CG  . LEU C 404  ? 1.5855 0.7588 0.8908 0.3415  0.5642  0.2320  404  LEU B CG  
17446 C CD1 . LEU C 404  ? 1.5399 0.7054 0.8269 0.3192  0.5532  0.2042  404  LEU B CD1 
17447 C CD2 . LEU C 404  ? 1.5635 0.7084 0.8631 0.3451  0.5767  0.2404  404  LEU B CD2 
17448 N N   . ASP C 405  ? 1.5958 0.8661 0.9974 0.3473  0.5324  0.2891  405  ASP B N   
17449 C CA  . ASP C 405  ? 1.5261 0.8312 0.9535 0.3399  0.5120  0.2964  405  ASP B CA  
17450 C C   . ASP C 405  ? 1.4626 0.7792 0.8841 0.3207  0.4955  0.2727  405  ASP B C   
17451 O O   . ASP C 405  ? 1.4668 0.7609 0.8644 0.3097  0.5009  0.2521  405  ASP B O   
17452 C CB  . ASP C 405  ? 1.6285 0.9245 1.0575 0.3402  0.5152  0.3069  405  ASP B CB  
17453 C CG  . ASP C 405  ? 1.7609 1.0653 1.2104 0.3602  0.5215  0.3359  405  ASP B CG  
17454 O OD1 . ASP C 405  ? 1.7818 1.1205 1.2583 0.3650  0.5087  0.3489  405  ASP B OD1 
17455 O OD2 . ASP C 405  ? 1.7912 1.0692 1.2313 0.3705  0.5378  0.3462  405  ASP B OD2 
17456 N N   . PRO C 406  ? 1.4167 0.7683 0.8602 0.3169  0.4745  0.2754  406  PRO B N   
17457 C CA  . PRO C 406  ? 1.3984 0.7664 0.8406 0.3029  0.4568  0.2553  406  PRO B CA  
17458 C C   . PRO C 406  ? 1.4443 0.8145 0.8819 0.2897  0.4501  0.2437  406  PRO B C   
17459 O O   . PRO C 406  ? 1.5077 0.8841 0.9547 0.2920  0.4478  0.2563  406  PRO B O   
17460 C CB  . PRO C 406  ? 1.3499 0.7513 0.8195 0.3070  0.4372  0.2683  406  PRO B CB  
17461 C CG  . PRO C 406  ? 1.3837 0.7879 0.8699 0.3224  0.4459  0.2954  406  PRO B CG  
17462 C CD  . PRO C 406  ? 1.4132 0.7905 0.8855 0.3270  0.4655  0.2996  406  PRO B CD  
17463 N N   . SER C 407  ? 1.4667 0.8337 0.8901 0.2761  0.4468  0.2205  407  SER B N   
17464 C CA  . SER C 407  ? 1.5061 0.8782 0.9256 0.2629  0.4422  0.2093  407  SER B CA  
17465 C C   . SER C 407  ? 1.4862 0.8900 0.9170 0.2569  0.4200  0.1971  407  SER B C   
17466 O O   . SER C 407  ? 1.4816 0.8951 0.9177 0.2603  0.4105  0.1941  407  SER B O   
17467 C CB  . SER C 407  ? 1.5614 0.9068 0.9580 0.2514  0.4559  0.1927  407  SER B CB  
17468 O OG  . SER C 407  ? 1.6104 0.9295 0.9946 0.2606  0.4697  0.1960  407  SER B OG  
17469 N N   . LYS C 408  ? 1.4544 0.8738 0.8881 0.2494  0.4117  0.1912  408  LYS B N   
17470 C CA  . LYS C 408  ? 1.3914 0.8393 0.8334 0.2450  0.3912  0.1776  408  LYS B CA  
17471 C C   . LYS C 408  ? 1.3416 0.7967 0.7759 0.2323  0.3932  0.1623  408  LYS B C   
17472 O O   . LYS C 408  ? 1.3576 0.8048 0.7865 0.2292  0.4037  0.1692  408  LYS B O   
17473 C CB  . LYS C 408  ? 1.3733 0.8409 0.8318 0.2539  0.3740  0.1905  408  LYS B CB  
17474 C CG  . LYS C 408  ? 1.3930 0.8859 0.8572 0.2512  0.3523  0.1757  408  LYS B CG  
17475 C CD  . LYS C 408  ? 1.4314 0.9377 0.9103 0.2603  0.3331  0.1890  408  LYS B CD  
17476 C CE  . LYS C 408  ? 1.4576 0.9539 0.9476 0.2691  0.3378  0.2123  408  LYS B CE  
17477 N NZ  . LYS C 408  ? 1.4524 0.9631 0.9602 0.2754  0.3157  0.2240  408  LYS B NZ  
17478 N N   . SER C 409  ? 1.2923 0.7629 0.7263 0.2247  0.3839  0.1424  409  SER B N   
17479 C CA  . SER C 409  ? 1.3172 0.8031 0.7485 0.2132  0.3843  0.1286  409  SER B CA  
17480 C C   . SER C 409  ? 1.2744 0.7905 0.7156 0.2164  0.3631  0.1161  409  SER B C   
17481 O O   . SER C 409  ? 1.2213 0.7423 0.6707 0.2268  0.3486  0.1213  409  SER B O   
17482 C CB  . SER C 409  ? 1.3699 0.8424 0.7898 0.1982  0.3974  0.1150  409  SER B CB  
17483 O OG  . SER C 409  ? 1.2789 0.7726 0.7004 0.1858  0.3971  0.1020  409  SER B OG  
17484 N N   . VAL C 410  ? 1.2541 0.7909 0.6955 0.2076  0.3612  0.1004  410  VAL B N   
17485 C CA  . VAL C 410  ? 1.2632 0.8281 0.7130 0.2122  0.3418  0.0870  410  VAL B CA  
17486 C C   . VAL C 410  ? 1.3210 0.9024 0.7716 0.2011  0.3421  0.0667  410  VAL B C   
17487 O O   . VAL C 410  ? 1.3437 0.9212 0.7897 0.1875  0.3570  0.0629  410  VAL B O   
17488 C CB  . VAL C 410  ? 1.2635 0.8463 0.7158 0.2190  0.3339  0.0900  410  VAL B CB  
17489 C CG1 . VAL C 410  ? 1.2809 0.8893 0.7400 0.2259  0.3130  0.0745  410  VAL B CG1 
17490 C CG2 . VAL C 410  ? 1.2561 0.8230 0.7091 0.2292  0.3313  0.1109  410  VAL B CG2 
17491 N N   . THR C 411  ? 1.3189 0.9182 0.7762 0.2066  0.3244  0.0543  411  THR B N   
17492 C CA  . THR C 411  ? 1.3062 0.9189 0.7656 0.1979  0.3218  0.0362  411  THR B CA  
17493 C C   . THR C 411  ? 1.2651 0.9087 0.7308 0.1922  0.3240  0.0257  411  THR B C   
17494 O O   . THR C 411  ? 1.2162 0.8782 0.6858 0.2024  0.3149  0.0253  411  THR B O   
17495 C CB  . THR C 411  ? 1.3157 0.9349 0.7795 0.2081  0.3013  0.0291  411  THR B CB  
17496 O OG1 . THR C 411  ? 1.3529 0.9818 0.8172 0.2000  0.2982  0.0128  411  THR B OG1 
17497 C CG2 . THR C 411  ? 1.2845 0.9266 0.7559 0.2199  0.2844  0.0249  411  THR B CG2 
17498 N N   . ARG C 412  ? 1.3446 0.9931 0.8105 0.1757  0.3363  0.0181  412  ARG B N   
17499 C CA  . ARG C 412  ? 1.4612 1.1425 0.9352 0.1684  0.3413  0.0104  412  ARG B CA  
17500 C C   . ARG C 412  ? 1.4634 1.1823 0.9490 0.1792  0.3238  -0.0044 412  ARG B C   
17501 O O   . ARG C 412  ? 1.4798 1.1971 0.9671 0.1885  0.3077  -0.0104 412  ARG B O   
17502 C CB  . ARG C 412  ? 1.6013 1.2832 1.0768 0.1467  0.3546  0.0041  412  ARG B CB  
17503 C CG  . ARG C 412  ? 1.7281 1.4453 1.2137 0.1375  0.3628  0.0000  412  ARG B CG  
17504 C CD  . ARG C 412  ? 1.8553 1.5716 1.3442 0.1130  0.3754  -0.0041 412  ARG B CD  
17505 N NE  . ARG C 412  ? 1.9660 1.6554 1.4441 0.1013  0.3949  0.0109  412  ARG B NE  
17506 C CZ  . ARG C 412  ? 2.0546 1.7385 1.5339 0.0784  0.4073  0.0104  412  ARG B CZ  
17507 N NH1 . ARG C 412  ? 2.0727 1.7788 1.5648 0.0642  0.4017  -0.0047 412  ARG B NH1 
17508 N NH2 . ARG C 412  ? 2.1005 1.7562 1.5684 0.0691  0.4243  0.0253  412  ARG B NH2 
17509 N N   . VAL C 413  ? 1.4789 1.2312 0.9716 0.1790  0.3272  -0.0097 413  VAL B N   
17510 C CA  . VAL C 413  ? 1.4944 1.2819 0.9966 0.1932  0.3111  -0.0235 413  VAL B CA  
17511 C C   . VAL C 413  ? 1.5041 1.3224 1.0213 0.1855  0.3066  -0.0406 413  VAL B C   
17512 O O   . VAL C 413  ? 1.5014 1.3346 1.0249 0.1975  0.2888  -0.0522 413  VAL B O   
17513 C CB  . VAL C 413  ? 1.5175 1.3293 1.0187 0.2001  0.3169  -0.0219 413  VAL B CB  
17514 C CG1 . VAL C 413  ? 1.5128 1.3530 1.0188 0.2201  0.2987  -0.0356 413  VAL B CG1 
17515 C CG2 . VAL C 413  ? 1.5372 1.3190 1.0231 0.2041  0.3235  -0.0036 413  VAL B CG2 
17516 N N   . ASP C 414  ? 1.5296 1.3575 1.0529 0.1650  0.3221  -0.0413 414  ASP B N   
17517 C CA  . ASP C 414  ? 1.5336 1.3941 1.0739 0.1537  0.3193  -0.0559 414  ASP B CA  
17518 C C   . ASP C 414  ? 1.4941 1.3273 1.0296 0.1435  0.3140  -0.0591 414  ASP B C   
17519 O O   . ASP C 414  ? 1.4855 1.3395 1.0326 0.1357  0.3066  -0.0718 414  ASP B O   
17520 C CB  . ASP C 414  ? 1.6013 1.4796 1.1499 0.1323  0.3390  -0.0525 414  ASP B CB  
17521 C CG  . ASP C 414  ? 1.6616 1.4945 1.1945 0.1165  0.3551  -0.0378 414  ASP B CG  
17522 O OD1 . ASP C 414  ? 1.6803 1.4920 1.2000 0.1242  0.3628  -0.0239 414  ASP B OD1 
17523 O OD2 . ASP C 414  ? 1.6884 1.5051 1.2211 0.0974  0.3590  -0.0403 414  ASP B OD2 
17524 N N   . ASP C 415  ? 1.4767 1.2636 0.9942 0.1436  0.3189  -0.0470 415  ASP B N   
17525 C CA  . ASP C 415  ? 1.4850 1.2392 0.9924 0.1310  0.3213  -0.0472 415  ASP B CA  
17526 C C   . ASP C 415  ? 1.3686 1.1042 0.8676 0.1459  0.3052  -0.0486 415  ASP B C   
17527 O O   . ASP C 415  ? 1.3438 1.0723 0.8393 0.1405  0.2979  -0.0572 415  ASP B O   
17528 C CB  . ASP C 415  ? 1.5944 1.3092 1.0866 0.1221  0.3404  -0.0313 415  ASP B CB  
17529 C CG  . ASP C 415  ? 1.7013 1.3833 1.1818 0.1054  0.3470  -0.0332 415  ASP B CG  
17530 O OD1 . ASP C 415  ? 1.7454 1.4358 1.2287 0.1012  0.3353  -0.0468 415  ASP B OD1 
17531 O OD2 . ASP C 415  ? 1.7267 1.3735 1.1938 0.0975  0.3630  -0.0216 415  ASP B OD2 
17532 N N   . GLY C 416  ? 1.3087 1.0370 0.8040 0.1642  0.2991  -0.0398 416  GLY B N   
17533 C CA  . GLY C 416  ? 1.2886 0.9932 0.7750 0.1775  0.2870  -0.0351 416  GLY B CA  
17534 C C   . GLY C 416  ? 1.3306 0.9919 0.8007 0.1722  0.3001  -0.0218 416  GLY B C   
17535 O O   . GLY C 416  ? 1.3806 1.0201 0.8425 0.1818  0.2940  -0.0148 416  GLY B O   
17536 N N   . VAL C 417  ? 1.3224 0.9704 0.7874 0.1575  0.3186  -0.0176 417  VAL B N   
17537 C CA  . VAL C 417  ? 1.3421 0.9474 0.7898 0.1529  0.3316  -0.0075 417  VAL B CA  
17538 C C   . VAL C 417  ? 1.3273 0.9107 0.7695 0.1596  0.3438  0.0118  417  VAL B C   
17539 O O   . VAL C 417  ? 1.3187 0.9139 0.7665 0.1574  0.3508  0.0170  417  VAL B O   
17540 C CB  . VAL C 417  ? 1.4241 1.0192 0.8662 0.1318  0.3440  -0.0146 417  VAL B CB  
17541 C CG1 . VAL C 417  ? 1.4501 0.9988 0.8733 0.1289  0.3612  -0.0017 417  VAL B CG1 
17542 C CG2 . VAL C 417  ? 1.4534 1.0580 0.8952 0.1239  0.3321  -0.0323 417  VAL B CG2 
17543 N N   . ALA C 418  ? 1.3474 0.9001 0.7787 0.1680  0.3469  0.0233  418  ALA B N   
17544 C CA  . ALA C 418  ? 1.3734 0.9043 0.8002 0.1739  0.3594  0.0425  418  ALA B CA  
17545 C C   . ALA C 418  ? 1.4083 0.9015 0.8183 0.1660  0.3772  0.0467  418  ALA B C   
17546 O O   . ALA C 418  ? 1.4111 0.8818 0.8103 0.1721  0.3786  0.0495  418  ALA B O   
17547 C CB  . ALA C 418  ? 1.3743 0.9012 0.8043 0.1913  0.3497  0.0550  418  ALA B CB  
17548 N N   . SER C 419  ? 1.4429 0.9278 0.8492 0.1530  0.3912  0.0477  419  SER B N   
17549 C CA  . SER C 419  ? 1.4902 0.9355 0.8782 0.1432  0.4072  0.0486  419  SER B CA  
17550 C C   . SER C 419  ? 1.4592 0.8701 0.8368 0.1537  0.4220  0.0685  419  SER B C   
17551 O O   . SER C 419  ? 1.4598 0.8754 0.8437 0.1577  0.4268  0.0819  419  SER B O   
17552 C CB  . SER C 419  ? 1.5490 0.9981 0.9376 0.1216  0.4151  0.0406  419  SER B CB  
17553 O OG  . SER C 419  ? 1.5480 1.0426 0.9549 0.1149  0.4036  0.0287  419  SER B OG  
17554 N N   . PHE C 420  ? 1.4703 0.8470 0.8312 0.1591  0.4295  0.0707  420  PHE B N   
17555 C CA  . PHE C 420  ? 1.5324 0.8750 0.8830 0.1686  0.4459  0.0889  420  PHE B CA  
17556 C C   . PHE C 420  ? 1.6622 0.9604 0.9901 0.1584  0.4625  0.0858  420  PHE B C   
17557 O O   . PHE C 420  ? 1.7256 1.0177 1.0451 0.1410  0.4608  0.0689  420  PHE B O   
17558 C CB  . PHE C 420  ? 1.4844 0.8189 0.8334 0.1884  0.4454  0.0998  420  PHE B CB  
17559 C CG  . PHE C 420  ? 1.3535 0.7225 0.7229 0.1988  0.4301  0.1065  420  PHE B CG  
17560 C CD1 . PHE C 420  ? 1.3429 0.7127 0.7219 0.2142  0.4320  0.1273  420  PHE B CD1 
17561 C CD2 . PHE C 420  ? 1.3309 0.7313 0.7106 0.1934  0.4127  0.0922  420  PHE B CD2 
17562 C CE1 . PHE C 420  ? 1.3370 0.7364 0.7345 0.2225  0.4157  0.1333  420  PHE B CE1 
17563 C CE2 . PHE C 420  ? 1.3467 0.7747 0.7433 0.2034  0.3972  0.0976  420  PHE B CE2 
17564 C CZ  . PHE C 420  ? 1.3254 0.7517 0.7304 0.2172  0.3982  0.1181  420  PHE B CZ  
17565 N N   . VAL C 421  ? 1.6177 0.8846 0.9363 0.1696  0.4773  0.1027  421  VAL B N   
17566 C CA  . VAL C 421  ? 1.6002 0.8168 0.8932 0.1665  0.4930  0.1013  421  VAL B CA  
17567 C C   . VAL C 421  ? 1.6108 0.8030 0.8989 0.1874  0.5064  0.1222  421  VAL B C   
17568 O O   . VAL C 421  ? 1.6244 0.8311 0.9274 0.1949  0.5075  0.1392  421  VAL B O   
17569 C CB  . VAL C 421  ? 1.5786 0.7793 0.8659 0.1459  0.5003  0.0981  421  VAL B CB  
17570 C CG1 . VAL C 421  ? 1.6108 0.7573 0.8761 0.1514  0.5191  0.1094  421  VAL B CG1 
17571 C CG2 . VAL C 421  ? 1.5696 0.7730 0.8513 0.1236  0.4925  0.0753  421  VAL B CG2 
17572 N N   . LEU C 422  ? 1.6226 0.7785 0.8890 0.1976  0.5163  0.1206  422  LEU B N   
17573 C CA  . LEU C 422  ? 1.6609 0.7910 0.9210 0.2188  0.5314  0.1399  422  LEU B CA  
17574 C C   . LEU C 422  ? 1.7441 0.8182 0.9732 0.2148  0.5464  0.1334  422  LEU B C   
17575 O O   . LEU C 422  ? 1.7762 0.8315 0.9859 0.2019  0.5437  0.1133  422  LEU B O   
17576 C CB  . LEU C 422  ? 1.6272 0.7691 0.8913 0.2401  0.5306  0.1470  422  LEU B CB  
17577 C CG  . LEU C 422  ? 1.5283 0.7012 0.7991 0.2371  0.5146  0.1345  422  LEU B CG  
17578 C CD1 . LEU C 422  ? 1.5636 0.7067 0.8051 0.2301  0.5171  0.1143  422  LEU B CD1 
17579 C CD2 . LEU C 422  ? 1.5047 0.6989 0.7906 0.2578  0.5133  0.1512  422  LEU B CD2 
17580 N N   . ASN C 423  ? 1.8112 0.8574 1.0352 0.2254  0.5608  0.1502  423  ASN B N   
17581 C CA  . ASN C 423  ? 1.8788 0.8651 1.0715 0.2228  0.5755  0.1456  423  ASN B CA  
17582 C C   . ASN C 423  ? 1.8854 0.8387 1.0576 0.2481  0.5891  0.1499  423  ASN B C   
17583 O O   . ASN C 423  ? 1.8596 0.8198 1.0430 0.2713  0.5973  0.1704  423  ASN B O   
17584 C CB  . ASN C 423  ? 1.8721 0.8429 1.0677 0.2164  0.5828  0.1595  423  ASN B CB  
17585 C CG  . ASN C 423  ? 1.8445 0.8547 1.0610 0.1938  0.5703  0.1562  423  ASN B CG  
17586 O OD1 . ASN C 423  ? 1.8772 0.8710 1.0850 0.1711  0.5707  0.1475  423  ASN B OD1 
17587 N ND2 . ASN C 423  ? 1.7777 0.8416 1.0219 0.1995  0.5582  0.1620  423  ASN B ND2 
17588 N N   . LEU C 424  ? 1.9238 0.8434 1.0660 0.2440  0.5910  0.1303  424  LEU B N   
17589 C CA  . LEU C 424  ? 1.9539 0.8527 1.0766 0.2686  0.6018  0.1313  424  LEU B CA  
17590 C C   . LEU C 424  ? 2.0381 0.8714 1.1264 0.2830  0.6212  0.1328  424  LEU B C   
17591 O O   . LEU C 424  ? 2.0826 0.8681 1.1423 0.2675  0.6228  0.1171  424  LEU B O   
17592 C CB  . LEU C 424  ? 1.9404 0.8512 1.0519 0.2619  0.5907  0.1109  424  LEU B CB  
17593 C CG  . LEU C 424  ? 1.8811 0.8550 1.0275 0.2669  0.5783  0.1203  424  LEU B CG  
17594 C CD1 . LEU C 424  ? 1.8976 0.8825 1.0323 0.2704  0.5712  0.1073  424  LEU B CD1 
17595 C CD2 . LEU C 424  ? 1.8561 0.8455 1.0228 0.2920  0.5887  0.1474  424  LEU B CD2 
17596 N N   . PRO C 425  ? 2.0418 0.8730 1.1336 0.3131  0.6356  0.1522  425  PRO B N   
17597 C CA  . PRO C 425  ? 2.1448 0.9163 1.2066 0.3316  0.6550  0.1564  425  PRO B CA  
17598 C C   . PRO C 425  ? 2.2695 0.9908 1.2861 0.3288  0.6583  0.1313  425  PRO B C   
17599 O O   . PRO C 425  ? 2.3214 1.0524 1.3281 0.3426  0.6601  0.1259  425  PRO B O   
17600 C CB  . PRO C 425  ? 2.1165 0.9114 1.1946 0.3654  0.6671  0.1789  425  PRO B CB  
17601 C CG  . PRO C 425  ? 2.0165 0.8817 1.1405 0.3593  0.6523  0.1923  425  PRO B CG  
17602 C CD  . PRO C 425  ? 1.9775 0.8620 1.1014 0.3317  0.6338  0.1707  425  PRO B CD  
17603 N N   . SER C 426  ? 2.3366 1.0049 1.3254 0.3107  0.6582  0.1168  426  SER B N   
17604 C CA  . SER C 426  ? 2.4354 1.0473 1.3765 0.3073  0.6600  0.0918  426  SER B CA  
17605 C C   . SER C 426  ? 2.5426 1.1511 1.4612 0.3348  0.6689  0.0868  426  SER B C   
17606 O O   . SER C 426  ? 2.5195 1.1312 1.4207 0.3253  0.6588  0.0667  426  SER B O   
17607 C CB  . SER C 426  ? 2.5330 1.0701 1.4418 0.3069  0.6712  0.0897  426  SER B CB  
17608 O OG  . SER C 426  ? 2.5367 1.0772 1.4671 0.3203  0.6817  0.1158  426  SER B OG  
17609 N N   . GLY C 427  ? 2.5670 1.1723 1.4871 0.3691  0.6876  0.1061  427  GLY B N   
17610 C CA  . GLY C 427  ? 2.5940 1.2029 1.4967 0.3969  0.6984  0.1054  427  GLY B CA  
17611 C C   . GLY C 427  ? 2.5097 1.1880 1.4423 0.3966  0.6881  0.1105  427  GLY B C   
17612 O O   . GLY C 427  ? 2.5049 1.2032 1.4396 0.4233  0.6996  0.1221  427  GLY B O   
17613 N N   . VAL C 428  ? 2.4276 1.1435 1.3838 0.3669  0.6666  0.1028  428  VAL B N   
17614 C CA  . VAL C 428  ? 2.3290 1.1064 1.3119 0.3655  0.6549  0.1068  428  VAL B CA  
17615 C C   . VAL C 428  ? 2.3217 1.0840 1.2702 0.3563  0.6462  0.0811  428  VAL B C   
17616 O O   . VAL C 428  ? 2.3725 1.0856 1.2856 0.3417  0.6430  0.0589  428  VAL B O   
17617 C CB  . VAL C 428  ? 2.2721 1.1000 1.2984 0.3414  0.6358  0.1120  428  VAL B CB  
17618 C CG1 . VAL C 428  ? 2.2918 1.1046 1.3045 0.3086  0.6194  0.0868  428  VAL B CG1 
17619 C CG2 . VAL C 428  ? 2.2084 1.0990 1.2666 0.3464  0.6261  0.1227  428  VAL B CG2 
17620 N N   . THR C 429  ? 2.2576 1.0638 1.2184 0.3625  0.6400  0.0846  429  THR B N   
17621 C CA  . THR C 429  ? 2.2475 1.0387 1.1706 0.3678  0.6391  0.0674  429  THR B CA  
17622 C C   . THR C 429  ? 2.1427 0.9851 1.0850 0.3528  0.6179  0.0622  429  THR B C   
17623 O O   . THR C 429  ? 2.1022 0.9392 1.0307 0.3297  0.6002  0.0396  429  THR B O   
17624 C CB  . THR C 429  ? 2.3997 1.1892 1.3117 0.4045  0.6620  0.0843  429  THR B CB  
17625 O OG1 . THR C 429  ? 2.3489 1.2011 1.3099 0.4133  0.6612  0.1111  429  THR B OG1 
17626 C CG2 . THR C 429  ? 2.4462 1.1870 1.3400 0.4245  0.6843  0.0913  429  THR B CG2 
17627 N N   . VAL C 430  ? 2.0697 0.9599 1.0424 0.3682  0.6206  0.0841  430  VAL B N   
17628 C CA  . VAL C 430  ? 1.9747 0.9198 0.9780 0.3567  0.6011  0.0874  430  VAL B CA  
17629 C C   . VAL C 430  ? 1.9580 0.9429 1.0126 0.3534  0.5971  0.1089  430  VAL B C   
17630 O O   . VAL C 430  ? 1.9563 0.9447 1.0264 0.3728  0.6130  0.1312  430  VAL B O   
17631 C CB  . VAL C 430  ? 1.9131 0.8808 0.9134 0.3779  0.6082  0.1002  430  VAL B CB  
17632 C CG1 . VAL C 430  ? 1.8350 0.8515 0.8597 0.3645  0.5859  0.1003  430  VAL B CG1 
17633 C CG2 . VAL C 430  ? 1.9613 0.8845 0.9074 0.3903  0.6201  0.0849  430  VAL B CG2 
17634 N N   . LEU C 431  ? 1.9124 0.9263 0.9914 0.3292  0.5754  0.1012  431  LEU B N   
17635 C CA  . LEU C 431  ? 1.7953 0.8563 0.9221 0.3236  0.5647  0.1180  431  LEU B CA  
17636 C C   . LEU C 431  ? 1.7732 0.8798 0.9189 0.3205  0.5470  0.1198  431  LEU B C   
17637 O O   . LEU C 431  ? 1.6517 0.7589 0.7820 0.3076  0.5331  0.1002  431  LEU B O   
17638 C CB  . LEU C 431  ? 1.7304 0.7876 0.8658 0.2992  0.5538  0.1057  431  LEU B CB  
17639 C CG  . LEU C 431  ? 1.6649 0.7575 0.8405 0.2895  0.5440  0.1174  431  LEU B CG  
17640 C CD1 . LEU C 431  ? 1.6196 0.7247 0.7983 0.2633  0.5252  0.0966  431  LEU B CD1 
17641 C CD2 . LEU C 431  ? 1.6150 0.7541 0.8247 0.3008  0.5373  0.1379  431  LEU B CD2 
17642 N N   . GLU C 432  ? 1.7212 0.8645 0.8999 0.3319  0.5463  0.1435  432  GLU B N   
17643 C CA  . GLU C 432  ? 1.6994 0.8839 0.8986 0.3277  0.5278  0.1468  432  GLU B CA  
17644 C C   . GLU C 432  ? 1.6744 0.8971 0.9150 0.3159  0.5097  0.1543  432  GLU B C   
17645 O O   . GLU C 432  ? 1.7026 0.9401 0.9694 0.3244  0.5146  0.1755  432  GLU B O   
17646 C CB  . GLU C 432  ? 1.7086 0.9069 0.9129 0.3491  0.5389  0.1690  432  GLU B CB  
17647 C CG  . GLU C 432  ? 1.8110 0.9775 0.9728 0.3629  0.5555  0.1619  432  GLU B CG  
17648 C CD  . GLU C 432  ? 1.8522 1.0248 0.9943 0.3562  0.5416  0.1476  432  GLU B CD  
17649 O OE1 . GLU C 432  ? 1.7788 0.9816 0.9423 0.3415  0.5187  0.1436  432  GLU B OE1 
17650 O OE2 . GLU C 432  ? 1.9355 1.0810 1.0385 0.3670  0.5540  0.1401  432  GLU B OE2 
17651 N N   . PHE C 433  ? 1.6020 0.8421 0.8490 0.2979  0.4887  0.1379  433  PHE B N   
17652 C CA  . PHE C 433  ? 1.5424 0.8178 0.8261 0.2903  0.4726  0.1455  433  PHE B CA  
17653 C C   . PHE C 433  ? 1.5674 0.8793 0.8715 0.2876  0.4506  0.1476  433  PHE B C   
17654 O O   . PHE C 433  ? 1.5980 0.9119 0.8882 0.2834  0.4407  0.1343  433  PHE B O   
17655 C CB  . PHE C 433  ? 1.4959 0.7663 0.7824 0.2738  0.4687  0.1323  433  PHE B CB  
17656 C CG  . PHE C 433  ? 1.5040 0.7655 0.7714 0.2567  0.4598  0.1055  433  PHE B CG  
17657 C CD1 . PHE C 433  ? 1.5482 0.7700 0.7819 0.2536  0.4719  0.0918  433  PHE B CD1 
17658 C CD2 . PHE C 433  ? 1.4321 0.7244 0.7157 0.2436  0.4387  0.0939  433  PHE B CD2 
17659 C CE1 . PHE C 433  ? 1.5224 0.7370 0.7402 0.2359  0.4619  0.0674  433  PHE B CE1 
17660 C CE2 . PHE C 433  ? 1.4447 0.7332 0.7145 0.2277  0.4300  0.0703  433  PHE B CE2 
17661 C CZ  . PHE C 433  ? 1.4894 0.7398 0.7271 0.2228  0.4410  0.0573  433  PHE B CZ  
17662 N N   . ASN C 434  ? 1.5557 0.8942 0.8919 0.2909  0.4428  0.1655  434  ASN B N   
17663 C CA  . ASN C 434  ? 1.5238 0.8948 0.8826 0.2867  0.4193  0.1674  434  ASN B CA  
17664 C C   . ASN C 434  ? 1.5588 0.9447 0.9342 0.2755  0.4064  0.1595  434  ASN B C   
17665 O O   . ASN C 434  ? 1.5759 0.9548 0.9562 0.2751  0.4161  0.1649  434  ASN B O   
17666 C CB  . ASN C 434  ? 1.4505 0.8396 0.8337 0.2984  0.4184  0.1945  434  ASN B CB  
17667 C CG  . ASN C 434  ? 1.4547 0.8336 0.8254 0.3117  0.4345  0.2073  434  ASN B CG  
17668 O OD1 . ASN C 434  ? 1.4271 0.8035 0.7809 0.3119  0.4308  0.1999  434  ASN B OD1 
17669 N ND2 . ASN C 434  ? 1.4625 0.8372 0.8414 0.3243  0.4526  0.2277  434  ASN B ND2 
17670 N N   . VAL C 435  ? 1.5420 0.9493 0.9265 0.2679  0.3848  0.1482  435  VAL B N   
17671 C CA  . VAL C 435  ? 1.5383 0.9589 0.9327 0.2575  0.3745  0.1362  435  VAL B CA  
17672 C C   . VAL C 435  ? 1.4654 0.9128 0.8799 0.2589  0.3512  0.1390  435  VAL B C   
17673 O O   . VAL C 435  ? 1.5282 0.9814 0.9395 0.2601  0.3397  0.1347  435  VAL B O   
17674 C CB  . VAL C 435  ? 1.3002 0.7145 0.6766 0.2450  0.3730  0.1107  435  VAL B CB  
17675 C CG1 . VAL C 435  ? 1.2776 0.7188 0.6673 0.2372  0.3531  0.0970  435  VAL B CG1 
17676 C CG2 . VAL C 435  ? 1.3230 0.7145 0.6863 0.2384  0.3910  0.1059  435  VAL B CG2 
17677 N N   . LYS C 436  ? 1.3921 0.8540 0.8255 0.2593  0.3433  0.1466  436  LYS B N   
17678 C CA  . LYS C 436  ? 1.3420 0.8255 0.7912 0.2606  0.3191  0.1465  436  LYS B CA  
17679 C C   . LYS C 436  ? 1.3378 0.8373 0.7972 0.2566  0.3075  0.1385  436  LYS B C   
17680 O O   . LYS C 436  ? 1.3666 0.8622 0.8239 0.2532  0.3194  0.1381  436  LYS B O   
17681 C CB  . LYS C 436  ? 1.2609 0.7479 0.7254 0.2695  0.3139  0.1705  436  LYS B CB  
17682 C CG  . LYS C 436  ? 1.2043 0.6946 0.6855 0.2737  0.3174  0.1899  436  LYS B CG  
17683 C CD  . LYS C 436  ? 1.4193 0.9241 0.9223 0.2776  0.2967  0.2062  436  LYS B CD  
17684 C CE  . LYS C 436  ? 1.4859 0.9931 1.0076 0.2839  0.3033  0.2341  436  LYS B CE  
17685 N NZ  . LYS C 436  ? 1.4701 0.9764 0.9993 0.2907  0.3138  0.2558  436  LYS B NZ  
17686 N N   . THR C 437  ? 1.3137 0.8295 0.7818 0.2579  0.2844  0.1320  437  THR B N   
17687 C CA  . THR C 437  ? 1.3497 0.8813 0.8272 0.2579  0.2702  0.1263  437  THR B CA  
17688 C C   . THR C 437  ? 1.3238 0.8561 0.8156 0.2639  0.2637  0.1471  437  THR B C   
17689 O O   . THR C 437  ? 1.3048 0.8340 0.8057 0.2683  0.2572  0.1632  437  THR B O   
17690 C CB  . THR C 437  ? 1.1762 0.7222 0.6566 0.2596  0.2467  0.1118  437  THR B CB  
17691 O OG1 . THR C 437  ? 1.1666 0.7080 0.6519 0.2645  0.2344  0.1228  437  THR B OG1 
17692 C CG2 . THR C 437  ? 1.1722 0.7247 0.6423 0.2536  0.2491  0.0895  437  THR B CG2 
17693 N N   . ASP C 438  ? 1.4151 0.9526 0.9090 0.2634  0.2648  0.1473  438  ASP B N   
17694 C CA  . ASP C 438  ? 1.5301 1.0703 1.0370 0.2686  0.2536  0.1645  438  ASP B CA  
17695 C C   . ASP C 438  ? 1.5126 1.0652 1.0221 0.2710  0.2300  0.1547  438  ASP B C   
17696 O O   . ASP C 438  ? 1.4933 1.0480 1.0067 0.2735  0.2242  0.1632  438  ASP B O   
17697 C CB  . ASP C 438  ? 1.6161 1.1487 1.1243 0.2693  0.2715  0.1805  438  ASP B CB  
17698 C CG  . ASP C 438  ? 1.7044 1.2334 1.2280 0.2749  0.2709  0.2062  438  ASP B CG  
17699 O OD1 . ASP C 438  ? 1.7193 1.2506 1.2513 0.2764  0.2594  0.2115  438  ASP B OD1 
17700 O OD2 . ASP C 438  ? 1.7404 1.2656 1.2683 0.2776  0.2820  0.2218  438  ASP B OD2 
17701 N N   . ALA C 439  ? 1.5318 1.0913 1.0376 0.2714  0.2158  0.1369  439  ALA B N   
17702 C CA  . ALA C 439  ? 1.5690 1.1357 1.0771 0.2766  0.1900  0.1293  439  ALA B CA  
17703 C C   . ALA C 439  ? 1.5758 1.1372 1.0945 0.2796  0.1781  0.1491  439  ALA B C   
17704 O O   . ALA C 439  ? 1.6153 1.1698 1.1457 0.2791  0.1762  0.1681  439  ALA B O   
17705 C CB  . ALA C 439  ? 1.5880 1.1542 1.0972 0.2787  0.1736  0.1212  439  ALA B CB  
17706 N N   . PRO C 440  ? 1.5647 1.1306 1.0790 0.2827  0.1696  0.1450  440  PRO B N   
17707 C CA  . PRO C 440  ? 1.5097 1.0711 1.0324 0.2846  0.1590  0.1635  440  PRO B CA  
17708 C C   . PRO C 440  ? 1.4764 1.0327 1.0062 0.2873  0.1292  0.1651  440  PRO B C   
17709 O O   . PRO C 440  ? 1.4732 1.0244 1.0160 0.2863  0.1175  0.1845  440  PRO B O   
17710 C CB  . PRO C 440  ? 1.5293 1.0970 1.0386 0.2876  0.1594  0.1533  440  PRO B CB  
17711 C CG  . PRO C 440  ? 1.6161 1.1949 1.1123 0.2872  0.1694  0.1280  440  PRO B CG  
17712 C CD  . PRO C 440  ? 1.5919 1.1690 1.0934 0.2859  0.1652  0.1218  440  PRO B CD  
17713 N N   . ASP C 441  ? 1.4523 1.0099 0.9741 0.2904  0.1171  0.1451  441  ASP B N   
17714 C CA  . ASP C 441  ? 1.4853 1.0344 1.0095 0.2939  0.0874  0.1420  441  ASP B CA  
17715 C C   . ASP C 441  ? 1.4351 0.9798 0.9665 0.2910  0.0866  0.1460  441  ASP B C   
17716 O O   . ASP C 441  ? 1.4290 0.9643 0.9635 0.2927  0.0633  0.1464  441  ASP B O   
17717 C CB  . ASP C 441  ? 1.6021 1.1560 1.1103 0.3020  0.0758  0.1156  441  ASP B CB  
17718 C CG  . ASP C 441  ? 1.7026 1.2700 1.2040 0.3018  0.0945  0.0981  441  ASP B CG  
17719 O OD1 . ASP C 441  ? 1.7770 1.3491 1.2712 0.3084  0.0831  0.0784  441  ASP B OD1 
17720 O OD2 . ASP C 441  ? 1.6897 1.2621 1.1933 0.2951  0.1199  0.1044  441  ASP B OD2 
17721 N N   . LEU C 442  ? 1.4049 0.9542 0.9364 0.2870  0.1112  0.1483  442  LEU B N   
17722 C CA  . LEU C 442  ? 1.3582 0.9021 0.8958 0.2843  0.1119  0.1573  442  LEU B CA  
17723 C C   . LEU C 442  ? 1.3579 0.8975 0.9122 0.2803  0.1166  0.1865  442  LEU B C   
17724 O O   . LEU C 442  ? 1.3772 0.9204 0.9359 0.2789  0.1350  0.1979  442  LEU B O   
17725 C CB  . LEU C 442  ? 1.2765 0.8251 0.8040 0.2824  0.1338  0.1459  442  LEU B CB  
17726 C CG  . LEU C 442  ? 1.2245 0.7757 0.7430 0.2862  0.1190  0.1244  442  LEU B CG  
17727 C CD1 . LEU C 442  ? 1.2085 0.7624 0.7188 0.2833  0.1350  0.1162  442  LEU B CD1 
17728 C CD2 . LEU C 442  ? 1.1934 0.7338 0.7184 0.2890  0.0915  0.1321  442  LEU B CD2 
17729 N N   . PRO C 443  ? 1.3368 0.8699 0.9015 0.2785  0.1004  0.1997  443  PRO B N   
17730 C CA  . PRO C 443  ? 1.3542 0.8877 0.9386 0.2744  0.1043  0.2293  443  PRO B CA  
17731 C C   . PRO C 443  ? 1.4604 0.9972 1.0421 0.2742  0.1342  0.2364  443  PRO B C   
17732 O O   . PRO C 443  ? 1.4939 1.0291 1.0588 0.2756  0.1438  0.2186  443  PRO B O   
17733 C CB  . PRO C 443  ? 1.2998 0.8249 0.8921 0.2718  0.0788  0.2373  443  PRO B CB  
17734 C CG  . PRO C 443  ? 1.3057 0.8239 0.8816 0.2762  0.0609  0.2113  443  PRO B CG  
17735 C CD  . PRO C 443  ? 1.3072 0.8332 0.8662 0.2802  0.0808  0.1891  443  PRO B CD  
17736 N N   . GLU C 444  ? 1.5049 1.0465 1.1021 0.2733  0.1486  0.2612  444  GLU B N   
17737 C CA  . GLU C 444  ? 1.5431 1.0854 1.1334 0.2757  0.1796  0.2652  444  GLU B CA  
17738 C C   . GLU C 444  ? 1.4610 0.9980 1.0377 0.2760  0.1845  0.2577  444  GLU B C   
17739 O O   . GLU C 444  ? 1.3979 0.9306 0.9549 0.2772  0.1998  0.2399  444  GLU B O   
17740 C CB  . GLU C 444  ? 1.7144 1.2640 1.3252 0.2770  0.1929  0.2949  444  GLU B CB  
17741 C CG  . GLU C 444  ? 1.8849 1.4328 1.4871 0.2819  0.2238  0.2949  444  GLU B CG  
17742 C CD  . GLU C 444  ? 2.0157 1.5545 1.5966 0.2845  0.2459  0.2847  444  GLU B CD  
17743 O OE1 . GLU C 444  ? 2.0573 1.5937 1.6313 0.2829  0.2379  0.2797  444  GLU B OE1 
17744 O OE2 . GLU C 444  ? 2.0572 1.5893 1.6269 0.2882  0.2704  0.2818  444  GLU B OE2 
17745 N N   . GLU C 445  ? 1.4667 1.0036 1.0536 0.2740  0.1702  0.2720  445  GLU B N   
17746 C CA  . GLU C 445  ? 1.4639 0.9951 1.0374 0.2743  0.1702  0.2675  445  GLU B CA  
17747 C C   . GLU C 445  ? 1.3939 0.9198 0.9435 0.2757  0.1693  0.2367  445  GLU B C   
17748 O O   . GLU C 445  ? 1.3912 0.9142 0.9237 0.2773  0.1893  0.2274  445  GLU B O   
17749 C CB  . GLU C 445  ? 1.5454 1.0739 1.1307 0.2706  0.1431  0.2792  445  GLU B CB  
17750 C CG  . GLU C 445  ? 1.6416 1.1777 1.2519 0.2673  0.1445  0.3132  445  GLU B CG  
17751 C CD  . GLU C 445  ? 1.7374 1.2680 1.3580 0.2615  0.1171  0.3250  445  GLU B CD  
17752 O OE1 . GLU C 445  ? 1.7648 1.2847 1.3797 0.2603  0.0905  0.3085  445  GLU B OE1 
17753 O OE2 . GLU C 445  ? 1.7679 1.3046 1.4018 0.2586  0.1228  0.3513  445  GLU B OE2 
17754 N N   . ASN C 446  ? 1.3461 0.8710 0.8947 0.2755  0.1451  0.2209  446  ASN B N   
17755 C CA  . ASN C 446  ? 1.3461 0.8705 0.8764 0.2775  0.1404  0.1924  446  ASN B CA  
17756 C C   . ASN C 446  ? 1.3111 0.8411 0.8311 0.2773  0.1583  0.1739  446  ASN B C   
17757 O O   . ASN C 446  ? 1.2923 0.8264 0.8010 0.2781  0.1542  0.1508  446  ASN B O   
17758 C CB  . ASN C 446  ? 1.4061 0.9280 0.9398 0.2794  0.1097  0.1831  446  ASN B CB  
17759 C CG  . ASN C 446  ? 1.4763 0.9902 1.0238 0.2771  0.0913  0.2053  446  ASN B CG  
17760 O OD1 . ASN C 446  ? 1.4752 0.9875 1.0377 0.2750  0.0779  0.2172  446  ASN B OD1 
17761 N ND2 . ASN C 446  ? 1.5352 1.0439 1.0774 0.2767  0.0905  0.2124  446  ASN B ND2 
17762 N N   . GLN C 447  ? 1.2943 0.8251 0.8190 0.2762  0.1784  0.1851  447  GLN B N   
17763 C CA  . GLN C 447  ? 1.2896 0.8217 0.8026 0.2746  0.1990  0.1708  447  GLN B CA  
17764 C C   . GLN C 447  ? 1.2934 0.8198 0.7885 0.2732  0.2141  0.1607  447  GLN B C   
17765 O O   . GLN C 447  ? 1.2711 0.7907 0.7630 0.2748  0.2213  0.1735  447  GLN B O   
17766 C CB  . GLN C 447  ? 1.3770 0.9072 0.8982 0.2750  0.2174  0.1888  447  GLN B CB  
17767 C CG  . GLN C 447  ? 1.4145 0.9506 0.9476 0.2754  0.2069  0.1931  447  GLN B CG  
17768 C CD  . GLN C 447  ? 1.4339 0.9749 0.9560 0.2740  0.2078  0.1705  447  GLN B CD  
17769 O OE1 . GLN C 447  ? 1.4332 0.9740 0.9415 0.2712  0.2191  0.1535  447  GLN B OE1 
17770 N NE2 . GLN C 447  ? 1.4524 0.9986 0.9802 0.2755  0.1952  0.1705  447  GLN B NE2 
17771 N N   . ALA C 448  ? 1.1762 0.7056 0.6592 0.2700  0.2200  0.1386  448  ALA B N   
17772 C CA  . ALA C 448  ? 1.1887 0.7118 0.6536 0.2674  0.2311  0.1272  448  ALA B CA  
17773 C C   . ALA C 448  ? 1.3260 0.8355 0.7790 0.2653  0.2590  0.1316  448  ALA B C   
17774 O O   . ALA C 448  ? 1.2823 0.7905 0.7356 0.2620  0.2713  0.1285  448  ALA B O   
17775 C CB  . ALA C 448  ? 1.1864 0.7207 0.6453 0.2640  0.2217  0.1014  448  ALA B CB  
17776 N N   . ARG C 449  ? 1.3649 0.8623 0.8044 0.2675  0.2690  0.1374  449  ARG B N   
17777 C CA  . ARG C 449  ? 1.3756 0.8557 0.8006 0.2681  0.2955  0.1420  449  ARG B CA  
17778 C C   . ARG C 449  ? 1.4097 0.8755 0.8077 0.2665  0.3041  0.1292  449  ARG B C   
17779 O O   . ARG C 449  ? 1.4244 0.8934 0.8147 0.2670  0.2912  0.1232  449  ARG B O   
17780 C CB  . ARG C 449  ? 1.3912 0.8676 0.8264 0.2761  0.3057  0.1694  449  ARG B CB  
17781 C CG  . ARG C 449  ? 1.4330 0.9178 0.8773 0.2795  0.2895  0.1817  449  ARG B CG  
17782 C CD  . ARG C 449  ? 1.4847 0.9733 0.9476 0.2854  0.2960  0.2104  449  ARG B CD  
17783 N NE  . ARG C 449  ? 1.5057 1.0081 0.9941 0.2835  0.2765  0.2187  449  ARG B NE  
17784 C CZ  . ARG C 449  ? 1.5387 1.0466 1.0468 0.2860  0.2815  0.2383  449  ARG B CZ  
17785 N NH1 . ARG C 449  ? 1.5637 1.0654 1.0697 0.2918  0.3067  0.2511  449  ARG B NH1 
17786 N NH2 . ARG C 449  ? 1.5230 1.0415 1.0514 0.2835  0.2610  0.2443  449  ARG B NH2 
17787 N N   . GLU C 450  ? 1.4533 0.9010 0.8355 0.2650  0.3256  0.1256  450  GLU B N   
17788 C CA  . GLU C 450  ? 1.5034 0.9326 0.8564 0.2626  0.3350  0.1115  450  GLU B CA  
17789 C C   . GLU C 450  ? 1.4994 0.9048 0.8396 0.2671  0.3610  0.1198  450  GLU B C   
17790 O O   . GLU C 450  ? 1.5108 0.9161 0.8650 0.2682  0.3698  0.1298  450  GLU B O   
17791 C CB  . GLU C 450  ? 1.5774 1.0105 0.9240 0.2501  0.3274  0.0855  450  GLU B CB  
17792 C CG  . GLU C 450  ? 1.6584 1.1109 1.0088 0.2475  0.3033  0.0727  450  GLU B CG  
17793 C CD  . GLU C 450  ? 1.7578 1.2010 1.0877 0.2526  0.2999  0.0734  450  GLU B CD  
17794 O OE1 . GLU C 450  ? 1.8176 1.2373 1.1227 0.2542  0.3170  0.0733  450  GLU B OE1 
17795 O OE2 . GLU C 450  ? 1.7568 1.2144 1.0936 0.2558  0.2803  0.0742  450  GLU B OE2 
17796 N N   . GLY C 451  ? 1.5115 0.8952 0.8231 0.2706  0.3729  0.1155  451  GLY B N   
17797 C CA  . GLY C 451  ? 1.5082 0.8648 0.8029 0.2775  0.3983  0.1221  451  GLY B CA  
17798 C C   . GLY C 451  ? 1.5330 0.8618 0.7917 0.2718  0.4051  0.1003  451  GLY B C   
17799 O O   . GLY C 451  ? 1.5696 0.9014 0.8142 0.2664  0.3915  0.0853  451  GLY B O   
17800 N N   . TYR C 452  ? 1.4845 0.7849 0.7277 0.2728  0.4247  0.0984  452  TYR B N   
17801 C CA  . TYR C 452  ? 1.5159 0.7853 0.7249 0.2650  0.4301  0.0766  452  TYR B CA  
17802 C C   . TYR C 452  ? 1.5913 0.8228 0.7763 0.2770  0.4564  0.0835  452  TYR B C   
17803 O O   . TYR C 452  ? 1.5874 0.8221 0.7884 0.2896  0.4694  0.1049  452  TYR B O   
17804 C CB  . TYR C 452  ? 1.4881 0.7635 0.7073 0.2456  0.4201  0.0592  452  TYR B CB  
17805 C CG  . TYR C 452  ? 1.4674 0.7801 0.7093 0.2357  0.3954  0.0506  452  TYR B CG  
17806 C CD1 . TYR C 452  ? 1.5246 0.8402 0.7552 0.2223  0.3816  0.0280  452  TYR B CD1 
17807 C CD2 . TYR C 452  ? 1.4482 0.7926 0.7225 0.2401  0.3850  0.0646  452  TYR B CD2 
17808 C CE1 . TYR C 452  ? 1.5269 0.8776 0.7785 0.2153  0.3595  0.0197  452  TYR B CE1 
17809 C CE2 . TYR C 452  ? 1.4489 0.8248 0.7415 0.2331  0.3623  0.0553  452  TYR B CE2 
17810 C CZ  . TYR C 452  ? 1.4792 0.8585 0.7605 0.2215  0.3504  0.0328  452  TYR B CZ  
17811 O OH  . TYR C 452  ? 1.4421 0.8525 0.7404 0.2163  0.3286  0.0225  452  TYR B OH  
17812 N N   . ARG C 453  ? 1.6246 0.8200 0.7711 0.2740  0.4633  0.0656  453  ARG B N   
17813 C CA  . ARG C 453  ? 1.6241 0.7776 0.7431 0.2861  0.4878  0.0689  453  ARG B CA  
17814 C C   . ARG C 453  ? 1.6671 0.7802 0.7558 0.2720  0.4902  0.0453  453  ARG B C   
17815 O O   . ARG C 453  ? 1.6812 0.7900 0.7523 0.2585  0.4760  0.0243  453  ARG B O   
17816 C CB  . ARG C 453  ? 1.6523 0.7942 0.7448 0.3059  0.4995  0.0764  453  ARG B CB  
17817 C CG  . ARG C 453  ? 1.7131 0.8075 0.7696 0.3192  0.5236  0.0744  453  ARG B CG  
17818 C CD  . ARG C 453  ? 1.7861 0.8582 0.7993 0.3328  0.5315  0.0682  453  ARG B CD  
17819 N NE  . ARG C 453  ? 1.8127 0.9018 0.8337 0.3563  0.5467  0.0937  453  ARG B NE  
17820 C CZ  . ARG C 453  ? 1.8479 0.9610 0.8677 0.3621  0.5404  0.1011  453  ARG B CZ  
17821 N NH1 . ARG C 453  ? 1.8574 0.9783 0.8667 0.3476  0.5185  0.0840  453  ARG B NH1 
17822 N NH2 . ARG C 453  ? 1.8635 0.9933 0.8929 0.3826  0.5559  0.1267  453  ARG B NH2 
17823 N N   . ALA C 454  ? 1.6907 0.7733 0.7732 0.2749  0.5070  0.0492  454  ALA B N   
17824 C CA  . ALA C 454  ? 1.7773 0.8211 0.8351 0.2584  0.5074  0.0283  454  ALA B CA  
17825 C C   . ALA C 454  ? 1.8747 0.8649 0.8944 0.2735  0.5294  0.0280  454  ALA B C   
17826 O O   . ALA C 454  ? 1.9095 0.8968 0.9353 0.2947  0.5472  0.0483  454  ALA B O   
17827 C CB  . ALA C 454  ? 1.7293 0.7845 0.8160 0.2424  0.5039  0.0308  454  ALA B CB  
17828 N N   . ILE C 455  ? 1.9490 0.8958 0.9298 0.2626  0.5278  0.0049  455  ILE B N   
17829 C CA  . ILE C 455  ? 2.0169 0.9060 0.9510 0.2791  0.5471  0.0000  455  ILE B CA  
17830 C C   . ILE C 455  ? 2.0284 0.8656 0.9355 0.2614  0.5469  -0.0194 455  ILE B C   
17831 O O   . ILE C 455  ? 2.0127 0.8548 0.9226 0.2346  0.5283  -0.0371 455  ILE B O   
17832 C CB  . ILE C 455  ? 1.9386 0.8189 0.8370 0.2881  0.5440  -0.0115 455  ILE B CB  
17833 C CG1 . ILE C 455  ? 1.9055 0.8233 0.8210 0.3114  0.5515  0.0111  455  ILE B CG1 
17834 C CG2 . ILE C 455  ? 2.0157 0.8311 0.8599 0.2976  0.5579  -0.0255 455  ILE B CG2 
17835 C CD1 . ILE C 455  ? 1.9154 0.8667 0.8312 0.3052  0.5319  0.0041  455  ILE B CD1 
17836 N N   . ALA C 456  ? 2.0524 0.8394 0.9336 0.2764  0.5673  -0.0158 456  ALA B N   
17837 C CA  . ALA C 456  ? 2.0954 0.8320 0.9571 0.2589  0.5679  -0.0295 456  ALA B CA  
17838 C C   . ALA C 456  ? 2.1563 0.8430 0.9677 0.2459  0.5589  -0.0589 456  ALA B C   
17839 O O   . ALA C 456  ? 2.1868 0.8459 0.9569 0.2644  0.5656  -0.0670 456  ALA B O   
17840 C CB  . ALA C 456  ? 2.1098 0.8101 0.9648 0.2792  0.5914  -0.0138 456  ALA B CB  
17841 N N   . TYR C 457  ? 2.1830 0.8606 0.9991 0.2136  0.5432  -0.0742 457  TYR B N   
17842 C CA  . TYR C 457  ? 2.2738 0.8978 1.0450 0.1964  0.5334  -0.1015 457  TYR B CA  
17843 C C   . TYR C 457  ? 2.3577 0.9103 1.0846 0.2170  0.5544  -0.1021 457  TYR B C   
17844 O O   . TYR C 457  ? 2.3564 0.8728 1.0825 0.2102  0.5623  -0.0985 457  TYR B O   
17845 C CB  . TYR C 457  ? 2.3131 0.9373 1.1040 0.1589  0.5181  -0.1109 457  TYR B CB  
17846 C CG  . TYR C 457  ? 2.4365 1.0131 1.1883 0.1345  0.5026  -0.1395 457  TYR B CG  
17847 C CD1 . TYR C 457  ? 2.4614 1.0594 1.2370 0.0973  0.4819  -0.1504 457  TYR B CD1 
17848 C CD2 . TYR C 457  ? 2.5333 1.0451 1.2250 0.1482  0.5080  -0.1555 457  TYR B CD2 
17849 C CE1 . TYR C 457  ? 2.5170 1.0747 1.2607 0.0724  0.4655  -0.1757 457  TYR B CE1 
17850 C CE2 . TYR C 457  ? 2.6022 1.0686 1.2570 0.1242  0.4911  -0.1826 457  TYR B CE2 
17851 C CZ  . TYR C 457  ? 2.5789 1.0695 1.2617 0.0852  0.4691  -0.1921 457  TYR B CZ  
17852 O OH  . TYR C 457  ? 2.6214 1.0704 1.2716 0.0592  0.4505  -0.2179 457  TYR B OH  
17853 N N   . SER C 458  ? 2.4604 0.9925 1.1486 0.2436  0.5640  -0.1062 458  SER B N   
17854 C CA  . SER C 458  ? 2.5642 1.0278 1.2037 0.2688  0.5850  -0.1088 458  SER B CA  
17855 C C   . SER C 458  ? 2.6376 1.0306 1.2290 0.2471  0.5736  -0.1378 458  SER B C   
17856 O O   . SER C 458  ? 2.5996 0.9902 1.1693 0.2299  0.5539  -0.1597 458  SER B O   
17857 C CB  . SER C 458  ? 2.6163 1.0884 1.2302 0.3025  0.5971  -0.1051 458  SER B CB  
17858 O OG  . SER C 458  ? 2.5468 1.0974 1.2073 0.3052  0.5914  -0.0877 458  SER B OG  
17859 N N   . SER C 459  ? 2.7264 1.0625 1.3030 0.2460  0.5842  -0.1372 459  SER B N   
17860 C CA  . SER C 459  ? 2.8312 1.0904 1.3583 0.2275  0.5749  -0.1634 459  SER B CA  
17861 C C   . SER C 459  ? 2.9238 1.1096 1.4178 0.2489  0.5969  -0.1592 459  SER B C   
17862 O O   . SER C 459  ? 2.8843 1.0743 1.4095 0.2495  0.6075  -0.1394 459  SER B O   
17863 C CB  . SER C 459  ? 2.7907 1.0640 1.3476 0.1814  0.5517  -0.1715 459  SER B CB  
17864 O OG  . SER C 459  ? 2.8345 1.0556 1.3473 0.1584  0.5334  -0.2010 459  SER B OG  
17865 N N   . LEU C 460  ? 3.0814 1.1991 1.5101 0.2676  0.6033  -0.1780 460  LEU B N   
17866 C CA  . LEU C 460  ? 3.2669 1.3144 1.6584 0.2970  0.6268  -0.1742 460  LEU B CA  
17867 C C   . LEU C 460  ? 3.3602 1.3491 1.7467 0.2719  0.6216  -0.1788 460  LEU B C   
17868 O O   . LEU C 460  ? 3.4230 1.3671 1.7985 0.2925  0.6408  -0.1674 460  LEU B O   
17869 C CB  . LEU C 460  ? 3.4141 1.4014 1.7321 0.3248  0.6347  -0.1954 460  LEU B CB  
17870 C CG  . LEU C 460  ? 3.5249 1.4685 1.8119 0.3728  0.6666  -0.1843 460  LEU B CG  
17871 C CD1 . LEU C 460  ? 3.4818 1.4930 1.7935 0.4083  0.6856  -0.1617 460  LEU B CD1 
17872 C CD2 . LEU C 460  ? 3.6707 1.5168 1.8730 0.3890  0.6706  -0.2125 460  LEU B CD2 
17873 N N   . SER C 461  ? 3.5031 1.2148 1.8403 0.6787  0.1678  -0.2522 461  SER B N   
17874 C CA  . SER C 461  ? 3.5508 1.2280 1.8712 0.6442  0.1235  -0.2472 461  SER B CA  
17875 C C   . SER C 461  ? 3.4487 1.2023 1.8641 0.6353  0.1214  -0.2308 461  SER B C   
17876 O O   . SER C 461  ? 3.4480 1.1881 1.8646 0.6072  0.0876  -0.2228 461  SER B O   
17877 C CB  . SER C 461  ? 3.5923 1.2654 1.8717 0.5933  0.0850  -0.2442 461  SER B CB  
17878 O OG  . SER C 461  ? 3.7221 1.3080 1.9031 0.5994  0.0787  -0.2603 461  SER B OG  
17879 N N   . GLN C 462  ? 3.3597 1.1934 1.8543 0.6593  0.1569  -0.2252 462  GLN B N   
17880 C CA  . GLN C 462  ? 3.2201 1.1352 1.8096 0.6523  0.1566  -0.2104 462  GLN B CA  
17881 C C   . GLN C 462  ? 3.1085 1.0815 1.7194 0.5992  0.1241  -0.1988 462  GLN B C   
17882 O O   . GLN C 462  ? 3.0267 1.0656 1.7060 0.5833  0.1149  -0.1861 462  GLN B O   
17883 C CB  . GLN C 462  ? 3.2712 1.1380 1.8628 0.6655  0.1456  -0.2088 462  GLN B CB  
17884 C CG  . GLN C 462  ? 3.2600 1.1204 1.8869 0.7192  0.1840  -0.2132 462  GLN B CG  
17885 C CD  . GLN C 462  ? 3.1462 1.1128 1.8785 0.7314  0.2101  -0.2023 462  GLN B CD  
17886 O OE1 . GLN C 462  ? 3.0447 1.0908 1.8234 0.7002  0.1994  -0.1925 462  GLN B OE1 
17887 N NE2 . GLN C 462  ? 3.1550 1.1235 1.9277 0.7777  0.2442  -0.2040 462  GLN B NE2 
17888 N N   . SER C 463  ? 3.0778 1.0243 1.6280 0.5725  0.1066  -0.2035 463  SER B N   
17889 C CA  . SER C 463  ? 3.0013 0.9887 1.5588 0.5201  0.0727  -0.1934 463  SER B CA  
17890 C C   . SER C 463  ? 2.8554 0.9435 1.4758 0.5104  0.0887  -0.1882 463  SER B C   
17891 O O   . SER C 463  ? 2.8749 0.9696 1.4905 0.5344  0.1167  -0.1956 463  SER B O   
17892 C CB  . SER C 463  ? 3.1010 1.0053 1.5624 0.4958  0.0432  -0.2009 463  SER B CB  
17893 O OG  . SER C 463  ? 3.0701 1.0209 1.5406 0.4477  0.0166  -0.1919 463  SER B OG  
17894 N N   . TYR C 464  ? 2.7032 0.8699 1.3828 0.4764  0.0717  -0.1755 464  TYR B N   
17895 C CA  . TYR C 464  ? 2.5811 0.8399 1.3163 0.4630  0.0818  -0.1717 464  TYR B CA  
17896 C C   . TYR C 464  ? 2.5199 0.8198 1.2651 0.4109  0.0474  -0.1618 464  TYR B C   
17897 O O   . TYR C 464  ? 2.5512 0.8062 1.2579 0.3853  0.0164  -0.1569 464  TYR B O   
17898 C CB  . TYR C 464  ? 2.4877 0.8303 1.3183 0.4891  0.1107  -0.1671 464  TYR B CB  
17899 C CG  . TYR C 464  ? 2.5323 0.8377 1.3683 0.5384  0.1396  -0.1723 464  TYR B CG  
17900 C CD1 . TYR C 464  ? 2.6042 0.8709 1.4079 0.5739  0.1695  -0.1822 464  TYR B CD1 
17901 C CD2 . TYR C 464  ? 2.5367 0.8483 1.4124 0.5499  0.1378  -0.1665 464  TYR B CD2 
17902 C CE1 . TYR C 464  ? 2.6512 0.8861 1.4636 0.6205  0.1982  -0.1864 464  TYR B CE1 
17903 C CE2 . TYR C 464  ? 2.5884 0.8680 1.4748 0.5953  0.1641  -0.1706 464  TYR B CE2 
17904 C CZ  . TYR C 464  ? 2.6487 0.8907 1.5048 0.6310  0.1950  -0.1806 464  TYR B CZ  
17905 O OH  . TYR C 464  ? 2.6830 0.8953 1.5534 0.6771  0.2226  -0.1840 464  TYR B OH  
17906 N N   . LEU C 465  ? 2.4563 0.8423 1.2550 0.3955  0.0531  -0.1584 465  LEU B N   
17907 C CA  . LEU C 465  ? 2.4423 0.8820 1.2632 0.3474  0.0242  -0.1485 465  LEU B CA  
17908 C C   . LEU C 465  ? 2.3556 0.9114 1.2692 0.3432  0.0381  -0.1443 465  LEU B C   
17909 O O   . LEU C 465  ? 2.3422 0.9302 1.2867 0.3686  0.0659  -0.1499 465  LEU B O   
17910 C CB  . LEU C 465  ? 2.5057 0.8984 1.2572 0.3158  -0.0003 -0.1509 465  LEU B CB  
17911 C CG  . LEU C 465  ? 2.4962 0.9440 1.2710 0.2653  -0.0296 -0.1399 465  LEU B CG  
17912 C CD1 . LEU C 465  ? 2.5330 0.9702 1.3081 0.2440  -0.0543 -0.1285 465  LEU B CD1 
17913 C CD2 . LEU C 465  ? 2.5490 0.9571 1.2643 0.2367  -0.0514 -0.1424 465  LEU B CD2 
17914 N N   . TYR C 466  ? 2.2798 0.8961 1.2358 0.3111  0.0183  -0.1341 466  TYR B N   
17915 C CA  . TYR C 466  ? 2.1384 0.8657 1.1833 0.3044  0.0268  -0.1305 466  TYR B CA  
17916 C C   . TYR C 466  ? 2.1073 0.8859 1.1661 0.2560  -0.0007 -0.1222 466  TYR B C   
17917 O O   . TYR C 466  ? 2.1426 0.9193 1.1963 0.2337  -0.0218 -0.1128 466  TYR B O   
17918 C CB  . TYR C 466  ? 2.0603 0.8260 1.1643 0.3255  0.0371  -0.1266 466  TYR B CB  
17919 C CG  . TYR C 466  ? 1.9262 0.8025 1.1199 0.3209  0.0447  -0.1248 466  TYR B CG  
17920 C CD1 . TYR C 466  ? 1.9023 0.8316 1.1187 0.3035  0.0452  -0.1274 466  TYR B CD1 
17921 C CD2 . TYR C 466  ? 1.8576 0.7842 1.1139 0.3356  0.0510  -0.1214 466  TYR B CD2 
17922 C CE1 . TYR C 466  ? 1.8077 0.8379 1.1072 0.3001  0.0514  -0.1274 466  TYR B CE1 
17923 C CE2 . TYR C 466  ? 1.7698 0.7978 1.1088 0.3331  0.0572  -0.1218 466  TYR B CE2 
17924 C CZ  . TYR C 466  ? 1.7316 0.8106 1.0915 0.3154  0.0576  -0.1253 466  TYR B CZ  
17925 O OH  . TYR C 466  ? 1.6226 0.7994 1.0624 0.3123  0.0624  -0.1272 466  TYR B OH  
17926 N N   . ILE C 467  ? 2.0400 0.8690 1.1213 0.2398  0.0000  -0.1246 467  ILE B N   
17927 C CA  . ILE C 467  ? 1.9840 0.8730 1.0902 0.1959  -0.0230 -0.1167 467  ILE B CA  
17928 C C   . ILE C 467  ? 1.9076 0.9091 1.1046 0.1954  -0.0109 -0.1180 467  ILE B C   
17929 O O   . ILE C 467  ? 1.8719 0.9056 1.1061 0.2197  0.0117  -0.1256 467  ILE B O   
17930 C CB  . ILE C 467  ? 2.0008 0.8510 1.0513 0.1648  -0.0435 -0.1163 467  ILE B CB  
17931 C CG1 . ILE C 467  ? 1.9502 0.8272 1.0182 0.1762  -0.0266 -0.1251 467  ILE B CG1 
17932 C CG2 . ILE C 467  ? 2.1111 0.8461 1.0703 0.1672  -0.0570 -0.1170 467  ILE B CG2 
17933 C CD1 . ILE C 467  ? 1.9713 0.8311 1.0010 0.1417  -0.0484 -0.1240 467  ILE B CD1 
17934 N N   . ASP C 468  ? 1.9048 0.9667 1.1375 0.1669  -0.0266 -0.1103 468  ASP B N   
17935 C CA  . ASP C 468  ? 1.8757 1.0425 1.1931 0.1669  -0.0170 -0.1129 468  ASP B CA  
17936 C C   . ASP C 468  ? 1.8705 1.0788 1.1933 0.1222  -0.0413 -0.1044 468  ASP B C   
17937 O O   . ASP C 468  ? 1.9002 1.0536 1.1634 0.0950  -0.0627 -0.0967 468  ASP B O   
17938 C CB  . ASP C 468  ? 1.9407 1.1413 1.3086 0.1956  -0.0029 -0.1135 468  ASP B CB  
17939 C CG  . ASP C 468  ? 1.9325 1.2333 1.3910 0.2084  0.0125  -0.1201 468  ASP B CG  
17940 O OD1 . ASP C 468  ? 1.9276 1.2660 1.4088 0.1998  0.0156  -0.1250 468  ASP B OD1 
17941 O OD2 . ASP C 468  ? 1.9198 1.2609 1.4279 0.2272  0.0200  -0.1206 468  ASP B OD2 
17942 N N   . TRP C 469  ? 1.8543 1.1594 1.2494 0.1150  -0.0383 -0.1056 469  TRP B N   
17943 C CA  . TRP C 469  ? 1.9541 1.3110 1.3632 0.0741  -0.0581 -0.0978 469  TRP B CA  
17944 C C   . TRP C 469  ? 2.0158 1.4766 1.5100 0.0821  -0.0474 -0.1033 469  TRP B C   
17945 O O   . TRP C 469  ? 1.9872 1.4764 1.5266 0.1132  -0.0275 -0.1138 469  TRP B O   
17946 C CB  . TRP C 469  ? 1.9278 1.2816 1.3201 0.0485  -0.0681 -0.0988 469  TRP B CB  
17947 C CG  . TRP C 469  ? 1.8466 1.2699 1.3018 0.0594  -0.0531 -0.1098 469  TRP B CG  
17948 C CD1 . TRP C 469  ? 1.7924 1.2964 1.2989 0.0356  -0.0592 -0.1109 469  TRP B CD1 
17949 C CD2 . TRP C 469  ? 1.8305 1.2492 1.3063 0.0967  -0.0299 -0.1203 469  TRP B CD2 
17950 N NE1 . TRP C 469  ? 1.7326 1.2818 1.2911 0.0555  -0.0428 -0.1219 469  TRP B NE1 
17951 C CE2 . TRP C 469  ? 1.7592 1.2574 1.2997 0.0926  -0.0246 -0.1269 469  TRP B CE2 
17952 C CE3 . TRP C 469  ? 1.8790 1.2353 1.3266 0.1336  -0.0125 -0.1240 469  TRP B CE3 
17953 C CZ2 . TRP C 469  ? 1.7278 1.2437 1.3049 0.1226  -0.0039 -0.1356 469  TRP B CZ2 
17954 C CZ3 . TRP C 469  ? 1.8356 1.2119 1.3200 0.1640  0.0101  -0.1326 469  TRP B CZ3 
17955 C CH2 . TRP C 469  ? 1.7573 1.2120 1.3053 0.1577  0.0136  -0.1376 469  TRP B CH2 
17956 N N   . THR C 470  ? 2.1391 1.6585 1.6580 0.0559  -0.0598 -0.0965 470  THR B N   
17957 C CA  . THR C 470  ? 2.2116 1.8350 1.8132 0.0621  -0.0503 -0.1052 470  THR B CA  
17958 C C   . THR C 470  ? 2.3651 2.0598 1.9961 0.0260  -0.0621 -0.1034 470  THR B C   
17959 O O   . THR C 470  ? 2.4251 2.1011 2.0175 -0.0091 -0.0801 -0.0914 470  THR B O   
17960 C CB  . THR C 470  ? 2.1246 1.7845 1.7641 0.0845  -0.0430 -0.1066 470  THR B CB  
17961 O OG1 . THR C 470  ? 2.1608 1.7604 1.7833 0.1208  -0.0302 -0.1091 470  THR B OG1 
17962 C CG2 . THR C 470  ? 2.0044 1.7640 1.7293 0.0962  -0.0325 -0.1192 470  THR B CG2 
17963 N N   . ASP C 471  ? 2.4765 2.2535 2.1802 0.0367  -0.0514 -0.1156 471  ASP B N   
17964 C CA  . ASP C 471  ? 2.6520 2.5094 2.4000 0.0100  -0.0582 -0.1181 471  ASP B CA  
17965 C C   . ASP C 471  ? 2.7251 2.6646 2.5564 0.0374  -0.0432 -0.1337 471  ASP B C   
17966 O O   . ASP C 471  ? 2.7224 2.6511 2.5757 0.0676  -0.0291 -0.1426 471  ASP B O   
17967 C CB  . ASP C 471  ? 2.7475 2.5800 2.4749 -0.0096 -0.0650 -0.1177 471  ASP B CB  
17968 C CG  . ASP C 471  ? 2.8169 2.7248 2.5837 -0.0427 -0.0752 -0.1177 471  ASP B CG  
17969 O OD1 . ASP C 471  ? 2.8912 2.7789 2.6204 -0.0781 -0.0922 -0.1053 471  ASP B OD1 
17970 O OD2 . ASP C 471  ? 2.7922 2.7796 2.6299 -0.0338 -0.0669 -0.1300 471  ASP B OD2 
17971 N N   . ASN C 472  ? 2.8266 2.8466 2.7035 0.0279  -0.0463 -0.1366 472  ASN B N   
17972 C CA  . ASN C 472  ? 2.8697 2.9651 2.8241 0.0551  -0.0348 -0.1520 472  ASN B CA  
17973 C C   . ASN C 472  ? 2.9179 3.0705 2.9366 0.0613  -0.0285 -0.1660 472  ASN B C   
17974 O O   . ASN C 472  ? 2.8502 3.0556 2.9335 0.0876  -0.0193 -0.1791 472  ASN B O   
17975 C CB  . ASN C 472  ? 2.8428 3.0025 2.8214 0.0474  -0.0401 -0.1521 472  ASN B CB  
17976 C CG  . ASN C 472  ? 2.8322 3.0058 2.7794 0.0048  -0.0544 -0.1395 472  ASN B CG  
17977 O OD1 . ASN C 472  ? 2.8524 2.9848 2.7596 -0.0202 -0.0625 -0.1302 472  ASN B OD1 
17978 N ND2 . ASN C 472  ? 2.7934 3.0255 2.7589 -0.0032 -0.0577 -0.1387 472  ASN B ND2 
17979 N N   . HIS C 473  ? 3.0283 3.1699 3.0316 0.0373  -0.0350 -0.1631 473  HIS B N   
17980 C CA  . HIS C 473  ? 3.0868 3.2807 3.1503 0.0408  -0.0310 -0.1750 473  HIS B CA  
17981 C C   . HIS C 473  ? 2.9322 3.0691 2.9756 0.0526  -0.0247 -0.1745 473  HIS B C   
17982 O O   . HIS C 473  ? 2.9868 3.0414 2.9585 0.0448  -0.0283 -0.1641 473  HIS B O   
17983 C CB  . HIS C 473  ? 3.3400 3.5952 3.4271 0.0054  -0.0431 -0.1754 473  HIS B CB  
17984 C CG  . HIS C 473  ? 3.6403 3.8612 3.6650 -0.0304 -0.0572 -0.1593 473  HIS B CG  
17985 N ND1 . HIS C 473  ? 3.8381 3.9951 3.8073 -0.0535 -0.0674 -0.1484 473  HIS B ND1 
17986 C CD2 . HIS C 473  ? 3.7657 4.0065 3.7752 -0.0474 -0.0636 -0.1514 473  HIS B CD2 
17987 C CE1 . HIS C 473  ? 3.9798 4.1190 3.9056 -0.0834 -0.0803 -0.1341 473  HIS B CE1 
17988 N NE2 . HIS C 473  ? 3.9254 4.1151 3.8741 -0.0806 -0.0774 -0.1348 473  HIS B NE2 
17989 N N   . LYS C 474  ? 2.7272 2.9110 2.8357 0.0708  -0.0160 -0.1860 474  LYS B N   
17990 C CA  . LYS C 474  ? 2.6108 2.7507 2.7123 0.0904  -0.0058 -0.1862 474  LYS B CA  
17991 C C   . LYS C 474  ? 2.4805 2.5706 2.5298 0.0651  -0.0153 -0.1786 474  LYS B C   
17992 O O   . LYS C 474  ? 2.5298 2.5761 2.5615 0.0794  -0.0074 -0.1775 474  LYS B O   
17993 C CB  . LYS C 474  ? 2.5661 2.7754 2.7572 0.1139  0.0039  -0.1989 474  LYS B CB  
17994 C CG  . LYS C 474  ? 2.5390 2.8383 2.7957 0.0940  -0.0062 -0.2083 474  LYS B CG  
17995 C CD  . LYS C 474  ? 2.4950 2.8479 2.8333 0.1161  0.0015  -0.2192 474  LYS B CD  
17996 C CE  . LYS C 474  ? 2.5323 2.8359 2.8477 0.1192  0.0062  -0.2130 474  LYS B CE  
17997 N NZ  . LYS C 474  ? 2.4749 2.8340 2.8720 0.1361  0.0114  -0.2214 474  LYS B NZ  
17998 N N   . ALA C 475  ? 2.2958 2.3915 2.3197 0.0279  -0.0323 -0.1727 475  ALA B N   
17999 C CA  . ALA C 475  ? 2.1293 2.1811 2.1090 0.0026  -0.0443 -0.1658 475  ALA B CA  
18000 C C   . ALA C 475  ? 1.9727 1.9934 1.8956 -0.0327 -0.0620 -0.1540 475  ALA B C   
18001 O O   . ALA C 475  ? 1.9187 1.9941 1.8672 -0.0498 -0.0681 -0.1531 475  ALA B O   
18002 C CB  . ALA C 475  ? 2.0690 2.1887 2.1129 -0.0089 -0.0488 -0.1731 475  ALA B CB  
18003 N N   . LEU C 476  ? 1.8859 1.8182 1.7312 -0.0434 -0.0704 -0.1446 476  LEU B N   
18004 C CA  . LEU C 476  ? 1.7727 1.6685 1.5629 -0.0778 -0.0895 -0.1318 476  LEU B CA  
18005 C C   . LEU C 476  ? 1.6940 1.6268 1.5052 -0.1131 -0.1060 -0.1293 476  LEU B C   
18006 O O   . LEU C 476  ? 1.7312 1.6382 1.5312 -0.1173 -0.1109 -0.1305 476  LEU B O   
18007 C CB  . LEU C 476  ? 1.7604 1.5440 1.4593 -0.0750 -0.0946 -0.1237 476  LEU B CB  
18008 C CG  . LEU C 476  ? 1.6826 1.4186 1.3612 -0.0334 -0.0751 -0.1286 476  LEU B CG  
18009 C CD1 . LEU C 476  ? 1.7415 1.3687 1.3275 -0.0342 -0.0826 -0.1206 476  LEU B CD1 
18010 C CD2 . LEU C 476  ? 1.6296 1.4136 1.3495 -0.0156 -0.0639 -0.1314 476  LEU B CD2 
18011 N N   . LEU C 477  ? 1.5953 1.5904 1.4383 -0.1383 -0.1142 -0.1255 477  LEU B N   
18012 C CA  . LEU C 477  ? 1.5141 1.5477 1.3807 -0.1734 -0.1301 -0.1220 477  LEU B CA  
18013 C C   . LEU C 477  ? 1.4974 1.4469 1.2875 -0.2015 -0.1505 -0.1073 477  LEU B C   
18014 O O   . LEU C 477  ? 1.5331 1.4241 1.2648 -0.2059 -0.1558 -0.0971 477  LEU B O   
18015 C CB  . LEU C 477  ? 1.5223 1.6446 1.4411 -0.1918 -0.1316 -0.1211 477  LEU B CB  
18016 C CG  . LEU C 477  ? 1.5360 1.7311 1.5191 -0.1608 -0.1124 -0.1358 477  LEU B CG  
18017 C CD1 . LEU C 477  ? 1.5537 1.8168 1.5640 -0.1761 -0.1133 -0.1328 477  LEU B CD1 
18018 C CD2 . LEU C 477  ? 1.4842 1.7389 1.5405 -0.1443 -0.1045 -0.1520 477  LEU B CD2 
18019 N N   . VAL C 478  ? 1.4602 1.4013 1.2510 -0.2197 -0.1634 -0.1066 478  VAL B N   
18020 C CA  . VAL C 478  ? 1.5370 1.4032 1.2611 -0.2493 -0.1866 -0.0933 478  VAL B CA  
18021 C C   . VAL C 478  ? 1.5578 1.4565 1.2888 -0.2841 -0.1999 -0.0799 478  VAL B C   
18022 O O   . VAL C 478  ? 1.4790 1.4701 1.2781 -0.2923 -0.1947 -0.0829 478  VAL B O   
18023 C CB  . VAL C 478  ? 1.5518 1.4213 1.2900 -0.2653 -0.1994 -0.0951 478  VAL B CB  
18024 C CG1 . VAL C 478  ? 1.5226 1.4626 1.3104 -0.3038 -0.2144 -0.0880 478  VAL B CG1 
18025 C CG2 . VAL C 478  ? 1.6374 1.3971 1.2888 -0.2722 -0.2159 -0.0883 478  VAL B CG2 
18026 N N   . GLY C 479  ? 1.6671 1.4915 1.3294 -0.3043 -0.2172 -0.0650 479  GLY B N   
18027 C CA  . GLY C 479  ? 1.7060 1.5559 1.3702 -0.3344 -0.2277 -0.0495 479  GLY B CA  
18028 C C   . GLY C 479  ? 1.7503 1.5790 1.3860 -0.3176 -0.2175 -0.0454 479  GLY B C   
18029 O O   . GLY C 479  ? 1.8118 1.6184 1.4164 -0.3409 -0.2301 -0.0287 479  GLY B O   
18030 N N   . GLU C 480  ? 1.7016 1.5360 1.3492 -0.2776 -0.1955 -0.0595 480  GLU B N   
18031 C CA  . GLU C 480  ? 1.7180 1.5302 1.3403 -0.2592 -0.1861 -0.0562 480  GLU B CA  
18032 C C   . GLU C 480  ? 1.7825 1.4791 1.3170 -0.2585 -0.1981 -0.0470 480  GLU B C   
18033 O O   . GLU C 480  ? 1.8129 1.4462 1.3040 -0.2723 -0.2142 -0.0438 480  GLU B O   
18034 C CB  . GLU C 480  ? 1.6987 1.5505 1.3632 -0.2164 -0.1604 -0.0735 480  GLU B CB  
18035 C CG  . GLU C 480  ? 1.7241 1.6865 1.4641 -0.2160 -0.1495 -0.0789 480  GLU B CG  
18036 C CD  . GLU C 480  ? 1.7878 1.7824 1.5651 -0.1737 -0.1272 -0.0942 480  GLU B CD  
18037 O OE1 . GLU C 480  ? 1.7646 1.8359 1.5907 -0.1694 -0.1193 -0.0984 480  GLU B OE1 
18038 O OE2 . GLU C 480  ? 1.8496 1.7927 1.6078 -0.1440 -0.1177 -0.1018 480  GLU B OE2 
18039 N N   . HIS C 481  ? 1.8204 1.4887 1.3287 -0.2423 -0.1917 -0.0432 481  HIS B N   
18040 C CA  . HIS C 481  ? 1.9314 1.4922 1.3591 -0.2413 -0.2037 -0.0346 481  HIS B CA  
18041 C C   . HIS C 481  ? 1.8867 1.4170 1.3013 -0.1992 -0.1845 -0.0437 481  HIS B C   
18042 O O   . HIS C 481  ? 1.8376 1.4103 1.2794 -0.1885 -0.1743 -0.0423 481  HIS B O   
18043 C CB  . HIS C 481  ? 2.0565 1.6046 1.4583 -0.2762 -0.2238 -0.0130 481  HIS B CB  
18044 C CG  . HIS C 481  ? 2.1646 1.6952 1.5495 -0.3180 -0.2494 -0.0003 481  HIS B CG  
18045 N ND1 . HIS C 481  ? 2.2799 1.7100 1.5935 -0.3325 -0.2724 0.0088  481  HIS B ND1 
18046 C CD2 . HIS C 481  ? 2.1542 1.7546 1.5862 -0.3484 -0.2567 0.0049  481  HIS B CD2 
18047 C CE1 . HIS C 481  ? 2.3075 1.7456 1.6255 -0.3705 -0.2937 0.0197  481  HIS B CE1 
18048 N NE2 . HIS C 481  ? 2.2320 1.7736 1.6223 -0.3810 -0.2841 0.0180  481  HIS B NE2 
18049 N N   . LEU C 482  ? 1.9055 1.3608 1.2772 -0.1754 -0.1801 -0.0525 482  LEU B N   
18050 C CA  . LEU C 482  ? 1.9036 1.3325 1.2696 -0.1319 -0.1589 -0.0628 482  LEU B CA  
18051 C C   . LEU C 482  ? 1.9839 1.3331 1.2893 -0.1257 -0.1658 -0.0540 482  LEU B C   
18052 O O   . LEU C 482  ? 2.0798 1.3361 1.3168 -0.1285 -0.1785 -0.0513 482  LEU B O   
18053 C CB  . LEU C 482  ? 1.9026 1.2927 1.2538 -0.1068 -0.1477 -0.0762 482  LEU B CB  
18054 C CG  . LEU C 482  ? 1.8433 1.2481 1.2251 -0.0601 -0.1191 -0.0895 482  LEU B CG  
18055 C CD1 . LEU C 482  ? 1.8051 1.2092 1.1981 -0.0425 -0.1070 -0.1010 482  LEU B CD1 
18056 C CD2 . LEU C 482  ? 1.9034 1.2298 1.2333 -0.0350 -0.1137 -0.0880 482  LEU B CD2 
18057 N N   . ASN C 483  ? 1.9356 1.3189 1.2652 -0.1166 -0.1585 -0.0499 483  ASN B N   
18058 C CA  . ASN C 483  ? 1.9840 1.2937 1.2619 -0.1064 -0.1635 -0.0424 483  ASN B CA  
18059 C C   . ASN C 483  ? 1.9480 1.2216 1.2212 -0.0592 -0.1414 -0.0562 483  ASN B C   
18060 O O   . ASN C 483  ? 1.8950 1.2288 1.2239 -0.0335 -0.1214 -0.0646 483  ASN B O   
18061 C CB  . ASN C 483  ? 1.9869 1.3426 1.2869 -0.1193 -0.1680 -0.0295 483  ASN B CB  
18062 C CG  . ASN C 483  ? 2.0980 1.3709 1.3364 -0.1245 -0.1835 -0.0157 483  ASN B CG  
18063 O OD1 . ASN C 483  ? 2.1627 1.3711 1.3481 -0.1500 -0.2056 -0.0053 483  ASN B OD1 
18064 N ND2 . ASN C 483  ? 2.1116 1.3849 1.3580 -0.1003 -0.1737 -0.0153 483  ASN B ND2 
18065 N N   . ILE C 484  ? 1.9826 1.1574 1.1894 -0.0478 -0.1457 -0.0583 484  ILE B N   
18066 C CA  . ILE C 484  ? 1.9352 1.0688 1.1317 -0.0034 -0.1235 -0.0719 484  ILE B CA  
18067 C C   . ILE C 484  ? 1.9546 0.9953 1.0917 0.0142  -0.1268 -0.0688 484  ILE B C   
18068 O O   . ILE C 484  ? 2.0265 0.9884 1.0975 -0.0035 -0.1477 -0.0625 484  ILE B O   
18069 C CB  . ILE C 484  ? 1.9384 1.0458 1.1150 0.0007  -0.1198 -0.0818 484  ILE B CB  
18070 C CG1 . ILE C 484  ? 1.9732 0.9983 1.1025 0.0391  -0.1046 -0.0916 484  ILE B CG1 
18071 C CG2 . ILE C 484  ? 1.9885 1.0616 1.1211 -0.0405 -0.1482 -0.0733 484  ILE B CG2 
18072 C CD1 . ILE C 484  ? 1.9549 0.9539 1.0604 0.0438  -0.1003 -0.1007 484  ILE B CD1 
18073 N N   . ILE C 485  ? 1.8918 0.9418 1.0552 0.0500  -0.1067 -0.0739 485  ILE B N   
18074 C CA  . ILE C 485  ? 1.9390 0.9223 1.0644 0.0647  -0.1106 -0.0687 485  ILE B CA  
18075 C C   . ILE C 485  ? 2.0237 0.9124 1.0949 0.0975  -0.1006 -0.0780 485  ILE B C   
18076 O O   . ILE C 485  ? 2.0405 0.9366 1.1363 0.1359  -0.0744 -0.0891 485  ILE B O   
18077 C CB  . ILE C 485  ? 1.8579 0.8976 1.0398 0.0856  -0.0967 -0.0680 485  ILE B CB  
18078 C CG1 . ILE C 485  ? 1.8212 0.9308 1.0348 0.0511  -0.1123 -0.0552 485  ILE B CG1 
18079 C CG2 . ILE C 485  ? 1.9281 0.8919 1.0723 0.1090  -0.0967 -0.0654 485  ILE B CG2 
18080 C CD1 . ILE C 485  ? 1.8353 0.9508 1.0279 0.0075  -0.1331 -0.0475 485  ILE B CD1 
18081 N N   . VAL C 486  ? 2.0810 0.8805 1.0793 0.0829  -0.1220 -0.0728 486  VAL B N   
18082 C CA  . VAL C 486  ? 2.1301 0.8334 1.0669 0.1103  -0.1157 -0.0829 486  VAL B CA  
18083 C C   . VAL C 486  ? 2.1763 0.8322 1.1002 0.1370  -0.1108 -0.0815 486  VAL B C   
18084 O O   . VAL C 486  ? 2.2479 0.8537 1.1337 0.1192  -0.1342 -0.0712 486  VAL B O   
18085 C CB  . VAL C 486  ? 2.1908 0.8163 1.0529 0.0809  -0.1445 -0.0795 486  VAL B CB  
18086 C CG1 . VAL C 486  ? 2.2743 0.8185 1.0778 0.1082  -0.1345 -0.0944 486  VAL B CG1 
18087 C CG2 . VAL C 486  ? 2.1373 0.8214 1.0213 0.0397  -0.1601 -0.0730 486  VAL B CG2 
18088 N N   . THR C 487  ? 2.1366 0.8089 1.0953 0.1792  -0.0814 -0.0908 487  THR B N   
18089 C CA  . THR C 487  ? 2.1816 0.8079 1.1321 0.2088  -0.0747 -0.0904 487  THR B CA  
18090 C C   . THR C 487  ? 2.2449 0.7856 1.1450 0.2460  -0.0582 -0.1038 487  THR B C   
18091 O O   . THR C 487  ? 2.2079 0.7720 1.1365 0.2782  -0.0289 -0.1140 487  THR B O   
18092 C CB  . THR C 487  ? 2.1350 0.8428 1.1675 0.2307  -0.0551 -0.0892 487  THR B CB  
18093 O OG1 . THR C 487  ? 2.0892 0.8593 1.1722 0.2493  -0.0295 -0.0992 487  THR B OG1 
18094 C CG2 . THR C 487  ? 2.0661 0.8424 1.1358 0.1968  -0.0739 -0.0753 487  THR B CG2 
18095 N N   . PRO C 488  ? 2.3552 0.7970 1.1806 0.2418  -0.0770 -0.1036 488  PRO B N   
18096 C CA  . PRO C 488  ? 2.4647 0.8147 1.2301 0.2747  -0.0652 -0.1170 488  PRO B CA  
18097 C C   . PRO C 488  ? 2.5579 0.8867 1.3419 0.3191  -0.0427 -0.1213 488  PRO B C   
18098 O O   . PRO C 488  ? 2.5485 0.8089 1.2901 0.3512  -0.0276 -0.1331 488  PRO B O   
18099 C CB  . PRO C 488  ? 2.5229 0.7836 1.2108 0.2479  -0.1002 -0.1130 488  PRO B CB  
18100 C CG  . PRO C 488  ? 2.4808 0.7927 1.1892 0.1990  -0.1279 -0.0971 488  PRO B CG  
18101 C CD  . PRO C 488  ? 2.3980 0.8097 1.1901 0.2023  -0.1133 -0.0898 488  PRO B CD  
18102 N N   . LYS C 489  ? 2.6847 1.0714 1.5306 0.3207  -0.0408 -0.1118 489  LYS B N   
18103 C CA  . LYS C 489  ? 2.8452 1.2240 1.7224 0.3618  -0.0202 -0.1140 489  LYS B CA  
18104 C C   . LYS C 489  ? 3.0064 1.3156 1.8479 0.4060  0.0051  -0.1286 489  LYS B C   
18105 O O   . LYS C 489  ? 3.0210 1.3325 1.8513 0.4184  0.0240  -0.1385 489  LYS B O   
18106 C CB  . LYS C 489  ? 2.7789 1.2635 1.7496 0.3731  -0.0003 -0.1110 489  LYS B CB  
18107 C CG  . LYS C 489  ? 2.8008 1.2850 1.8137 0.4170  0.0222  -0.1130 489  LYS B CG  
18108 C CD  . LYS C 489  ? 2.7595 1.3289 1.8490 0.4104  0.0186  -0.1029 489  LYS B CD  
18109 C CE  . LYS C 489  ? 2.7926 1.3397 1.9068 0.4413  0.0244  -0.0999 489  LYS B CE  
18110 N NZ  . LYS C 489  ? 2.8929 1.3519 1.9455 0.4329  0.0006  -0.0942 489  LYS B NZ  
18111 N N   . SER C 490  ? 3.1376 1.3851 1.9614 0.4295  0.0048  -0.1291 490  SER B N   
18112 C CA  . SER C 490  ? 3.2500 1.4356 2.0503 0.4770  0.0315  -0.1420 490  SER B CA  
18113 C C   . SER C 490  ? 3.3838 1.4545 2.0880 0.4789  0.0171  -0.1513 490  SER B C   
18114 O O   . SER C 490  ? 3.4657 1.4706 2.1461 0.4959  0.0109  -0.1524 490  SER B O   
18115 C CB  . SER C 490  ? 3.2384 1.4748 2.0772 0.5052  0.0691  -0.1502 490  SER B CB  
18116 O OG  . SER C 490  ? 3.1661 1.5066 2.0953 0.5022  0.0782  -0.1419 490  SER B OG  
18117 N N   . PRO C 491  ? 3.4034 1.4482 2.0526 0.4606  0.0090  -0.1580 491  PRO B N   
18118 C CA  . PRO C 491  ? 3.4471 1.3814 2.0024 0.4635  -0.0055 -0.1689 491  PRO B CA  
18119 C C   . PRO C 491  ? 3.3699 1.2343 1.9014 0.4708  -0.0232 -0.1666 491  PRO B C   
18120 O O   . PRO C 491  ? 3.3092 1.1833 1.8538 0.4397  -0.0528 -0.1523 491  PRO B O   
18121 C CB  . PRO C 491  ? 3.5201 1.4559 2.0400 0.4137  -0.0385 -0.1637 491  PRO B CB  
18122 C CG  . PRO C 491  ? 3.4568 1.4974 2.0396 0.4042  -0.0209 -0.1599 491  PRO B CG  
18123 C CD  . PRO C 491  ? 3.3728 1.4864 2.0418 0.4324  0.0076  -0.1554 491  PRO B CD  
18124 N N   . TYR C 492  ? 3.3446 1.1409 1.8436 0.5139  -0.0031 -0.1805 492  TYR B N   
18125 C CA  . TYR C 492  ? 3.3493 1.0780 1.8302 0.5284  -0.0150 -0.1804 492  TYR B CA  
18126 C C   . TYR C 492  ? 3.3974 1.0908 1.8404 0.4820  -0.0620 -0.1701 492  TYR B C   
18127 O O   . TYR C 492  ? 3.4327 1.1057 1.8866 0.4762  -0.0812 -0.1604 492  TYR B O   
18128 C CB  . TYR C 492  ? 3.4288 1.0630 1.8457 0.5702  0.0021  -0.2003 492  TYR B CB  
18129 C CG  . TYR C 492  ? 3.4898 1.0356 1.8080 0.5560  -0.0203 -0.2130 492  TYR B CG  
18130 C CD1 . TYR C 492  ? 3.5654 1.0067 1.8137 0.5891  -0.0162 -0.2311 492  TYR B CD1 
18131 C CD2 . TYR C 492  ? 3.4459 1.0107 1.7408 0.5113  -0.0455 -0.2078 492  TYR B CD2 
18132 C CE1 . TYR C 492  ? 3.6370 0.9947 1.7936 0.5782  -0.0379 -0.2441 492  TYR B CE1 
18133 C CE2 . TYR C 492  ? 3.5184 0.9998 1.7238 0.4992  -0.0678 -0.2195 492  TYR B CE2 
18134 C CZ  . TYR C 492  ? 3.6233 1.0009 1.7590 0.5330  -0.0643 -0.2380 492  TYR B CZ  
18135 O OH  . TYR C 492  ? 3.7279 1.0205 1.7732 0.5221  -0.0881 -0.2510 492  TYR B OH  
18136 N N   . ILE C 493  ? 3.4139 1.1022 1.8160 0.4474  -0.0821 -0.1703 493  ILE B N   
18137 C CA  . ILE C 493  ? 3.5072 1.1726 1.8846 0.3996  -0.1278 -0.1565 493  ILE B CA  
18138 C C   . ILE C 493  ? 3.5056 1.2314 1.8936 0.3497  -0.1481 -0.1447 493  ILE B C   
18139 O O   . ILE C 493  ? 3.4835 1.2675 1.8922 0.3490  -0.1289 -0.1489 493  ILE B O   
18140 C CB  . ILE C 493  ? 4.4817 2.0214 2.7769 0.4029  -0.1556 -0.1647 493  ILE B CB  
18141 C CG1 . ILE C 493  ? 4.4962 2.0091 2.8135 0.4154  -0.1643 -0.1564 493  ILE B CG1 
18142 C CG2 . ILE C 493  ? 4.5269 2.0324 2.7735 0.3533  -0.1996 -0.1570 493  ILE B CG2 
18143 C CD1 . ILE C 493  ? 4.6115 2.0021 2.8556 0.4199  -0.1930 -0.1640 493  ILE B CD1 
18144 N N   . ASP C 494  ? 3.5589 1.2721 1.9378 0.3088  -0.1869 -0.1284 494  ASP B N   
18145 C CA  . ASP C 494  ? 3.5115 1.2842 1.9100 0.2573  -0.2111 -0.1116 494  ASP B CA  
18146 C C   . ASP C 494  ? 3.5987 1.3021 1.9264 0.2239  -0.2473 -0.1120 494  ASP B C   
18147 O O   . ASP C 494  ? 3.5816 1.3177 1.9201 0.1779  -0.2747 -0.0949 494  ASP B O   
18148 C CB  . ASP C 494  ? 3.4937 1.3025 1.9352 0.2337  -0.2305 -0.0891 494  ASP B CB  
18149 C CG  . ASP C 494  ? 3.5148 1.2239 1.9070 0.2299  -0.2620 -0.0840 494  ASP B CG  
18150 O OD1 . ASP C 494  ? 3.5636 1.1912 1.9156 0.2665  -0.2541 -0.1001 494  ASP B OD1 
18151 O OD2 . ASP C 494  ? 3.5203 1.2341 1.9161 0.1907  -0.2946 -0.0633 494  ASP B OD2 
18152 N N   . LYS C 495  ? 3.6825 1.2898 1.9384 0.2464  -0.2487 -0.1309 495  LYS B N   
18153 C CA  . LYS C 495  ? 3.7467 1.2774 1.9311 0.2167  -0.2866 -0.1327 495  LYS B CA  
18154 C C   . LYS C 495  ? 3.6560 1.2279 1.8360 0.1914  -0.2886 -0.1341 495  LYS B C   
18155 O O   . LYS C 495  ? 3.6950 1.1993 1.8085 0.1881  -0.3030 -0.1466 495  LYS B O   
18156 C CB  . LYS C 495  ? 3.8854 1.2947 1.9902 0.2495  -0.2903 -0.1539 495  LYS B CB  
18157 C CG  . LYS C 495  ? 3.9618 1.3039 2.0532 0.2567  -0.3103 -0.1489 495  LYS B CG  
18158 C CD  . LYS C 495  ? 3.9309 1.3078 2.0574 0.2083  -0.3450 -0.1205 495  LYS B CD  
18159 C CE  . LYS C 495  ? 3.8105 1.2893 2.0233 0.2114  -0.3225 -0.1048 495  LYS B CE  
18160 N NZ  . LYS C 495  ? 3.7203 1.2904 1.9806 0.1639  -0.3358 -0.0823 495  LYS B NZ  
18161 N N   . ILE C 496  ? 3.5308 1.2135 1.7827 0.1736  -0.2754 -0.1213 496  ILE B N   
18162 C CA  . ILE C 496  ? 3.4583 1.1948 1.7206 0.1506  -0.2743 -0.1214 496  ILE B CA  
18163 C C   . ILE C 496  ? 3.5240 1.2407 1.7605 0.0975  -0.3192 -0.1073 496  ILE B C   
18164 O O   . ILE C 496  ? 3.5155 1.2543 1.7782 0.0659  -0.3422 -0.0869 496  ILE B O   
18165 C CB  . ILE C 496  ? 3.2869 1.1502 1.6387 0.1503  -0.2458 -0.1133 496  ILE B CB  
18166 C CG1 . ILE C 496  ? 3.1801 1.0656 1.5682 0.2003  -0.2054 -0.1227 496  ILE B CG1 
18167 C CG2 . ILE C 496  ? 3.2930 1.2045 1.6532 0.1374  -0.2384 -0.1182 496  ILE B CG2 
18168 C CD1 . ILE C 496  ? 3.1154 1.0256 1.5488 0.2036  -0.2064 -0.1092 496  ILE B CD1 
18169 N N   . THR C 497  ? 3.6138 1.2874 1.7983 0.0882  -0.3319 -0.1177 497  THR B N   
18170 C CA  . THR C 497  ? 3.7156 1.3711 1.8774 0.0384  -0.3741 -0.1052 497  THR B CA  
18171 C C   . THR C 497  ? 3.6229 1.3907 1.8514 0.0051  -0.3706 -0.0909 497  THR B C   
18172 O O   . THR C 497  ? 3.6058 1.4266 1.8786 -0.0291 -0.3864 -0.0693 497  THR B O   
18173 C CB  . THR C 497  ? 3.8577 1.4192 1.9355 0.0424  -0.3911 -0.1230 497  THR B CB  
18174 O OG1 . THR C 497  ? 3.8975 1.4598 1.9660 -0.0072 -0.4290 -0.1104 497  THR B OG1 
18175 C CG2 . THR C 497  ? 3.8535 1.4366 1.9262 0.0774  -0.3534 -0.1428 497  THR B CG2 
18176 N N   . HIS C 498  ? 3.5730 1.3771 1.8084 0.0164  -0.3491 -0.1030 498  HIS B N   
18177 C CA  . HIS C 498  ? 3.4748 1.3806 1.7703 -0.0125 -0.3455 -0.0928 498  HIS B CA  
18178 C C   . HIS C 498  ? 3.3232 1.3065 1.6698 0.0208  -0.3005 -0.1034 498  HIS B C   
18179 O O   . HIS C 498  ? 3.3675 1.3112 1.6831 0.0617  -0.2761 -0.1215 498  HIS B O   
18180 C CB  . HIS C 498  ? 3.5554 1.4277 1.8082 -0.0401 -0.3718 -0.0957 498  HIS B CB  
18181 C CG  . HIS C 498  ? 3.6677 1.4813 1.8841 -0.0817 -0.4196 -0.0819 498  HIS B CG  
18182 N ND1 . HIS C 498  ? 3.8127 1.5075 1.9448 -0.0779 -0.4465 -0.0919 498  HIS B ND1 
18183 C CD2 . HIS C 498  ? 3.6666 1.5248 1.9208 -0.1282 -0.4457 -0.0583 498  HIS B CD2 
18184 C CE1 . HIS C 498  ? 3.8614 1.5289 1.9829 -0.1210 -0.4888 -0.0745 498  HIS B CE1 
18185 N NE2 . HIS C 498  ? 3.7753 1.5415 1.9704 -0.1523 -0.4883 -0.0531 498  HIS B NE2 
18186 N N   . TYR C 499  ? 3.1491 1.2426 1.5748 0.0035  -0.2897 -0.0916 499  TYR B N   
18187 C CA  . TYR C 499  ? 2.9778 1.1508 1.4556 0.0255  -0.2542 -0.1002 499  TYR B CA  
18188 C C   . TYR C 499  ? 2.9136 1.1009 1.3819 0.0018  -0.2655 -0.1026 499  TYR B C   
18189 O O   . TYR C 499  ? 2.8947 1.0914 1.3640 -0.0417 -0.2964 -0.0899 499  TYR B O   
18190 C CB  . TYR C 499  ? 2.8663 1.1508 1.4336 0.0178  -0.2396 -0.0881 499  TYR B CB  
18191 C CG  . TYR C 499  ? 2.8636 1.1435 1.4480 0.0411  -0.2281 -0.0848 499  TYR B CG  
18192 C CD1 . TYR C 499  ? 2.8372 1.1156 1.4343 0.0892  -0.1939 -0.0976 499  TYR B CD1 
18193 C CD2 . TYR C 499  ? 2.8840 1.1611 1.4731 0.0148  -0.2519 -0.0676 499  TYR B CD2 
18194 C CE1 . TYR C 499  ? 2.8381 1.1113 1.4532 0.1105  -0.1848 -0.0941 499  TYR B CE1 
18195 C CE2 . TYR C 499  ? 2.8900 1.1622 1.4947 0.0351  -0.2432 -0.0636 499  TYR B CE2 
18196 C CZ  . TYR C 499  ? 2.8618 1.1312 1.4797 0.0831  -0.2103 -0.0773 499  TYR B CZ  
18197 O OH  . TYR C 499  ? 2.8549 1.1184 1.4904 0.1024  -0.2040 -0.0726 499  TYR B OH  
18198 N N   . ASN C 500  ? 2.8722 1.0631 1.3339 0.0299  -0.2406 -0.1176 500  ASN B N   
18199 C CA  . ASN C 500  ? 2.8233 1.0320 1.2797 0.0108  -0.2487 -0.1204 500  ASN B CA  
18200 C C   . ASN C 500  ? 2.6932 0.9989 1.2194 0.0272  -0.2152 -0.1244 500  ASN B C   
18201 O O   . ASN C 500  ? 2.6701 0.9823 1.2071 0.0690  -0.1813 -0.1346 500  ASN B O   
18202 C CB  . ASN C 500  ? 2.9420 1.0433 1.3049 0.0250  -0.2583 -0.1349 500  ASN B CB  
18203 C CG  . ASN C 500  ? 3.0488 1.0430 1.3405 0.0323  -0.2775 -0.1380 500  ASN B CG  
18204 O OD1 . ASN C 500  ? 3.0784 1.0512 1.3625 -0.0005 -0.3102 -0.1253 500  ASN B OD1 
18205 N ND2 . ASN C 500  ? 3.1017 1.0275 1.3411 0.0757  -0.2575 -0.1546 500  ASN B ND2 
18206 N N   . TYR C 501  ? 2.5740 0.9554 1.1503 -0.0057 -0.2252 -0.1161 501  TYR B N   
18207 C CA  . TYR C 501  ? 2.4811 0.9526 1.1245 0.0071  -0.1976 -0.1199 501  TYR B CA  
18208 C C   . TYR C 501  ? 2.4771 0.9357 1.0945 -0.0018 -0.2047 -0.1258 501  TYR B C   
18209 O O   . TYR C 501  ? 2.5446 0.9227 1.0896 -0.0171 -0.2313 -0.1277 501  TYR B O   
18210 C CB  . TYR C 501  ? 2.4168 0.9964 1.1475 -0.0192 -0.1992 -0.1076 501  TYR B CB  
18211 C CG  . TYR C 501  ? 2.4663 1.0593 1.1976 -0.0694 -0.2339 -0.0960 501  TYR B CG  
18212 C CD1 . TYR C 501  ? 2.4395 1.0940 1.2104 -0.0887 -0.2366 -0.0955 501  TYR B CD1 
18213 C CD2 . TYR C 501  ? 2.5513 1.0949 1.2459 -0.0976 -0.2645 -0.0847 501  TYR B CD2 
18214 C CE1 . TYR C 501  ? 2.4681 1.1354 1.2429 -0.1348 -0.2686 -0.0842 501  TYR B CE1 
18215 C CE2 . TYR C 501  ? 2.5800 1.1359 1.2783 -0.1440 -0.2964 -0.0723 501  TYR B CE2 
18216 C CZ  . TYR C 501  ? 2.5471 1.1649 1.2855 -0.1624 -0.2981 -0.0722 501  TYR B CZ  
18217 O OH  . TYR C 501  ? 2.5724 1.2014 1.3165 -0.2088 -0.3303 -0.0589 501  TYR B OH  
18218 N N   . LEU C 502  ? 2.4029 0.9434 1.0827 0.0066  -0.1828 -0.1281 502  LEU B N   
18219 C CA  . LEU C 502  ? 2.3906 0.9235 1.0510 0.0077  -0.1819 -0.1346 502  LEU B CA  
18220 C C   . LEU C 502  ? 2.2850 0.9297 1.0378 0.0122  -0.1592 -0.1337 502  LEU B C   
18221 O O   . LEU C 502  ? 2.2366 0.9183 1.0292 0.0472  -0.1262 -0.1384 502  LEU B O   
18222 C CB  . LEU C 502  ? 2.3977 0.8436 0.9841 0.0488  -0.1639 -0.1477 502  LEU B CB  
18223 C CG  . LEU C 502  ? 2.3970 0.7899 0.9219 0.0513  -0.1701 -0.1554 502  LEU B CG  
18224 C CD1 . LEU C 502  ? 2.4210 0.7759 0.9057 0.0059  -0.2146 -0.1502 502  LEU B CD1 
18225 C CD2 . LEU C 502  ? 2.4690 0.7691 0.9151 0.0931  -0.1524 -0.1680 502  LEU B CD2 
18226 N N   . ILE C 503  ? 2.2683 0.9666 1.0579 -0.0233 -0.1781 -0.1276 503  ILE B N   
18227 C CA  . ILE C 503  ? 2.1688 0.9777 1.0524 -0.0239 -0.1614 -0.1263 503  ILE B CA  
18228 C C   . ILE C 503  ? 2.2035 1.0234 1.0878 -0.0277 -0.1628 -0.1297 503  ILE B C   
18229 O O   . ILE C 503  ? 2.2256 1.0236 1.0831 -0.0610 -0.1926 -0.1258 503  ILE B O   
18230 C CB  . ILE C 503  ? 2.1317 1.0188 1.0804 -0.0616 -0.1785 -0.1156 503  ILE B CB  
18231 C CG1 . ILE C 503  ? 2.1490 1.0223 1.0921 -0.0623 -0.1810 -0.1098 503  ILE B CG1 
18232 C CG2 . ILE C 503  ? 2.0173 1.0186 1.0649 -0.0571 -0.1593 -0.1169 503  ILE B CG2 
18233 C CD1 . ILE C 503  ? 2.0901 1.0343 1.0881 -0.0999 -0.1980 -0.0977 503  ILE B CD1 
18234 N N   . LEU C 504  ? 2.1623 1.0174 1.0803 0.0057  -0.1317 -0.1358 504  LEU B N   
18235 C CA  . LEU C 504  ? 2.1517 1.0250 1.0784 0.0061  -0.1291 -0.1379 504  LEU B CA  
18236 C C   . LEU C 504  ? 2.1290 1.1193 1.1620 -0.0063 -0.1237 -0.1345 504  LEU B C   
18237 O O   . LEU C 504  ? 2.0893 1.1461 1.1880 -0.0058 -0.1148 -0.1328 504  LEU B O   
18238 C CB  . LEU C 504  ? 2.1146 0.9537 1.0130 0.0515  -0.0973 -0.1450 504  LEU B CB  
18239 C CG  . LEU C 504  ? 2.1590 0.8849 0.9538 0.0754  -0.0935 -0.1515 504  LEU B CG  
18240 C CD1 . LEU C 504  ? 2.2225 0.8876 0.9670 0.0578  -0.1174 -0.1503 504  LEU B CD1 
18241 C CD2 . LEU C 504  ? 2.0803 0.8102 0.8893 0.1245  -0.0524 -0.1561 504  LEU B CD2 
18242 N N   . SER C 505  ? 2.1483 1.1629 1.1977 -0.0158 -0.1290 -0.1343 505  SER B N   
18243 C CA  . SER C 505  ? 2.0799 1.2033 1.2309 -0.0245 -0.1234 -0.1326 505  SER B CA  
18244 C C   . SER C 505  ? 2.1064 1.2382 1.2609 -0.0321 -0.1303 -0.1321 505  SER B C   
18245 O O   . SER C 505  ? 2.1352 1.2257 1.2442 -0.0608 -0.1591 -0.1291 505  SER B O   
18246 C CB  . SER C 505  ? 2.0232 1.2057 1.2249 -0.0620 -0.1448 -0.1272 505  SER B CB  
18247 O OG  . SER C 505  ? 1.9339 1.2198 1.2324 -0.0680 -0.1389 -0.1276 505  SER B OG  
18248 N N   . LYS C 506  ? 2.0965 1.2840 1.3091 -0.0070 -0.1053 -0.1340 506  LYS B N   
18249 C CA  . LYS C 506  ? 2.1285 1.3169 1.3389 -0.0082 -0.1083 -0.1326 506  LYS B CA  
18250 C C   . LYS C 506  ? 2.2394 1.3164 1.3366 0.0016  -0.1127 -0.1340 506  LYS B C   
18251 O O   . LYS C 506  ? 2.3187 1.3500 1.3645 -0.0250 -0.1414 -0.1320 506  LYS B O   
18252 C CB  . LYS C 506  ? 2.0850 1.3182 1.3337 -0.0510 -0.1393 -0.1285 506  LYS B CB  
18253 C CG  . LYS C 506  ? 1.9563 1.3062 1.3224 -0.0562 -0.1321 -0.1288 506  LYS B CG  
18254 C CD  . LYS C 506  ? 1.9092 1.2997 1.3092 -0.1007 -0.1631 -0.1252 506  LYS B CD  
18255 C CE  . LYS C 506  ? 1.9511 1.2875 1.2929 -0.1229 -0.1827 -0.1222 506  LYS B CE  
18256 N NZ  . LYS C 506  ? 1.8979 1.2746 1.2774 -0.1145 -0.1686 -0.1238 506  LYS B NZ  
18257 N N   . GLY C 507  ? 2.2727 1.3053 1.3314 0.0401  -0.0851 -0.1378 507  GLY B N   
18258 C CA  . GLY C 507  ? 2.3965 1.3268 1.3502 0.0597  -0.0810 -0.1410 507  GLY B CA  
18259 C C   . GLY C 507  ? 2.5192 1.3523 1.3739 0.0386  -0.1114 -0.1435 507  GLY B C   
18260 O O   . GLY C 507  ? 2.6047 1.3479 1.3658 0.0540  -0.1109 -0.1479 507  GLY B O   
18261 N N   . LYS C 508  ? 2.5223 1.3733 1.3978 0.0042  -0.1375 -0.1406 508  LYS B N   
18262 C CA  . LYS C 508  ? 2.5899 1.3582 1.3848 -0.0233 -0.1726 -0.1406 508  LYS B CA  
18263 C C   . LYS C 508  ? 2.5388 1.3004 1.3367 -0.0335 -0.1803 -0.1391 508  LYS B C   
18264 O O   . LYS C 508  ? 2.4529 1.2955 1.3310 -0.0463 -0.1780 -0.1344 508  LYS B O   
18265 C CB  . LYS C 508  ? 2.6123 1.3986 1.4194 -0.0671 -0.2088 -0.1347 508  LYS B CB  
18266 C CG  . LYS C 508  ? 2.7010 1.4193 1.4337 -0.0665 -0.2217 -0.1369 508  LYS B CG  
18267 C CD  . LYS C 508  ? 2.6771 1.4375 1.4477 -0.1034 -0.2498 -0.1304 508  LYS B CD  
18268 C CE  . LYS C 508  ? 2.7233 1.4558 1.4561 -0.0886 -0.2450 -0.1319 508  LYS B CE  
18269 N NZ  . LYS C 508  ? 2.6770 1.4677 1.4656 -0.1181 -0.2654 -0.1251 508  LYS B NZ  
18270 N N   . ILE C 509  ? 2.5666 1.2295 1.2746 -0.0275 -0.1903 -0.1431 509  ILE B N   
18271 C CA  . ILE C 509  ? 2.5161 1.1566 1.2126 -0.0449 -0.2073 -0.1396 509  ILE B CA  
18272 C C   . ILE C 509  ? 2.4758 1.1439 1.1973 -0.0957 -0.2450 -0.1300 509  ILE B C   
18273 O O   . ILE C 509  ? 2.5162 1.1504 1.2015 -0.1172 -0.2706 -0.1291 509  ILE B O   
18274 C CB  . ILE C 509  ? 2.6027 1.1213 1.1896 -0.0321 -0.2174 -0.1464 509  ILE B CB  
18275 C CG1 . ILE C 509  ? 2.5921 1.0778 1.1469 0.0190  -0.1797 -0.1563 509  ILE B CG1 
18276 C CG2 . ILE C 509  ? 2.6249 1.1178 1.2013 -0.0468 -0.2334 -0.1419 509  ILE B CG2 
18277 C CD1 . ILE C 509  ? 2.6980 1.0625 1.1416 0.0369  -0.1862 -0.1657 509  ILE B CD1 
18278 N N   . ILE C 510  ? 2.4005 1.1288 1.1824 -0.1149 -0.2491 -0.1223 510  ILE B N   
18279 C CA  . ILE C 510  ? 2.3809 1.1448 1.1951 -0.1630 -0.2820 -0.1115 510  ILE B CA  
18280 C C   . ILE C 510  ? 2.4188 1.1592 1.2188 -0.1850 -0.3011 -0.1029 510  ILE B C   
18281 O O   . ILE C 510  ? 2.4093 1.1487 1.2107 -0.2258 -0.3335 -0.0926 510  ILE B O   
18282 C CB  . ILE C 510  ? 2.3874 1.2753 1.3105 -0.1742 -0.2711 -0.1078 510  ILE B CB  
18283 C CG1 . ILE C 510  ? 2.3096 1.2598 1.2905 -0.1367 -0.2311 -0.1136 510  ILE B CG1 
18284 C CG2 . ILE C 510  ? 2.3808 1.2838 1.3136 -0.1835 -0.2797 -0.1093 510  ILE B CG2 
18285 C CD1 . ILE C 510  ? 2.1974 1.2677 1.2854 -0.1454 -0.2211 -0.1119 510  ILE B CD1 
18286 N N   . HIS C 511  ? 2.4728 1.1941 1.2606 -0.1581 -0.2814 -0.1059 511  HIS B N   
18287 C CA  . HIS C 511  ? 2.5569 1.2470 1.3243 -0.1754 -0.2987 -0.0972 511  HIS B CA  
18288 C C   . HIS C 511  ? 2.6563 1.2573 1.3525 -0.1408 -0.2872 -0.1056 511  HIS B C   
18289 O O   . HIS C 511  ? 2.6510 1.2418 1.3371 -0.1008 -0.2576 -0.1169 511  HIS B O   
18290 C CB  . HIS C 511  ? 2.5126 1.3023 1.3666 -0.1834 -0.2859 -0.0890 511  HIS B CB  
18291 C CG  . HIS C 511  ? 2.4680 1.3595 1.4041 -0.2079 -0.2879 -0.0842 511  HIS B CG  
18292 N ND1 . HIS C 511  ? 2.4874 1.3906 1.4324 -0.2523 -0.3198 -0.0733 511  HIS B ND1 
18293 C CD2 . HIS C 511  ? 2.3807 1.3670 1.3961 -0.1937 -0.2627 -0.0890 511  HIS B CD2 
18294 C CE1 . HIS C 511  ? 2.4056 1.4069 1.4312 -0.2639 -0.3131 -0.0721 511  HIS B CE1 
18295 N NE2 . HIS C 511  ? 2.3411 1.3936 1.4101 -0.2288 -0.2792 -0.0820 511  HIS B NE2 
18296 N N   . PHE C 512  ? 2.7439 1.2807 1.3928 -0.1566 -0.3110 -0.0994 512  PHE B N   
18297 C CA  . PHE C 512  ? 2.8562 1.3041 1.4373 -0.1268 -0.3043 -0.1068 512  PHE B CA  
18298 C C   . PHE C 512  ? 2.8679 1.2709 1.4215 -0.1568 -0.3367 -0.0948 512  PHE B C   
18299 O O   . PHE C 512  ? 2.8550 1.2627 1.4126 -0.1985 -0.3688 -0.0836 512  PHE B O   
18300 C CB  . PHE C 512  ? 3.0052 1.3593 1.5005 -0.1061 -0.3070 -0.1206 512  PHE B CB  
18301 C CG  . PHE C 512  ? 3.1246 1.4152 1.5641 -0.1414 -0.3496 -0.1173 512  PHE B CG  
18302 C CD1 . PHE C 512  ? 3.2569 1.4296 1.6003 -0.1354 -0.3704 -0.1245 512  PHE B CD1 
18303 C CD2 . PHE C 512  ? 3.1038 1.4531 1.5897 -0.1808 -0.3702 -0.1070 512  PHE B CD2 
18304 C CE1 . PHE C 512  ? 3.3353 1.4488 1.6293 -0.1683 -0.4122 -0.1215 512  PHE B CE1 
18305 C CE2 . PHE C 512  ? 3.1717 1.4640 1.6109 -0.2141 -0.4110 -0.1029 512  PHE B CE2 
18306 C CZ  . PHE C 512  ? 3.2916 1.4653 1.6345 -0.2083 -0.4329 -0.1100 512  PHE B CZ  
18307 N N   . GLY C 513  ? 2.9166 1.2772 1.4455 -0.1364 -0.3291 -0.0959 513  GLY B N   
18308 C CA  . GLY C 513  ? 2.9679 1.2935 1.4792 -0.1646 -0.3585 -0.0822 513  GLY B CA  
18309 C C   . GLY C 513  ? 3.0087 1.2832 1.4916 -0.1383 -0.3492 -0.0843 513  GLY B C   
18310 O O   . GLY C 513  ? 3.0012 1.2494 1.4646 -0.0948 -0.3209 -0.0985 513  GLY B O   
18311 N N   . THR C 514  ? 3.0400 1.3015 1.5230 -0.1653 -0.3734 -0.0688 514  THR B N   
18312 C CA  . THR C 514  ? 3.0946 1.2998 1.5474 -0.1444 -0.3705 -0.0691 514  THR B CA  
18313 C C   . THR C 514  ? 3.0659 1.3133 1.5609 -0.1720 -0.3833 -0.0479 514  THR B C   
18314 O O   . THR C 514  ? 3.0654 1.3222 1.5678 -0.2155 -0.4138 -0.0313 514  THR B O   
18315 C CB  . THR C 514  ? 3.2591 1.3316 1.6135 -0.1370 -0.3950 -0.0788 514  THR B CB  
18316 O OG1 . THR C 514  ? 3.2830 1.3153 1.5985 -0.0925 -0.3684 -0.1006 514  THR B OG1 
18317 C CG2 . THR C 514  ? 3.3203 1.3332 1.6473 -0.1350 -0.4088 -0.0718 514  THR B CG2 
18318 N N   . ARG C 515  ? 3.0324 1.3088 1.5576 -0.1464 -0.3591 -0.0476 515  ARG B N   
18319 C CA  . ARG C 515  ? 3.0634 1.3637 1.6156 -0.1666 -0.3706 -0.0283 515  ARG B CA  
18320 C C   . ARG C 515  ? 3.1277 1.3295 1.6216 -0.1463 -0.3791 -0.0311 515  ARG B C   
18321 O O   . ARG C 515  ? 3.1440 1.3042 1.6116 -0.1033 -0.3565 -0.0488 515  ARG B O   
18322 C CB  . ARG C 515  ? 3.0306 1.4394 1.6630 -0.1539 -0.3395 -0.0250 515  ARG B CB  
18323 C CG  . ARG C 515  ? 3.0079 1.5147 1.7011 -0.1643 -0.3254 -0.0271 515  ARG B CG  
18324 C CD  . ARG C 515  ? 3.0855 1.5978 1.7746 -0.2117 -0.3570 -0.0149 515  ARG B CD  
18325 N NE  . ARG C 515  ? 3.0569 1.6632 1.8066 -0.2215 -0.3442 -0.0174 515  ARG B NE  
18326 C CZ  . ARG C 515  ? 3.0221 1.7343 1.8473 -0.2245 -0.3260 -0.0119 515  ARG B CZ  
18327 N NH1 . ARG C 515  ? 3.0210 1.7576 1.8677 -0.2186 -0.3184 -0.0031 515  ARG B NH1 
18328 N NH2 . ARG C 515  ? 2.9713 1.7637 1.8498 -0.2326 -0.3160 -0.0158 515  ARG B NH2 
18329 N N   . GLU C 516  ? 3.1465 1.3115 1.6220 -0.1768 -0.4112 -0.0131 516  GLU B N   
18330 C CA  . GLU C 516  ? 3.1964 1.2723 1.6235 -0.1590 -0.4210 -0.0141 516  GLU B CA  
18331 C C   . GLU C 516  ? 3.0946 1.2203 1.5672 -0.1304 -0.3912 -0.0131 516  GLU B C   
18332 O O   . GLU C 516  ? 2.9878 1.2119 1.5268 -0.1432 -0.3793 -0.0011 516  GLU B O   
18333 C CB  . GLU C 516  ? 3.2680 1.2943 1.6687 -0.2007 -0.4648 0.0072  516  GLU B CB  
18334 C CG  . GLU C 516  ? 3.3655 1.2988 1.7190 -0.1832 -0.4773 0.0069  516  GLU B CG  
18335 C CD  . GLU C 516  ? 3.4842 1.3085 1.7688 -0.2059 -0.5217 0.0104  516  GLU B CD  
18336 O OE1 . GLU C 516  ? 3.5364 1.3052 1.8001 -0.2104 -0.5422 0.0211  516  GLU B OE1 
18337 O OE2 . GLU C 516  ? 3.5260 1.3175 1.7772 -0.2184 -0.5375 0.0022  516  GLU B OE2 
18338 N N   . LYS C 517  ? 3.1466 1.2053 1.5840 -0.0903 -0.3788 -0.0267 517  LYS B N   
18339 C CA  . LYS C 517  ? 3.1185 1.2166 1.5975 -0.0604 -0.3518 -0.0265 517  LYS B CA  
18340 C C   . LYS C 517  ? 3.2187 1.3104 1.7062 -0.0812 -0.3732 -0.0047 517  LYS B C   
18341 O O   . LYS C 517  ? 3.3382 1.3433 1.7738 -0.0944 -0.4039 0.0016  517  LYS B O   
18342 C CB  . LYS C 517  ? 3.1063 1.1380 1.5493 -0.0083 -0.3287 -0.0486 517  LYS B CB  
18343 C CG  . LYS C 517  ? 3.0101 1.0966 1.5075 0.0269  -0.2948 -0.0510 517  LYS B CG  
18344 C CD  . LYS C 517  ? 3.0361 1.0653 1.5168 0.0429  -0.3020 -0.0461 517  LYS B CD  
18345 C CE  . LYS C 517  ? 2.9535 1.0318 1.4864 0.0834  -0.2661 -0.0519 517  LYS B CE  
18346 N NZ  . LYS C 517  ? 3.0089 1.0023 1.5063 0.1224  -0.2597 -0.0621 517  LYS B NZ  
18347 N N   . PHE C 518  ? 3.1877 1.3697 1.7402 -0.0833 -0.3578 0.0069  518  PHE B N   
18348 C CA  . PHE C 518  ? 3.2514 1.4368 1.8156 -0.1029 -0.3760 0.0295  518  PHE B CA  
18349 C C   . PHE C 518  ? 3.3454 1.4488 1.8759 -0.0719 -0.3772 0.0248  518  PHE B C   
18350 O O   . PHE C 518  ? 3.2806 1.4063 1.8388 -0.0353 -0.3500 0.0162  518  PHE B O   
18351 C CB  . PHE C 518  ? 3.2004 1.5040 1.8396 -0.1106 -0.3581 0.0411  518  PHE B CB  
18352 C CG  . PHE C 518  ? 3.2146 1.5926 1.8850 -0.1531 -0.3679 0.0540  518  PHE B CG  
18353 C CD1 . PHE C 518  ? 3.2919 1.6243 1.9246 -0.1898 -0.3998 0.0635  518  PHE B CD1 
18354 C CD2 . PHE C 518  ? 3.1539 1.6461 1.8923 -0.1563 -0.3467 0.0568  518  PHE B CD2 
18355 C CE1 . PHE C 518  ? 3.2711 1.6719 1.9355 -0.2291 -0.4090 0.0764  518  PHE B CE1 
18356 C CE2 . PHE C 518  ? 3.1308 1.6921 1.8994 -0.1947 -0.3552 0.0682  518  PHE B CE2 
18357 C CZ  . PHE C 518  ? 3.1877 1.7039 1.9202 -0.2313 -0.3858 0.0786  518  PHE B CZ  
18358 N N   . SER C 519  ? 3.5067 1.5156 1.9799 -0.0882 -0.4109 0.0313  519  SER B N   
18359 C CA  . SER C 519  ? 3.6369 1.5470 2.0646 -0.0595 -0.4174 0.0233  519  SER B CA  
18360 C C   . SER C 519  ? 3.6439 1.5855 2.1112 -0.0307 -0.3961 0.0258  519  SER B C   
18361 O O   . SER C 519  ? 3.6908 1.5954 2.1482 0.0138  -0.3744 0.0075  519  SER B O   
18362 C CB  . SER C 519  ? 3.7179 1.5512 2.1018 -0.0940 -0.4627 0.0411  519  SER B CB  
18363 O OG  . SER C 519  ? 3.7235 1.5541 2.0893 -0.1322 -0.4861 0.0469  519  SER B OG  
18364 N N   . ASP C 520  ? 3.6044 1.6148 2.1169 -0.0567 -0.4029 0.0493  520  ASP B N   
18365 C CA  . ASP C 520  ? 3.6021 1.6510 2.1562 -0.0335 -0.3855 0.0541  520  ASP B CA  
18366 C C   . ASP C 520  ? 3.4971 1.6118 2.0960 0.0050  -0.3432 0.0344  520  ASP B C   
18367 O O   . ASP C 520  ? 3.5191 1.5861 2.0984 0.0454  -0.3240 0.0128  520  ASP B O   
18368 C CB  . ASP C 520  ? 3.6744 1.7930 2.2672 -0.0714 -0.4004 0.0835  520  ASP B CB  
18369 C CG  . ASP C 520  ? 3.7399 1.9476 2.3649 -0.1065 -0.3990 0.0916  520  ASP B CG  
18370 O OD1 . ASP C 520  ? 3.7749 1.9886 2.3929 -0.1030 -0.3886 0.0750  520  ASP B OD1 
18371 O OD2 . ASP C 520  ? 3.7576 2.0298 2.4150 -0.1372 -0.4081 0.1150  520  ASP B OD2 
18372 N N   . ALA C 521  ? 3.3633 1.5870 2.0222 -0.0078 -0.3290 0.0420  521  ALA B N   
18373 C CA  . ALA C 521  ? 3.2092 1.5043 1.9230 0.0273  -0.2922 0.0284  521  ALA B CA  
18374 C C   . ALA C 521  ? 3.0447 1.3354 1.7547 0.0577  -0.2654 0.0031  521  ALA B C   
18375 O O   . ALA C 521  ? 3.0658 1.3088 1.7312 0.0484  -0.2742 -0.0050 521  ALA B O   
18376 C CB  . ALA C 521  ? 3.1562 1.5676 1.9328 0.0043  -0.2867 0.0420  521  ALA B CB  
18377 N N   . SER C 522  ? 2.8655 1.2063 1.6236 0.0940  -0.2334 -0.0083 522  SER B N   
18378 C CA  . SER C 522  ? 2.7475 1.0965 1.5136 0.1265  -0.2035 -0.0300 522  SER B CA  
18379 C C   . SER C 522  ? 2.6362 1.0426 1.4157 0.1023  -0.2012 -0.0332 522  SER B C   
18380 O O   . SER C 522  ? 2.6840 1.0402 1.4137 0.0868  -0.2147 -0.0375 522  SER B O   
18381 C CB  . SER C 522  ? 2.6635 1.0702 1.4925 0.1650  -0.1724 -0.0367 522  SER B CB  
18382 O OG  . SER C 522  ? 2.6356 1.0469 1.4744 0.1995  -0.1420 -0.0560 522  SER B OG  
18383 N N   . TYR C 523  ? 2.4680 0.9787 1.3156 0.0996  -0.1854 -0.0313 523  TYR B N   
18384 C CA  . TYR C 523  ? 2.3355 0.9104 1.2084 0.0835  -0.1784 -0.0364 523  TYR B CA  
18385 C C   . TYR C 523  ? 2.2804 0.8908 1.1540 0.0328  -0.2045 -0.0200 523  TYR B C   
18386 O O   . TYR C 523  ? 2.2553 0.8877 1.1411 0.0114  -0.2198 -0.0027 523  TYR B O   
18387 C CB  . TYR C 523  ? 2.2396 0.9134 1.1906 0.1045  -0.1504 -0.0426 523  TYR B CB  
18388 C CG  . TYR C 523  ? 2.1840 0.9216 1.1829 0.0964  -0.1541 -0.0293 523  TYR B CG  
18389 C CD1 . TYR C 523  ? 2.1376 0.9503 1.1665 0.0588  -0.1667 -0.0168 523  TYR B CD1 
18390 C CD2 . TYR C 523  ? 2.1624 0.8866 1.1773 0.1273  -0.1445 -0.0295 523  TYR B CD2 
18391 C CE1 . TYR C 523  ? 2.0830 0.9533 1.1513 0.0529  -0.1694 -0.0053 523  TYR B CE1 
18392 C CE2 . TYR C 523  ? 2.1012 0.8815 1.1569 0.1209  -0.1488 -0.0179 523  TYR B CE2 
18393 C CZ  . TYR C 523  ? 2.0755 0.9279 1.1553 0.0840  -0.1611 -0.0060 523  TYR B CZ  
18394 O OH  . TYR C 523  ? 2.0555 0.9626 1.1714 0.0788  -0.1651 0.0052  523  TYR B OH  
18395 N N   . GLN C 524  ? 2.2821 0.9044 1.1472 0.0136  -0.2085 -0.0244 524  GLN B N   
18396 C CA  . GLN C 524  ? 2.2977 0.9843 1.1873 -0.0310 -0.2253 -0.0102 524  GLN B CA  
18397 C C   . GLN C 524  ? 2.2677 1.0368 1.2057 -0.0335 -0.2088 -0.0199 524  GLN B C   
18398 O O   . GLN C 524  ? 2.2463 1.0349 1.2087 0.0005  -0.1824 -0.0362 524  GLN B O   
18399 C CB  . GLN C 524  ? 2.3717 0.9891 1.2020 -0.0672 -0.2590 0.0011  524  GLN B CB  
18400 C CG  . GLN C 524  ? 2.4152 0.9692 1.1977 -0.0619 -0.2620 -0.0130 524  GLN B CG  
18401 C CD  . GLN C 524  ? 2.5361 0.9794 1.2439 -0.0733 -0.2910 -0.0080 524  GLN B CD  
18402 O OE1 . GLN C 524  ? 2.5749 0.9628 1.2587 -0.0564 -0.2943 -0.0058 524  GLN B OE1 
18403 N NE2 . GLN C 524  ? 2.5897 0.9985 1.2615 -0.1025 -0.3143 -0.0059 524  GLN B NE2 
18404 N N   . SER C 525  ? 2.2613 1.0822 1.2175 -0.0741 -0.2244 -0.0085 525  SER B N   
18405 C CA  . SER C 525  ? 2.2135 1.1144 1.2181 -0.0806 -0.2123 -0.0164 525  SER B CA  
18406 C C   . SER C 525  ? 2.2520 1.1056 1.2134 -0.1038 -0.2304 -0.0175 525  SER B C   
18407 O O   . SER C 525  ? 2.2892 1.0783 1.1999 -0.1299 -0.2580 -0.0057 525  SER B O   
18408 C CB  . SER C 525  ? 2.1729 1.1761 1.2365 -0.1084 -0.2149 -0.0039 525  SER B CB  
18409 O OG  . SER C 525  ? 2.1812 1.2118 1.2681 -0.0970 -0.2089 0.0031  525  SER B OG  
18410 N N   . ILE C 526  ? 2.2305 1.1124 1.2115 -0.0933 -0.2160 -0.0316 526  ILE B N   
18411 C CA  . ILE C 526  ? 2.2077 1.0640 1.1602 -0.1181 -0.2331 -0.0325 526  ILE B CA  
18412 C C   . ILE C 526  ? 2.0890 1.0507 1.1092 -0.1394 -0.2288 -0.0308 526  ILE B C   
18413 O O   . ILE C 526  ? 1.9848 1.0138 1.0595 -0.1168 -0.2040 -0.0419 526  ILE B O   
18414 C CB  . ILE C 526  ? 2.1647 0.9594 1.0772 -0.0879 -0.2212 -0.0505 526  ILE B CB  
18415 C CG1 . ILE C 526  ? 2.2106 0.9106 1.0655 -0.0561 -0.2168 -0.0564 526  ILE B CG1 
18416 C CG2 . ILE C 526  ? 2.2211 0.9741 1.0922 -0.1163 -0.2451 -0.0495 526  ILE B CG2 
18417 C CD1 . ILE C 526  ? 2.1649 0.7867 0.9621 -0.0323 -0.2111 -0.0719 526  ILE B CD1 
18418 N N   . ASN C 527  ? 2.1622 1.1404 1.1831 -0.1828 -0.2533 -0.0168 527  ASN B N   
18419 C CA  . ASN C 527  ? 2.1429 1.2244 1.2319 -0.2019 -0.2482 -0.0156 527  ASN B CA  
18420 C C   . ASN C 527  ? 2.2043 1.2866 1.2916 -0.2183 -0.2573 -0.0209 527  ASN B C   
18421 O O   . ASN C 527  ? 2.2560 1.3140 1.3199 -0.2549 -0.2842 -0.0093 527  ASN B O   
18422 C CB  . ASN C 527  ? 2.1553 1.2893 1.2710 -0.2373 -0.2621 0.0042  527  ASN B CB  
18423 C CG  . ASN C 527  ? 2.0892 1.3424 1.2852 -0.2429 -0.2469 0.0019  527  ASN B CG  
18424 O OD1 . ASN C 527  ? 2.0460 1.3416 1.2718 -0.2570 -0.2483 -0.0026 527  ASN B OD1 
18425 N ND2 . ASN C 527  ? 2.0800 1.3882 1.3123 -0.2308 -0.2328 0.0041  527  ASN B ND2 
18426 N N   . ILE C 528  ? 2.2026 1.3154 1.3186 -0.1917 -0.2356 -0.0375 528  ILE B N   
18427 C CA  . ILE C 528  ? 2.2487 1.3677 1.3681 -0.2040 -0.2423 -0.0433 528  ILE B CA  
18428 C C   . ILE C 528  ? 2.1662 1.3978 1.3668 -0.2227 -0.2377 -0.0420 528  ILE B C   
18429 O O   . ILE C 528  ? 2.1119 1.4185 1.3731 -0.2011 -0.2138 -0.0503 528  ILE B O   
18430 C CB  . ILE C 528  ? 2.2740 1.3626 1.3790 -0.1649 -0.2215 -0.0611 528  ILE B CB  
18431 C CG1 . ILE C 528  ? 2.3714 1.3592 1.4052 -0.1373 -0.2183 -0.0651 528  ILE B CG1 
18432 C CG2 . ILE C 528  ? 2.3142 1.3910 1.4075 -0.1790 -0.2328 -0.0655 528  ILE B CG2 
18433 C CD1 . ILE C 528  ? 2.3423 1.3544 1.4039 -0.1055 -0.1945 -0.0680 528  ILE B CD1 
18434 N N   . PRO C 529  ? 2.1788 1.4226 1.3828 -0.2627 -0.2612 -0.0319 529  PRO B N   
18435 C CA  . PRO C 529  ? 2.1005 1.4432 1.3786 -0.2776 -0.2567 -0.0341 529  PRO B CA  
18436 C C   . PRO C 529  ? 2.0940 1.4558 1.3971 -0.2466 -0.2364 -0.0525 529  PRO B C   
18437 O O   . PRO C 529  ? 2.1512 1.4362 1.4002 -0.2287 -0.2364 -0.0597 529  PRO B O   
18438 C CB  . PRO C 529  ? 2.1438 1.4608 1.4001 -0.3206 -0.2882 -0.0219 529  PRO B CB  
18439 C CG  . PRO C 529  ? 2.2166 1.4574 1.4112 -0.3366 -0.3087 -0.0072 529  PRO B CG  
18440 C CD  . PRO C 529  ? 2.2489 1.4224 1.3961 -0.2971 -0.2938 -0.0167 529  PRO B CD  
18441 N N   . VAL C 530  ? 1.9872 1.4483 1.3696 -0.2391 -0.2191 -0.0598 530  VAL B N   
18442 C CA  . VAL C 530  ? 1.9440 1.4287 1.3564 -0.2190 -0.2057 -0.0739 530  VAL B CA  
18443 C C   . VAL C 530  ? 1.9194 1.4218 1.3451 -0.2539 -0.2271 -0.0695 530  VAL B C   
18444 O O   . VAL C 530  ? 1.8760 1.4468 1.3497 -0.2829 -0.2361 -0.0622 530  VAL B O   
18445 C CB  . VAL C 530  ? 1.5548 1.1342 1.0489 -0.1922 -0.1787 -0.0852 530  VAL B CB  
18446 C CG1 . VAL C 530  ? 1.4833 1.1624 1.0523 -0.2167 -0.1831 -0.0846 530  VAL B CG1 
18447 C CG2 . VAL C 530  ? 1.5383 1.1072 1.0404 -0.1563 -0.1595 -0.0988 530  VAL B CG2 
18448 N N   . THR C 531  ? 1.9580 1.3959 1.3381 -0.2519 -0.2363 -0.0731 531  THR B N   
18449 C CA  . THR C 531  ? 1.9623 1.4103 1.3522 -0.2844 -0.2587 -0.0689 531  THR B CA  
18450 C C   . THR C 531  ? 1.9198 1.4203 1.3621 -0.2717 -0.2475 -0.0800 531  THR B C   
18451 O O   . THR C 531  ? 1.8978 1.3944 1.3438 -0.2354 -0.2250 -0.0911 531  THR B O   
18452 C CB  . THR C 531  ? 2.0682 1.4084 1.3709 -0.2992 -0.2847 -0.0635 531  THR B CB  
18453 O OG1 . THR C 531  ? 2.0700 1.4300 1.3918 -0.3361 -0.3097 -0.0567 531  THR B OG1 
18454 C CG2 . THR C 531  ? 2.0999 1.3764 1.3552 -0.2648 -0.2724 -0.0758 531  THR B CG2 
18455 N N   . GLN C 532  ? 1.9158 1.4628 1.3984 -0.3032 -0.2647 -0.0756 532  GLN B N   
18456 C CA  . GLN C 532  ? 1.8908 1.4903 1.4276 -0.2974 -0.2591 -0.0843 532  GLN B CA  
18457 C C   . GLN C 532  ? 1.9591 1.4850 1.4413 -0.2740 -0.2559 -0.0910 532  GLN B C   
18458 O O   . GLN C 532  ? 1.9258 1.4890 1.4486 -0.2570 -0.2436 -0.0992 532  GLN B O   
18459 C CB  . GLN C 532  ? 1.8965 1.5372 1.4700 -0.3393 -0.2841 -0.0762 532  GLN B CB  
18460 C CG  . GLN C 532  ? 1.8688 1.5571 1.4956 -0.3378 -0.2839 -0.0836 532  GLN B CG  
18461 C CD  . GLN C 532  ? 1.7666 1.5649 1.4904 -0.3212 -0.2608 -0.0939 532  GLN B CD  
18462 O OE1 . GLN C 532  ? 1.7340 1.5851 1.4927 -0.3186 -0.2489 -0.0942 532  GLN B OE1 
18463 N NE2 . GLN C 532  ? 1.7081 1.5405 1.4756 -0.3098 -0.2558 -0.1022 532  GLN B NE2 
18464 N N   . ASN C 533  ? 2.0500 1.4716 1.4401 -0.2724 -0.2670 -0.0875 533  ASN B N   
18465 C CA  . ASN C 533  ? 2.1052 1.4534 1.4360 -0.2472 -0.2614 -0.0945 533  ASN B CA  
18466 C C   . ASN C 533  ? 2.0602 1.4121 1.3973 -0.2003 -0.2263 -0.1043 533  ASN B C   
18467 O O   . ASN C 533  ? 2.0861 1.4013 1.3949 -0.1749 -0.2145 -0.1104 533  ASN B O   
18468 C CB  . ASN C 533  ? 2.2384 1.4705 1.4658 -0.2581 -0.2846 -0.0896 533  ASN B CB  
18469 C CG  . ASN C 533  ? 2.2957 1.5152 1.5137 -0.3036 -0.3216 -0.0793 533  ASN B CG  
18470 O OD1 . ASN C 533  ? 2.3541 1.5441 1.5455 -0.3284 -0.3414 -0.0694 533  ASN B OD1 
18471 N ND2 . ASN C 533  ? 2.2801 1.5229 1.5229 -0.3154 -0.3321 -0.0803 533  ASN B ND2 
18472 N N   . MET C 534  ? 1.9853 1.3805 1.3586 -0.1890 -0.2101 -0.1048 534  MET B N   
18473 C CA  . MET C 534  ? 1.9278 1.3273 1.3111 -0.1457 -0.1785 -0.1129 534  MET B CA  
18474 C C   . MET C 534  ? 1.7996 1.2981 1.2777 -0.1302 -0.1590 -0.1200 534  MET B C   
18475 O O   . MET C 534  ? 1.7623 1.2781 1.2649 -0.0945 -0.1328 -0.1265 534  MET B O   
18476 C CB  . MET C 534  ? 1.9180 1.3120 1.2925 -0.1415 -0.1734 -0.1096 534  MET B CB  
18477 C CG  . MET C 534  ? 1.9982 1.3158 1.2991 -0.1689 -0.1999 -0.0998 534  MET B CG  
18478 S SD  . MET C 534  ? 1.9366 1.2582 1.2353 -0.1732 -0.1994 -0.0921 534  MET B SD  
18479 C CE  . MET C 534  ? 1.6565 0.9220 0.9182 -0.1218 -0.1711 -0.1013 534  MET B CE  
18480 N N   . VAL C 535  ? 1.7541 1.3141 1.2853 -0.1571 -0.1732 -0.1186 535  VAL B N   
18481 C CA  . VAL C 535  ? 1.6541 1.3240 1.2882 -0.1528 -0.1614 -0.1246 535  VAL B CA  
18482 C C   . VAL C 535  ? 1.6006 1.3110 1.2861 -0.1131 -0.1334 -0.1340 535  VAL B C   
18483 O O   . VAL C 535  ? 1.5502 1.3407 1.3106 -0.1032 -0.1209 -0.1396 535  VAL B O   
18484 C CB  . VAL C 535  ? 1.6421 1.3594 1.3190 -0.1853 -0.1819 -0.1224 535  VAL B CB  
18485 C CG1 . VAL C 535  ? 1.6212 1.3888 1.3298 -0.2203 -0.1978 -0.1164 535  VAL B CG1 
18486 C CG2 . VAL C 535  ? 1.7320 1.3685 1.3394 -0.1976 -0.2007 -0.1177 535  VAL B CG2 
18487 N N   . PRO C 536  ? 1.6178 1.2783 1.2684 -0.0912 -0.1242 -0.1354 536  PRO B N   
18488 C CA  . PRO C 536  ? 1.5209 1.2373 1.2383 -0.0560 -0.0975 -0.1425 536  PRO B CA  
18489 C C   . PRO C 536  ? 1.4821 1.1720 1.1802 -0.0237 -0.0757 -0.1447 536  PRO B C   
18490 O O   . PRO C 536  ? 1.4318 1.1839 1.1964 -0.0028 -0.0587 -0.1501 536  PRO B O   
18491 C CB  . PRO C 536  ? 1.5839 1.2670 1.2810 -0.0431 -0.0932 -0.1417 536  PRO B CB  
18492 C CG  . PRO C 536  ? 1.6671 1.3106 1.3168 -0.0804 -0.1231 -0.1359 536  PRO B CG  
18493 C CD  . PRO C 536  ? 1.7034 1.3028 1.2984 -0.1025 -0.1390 -0.1317 536  PRO B CD  
18494 N N   . SER C 537  ? 1.5144 1.1095 1.1207 -0.0200 -0.0780 -0.1408 537  SER B N   
18495 C CA  . SER C 537  ? 1.5095 1.0628 1.0830 0.0082  -0.0605 -0.1418 537  SER B CA  
18496 C C   . SER C 537  ? 1.6305 1.0745 1.0961 -0.0008 -0.0740 -0.1373 537  SER B C   
18497 O O   . SER C 537  ? 1.6868 1.1024 1.1170 -0.0296 -0.0970 -0.1336 537  SER B O   
18498 C CB  . SER C 537  ? 1.4314 0.9947 1.0345 0.0523  -0.0300 -0.1462 537  SER B CB  
18499 O OG  . SER C 537  ? 1.4735 0.9603 1.0096 0.0685  -0.0227 -0.1446 537  SER B OG  
18500 N N   . SER C 538  ? 1.6265 1.0089 1.0415 0.0235  -0.0613 -0.1378 538  SER B N   
18501 C CA  . SER C 538  ? 1.6452 0.9192 0.9565 0.0201  -0.0728 -0.1355 538  SER B CA  
18502 C C   . SER C 538  ? 1.6518 0.8811 0.9356 0.0593  -0.0487 -0.1386 538  SER B C   
18503 O O   . SER C 538  ? 1.6088 0.8938 0.9552 0.0822  -0.0281 -0.1409 538  SER B O   
18504 C CB  . SER C 538  ? 1.6428 0.8997 0.9266 -0.0181 -0.1017 -0.1290 538  SER B CB  
18505 O OG  . SER C 538  ? 1.5847 0.8872 0.8996 -0.0560 -0.1244 -0.1250 538  SER B OG  
18506 N N   . ARG C 539  ? 1.7046 0.8333 0.8965 0.0678  -0.0519 -0.1392 539  ARG B N   
18507 C CA  . ARG C 539  ? 1.7288 0.8118 0.8917 0.0971  -0.0358 -0.1411 539  ARG B CA  
18508 C C   . ARG C 539  ? 1.8148 0.8144 0.8969 0.0776  -0.0600 -0.1382 539  ARG B C   
18509 O O   . ARG C 539  ? 1.8090 0.7596 0.8354 0.0519  -0.0844 -0.1366 539  ARG B O   
18510 C CB  . ARG C 539  ? 1.7014 0.7384 0.8336 0.1398  -0.0076 -0.1463 539  ARG B CB  
18511 C CG  . ARG C 539  ? 1.6936 0.7850 0.8774 0.1539  0.0101  -0.1474 539  ARG B CG  
18512 C CD  . ARG C 539  ? 1.8002 0.8391 0.9464 0.1967  0.0390  -0.1506 539  ARG B CD  
18513 N NE  . ARG C 539  ? 1.7958 0.8936 1.0178 0.2293  0.0683  -0.1506 539  ARG B NE  
18514 C CZ  . ARG C 539  ? 1.8104 0.9825 1.1081 0.2393  0.0832  -0.1491 539  ARG B CZ  
18515 N NH1 . ARG C 539  ? 1.7876 0.9815 1.0918 0.2190  0.0714  -0.1475 539  ARG B NH1 
18516 N NH2 . ARG C 539  ? 1.7792 1.0029 1.1478 0.2692  0.1081  -0.1488 539  ARG B NH2 
18517 N N   . LEU C 540  ? 1.8457 0.8286 0.9230 0.0895  -0.0549 -0.1371 540  LEU B N   
18518 C CA  . LEU C 540  ? 1.9523 0.8427 0.9469 0.0797  -0.0742 -0.1351 540  LEU B CA  
18519 C C   . LEU C 540  ? 1.9925 0.8209 0.9495 0.1206  -0.0528 -0.1403 540  LEU B C   
18520 O O   . LEU C 540  ? 1.9147 0.7846 0.9231 0.1528  -0.0246 -0.1428 540  LEU B O   
18521 C CB  . LEU C 540  ? 1.9955 0.9077 1.0028 0.0413  -0.1011 -0.1252 540  LEU B CB  
18522 C CG  . LEU C 540  ? 2.0044 0.9682 1.0632 0.0425  -0.0960 -0.1199 540  LEU B CG  
18523 C CD1 . LEU C 540  ? 2.0494 0.9762 1.0956 0.0837  -0.0732 -0.1243 540  LEU B CD1 
18524 C CD2 . LEU C 540  ? 2.0452 0.9915 1.0793 0.0021  -0.1277 -0.1084 540  LEU B CD2 
18525 N N   . LEU C 541  ? 2.0970 0.8241 0.9644 0.1189  -0.0678 -0.1421 541  LEU B N   
18526 C CA  . LEU C 541  ? 2.1571 0.8104 0.9751 0.1560  -0.0509 -0.1483 541  LEU B CA  
18527 C C   . LEU C 541  ? 2.2771 0.8541 1.0305 0.1345  -0.0809 -0.1448 541  LEU B C   
18528 O O   . LEU C 541  ? 2.3109 0.8643 1.0312 0.0975  -0.1123 -0.1404 541  LEU B O   
18529 C CB  . LEU C 541  ? 2.1763 0.7772 0.9434 0.1841  -0.0334 -0.1577 541  LEU B CB  
18530 C CG  . LEU C 541  ? 2.3014 0.7934 0.9794 0.2135  -0.0265 -0.1663 541  LEU B CG  
18531 C CD1 . LEU C 541  ? 2.2336 0.7202 0.9081 0.2568  0.0103  -0.1735 541  LEU B CD1 
18532 C CD2 . LEU C 541  ? 2.3826 0.7897 0.9712 0.1857  -0.0614 -0.1686 541  LEU B CD2 
18533 N N   . VAL C 542  ? 2.3427 0.8846 1.0842 0.1568  -0.0723 -0.1455 542  VAL B N   
18534 C CA  . VAL C 542  ? 2.4504 0.9341 1.1474 0.1360  -0.1004 -0.1397 542  VAL B CA  
18535 C C   . VAL C 542  ? 2.5926 0.9837 1.2274 0.1722  -0.0893 -0.1484 542  VAL B C   
18536 O O   . VAL C 542  ? 2.5715 0.9779 1.2350 0.2111  -0.0578 -0.1532 542  VAL B O   
18537 C CB  . VAL C 542  ? 2.3772 0.9329 1.1427 0.1213  -0.1038 -0.1282 542  VAL B CB  
18538 C CG1 . VAL C 542  ? 2.4382 0.9280 1.1632 0.1206  -0.1191 -0.1234 542  VAL B CG1 
18539 C CG2 . VAL C 542  ? 2.3245 0.9499 1.1307 0.0759  -0.1255 -0.1182 542  VAL B CG2 
18540 N N   . TYR C 543  ? 2.7391 1.0342 1.2909 0.1595  -0.1159 -0.1507 543  TYR B N   
18541 C CA  . TYR C 543  ? 2.8623 1.0606 1.3474 0.1930  -0.1086 -0.1608 543  TYR B CA  
18542 C C   . TYR C 543  ? 2.9594 1.0782 1.3879 0.1722  -0.1433 -0.1567 543  TYR B C   
18543 O O   . TYR C 543  ? 2.9898 1.0879 1.3901 0.1325  -0.1781 -0.1505 543  TYR B O   
18544 C CB  . TYR C 543  ? 2.9416 1.0795 1.3616 0.2150  -0.0978 -0.1749 543  TYR B CB  
18545 C CG  . TYR C 543  ? 3.0213 1.1139 1.3819 0.1808  -0.1316 -0.1758 543  TYR B CG  
18546 C CD1 . TYR C 543  ? 2.9859 1.1428 1.3810 0.1562  -0.1363 -0.1713 543  TYR B CD1 
18547 C CD2 . TYR C 543  ? 3.1280 1.1113 1.3982 0.1748  -0.1593 -0.1820 543  TYR B CD2 
18548 C CE1 . TYR C 543  ? 3.0417 1.1563 1.3840 0.1255  -0.1680 -0.1719 543  TYR B CE1 
18549 C CE2 . TYR C 543  ? 3.1835 1.1224 1.3988 0.1440  -0.1922 -0.1832 543  TYR B CE2 
18550 C CZ  . TYR C 543  ? 3.1242 1.1295 1.3762 0.1191  -0.1964 -0.1777 543  TYR B CZ  
18551 O OH  . TYR C 543  ? 3.1420 1.1054 1.3437 0.0883  -0.2299 -0.1782 543  TYR B OH  
18552 N N   . TYR C 544  ? 3.0037 1.0787 1.4192 0.1995  -0.1342 -0.1595 544  TYR B N   
18553 C CA  . TYR C 544  ? 3.1024 1.0809 1.4514 0.1909  -0.1636 -0.1594 544  TYR B CA  
18554 C C   . TYR C 544  ? 3.1809 1.0609 1.4521 0.2306  -0.1507 -0.1783 544  TYR B C   
18555 O O   . TYR C 544  ? 3.1640 1.0593 1.4491 0.2717  -0.1126 -0.1880 544  TYR B O   
18556 C CB  . TYR C 544  ? 3.0898 1.0847 1.4779 0.1917  -0.1661 -0.1484 544  TYR B CB  
18557 C CG  . TYR C 544  ? 3.0579 1.0702 1.4812 0.2397  -0.1277 -0.1549 544  TYR B CG  
18558 C CD1 . TYR C 544  ? 2.9778 1.0687 1.4603 0.2617  -0.0925 -0.1582 544  TYR B CD1 
18559 C CD2 . TYR C 544  ? 3.1083 1.0589 1.5093 0.2625  -0.1279 -0.1570 544  TYR B CD2 
18560 C CE1 . TYR C 544  ? 2.9486 1.0570 1.4677 0.3045  -0.0586 -0.1628 544  TYR B CE1 
18561 C CE2 . TYR C 544  ? 3.0736 1.0417 1.5112 0.3062  -0.0932 -0.1621 544  TYR B CE2 
18562 C CZ  . TYR C 544  ? 2.9995 1.0472 1.4965 0.3267  -0.0586 -0.1647 544  TYR B CZ  
18563 O OH  . TYR C 544  ? 2.9696 1.0388 1.5089 0.3695  -0.0242 -0.1685 544  TYR B OH  
18564 N N   . ILE C 545  ? 3.2631 1.0433 1.4530 0.2183  -0.1827 -0.1833 545  ILE B N   
18565 C CA  . ILE C 545  ? 3.3336 1.0117 1.4410 0.2549  -0.1744 -0.2027 545  ILE B CA  
18566 C C   . ILE C 545  ? 3.3944 1.0100 1.4833 0.2762  -0.1771 -0.2051 545  ILE B C   
18567 O O   . ILE C 545  ? 3.3926 0.9644 1.4598 0.2488  -0.2136 -0.1973 545  ILE B O   
18568 C CB  . ILE C 545  ? 3.3405 0.9386 1.3622 0.2327  -0.2083 -0.2106 545  ILE B CB  
18569 C CG1 . ILE C 545  ? 3.2297 0.8950 1.2814 0.1935  -0.2217 -0.2011 545  ILE B CG1 
18570 C CG2 . ILE C 545  ? 3.4422 0.9629 1.3880 0.2753  -0.1879 -0.2328 545  ILE B CG2 
18571 C CD1 . ILE C 545  ? 3.2494 0.8381 1.2204 0.1689  -0.2584 -0.2076 545  ILE B CD1 
18572 N N   . VAL C 546  ? 3.4414 1.0545 1.5420 0.3249  -0.1383 -0.2148 546  VAL B N   
18573 C CA  . VAL C 546  ? 3.5297 1.1018 1.6319 0.3503  -0.1335 -0.2161 546  VAL B CA  
18574 C C   . VAL C 546  ? 3.7851 1.2400 1.7998 0.3852  -0.1319 -0.2363 546  VAL B C   
18575 O O   . VAL C 546  ? 3.8025 1.2403 1.7917 0.4239  -0.0991 -0.2513 546  VAL B O   
18576 C CB  . VAL C 546  ? 3.3872 1.0388 1.5716 0.3832  -0.0910 -0.2124 546  VAL B CB  
18577 C CG1 . VAL C 546  ? 3.4145 1.0017 1.5737 0.4338  -0.0671 -0.2255 546  VAL B CG1 
18578 C CG2 . VAL C 546  ? 3.2813 1.0104 1.5436 0.3553  -0.1029 -0.1922 546  VAL B CG2 
18579 N N   . THR C 547  ? 4.0021 1.3773 1.9725 0.3729  -0.1664 -0.2363 547  THR B N   
18580 C CA  . THR C 547  ? 4.2754 1.5336 2.1601 0.4047  -0.1694 -0.2569 547  THR B CA  
18581 C C   . THR C 547  ? 4.4617 1.7023 2.3659 0.4525  -0.1389 -0.2636 547  THR B C   
18582 O O   . THR C 547  ? 4.5224 1.7096 2.4158 0.4530  -0.1593 -0.2619 547  THR B O   
18583 C CB  . THR C 547  ? 4.3474 1.5178 2.1711 0.3712  -0.2233 -0.2556 547  THR B CB  
18584 O OG1 . THR C 547  ? 4.3255 1.5184 2.1403 0.3246  -0.2526 -0.2469 547  THR B OG1 
18585 C CG2 . THR C 547  ? 4.4809 1.5264 2.2072 0.4035  -0.2286 -0.2804 547  THR B CG2 
18586 N N   . GLY C 548  ? 4.5831 1.8681 2.5179 0.4926  -0.0907 -0.2703 548  GLY B N   
18587 C CA  . GLY C 548  ? 4.7830 2.0367 2.7228 0.5436  -0.0595 -0.2804 548  GLY B CA  
18588 C C   . GLY C 548  ? 5.0976 2.2232 2.9355 0.5632  -0.0747 -0.3017 548  GLY B C   
18589 O O   . GLY C 548  ? 5.1861 2.2629 2.9519 0.5535  -0.0892 -0.3130 548  GLY B O   
18590 N N   . GLU C 549  ? 5.2833 2.3524 3.1141 0.5908  -0.0732 -0.3078 549  GLU B N   
18591 C CA  . GLU C 549  ? 5.5381 2.4816 3.2734 0.6104  -0.0902 -0.3294 549  GLU B CA  
18592 C C   . GLU C 549  ? 5.5959 2.4966 3.2629 0.6488  -0.0596 -0.3526 549  GLU B C   
18593 O O   . GLU C 549  ? 5.7039 2.5125 3.2782 0.6481  -0.0824 -0.3699 549  GLU B O   
18594 C CB  . GLU C 549  ? 5.6786 2.5762 3.4277 0.6386  -0.0885 -0.3322 549  GLU B CB  
18595 C CG  . GLU C 549  ? 5.7312 2.6687 3.5321 0.6909  -0.0343 -0.3361 549  GLU B CG  
18596 C CD  . GLU C 549  ? 5.6739 2.7341 3.5846 0.6790  -0.0156 -0.3129 549  GLU B CD  
18597 O OE1 . GLU C 549  ? 5.6461 2.7566 3.5926 0.6311  -0.0458 -0.2939 549  GLU B OE1 
18598 O OE2 . GLU C 549  ? 5.6512 2.7577 3.6131 0.7181  0.0292  -0.3136 549  GLU B OE2 
18599 N N   . GLN C 550  ? 5.5167 2.4850 3.2299 0.6817  -0.0087 -0.3521 550  GLN B N   
18600 C CA  . GLN C 550  ? 5.5249 2.4632 3.1817 0.7218  0.0272  -0.3712 550  GLN B CA  
18601 C C   . GLN C 550  ? 5.4187 2.3689 3.0326 0.6954  0.0168  -0.3726 550  GLN B C   
18602 O O   . GLN C 550  ? 5.5278 2.4012 3.0495 0.7107  0.0149  -0.3921 550  GLN B O   
18603 C CB  . GLN C 550  ? 5.5016 2.5119 3.2292 0.7653  0.0854  -0.3672 550  GLN B CB  
18604 C CG  . GLN C 550  ? 5.4010 2.5391 3.2236 0.7440  0.1021  -0.3455 550  GLN B CG  
18605 C CD  . GLN C 550  ? 5.3364 2.5404 3.2495 0.7158  0.0841  -0.3244 550  GLN B CD  
18606 O OE1 . GLN C 550  ? 5.3847 2.5421 3.2947 0.7134  0.0613  -0.3240 550  GLN B OE1 
18607 N NE2 . GLN C 550  ? 5.2209 2.5335 3.2142 0.6948  0.0939  -0.3068 550  GLN B NE2 
18608 N N   . THR C 551  ? 5.1983 2.2433 2.8783 0.6562  0.0089  -0.3523 551  THR B N   
18609 C CA  . THR C 551  ? 5.0659 2.1388 2.7221 0.6323  0.0038  -0.3510 551  THR B CA  
18610 C C   . THR C 551  ? 4.8280 1.9932 2.5573 0.5791  -0.0199 -0.3278 551  THR B C   
18611 O O   . THR C 551  ? 4.7304 1.9768 2.5513 0.5741  -0.0082 -0.3116 551  THR B O   
18612 C CB  . THR C 551  ? 5.0593 2.1781 2.7285 0.6713  0.0576  -0.3553 551  THR B CB  
18613 O OG1 . THR C 551  ? 5.1733 2.2062 2.7676 0.7210  0.0814  -0.3773 551  THR B OG1 
18614 C CG2 . THR C 551  ? 5.0412 2.1944 2.6925 0.6449  0.0511  -0.3518 551  THR B CG2 
18615 N N   . ALA C 552  ? 4.7070 1.8602 2.3961 0.5404  -0.0529 -0.3267 552  ALA B N   
18616 C CA  . ALA C 552  ? 4.4640 1.7007 2.2171 0.4888  -0.0769 -0.3058 552  ALA B CA  
18617 C C   . ALA C 552  ? 4.2024 1.5585 2.0439 0.4943  -0.0391 -0.2937 552  ALA B C   
18618 O O   . ALA C 552  ? 4.1747 1.5442 1.9991 0.5144  -0.0119 -0.3005 552  ALA B O   
18619 C CB  . ALA C 552  ? 4.5228 1.7177 2.2119 0.4501  -0.1178 -0.3084 552  ALA B CB  
18620 N N   . GLU C 553  ? 3.9840 1.4248 1.9184 0.4765  -0.0388 -0.2756 553  GLU B N   
18621 C CA  . GLU C 553  ? 3.7275 1.2881 1.7557 0.4761  -0.0092 -0.2628 553  GLU B CA  
18622 C C   . GLU C 553  ? 3.5615 1.1993 1.6369 0.4248  -0.0341 -0.2472 553  GLU B C   
18623 O O   . GLU C 553  ? 3.5107 1.1683 1.6160 0.3900  -0.0638 -0.2347 553  GLU B O   
18624 C CB  . GLU C 553  ? 3.6040 1.2189 1.7140 0.5002  0.0171  -0.2548 553  GLU B CB  
18625 C CG  . GLU C 553  ? 3.5244 1.1761 1.6684 0.5489  0.0697  -0.2596 553  GLU B CG  
18626 C CD  . GLU C 553  ? 3.3903 1.1298 1.6392 0.5601  0.0917  -0.2467 553  GLU B CD  
18627 O OE1 . GLU C 553  ? 3.3287 1.1300 1.6340 0.5245  0.0702  -0.2326 553  GLU B OE1 
18628 O OE2 . GLU C 553  ? 3.3595 1.1066 1.6349 0.6048  0.1302  -0.2504 553  GLU B OE2 
18629 N N   . LEU C 554  ? 3.4742 1.1566 1.5575 0.4211  -0.0210 -0.2475 554  LEU B N   
18630 C CA  . LEU C 554  ? 3.3525 1.1285 1.5015 0.3813  -0.0333 -0.2327 554  LEU B CA  
18631 C C   . LEU C 554  ? 3.2308 1.1049 1.4807 0.3994  0.0002  -0.2235 554  LEU B C   
18632 O O   . LEU C 554  ? 3.2270 1.1068 1.4912 0.4433  0.0391  -0.2294 554  LEU B O   
18633 C CB  . LEU C 554  ? 3.3556 1.1433 1.4792 0.3729  -0.0311 -0.2364 554  LEU B CB  
18634 C CG  . LEU C 554  ? 3.4467 1.1633 1.4881 0.3406  -0.0722 -0.2414 554  LEU B CG  
18635 C CD1 . LEU C 554  ? 3.3958 1.1714 1.4585 0.3145  -0.0773 -0.2358 554  LEU B CD1 
18636 C CD2 . LEU C 554  ? 3.4748 1.1673 1.5132 0.3020  -0.1150 -0.2329 554  LEU B CD2 
18637 N N   . VAL C 555  ? 3.1400 1.0921 1.4609 0.3660  -0.0151 -0.2089 555  VAL B N   
18638 C CA  . VAL C 555  ? 3.0265 1.0749 1.4456 0.3800  0.0123  -0.2003 555  VAL B CA  
18639 C C   . VAL C 555  ? 2.8790 1.0213 1.3634 0.3377  -0.0045 -0.1875 555  VAL B C   
18640 O O   . VAL C 555  ? 2.8783 1.0099 1.3442 0.2961  -0.0408 -0.1809 555  VAL B O   
18641 C CB  . VAL C 555  ? 3.0462 1.0766 1.4850 0.3968  0.0146  -0.1975 555  VAL B CB  
18642 C CG1 . VAL C 555  ? 2.9678 1.1019 1.5101 0.3980  0.0300  -0.1862 555  VAL B CG1 
18643 C CG2 . VAL C 555  ? 3.1123 1.0730 1.5087 0.4471  0.0426  -0.2106 555  VAL B CG2 
18644 N N   . SER C 556  ? 2.7440 0.9780 1.3052 0.3483  0.0219  -0.1838 556  SER B N   
18645 C CA  . SER C 556  ? 2.6528 0.9771 1.2773 0.3112  0.0080  -0.1736 556  SER B CA  
18646 C C   . SER C 556  ? 2.5713 0.9946 1.2895 0.3314  0.0397  -0.1706 556  SER B C   
18647 O O   . SER C 556  ? 2.6078 1.0272 1.3338 0.3719  0.0729  -0.1763 556  SER B O   
18648 C CB  . SER C 556  ? 2.6554 0.9647 1.2372 0.2834  -0.0110 -0.1757 556  SER B CB  
18649 O OG  . SER C 556  ? 2.6239 0.9622 1.2204 0.3061  0.0169  -0.1806 556  SER B OG  
18650 N N   . ASP C 557  ? 2.4382 0.9496 1.2276 0.3028  0.0286  -0.1613 557  ASP B N   
18651 C CA  . ASP C 557  ? 2.2783 0.8920 1.1610 0.3134  0.0514  -0.1585 557  ASP B CA  
18652 C C   . ASP C 557  ? 2.1856 0.8557 1.0908 0.2739  0.0323  -0.1547 557  ASP B C   
18653 O O   . ASP C 557  ? 2.1942 0.8212 1.0440 0.2416  0.0035  -0.1534 557  ASP B O   
18654 C CB  . ASP C 557  ? 2.2414 0.9079 1.1917 0.3194  0.0554  -0.1524 557  ASP B CB  
18655 C CG  . ASP C 557  ? 2.1620 0.9432 1.2134 0.3186  0.0682  -0.1490 557  ASP B CG  
18656 O OD1 . ASP C 557  ? 2.1545 0.9676 1.2449 0.3483  0.0966  -0.1525 557  ASP B OD1 
18657 O OD2 . ASP C 557  ? 2.0977 0.9376 1.1907 0.2889  0.0498  -0.1426 557  ASP B OD2 
18658 N N   . SER C 558  ? 2.1166 0.8807 1.1039 0.2769  0.0476  -0.1529 558  SER B N   
18659 C CA  . SER C 558  ? 2.0739 0.8962 1.0900 0.2446  0.0337  -0.1505 558  SER B CA  
18660 C C   . SER C 558  ? 1.9630 0.8987 1.0857 0.2478  0.0475  -0.1481 558  SER B C   
18661 O O   . SER C 558  ? 1.9007 0.8644 1.0709 0.2816  0.0729  -0.1494 558  SER B O   
18662 C CB  . SER C 558  ? 2.1222 0.9030 1.0885 0.2513  0.0395  -0.1558 558  SER B CB  
18663 O OG  . SER C 558  ? 2.1115 0.9030 1.1013 0.2938  0.0752  -0.1595 558  SER B OG  
18664 N N   . VAL C 559  ? 1.9399 0.9396 1.1010 0.2132  0.0299  -0.1449 559  VAL B N   
18665 C CA  . VAL C 559  ? 1.8504 0.9595 1.1123 0.2113  0.0375  -0.1438 559  VAL B CA  
18666 C C   . VAL C 559  ? 1.8232 0.9887 1.1185 0.1869  0.0287  -0.1441 559  VAL B C   
18667 O O   . VAL C 559  ? 1.8910 1.0300 1.1430 0.1538  0.0046  -0.1417 559  VAL B O   
18668 C CB  . VAL C 559  ? 1.6660 0.8154 0.9597 0.1906  0.0217  -0.1387 559  VAL B CB  
18669 C CG1 . VAL C 559  ? 1.6718 0.7657 0.9341 0.2117  0.0269  -0.1373 559  VAL B CG1 
18670 C CG2 . VAL C 559  ? 1.5945 0.7373 0.8568 0.1439  -0.0101 -0.1331 559  VAL B CG2 
18671 N N   . TRP C 560  ? 1.7161 0.9589 1.0908 0.2029  0.0466  -0.1465 560  TRP B N   
18672 C CA  . TRP C 560  ? 1.6626 0.9614 1.0753 0.1818  0.0387  -0.1469 560  TRP B CA  
18673 C C   . TRP C 560  ? 1.5569 0.9335 1.0269 0.1500  0.0202  -0.1454 560  TRP B C   
18674 O O   . TRP C 560  ? 1.5066 0.9398 1.0365 0.1603  0.0277  -0.1466 560  TRP B O   
18675 C CB  . TRP C 560  ? 1.6895 1.0367 1.1645 0.2126  0.0648  -0.1496 560  TRP B CB  
18676 C CG  . TRP C 560  ? 1.7235 1.1327 1.2456 0.1924  0.0563  -0.1499 560  TRP B CG  
18677 C CD1 . TRP C 560  ? 1.8038 1.1823 1.2838 0.1757  0.0455  -0.1486 560  TRP B CD1 
18678 C CD2 . TRP C 560  ? 1.6707 1.1832 1.2922 0.1866  0.0562  -0.1521 560  TRP B CD2 
18679 N NE1 . TRP C 560  ? 1.7604 1.2175 1.3097 0.1591  0.0386  -0.1490 560  TRP B NE1 
18680 C CE2 . TRP C 560  ? 1.6658 1.2059 1.3025 0.1658  0.0452  -0.1518 560  TRP B CE2 
18681 C CE3 . TRP C 560  ? 1.6390 1.2219 1.3370 0.1971  0.0628  -0.1551 560  TRP B CE3 
18682 C CZ2 . TRP C 560  ? 1.5866 1.2215 1.3134 0.1559  0.0414  -0.1547 560  TRP B CZ2 
18683 C CZ3 . TRP C 560  ? 1.5665 1.2430 1.3515 0.1876  0.0588  -0.1588 560  TRP B CZ3 
18684 C CH2 . TRP C 560  ? 1.5358 1.2376 1.3354 0.1675  0.0486  -0.1588 560  TRP B CH2 
18685 N N   . LEU C 561  ? 1.5584 0.9397 1.0118 0.1120  -0.0038 -0.1427 561  LEU B N   
18686 C CA  . LEU C 561  ? 1.5537 1.0068 1.0568 0.0803  -0.0212 -0.1404 561  LEU B CA  
18687 C C   . LEU C 561  ? 1.5392 1.0796 1.1165 0.0658  -0.0244 -0.1435 561  LEU B C   
18688 O O   . LEU C 561  ? 1.6029 1.1362 1.1614 0.0375  -0.0423 -0.1411 561  LEU B O   
18689 C CB  . LEU C 561  ? 1.5939 0.9962 1.0320 0.0425  -0.0494 -0.1331 561  LEU B CB  
18690 C CG  . LEU C 561  ? 1.6329 0.9503 0.9981 0.0488  -0.0533 -0.1290 561  LEU B CG  
18691 C CD1 . LEU C 561  ? 1.6642 0.9453 0.9797 0.0074  -0.0839 -0.1205 561  LEU B CD1 
18692 C CD2 . LEU C 561  ? 1.6084 0.9646 1.0162 0.0663  -0.0411 -0.1290 561  LEU B CD2 
18693 N N   . ASN C 562  ? 1.4739 1.0964 1.1368 0.0837  -0.0096 -0.1490 562  ASN B N   
18694 C CA  . ASN C 562  ? 1.3979 1.1053 1.1360 0.0710  -0.0135 -0.1531 562  ASN B CA  
18695 C C   . ASN C 562  ? 1.4111 1.1673 1.1698 0.0324  -0.0352 -0.1512 562  ASN B C   
18696 O O   . ASN C 562  ? 1.4062 1.1910 1.1814 0.0286  -0.0369 -0.1507 562  ASN B O   
18697 C CB  . ASN C 562  ? 1.2741 1.0560 1.1018 0.1018  0.0067  -0.1605 562  ASN B CB  
18698 C CG  . ASN C 562  ? 1.5742 1.4459 1.4838 0.0883  0.0006  -0.1658 562  ASN B CG  
18699 O OD1 . ASN C 562  ? 1.5655 1.4393 1.4645 0.0597  -0.0157 -0.1637 562  ASN B OD1 
18700 N ND2 . ASN C 562  ? 1.5078 1.4527 1.5012 0.1096  0.0127  -0.1731 562  ASN B ND2 
18701 N N   . ILE C 563  ? 1.4083 1.1772 1.1687 0.0038  -0.0516 -0.1495 563  ILE B N   
18702 C CA  . ILE C 563  ? 1.3956 1.2103 1.1759 -0.0329 -0.0710 -0.1465 563  ILE B CA  
18703 C C   . ILE C 563  ? 1.3758 1.2761 1.2341 -0.0461 -0.0758 -0.1521 563  ILE B C   
18704 O O   . ILE C 563  ? 1.3593 1.2765 1.2511 -0.0289 -0.0665 -0.1572 563  ILE B O   
18705 C CB  . ILE C 563  ? 1.4332 1.1721 1.1299 -0.0638 -0.0930 -0.1358 563  ILE B CB  
18706 C CG1 . ILE C 563  ? 1.4442 1.1915 1.1431 -0.0956 -0.1127 -0.1330 563  ILE B CG1 
18707 C CG2 . ILE C 563  ? 1.4853 1.1203 1.0983 -0.0432 -0.0869 -0.1335 563  ILE B CG2 
18708 C CD1 . ILE C 563  ? 1.5076 1.2136 1.1530 -0.1339 -0.1382 -0.1218 563  ILE B CD1 
18709 N N   . GLU C 564  ? 1.3769 1.3333 1.2666 -0.0757 -0.0896 -0.1506 564  GLU B N   
18710 C CA  . GLU C 564  ? 1.3418 1.3913 1.3149 -0.0877 -0.0936 -0.1575 564  GLU B CA  
18711 C C   . GLU C 564  ? 1.3850 1.4256 1.3604 -0.1015 -0.1044 -0.1565 564  GLU B C   
18712 O O   . GLU C 564  ? 1.4686 1.4451 1.3802 -0.1237 -0.1205 -0.1475 564  GLU B O   
18713 C CB  . GLU C 564  ? 1.3279 1.4273 1.3194 -0.1199 -0.1070 -0.1539 564  GLU B CB  
18714 C CG  . GLU C 564  ? 1.4145 1.4611 1.3431 -0.1587 -0.1296 -0.1400 564  GLU B CG  
18715 C CD  . GLU C 564  ? 1.4159 1.5357 1.3894 -0.1929 -0.1425 -0.1370 564  GLU B CD  
18716 O OE1 . GLU C 564  ? 1.4709 1.5623 1.4016 -0.2226 -0.1576 -0.1240 564  GLU B OE1 
18717 O OE2 . GLU C 564  ? 1.3484 1.5557 1.4025 -0.1896 -0.1373 -0.1476 564  GLU B OE2 
18718 N N   . GLU C 565  ? 1.3671 1.4720 1.4174 -0.0890 -0.0975 -0.1654 565  GLU B N   
18719 C CA  . GLU C 565  ? 1.4275 1.5354 1.4905 -0.1043 -0.1097 -0.1642 565  GLU B CA  
18720 C C   . GLU C 565  ? 1.4059 1.5535 1.4900 -0.1454 -0.1320 -0.1610 565  GLU B C   
18721 O O   . GLU C 565  ? 1.3425 1.5558 1.4951 -0.1540 -0.1375 -0.1664 565  GLU B O   
18722 C CB  . GLU C 565  ? 1.4466 1.6144 1.5890 -0.0795 -0.0971 -0.1737 565  GLU B CB  
18723 C CG  . GLU C 565  ? 1.5441 1.6625 1.6612 -0.0424 -0.0774 -0.1732 565  GLU B CG  
18724 C CD  . GLU C 565  ? 1.5296 1.7152 1.7350 -0.0167 -0.0642 -0.1815 565  GLU B CD  
18725 O OE1 . GLU C 565  ? 1.4772 1.7487 1.7636 -0.0261 -0.0705 -0.1899 565  GLU B OE1 
18726 O OE2 . GLU C 565  ? 1.5538 1.7061 1.7482 0.0133  -0.0476 -0.1794 565  GLU B OE2 
18727 N N   . LYS C 566  ? 1.4747 1.5838 1.5033 -0.1708 -0.1449 -0.1515 566  LYS B N   
18728 C CA  . LYS C 566  ? 1.4817 1.6126 1.5190 -0.2120 -0.1676 -0.1448 566  LYS B CA  
18729 C C   . LYS C 566  ? 1.5073 1.5925 1.5179 -0.2243 -0.1830 -0.1404 566  LYS B C   
18730 O O   . LYS C 566  ? 1.5933 1.5913 1.5302 -0.2140 -0.1833 -0.1360 566  LYS B O   
18731 C CB  . LYS C 566  ? 1.5453 1.6305 1.5199 -0.2359 -0.1792 -0.1326 566  LYS B CB  
18732 C CG  . LYS C 566  ? 1.5492 1.6520 1.5310 -0.2794 -0.2032 -0.1231 566  LYS B CG  
18733 C CD  . LYS C 566  ? 1.5763 1.6950 1.5479 -0.2997 -0.2071 -0.1140 566  LYS B CD  
18734 C CE  . LYS C 566  ? 1.6089 1.7411 1.5865 -0.3444 -0.2314 -0.1018 566  LYS B CE  
18735 N NZ  . LYS C 566  ? 1.6849 1.7234 1.5917 -0.3628 -0.2542 -0.0914 566  LYS B NZ  
18736 N N   . CYS C 567  ? 2.2098 1.8059 1.7331 0.1703  -0.0560 0.0859  567  CYS B N   
18737 C CA  . CYS C 567  ? 2.1800 1.7780 1.6977 0.1417  -0.0517 0.0889  567  CYS B CA  
18738 C C   . CYS C 567  ? 2.1796 1.7646 1.6830 0.1213  -0.0445 0.1029  567  CYS B C   
18739 O O   . CYS C 567  ? 2.2078 1.7825 1.7049 0.1295  -0.0427 0.1110  567  CYS B O   
18740 C CB  . CYS C 567  ? 2.1502 1.7767 1.6676 0.1439  -0.0595 0.0980  567  CYS B CB  
18741 S SG  . CYS C 567  ? 2.9614 2.5996 2.4912 0.1572  -0.0683 0.0813  567  CYS B SG  
18742 N N   . GLY C 568  ? 2.1853 1.7684 1.6817 0.0937  -0.0414 0.1060  568  GLY B N   
18743 C CA  . GLY C 568  ? 2.1968 1.7726 1.6796 0.0729  -0.0368 0.1215  568  GLY B CA  
18744 C C   . GLY C 568  ? 2.2066 1.8130 1.6883 0.0713  -0.0427 0.1407  568  GLY B C   
18745 O O   . GLY C 568  ? 2.1985 1.8099 1.6739 0.0694  -0.0406 0.1570  568  GLY B O   
18746 N N   . ASN C 569  ? 2.1887 1.8153 1.6770 0.0713  -0.0499 0.1385  569  ASN B N   
18747 C CA  . ASN C 569  ? 2.1713 1.8305 1.6636 0.0744  -0.0567 0.1539  569  ASN B CA  
18748 C C   . ASN C 569  ? 2.1353 1.8159 1.6376 0.1035  -0.0638 0.1501  569  ASN B C   
18749 O O   . ASN C 569  ? 2.1422 1.8260 1.6494 0.1062  -0.0702 0.1397  569  ASN B O   
18750 C CB  . ASN C 569  ? 2.1787 1.8424 1.6687 0.0495  -0.0618 0.1562  569  ASN B CB  
18751 C CG  . ASN C 569  ? 2.1926 1.8616 1.6773 0.0272  -0.0602 0.1730  569  ASN B CG  
18752 O OD1 . ASN C 569  ? 2.2141 1.8867 1.6974 0.0307  -0.0547 0.1844  569  ASN B OD1 
18753 N ND2 . ASN C 569  ? 2.1951 1.8634 1.6756 0.0032  -0.0658 0.1752  569  ASN B ND2 
18754 N N   . GLN C 570  ? 2.1072 1.7999 1.6102 0.1248  -0.0629 0.1583  570  GLN B N   
18755 C CA  . GLN C 570  ? 2.0740 1.7847 1.5838 0.1528  -0.0697 0.1541  570  GLN B CA  
18756 C C   . GLN C 570  ? 2.1207 1.8590 1.6374 0.1502  -0.0770 0.1602  570  GLN B C   
18757 O O   . GLN C 570  ? 2.0907 1.8522 1.6098 0.1484  -0.0761 0.1753  570  GLN B O   
18758 C CB  . GLN C 570  ? 2.0440 1.7615 1.5486 0.1751  -0.0670 0.1630  570  GLN B CB  
18759 C CG  . GLN C 570  ? 2.4942 2.1868 1.9945 0.1919  -0.0664 0.1523  570  GLN B CG  
18760 C CD  . GLN C 570  ? 2.4958 2.1627 1.9856 0.1804  -0.0585 0.1578  570  GLN B CD  
18761 O OE1 . GLN C 570  ? 2.4893 2.1446 1.9769 0.1552  -0.0533 0.1598  570  GLN B OE1 
18762 N NE2 . GLN C 570  ? 2.5011 2.1561 1.9820 0.1991  -0.0586 0.1601  570  GLN B NE2 
18763 N N   . LEU C 571  ? 2.1606 1.8954 1.6811 0.1486  -0.0843 0.1481  571  LEU B N   
18764 C CA  . LEU C 571  ? 2.1614 1.9193 1.6882 0.1516  -0.0940 0.1519  571  LEU B CA  
18765 C C   . LEU C 571  ? 2.1763 1.9464 1.7073 0.1824  -0.0999 0.1459  571  LEU B C   
18766 O O   . LEU C 571  ? 2.2181 1.9726 1.7483 0.1930  -0.1016 0.1314  571  LEU B O   
18767 C CB  . LEU C 571  ? 2.0897 1.8331 1.6136 0.1315  -0.1000 0.1430  571  LEU B CB  
18768 C CG  . LEU C 571  ? 1.9098 1.6640 1.4379 0.1441  -0.1124 0.1375  571  LEU B CG  
18769 C CD1 . LEU C 571  ? 1.8868 1.6740 1.4238 0.1577  -0.1186 0.1508  571  LEU B CD1 
18770 C CD2 . LEU C 571  ? 1.9220 1.6581 1.4423 0.1196  -0.1181 0.1311  571  LEU B CD2 
18771 N N   . GLN C 572  ? 2.1857 1.9843 1.7221 0.1965  -0.1029 0.1562  572  GLN B N   
18772 C CA  . GLN C 572  ? 2.2045 2.0139 1.7424 0.2259  -0.1086 0.1504  572  GLN B CA  
18773 C C   . GLN C 572  ? 2.1218 1.9570 1.6681 0.2328  -0.1172 0.1554  572  GLN B C   
18774 O O   . GLN C 572  ? 2.0931 1.9530 1.6465 0.2300  -0.1144 0.1689  572  GLN B O   
18775 C CB  . GLN C 572  ? 2.3391 2.1540 1.8713 0.2455  -0.1010 0.1560  572  GLN B CB  
18776 C CG  . GLN C 572  ? 2.4772 2.2964 2.0063 0.2762  -0.1070 0.1478  572  GLN B CG  
18777 C CD  . GLN C 572  ? 2.5927 2.3914 2.1225 0.2808  -0.1158 0.1295  572  GLN B CD  
18778 O OE1 . GLN C 572  ? 2.6320 2.4086 2.1623 0.2659  -0.1140 0.1213  572  GLN B OE1 
18779 N NE2 . GLN C 572  ? 2.6368 2.4428 2.1666 0.3012  -0.1249 0.1225  572  GLN B NE2 
18780 N N   . VAL C 573  ? 2.1007 1.9298 1.6471 0.2422  -0.1280 0.1438  573  VAL B N   
18781 C CA  . VAL C 573  ? 2.0332 1.8812 1.5866 0.2509  -0.1388 0.1461  573  VAL B CA  
18782 C C   . VAL C 573  ? 2.0672 1.9310 1.6210 0.2840  -0.1412 0.1434  573  VAL B C   
18783 O O   . VAL C 573  ? 2.0933 1.9434 1.6390 0.2995  -0.1407 0.1336  573  VAL B O   
18784 C CB  . VAL C 573  ? 1.9296 1.7567 1.4790 0.2371  -0.1501 0.1360  573  VAL B CB  
18785 C CG1 . VAL C 573  ? 1.8865 1.7096 1.4362 0.2067  -0.1505 0.1437  573  VAL B CG1 
18786 C CG2 . VAL C 573  ? 1.8828 1.6813 1.4239 0.2351  -0.1474 0.1210  573  VAL B CG2 
18787 N N   . HIS C 574  ? 2.0411 1.9337 1.6047 0.2949  -0.1437 0.1516  574  HIS B N   
18788 C CA  . HIS C 574  ? 2.0579 1.9656 1.6206 0.3260  -0.1448 0.1486  574  HIS B CA  
18789 C C   . HIS C 574  ? 2.0885 2.0162 1.6625 0.3371  -0.1557 0.1494  574  HIS B C   
18790 O O   . HIS C 574  ? 2.0598 2.0041 1.6475 0.3234  -0.1585 0.1584  574  HIS B O   
18791 C CB  . HIS C 574  ? 2.0831 2.0100 1.6445 0.3352  -0.1300 0.1587  574  HIS B CB  
18792 C CG  . HIS C 574  ? 2.1368 2.0414 1.6843 0.3313  -0.1215 0.1571  574  HIS B CG  
18793 N ND1 . HIS C 574  ? 2.1693 2.0486 1.7053 0.3427  -0.1265 0.1438  574  HIS B ND1 
18794 C CD2 . HIS C 574  ? 2.1684 2.0710 1.7123 0.3174  -0.1095 0.1670  574  HIS B CD2 
18795 C CE1 . HIS C 574  ? 2.1851 2.0487 1.7124 0.3373  -0.1186 0.1453  574  HIS B CE1 
18796 N NE2 . HIS C 574  ? 2.1876 2.0632 1.7180 0.3220  -0.1082 0.1594  574  HIS B NE2 
18797 N N   . LEU C 575  ? 2.1817 2.1066 1.7500 0.3624  -0.1629 0.1395  575  LEU B N   
18798 C CA  . LEU C 575  ? 2.2629 2.2053 1.8411 0.3780  -0.1734 0.1389  575  LEU B CA  
18799 C C   . LEU C 575  ? 2.3956 2.3735 1.9830 0.3988  -0.1630 0.1458  575  LEU B C   
18800 O O   . LEU C 575  ? 2.4539 2.4332 2.0302 0.4118  -0.1514 0.1453  575  LEU B O   
18801 C CB  . LEU C 575  ? 2.2145 2.1336 1.7807 0.3941  -0.1871 0.1241  575  LEU B CB  
18802 C CG  . LEU C 575  ? 2.1548 2.0433 1.7147 0.3737  -0.2000 0.1172  575  LEU B CG  
18803 C CD1 . LEU C 575  ? 2.1323 2.0002 1.6810 0.3902  -0.2141 0.1036  575  LEU B CD1 
18804 C CD2 . LEU C 575  ? 2.1272 2.0245 1.6991 0.3544  -0.2074 0.1266  575  LEU B CD2 
18805 N N   . SER C 576  ? 2.4503 2.4564 2.0579 0.4021  -0.1672 0.1518  576  SER B N   
18806 C CA  . SER C 576  ? 2.5211 2.5666 2.1426 0.4189  -0.1551 0.1587  576  SER B CA  
18807 C C   . SER C 576  ? 2.5854 2.6316 2.1936 0.4513  -0.1513 0.1493  576  SER B C   
18808 O O   . SER C 576  ? 2.5716 2.6262 2.1698 0.4594  -0.1353 0.1522  576  SER B O   
18809 C CB  . SER C 576  ? 2.5719 2.6486 2.2221 0.4178  -0.1628 0.1649  576  SER B CB  
18810 O OG  . SER C 576  ? 2.5978 2.6952 2.2647 0.3932  -0.1551 0.1786  576  SER B OG  
18811 N N   . PRO C 577  ? 2.6323 2.6678 2.2378 0.4695  -0.1663 0.1382  577  PRO B N   
18812 C CA  . PRO C 577  ? 2.6960 2.7217 2.2817 0.4972  -0.1639 0.1276  577  PRO B CA  
18813 C C   . PRO C 577  ? 2.6794 2.6666 2.2406 0.4901  -0.1666 0.1204  577  PRO B C   
18814 O O   . PRO C 577  ? 2.7132 2.6731 2.2691 0.4832  -0.1817 0.1123  577  PRO B O   
18815 C CB  . PRO C 577  ? 2.7148 2.7360 2.3049 0.5154  -0.1813 0.1178  577  PRO B CB  
18816 C CG  . PRO C 577  ? 2.7068 2.7478 2.3241 0.5015  -0.1893 0.1261  577  PRO B CG  
18817 C CD  . PRO C 577  ? 2.6766 2.7103 2.2955 0.4685  -0.1852 0.1356  577  PRO B CD  
18818 N N   . ASP C 578  ? 2.6376 2.6221 2.1847 0.4910  -0.1529 0.1233  578  ASP B N   
18819 C CA  . ASP C 578  ? 2.6010 2.5512 2.1299 0.4837  -0.1564 0.1166  578  ASP B CA  
18820 C C   . ASP C 578  ? 2.5815 2.5090 2.0933 0.5053  -0.1687 0.1013  578  ASP B C   
18821 O O   . ASP C 578  ? 2.5572 2.4585 2.0552 0.5037  -0.1728 0.0938  578  ASP B O   
18822 C CB  . ASP C 578  ? 2.6365 2.5867 2.1537 0.4793  -0.1408 0.1243  578  ASP B CB  
18823 C CG  . ASP C 578  ? 2.6731 2.5923 2.1820 0.4627  -0.1439 0.1206  578  ASP B CG  
18824 O OD1 . ASP C 578  ? 2.6826 2.5791 2.1903 0.4600  -0.1572 0.1092  578  ASP B OD1 
18825 O OD2 . ASP C 578  ? 2.6937 2.6111 2.1976 0.4523  -0.1328 0.1289  578  ASP B OD2 
18826 N N   . ALA C 579  ? 2.5950 2.5323 2.1090 0.5256  -0.1752 0.0960  579  ALA B N   
18827 C CA  . ALA C 579  ? 2.6055 2.5198 2.1017 0.5464  -0.1877 0.0812  579  ALA B CA  
18828 C C   . ALA C 579  ? 2.5520 2.4333 2.0445 0.5316  -0.2029 0.0719  579  ALA B C   
18829 O O   . ALA C 579  ? 2.5505 2.4283 2.0558 0.5085  -0.2071 0.0757  579  ALA B O   
18830 C CB  . ALA C 579  ? 2.6398 2.5679 2.1409 0.5686  -0.1934 0.0769  579  ALA B CB  
18831 N N   . ASP C 580  ? 2.5164 2.3737 1.9906 0.5442  -0.2108 0.0596  580  ASP B N   
18832 C CA  . ASP C 580  ? 2.5026 2.3301 1.9735 0.5299  -0.2225 0.0497  580  ASP B CA  
18833 C C   . ASP C 580  ? 2.4792 2.2901 1.9481 0.5332  -0.2398 0.0400  580  ASP B C   
18834 O O   . ASP C 580  ? 2.4846 2.2693 1.9465 0.5273  -0.2507 0.0289  580  ASP B O   
18835 C CB  . ASP C 580  ? 2.5706 2.3812 2.0252 0.5401  -0.2231 0.0414  580  ASP B CB  
18836 C CG  . ASP C 580  ? 2.6834 2.4884 2.1188 0.5696  -0.2297 0.0324  580  ASP B CG  
18837 O OD1 . ASP C 580  ? 2.7279 2.5328 2.1629 0.5801  -0.2383 0.0280  580  ASP B OD1 
18838 O OD2 . ASP C 580  ? 2.7249 2.5235 2.1442 0.5824  -0.2273 0.0295  580  ASP B OD2 
18839 N N   . ALA C 581  ? 2.4563 2.2823 1.9318 0.5431  -0.2424 0.0440  581  ALA B N   
18840 C CA  . ALA C 581  ? 2.4494 2.2584 1.9228 0.5456  -0.2599 0.0368  581  ALA B CA  
18841 C C   . ALA C 581  ? 2.3938 2.2271 1.8833 0.5495  -0.2599 0.0461  581  ALA B C   
18842 O O   . ALA C 581  ? 2.4058 2.2685 1.9027 0.5647  -0.2479 0.0523  581  ALA B O   
18843 C CB  . ALA C 581  ? 2.4760 2.2674 1.9300 0.5710  -0.2695 0.0233  581  ALA B CB  
18844 N N   . TYR C 582  ? 2.3542 2.1754 1.8495 0.5353  -0.2734 0.0471  582  TYR B N   
18845 C CA  . TYR C 582  ? 2.2716 2.1149 1.7851 0.5369  -0.2766 0.0562  582  TYR B CA  
18846 C C   . TYR C 582  ? 2.2562 2.0803 1.7642 0.5486  -0.2973 0.0493  582  TYR B C   
18847 O O   . TYR C 582  ? 2.2702 2.0589 1.7598 0.5453  -0.3104 0.0393  582  TYR B O   
18848 C CB  . TYR C 582  ? 2.2359 2.0846 1.7629 0.5049  -0.2746 0.0678  582  TYR B CB  
18849 C CG  . TYR C 582  ? 2.1968 2.0666 1.7322 0.4918  -0.2547 0.0770  582  TYR B CG  
18850 C CD1 . TYR C 582  ? 2.1846 2.0926 1.7388 0.4967  -0.2423 0.0883  582  TYR B CD1 
18851 C CD2 . TYR C 582  ? 2.1823 2.0334 1.7078 0.4739  -0.2485 0.0741  582  TYR B CD2 
18852 C CE1 . TYR C 582  ? 2.1703 2.0941 1.7295 0.4832  -0.2245 0.0972  582  TYR B CE1 
18853 C CE2 . TYR C 582  ? 2.1672 2.0336 1.6986 0.4624  -0.2316 0.0824  582  TYR B CE2 
18854 C CZ  . TYR C 582  ? 2.1634 2.0644 1.7099 0.4665  -0.2198 0.0943  582  TYR B CZ  
18855 O OH  . TYR C 582  ? 2.1508 2.0629 1.7003 0.4536  -0.2036 0.1029  582  TYR B OH  
18856 N N   . SER C 583  ? 2.2181 2.0663 1.7434 0.5619  -0.3002 0.0549  583  SER B N   
18857 C CA  . SER C 583  ? 2.2449 2.0769 1.7682 0.5745  -0.3210 0.0500  583  SER B CA  
18858 C C   . SER C 583  ? 2.1671 1.9775 1.6905 0.5464  -0.3370 0.0558  583  SER B C   
18859 O O   . SER C 583  ? 2.1333 1.9606 1.6716 0.5244  -0.3312 0.0674  583  SER B O   
18860 C CB  . SER C 583  ? 2.2796 2.1495 1.8261 0.5998  -0.3174 0.0537  583  SER B CB  
18861 O OG  . SER C 583  ? 2.2930 2.2008 1.8646 0.5857  -0.3033 0.0674  583  SER B OG  
18862 N N   . PRO C 584  ? 2.2052 1.9763 1.7096 0.5464  -0.3575 0.0479  584  PRO B N   
18863 C CA  . PRO C 584  ? 2.1520 1.8952 1.6491 0.5187  -0.3737 0.0526  584  PRO B CA  
18864 C C   . PRO C 584  ? 2.1471 1.9112 1.6658 0.5187  -0.3831 0.0640  584  PRO B C   
18865 O O   . PRO C 584  ? 2.1458 1.8898 1.6593 0.5263  -0.4045 0.0626  584  PRO B O   
18866 C CB  . PRO C 584  ? 2.2221 1.9212 1.6935 0.5270  -0.3937 0.0409  584  PRO B CB  
18867 C CG  . PRO C 584  ? 2.2404 1.9409 1.7033 0.5523  -0.3853 0.0290  584  PRO B CG  
18868 C CD  . PRO C 584  ? 2.2258 1.9741 1.7117 0.5722  -0.3668 0.0340  584  PRO B CD  
18869 N N   . GLY C 585  ? 2.1082 1.9109 1.6510 0.5104  -0.3687 0.0751  585  GLY B N   
18870 C CA  . GLY C 585  ? 2.1227 1.9464 1.6884 0.5066  -0.3786 0.0865  585  GLY B CA  
18871 C C   . GLY C 585  ? 2.1114 1.9873 1.7075 0.5094  -0.3584 0.0957  585  GLY B C   
18872 O O   . GLY C 585  ? 2.0953 1.9968 1.7158 0.5038  -0.3632 0.1061  585  GLY B O   
18873 N N   . GLN C 586  ? 2.1287 2.0195 1.7226 0.5171  -0.3363 0.0920  586  GLN B N   
18874 C CA  . GLN C 586  ? 2.1424 2.0809 1.7614 0.5208  -0.3152 0.1002  586  GLN B CA  
18875 C C   . GLN C 586  ? 2.1574 2.1094 1.7905 0.4894  -0.3122 0.1140  586  GLN B C   
18876 O O   . GLN C 586  ? 2.1441 2.0686 1.7602 0.4610  -0.3135 0.1157  586  GLN B O   
18877 C CB  . GLN C 586  ? 2.1392 2.0813 1.7455 0.5274  -0.2934 0.0953  586  GLN B CB  
18878 C CG  . GLN C 586  ? 2.1499 2.1392 1.7783 0.5344  -0.2714 0.1032  586  GLN B CG  
18879 C CD  . GLN C 586  ? 2.1905 2.1795 1.8020 0.5444  -0.2523 0.0982  586  GLN B CD  
18880 O OE1 . GLN C 586  ? 2.2142 2.1695 1.8000 0.5475  -0.2566 0.0880  586  GLN B OE1 
18881 N NE2 . GLN C 586  ? 2.2010 2.2272 1.8265 0.5486  -0.2317 0.1054  586  GLN B NE2 
18882 N N   . THR C 587  ? 2.1923 2.1874 1.8573 0.4946  -0.3082 0.1231  587  THR B N   
18883 C CA  . THR C 587  ? 2.2387 2.2551 1.9199 0.4672  -0.3005 0.1365  587  THR B CA  
18884 C C   . THR C 587  ? 2.2544 2.2819 1.9290 0.4626  -0.2740 0.1375  587  THR B C   
18885 O O   . THR C 587  ? 2.2275 2.2708 1.9022 0.4871  -0.2606 0.1319  587  THR B O   
18886 C CB  . THR C 587  ? 2.2702 2.3344 1.9910 0.4777  -0.3029 0.1446  587  THR B CB  
18887 O OG1 . THR C 587  ? 2.2831 2.3791 2.0177 0.5103  -0.2887 0.1387  587  THR B OG1 
18888 C CG2 . THR C 587  ? 2.2942 2.3448 2.0217 0.4815  -0.3323 0.1445  587  THR B CG2 
18889 N N   . VAL C 588  ? 2.2991 2.3158 1.9658 0.4316  -0.2670 0.1443  588  VAL B N   
18890 C CA  . VAL C 588  ? 2.3220 2.3427 1.9796 0.4258  -0.2440 0.1454  588  VAL B CA  
18891 C C   . VAL C 588  ? 2.3091 2.3279 1.9674 0.3915  -0.2366 0.1557  588  VAL B C   
18892 O O   . VAL C 588  ? 2.3455 2.3347 1.9913 0.3677  -0.2473 0.1557  588  VAL B O   
18893 C CB  . VAL C 588  ? 2.3314 2.3154 1.9591 0.4327  -0.2425 0.1328  588  VAL B CB  
18894 C CG1 . VAL C 588  ? 2.3366 2.2780 1.9459 0.4155  -0.2604 0.1270  588  VAL B CG1 
18895 C CG2 . VAL C 588  ? 2.3220 2.3050 1.9405 0.4214  -0.2226 0.1353  588  VAL B CG2 
18896 N N   . SER C 589  ? 2.2814 2.3297 1.9516 0.3887  -0.2172 0.1639  589  SER B N   
18897 C CA  . SER C 589  ? 2.2694 2.3194 1.9423 0.3573  -0.2093 0.1746  589  SER B CA  
18898 C C   . SER C 589  ? 2.2426 2.2601 1.8896 0.3439  -0.1986 0.1704  589  SER B C   
18899 O O   . SER C 589  ? 2.2251 2.2409 1.8615 0.3602  -0.1866 0.1653  589  SER B O   
18900 C CB  . SER C 589  ? 2.3133 2.4098 2.0111 0.3595  -0.1934 0.1859  589  SER B CB  
18901 O OG  . SER C 589  ? 2.3522 2.4828 2.0734 0.3855  -0.1970 0.1847  589  SER B OG  
18902 N N   . LEU C 590  ? 2.2313 2.2227 1.8682 0.3146  -0.2034 0.1719  590  LEU B N   
18903 C CA  . LEU C 590  ? 2.1811 2.1446 1.7983 0.2999  -0.1924 0.1681  590  LEU B CA  
18904 C C   . LEU C 590  ? 2.1574 2.1323 1.7805 0.2768  -0.1791 0.1800  590  LEU B C   
18905 O O   . LEU C 590  ? 2.1760 2.1652 1.8126 0.2593  -0.1842 0.1898  590  LEU B O   
18906 C CB  . LEU C 590  ? 2.1296 2.0524 1.7282 0.2829  -0.2041 0.1590  590  LEU B CB  
18907 C CG  . LEU C 590  ? 2.0395 1.9371 1.6246 0.2572  -0.1941 0.1577  590  LEU B CG  
18908 C CD1 . LEU C 590  ? 2.0076 1.8983 1.5844 0.2713  -0.1807 0.1508  590  LEU B CD1 
18909 C CD2 . LEU C 590  ? 2.0082 1.8696 1.5770 0.2369  -0.2052 0.1497  590  LEU B CD2 
18910 N N   . ASN C 591  ? 2.1068 2.0736 1.7193 0.2768  -0.1634 0.1792  591  ASN B N   
18911 C CA  . ASN C 591  ? 2.0757 2.0486 1.6902 0.2561  -0.1498 0.1902  591  ASN B CA  
18912 C C   . ASN C 591  ? 2.0548 1.9908 1.6516 0.2328  -0.1459 0.1858  591  ASN B C   
18913 O O   . ASN C 591  ? 2.0514 1.9619 1.6339 0.2405  -0.1451 0.1742  591  ASN B O   
18914 C CB  . ASN C 591  ? 2.0807 2.0751 1.6967 0.2733  -0.1333 0.1954  591  ASN B CB  
18915 C CG  . ASN C 591  ? 2.1100 2.1486 1.7485 0.2869  -0.1313 0.2036  591  ASN B CG  
18916 O OD1 . ASN C 591  ? 2.1181 2.1799 1.7747 0.2704  -0.1310 0.2146  591  ASN B OD1 
18917 N ND2 . ASN C 591  ? 2.1227 2.1737 1.7607 0.3169  -0.1295 0.1977  591  ASN B ND2 
18918 N N   . MET C 592  ? 2.0320 1.9657 1.6306 0.2045  -0.1435 0.1945  592  MET B N   
18919 C CA  . MET C 592  ? 2.0169 1.9187 1.5998 0.1833  -0.1361 0.1912  592  MET B CA  
18920 C C   . MET C 592  ? 2.0205 1.9295 1.6024 0.1812  -0.1198 0.2001  592  MET B C   
18921 O O   . MET C 592  ? 2.0281 1.9688 1.6223 0.1886  -0.1144 0.2111  592  MET B O   
18922 C CB  . MET C 592  ? 1.9961 1.8833 1.5757 0.1519  -0.1437 0.1939  592  MET B CB  
18923 C CG  . MET C 592  ? 1.9917 1.8465 1.5569 0.1443  -0.1539 0.1806  592  MET B CG  
18924 S SD  . MET C 592  ? 2.2445 2.1093 1.8162 0.1552  -0.1749 0.1791  592  MET B SD  
18925 C CE  . MET C 592  ? 2.0828 1.9899 1.6785 0.1513  -0.1778 0.1974  592  MET B CE  
18926 N N   . ALA C 593  ? 2.0506 1.9298 1.6178 0.1711  -0.1118 0.1953  593  ALA B N   
18927 C CA  . ALA C 593  ? 2.0830 1.9612 1.6447 0.1696  -0.0975 0.2030  593  ALA B CA  
18928 C C   . ALA C 593  ? 2.1475 1.9906 1.6956 0.1479  -0.0916 0.1993  593  ALA B C   
18929 O O   . ALA C 593  ? 2.1292 1.9454 1.6697 0.1467  -0.0946 0.1853  593  ALA B O   
18930 C CB  . ALA C 593  ? 2.0662 1.9481 1.6228 0.1997  -0.0926 0.1991  593  ALA B CB  
18931 N N   . THR C 594  ? 2.2294 2.0730 1.7750 0.1307  -0.0827 0.2112  594  THR B N   
18932 C CA  . THR C 594  ? 2.3067 2.1160 1.8387 0.1109  -0.0762 0.2083  594  THR B CA  
18933 C C   . THR C 594  ? 2.3703 2.1806 1.8971 0.1009  -0.0652 0.2223  594  THR B C   
18934 O O   . THR C 594  ? 2.3860 2.2254 1.9222 0.0956  -0.0632 0.2365  594  THR B O   
18935 C CB  . THR C 594  ? 2.3205 2.1149 1.8499 0.0814  -0.0816 0.2059  594  THR B CB  
18936 O OG1 . THR C 594  ? 2.3146 2.1231 1.8525 0.0842  -0.0943 0.2024  594  THR B OG1 
18937 C CG2 . THR C 594  ? 2.3334 2.0873 1.8487 0.0718  -0.0772 0.1918  594  THR B CG2 
18938 N N   . GLY C 595  ? 2.4029 2.1806 1.9153 0.0972  -0.0582 0.2179  595  GLY B N   
18939 C CA  . GLY C 595  ? 2.4881 2.2575 1.9909 0.0856  -0.0485 0.2304  595  GLY B CA  
18940 C C   . GLY C 595  ? 2.5553 2.3139 2.0552 0.0517  -0.0477 0.2361  595  GLY B C   
18941 O O   . GLY C 595  ? 2.5827 2.3325 2.0740 0.0366  -0.0405 0.2470  595  GLY B O   
18942 N N   . MET C 596  ? 2.6293 2.3862 2.1339 0.0388  -0.0559 0.2288  596  MET B N   
18943 C CA  . MET C 596  ? 2.6811 2.4258 2.1805 0.0058  -0.0572 0.2330  596  MET B CA  
18944 C C   . MET C 596  ? 2.6779 2.4351 2.1856 -0.0016 -0.0695 0.2289  596  MET B C   
18945 O O   . MET C 596  ? 2.6922 2.4465 2.2017 0.0135  -0.0749 0.2164  596  MET B O   
18946 C CB  . MET C 596  ? 2.7138 2.4127 2.1949 -0.0070 -0.0511 0.2220  596  MET B CB  
18947 C CG  . MET C 596  ? 2.7330 2.4131 2.2026 -0.0085 -0.0408 0.2290  596  MET B CG  
18948 S SD  . MET C 596  ? 3.0594 2.7473 2.5254 -0.0402 -0.0382 0.2493  596  MET B SD  
18949 C CE  . MET C 596  ? 2.4486 2.0985 1.8995 -0.0728 -0.0402 0.2395  596  MET B CE  
18950 N N   . ASP C 597  ? 2.6512 2.4217 2.1635 -0.0251 -0.0751 0.2399  597  ASP B N   
18951 C CA  . ASP C 597  ? 2.6209 2.3994 2.1383 -0.0351 -0.0891 0.2376  597  ASP B CA  
18952 C C   . ASP C 597  ? 2.5413 2.2860 2.0436 -0.0356 -0.0913 0.2194  597  ASP B C   
18953 O O   . ASP C 597  ? 2.5197 2.2296 2.0055 -0.0459 -0.0826 0.2107  597  ASP B O   
18954 C CB  . ASP C 597  ? 2.7201 2.4981 2.2350 -0.0685 -0.0941 0.2485  597  ASP B CB  
18955 C CG  . ASP C 597  ? 2.8031 2.6130 2.3333 -0.0721 -0.0896 0.2662  597  ASP B CG  
18956 O OD1 . ASP C 597  ? 2.8186 2.6683 2.3704 -0.0517 -0.0911 0.2725  597  ASP B OD1 
18957 O OD2 . ASP C 597  ? 2.8493 2.6441 2.3695 -0.0958 -0.0840 0.2733  597  ASP B OD2 
18958 N N   . SER C 598  ? 2.4675 2.2220 1.9755 -0.0249 -0.1026 0.2133  598  SER B N   
18959 C CA  . SER C 598  ? 2.3811 2.1062 1.8758 -0.0240 -0.1035 0.1957  598  SER B CA  
18960 C C   . SER C 598  ? 2.2757 2.0045 1.7702 -0.0256 -0.1190 0.1921  598  SER B C   
18961 O O   . SER C 598  ? 2.2573 2.0165 1.7669 -0.0166 -0.1303 0.2015  598  SER B O   
18962 C CB  . SER C 598  ? 2.3609 2.0829 1.8593 0.0047  -0.0953 0.1851  598  SER B CB  
18963 O OG  . SER C 598  ? 2.3420 2.0366 1.8302 0.0036  -0.0943 0.1673  598  SER B OG  
18964 N N   . TRP C 599  ? 2.1887 1.8850 1.6655 -0.0372 -0.1189 0.1779  599  TRP B N   
18965 C CA  . TRP C 599  ? 2.1311 1.8234 1.6028 -0.0366 -0.1324 0.1718  599  TRP B CA  
18966 C C   . TRP C 599  ? 2.0666 1.7647 1.5468 -0.0065 -0.1315 0.1607  599  TRP B C   
18967 O O   . TRP C 599  ? 2.0793 1.7671 1.5601 0.0044  -0.1191 0.1506  599  TRP B O   
18968 C CB  . TRP C 599  ? 2.1688 1.8223 1.6139 -0.0671 -0.1326 0.1626  599  TRP B CB  
18969 C CG  . TRP C 599  ? 2.2548 1.9041 1.6901 -0.0963 -0.1392 0.1748  599  TRP B CG  
18970 C CD1 . TRP C 599  ? 2.3071 1.9321 1.7262 -0.1220 -0.1296 0.1743  599  TRP B CD1 
18971 C CD2 . TRP C 599  ? 2.2795 1.9504 1.7222 -0.1020 -0.1577 0.1892  599  TRP B CD2 
18972 N NE1 . TRP C 599  ? 2.3247 1.9539 1.7388 -0.1447 -0.1415 0.1878  599  TRP B NE1 
18973 C CE2 . TRP C 599  ? 2.2984 1.9569 1.7285 -0.1327 -0.1592 0.1972  599  TRP B CE2 
18974 C CE3 . TRP C 599  ? 2.2720 1.9710 1.7316 -0.0836 -0.1739 0.1955  599  TRP B CE3 
18975 C CZ2 . TRP C 599  ? 2.2940 1.9692 1.7296 -0.1455 -0.1771 0.2113  599  TRP B CZ2 
18976 C CZ3 . TRP C 599  ? 2.2704 1.9858 1.7364 -0.0953 -0.1910 0.2091  599  TRP B CZ3 
18977 C CH2 . TRP C 599  ? 2.2811 1.9857 1.7362 -0.1261 -0.1929 0.2171  599  TRP B CH2 
18978 N N   . VAL C 600  ? 1.9853 1.7000 1.4727 0.0075  -0.1457 0.1627  600  VAL B N   
18979 C CA  . VAL C 600  ? 1.8989 1.6192 1.3932 0.0355  -0.1475 0.1530  600  VAL B CA  
18980 C C   . VAL C 600  ? 1.8635 1.5570 1.3406 0.0233  -0.1559 0.1418  600  VAL B C   
18981 O O   . VAL C 600  ? 1.8920 1.5626 1.3513 -0.0054 -0.1574 0.1415  600  VAL B O   
18982 C CB  . VAL C 600  ? 1.8708 1.6279 1.3844 0.0601  -0.1578 0.1633  600  VAL B CB  
18983 C CG1 . VAL C 600  ? 1.8569 1.6200 1.3766 0.0908  -0.1583 0.1536  600  VAL B CG1 
18984 C CG2 . VAL C 600  ? 1.8483 1.6324 1.3764 0.0634  -0.1500 0.1772  600  VAL B CG2 
18985 N N   . ALA C 601  ? 1.8332 1.5272 1.3130 0.0435  -0.1611 0.1325  601  ALA B N   
18986 C CA  . ALA C 601  ? 1.8177 1.4890 1.2809 0.0334  -0.1723 0.1245  601  ALA B CA  
18987 C C   . ALA C 601  ? 1.8236 1.5011 1.2937 0.0609  -0.1787 0.1161  601  ALA B C   
18988 O O   . ALA C 601  ? 1.8383 1.5018 1.3060 0.0657  -0.1708 0.1015  601  ALA B O   
18989 C CB  . ALA C 601  ? 1.8129 1.4482 1.2553 0.0059  -0.1618 0.1119  601  ALA B CB  
18990 N N   . LEU C 602  ? 1.8066 1.5053 1.2861 0.0788  -0.1934 0.1249  602  LEU B N   
18991 C CA  . LEU C 602  ? 1.7939 1.5000 1.2799 0.1073  -0.2005 0.1182  602  LEU B CA  
18992 C C   . LEU C 602  ? 1.8276 1.5031 1.2949 0.0989  -0.2088 0.1059  602  LEU B C   
18993 O O   . LEU C 602  ? 1.8482 1.4963 1.2958 0.0702  -0.2097 0.1031  602  LEU B O   
18994 C CB  . LEU C 602  ? 1.7468 1.4838 1.2485 0.1292  -0.2132 0.1300  602  LEU B CB  
18995 C CG  . LEU C 602  ? 1.7088 1.4775 1.2284 0.1319  -0.2060 0.1441  602  LEU B CG  
18996 C CD1 . LEU C 602  ? 1.6761 1.4799 1.2155 0.1592  -0.2146 0.1524  602  LEU B CD1 
18997 C CD2 . LEU C 602  ? 1.6820 1.4530 1.2054 0.1350  -0.1861 0.1411  602  LEU B CD2 
18998 N N   . ALA C 603  ? 1.8066 1.4857 1.2786 0.1236  -0.2143 0.0984  603  ALA B N   
18999 C CA  . ALA C 603  ? 1.7799 1.4320 1.2357 0.1190  -0.2227 0.0867  603  ALA B CA  
19000 C C   . ALA C 603  ? 1.7333 1.3992 1.2002 0.1528  -0.2278 0.0814  603  ALA B C   
19001 O O   . ALA C 603  ? 1.7244 1.4123 1.2074 0.1735  -0.2187 0.0816  603  ALA B O   
19002 C CB  . ALA C 603  ? 1.7588 1.3861 1.2045 0.0977  -0.2083 0.0727  603  ALA B CB  
19003 N N   . ALA C 604  ? 1.7493 1.4002 1.2052 0.1582  -0.2433 0.0772  604  ALA B N   
19004 C CA  . ALA C 604  ? 1.7282 1.3890 1.1915 0.1900  -0.2502 0.0719  604  ALA B CA  
19005 C C   . ALA C 604  ? 1.7660 1.3952 1.2117 0.1825  -0.2581 0.0589  604  ALA B C   
19006 O O   . ALA C 604  ? 1.7904 1.4006 1.2201 0.1754  -0.2742 0.0613  604  ALA B O   
19007 C CB  . ALA C 604  ? 1.7117 1.3933 1.1831 0.2113  -0.2645 0.0835  604  ALA B CB  
19008 N N   . VAL C 605  ? 1.7488 1.3717 1.1975 0.1827  -0.2471 0.0453  605  VAL B N   
19009 C CA  . VAL C 605  ? 1.7702 1.3650 1.2048 0.1727  -0.2516 0.0316  605  VAL B CA  
19010 C C   . VAL C 605  ? 1.8100 1.4089 1.2481 0.2027  -0.2625 0.0254  605  VAL B C   
19011 O O   . VAL C 605  ? 1.7992 1.4224 1.2531 0.2294  -0.2590 0.0266  605  VAL B O   
19012 C CB  . VAL C 605  ? 1.7563 1.3453 1.1970 0.1573  -0.2335 0.0185  605  VAL B CB  
19013 C CG1 . VAL C 605  ? 1.7624 1.3283 1.1940 0.1499  -0.2368 0.0029  605  VAL B CG1 
19014 C CG2 . VAL C 605  ? 1.7577 1.3381 1.1913 0.1260  -0.2220 0.0227  605  VAL B CG2 
19015 N N   . ASP C 606  ? 1.8445 1.4173 1.2654 0.1981  -0.2758 0.0189  606  ASP B N   
19016 C CA  . ASP C 606  ? 1.8733 1.4458 1.2966 0.2232  -0.2838 0.0095  606  ASP B CA  
19017 C C   . ASP C 606  ? 1.8716 1.4505 1.3091 0.2220  -0.2686 -0.0035 606  ASP B C   
19018 O O   . ASP C 606  ? 1.8732 1.4336 1.3058 0.1988  -0.2626 -0.0144 606  ASP B O   
19019 C CB  . ASP C 606  ? 1.9154 1.4541 1.3160 0.2141  -0.2996 0.0031  606  ASP B CB  
19020 C CG  . ASP C 606  ? 1.9195 1.4538 1.3222 0.2334  -0.3050 -0.0101 606  ASP B CG  
19021 O OD1 . ASP C 606  ? 1.9066 1.4648 1.3279 0.2546  -0.2970 -0.0137 606  ASP B OD1 
19022 O OD2 . ASP C 606  ? 1.9324 1.4381 1.3167 0.2271  -0.3178 -0.0167 606  ASP B OD2 
19023 N N   . SER C 607  ? 1.4780 1.1997 1.3779 0.1563  -0.7706 -0.4999 607  SER B N   
19024 C CA  . SER C 607  ? 1.5675 1.2250 1.4252 0.1437  -0.7493 -0.4661 607  SER B CA  
19025 C C   . SER C 607  ? 1.5929 1.1908 1.3990 0.1533  -0.8044 -0.4245 607  SER B C   
19026 O O   . SER C 607  ? 1.6069 1.1576 1.3859 0.1401  -0.7927 -0.3928 607  SER B O   
19027 C CB  . SER C 607  ? 1.6893 1.3040 1.5092 0.1586  -0.7083 -0.4665 607  SER B CB  
19028 O OG  . SER C 607  ? 1.7800 1.3320 1.5330 0.1938  -0.7511 -0.4487 607  SER B OG  
19029 N N   . ALA C 608  ? 1.5945 1.1926 1.3876 0.1763  -0.8651 -0.4225 608  ALA B N   
19030 C CA  . ALA C 608  ? 1.6042 1.1400 1.3470 0.1877  -0.9210 -0.3803 608  ALA B CA  
19031 C C   . ALA C 608  ? 1.5531 1.0960 1.3134 0.1653  -0.9415 -0.3483 608  ALA B C   
19032 O O   . ALA C 608  ? 1.5669 1.0558 1.2913 0.1682  -0.9753 -0.3052 608  ALA B O   
19033 C CB  . ALA C 608  ? 1.6513 1.1787 1.3702 0.2197  -0.9818 -0.3864 608  ALA B CB  
19034 N N   . VAL C 609  ? 1.4701 1.0771 1.2841 0.1447  -0.9227 -0.3670 609  VAL B N   
19035 C CA  . VAL C 609  ? 1.3888 1.0036 1.2157 0.1280  -0.9380 -0.3369 609  VAL B CA  
19036 C C   . VAL C 609  ? 1.4138 0.9744 1.2110 0.1158  -0.9139 -0.2968 609  VAL B C   
19037 O O   . VAL C 609  ? 1.4486 0.9647 1.2160 0.1226  -0.9526 -0.2529 609  VAL B O   
19038 C CB  . VAL C 609  ? 1.3135 0.9941 1.1929 0.1096  -0.9128 -0.3666 609  VAL B CB  
19039 C CG1 . VAL C 609  ? 1.3055 1.0335 1.2109 0.1232  -0.9518 -0.3959 609  VAL B CG1 
19040 C CG2 . VAL C 609  ? 1.2902 0.9866 1.1900 0.0948  -0.8486 -0.3987 609  VAL B CG2 
19041 N N   . TYR C 610  ? 1.3905 0.9535 1.1967 0.0979  -0.8522 -0.3110 610  TYR B N   
19042 C CA  . TYR C 610  ? 1.3849 0.8935 1.1598 0.0875  -0.8225 -0.2795 610  TYR B CA  
19043 C C   . TYR C 610  ? 2.1939 1.6292 1.9136 0.1075  -0.8515 -0.2512 610  TYR B C   
19044 O O   . TYR C 610  ? 2.1431 1.5390 1.8399 0.1113  -0.8904 -0.2060 610  TYR B O   
19045 C CB  . TYR C 610  ? 1.3942 0.9115 1.1811 0.0709  -0.7538 -0.3095 610  TYR B CB  
19046 C CG  . TYR C 610  ? 1.3353 0.9232 1.1765 0.0583  -0.7291 -0.3549 610  TYR B CG  
19047 C CD1 . TYR C 610  ? 1.3781 0.9932 1.2460 0.0361  -0.7054 -0.3588 610  TYR B CD1 
19048 C CD2 . TYR C 610  ? 1.3333 0.9575 1.1975 0.0697  -0.7296 -0.3930 610  TYR B CD2 
19049 C CE1 . TYR C 610  ? 1.3713 1.0452 1.2885 0.0233  -0.6876 -0.3996 610  TYR B CE1 
19050 C CE2 . TYR C 610  ? 1.3198 1.0103 1.2405 0.0562  -0.7094 -0.4329 610  TYR B CE2 
19051 C CZ  . TYR C 610  ? 1.3171 1.0301 1.2641 0.0318  -0.6902 -0.4361 610  TYR B CZ  
19052 O OH  . TYR C 610  ? 1.2785 1.0493 1.2794 0.0166  -0.6746 -0.4737 610  TYR B OH  
19053 N N   . GLY C 611  ? 2.2905 1.7064 1.9890 0.1211  -0.8322 -0.2769 611  GLY B N   
19054 C CA  . GLY C 611  ? 2.4276 1.7723 2.0678 0.1460  -0.8626 -0.2593 611  GLY B CA  
19055 C C   . GLY C 611  ? 2.5551 1.8247 2.1519 0.1442  -0.8803 -0.2091 611  GLY B C   
19056 O O   . GLY C 611  ? 2.6007 1.8312 2.1749 0.1355  -0.8368 -0.2023 611  GLY B O   
19057 N N   . VAL C 612  ? 2.6521 1.9015 2.2394 0.1520  -0.9454 -0.1726 612  VAL B N   
19058 C CA  . VAL C 612  ? 2.7849 1.9569 2.3303 0.1548  -0.9770 -0.1215 612  VAL B CA  
19059 C C   . VAL C 612  ? 2.9310 2.0883 2.4798 0.1319  -0.9270 -0.1010 612  VAL B C   
19060 O O   . VAL C 612  ? 2.8950 2.0989 2.4845 0.1124  -0.9110 -0.0896 612  VAL B O   
19061 C CB  . VAL C 612  ? 3.8060 2.9774 3.3625 0.1575  -1.0499 -0.0791 612  VAL B CB  
19062 C CG1 . VAL C 612  ? 3.8547 2.9801 3.3896 0.1822  -1.0902 -0.0900 612  VAL B CG1 
19063 C CG2 . VAL C 612  ? 3.7545 3.0014 3.3745 0.1397  -1.0352 -0.0812 612  VAL B CG2 
19064 N N   . GLN C 613  ? 3.0960 2.1848 2.5973 0.1368  -0.9037 -0.0960 613  GLN B N   
19065 C CA  . GLN C 613  ? 3.2428 2.3169 2.7425 0.1164  -0.8455 -0.0882 613  GLN B CA  
19066 C C   . GLN C 613  ? 3.2923 2.4458 2.8468 0.0934  -0.7960 -0.1138 613  GLN B C   
19067 O O   . GLN C 613  ? 3.2551 2.4393 2.8399 0.0796  -0.8013 -0.0895 613  GLN B O   
19068 C CB  . GLN C 613  ? 3.2639 2.2853 2.7471 0.1097  -0.8711 -0.0301 613  GLN B CB  
19069 C CG  . GLN C 613  ? 3.2349 2.2495 2.7213 0.0878  -0.8106 -0.0212 613  GLN B CG  
19070 C CD  . GLN C 613  ? 3.2522 2.1884 2.7017 0.0876  -0.8264 0.0280  613  GLN B CD  
19071 O OE1 . GLN C 613  ? 3.2979 2.1602 2.6976 0.1044  -0.8557 0.0380  613  GLN B OE1 
19072 N NE2 . GLN C 613  ? 3.2182 2.1680 2.6900 0.0702  -0.8066 0.0582  613  GLN B NE2 
19073 N N   . ARG C 614  ? 3.3921 2.5775 2.9589 0.0909  -0.7494 -0.1613 614  ARG B N   
19074 C CA  . ARG C 614  ? 3.4309 2.6797 3.0445 0.0676  -0.7012 -0.1867 614  ARG B CA  
19075 C C   . ARG C 614  ? 3.4878 2.7009 3.0848 0.0492  -0.6573 -0.1670 614  ARG B C   
19076 O O   . ARG C 614  ? 3.5440 2.7317 3.1222 0.0437  -0.6095 -0.1848 614  ARG B O   
19077 C CB  . ARG C 614  ? 3.4199 2.7083 3.0540 0.0682  -0.6640 -0.2385 614  ARG B CB  
19078 C CG  . ARG C 614  ? 3.3580 2.7209 3.0494 0.0466  -0.6340 -0.2682 614  ARG B CG  
19079 C CD  . ARG C 614  ? 3.3302 2.7486 3.0553 0.0567  -0.6415 -0.3092 614  ARG B CD  
19080 N NE  . ARG C 614  ? 3.3048 2.7750 3.0751 0.0364  -0.5916 -0.3466 614  ARG B NE  
19081 C CZ  . ARG C 614  ? 3.3149 2.8207 3.1105 0.0421  -0.5726 -0.3825 614  ARG B CZ  
19082 N NH1 . ARG C 614  ? 3.3414 2.8338 3.1146 0.0708  -0.5974 -0.3869 614  ARG B NH1 
19083 N NH2 . ARG C 614  ? 3.3059 2.8587 3.1485 0.0202  -0.5298 -0.4121 614  ARG B NH2 
19084 N N   . GLY C 615  ? 3.4990 2.7106 3.1028 0.0412  -0.6736 -0.1285 615  GLY B N   
19085 C CA  . GLY C 615  ? 3.5373 2.7097 3.1212 0.0276  -0.6401 -0.1024 615  GLY B CA  
19086 C C   . GLY C 615  ? 3.5981 2.7701 3.1790 0.0117  -0.5733 -0.1374 615  GLY B C   
19087 O O   . GLY C 615  ? 3.5903 2.8182 3.2071 0.0007  -0.5473 -0.1748 615  GLY B O   
19088 N N   . ALA C 616  ? 3.6650 2.7717 3.2036 0.0098  -0.5475 -0.1242 616  ALA B N   
19089 C CA  . ALA C 616  ? 3.7057 2.8035 3.2365 -0.0053 -0.4843 -0.1539 616  ALA B CA  
19090 C C   . ALA C 616  ? 3.6761 2.8289 3.2464 -0.0281 -0.4498 -0.1732 616  ALA B C   
19091 O O   . ALA C 616  ? 3.6798 2.8761 3.2803 -0.0377 -0.4228 -0.2136 616  ALA B O   
19092 C CB  . ALA C 616  ? 3.7529 2.7705 3.2316 -0.0063 -0.4642 -0.1281 616  ALA B CB  
19093 N N   . LYS C 617  ? 3.6395 2.7893 3.2094 -0.0349 -0.4531 -0.1430 617  LYS B N   
19094 C CA  . LYS C 617  ? 3.5894 2.7771 3.1834 -0.0530 -0.4222 -0.1577 617  LYS B CA  
19095 C C   . LYS C 617  ? 3.5502 2.7487 3.1546 -0.0706 -0.3726 -0.2024 617  LYS B C   
19096 O O   . LYS C 617  ? 3.5942 2.7465 3.1688 -0.0797 -0.3346 -0.2023 617  LYS B O   
19097 C CB  . LYS C 617  ? 3.5710 2.8229 3.2052 -0.0482 -0.4554 -0.1624 617  LYS B CB  
19098 C CG  . LYS C 617  ? 3.5718 2.8498 3.2186 -0.0609 -0.4324 -0.1675 617  LYS B CG  
19099 C CD  . LYS C 617  ? 3.5918 2.8267 3.2053 -0.0604 -0.4198 -0.1249 617  LYS B CD  
19100 C CE  . LYS C 617  ? 3.5895 2.8471 3.2075 -0.0651 -0.4040 -0.1247 617  LYS B CE  
19101 N NZ  . LYS C 617  ? 3.6033 2.8202 3.1880 -0.0613 -0.3895 -0.0818 617  LYS B NZ  
19102 N N   . LYS C 618  ? 3.4550 2.7145 3.1034 -0.0753 -0.3749 -0.2387 618  LYS B N   
19103 C CA  . LYS C 618  ? 3.3915 2.6731 3.0636 -0.0911 -0.3349 -0.2807 618  LYS B CA  
19104 C C   . LYS C 618  ? 3.2200 2.5748 2.9471 -0.0917 -0.3542 -0.3138 618  LYS B C   
19105 O O   . LYS C 618  ? 3.1473 2.5324 2.8899 -0.0842 -0.3910 -0.3062 618  LYS B O   
19106 C CB  . LYS C 618  ? 3.4874 2.7520 3.1524 -0.1161 -0.2876 -0.2881 618  LYS B CB  
19107 C CG  . LYS C 618  ? 3.5821 2.7743 3.1945 -0.1193 -0.2585 -0.2635 618  LYS B CG  
19108 C CD  . LYS C 618  ? 3.6553 2.8167 3.2506 -0.1182 -0.2302 -0.2751 618  LYS B CD  
19109 C CE  . LYS C 618  ? 3.7043 2.7926 3.2471 -0.1252 -0.1963 -0.2551 618  LYS B CE  
19110 N NZ  . LYS C 618  ? 3.7025 2.7437 3.2055 -0.1110 -0.2250 -0.2115 618  LYS B NZ  
19111 N N   . PRO C 619  ? 3.1246 2.5088 2.8828 -0.0996 -0.3294 -0.3489 619  PRO B N   
19112 C CA  . PRO C 619  ? 3.0365 2.4918 2.8530 -0.1034 -0.3430 -0.3831 619  PRO B CA  
19113 C C   . PRO C 619  ? 2.9493 2.4325 2.7987 -0.1307 -0.3205 -0.4055 619  PRO B C   
19114 O O   . PRO C 619  ? 2.9172 2.4268 2.7814 -0.1304 -0.3482 -0.4079 619  PRO B O   
19115 C CB  . PRO C 619  ? 3.0712 2.5412 2.9046 -0.0972 -0.3234 -0.4048 619  PRO B CB  
19116 C CG  . PRO C 619  ? 3.1220 2.5213 2.8959 -0.0851 -0.3065 -0.3796 619  PRO B CG  
19117 C CD  . PRO C 619  ? 3.1450 2.4963 2.8832 -0.0986 -0.2935 -0.3540 619  PRO B CD  
19118 N N   . LEU C 620  ? 2.9129 2.3865 2.7706 -0.1528 -0.2731 -0.4207 620  LEU B N   
19119 C CA  . LEU C 620  ? 2.8504 2.3393 2.7351 -0.1816 -0.2508 -0.4414 620  LEU B CA  
19120 C C   . LEU C 620  ? 2.8652 2.3036 2.7033 -0.1897 -0.2411 -0.4199 620  LEU B C   
19121 O O   . LEU C 620  ? 2.8793 2.3232 2.7284 -0.2078 -0.2347 -0.4340 620  LEU B O   
19122 C CB  . LEU C 620  ? 2.8094 2.3076 2.7243 -0.2032 -0.2045 -0.4628 620  LEU B CB  
19123 C CG  . LEU C 620  ? 2.7780 2.2708 2.7090 -0.2367 -0.1746 -0.4776 620  LEU B CG  
19124 C CD1 . LEU C 620  ? 2.7547 2.3044 2.7438 -0.2487 -0.1988 -0.5062 620  LEU B CD1 
19125 C CD2 . LEU C 620  ? 2.7922 2.2764 2.7367 -0.2551 -0.1243 -0.4847 620  LEU B CD2 
19126 N N   . GLU C 621  ? 2.8712 2.2576 2.6558 -0.1752 -0.2410 -0.3856 621  GLU B N   
19127 C CA  . GLU C 621  ? 2.8888 2.2289 2.6271 -0.1761 -0.2358 -0.3589 621  GLU B CA  
19128 C C   . GLU C 621  ? 2.8021 2.1643 2.5406 -0.1593 -0.2780 -0.3447 621  GLU B C   
19129 O O   . GLU C 621  ? 2.8077 2.1499 2.5207 -0.1603 -0.2751 -0.3316 621  GLU B O   
19130 C CB  . GLU C 621  ? 2.9817 2.2599 2.6682 -0.1665 -0.2218 -0.3260 621  GLU B CB  
19131 C CG  . GLU C 621  ? 3.0624 2.2929 2.7004 -0.1610 -0.2214 -0.2900 621  GLU B CG  
19132 C CD  . GLU C 621  ? 3.1257 2.2954 2.7175 -0.1515 -0.2124 -0.2582 621  GLU B CD  
19133 O OE1 . GLU C 621  ? 3.1715 2.3121 2.7508 -0.1618 -0.1788 -0.2693 621  GLU B OE1 
19134 O OE2 . GLU C 621  ? 3.1252 2.2754 2.6940 -0.1334 -0.2396 -0.2207 621  GLU B OE2 
19135 N N   . ARG C 622  ? 2.7061 2.1088 2.4713 -0.1425 -0.3164 -0.3473 622  ARG B N   
19136 C CA  . ARG C 622  ? 2.6056 2.0363 2.3774 -0.1273 -0.3568 -0.3374 622  ARG B CA  
19137 C C   . ARG C 622  ? 2.5278 1.9723 2.3101 -0.1414 -0.3478 -0.3603 622  ARG B C   
19138 O O   . ARG C 622  ? 2.5370 1.9629 2.2894 -0.1339 -0.3521 -0.3404 622  ARG B O   
19139 C CB  . ARG C 622  ? 2.5811 2.0605 2.3897 -0.1131 -0.3960 -0.3505 622  ARG B CB  
19140 C CG  . ARG C 622  ? 2.5584 2.0585 2.3660 -0.0923 -0.4427 -0.3292 622  ARG B CG  
19141 C CD  . ARG C 622  ? 2.3359 1.8801 2.1769 -0.0786 -0.4827 -0.3439 622  ARG B CD  
19142 N NE  . ARG C 622  ? 2.3396 1.9332 2.2285 -0.0900 -0.4815 -0.3906 622  ARG B NE  
19143 C CZ  . ARG C 622  ? 2.3177 1.9553 2.2411 -0.0801 -0.5120 -0.4112 622  ARG B CZ  
19144 N NH1 . ARG C 622  ? 2.3112 1.9461 2.2223 -0.0583 -0.5478 -0.3901 622  ARG B NH1 
19145 N NH2 . ARG C 622  ? 2.2998 1.9824 2.2704 -0.0919 -0.5090 -0.4523 622  ARG B NH2 
19146 N N   . VAL C 623  ? 2.4560 1.9298 2.2791 -0.1611 -0.3352 -0.4006 623  VAL B N   
19147 C CA  . VAL C 623  ? 2.4070 1.8872 2.2399 -0.1766 -0.3306 -0.4247 623  VAL B CA  
19148 C C   . VAL C 623  ? 2.3847 1.8093 2.1749 -0.1913 -0.2939 -0.4156 623  VAL B C   
19149 O O   . VAL C 623  ? 2.3950 1.7976 2.1528 -0.1858 -0.2986 -0.4075 623  VAL B O   
19150 C CB  . VAL C 623  ? 1.8448 1.3742 1.7412 -0.1955 -0.3321 -0.4686 623  VAL B CB  
19151 C CG1 . VAL C 623  ? 1.8746 1.3841 1.7764 -0.2253 -0.3006 -0.4891 623  VAL B CG1 
19152 C CG2 . VAL C 623  ? 1.7920 1.3679 1.7180 -0.1832 -0.3773 -0.4853 623  VAL B CG2 
19153 N N   . PHE C 624  ? 2.3448 1.7436 2.1299 -0.2073 -0.2572 -0.4159 624  PHE B N   
19154 C CA  . PHE C 624  ? 2.3264 1.6705 2.0699 -0.2221 -0.2231 -0.4087 624  PHE B CA  
19155 C C   . PHE C 624  ? 2.3816 1.6849 2.0662 -0.2017 -0.2287 -0.3722 624  PHE B C   
19156 O O   . PHE C 624  ? 2.4197 1.6889 2.0701 -0.2067 -0.2160 -0.3714 624  PHE B O   
19157 C CB  . PHE C 624  ? 2.2161 1.5324 1.9536 -0.2370 -0.1837 -0.4064 624  PHE B CB  
19158 C CG  . PHE C 624  ? 2.0999 1.4234 1.8706 -0.2689 -0.1558 -0.4377 624  PHE B CG  
19159 C CD1 . PHE C 624  ? 2.0445 1.3911 1.8539 -0.2801 -0.1347 -0.4511 624  PHE B CD1 
19160 C CD2 . PHE C 624  ? 2.0607 1.3669 1.8236 -0.2864 -0.1520 -0.4523 624  PHE B CD2 
19161 C CE1 . PHE C 624  ? 2.0335 1.3918 1.8810 -0.3108 -0.1084 -0.4758 624  PHE B CE1 
19162 C CE2 . PHE C 624  ? 2.0522 1.3647 1.8503 -0.3181 -0.1305 -0.4785 624  PHE B CE2 
19163 C CZ  . PHE C 624  ? 2.0424 1.3841 1.8870 -0.3316 -0.1078 -0.4891 624  PHE B CZ  
19164 N N   . GLN C 625  ? 2.4103 1.7160 2.0830 -0.1779 -0.2483 -0.3402 625  GLN B N   
19165 C CA  . GLN C 625  ? 2.4916 1.7641 2.1161 -0.1576 -0.2528 -0.2992 625  GLN B CA  
19166 C C   . GLN C 625  ? 2.4739 1.7577 2.0887 -0.1475 -0.2694 -0.3035 625  GLN B C   
19167 O O   . GLN C 625  ? 2.5120 1.7579 2.0855 -0.1476 -0.2513 -0.2975 625  GLN B O   
19168 C CB  . GLN C 625  ? 2.5700 1.8527 2.1959 -0.1346 -0.2811 -0.2640 625  GLN B CB  
19169 C CG  . GLN C 625  ? 2.6925 1.9404 2.3037 -0.1371 -0.2655 -0.2470 625  GLN B CG  
19170 C CD  . GLN C 625  ? 2.7724 2.0141 2.3729 -0.1136 -0.2967 -0.2030 625  GLN B CD  
19171 O OE1 . GLN C 625  ? 2.8108 2.0304 2.3833 -0.1008 -0.2997 -0.1647 625  GLN B OE1 
19172 N NE2 . GLN C 625  ? 2.7847 2.0447 2.4078 -0.1071 -0.3209 -0.2066 625  GLN B NE2 
19173 N N   . PHE C 626  ? 2.4190 1.7519 2.0682 -0.1370 -0.3048 -0.3150 626  PHE B N   
19174 C CA  . PHE C 626  ? 2.3843 1.7305 2.0262 -0.1251 -0.3252 -0.3232 626  PHE B CA  
19175 C C   . PHE C 626  ? 2.3161 1.6377 1.9461 -0.1452 -0.3061 -0.3569 626  PHE B C   
19176 O O   . PHE C 626  ? 2.3014 1.5830 1.8813 -0.1364 -0.2952 -0.3454 626  PHE B O   
19177 C CB  . PHE C 626  ? 2.4303 1.8344 2.1198 -0.1173 -0.3646 -0.3405 626  PHE B CB  
19178 C CG  . PHE C 626  ? 2.5198 1.9389 2.2090 -0.1099 -0.3867 -0.3616 626  PHE B CG  
19179 C CD1 . PHE C 626  ? 2.5442 1.9730 2.2132 -0.0804 -0.4126 -0.3361 626  PHE B CD1 
19180 C CD2 . PHE C 626  ? 2.5691 1.9910 2.2786 -0.1320 -0.3829 -0.4058 626  PHE B CD2 
19181 C CE1 . PHE C 626  ? 2.5826 2.0191 2.2445 -0.0706 -0.4333 -0.3562 626  PHE B CE1 
19182 C CE2 . PHE C 626  ? 2.6083 2.0364 2.3132 -0.1242 -0.4072 -0.4263 626  PHE B CE2 
19183 C CZ  . PHE C 626  ? 2.6122 2.0456 2.2898 -0.0922 -0.4320 -0.4026 626  PHE B CZ  
19184 N N   . LEU C 627  ? 2.2345 1.5784 1.9104 -0.1715 -0.3024 -0.3962 627  LEU B N   
19185 C CA  . LEU C 627  ? 2.1877 1.5178 1.8673 -0.1932 -0.2958 -0.4314 627  LEU B CA  
19186 C C   . LEU C 627  ? 2.2318 1.4978 1.8589 -0.2046 -0.2619 -0.4245 627  LEU B C   
19187 O O   . LEU C 627  ? 2.2907 1.5366 1.9175 -0.2256 -0.2561 -0.4519 627  LEU B O   
19188 C CB  . LEU C 627  ? 2.1082 1.4810 1.8578 -0.2205 -0.2956 -0.4677 627  LEU B CB  
19189 C CG  . LEU C 627  ? 2.0847 1.4434 1.8553 -0.2557 -0.2745 -0.4983 627  LEU B CG  
19190 C CD1 . LEU C 627  ? 2.0404 1.4589 1.8893 -0.2728 -0.2912 -0.5325 627  LEU B CD1 
19191 C CD2 . LEU C 627  ? 2.0812 1.4077 1.8379 -0.2724 -0.2312 -0.4856 627  LEU B CD2 
19192 N N   . GLU C 628  ? 2.1951 1.4268 1.7777 -0.1909 -0.2422 -0.3874 628  GLU B N   
19193 C CA  . GLU C 628  ? 2.2607 1.4295 1.7883 -0.1982 -0.2110 -0.3787 628  GLU B CA  
19194 C C   . GLU C 628  ? 2.2253 1.3656 1.6944 -0.1649 -0.2111 -0.3366 628  GLU B C   
19195 O O   . GLU C 628  ? 2.2558 1.3548 1.6858 -0.1623 -0.1849 -0.3105 628  GLU B O   
19196 C CB  . GLU C 628  ? 2.3678 1.5157 1.9027 -0.2233 -0.1753 -0.3790 628  GLU B CB  
19197 C CG  . GLU C 628  ? 2.5577 1.6956 2.0773 -0.2089 -0.1638 -0.3409 628  GLU B CG  
19198 C CD  . GLU C 628  ? 2.6834 1.7702 2.1752 -0.2276 -0.1234 -0.3353 628  GLU B CD  
19199 O OE1 . GLU C 628  ? 2.7624 1.7993 2.2074 -0.2332 -0.1044 -0.3345 628  GLU B OE1 
19200 O OE2 . GLU C 628  ? 2.6823 1.7749 2.1942 -0.2348 -0.1114 -0.3316 628  GLU B OE2 
19201 N N   . LYS C 629  ? 2.1843 1.3492 1.6498 -0.1381 -0.2408 -0.3280 629  LYS B N   
19202 C CA  . LYS C 629  ? 2.1787 1.3156 1.5854 -0.1047 -0.2394 -0.2913 629  LYS B CA  
19203 C C   . LYS C 629  ? 2.1866 1.2874 1.5490 -0.0998 -0.2425 -0.3145 629  LYS B C   
19204 O O   . LYS C 629  ? 2.1686 1.2429 1.4750 -0.0685 -0.2427 -0.2918 629  LYS B O   
19205 C CB  . LYS C 629  ? 2.1421 1.3235 1.5664 -0.0752 -0.2671 -0.2597 629  LYS B CB  
19206 C CG  . LYS C 629  ? 2.1077 1.3192 1.5761 -0.0826 -0.2713 -0.2424 629  LYS B CG  
19207 C CD  . LYS C 629  ? 2.4260 1.5971 1.8790 -0.1004 -0.2369 -0.2318 629  LYS B CD  
19208 C CE  . LYS C 629  ? 2.1991 1.3888 1.6830 -0.1010 -0.2449 -0.2090 629  LYS B CE  
19209 N NZ  . LYS C 629  ? 2.2057 1.3538 1.6746 -0.1191 -0.2132 -0.2054 629  LYS B NZ  
19210 N N   . SER C 630  ? 2.2007 1.2991 1.5889 -0.1308 -0.2453 -0.3594 630  SER B N   
19211 C CA  . SER C 630  ? 2.2403 1.2916 1.5862 -0.1346 -0.2477 -0.3849 630  SER B CA  
19212 C C   . SER C 630  ? 2.3169 1.3066 1.6156 -0.1476 -0.2119 -0.3773 630  SER B C   
19213 O O   . SER C 630  ? 2.4293 1.3678 1.6869 -0.1557 -0.2098 -0.3976 630  SER B O   
19214 C CB  . SER C 630  ? 2.1963 1.2718 1.5982 -0.1665 -0.2672 -0.4326 630  SER B CB  
19215 O OG  . SER C 630  ? 2.1347 1.2318 1.5909 -0.2011 -0.2474 -0.4431 630  SER B OG  
19216 N N   . ASP C 631  ? 2.2684 1.2591 1.5716 -0.1506 -0.1862 -0.3492 631  ASP B N   
19217 C CA  . ASP C 631  ? 2.3280 1.2574 1.5771 -0.1553 -0.1521 -0.3341 631  ASP B CA  
19218 C C   . ASP C 631  ? 2.3574 1.2538 1.5347 -0.1131 -0.1513 -0.3011 631  ASP B C   
19219 O O   . ASP C 631  ? 2.3160 1.2351 1.4914 -0.0850 -0.1521 -0.2605 631  ASP B O   
19220 C CB  . ASP C 631  ? 2.3071 1.2437 1.5794 -0.1682 -0.1273 -0.3127 631  ASP B CB  
19221 C CG  . ASP C 631  ? 2.6468 1.5170 1.8679 -0.1807 -0.0911 -0.3050 631  ASP B CG  
19222 O OD1 . ASP C 631  ? 2.6724 1.5072 1.8360 -0.1538 -0.0799 -0.2720 631  ASP B OD1 
19223 O OD2 . ASP C 631  ? 2.6707 1.5258 1.9103 -0.2163 -0.0732 -0.3298 631  ASP B OD2 
19224 N N   . LEU C 632  ? 2.4425 1.2849 1.5614 -0.1079 -0.1515 -0.3179 632  LEU B N   
19225 C CA  . LEU C 632  ? 2.4830 1.2890 1.5256 -0.0638 -0.1508 -0.2914 632  LEU B CA  
19226 C C   . LEU C 632  ? 2.4516 1.2306 1.4557 -0.0482 -0.1184 -0.2477 632  LEU B C   
19227 O O   . LEU C 632  ? 2.4658 1.2562 1.4465 -0.0090 -0.1168 -0.2055 632  LEU B O   
19228 C CB  . LEU C 632  ? 2.5605 1.3030 1.5430 -0.0645 -0.1590 -0.3234 632  LEU B CB  
19229 C CG  . LEU C 632  ? 2.5480 1.3048 1.5771 -0.0972 -0.1876 -0.3736 632  LEU B CG  
19230 C CD1 . LEU C 632  ? 2.6141 1.2948 1.5877 -0.1113 -0.1923 -0.4053 632  LEU B CD1 
19231 C CD2 . LEU C 632  ? 2.5258 1.3305 1.5806 -0.0742 -0.2229 -0.3785 632  LEU B CD2 
19232 N N   . GLY C 633  ? 2.4262 1.1714 1.4278 -0.0794 -0.0931 -0.2566 633  GLY B N   
19233 C CA  . GLY C 633  ? 2.3665 1.0773 1.3302 -0.0701 -0.0621 -0.2207 633  GLY B CA  
19234 C C   . GLY C 633  ? 2.2891 1.0416 1.2808 -0.0492 -0.0595 -0.1722 633  GLY B C   
19235 O O   . GLY C 633  ? 2.2217 1.0257 1.2437 -0.0275 -0.0820 -0.1554 633  GLY B O   
19236 N N   . CYS C 634  ? 2.2524 0.9796 1.2332 -0.0560 -0.0344 -0.1486 634  CYS B N   
19237 C CA  . CYS C 634  ? 2.2278 0.9854 1.2329 -0.0379 -0.0345 -0.1000 634  CYS B CA  
19238 C C   . CYS C 634  ? 2.2837 0.9967 1.2661 -0.0488 -0.0060 -0.0810 634  CYS B C   
19239 O O   . CYS C 634  ? 2.3800 1.0336 1.3097 -0.0577 0.0169  -0.0956 634  CYS B O   
19240 C CB  . CYS C 634  ? 2.2395 1.0107 1.2156 0.0099  -0.0414 -0.0581 634  CYS B CB  
19241 S SG  . CYS C 634  ? 2.6399 1.4626 1.6630 0.0313  -0.0524 0.0048  634  CYS B SG  
19242 N N   . GLY C 635  ? 2.2088 0.9457 1.2280 -0.0478 -0.0099 -0.0483 635  GLY B N   
19243 C CA  . GLY C 635  ? 2.2070 0.9003 1.2047 -0.0548 0.0132  -0.0260 635  GLY B CA  
19244 C C   . GLY C 635  ? 2.2356 0.9003 1.2440 -0.0950 0.0288  -0.0592 635  GLY B C   
19245 O O   . GLY C 635  ? 2.2040 0.8877 1.2440 -0.1208 0.0230  -0.1009 635  GLY B O   
19246 N N   . ALA C 636  ? 2.2695 0.8892 1.2527 -0.0992 0.0489  -0.0386 636  ALA B N   
19247 C CA  . ALA C 636  ? 2.3076 0.8939 1.2934 -0.1332 0.0673  -0.0638 636  ALA B CA  
19248 C C   . ALA C 636  ? 2.3169 0.8523 1.2558 -0.1516 0.0926  -0.0969 636  ALA B C   
19249 O O   . ALA C 636  ? 2.3429 0.8566 1.2872 -0.1841 0.1087  -0.1283 636  ALA B O   
19250 C CB  . ALA C 636  ? 2.3476 0.9002 1.3192 -0.1275 0.0758  -0.0276 636  ALA B CB  
19251 N N   . GLY C 637  ? 2.3393 0.8547 1.2304 -0.1282 0.0953  -0.0869 637  GLY B N   
19252 C CA  . GLY C 637  ? 2.4294 0.8929 1.2676 -0.1398 0.1119  -0.1169 637  GLY B CA  
19253 C C   . GLY C 637  ? 2.5197 0.9384 1.2869 -0.1068 0.1242  -0.0872 637  GLY B C   
19254 O O   . GLY C 637  ? 2.4861 0.9225 1.2537 -0.0750 0.1202  -0.0416 637  GLY B O   
19255 N N   . GLY C 638  ? 2.6539 1.0149 1.3616 -0.1137 0.1377  -0.1118 638  GLY B N   
19256 C CA  . GLY C 638  ? 2.7270 1.0297 1.3566 -0.0868 0.1553  -0.0894 638  GLY B CA  
19257 C C   . GLY C 638  ? 2.7076 1.0315 1.3129 -0.0359 0.1460  -0.0528 638  GLY B C   
19258 O O   . GLY C 638  ? 2.6955 1.0745 1.3445 -0.0150 0.1344  -0.0166 638  GLY B O   
19259 N N   . GLY C 639  ? 2.7214 0.9979 1.2534 -0.0144 0.1510  -0.0607 639  GLY B N   
19260 C CA  . GLY C 639  ? 2.6852 0.9740 1.1815 0.0391  0.1471  -0.0257 639  GLY B CA  
19261 C C   . GLY C 639  ? 2.7324 0.9928 1.1822 0.0737  0.1700  0.0225  639  GLY B C   
19262 O O   . GLY C 639  ? 2.6846 0.9604 1.1700 0.0675  0.1781  0.0530  639  GLY B O   
19263 N N   . LEU C 640  ? 2.7981 1.0124 1.1650 0.1111  0.1790  0.0283  640  LEU B N   
19264 C CA  . LEU C 640  ? 2.8036 1.0054 1.1265 0.1587  0.1984  0.0807  640  LEU B CA  
19265 C C   . LEU C 640  ? 2.8849 1.0086 1.0983 0.1875  0.2102  0.0664  640  LEU B C   
19266 O O   . LEU C 640  ? 2.9067 0.9890 1.0623 0.2156  0.2324  0.0943  640  LEU B O   
19267 C CB  . LEU C 640  ? 2.6395 0.9196 1.0089 0.1971  0.1863  0.1258  640  LEU B CB  
19268 C CG  . LEU C 640  ? 2.3864 0.6883 0.7416 0.2514  0.2010  0.1921  640  LEU B CG  
19269 C CD1 . LEU C 640  ? 2.3487 0.5913 0.6515 0.2586  0.2288  0.2116  640  LEU B CD1 
19270 C CD2 . LEU C 640  ? 2.1389 0.5274 0.5909 0.2515  0.1854  0.2340  640  LEU B CD2 
19271 N N   . ASN C 641  ? 2.8998 1.0028 1.0864 0.1801  0.1920  0.0220  641  ASN B N   
19272 C CA  . ASN C 641  ? 2.9876 1.0058 1.0731 0.1930  0.1928  -0.0082 641  ASN B CA  
19273 C C   . ASN C 641  ? 3.0015 1.0071 1.1171 0.1367  0.1723  -0.0666 641  ASN B C   
19274 O O   . ASN C 641  ? 2.9520 1.0230 1.1558 0.1076  0.1577  -0.0760 641  ASN B O   
19275 C CB  . ASN C 641  ? 3.0313 1.0510 1.0649 0.2482  0.1808  0.0009  641  ASN B CB  
19276 C CG  . ASN C 641  ? 3.0324 1.1156 1.0880 0.3007  0.1924  0.0642  641  ASN B CG  
19277 O OD1 . ASN C 641  ? 3.0524 1.1300 1.0918 0.3237  0.2174  0.1065  641  ASN B OD1 
19278 N ND2 . ASN C 641  ? 3.0126 1.1563 1.1058 0.3206  0.1735  0.0726  641  ASN B ND2 
19279 N N   . ASN C 642  ? 3.1014 1.0245 1.1461 0.1218  0.1692  -0.1048 642  ASN B N   
19280 C CA  . ASN C 642  ? 3.1160 1.0287 1.1912 0.0703  0.1465  -0.1581 642  ASN B CA  
19281 C C   . ASN C 642  ? 3.0524 1.0167 1.1615 0.0850  0.1167  -0.1680 642  ASN B C   
19282 O O   . ASN C 642  ? 2.9809 0.9761 1.1534 0.0447  0.0953  -0.2021 642  ASN B O   
19283 C CB  . ASN C 642  ? 3.2759 1.0855 1.2584 0.0608  0.1421  -0.1924 642  ASN B CB  
19284 C CG  . ASN C 642  ? 3.3438 1.1425 1.3598 0.0090  0.1148  -0.2442 642  ASN B CG  
19285 O OD1 . ASN C 642  ? 3.4427 1.1770 1.3935 0.0136  0.0921  -0.2728 642  ASN B OD1 
19286 N ND2 . ASN C 642  ? 3.2890 1.1502 1.4073 -0.0390 0.1153  -0.2551 642  ASN B ND2 
19287 N N   . ALA C 643  ? 3.0811 1.0547 1.1465 0.1450  0.1163  -0.1365 643  ALA B N   
19288 C CA  . ALA C 643  ? 3.0752 1.1047 1.1754 0.1642  0.0912  -0.1377 643  ALA B CA  
19289 C C   . ALA C 643  ? 2.8920 1.0192 1.1101 0.1386  0.0905  -0.1215 643  ALA B C   
19290 O O   . ALA C 643  ? 2.8173 0.9752 1.1048 0.0915  0.0735  -0.1552 643  ALA B O   
19291 C CB  . ALA C 643  ? 3.1626 1.1853 1.1930 0.2370  0.0972  -0.0994 643  ALA B CB  
19292 N N   . ASN C 644  ? 2.8405 1.0138 1.0796 0.1703  0.1082  -0.0684 644  ASN B N   
19293 C CA  . ASN C 644  ? 2.7397 0.9991 1.0823 0.1519  0.1054  -0.0462 644  ASN B CA  
19294 C C   . ASN C 644  ? 2.7458 1.0153 1.1540 0.0871  0.0976  -0.0878 644  ASN B C   
19295 O O   . ASN C 644  ? 2.7450 1.0667 1.2187 0.0667  0.0748  -0.1085 644  ASN B O   
19296 C CB  . ASN C 644  ? 2.6914 0.9673 1.0420 0.1731  0.1312  0.0103  644  ASN B CB  
19297 C CG  . ASN C 644  ? 2.6060 0.9728 1.0441 0.1816  0.1216  0.0508  644  ASN B CG  
19298 O OD1 . ASN C 644  ? 2.5647 0.9531 1.0223 0.1977  0.1360  0.1005  644  ASN B OD1 
19299 N ND2 . ASN C 644  ? 2.5769 0.9949 1.0682 0.1706  0.0946  0.0306  644  ASN B ND2 
19300 N N   . VAL C 645  ? 2.7635 0.9817 1.1515 0.0567  0.1174  -0.0998 645  VAL B N   
19301 C CA  . VAL C 645  ? 2.7527 0.9730 1.1948 -0.0032 0.1159  -0.1375 645  VAL B CA  
19302 C C   . VAL C 645  ? 2.7469 0.9868 1.2233 -0.0280 0.0871  -0.1828 645  VAL B C   
19303 O O   . VAL C 645  ? 2.6902 0.9892 1.2501 -0.0578 0.0762  -0.1956 645  VAL B O   
19304 C CB  . VAL C 645  ? 2.8352 0.9730 1.2203 -0.0286 0.1364  -0.1570 645  VAL B CB  
19305 C CG1 . VAL C 645  ? 2.8336 0.9777 1.2769 -0.0888 0.1357  -0.1948 645  VAL B CG1 
19306 C CG2 . VAL C 645  ? 2.8434 0.9564 1.1961 -0.0094 0.1649  -0.1163 645  VAL B CG2 
19307 N N   . PHE C 646  ? 2.7872 0.9742 1.1970 -0.0147 0.0733  -0.2067 646  PHE B N   
19308 C CA  . PHE C 646  ? 2.7675 0.9658 1.2029 -0.0342 0.0415  -0.2480 646  PHE B CA  
19309 C C   . PHE C 646  ? 2.7202 0.9957 1.2076 -0.0102 0.0201  -0.2354 646  PHE B C   
19310 O O   . PHE C 646  ? 2.6914 1.0115 1.2459 -0.0378 -0.0025 -0.2632 646  PHE B O   
19311 C CB  . PHE C 646  ? 2.8185 0.9333 1.1583 -0.0167 0.0276  -0.2707 646  PHE B CB  
19312 C CG  . PHE C 646  ? 2.8000 0.8556 1.1281 -0.0657 0.0242  -0.3110 646  PHE B CG  
19313 C CD1 . PHE C 646  ? 2.8374 0.8096 1.0853 -0.0651 0.0428  -0.3098 646  PHE B CD1 
19314 C CD2 . PHE C 646  ? 2.7557 0.8406 1.1562 -0.1131 0.0023  -0.3484 646  PHE B CD2 
19315 C CE1 . PHE C 646  ? 2.8529 0.7706 1.0929 -0.1125 0.0383  -0.3448 646  PHE B CE1 
19316 C CE2 . PHE C 646  ? 2.7680 0.8022 1.1653 -0.1605 -0.0009 -0.3816 646  PHE B CE2 
19317 C CZ  . PHE C 646  ? 2.8247 0.7751 1.1421 -0.1610 0.0166  -0.3795 646  PHE B CZ  
19318 N N   . HIS C 647  ? 2.7449 1.0369 1.2028 0.0416  0.0276  -0.1918 647  HIS B N   
19319 C CA  . HIS C 647  ? 2.7192 1.0819 1.2197 0.0695  0.0085  -0.1733 647  HIS B CA  
19320 C C   . HIS C 647  ? 2.5327 0.9755 1.1410 0.0362  0.0023  -0.1717 647  HIS B C   
19321 O O   . HIS C 647  ? 2.4697 0.9470 1.1326 0.0100  -0.0215 -0.2047 647  HIS B O   
19322 C CB  . HIS C 647  ? 2.8604 1.2301 1.3168 0.1291  0.0242  -0.1176 647  HIS B CB  
19323 C CG  . HIS C 647  ? 2.9831 1.3990 1.4470 0.1688  0.0035  -0.1020 647  HIS B CG  
19324 N ND1 . HIS C 647  ? 2.9670 1.4531 1.5129 0.1509  -0.0216 -0.1136 647  HIS B ND1 
19325 C CD2 . HIS C 647  ? 3.0802 1.4815 1.4776 0.2277  0.0056  -0.0742 647  HIS B CD2 
19326 C CE1 . HIS C 647  ? 2.9975 1.5085 1.5272 0.1948  -0.0355 -0.0950 647  HIS B CE1 
19327 N NE2 . HIS C 647  ? 3.0697 1.5309 1.5099 0.2426  -0.0182 -0.0699 647  HIS B NE2 
19328 N N   . LEU C 648  ? 2.4391 0.9079 1.0752 0.0393  0.0222  -0.1324 648  LEU B N   
19329 C CA  . LEU C 648  ? 2.3280 0.8593 1.0544 0.0099  0.0175  -0.1283 648  LEU B CA  
19330 C C   . LEU C 648  ? 2.3173 0.8527 1.0925 -0.0437 0.0100  -0.1784 648  LEU B C   
19331 O O   . LEU C 648  ? 2.2437 0.8375 1.0949 -0.0639 -0.0023 -0.1844 648  LEU B O   
19332 C CB  . LEU C 648  ? 2.2961 0.8205 1.0241 0.0120  0.0426  -0.0882 648  LEU B CB  
19333 C CG  . LEU C 648  ? 2.2475 0.7973 0.9636 0.0608  0.0457  -0.0298 648  LEU B CG  
19334 C CD1 . LEU C 648  ? 2.2460 0.7548 0.9238 0.0712  0.0744  0.0054  648  LEU B CD1 
19335 C CD2 . LEU C 648  ? 2.1603 0.7885 0.9593 0.0596  0.0248  -0.0076 648  LEU B CD2 
19336 N N   . ALA C 649  ? 2.3334 0.8072 1.0658 -0.0657 0.0170  -0.2122 649  ALA B N   
19337 C CA  . ALA C 649  ? 2.3056 0.7846 1.0855 -0.1151 0.0094  -0.2574 649  ALA B CA  
19338 C C   . ALA C 649  ? 2.2331 0.7612 1.0594 -0.1166 -0.0248 -0.2825 649  ALA B C   
19339 O O   . ALA C 649  ? 2.1721 0.7316 1.0625 -0.1540 -0.0342 -0.3128 649  ALA B O   
19340 C CB  . ALA C 649  ? 2.4108 0.8119 1.1309 -0.1335 0.0178  -0.2843 649  ALA B CB  
19341 N N   . GLY C 650  ? 2.2633 0.7972 1.0556 -0.0742 -0.0425 -0.2687 650  GLY B N   
19342 C CA  . GLY C 650  ? 2.2783 0.8449 1.0975 -0.0703 -0.0776 -0.2940 650  GLY B CA  
19343 C C   . GLY C 650  ? 2.3526 0.8533 1.1040 -0.0636 -0.0948 -0.3242 650  GLY B C   
19344 O O   . GLY C 650  ? 2.3454 0.8589 1.1098 -0.0619 -0.1274 -0.3504 650  GLY B O   
19345 N N   . LEU C 651  ? 2.4488 0.8738 1.1238 -0.0590 -0.0750 -0.3205 651  LEU B N   
19346 C CA  . LEU C 651  ? 2.5605 0.9082 1.1637 -0.0575 -0.0917 -0.3505 651  LEU B CA  
19347 C C   . LEU C 651  ? 2.6549 0.9464 1.1510 0.0018  -0.0891 -0.3267 651  LEU B C   
19348 O O   . LEU C 651  ? 2.6499 0.9480 1.1187 0.0357  -0.0629 -0.2836 651  LEU B O   
19349 C CB  . LEU C 651  ? 2.5885 0.8806 1.1790 -0.1011 -0.0746 -0.3704 651  LEU B CB  
19350 C CG  . LEU C 651  ? 2.5275 0.8598 1.2131 -0.1617 -0.0778 -0.4002 651  LEU B CG  
19351 C CD1 . LEU C 651  ? 2.5587 0.8378 1.2267 -0.1983 -0.0530 -0.4085 651  LEU B CD1 
19352 C CD2 . LEU C 651  ? 2.5512 0.8895 1.2660 -0.1795 -0.1184 -0.4395 651  LEU B CD2 
19353 N N   . THR C 652  ? 2.7276 0.9623 1.1625 0.0157  -0.1175 -0.3538 652  THR B N   
19354 C CA  . THR C 652  ? 2.7955 0.9408 1.1095 0.0573  -0.1102 -0.3436 652  THR B CA  
19355 C C   . THR C 652  ? 2.8524 0.9127 1.1210 0.0268  -0.1333 -0.3886 652  THR B C   
19356 O O   . THR C 652  ? 2.8112 0.8826 1.1306 -0.0097 -0.1657 -0.4261 652  THR B O   
19357 C CB  . THR C 652  ? 2.7966 0.9410 1.0464 0.1278  -0.1152 -0.3145 652  THR B CB  
19358 O OG1 . THR C 652  ? 2.8522 0.9379 1.0064 0.1701  -0.0865 -0.2833 652  THR B OG1 
19359 C CG2 . THR C 652  ? 2.8637 0.9669 1.0690 0.1436  -0.1577 -0.3483 652  THR B CG2 
19360 N N   . PHE C 653  ? 2.9086 0.8861 1.0883 0.0380  -0.1165 -0.3832 653  PHE B N   
19361 C CA  . PHE C 653  ? 3.0091 0.9127 1.1631 -0.0037 -0.1321 -0.4207 653  PHE B CA  
19362 C C   . PHE C 653  ? 3.1669 0.9647 1.1914 0.0377  -0.1536 -0.4307 653  PHE B C   
19363 O O   . PHE C 653  ? 3.1574 0.9410 1.1099 0.1010  -0.1484 -0.4051 653  PHE B O   
19364 C CB  . PHE C 653  ? 3.0362 0.9266 1.2017 -0.0375 -0.0952 -0.4108 653  PHE B CB  
19365 C CG  . PHE C 653  ? 3.1212 0.9782 1.2065 0.0092  -0.0595 -0.3709 653  PHE B CG  
19366 C CD1 . PHE C 653  ? 3.2297 0.9910 1.2237 0.0106  -0.0488 -0.3751 653  PHE B CD1 
19367 C CD2 . PHE C 653  ? 3.0746 0.9964 1.1790 0.0503  -0.0376 -0.3277 653  PHE B CD2 
19368 C CE1 . PHE C 653  ? 3.2559 0.9886 1.1788 0.0541  -0.0154 -0.3377 653  PHE B CE1 
19369 C CE2 . PHE C 653  ? 3.1003 0.9962 1.1391 0.0925  -0.0046 -0.2877 653  PHE B CE2 
19370 C CZ  . PHE C 653  ? 3.1885 0.9910 1.1367 0.0952  0.0073  -0.2931 653  PHE B CZ  
19371 N N   . LEU C 654  ? 3.3210 1.0419 1.3142 0.0021  -0.1767 -0.4658 654  LEU B N   
19372 C CA  . LEU C 654  ? 3.5023 1.1156 1.3799 0.0320  -0.2125 -0.4866 654  LEU B CA  
19373 C C   . LEU C 654  ? 3.6947 1.2111 1.5005 0.0122  -0.2066 -0.4968 654  LEU B C   
19374 O O   . LEU C 654  ? 3.7971 1.2756 1.6253 -0.0402 -0.2346 -0.5305 654  LEU B O   
19375 C CB  . LEU C 654  ? 3.4438 1.0597 1.3722 -0.0035 -0.2642 -0.5276 654  LEU B CB  
19376 C CG  . LEU C 654  ? 3.5101 1.0491 1.3336 0.0486  -0.3056 -0.5406 654  LEU B CG  
19377 C CD1 . LEU C 654  ? 3.5091 1.0400 1.2430 0.1274  -0.2747 -0.5000 654  LEU B CD1 
19378 C CD2 . LEU C 654  ? 3.4634 1.0659 1.3702 0.0340  -0.3419 -0.5612 654  LEU B CD2 
19379 N N   . THR C 655  ? 3.7878 1.2633 1.5079 0.0543  -0.1719 -0.4667 655  THR B N   
19380 C CA  . THR C 655  ? 3.9147 1.3095 1.5755 0.0335  -0.1566 -0.4706 655  THR B CA  
19381 C C   . THR C 655  ? 4.1039 1.4090 1.6173 0.1014  -0.1432 -0.4495 655  THR B C   
19382 O O   . THR C 655  ? 4.0514 1.3911 1.5503 0.1419  -0.1020 -0.4092 655  THR B O   
19383 C CB  . THR C 655  ? 4.1516 1.6143 1.8994 -0.0069 -0.1095 -0.4503 655  THR B CB  
19384 O OG1 . THR C 655  ? 4.0582 1.5887 1.9332 -0.0747 -0.1191 -0.4725 655  THR B OG1 
19385 C CG2 . THR C 655  ? 4.2223 1.5988 1.8942 -0.0164 -0.0888 -0.4482 655  THR B CG2 
19386 N N   . ASN C 656  ? 4.3564 1.5443 1.7596 0.1148  -0.1784 -0.4750 656  ASN B N   
19387 C CA  . ASN C 656  ? 4.5670 1.6689 1.8248 0.1852  -0.1655 -0.4547 656  ASN B CA  
19388 C C   . ASN C 656  ? 4.6065 1.6718 1.8306 0.1734  -0.1276 -0.4395 656  ASN B C   
19389 O O   . ASN C 656  ? 4.6783 1.6692 1.8754 0.1304  -0.1422 -0.4652 656  ASN B O   
19390 C CB  . ASN C 656  ? 4.7652 1.7481 1.8967 0.2209  -0.2168 -0.4825 656  ASN B CB  
19391 C CG  . ASN C 656  ? 4.7557 1.7658 1.8665 0.2794  -0.2347 -0.4750 656  ASN B CG  
19392 O OD1 . ASN C 656  ? 4.8529 1.7791 1.8796 0.3046  -0.2822 -0.5006 656  ASN B OD1 
19393 N ND2 . ASN C 656  ? 4.6243 1.7482 1.8099 0.3012  -0.1985 -0.4391 656  ASN B ND2 
19394 N N   . ALA C 657  ? 4.5376 1.6600 1.7690 0.2119  -0.0799 -0.3953 657  ALA B N   
19395 C CA  . ALA C 657  ? 4.5149 1.6246 1.7285 0.2080  -0.0370 -0.3718 657  ALA B CA  
19396 C C   . ALA C 657  ? 4.4240 1.6323 1.6864 0.2481  0.0053  -0.3213 657  ALA B C   
19397 O O   . ALA C 657  ? 4.4574 1.6427 1.6367 0.3156  0.0276  -0.2874 657  ALA B O   
19398 C CB  . ALA C 657  ? 4.4465 1.5787 1.7544 0.1229  -0.0313 -0.3922 657  ALA B CB  
19399 N N   . ASN C 658  ? 4.2917 1.6100 1.6905 0.2071  0.0144  -0.3153 658  ASN B N   
19400 C CA  . ASN C 658  ? 4.1819 1.6000 1.6421 0.2386  0.0460  -0.2685 658  ASN B CA  
19401 C C   . ASN C 658  ? 4.1375 1.6105 1.6190 0.2756  0.0264  -0.2610 658  ASN B C   
19402 O O   . ASN C 658  ? 4.1270 1.6011 1.6363 0.2508  -0.0113 -0.2968 658  ASN B O   
19403 C CB  . ASN C 658  ? 4.0567 1.5597 1.6459 0.1791  0.0668  -0.2622 658  ASN B CB  
19404 C CG  . ASN C 658  ? 4.0153 1.4959 1.5849 0.1744  0.1046  -0.2386 658  ASN B CG  
19405 O OD1 . ASN C 658  ? 3.9141 1.4602 1.5718 0.1435  0.1271  -0.2218 658  ASN B OD1 
19406 N ND2 . ASN C 658  ? 4.0956 1.4792 1.5447 0.2076  0.1104  -0.2373 658  ASN B ND2 
19407 N N   . ALA C 659  ? 4.0860 1.6057 1.5571 0.3347  0.0519  -0.2126 659  ALA B N   
19408 C CA  . ALA C 659  ? 4.0492 1.6302 1.5472 0.3711  0.0385  -0.1986 659  ALA B CA  
19409 C C   . ALA C 659  ? 3.9336 1.6097 1.5718 0.3127  0.0246  -0.2139 659  ALA B C   
19410 O O   . ALA C 659  ? 3.8551 1.6103 1.5838 0.2914  0.0489  -0.1869 659  ALA B O   
19411 C CB  . ALA C 659  ? 4.0280 1.6569 1.5128 0.4354  0.0742  -0.1368 659  ALA B CB  
19412 N N   . ASP C 660  ? 3.9287 1.5946 1.5836 0.2880  -0.0162 -0.2568 660  ASP B N   
19413 C CA  . ASP C 660  ? 3.8227 1.5790 1.6089 0.2356  -0.0319 -0.2735 660  ASP B CA  
19414 C C   . ASP C 660  ? 3.7149 1.5692 1.5618 0.2687  -0.0261 -0.2377 660  ASP B C   
19415 O O   . ASP C 660  ? 3.6022 1.5321 1.5499 0.2352  -0.0420 -0.2496 660  ASP B O   
19416 C CB  . ASP C 660  ? 3.8863 1.6060 1.6812 0.1959  -0.0785 -0.3292 660  ASP B CB  
19417 C CG  . ASP C 660  ? 4.0289 1.6764 1.7187 0.2473  -0.1116 -0.3436 660  ASP B CG  
19418 O OD1 . ASP C 660  ? 4.0398 1.7204 1.7101 0.3033  -0.1089 -0.3164 660  ASP B OD1 
19419 O OD2 . ASP C 660  ? 4.1363 1.6921 1.7636 0.2310  -0.1424 -0.3819 660  ASP B OD2 
19420 N N   . ASP C 661  ? 3.7514 1.6036 1.5367 0.3343  -0.0017 -0.1914 661  ASP B N   
19421 C CA  . ASP C 661  ? 3.6826 1.6118 1.4999 0.3793  0.0039  -0.1509 661  ASP B CA  
19422 C C   . ASP C 661  ? 3.5878 1.6298 1.5422 0.3421  0.0101  -0.1326 661  ASP B C   
19423 O O   . ASP C 661  ? 3.5510 1.6131 1.5756 0.2833  0.0139  -0.1495 661  ASP B O   
19424 C CB  . ASP C 661  ? 3.6385 1.5481 1.3751 0.4496  0.0380  -0.0976 661  ASP B CB  
19425 C CG  . ASP C 661  ? 3.4552 1.4280 1.2584 0.4411  0.0746  -0.0501 661  ASP B CG  
19426 O OD1 . ASP C 661  ? 3.4107 1.3399 1.1862 0.4262  0.0960  -0.0478 661  ASP B OD1 
19427 O OD2 . ASP C 661  ? 3.3529 1.4173 1.2370 0.4485  0.0793  -0.0149 661  ASP B OD2 
19428 N N   . SER C 662  ? 3.5615 1.6731 1.5488 0.3794  0.0105  -0.0968 662  SER B N   
19429 C CA  . SER C 662  ? 3.4887 1.7036 1.5994 0.3496  0.0061  -0.0824 662  SER B CA  
19430 C C   . SER C 662  ? 3.5014 1.7786 1.6233 0.4051  0.0193  -0.0229 662  SER B C   
19431 O O   . SER C 662  ? 3.4283 1.7580 1.5892 0.4165  -0.0015 -0.0204 662  SER B O   
19432 C CB  . SER C 662  ? 3.4868 1.7240 1.6528 0.3105  -0.0336 -0.1326 662  SER B CB  
19433 O OG  . SER C 662  ? 3.5163 1.7680 1.6592 0.3530  -0.0553 -0.1294 662  SER B OG  
19434 N N   . GLN C 663  ? 3.6042 1.8761 1.6944 0.4385  0.0537  0.0267  663  GLN B N   
19435 C CA  . GLN C 663  ? 3.6739 1.9947 1.7609 0.4985  0.0717  0.0909  663  GLN B CA  
19436 C C   . GLN C 663  ? 3.7411 2.1368 1.8877 0.5105  0.0495  0.1025  663  GLN B C   
19437 O O   . GLN C 663  ? 3.6532 2.1252 1.9037 0.4768  0.0404  0.1134  663  GLN B O   
19438 C CB  . GLN C 663  ? 3.5472 1.9075 1.6815 0.4958  0.1025  0.1442  663  GLN B CB  
19439 C CG  . GLN C 663  ? 3.5304 1.8142 1.5971 0.4917  0.1263  0.1373  663  GLN B CG  
19440 C CD  . GLN C 663  ? 3.5809 1.7774 1.5144 0.5450  0.1331  0.1277  663  GLN B CD  
19441 O OE1 . GLN C 663  ? 3.5930 1.7943 1.4826 0.5991  0.1297  0.1450  663  GLN B OE1 
19442 N NE2 . GLN C 663  ? 3.6213 1.7336 1.4853 0.5320  0.1423  0.1008  663  GLN B NE2 
19443 N N   . GLU C 664  ? 3.9452 2.3110 2.0167 0.5611  0.0399  0.0988  664  GLU B N   
19444 C CA  . GLU C 664  ? 4.0528 2.4764 2.1528 0.5903  0.0228  0.1163  664  GLU B CA  
19445 C C   . GLU C 664  ? 4.0779 2.5835 2.2982 0.5407  -0.0045 0.1027  664  GLU B C   
19446 O O   . GLU C 664  ? 3.9884 2.5466 2.2956 0.5017  0.0019  0.1195  664  GLU B O   
19447 C CB  . GLU C 664  ? 4.0882 2.5491 2.1673 0.6585  0.0537  0.1927  664  GLU B CB  
19448 C CG  . GLU C 664  ? 4.0479 2.5677 2.1987 0.6486  0.0818  0.2504  664  GLU B CG  
19449 C CD  . GLU C 664  ? 4.1006 2.6611 2.2362 0.7169  0.1110  0.3290  664  GLU B CD  
19450 O OE1 . GLU C 664  ? 4.0933 2.7104 2.2602 0.7421  0.1007  0.3548  664  GLU B OE1 
19451 O OE2 . GLU C 664  ? 4.1481 2.6855 2.2425 0.7456  0.1446  0.3663  664  GLU B OE2 
19452 N N   . ASN C 665  ? 4.2150 2.7278 2.4356 0.5452  -0.0364 0.0728  665  ASN B N   
19453 C CA  . ASN C 665  ? 4.2309 2.8240 2.5597 0.5077  -0.0625 0.0647  665  ASN B CA  
19454 C C   . ASN C 665  ? 4.2581 2.8577 2.6570 0.4350  -0.0691 0.0273  665  ASN B C   
19455 O O   . ASN C 665  ? 4.3308 2.8622 2.6841 0.4129  -0.0648 -0.0093 665  ASN B O   
19456 C CB  . ASN C 665  ? 4.1756 2.8513 2.5617 0.5352  -0.0465 0.1366  665  ASN B CB  
19457 C CG  . ASN C 665  ? 4.0816 2.8381 2.5699 0.5058  -0.0756 0.1343  665  ASN B CG  
19458 O OD1 . ASN C 665  ? 3.9984 2.7974 2.5722 0.4574  -0.0808 0.1327  665  ASN B OD1 
19459 N ND2 . ASN C 665  ? 4.0939 2.8698 2.5700 0.5377  -0.0950 0.1360  665  ASN B ND2 
19460 N N   . ASP C 666  ? 4.2046 2.8814 2.7096 0.3991  -0.0794 0.0369  666  ASP B N   
19461 C CA  . ASP C 666  ? 4.2049 2.8884 2.7726 0.3366  -0.0786 0.0108  666  ASP B CA  
19462 C C   . ASP C 666  ? 4.0388 2.8015 2.7117 0.3080  -0.0820 0.0387  666  ASP B C   
19463 O O   . ASP C 666  ? 3.9781 2.7936 2.7164 0.2896  -0.1094 0.0244  666  ASP B O   
19464 C CB  . ASP C 666  ? 4.3363 2.9845 2.9058 0.2931  -0.1040 -0.0613 666  ASP B CB  
19465 C CG  . ASP C 666  ? 4.3995 3.0982 3.0256 0.2817  -0.1410 -0.0871 666  ASP B CG  
19466 O OD1 . ASP C 666  ? 4.4208 3.1612 3.0528 0.3193  -0.1491 -0.0553 666  ASP B OD1 
19467 O OD2 . ASP C 666  ? 4.4254 3.1226 3.0910 0.2354  -0.1617 -0.1385 666  ASP B OD2 
19468 N N   . GLU C 667  ? 3.9767 2.7420 2.6595 0.3075  -0.0556 0.0795  667  GLU B N   
19469 C CA  . GLU C 667  ? 3.8366 2.6405 2.6010 0.2654  -0.0563 0.0888  667  GLU B CA  
19470 C C   . GLU C 667  ? 3.7733 2.6426 2.6263 0.2361  -0.0880 0.0745  667  GLU B C   
19471 O O   . GLU C 667  ? 3.7635 2.6292 2.6508 0.1908  -0.0988 0.0276  667  GLU B O   
19472 C CB  . GLU C 667  ? 3.7722 2.5204 2.5202 0.2221  -0.0441 0.0449  667  GLU B CB  
19473 C CG  . GLU C 667  ? 3.7740 2.4434 2.4272 0.2367  -0.0330 0.0151  667  GLU B CG  
19474 C CD  . GLU C 667  ? 3.7454 2.3803 2.3265 0.2850  -0.0034 0.0619  667  GLU B CD  
19475 O OE1 . GLU C 667  ? 3.6868 2.3688 2.2911 0.3174  0.0040  0.1197  667  GLU B OE1 
19476 O OE2 . GLU C 667  ? 3.7931 2.3543 2.2958 0.2911  0.0118  0.0428  667  GLU B OE2 
19477 N N   . PRO C 668  ? 3.7152 2.6450 2.6074 0.2615  -0.1023 0.1170  668  PRO B N   
19478 C CA  . PRO C 668  ? 3.6363 2.6260 2.6109 0.2343  -0.1346 0.1046  668  PRO B CA  
19479 C C   . PRO C 668  ? 3.5844 2.5887 2.6210 0.1914  -0.1362 0.1044  668  PRO B C   
19480 O O   . PRO C 668  ? 3.5142 2.5713 2.6158 0.1833  -0.1589 0.1241  668  PRO B O   
19481 C CB  . PRO C 668  ? 3.6070 2.6512 2.6026 0.2744  -0.1453 0.1617  668  PRO B CB  
19482 C CG  . PRO C 668  ? 3.6731 2.6827 2.5862 0.3252  -0.1230 0.1830  668  PRO B CG  
19483 C CD  . PRO C 668  ? 3.7249 2.6690 2.5828 0.3182  -0.0918 0.1728  668  PRO B CD  
19484 N N   . CYS C 669  ? 3.6122 2.5660 2.6242 0.1659  -0.1140 0.0815  669  CYS B N   
19485 C CA  . CYS C 669  ? 3.5845 2.5379 2.6397 0.1287  -0.1104 0.0800  669  CYS B CA  
19486 C C   . CYS C 669  ? 3.5217 2.5329 2.6553 0.1098  -0.1415 0.0810  669  CYS B C   
19487 O O   . CYS C 669  ? 3.5047 2.5491 2.6644 0.1063  -0.1666 0.0531  669  CYS B O   
19488 C CB  . CYS C 669  ? 3.6236 2.5253 2.6552 0.0919  -0.0951 0.0246  669  CYS B CB  
19489 S SG  . CYS C 669  ? 4.2100 3.1197 3.3027 0.0418  -0.0978 0.0026  669  CYS B SG  
19490 N N   . LYS C 670  ? 3.4888 2.5063 2.6558 0.0981  -0.1416 0.1121  670  LYS B N   
19491 C CA  . LYS C 670  ? 3.4176 2.4827 2.6518 0.0853  -0.1735 0.1216  670  LYS B CA  
19492 C C   . LYS C 670  ? 3.3648 2.4087 2.6184 0.0621  -0.1691 0.1344  670  LYS B C   
19493 O O   . LYS C 670  ? 3.3477 2.3849 2.6013 0.0759  -0.1651 0.1869  670  LYS B O   
19494 C CB  . LYS C 670  ? 3.4108 2.5244 2.6685 0.1191  -0.1942 0.1775  670  LYS B CB  
19495 C CG  . LYS C 670  ? 3.3700 2.5299 2.6937 0.1089  -0.2321 0.1929  670  LYS B CG  
19496 C CD  . LYS C 670  ? 3.3669 2.5502 2.7167 0.0888  -0.2546 0.1357  670  LYS B CD  
19497 C CE  . LYS C 670  ? 3.3245 2.5465 2.7338 0.0783  -0.2930 0.1473  670  LYS B CE  
19498 N NZ  . LYS C 670  ? 3.3008 2.5682 2.7360 0.1059  -0.3198 0.1997  670  LYS B NZ  
19499 N N   . GLU C 671  ? 3.3114 2.3429 2.5805 0.0283  -0.1695 0.0873  671  GLU B N   
19500 C CA  . GLU C 671  ? 3.2364 2.2483 2.5246 0.0074  -0.1705 0.0943  671  GLU B CA  
19501 C C   . GLU C 671  ? 3.0765 2.0340 2.3274 0.0078  -0.1425 0.1226  671  GLU B C   
19502 O O   . GLU C 671  ? 3.0724 2.0239 2.3402 0.0098  -0.1542 0.1613  671  GLU B O   
19503 C CB  . GLU C 671  ? 3.2042 2.2585 2.5446 0.0138  -0.2101 0.1268  671  GLU B CB  
19504 C CG  . GLU C 671  ? 3.1726 2.2776 2.5526 0.0098  -0.2405 0.0954  671  GLU B CG  
19505 C CD  . GLU C 671  ? 3.1051 2.2439 2.5321 0.0144  -0.2821 0.1257  671  GLU B CD  
19506 O OE1 . GLU C 671  ? 3.0866 2.2079 2.5173 0.0193  -0.2895 0.1718  671  GLU B OE1 
19507 O OE2 . GLU C 671  ? 3.0713 2.2515 2.5307 0.0129  -0.3098 0.1036  671  GLU B OE2 
19508 N N   . ILE C 672  ? 3.0079 1.9227 2.2068 0.0062  -0.1089 0.1034  672  ILE B N   
19509 C CA  . ILE C 672  ? 2.9166 1.7728 2.0745 0.0025  -0.0796 0.1196  672  ILE B CA  
19510 C C   . ILE C 672  ? 2.8465 1.6577 1.9861 -0.0326 -0.0571 0.0692  672  ILE B C   
19511 O O   . ILE C 672  ? 2.8446 1.6064 1.9575 -0.0419 -0.0368 0.0774  672  ILE B O   
19512 C CB  . ILE C 672  ? 3.1976 2.0299 2.3005 0.0312  -0.0554 0.1434  672  ILE B CB  
19513 C CG1 . ILE C 672  ? 3.1955 1.9913 2.2765 0.0417  -0.0391 0.1905  672  ILE B CG1 
19514 C CG2 . ILE C 672  ? 3.2512 2.0445 2.3045 0.0196  -0.0316 0.0922  672  ILE B CG2 
19515 C CD1 . ILE C 672  ? 3.2405 2.0057 2.2607 0.0697  -0.0107 0.2092  672  ILE B CD1 
19516 N N   . LEU C 673  ? 2.7487 1.5778 1.9045 -0.0518 -0.0610 0.0186  673  LEU B N   
19517 C CA  . LEU C 673  ? 2.6602 1.4533 1.8042 -0.0851 -0.0383 -0.0271 673  LEU B CA  
19518 C C   . LEU C 673  ? 2.6236 1.3981 1.7832 -0.1011 -0.0361 -0.0205 673  LEU B C   
19519 O O   . LEU C 673  ? 2.6260 1.3810 1.7877 -0.1282 -0.0201 -0.0560 673  LEU B O   
19520 C CB  . LEU C 673  ? 2.5551 1.3826 1.7306 -0.1031 -0.0490 -0.0769 673  LEU B CB  
19521 C CG  . LEU C 673  ? 2.4062 1.2679 1.6369 -0.1231 -0.0640 -0.0991 673  LEU B CG  
19522 C CD1 . LEU C 673  ? 2.3842 1.2483 1.6276 -0.1518 -0.0527 -0.1528 673  LEU B CD1 
19523 C CD2 . LEU C 673  ? 2.3229 1.2457 1.6000 -0.1050 -0.1030 -0.0826 673  LEU B CD2 
19524 N N   . LEU C 679  ? 2.6319 3.5658 2.8762 -0.0582 -0.3241 0.7152  679  LEU B N   
19525 C CA  . LEU C 679  ? 2.6325 3.5530 2.8342 -0.0793 -0.3671 0.6970  679  LEU B CA  
19526 C C   . LEU C 679  ? 2.6253 3.4966 2.8688 -0.0598 -0.3763 0.6574  679  LEU B C   
19527 O O   . LEU C 679  ? 2.6290 3.5010 2.8468 -0.0657 -0.4050 0.6498  679  LEU B O   
19528 C CB  . LEU C 679  ? 2.6408 3.5323 2.7966 -0.1145 -0.3932 0.6791  679  LEU B CB  
19529 C CG  . LEU C 679  ? 2.6430 3.5871 2.7427 -0.1411 -0.3933 0.7170  679  LEU B CG  
19530 C CD1 . LEU C 679  ? 2.6553 3.5584 2.7313 -0.1672 -0.4017 0.6970  679  LEU B CD1 
19531 C CD2 . LEU C 679  ? 2.6439 3.6380 2.6843 -0.1614 -0.4207 0.7411  679  LEU B CD2 
19532 N N   . GLN C 680  ? 2.6181 3.4476 2.9263 -0.0365 -0.3517 0.6320  680  GLN B N   
19533 C CA  . GLN C 680  ? 2.6091 3.3983 2.9645 -0.0147 -0.3544 0.5963  680  GLN B CA  
19534 C C   . GLN C 680  ? 2.5649 3.3908 2.9503 0.0143  -0.3269 0.6217  680  GLN B C   
19535 O O   . GLN C 680  ? 2.5563 3.3616 2.9711 0.0318  -0.3302 0.6000  680  GLN B O   
19536 C CB  . GLN C 680  ? 2.6375 3.3636 3.0501 -0.0044 -0.3414 0.5547  680  GLN B CB  
19537 C CG  . GLN C 680  ? 2.6485 3.3689 3.1338 0.0293  -0.2974 0.5539  680  GLN B CG  
19538 C CD  . GLN C 680  ? 2.6635 3.4243 3.1539 0.0371  -0.2588 0.5954  680  GLN B CD  
19539 O OE1 . GLN C 680  ? 2.6826 3.4732 3.1244 0.0161  -0.2654 0.6220  680  GLN B OE1 
19540 N NE2 . GLN C 680  ? 2.6546 3.4172 3.2041 0.0678  -0.2171 0.6007  680  GLN B NE2 
19541 N N   . LYS C 681  ? 2.5308 3.4118 2.9074 0.0195  -0.2989 0.6682  681  LYS B N   
19542 C CA  . LYS C 681  ? 2.4742 3.3964 2.8724 0.0463  -0.2693 0.7002  681  LYS B CA  
19543 C C   . LYS C 681  ? 2.4751 3.4317 2.8271 0.0392  -0.2966 0.7192  681  LYS B C   
19544 O O   . LYS C 681  ? 2.4690 3.4390 2.8404 0.0616  -0.2828 0.7303  681  LYS B O   
19545 C CB  . LYS C 681  ? 2.4252 3.4010 2.8218 0.0529  -0.2324 0.7476  681  LYS B CB  
19546 C CG  . LYS C 681  ? 2.3856 3.3390 2.7957 0.0457  -0.2185 0.7379  681  LYS B CG  
19547 C CD  . LYS C 681  ? 2.3556 3.3733 2.7346 0.0399  -0.1992 0.7883  681  LYS B CD  
19548 C CE  . LYS C 681  ? 2.3504 3.3450 2.7228 0.0237  -0.1982 0.7776  681  LYS B CE  
19549 N NZ  . LYS C 681  ? 2.3565 3.4168 2.6912 0.0146  -0.1847 0.8254  681  LYS B NZ  
19550 N N   . LYS C 682  ? 2.4873 3.4565 2.7779 0.0078  -0.3337 0.7232  682  LYS B N   
19551 C CA  . LYS C 682  ? 2.4981 3.4980 2.7390 -0.0030 -0.3636 0.7401  682  LYS B CA  
19552 C C   . LYS C 682  ? 2.5355 3.4906 2.7928 0.0079  -0.3854 0.7022  682  LYS B C   
19553 O O   . LYS C 682  ? 2.5200 3.4971 2.7558 0.0131  -0.3983 0.7172  682  LYS B O   
19554 C CB  . LYS C 682  ? 2.4834 3.4990 2.6580 -0.0410 -0.3968 0.7468  682  LYS B CB  
19555 C CG  . LYS C 682  ? 2.4671 3.4845 2.5948 -0.0559 -0.4371 0.7416  682  LYS B CG  
19556 C CD  . LYS C 682  ? 2.4432 3.5232 2.5473 -0.0479 -0.4334 0.7880  682  LYS B CD  
19557 C CE  . LYS C 682  ? 2.4301 3.5073 2.4911 -0.0600 -0.4725 0.7813  682  LYS B CE  
19558 N NZ  . LYS C 682  ? 2.4141 3.5512 2.4512 -0.0525 -0.4697 0.8279  682  LYS B NZ  
19559 N N   . ILE C 683  ? 2.5943 3.4869 2.8886 0.0115  -0.3901 0.6533  683  ILE B N   
19560 C CA  . ILE C 683  ? 2.6453 3.4958 2.9637 0.0252  -0.4067 0.6148  683  ILE B CA  
19561 C C   . ILE C 683  ? 2.6801 3.5251 3.0606 0.0593  -0.3695 0.6137  683  ILE B C   
19562 O O   . ILE C 683  ? 2.7040 3.5456 3.0928 0.0752  -0.3742 0.6082  683  ILE B O   
19563 C CB  . ILE C 683  ? 2.1763 2.9639 2.5063 0.0137  -0.4302 0.5616  683  ILE B CB  
19564 C CG1 . ILE C 683  ? 2.1619 2.9519 2.4405 -0.0195 -0.4509 0.5662  683  ILE B CG1 
19565 C CG2 . ILE C 683  ? 2.1898 2.9476 2.5170 0.0190  -0.4614 0.5283  683  ILE B CG2 
19566 C CD1 . ILE C 683  ? 2.1425 2.8722 2.4369 -0.0294 -0.4637 0.5205  683  ILE B CD1 
19567 N N   . GLU C 684  ? 2.6917 3.5361 3.1140 0.0706  -0.3311 0.6203  684  GLU B N   
19568 C CA  . GLU C 684  ? 2.6991 3.5297 3.1868 0.1024  -0.2913 0.6134  684  GLU B CA  
19569 C C   . GLU C 684  ? 2.6577 3.5342 3.1415 0.1221  -0.2686 0.6549  684  GLU B C   
19570 O O   . GLU C 684  ? 2.6383 3.5025 3.1707 0.1485  -0.2371 0.6493  684  GLU B O   
19571 C CB  . GLU C 684  ? 2.7570 3.5752 3.2899 0.1102  -0.2536 0.6116  684  GLU B CB  
19572 C CG  . GLU C 684  ? 2.8155 3.5698 3.3820 0.1037  -0.2655 0.5583  684  GLU B CG  
19573 C CD  . GLU C 684  ? 2.8527 3.5844 3.4829 0.1215  -0.2221 0.5492  684  GLU B CD  
19574 O OE1 . GLU C 684  ? 2.8611 3.6253 3.5121 0.1407  -0.1801 0.5831  684  GLU B OE1 
19575 O OE2 . GLU C 684  ? 2.8688 3.5498 3.5289 0.1170  -0.2290 0.5085  684  GLU B OE2 
19576 N N   . GLU C 685  ? 2.6411 3.5697 3.0666 0.1086  -0.2837 0.6965  685  GLU B N   
19577 C CA  . GLU C 685  ? 2.6205 3.5944 3.0338 0.1251  -0.2674 0.7387  685  GLU B CA  
19578 C C   . GLU C 685  ? 2.5701 3.5201 2.9757 0.1312  -0.2945 0.7167  685  GLU B C   
19579 O O   . GLU C 685  ? 2.5672 3.5299 2.9843 0.1529  -0.2757 0.7347  685  GLU B O   
19580 C CB  . GLU C 685  ? 2.6457 3.6851 2.9984 0.1063  -0.2770 0.7900  685  GLU B CB  
19581 C CG  . GLU C 685  ? 2.6679 3.7020 2.9644 0.0742  -0.3282 0.7761  685  GLU B CG  
19582 C CD  . GLU C 685  ? 2.6874 3.7789 2.9309 0.0497  -0.3352 0.8176  685  GLU B CD  
19583 O OE1 . GLU C 685  ? 2.6870 3.8190 2.9406 0.0570  -0.3010 0.8528  685  GLU B OE1 
19584 O OE2 . GLU C 685  ? 2.7008 3.7973 2.8926 0.0234  -0.3743 0.8144  685  GLU B OE2 
19585 N N   . ILE C 686  ? 2.5269 3.4413 2.9118 0.1125  -0.3376 0.6783  686  ILE B N   
19586 C CA  . ILE C 686  ? 2.4811 3.3712 2.8545 0.1169  -0.3681 0.6541  686  ILE B CA  
19587 C C   . ILE C 686  ? 2.4285 3.2668 2.8625 0.1400  -0.3555 0.6092  686  ILE B C   
19588 O O   . ILE C 686  ? 2.4437 3.2476 2.8762 0.1407  -0.3853 0.5723  686  ILE B O   
19589 C CB  . ILE C 686  ? 2.5034 3.3778 2.8291 0.0893  -0.4178 0.6318  686  ILE B CB  
19590 C CG1 . ILE C 686  ? 2.5018 3.4234 2.7740 0.0632  -0.4258 0.6710  686  ILE B CG1 
19591 C CG2 . ILE C 686  ? 2.5102 3.3757 2.8105 0.0941  -0.4489 0.6216  686  ILE B CG2 
19592 C CD1 . ILE C 686  ? 2.4974 3.4809 2.7335 0.0664  -0.4188 0.7269  686  ILE B CD1 
19593 N N   . ALA C 687  ? 2.3513 3.1853 2.8386 0.1586  -0.3106 0.6119  687  ALA B N   
19594 C CA  . ALA C 687  ? 2.2662 3.0635 2.8106 0.1836  -0.2885 0.5815  687  ALA B CA  
19595 C C   . ALA C 687  ? 2.2078 3.0343 2.7365 0.2013  -0.2754 0.6165  687  ALA B C   
19596 O O   . ALA C 687  ? 2.1764 2.9816 2.7429 0.2235  -0.2532 0.6027  687  ALA B O   
19597 C CB  . ALA C 687  ? 2.2464 3.0322 2.8505 0.1971  -0.2412 0.5774  687  ALA B CB  
19598 N N   . ALA C 688  ? 2.1701 3.0459 2.6415 0.1902  -0.2887 0.6628  688  ALA B N   
19599 C CA  . ALA C 688  ? 2.1401 3.0497 2.5842 0.2032  -0.2824 0.7032  688  ALA B CA  
19600 C C   . ALA C 688  ? 2.0938 2.9702 2.5298 0.2097  -0.3127 0.6726  688  ALA B C   
19601 O O   . ALA C 688  ? 2.0862 2.9786 2.5064 0.2243  -0.3065 0.6986  688  ALA B O   
19602 C CB  . ALA C 688  ? 2.1313 3.0992 2.5141 0.1850  -0.2977 0.7536  688  ALA B CB  
19603 N N   . LYS C 689  ? 2.1014 2.9325 2.5459 0.1992  -0.3458 0.6189  689  LYS B N   
19604 C CA  . LYS C 689  ? 2.1065 2.9024 2.5514 0.2083  -0.3718 0.5837  689  LYS B CA  
19605 C C   . LYS C 689  ? 2.1963 2.9434 2.7061 0.2244  -0.3537 0.5344  689  LYS B C   
19606 O O   . LYS C 689  ? 2.2130 2.9216 2.7321 0.2241  -0.3826 0.4867  689  LYS B O   
19607 C CB  . LYS C 689  ? 2.0413 2.8256 2.4417 0.1879  -0.4258 0.5612  689  LYS B CB  
19608 C CG  . LYS C 689  ? 1.9711 2.7290 2.3812 0.1680  -0.4441 0.5241  689  LYS B CG  
19609 C CD  . LYS C 689  ? 1.9272 2.6790 2.2860 0.1497  -0.4937 0.5104  689  LYS B CD  
19610 C CE  . LYS C 689  ? 1.8968 2.6984 2.1938 0.1378  -0.5041 0.5629  689  LYS B CE  
19611 N NZ  . LYS C 689  ? 1.8818 2.6778 2.1306 0.1304  -0.5473 0.5541  689  LYS B NZ  
19612 N N   . TYR C 690  ? 2.2560 3.0065 2.8113 0.2386  -0.3049 0.5462  690  TYR B N   
19613 C CA  . TYR C 690  ? 2.3476 3.0560 2.9649 0.2567  -0.2807 0.5057  690  TYR B CA  
19614 C C   . TYR C 690  ? 2.3887 3.0869 2.9992 0.2744  -0.2837 0.5028  690  TYR B C   
19615 O O   . TYR C 690  ? 2.3826 3.1136 2.9571 0.2819  -0.2765 0.5489  690  TYR B O   
19616 C CB  . TYR C 690  ? 2.4196 3.1357 3.0848 0.2696  -0.2234 0.5236  690  TYR B CB  
19617 C CG  . TYR C 690  ? 2.5048 3.1884 3.2260 0.2926  -0.1883 0.4984  690  TYR B CG  
19618 C CD1 . TYR C 690  ? 2.5380 3.1716 3.3059 0.2930  -0.1979 0.4360  690  TYR B CD1 
19619 C CD2 . TYR C 690  ? 2.5505 3.2540 3.2772 0.3136  -0.1445 0.5372  690  TYR B CD2 
19620 C CE1 . TYR C 690  ? 2.5707 3.1748 3.3897 0.3121  -0.1655 0.4109  690  TYR B CE1 
19621 C CE2 . TYR C 690  ? 2.5830 3.2546 3.3593 0.3336  -0.1100 0.5136  690  TYR B CE2 
19622 C CZ  . TYR C 690  ? 2.5956 3.2175 3.4181 0.3320  -0.1209 0.4495  690  TYR B CZ  
19623 O OH  . TYR C 690  ? 2.6156 3.2062 3.4874 0.3502  -0.0859 0.4246  690  TYR B OH  
19624 N N   . LYS C 691  ? 2.4257 3.0786 3.0702 0.2807  -0.2954 0.4480  691  LYS B N   
19625 C CA  . LYS C 691  ? 2.4698 3.1053 3.1097 0.2963  -0.3030 0.4348  691  LYS B CA  
19626 C C   . LYS C 691  ? 2.4766 3.0630 3.1660 0.2981  -0.3137 0.3667  691  LYS B C   
19627 O O   . LYS C 691  ? 2.5049 3.0674 3.1960 0.3074  -0.3308 0.3369  691  LYS B O   
19628 C CB  . LYS C 691  ? 2.4647 3.1165 3.0385 0.2891  -0.3492 0.4507  691  LYS B CB  
19629 C CG  . LYS C 691  ? 2.4474 3.0933 2.9954 0.2665  -0.3973 0.4256  691  LYS B CG  
19630 C CD  . LYS C 691  ? 2.4336 3.1008 2.9141 0.2597  -0.4366 0.4495  691  LYS B CD  
19631 C CE  . LYS C 691  ? 2.4136 3.0822 2.8636 0.2352  -0.4757 0.4365  691  LYS B CE  
19632 N NZ  . LYS C 691  ? 2.4159 3.1091 2.8001 0.2280  -0.5083 0.4654  691  LYS B NZ  
19633 N N   . HIS C 692  ? 2.4663 3.0396 3.1954 0.2890  -0.3034 0.3438  692  HIS B N   
19634 C CA  . HIS C 692  ? 2.4546 2.9850 3.2369 0.2882  -0.3101 0.2809  692  HIS B CA  
19635 C C   . HIS C 692  ? 2.3710 2.8986 3.1725 0.2723  -0.3093 0.2724  692  HIS B C   
19636 O O   . HIS C 692  ? 2.3428 2.8959 3.1019 0.2572  -0.3251 0.3026  692  HIS B O   
19637 C CB  . HIS C 692  ? 2.5238 3.0336 3.2852 0.2847  -0.3614 0.2403  692  HIS B CB  
19638 C CG  . HIS C 692  ? 2.6020 3.0710 3.4201 0.2892  -0.3643 0.1768  692  HIS B CG  
19639 N ND1 . HIS C 692  ? 2.6397 3.0894 3.5069 0.3054  -0.3283 0.1587  692  HIS B ND1 
19640 C CD2 . HIS C 692  ? 2.6255 3.0707 3.4589 0.2792  -0.3983 0.1273  692  HIS B CD2 
19641 C CE1 . HIS C 692  ? 2.6626 3.0798 3.5739 0.3042  -0.3412 0.0996  692  HIS B CE1 
19642 N NE2 . HIS C 692  ? 2.6528 3.0678 3.5450 0.2890  -0.3838 0.0803  692  HIS B NE2 
19643 N N   . SER C 693  ? 2.3216 2.8176 3.1868 0.2754  -0.2897 0.2319  693  SER B N   
19644 C CA  . SER C 693  ? 2.2456 2.7331 3.1325 0.2619  -0.2886 0.2206  693  SER B CA  
19645 C C   . SER C 693  ? 2.1617 2.6466 3.0062 0.2420  -0.3424 0.2054  693  SER B C   
19646 O O   . SER C 693  ? 2.1488 2.6525 2.9592 0.2268  -0.3511 0.2325  693  SER B O   
19647 C CB  . SER C 693  ? 2.2464 2.6950 3.2102 0.2687  -0.2661 0.1708  693  SER B CB  
19648 O OG  . SER C 693  ? 2.2265 2.6594 3.2086 0.2546  -0.2766 0.1503  693  SER B OG  
19649 N N   . VAL C 694  ? 2.0989 2.5608 2.9441 0.2428  -0.3771 0.1624  694  VAL B N   
19650 C CA  . VAL C 694  ? 2.0399 2.4906 2.8572 0.2268  -0.4260 0.1360  694  VAL B CA  
19651 C C   . VAL C 694  ? 1.9928 2.4737 2.7362 0.2118  -0.4518 0.1773  694  VAL B C   
19652 O O   . VAL C 694  ? 1.9904 2.4646 2.7093 0.1952  -0.4823 0.1658  694  VAL B O   
19653 C CB  . VAL C 694  ? 1.9740 2.4014 2.7996 0.2344  -0.4582 0.0871  694  VAL B CB  
19654 C CG1 . VAL C 694  ? 1.9655 2.3782 2.7734 0.2201  -0.5026 0.0555  694  VAL B CG1 
19655 C CG2 . VAL C 694  ? 1.9772 2.3776 2.8755 0.2482  -0.4312 0.0465  694  VAL B CG2 
19656 N N   . VAL C 695  ? 1.9586 2.4727 2.6666 0.2172  -0.4384 0.2258  695  VAL B N   
19657 C CA  . VAL C 695  ? 1.9296 2.4758 2.5709 0.2017  -0.4588 0.2671  695  VAL B CA  
19658 C C   . VAL C 695  ? 1.8842 2.4461 2.5280 0.1887  -0.4358 0.2945  695  VAL B C   
19659 O O   . VAL C 695  ? 1.8697 2.4422 2.4714 0.1686  -0.4583 0.3070  695  VAL B O   
19660 C CB  . VAL C 695  ? 1.9403 2.5190 2.5395 0.2113  -0.4564 0.3103  695  VAL B CB  
19661 C CG1 . VAL C 695  ? 1.9433 2.5555 2.4744 0.1932  -0.4803 0.3496  695  VAL B CG1 
19662 C CG2 . VAL C 695  ? 1.9607 2.5202 2.5580 0.2253  -0.4789 0.2813  695  VAL B CG2 
19663 N N   . LYS C 696  ? 1.8499 2.4117 2.5426 0.2003  -0.3902 0.3027  696  LYS B N   
19664 C CA  . LYS C 696  ? 1.8291 2.4021 2.5296 0.1904  -0.3670 0.3244  696  LYS B CA  
19665 C C   . LYS C 696  ? 1.8124 2.3564 2.5148 0.1720  -0.3945 0.2895  696  LYS B C   
19666 O O   . LYS C 696  ? 1.8169 2.3746 2.4728 0.1520  -0.4145 0.3076  696  LYS B O   
19667 C CB  . LYS C 696  ? 1.8126 2.3783 2.5771 0.2080  -0.3142 0.3253  696  LYS B CB  
19668 C CG  . LYS C 696  ? 1.8103 2.3740 2.5955 0.1994  -0.2927 0.3325  696  LYS B CG  
19669 C CD  . LYS C 696  ? 1.7589 2.3668 2.4865 0.1842  -0.2955 0.3849  696  LYS B CD  
19670 C CE  . LYS C 696  ? 1.7402 2.3464 2.4882 0.1777  -0.2711 0.3938  696  LYS B CE  
19671 N NZ  . LYS C 696  ? 1.7184 2.3686 2.4101 0.1613  -0.2746 0.4423  696  LYS B NZ  
19672 N N   . LYS C 697  ? 1.8025 2.3059 2.5584 0.1788  -0.3947 0.2392  697  LYS B N   
19673 C CA  . LYS C 697  ? 1.7834 2.2551 2.5459 0.1643  -0.4213 0.2014  697  LYS B CA  
19674 C C   . LYS C 697  ? 1.7794 2.2596 2.4741 0.1474  -0.4682 0.2052  697  LYS B C   
19675 O O   . LYS C 697  ? 1.7930 2.2648 2.4642 0.1286  -0.4853 0.2027  697  LYS B O   
19676 C CB  . LYS C 697  ? 1.7850 2.2180 2.6089 0.1763  -0.4221 0.1454  697  LYS B CB  
19677 C CG  . LYS C 697  ? 1.8017 2.2024 2.6329 0.1641  -0.4533 0.1032  697  LYS B CG  
19678 C CD  . LYS C 697  ? 1.8128 2.1960 2.6731 0.1552  -0.4340 0.1009  697  LYS B CD  
19679 C CE  . LYS C 697  ? 1.8260 2.1748 2.6968 0.1452  -0.4641 0.0572  697  LYS B CE  
19680 N NZ  . LYS C 697  ? 1.8286 2.1584 2.7143 0.1336  -0.4518 0.0581  697  LYS B NZ  
19681 N N   . CYS C 698  ? 1.7659 2.2617 2.4280 0.1542  -0.4868 0.2130  698  CYS B N   
19682 C CA  . CYS C 698  ? 1.7453 2.2501 2.3427 0.1404  -0.5289 0.2187  698  CYS B CA  
19683 C C   . CYS C 698  ? 1.7414 2.2732 2.2871 0.1188  -0.5308 0.2602  698  CYS B C   
19684 O O   . CYS C 698  ? 1.7021 2.2219 2.2185 0.1002  -0.5556 0.2498  698  CYS B O   
19685 C CB  . CYS C 698  ? 1.7585 2.2794 2.3287 0.1537  -0.5427 0.2286  698  CYS B CB  
19686 S SG  . CYS C 698  ? 2.1810 2.6677 2.7786 0.1699  -0.5692 0.1705  698  CYS B SG  
19687 N N   . CYS C 699  ? 1.7582 2.3268 2.2918 0.1208  -0.5040 0.3072  699  CYS B N   
19688 C CA  . CYS C 699  ? 1.8209 2.4182 2.3060 0.0992  -0.5062 0.3453  699  CYS B CA  
19689 C C   . CYS C 699  ? 1.8469 2.4256 2.3573 0.0881  -0.4905 0.3358  699  CYS B C   
19690 O O   . CYS C 699  ? 1.8561 2.4307 2.3304 0.0657  -0.5088 0.3372  699  CYS B O   
19691 C CB  . CYS C 699  ? 1.8299 2.4763 2.2959 0.1048  -0.4811 0.3999  699  CYS B CB  
19692 S SG  . CYS C 699  ? 1.8080 2.4920 2.2323 0.0801  -0.4720 0.4451  699  CYS B SG  
19693 N N   . TYR C 700  ? 1.9002 2.4659 2.4725 0.1043  -0.4549 0.3263  700  TYR B N   
19694 C CA  . TYR C 700  ? 1.9925 2.5420 2.5948 0.0980  -0.4330 0.3218  700  TYR B CA  
19695 C C   . TYR C 700  ? 2.0337 2.5456 2.6263 0.0801  -0.4627 0.2868  700  TYR B C   
19696 O O   . TYR C 700  ? 2.0550 2.5731 2.6048 0.0583  -0.4736 0.3031  700  TYR B O   
19697 C CB  . TYR C 700  ? 2.0578 2.5883 2.7365 0.1213  -0.3942 0.3040  700  TYR B CB  
19698 C CG  . TYR C 700  ? 2.1481 2.6806 2.8568 0.1227  -0.3556 0.3214  700  TYR B CG  
19699 C CD1 . TYR C 700  ? 2.1943 2.6863 2.9437 0.1197  -0.3498 0.2892  700  TYR B CD1 
19700 C CD2 . TYR C 700  ? 2.1843 2.7598 2.8815 0.1287  -0.3240 0.3708  700  TYR B CD2 
19701 C CE1 . TYR C 700  ? 2.2219 2.7137 2.9990 0.1228  -0.3141 0.3051  700  TYR B CE1 
19702 C CE2 . TYR C 700  ? 2.2140 2.7924 2.9386 0.1322  -0.2878 0.3870  700  TYR B CE2 
19703 C CZ  . TYR C 700  ? 2.2334 2.7684 2.9978 0.1295  -0.2830 0.3536  700  TYR B CZ  
19704 O OH  . TYR C 700  ? 2.2440 2.7797 3.0359 0.1345  -0.2466 0.3697  700  TYR B OH  
19705 N N   . ASP C 701  ? 2.0712 2.5448 2.7025 0.0890  -0.4753 0.2389  701  ASP B N   
19706 C CA  . ASP C 701  ? 2.0928 2.5311 2.7150 0.0746  -0.5048 0.2045  701  ASP B CA  
19707 C C   . ASP C 701  ? 2.0919 2.5424 2.6449 0.0603  -0.5445 0.2111  701  ASP B C   
19708 O O   . ASP C 701  ? 2.1107 2.5366 2.6423 0.0470  -0.5711 0.1884  701  ASP B O   
19709 C CB  . ASP C 701  ? 2.1084 2.5068 2.7936 0.0891  -0.5067 0.1518  701  ASP B CB  
19710 C CG  . ASP C 701  ? 2.1160 2.5146 2.7991 0.1015  -0.5312 0.1283  701  ASP B CG  
19711 O OD1 . ASP C 701  ? 2.1254 2.5507 2.7568 0.0992  -0.5489 0.1513  701  ASP B OD1 
19712 O OD2 . ASP C 701  ? 2.1082 2.4801 2.8422 0.1138  -0.5330 0.0859  701  ASP B OD2 
19713 N N   . GLY C 702  ? 2.0469 2.5354 2.5656 0.0640  -0.5459 0.2439  702  GLY B N   
19714 C CA  . GLY C 702  ? 2.0121 2.5169 2.4650 0.0519  -0.5794 0.2561  702  GLY B CA  
19715 C C   . GLY C 702  ? 1.9727 2.4876 2.3714 0.0242  -0.5882 0.2799  702  GLY B C   
19716 O O   . GLY C 702  ? 1.9739 2.4759 2.3312 0.0091  -0.6178 0.2681  702  GLY B O   
19717 N N   . ALA C 703  ? 1.9341 2.4726 2.3320 0.0174  -0.5611 0.3139  703  ALA B N   
19718 C CA  . ALA C 703  ? 1.9174 2.4666 2.2637 -0.0102 -0.5677 0.3365  703  ALA B CA  
19719 C C   . ALA C 703  ? 1.8752 2.3801 2.2413 -0.0202 -0.5669 0.3072  703  ALA B C   
19720 O O   . ALA C 703  ? 1.9048 2.3993 2.2265 -0.0440 -0.5832 0.3079  703  ALA B O   
19721 C CB  . ALA C 703  ? 1.9250 2.5185 2.2626 -0.0130 -0.5395 0.3835  703  ALA B CB  
19722 N N   . CYS C 704  ? 1.8232 2.3002 2.2566 -0.0017 -0.5476 0.2802  704  CYS B N   
19723 C CA  . CYS C 704  ? 1.7866 2.2276 2.2498 -0.0076 -0.5343 0.2624  704  CYS B CA  
19724 C C   . CYS C 704  ? 1.8153 2.2478 2.2210 -0.0371 -0.5499 0.2717  704  CYS B C   
19725 O O   . CYS C 704  ? 1.8149 2.2722 2.1925 -0.0508 -0.5359 0.3062  704  CYS B O   
19726 C CB  . CYS C 704  ? 1.7660 2.1622 2.2859 0.0072  -0.5393 0.2126  704  CYS B CB  
19727 S SG  . CYS C 704  ? 1.4601 1.8212 2.0466 0.0135  -0.5053 0.1973  704  CYS B SG  
19728 N N   . VAL C 705  ? 1.8276 2.2275 2.2133 -0.0469 -0.5779 0.2426  705  VAL B N   
19729 C CA  . VAL C 705  ? 1.8468 2.2313 2.1802 -0.0750 -0.5895 0.2483  705  VAL B CA  
19730 C C   . VAL C 705  ? 1.9049 2.2562 2.2158 -0.0818 -0.6198 0.2167  705  VAL B C   
19731 O O   . VAL C 705  ? 1.9327 2.2415 2.2693 -0.0818 -0.6193 0.1885  705  VAL B O   
19732 C CB  . VAL C 705  ? 1.8313 2.1839 2.1956 -0.0792 -0.5667 0.2421  705  VAL B CB  
19733 C CG1 . VAL C 705  ? 1.8329 2.2167 2.1802 -0.0890 -0.5421 0.2830  705  VAL B CG1 
19734 C CG2 . VAL C 705  ? 1.7922 2.1168 2.2380 -0.0532 -0.5509 0.2099  705  VAL B CG2 
19735 N N   . ASN C 706  ? 1.9214 2.2908 2.1841 -0.0875 -0.6450 0.2220  706  ASN B N   
19736 C CA  . ASN C 706  ? 1.9556 2.2926 2.2007 -0.0903 -0.6717 0.1904  706  ASN B CA  
19737 C C   . ASN C 706  ? 1.9583 2.3023 2.1267 -0.1143 -0.6923 0.2049  706  ASN B C   
19738 O O   . ASN C 706  ? 1.9607 2.3329 2.0962 -0.1128 -0.7080 0.2171  706  ASN B O   
19739 C CB  . ASN C 706  ? 1.9834 2.3179 2.2656 -0.0636 -0.6853 0.1615  706  ASN B CB  
19740 C CG  . ASN C 706  ? 2.0240 2.3152 2.3294 -0.0576 -0.6987 0.1192  706  ASN B CG  
19741 O OD1 . ASN C 706  ? 2.0524 2.3160 2.3302 -0.0752 -0.7037 0.1135  706  ASN B OD1 
19742 N ND2 . ASN C 706  ? 2.0235 2.3087 2.3800 -0.0329 -0.7034 0.0893  706  ASN B ND2 
19743 N N   . ASN C 707  ? 1.9554 2.2709 2.0958 -0.1365 -0.6908 0.2029  707  ASN B N   
19744 C CA  . ASN C 707  ? 1.9645 2.2846 2.0298 -0.1641 -0.7045 0.2193  707  ASN B CA  
19745 C C   . ASN C 707  ? 1.9220 2.2087 1.9606 -0.1668 -0.7269 0.1918  707  ASN B C   
19746 O O   . ASN C 707  ? 1.9006 2.1860 1.8767 -0.1894 -0.7372 0.2021  707  ASN B O   
19747 C CB  . ASN C 707  ? 2.0031 2.3201 2.0394 -0.1916 -0.6871 0.2425  707  ASN B CB  
19748 C CG  . ASN C 707  ? 2.0064 2.2875 2.0925 -0.1860 -0.6661 0.2280  707  ASN B CG  
19749 O OD1 . ASN C 707  ? 1.9915 2.2557 2.1404 -0.1612 -0.6613 0.2032  707  ASN B OD1 
19750 N ND2 . ASN C 707  ? 2.0216 2.2908 2.0794 -0.2097 -0.6530 0.2436  707  ASN B ND2 
19751 N N   . ASP C 708  ? 1.9003 2.1613 1.9860 -0.1437 -0.7334 0.1570  708  ASP B N   
19752 C CA  . ASP C 708  ? 1.8755 2.1071 1.9390 -0.1430 -0.7534 0.1309  708  ASP B CA  
19753 C C   . ASP C 708  ? 1.8504 2.1039 1.9003 -0.1266 -0.7759 0.1246  708  ASP B C   
19754 O O   . ASP C 708  ? 1.8452 2.0815 1.8677 -0.1253 -0.7934 0.1076  708  ASP B O   
19755 C CB  . ASP C 708  ? 1.8002 1.9900 1.9152 -0.1300 -0.7493 0.0962  708  ASP B CB  
19756 C CG  . ASP C 708  ? 1.7190 1.8717 1.8146 -0.1524 -0.7365 0.0984  708  ASP B CG  
19757 O OD1 . ASP C 708  ? 1.6845 1.8423 1.7203 -0.1792 -0.7339 0.1236  708  ASP B OD1 
19758 O OD2 . ASP C 708  ? 1.6729 1.7915 1.8125 -0.1437 -0.7290 0.0752  708  ASP B OD2 
19759 N N   . GLU C 709  ? 1.8417 2.1329 1.9094 -0.1132 -0.7740 0.1400  709  GLU B N   
19760 C CA  . GLU C 709  ? 1.8601 2.1746 1.9097 -0.0987 -0.7940 0.1403  709  GLU B CA  
19761 C C   . GLU C 709  ? 1.8709 2.2319 1.9065 -0.1003 -0.7879 0.1770  709  GLU B C   
19762 O O   . GLU C 709  ? 1.9102 2.2869 1.9720 -0.1023 -0.7667 0.1951  709  GLU B O   
19763 C CB  . GLU C 709  ? 1.8673 2.1704 1.9703 -0.0671 -0.8040 0.1042  709  GLU B CB  
19764 C CG  . GLU C 709  ? 1.8601 2.1541 2.0380 -0.0520 -0.7856 0.0879  709  GLU B CG  
19765 C CD  . GLU C 709  ? 1.8451 2.1205 2.0710 -0.0261 -0.7979 0.0455  709  GLU B CD  
19766 O OE1 . GLU C 709  ? 1.8406 2.1205 2.0443 -0.0147 -0.8206 0.0334  709  GLU B OE1 
19767 O OE2 . GLU C 709  ? 1.8298 2.0873 2.1153 -0.0173 -0.7847 0.0245  709  GLU B OE2 
19768 N N   . THR C 710  ? 1.8623 2.2452 1.8567 -0.0983 -0.8054 0.1888  710  THR B N   
19769 C CA  . THR C 710  ? 1.8795 2.3083 1.8553 -0.0990 -0.8022 0.2255  710  THR B CA  
19770 C C   . THR C 710  ? 1.9033 2.3506 1.9367 -0.0744 -0.7882 0.2282  710  THR B C   
19771 O O   . THR C 710  ? 1.8813 2.3057 1.9697 -0.0556 -0.7838 0.1980  710  THR B O   
19772 C CB  . THR C 710  ? 2.1537 2.5975 2.0841 -0.0941 -0.8253 0.2316  710  THR B CB  
19773 O OG1 . THR C 710  ? 2.1381 2.5839 2.1038 -0.0618 -0.8346 0.2138  710  THR B OG1 
19774 C CG2 . THR C 710  ? 2.1707 2.5844 2.0576 -0.1074 -0.8407 0.2139  710  THR B CG2 
19775 N N   . CYS C 711  ? 1.9446 2.4338 1.9662 -0.0746 -0.7800 0.2645  711  CYS B N   
19776 C CA  . CYS C 711  ? 1.9681 2.4735 2.0404 -0.0495 -0.7658 0.2677  711  CYS B CA  
19777 C C   . CYS C 711  ? 1.9670 2.4613 2.0550 -0.0231 -0.7843 0.2411  711  CYS B C   
19778 O O   . CYS C 711  ? 1.9776 2.4533 2.1201 -0.0027 -0.7789 0.2124  711  CYS B O   
19779 C CB  . CYS C 711  ? 1.9923 2.5464 2.0476 -0.0536 -0.7515 0.3148  711  CYS B CB  
19780 S SG  . CYS C 711  ? 1.9604 2.5276 2.0551 -0.0586 -0.7144 0.3349  711  CYS B SG  
19781 N N   . GLU C 712  ? 1.9615 2.4663 2.0020 -0.0235 -0.8062 0.2490  712  GLU B N   
19782 C CA  . GLU C 712  ? 1.9686 2.4650 2.0200 0.0033  -0.8244 0.2259  712  GLU B CA  
19783 C C   . GLU C 712  ? 1.9080 2.3641 1.9766 0.0120  -0.8405 0.1784  712  GLU B C   
19784 O O   . GLU C 712  ? 1.8828 2.3309 1.9676 0.0359  -0.8549 0.1543  712  GLU B O   
19785 C CB  . GLU C 712  ? 2.0614 2.5834 2.0597 0.0042  -0.8410 0.2517  712  GLU B CB  
19786 C CG  . GLU C 712  ? 2.1668 2.6838 2.1039 -0.0188 -0.8569 0.2575  712  GLU B CG  
19787 C CD  . GLU C 712  ? 2.2385 2.7813 2.1273 -0.0165 -0.8715 0.2836  712  GLU B CD  
19788 O OE1 . GLU C 712  ? 2.2552 2.8323 2.1438 -0.0119 -0.8622 0.3169  712  GLU B OE1 
19789 O OE2 . GLU C 712  ? 2.2670 2.7952 2.1183 -0.0184 -0.8910 0.2718  712  GLU B OE2 
19790 N N   . GLN C 713  ? 1.8869 2.3185 1.9517 -0.0067 -0.8376 0.1656  713  GLN B N   
19791 C CA  . GLN C 713  ? 1.8527 2.2473 1.9431 0.0027  -0.8480 0.1217  713  GLN B CA  
19792 C C   . GLN C 713  ? 1.7781 2.1635 1.9410 0.0199  -0.8331 0.0994  713  GLN B C   
19793 O O   . GLN C 713  ? 1.7765 2.1471 1.9740 0.0410  -0.8435 0.0646  713  GLN B O   
19794 C CB  . GLN C 713  ? 1.8726 2.2416 1.9378 -0.0224 -0.8462 0.1171  713  GLN B CB  
19795 C CG  . GLN C 713  ? 1.8946 2.2595 1.8941 -0.0344 -0.8646 0.1224  713  GLN B CG  
19796 C CD  . GLN C 713  ? 1.9098 2.2548 1.8737 -0.0650 -0.8573 0.1293  713  GLN B CD  
19797 O OE1 . GLN C 713  ? 1.9065 2.2442 1.8897 -0.0790 -0.8386 0.1355  713  GLN B OE1 
19798 N NE2 . GLN C 713  ? 1.9252 2.2603 1.8353 -0.0750 -0.8708 0.1289  713  GLN B NE2 
19799 N N   . ARG C 714  ? 1.7164 2.1121 1.9019 0.0108  -0.8076 0.1200  714  ARG B N   
19800 C CA  . ARG C 714  ? 1.6577 2.0468 1.9127 0.0263  -0.7882 0.1036  714  ARG B CA  
19801 C C   . ARG C 714  ? 1.5964 2.0041 1.8739 0.0515  -0.7892 0.1025  714  ARG B C   
19802 O O   . ARG C 714  ? 1.5697 1.9630 1.8976 0.0708  -0.7892 0.0694  714  ARG B O   
19803 C CB  . ARG C 714  ? 1.6774 2.0756 1.9465 0.0117  -0.7584 0.1305  714  ARG B CB  
19804 C CG  . ARG C 714  ? 1.7177 2.0905 1.9761 -0.0108 -0.7536 0.1263  714  ARG B CG  
19805 C CD  . ARG C 714  ? 1.7567 2.1485 2.0006 -0.0298 -0.7301 0.1645  714  ARG B CD  
19806 N NE  . ARG C 714  ? 1.7845 2.1829 2.0870 -0.0165 -0.7014 0.1684  714  ARG B NE  
19807 C CZ  . ARG C 714  ? 1.8186 2.2386 2.1202 -0.0257 -0.6765 0.2019  714  ARG B CZ  
19808 N NH1 . ARG C 714  ? 1.8322 2.2715 2.0771 -0.0500 -0.6780 0.2343  714  ARG B NH1 
19809 N NH2 . ARG C 714  ? 1.8201 2.2436 2.1783 -0.0104 -0.6487 0.2029  714  ARG B NH2 
19810 N N   . ALA C 715  ? 1.5718 2.0114 1.8115 0.0508  -0.7900 0.1385  715  ALA B N   
19811 C CA  . ALA C 715  ? 1.4914 1.9483 1.7474 0.0741  -0.7884 0.1431  715  ALA B CA  
19812 C C   . ALA C 715  ? 1.5277 1.9671 1.7907 0.0941  -0.8139 0.1051  715  ALA B C   
19813 O O   . ALA C 715  ? 1.5223 1.9605 1.8227 0.1161  -0.8109 0.0883  715  ALA B O   
19814 C CB  . ALA C 715  ? 1.4978 1.9906 1.7035 0.0689  -0.7892 0.1891  715  ALA B CB  
19815 N N   . ALA C 716  ? 1.5299 1.9557 1.7556 0.0866  -0.8379 0.0918  716  ALA B N   
19816 C CA  . ALA C 716  ? 1.5545 1.9648 1.7847 0.1061  -0.8626 0.0551  716  ALA B CA  
19817 C C   . ALA C 716  ? 1.5612 1.9523 1.8610 0.1213  -0.8558 0.0141  716  ALA B C   
19818 O O   . ALA C 716  ? 1.5474 1.9398 1.8731 0.1438  -0.8617 -0.0057 716  ALA B O   
19819 C CB  . ALA C 716  ? 1.5778 1.9721 1.7661 0.0943  -0.8828 0.0445  716  ALA B CB  
19820 N N   . ARG C 717  ? 1.5701 1.9432 1.8998 0.1083  -0.8422 0.0020  717  ARG B N   
19821 C CA  . ARG C 717  ? 1.5909 1.9437 1.9873 0.1197  -0.8360 -0.0387 717  ARG B CA  
19822 C C   . ARG C 717  ? 1.5695 1.9317 2.0166 0.1335  -0.8133 -0.0382 717  ARG B C   
19823 O O   . ARG C 717  ? 1.5500 1.8971 2.0563 0.1429  -0.8049 -0.0712 717  ARG B O   
19824 C CB  . ARG C 717  ? 1.6372 1.9686 2.0513 0.1012  -0.8232 -0.0448 717  ARG B CB  
19825 C CG  . ARG C 717  ? 1.6714 1.9766 2.1344 0.1095  -0.8298 -0.0918 717  ARG B CG  
19826 C CD  . ARG C 717  ? 1.6889 1.9711 2.1586 0.0898  -0.8177 -0.0914 717  ARG B CD  
19827 N NE  . ARG C 717  ? 1.6909 1.9738 2.0936 0.0683  -0.8229 -0.0615 717  ARG B NE  
19828 C CZ  . ARG C 717  ? 1.6683 1.9607 2.0470 0.0496  -0.8046 -0.0242 717  ARG B CZ  
19829 N NH1 . ARG C 717  ? 1.6454 1.9478 2.0613 0.0513  -0.7788 -0.0102 717  ARG B NH1 
19830 N NH2 . ARG C 717  ? 1.6828 1.9754 1.9998 0.0293  -0.8112 -0.0011 717  ARG B NH2 
19831 N N   . ILE C 718  ? 1.5760 1.9631 2.0002 0.1345  -0.8019 -0.0002 718  ILE B N   
19832 C CA  . ILE C 718  ? 1.5949 1.9913 2.0625 0.1474  -0.7759 0.0059  718  ILE B CA  
19833 C C   . ILE C 718  ? 1.6653 2.0600 2.1503 0.1714  -0.7888 -0.0207 718  ILE B C   
19834 O O   . ILE C 718  ? 1.6528 2.0553 2.0952 0.1791  -0.8132 -0.0171 718  ILE B O   
19835 C CB  . ILE C 718  ? 1.5751 2.0010 2.0108 0.1416  -0.7577 0.0586  718  ILE B CB  
19836 C CG1 . ILE C 718  ? 1.5805 2.0100 2.0168 0.1207  -0.7351 0.0834  718  ILE B CG1 
19837 C CG2 . ILE C 718  ? 1.5470 1.9830 2.0181 0.1607  -0.7352 0.0645  718  ILE B CG2 
19838 C CD1 . ILE C 718  ? 1.5916 2.0544 2.0019 0.1157  -0.7151 0.1349  718  ILE B CD1 
19839 N N   . SER C 719  ? 1.7361 2.1196 2.2839 0.1833  -0.7718 -0.0482 719  SER B N   
19840 C CA  . SER C 719  ? 1.7869 2.1687 2.3546 0.2053  -0.7805 -0.0743 719  SER B CA  
19841 C C   . SER C 719  ? 1.8864 2.2795 2.4754 0.2154  -0.7496 -0.0523 719  SER B C   
19842 O O   . SER C 719  ? 1.9194 2.3233 2.4856 0.2292  -0.7551 -0.0403 719  SER B O   
19843 C CB  . SER C 719  ? 1.7188 2.0785 2.3424 0.2119  -0.7871 -0.1288 719  SER B CB  
19844 O OG  . SER C 719  ? 1.6989 2.0587 2.3299 0.2320  -0.8028 -0.1553 719  SER B OG  
19845 N N   . LEU C 720  ? 1.9635 2.3535 2.5943 0.2089  -0.7154 -0.0445 720  LEU B N   
19846 C CA  . LEU C 720  ? 2.0636 2.4590 2.7300 0.2200  -0.6792 -0.0316 720  LEU B CA  
19847 C C   . LEU C 720  ? 2.1468 2.5620 2.7769 0.2327  -0.6769 0.0010  720  LEU B C   
19848 O O   . LEU C 720  ? 2.1392 2.5516 2.7998 0.2477  -0.6554 -0.0037 720  LEU B O   
19849 C CB  . LEU C 720  ? 2.1035 2.5031 2.7935 0.2084  -0.6424 -0.0053 720  LEU B CB  
19850 C CG  . LEU C 720  ? 2.1763 2.5521 2.9170 0.1996  -0.6340 -0.0374 720  LEU B CG  
19851 C CD1 . LEU C 720  ? 2.1944 2.5753 2.9575 0.1919  -0.5945 -0.0081 720  LEU B CD1 
19852 C CD2 . LEU C 720  ? 2.2194 2.5731 3.0224 0.2129  -0.6321 -0.0900 720  LEU B CD2 
19853 N N   . GLY C 721  ? 2.2545 2.6884 2.8200 0.2266  -0.6972 0.0345  721  GLY B N   
19854 C CA  . GLY C 721  ? 2.3472 2.7991 2.8757 0.2390  -0.6977 0.0662  721  GLY B CA  
19855 C C   . GLY C 721  ? 2.4008 2.8811 2.8689 0.2264  -0.7011 0.1196  721  GLY B C   
19856 O O   . GLY C 721  ? 2.4119 2.9074 2.8815 0.2135  -0.6768 0.1510  721  GLY B O   
19857 N N   . PRO C 722  ? 2.4132 2.9017 2.8277 0.2304  -0.7310 0.1301  722  PRO B N   
19858 C CA  . PRO C 722  ? 2.3969 2.9140 2.7513 0.2193  -0.7363 0.1809  722  PRO B CA  
19859 C C   . PRO C 722  ? 2.3408 2.8848 2.6982 0.2194  -0.6998 0.2296  722  PRO B C   
19860 O O   . PRO C 722  ? 2.3303 2.9032 2.6436 0.2087  -0.6990 0.2751  722  PRO B O   
19861 C CB  . PRO C 722  ? 2.4101 2.9269 2.7247 0.2347  -0.7653 0.1794  722  PRO B CB  
19862 C CG  . PRO C 722  ? 2.4121 2.8989 2.7523 0.2440  -0.7890 0.1207  722  PRO B CG  
19863 C CD  . PRO C 722  ? 2.4143 2.8847 2.8230 0.2451  -0.7635 0.0909  722  PRO B CD  
19864 N N   . ARG C 723  ? 2.3067 2.8416 2.7169 0.2317  -0.6686 0.2194  723  ARG B N   
19865 C CA  . ARG C 723  ? 2.2536 2.8111 2.6756 0.2344  -0.6283 0.2617  723  ARG B CA  
19866 C C   . ARG C 723  ? 2.2245 2.7986 2.6479 0.2133  -0.6119 0.2840  723  ARG B C   
19867 O O   . ARG C 723  ? 2.2294 2.8358 2.6348 0.2091  -0.5898 0.3328  723  ARG B O   
19868 C CB  . ARG C 723  ? 2.2176 2.7545 2.7011 0.2522  -0.5980 0.2364  723  ARG B CB  
19869 C CG  . ARG C 723  ? 2.1676 2.6748 2.6673 0.2681  -0.6202 0.1873  723  ARG B CG  
19870 C CD  . ARG C 723  ? 2.1198 2.6074 2.6813 0.2830  -0.5866 0.1629  723  ARG B CD  
19871 N NE  . ARG C 723  ? 2.0912 2.5549 2.6653 0.2991  -0.6042 0.1212  723  ARG B NE  
19872 C CZ  . ARG C 723  ? 2.0752 2.5131 2.6893 0.2995  -0.6180 0.0645  723  ARG B CZ  
19873 N NH1 . ARG C 723  ? 2.0585 2.4889 2.7040 0.2849  -0.6159 0.0439  723  ARG B NH1 
19874 N NH2 . ARG C 723  ? 2.0818 2.5021 2.7044 0.3145  -0.6341 0.0286  723  ARG B NH2 
19875 N N   . CYS C 724  ? 2.1831 2.7352 2.6275 0.2007  -0.6226 0.2485  724  CYS B N   
19876 C CA  . CYS C 724  ? 2.1412 2.7022 2.5913 0.1814  -0.6069 0.2635  724  CYS B CA  
19877 C C   . CYS C 724  ? 2.1450 2.7082 2.5472 0.1585  -0.6384 0.2648  724  CYS B C   
19878 O O   . CYS C 724  ? 2.1221 2.6946 2.5173 0.1401  -0.6287 0.2814  724  CYS B O   
19879 C CB  . CYS C 724  ? 2.1132 2.6455 2.6312 0.1845  -0.5849 0.2262  724  CYS B CB  
19880 S SG  . CYS C 724  ? 1.7132 2.2047 2.2517 0.1774  -0.6178 0.1632  724  CYS B SG  
19881 N N   . ILE C 725  ? 2.1687 2.7222 2.5375 0.1599  -0.6747 0.2471  725  ILE B N   
19882 C CA  . ILE C 725  ? 2.1745 2.7287 2.4953 0.1388  -0.7026 0.2488  725  ILE B CA  
19883 C C   . ILE C 725  ? 2.1902 2.7817 2.4654 0.1206  -0.6944 0.3017  725  ILE B C   
19884 O O   . ILE C 725  ? 2.2026 2.7952 2.4552 0.0978  -0.7001 0.3069  725  ILE B O   
19885 C CB  . ILE C 725  ? 2.1627 2.7079 2.4477 0.1464  -0.7391 0.2318  725  ILE B CB  
19886 C CG1 . ILE C 725  ? 2.1480 2.6578 2.4746 0.1607  -0.7519 0.1755  725  ILE B CG1 
19887 C CG2 . ILE C 725  ? 2.1659 2.7170 2.3941 0.1240  -0.7627 0.2435  725  ILE B CG2 
19888 C CD1 . ILE C 725  ? 2.1528 2.6528 2.4473 0.1709  -0.7877 0.1548  725  ILE B CD1 
19889 N N   . LYS C 726  ? 2.2000 2.8222 2.4609 0.1305  -0.6809 0.3411  726  LYS B N   
19890 C CA  . LYS C 726  ? 2.2127 2.8771 2.4344 0.1150  -0.6701 0.3945  726  LYS B CA  
19891 C C   . LYS C 726  ? 2.1217 2.7941 2.3739 0.1049  -0.6385 0.4057  726  LYS B C   
19892 O O   . LYS C 726  ? 2.0920 2.7801 2.3166 0.0817  -0.6397 0.4242  726  LYS B O   
19893 C CB  . LYS C 726  ? 2.3194 3.0148 2.5276 0.1315  -0.6577 0.4345  726  LYS B CB  
19894 C CG  . LYS C 726  ? 2.4310 3.1401 2.5822 0.1313  -0.6875 0.4519  726  LYS B CG  
19895 C CD  . LYS C 726  ? 2.5089 3.2603 2.6384 0.1394  -0.6705 0.5071  726  LYS B CD  
19896 C CE  . LYS C 726  ? 2.5631 3.3244 2.6410 0.1430  -0.6989 0.5229  726  LYS B CE  
19897 N NZ  . LYS C 726  ? 2.5813 3.3835 2.6390 0.1518  -0.6820 0.5779  726  LYS B NZ  
19898 N N   . ALA C 727  ? 2.0794 2.7400 2.3887 0.1229  -0.6092 0.3938  727  ALA B N   
19899 C CA  . ALA C 727  ? 2.0259 2.6904 2.3710 0.1179  -0.5759 0.4018  727  ALA B CA  
19900 C C   . ALA C 727  ? 1.9637 2.6046 2.3079 0.0965  -0.5892 0.3760  727  ALA B C   
19901 O O   . ALA C 727  ? 1.9404 2.5910 2.2917 0.0844  -0.5691 0.3919  727  ALA B O   
19902 C CB  . ALA C 727  ? 2.0405 2.6844 2.4517 0.1412  -0.5461 0.3802  727  ALA B CB  
19903 N N   . PHE C 728  ? 1.9108 2.5206 2.2453 0.0931  -0.6220 0.3372  728  PHE B N   
19904 C CA  . PHE C 728  ? 1.8459 2.4287 2.1775 0.0742  -0.6359 0.3108  728  PHE B CA  
19905 C C   . PHE C 728  ? 1.9059 2.5084 2.1707 0.0475  -0.6549 0.3372  728  PHE B C   
19906 O O   . PHE C 728  ? 1.9201 2.5277 2.1761 0.0283  -0.6441 0.3508  728  PHE B O   
19907 C CB  . PHE C 728  ? 1.7354 2.2777 2.0878 0.0837  -0.6605 0.2577  728  PHE B CB  
19908 C CG  . PHE C 728  ? 1.6460 2.1567 2.0031 0.0678  -0.6714 0.2281  728  PHE B CG  
19909 C CD1 . PHE C 728  ? 1.6064 2.1014 2.0069 0.0640  -0.6469 0.2192  728  PHE B CD1 
19910 C CD2 . PHE C 728  ? 1.6231 2.1181 1.9417 0.0582  -0.7046 0.2095  728  PHE B CD2 
19911 C CE1 . PHE C 728  ? 1.6003 2.0644 2.0046 0.0502  -0.6562 0.1935  728  PHE B CE1 
19912 C CE2 . PHE C 728  ? 1.6128 2.0777 1.9344 0.0444  -0.7126 0.1841  728  PHE B CE2 
19913 C CZ  . PHE C 728  ? 1.6073 2.0564 1.9715 0.0401  -0.6888 0.1764  728  PHE B CZ  
19914 N N   . THR C 729  ? 1.9225 2.5352 2.1403 0.0466  -0.6821 0.3443  729  THR B N   
19915 C CA  . THR C 729  ? 1.9395 2.5698 2.0927 0.0211  -0.7011 0.3670  729  THR B CA  
19916 C C   . THR C 729  ? 1.9480 2.6249 2.0784 0.0080  -0.6806 0.4186  729  THR B C   
19917 O O   . THR C 729  ? 1.9587 2.6469 2.0539 -0.0181 -0.6833 0.4342  729  THR B O   
19918 C CB  . THR C 729  ? 2.2961 2.9280 2.4061 0.0260  -0.7326 0.3647  729  THR B CB  
19919 O OG1 . THR C 729  ? 2.2866 2.9111 2.4273 0.0553  -0.7327 0.3504  729  THR B OG1 
19920 C CG2 . THR C 729  ? 2.3074 2.9044 2.3961 0.0149  -0.7598 0.3292  729  THR B CG2 
19921 N N   . GLU C 730  ? 1.9626 2.6673 2.1132 0.0262  -0.6590 0.4452  730  GLU B N   
19922 C CA  . GLU C 730  ? 1.9941 2.7473 2.1282 0.0173  -0.6366 0.4955  730  GLU B CA  
19923 C C   . GLU C 730  ? 2.0012 2.7504 2.1539 0.0026  -0.6163 0.4952  730  GLU B C   
19924 O O   . GLU C 730  ? 2.0157 2.7771 2.1293 -0.0241 -0.6239 0.5087  730  GLU B O   
19925 C CB  . GLU C 730  ? 1.9944 2.7702 2.1594 0.0437  -0.6100 0.5189  730  GLU B CB  
19926 C CG  . GLU C 730  ? 1.9928 2.7876 2.1272 0.0556  -0.6253 0.5382  730  GLU B CG  
19927 C CD  . GLU C 730  ? 1.9811 2.8333 2.0719 0.0445  -0.6192 0.5955  730  GLU B CD  
19928 O OE1 . GLU C 730  ? 1.9569 2.8407 2.0616 0.0432  -0.5888 0.6265  730  GLU B OE1 
19929 O OE2 . GLU C 730  ? 1.9861 2.8528 2.0296 0.0377  -0.6444 0.6094  730  GLU B OE2 
19930 N N   . CYS C 731  ? 2.0098 2.7396 2.2229 0.0204  -0.5897 0.4783  731  CYS B N   
19931 C CA  . CYS C 731  ? 2.0194 2.7461 2.2579 0.0122  -0.5644 0.4810  731  CYS B CA  
19932 C C   . CYS C 731  ? 2.0728 2.7678 2.2909 -0.0123 -0.5841 0.4553  731  CYS B C   
19933 O O   . CYS C 731  ? 2.0771 2.7792 2.2880 -0.0290 -0.5712 0.4688  731  CYS B O   
19934 C CB  . CYS C 731  ? 2.0031 2.7051 2.3144 0.0375  -0.5345 0.4589  731  CYS B CB  
19935 S SG  . CYS C 731  ? 2.5810 3.3149 2.9199 0.0677  -0.5037 0.4889  731  CYS B SG  
19936 N N   . CYS C 732  ? 2.1041 2.7646 2.3116 -0.0139 -0.6144 0.4194  732  CYS B N   
19937 C CA  . CYS C 732  ? 2.1269 2.7537 2.3150 -0.0354 -0.6318 0.3940  732  CYS B CA  
19938 C C   . CYS C 732  ? 2.1635 2.8173 2.2842 -0.0657 -0.6439 0.4242  732  CYS B C   
19939 O O   . CYS C 732  ? 2.1745 2.8212 2.2831 -0.0863 -0.6371 0.4274  732  CYS B O   
19940 C CB  . CYS C 732  ? 2.1315 2.7189 2.3226 -0.0278 -0.6602 0.3507  732  CYS B CB  
19941 S SG  . CYS C 732  ? 2.0636 2.6081 2.2322 -0.0523 -0.6775 0.3212  732  CYS B SG  
19942 N N   . VAL C 733  ? 2.1603 2.8441 2.2369 -0.0688 -0.6614 0.4460  733  VAL B N   
19943 C CA  . VAL C 733  ? 2.1561 2.8696 2.1683 -0.0984 -0.6728 0.4755  733  VAL B CA  
19944 C C   . VAL C 733  ? 2.1318 2.8836 2.1443 -0.1091 -0.6458 0.5125  733  VAL B C   
19945 O O   . VAL C 733  ? 2.1258 2.8774 2.1105 -0.1353 -0.6451 0.5183  733  VAL B O   
19946 C CB  . VAL C 733  ? 2.1555 2.9001 2.1258 -0.0968 -0.6924 0.4972  733  VAL B CB  
19947 C CG1 . VAL C 733  ? 2.1771 2.9634 2.0879 -0.1271 -0.6972 0.5347  733  VAL B CG1 
19948 C CG2 . VAL C 733  ? 2.1516 2.8581 2.1092 -0.0912 -0.7218 0.4612  733  VAL B CG2 
19949 N N   . VAL C 734  ? 2.1136 2.8966 2.1584 -0.0877 -0.6220 0.5368  734  VAL B N   
19950 C CA  . VAL C 734  ? 2.1157 2.9380 2.1665 -0.0923 -0.5929 0.5730  734  VAL B CA  
19951 C C   . VAL C 734  ? 2.1331 2.9271 2.1971 -0.1065 -0.5813 0.5567  734  VAL B C   
19952 O O   . VAL C 734  ? 2.1701 2.9906 2.2025 -0.1291 -0.5751 0.5816  734  VAL B O   
19953 C CB  . VAL C 734  ? 2.0824 2.9236 2.1846 -0.0602 -0.5624 0.5885  734  VAL B CB  
19954 C CG1 . VAL C 734  ? 2.0656 2.9402 2.1830 -0.0611 -0.5280 0.6205  734  VAL B CG1 
19955 C CG2 . VAL C 734  ? 2.0762 2.9533 2.1577 -0.0485 -0.5702 0.6154  734  VAL B CG2 
19956 N N   . ALA C 735  ? 2.1166 2.8570 2.2266 -0.0935 -0.5786 0.5149  735  ALA B N   
19957 C CA  . ALA C 735  ? 2.1136 2.8219 2.2426 -0.1031 -0.5655 0.4983  735  ALA B CA  
19958 C C   . ALA C 735  ? 2.1498 2.8265 2.2335 -0.1322 -0.5909 0.4785  735  ALA B C   
19959 O O   . ALA C 735  ? 2.1598 2.8119 2.2460 -0.1455 -0.5819 0.4699  735  ALA B O   
19960 C CB  . ALA C 735  ? 2.0895 2.7550 2.2904 -0.0769 -0.5493 0.4633  735  ALA B CB  
19961 N N   . SER C 736  ? 2.1719 2.8472 2.2142 -0.1413 -0.6207 0.4716  736  SER B N   
19962 C CA  . SER C 736  ? 2.1987 2.8427 2.1959 -0.1679 -0.6430 0.4528  736  SER B CA  
19963 C C   . SER C 736  ? 2.2337 2.9133 2.1665 -0.2013 -0.6470 0.4859  736  SER B C   
19964 O O   . SER C 736  ? 2.2523 2.9088 2.1576 -0.2263 -0.6486 0.4786  736  SER B O   
19965 C CB  . SER C 736  ? 2.1988 2.8200 2.1832 -0.1606 -0.6715 0.4265  736  SER B CB  
19966 O OG  . SER C 736  ? 2.1829 2.7668 2.2252 -0.1336 -0.6694 0.3905  736  SER B OG  
19967 N N   . GLN C 737  ? 2.2212 2.9567 2.1296 -0.2021 -0.6482 0.5223  737  GLN B N   
19968 C CA  . GLN C 737  ? 2.2222 3.0013 2.0726 -0.2331 -0.6509 0.5568  737  GLN B CA  
19969 C C   . GLN C 737  ? 2.2192 3.0159 2.0846 -0.2390 -0.6233 0.5763  737  GLN B C   
19970 O O   . GLN C 737  ? 2.2134 3.0218 2.0371 -0.2689 -0.6231 0.5896  737  GLN B O   
19971 C CB  . GLN C 737  ? 2.2047 3.0420 2.0326 -0.2285 -0.6574 0.5923  737  GLN B CB  
19972 C CG  . GLN C 737  ? 2.1939 3.0184 2.0437 -0.2001 -0.6705 0.5770  737  GLN B CG  
19973 C CD  . GLN C 737  ? 2.2104 3.0113 2.0182 -0.2116 -0.7018 0.5572  737  GLN B CD  
19974 O OE1 . GLN C 737  ? 2.2305 3.0649 1.9883 -0.2296 -0.7151 0.5808  737  GLN B OE1 
19975 N NE2 . GLN C 737  ? 2.1995 2.9441 2.0288 -0.1998 -0.7126 0.5141  737  GLN B NE2 
19976 N N   . LEU C 738  ? 2.2316 3.0282 2.1570 -0.2097 -0.5989 0.5767  738  LEU B N   
19977 C CA  . LEU C 738  ? 2.2778 3.0912 2.2242 -0.2090 -0.5694 0.5956  738  LEU B CA  
19978 C C   . LEU C 738  ? 2.3641 3.1292 2.3063 -0.2271 -0.5670 0.5718  738  LEU B C   
19979 O O   . LEU C 738  ? 2.3960 3.1790 2.3251 -0.2412 -0.5512 0.5917  738  LEU B O   
19980 C CB  . LEU C 738  ? 2.2168 3.0315 2.2328 -0.1715 -0.5417 0.5960  738  LEU B CB  
19981 C CG  . LEU C 738  ? 2.1726 3.0157 2.2124 -0.1651 -0.5066 0.6233  738  LEU B CG  
19982 C CD1 . LEU C 738  ? 2.1545 3.0748 2.1725 -0.1636 -0.4958 0.6744  738  LEU B CD1 
19983 C CD2 . LEU C 738  ? 2.1340 2.9438 2.2491 -0.1321 -0.4796 0.6028  738  LEU B CD2 
19984 N N   . ARG C 739  ? 2.4393 3.1436 2.3921 -0.2259 -0.5819 0.5303  739  ARG B N   
19985 C CA  . ARG C 739  ? 2.5462 3.2009 2.4980 -0.2408 -0.5774 0.5084  739  ARG B CA  
19986 C C   . ARG C 739  ? 2.5909 3.2494 2.4696 -0.2808 -0.5926 0.5177  739  ARG B C   
19987 O O   . ARG C 739  ? 2.6141 3.2398 2.4797 -0.2984 -0.5864 0.5086  739  ARG B O   
19988 C CB  . ARG C 739  ? 2.6213 3.2104 2.6119 -0.2253 -0.5854 0.4620  739  ARG B CB  
19989 C CG  . ARG C 739  ? 2.7158 3.2840 2.6746 -0.2326 -0.6165 0.4398  739  ARG B CG  
19990 C CD  . ARG C 739  ? 2.7988 3.3072 2.8016 -0.2148 -0.6215 0.3955  739  ARG B CD  
19991 N NE  . ARG C 739  ? 2.8792 3.3685 2.8540 -0.2180 -0.6502 0.3737  739  ARG B NE  
19992 C CZ  . ARG C 739  ? 2.9223 3.3646 2.9246 -0.2046 -0.6603 0.3351  739  ARG B CZ  
19993 N NH1 . ARG C 739  ? 2.9239 3.3326 2.9842 -0.1883 -0.6449 0.3131  739  ARG B NH1 
19994 N NH2 . ARG C 739  ? 2.9435 3.3738 2.9159 -0.2068 -0.6855 0.3189  739  ARG B NH2 
19995 N N   . ALA C 740  ? 2.6145 3.3123 2.4455 -0.2952 -0.6112 0.5363  740  ALA B N   
19996 C CA  . ALA C 740  ? 2.6484 3.3572 2.4084 -0.3347 -0.6244 0.5477  740  ALA B CA  
19997 C C   . ALA C 740  ? 2.6475 3.4091 2.3875 -0.3506 -0.6070 0.5859  740  ALA B C   
19998 O O   . ALA C 740  ? 2.7066 3.4737 2.3931 -0.3850 -0.6116 0.5943  740  ALA B O   
19999 C CB  . ALA C 740  ? 2.6614 3.3935 2.3803 -0.3435 -0.6497 0.5535  740  ALA B CB  
20000 N N   . ASN C 741  ? 2.5636 3.3638 2.3469 -0.3248 -0.5858 0.6086  741  ASN B N   
20001 C CA  . ASN C 741  ? 2.4969 3.3603 2.2643 -0.3341 -0.5686 0.6502  741  ASN B CA  
20002 C C   . ASN C 741  ? 2.6194 3.4754 2.4239 -0.3225 -0.5380 0.6553  741  ASN B C   
20003 O O   . ASN C 741  ? 2.6379 3.5309 2.4148 -0.3402 -0.5271 0.6819  741  ASN B O   
20004 C CB  . ASN C 741  ? 2.3237 3.2540 2.0979 -0.3172 -0.5668 0.6839  741  ASN B CB  
20005 C CG  . ASN C 741  ? 2.2212 3.1808 1.9382 -0.3403 -0.5947 0.6949  741  ASN B CG  
20006 O OD1 . ASN C 741  ? 2.1738 3.1380 1.8992 -0.3241 -0.6075 0.6925  741  ASN B OD1 
20007 N ND2 . ASN C 741  ? 2.1709 3.1478 1.8289 -0.3789 -0.6039 0.7055  741  ASN B ND2 
20008 N N   . ILE C 742  ? 2.7261 3.5364 2.5933 -0.2925 -0.5235 0.6304  742  ILE B N   
20009 C CA  . ILE C 742  ? 2.8340 3.6296 2.7396 -0.2798 -0.4935 0.6322  742  ILE B CA  
20010 C C   . ILE C 742  ? 2.9230 3.6744 2.7937 -0.3091 -0.4981 0.6163  742  ILE B C   
20011 O O   . ILE C 742  ? 2.9328 3.6785 2.8141 -0.3090 -0.4760 0.6242  742  ILE B O   
20012 C CB  . ILE C 742  ? 2.8362 3.5869 2.8188 -0.2424 -0.4777 0.6046  742  ILE B CB  
20013 C CG1 . ILE C 742  ? 2.8188 3.5976 2.8314 -0.2157 -0.4793 0.6104  742  ILE B CG1 
20014 C CG2 . ILE C 742  ? 2.8372 3.5857 2.8632 -0.2250 -0.4420 0.6144  742  ILE B CG2 
20015 C CD1 . ILE C 742  ? 2.7947 3.5290 2.8803 -0.1817 -0.4664 0.5796  742  ILE B CD1 
20016 N N   . SER C 743  ? 2.9789 3.6981 2.8064 -0.3335 -0.5256 0.5947  743  SER B N   
20017 C CA  . SER C 743  ? 3.0368 3.7046 2.8288 -0.3616 -0.5311 0.5755  743  SER B CA  
20018 C C   . SER C 743  ? 3.0586 3.7235 2.7831 -0.3951 -0.5600 0.5693  743  SER B C   
20019 O O   . SER C 743  ? 3.0450 3.7079 2.7694 -0.3880 -0.5791 0.5574  743  SER B O   
20020 C CB  . SER C 743  ? 3.0431 3.6352 2.8848 -0.3422 -0.5254 0.5368  743  SER B CB  
20021 O OG  . SER C 743  ? 3.0314 3.6053 2.8997 -0.3234 -0.5416 0.5129  743  SER B OG  
20022 N N   . LEU C 749  ? 3.1287 3.3487 2.7596 -0.4936 -0.5011 0.4526  749  LEU B N   
20023 C CA  . LEU C 749  ? 3.1039 3.2740 2.7957 -0.4630 -0.5015 0.4230  749  LEU B CA  
20024 C C   . LEU C 749  ? 3.0934 3.2938 2.8058 -0.4467 -0.5220 0.4134  749  LEU B C   
20025 O O   . LEU C 749  ? 3.0938 3.3505 2.7725 -0.4593 -0.5351 0.4306  749  LEU B O   
20026 C CB  . LEU C 749  ? 3.0599 3.2203 2.8254 -0.4292 -0.4773 0.4242  749  LEU B CB  
20027 C CG  . LEU C 749  ? 3.0235 3.1172 2.8473 -0.4039 -0.4719 0.3930  749  LEU B CG  
20028 C CD1 . LEU C 749  ? 3.0572 3.0803 2.8400 -0.4271 -0.4704 0.3793  749  LEU B CD1 
20029 C CD2 . LEU C 749  ? 2.9863 3.0800 2.8841 -0.3707 -0.4464 0.3970  749  LEU B CD2 
20030 N N   . GLY C 750  ? 3.0850 3.2488 2.8532 -0.4186 -0.5247 0.3861  750  GLY B N   
20031 C CA  . GLY C 750  ? 3.0793 3.2635 2.8677 -0.4018 -0.5445 0.3730  750  GLY B CA  
20032 C C   . GLY C 750  ? 3.0727 3.2638 2.9458 -0.3607 -0.5360 0.3629  750  GLY B C   
20033 O O   . GLY C 750  ? 3.0398 3.2193 2.9445 -0.3416 -0.5493 0.3395  750  GLY B O   
20034 N N   . ARG C 751  ? 3.0918 3.3019 3.0015 -0.3469 -0.5126 0.3802  751  ARG B N   
20035 C CA  . ARG C 751  ? 3.0807 3.2990 3.0720 -0.3083 -0.4991 0.3729  751  ARG B CA  
20036 C C   . ARG C 751  ? 3.1310 3.4206 3.1347 -0.2946 -0.5005 0.3947  751  ARG B C   
20037 O O   . ARG C 751  ? 3.1384 3.4744 3.1313 -0.2979 -0.4860 0.4263  751  ARG B O   
20038 C CB  . ARG C 751  ? 2.9917 3.1849 3.0247 -0.2956 -0.4689 0.3774  751  ARG B CB  
20039 C CG  . ARG C 751  ? 2.9259 3.0432 2.9597 -0.3027 -0.4644 0.3549  751  ARG B CG  
20040 C CD  . ARG C 751  ? 2.8278 2.9009 2.9025 -0.2857 -0.4774 0.3173  751  ARG B CD  
20041 N NE  . ARG C 751  ? 2.7726 2.7771 2.8317 -0.2980 -0.4771 0.2990  751  ARG B NE  
20042 C CZ  . ARG C 751  ? 2.7293 2.7069 2.7376 -0.3189 -0.4968 0.2863  751  ARG B CZ  
20043 N NH1 . ARG C 751  ? 2.7053 2.7183 2.6743 -0.3295 -0.5193 0.2884  751  ARG B NH1 
20044 N NH2 . ARG C 751  ? 2.7292 2.6436 2.7260 -0.3280 -0.4924 0.2721  751  ARG B NH2 
20045 N N   . LEU C 752  ? 3.1757 3.4735 3.2013 -0.2786 -0.5174 0.3783  752  LEU B N   
20046 C CA  . LEU C 752  ? 3.2000 3.5562 3.2488 -0.2593 -0.5167 0.3947  752  LEU B CA  
20047 C C   . LEU C 752  ? 3.1586 3.4977 3.2714 -0.2274 -0.5209 0.3657  752  LEU B C   
20048 O O   . LEU C 752  ? 3.1766 3.4815 3.2864 -0.2278 -0.5413 0.3367  752  LEU B O   
20049 C CB  . LEU C 752  ? 3.2607 3.6645 3.2451 -0.2807 -0.5385 0.4150  752  LEU B CB  
20050 C CG  . LEU C 752  ? 3.2835 3.7442 3.2899 -0.2599 -0.5392 0.4321  752  LEU B CG  
20051 C CD1 . LEU C 752  ? 3.2886 3.7993 3.3107 -0.2516 -0.5123 0.4680  752  LEU B CD1 
20052 C CD2 . LEU C 752  ? 3.3080 3.8004 3.2574 -0.2775 -0.5663 0.4415  752  LEU B CD2 
20053 N N   . HIS C 753  ? 3.0973 3.4620 3.2668 -0.1996 -0.5002 0.3742  753  HIS B N   
20054 C CA  . HIS C 753  ? 3.0117 3.3610 3.2480 -0.1687 -0.4988 0.3469  753  HIS B CA  
20055 C C   . HIS C 753  ? 2.8548 3.2553 3.1250 -0.1458 -0.4807 0.3694  753  HIS B C   
20056 O O   . HIS C 753  ? 2.8153 3.2230 3.1259 -0.1307 -0.4501 0.3819  753  HIS B O   
20057 C CB  . HIS C 753  ? 3.0953 3.3902 3.3900 -0.1546 -0.4807 0.3209  753  HIS B CB  
20058 C CG  . HIS C 753  ? 3.2020 3.4600 3.4649 -0.1770 -0.4760 0.3228  753  HIS B CG  
20059 N ND1 . HIS C 753  ? 3.2460 3.5145 3.5043 -0.1819 -0.4508 0.3492  753  HIS B ND1 
20060 C CD2 . HIS C 753  ? 3.2505 3.4605 3.4840 -0.1950 -0.4921 0.3022  753  HIS B CD2 
20061 C CE1 . HIS C 753  ? 3.2893 3.5155 3.5159 -0.2027 -0.4524 0.3439  753  HIS B CE1 
20062 N NE2 . HIS C 753  ? 3.2927 3.4825 3.5036 -0.2112 -0.4764 0.3161  753  HIS B NE2 
20063 N N   . MET C 754  ? 2.7375 3.1725 2.9909 -0.1420 -0.4979 0.3755  754  MET B N   
20064 C CA  . MET C 754  ? 2.6092 3.0914 2.8919 -0.1198 -0.4805 0.3978  754  MET B CA  
20065 C C   . MET C 754  ? 2.5170 2.9721 2.8813 -0.0887 -0.4584 0.3734  754  MET B C   
20066 O O   . MET C 754  ? 2.5164 2.9195 2.9117 -0.0858 -0.4603 0.3395  754  MET B O   
20067 C CB  . MET C 754  ? 2.5679 3.0794 2.8219 -0.1194 -0.5055 0.4015  754  MET B CB  
20068 C CG  . MET C 754  ? 2.5625 3.0816 2.7399 -0.1508 -0.5346 0.4095  754  MET B CG  
20069 S SD  . MET C 754  ? 2.2541 2.7824 2.4119 -0.1447 -0.5670 0.3965  754  MET B SD  
20070 C CE  . MET C 754  ? 1.4298 1.9804 1.6559 -0.1061 -0.5456 0.3995  754  MET B CE  
20071 N N   . LYS C 755  ? 2.4360 2.9263 2.8351 -0.0657 -0.4363 0.3910  755  LYS B N   
20072 C CA  . LYS C 755  ? 2.3824 2.8505 2.8586 -0.0355 -0.4163 0.3662  755  LYS B CA  
20073 C C   . LYS C 755  ? 2.3858 2.8996 2.8866 -0.0129 -0.3917 0.3926  755  LYS B C   
20074 O O   . LYS C 755  ? 2.3677 2.9327 2.8291 -0.0193 -0.3868 0.4336  755  LYS B O   
20075 C CB  . LYS C 755  ? 2.3365 2.7636 2.8627 -0.0280 -0.3901 0.3508  755  LYS B CB  
20076 C CG  . LYS C 755  ? 2.3137 2.6795 2.8541 -0.0352 -0.4082 0.3080  755  LYS B CG  
20077 C CD  . LYS C 755  ? 2.2879 2.6377 2.8373 -0.0294 -0.4371 0.2734  755  LYS B CD  
20078 C CE  . LYS C 755  ? 2.2529 2.5950 2.8773 0.0003  -0.4196 0.2504  755  LYS B CE  
20079 N NZ  . LYS C 755  ? 2.2366 2.5620 2.8672 0.0046  -0.4499 0.2144  755  LYS B NZ  
20080 N N   . THR C 756  ? 2.4270 2.9212 2.9931 0.0131  -0.3760 0.3681  756  THR B N   
20081 C CA  . THR C 756  ? 2.4635 2.9887 3.0683 0.0387  -0.3426 0.3881  756  THR B CA  
20082 C C   . THR C 756  ? 2.5282 3.0116 3.2126 0.0623  -0.3227 0.3496  756  THR B C   
20083 O O   . THR C 756  ? 2.5386 3.0099 3.2457 0.0733  -0.3348 0.3228  756  THR B O   
20084 C CB  . THR C 756  ? 2.4299 2.9956 3.0035 0.0423  -0.3572 0.4066  756  THR B CB  
20085 O OG1 . THR C 756  ? 2.4311 3.0384 2.9327 0.0199  -0.3738 0.4437  756  THR B OG1 
20086 C CG2 . THR C 756  ? 2.4031 2.9960 3.0189 0.0701  -0.3187 0.4270  756  THR B CG2 
20087 N N   . LEU C 757  ? 2.5923 3.0542 3.3190 0.0697  -0.2921 0.3468  757  LEU B N   
20088 C CA  . LEU C 757  ? 2.6621 3.0785 3.4653 0.0882  -0.2738 0.3073  757  LEU B CA  
20089 C C   . LEU C 757  ? 2.6979 3.1229 3.5493 0.1135  -0.2543 0.2981  757  LEU B C   
20090 O O   . LEU C 757  ? 2.6646 3.1322 3.5049 0.1238  -0.2355 0.3324  757  LEU B O   
20091 C CB  . LEU C 757  ? 2.7147 3.1136 3.5538 0.0948  -0.2373 0.3150  757  LEU B CB  
20092 C CG  . LEU C 757  ? 2.7627 3.1138 3.6848 0.1137  -0.2124 0.2777  757  LEU B CG  
20093 C CD1 . LEU C 757  ? 2.7840 3.0847 3.7131 0.1007  -0.2445 0.2335  757  LEU B CD1 
20094 C CD2 . LEU C 757  ? 2.7774 3.1244 3.7326 0.1257  -0.1680 0.2978  757  LEU B CD2 
20095 N N   . LEU C 758  ? 2.7620 3.1463 3.6657 0.1227  -0.2591 0.2515  758  LEU B N   
20096 C CA  . LEU C 758  ? 2.8091 3.1903 3.7709 0.1468  -0.2352 0.2347  758  LEU B CA  
20097 C C   . LEU C 758  ? 2.9682 3.3000 3.9799 0.1489  -0.2492 0.1790  758  LEU B C   
20098 O O   . LEU C 758  ? 2.9814 3.3044 3.9736 0.1409  -0.2875 0.1530  758  LEU B O   
20099 C CB  . LEU C 758  ? 2.6727 3.0875 3.6006 0.1500  -0.2510 0.2477  758  LEU B CB  
20100 C CG  . LEU C 758  ? 2.5324 2.9624 3.5026 0.1754  -0.2131 0.2559  758  LEU B CG  
20101 C CD1 . LEU C 758  ? 2.4843 2.9295 3.4284 0.1778  -0.2383 0.2511  758  LEU B CD1 
20102 C CD2 . LEU C 758  ? 2.4766 2.8669 3.5308 0.1926  -0.1824 0.2183  758  LEU B CD2 
20103 N N   . PRO C 759  ? 3.1078 3.4081 4.1843 0.1600  -0.2179 0.1608  759  PRO B N   
20104 C CA  . PRO C 759  ? 3.1994 3.4536 4.3312 0.1627  -0.2271 0.1078  759  PRO B CA  
20105 C C   . PRO C 759  ? 3.3075 3.5607 4.4629 0.1721  -0.2405 0.0754  759  PRO B C   
20106 O O   . PRO C 759  ? 3.3314 3.5518 4.5366 0.1757  -0.2473 0.0300  759  PRO B O   
20107 C CB  . PRO C 759  ? 3.1785 3.4114 4.3804 0.1794  -0.1781 0.1050  759  PRO B CB  
20108 C CG  . PRO C 759  ? 3.1533 3.4114 4.3195 0.1768  -0.1564 0.1547  759  PRO B CG  
20109 C CD  . PRO C 759  ? 3.1288 3.4365 4.2279 0.1704  -0.1721 0.1912  759  PRO B CD  
20110 N N   . VAL C 760  ? 4.2286 3.4301 3.5144 -0.4061 -0.1072 -0.2924 760  VAL B N   
20111 C CA  . VAL C 760  ? 4.3121 3.4966 3.5699 -0.4469 -0.0782 -0.2945 760  VAL B CA  
20112 C C   . VAL C 760  ? 4.2163 3.4290 3.4942 -0.4279 -0.0645 -0.2904 760  VAL B C   
20113 O O   . VAL C 760  ? 4.2551 3.4497 3.5028 -0.4552 -0.0449 -0.2878 760  VAL B O   
20114 C CB  . VAL C 760  ? 4.7106 3.8256 3.8858 -0.4780 -0.0903 -0.2772 760  VAL B CB  
20115 C CG1 . VAL C 760  ? 4.7750 3.8701 3.9205 -0.5294 -0.0573 -0.2846 760  VAL B CG1 
20116 C CG2 . VAL C 760  ? 4.7569 3.8398 3.9093 -0.4860 -0.1128 -0.2766 760  VAL B CG2 
20117 N N   . SER C 761  ? 4.0016 3.2563 3.3282 -0.3820 -0.0753 -0.2900 761  SER B N   
20118 C CA  . SER C 761  ? 3.8117 3.0953 3.1619 -0.3602 -0.0644 -0.2863 761  SER B CA  
20119 C C   . SER C 761  ? 3.6129 2.8648 2.9139 -0.3490 -0.0821 -0.2606 761  SER B C   
20120 O O   . SER C 761  ? 3.5940 2.8537 2.8943 -0.3484 -0.0685 -0.2561 761  SER B O   
20121 C CB  . SER C 761  ? 3.8338 3.1345 3.2025 -0.3917 -0.0251 -0.3042 761  SER B CB  
20122 O OG  . SER C 761  ? 3.8006 3.1337 3.2011 -0.3679 -0.0144 -0.3039 761  SER B OG  
20123 N N   . LYS C 762  ? 3.4314 2.6480 2.6928 -0.3398 -0.1126 -0.2444 762  LYS B N   
20124 C CA  . LYS C 762  ? 3.2120 2.4000 2.4301 -0.3271 -0.1326 -0.2201 762  LYS B CA  
20125 C C   . LYS C 762  ? 3.0375 2.2563 2.2859 -0.2754 -0.1519 -0.2099 762  LYS B C   
20126 O O   . LYS C 762  ? 3.0404 2.2743 2.3129 -0.2477 -0.1687 -0.2130 762  LYS B O   
20127 C CB  . LYS C 762  ? 3.1284 2.2599 2.2865 -0.3422 -0.1571 -0.2071 762  LYS B CB  
20128 C CG  . LYS C 762  ? 3.0574 2.1447 2.1666 -0.3959 -0.1421 -0.2106 762  LYS B CG  
20129 C CD  . LYS C 762  ? 2.9890 2.0203 2.0428 -0.4062 -0.1703 -0.1984 762  LYS B CD  
20130 C CE  . LYS C 762  ? 2.9664 1.9549 1.9755 -0.4609 -0.1550 -0.2052 762  LYS B CE  
20131 N NZ  . LYS C 762  ? 2.9835 1.9101 1.9304 -0.4703 -0.1852 -0.1895 762  LYS B NZ  
20132 N N   . PRO C 763  ? 2.8957 2.1226 2.1410 -0.2634 -0.1493 -0.1975 763  PRO B N   
20133 C CA  . PRO C 763  ? 2.7484 2.0019 2.0170 -0.2168 -0.1666 -0.1858 763  PRO B CA  
20134 C C   . PRO C 763  ? 2.6848 1.9083 1.9174 -0.1986 -0.1996 -0.1671 763  PRO B C   
20135 O O   . PRO C 763  ? 2.6947 1.8954 1.8927 -0.2021 -0.2085 -0.1500 763  PRO B O   
20136 C CB  . PRO C 763  ? 2.7355 1.9997 2.0041 -0.2191 -0.1516 -0.1782 763  PRO B CB  
20137 C CG  . PRO C 763  ? 2.7679 2.0248 2.0310 -0.2612 -0.1215 -0.1926 763  PRO B CG  
20138 C CD  . PRO C 763  ? 2.8510 2.0689 2.0779 -0.2929 -0.1260 -0.1970 763  PRO B CD  
20139 N N   . GLU C 764  ? 2.5720 1.7948 1.8127 -0.1796 -0.2180 -0.1708 764  GLU B N   
20140 C CA  . GLU C 764  ? 2.4740 1.6753 1.6893 -0.1535 -0.2494 -0.1547 764  GLU B CA  
20141 C C   . GLU C 764  ? 2.3182 1.5605 1.5715 -0.1068 -0.2569 -0.1506 764  GLU B C   
20142 O O   . GLU C 764  ? 2.2791 1.5612 1.5763 -0.0963 -0.2406 -0.1617 764  GLU B O   
20143 C CB  . GLU C 764  ? 2.4985 1.6714 1.6964 -0.1588 -0.2661 -0.1607 764  GLU B CB  
20144 C CG  . GLU C 764  ? 2.4948 1.6938 1.7322 -0.1624 -0.2536 -0.1821 764  GLU B CG  
20145 C CD  . GLU C 764  ? 2.5522 1.7144 1.7635 -0.1862 -0.2631 -0.1895 764  GLU B CD  
20146 O OE1 . GLU C 764  ? 2.5826 1.7033 1.7515 -0.1827 -0.2878 -0.1773 764  GLU B OE1 
20147 O OE2 . GLU C 764  ? 2.5671 1.7418 1.8011 -0.2087 -0.2461 -0.2078 764  GLU B OE2 
20148 N N   . ILE C 765  ? 2.2323 1.4646 1.4690 -0.0787 -0.2811 -0.1350 765  ILE B N   
20149 C CA  . ILE C 765  ? 2.1167 1.3866 1.3850 -0.0355 -0.2868 -0.1296 765  ILE B CA  
20150 C C   . ILE C 765  ? 2.1326 1.3882 1.3827 -0.0044 -0.3154 -0.1172 765  ILE B C   
20151 O O   . ILE C 765  ? 2.1652 1.4061 1.3917 -0.0010 -0.3262 -0.1012 765  ILE B O   
20152 C CB  . ILE C 765  ? 2.0346 1.3263 1.3132 -0.0353 -0.2721 -0.1204 765  ILE B CB  
20153 C CG1 . ILE C 765  ? 1.9744 1.3075 1.2885 0.0059  -0.2737 -0.1166 765  ILE B CG1 
20154 C CG2 . ILE C 765  ? 2.0354 1.2963 1.2734 -0.0467 -0.2836 -0.1026 765  ILE B CG2 
20155 C CD1 . ILE C 765  ? 1.9422 1.3052 1.2818 0.0026  -0.2512 -0.1170 765  ILE B CD1 
20156 N N   . ARG C 766  ? 2.0966 1.3575 1.3591 0.0191  -0.3278 -0.1252 766  ARG B N   
20157 C CA  . ARG C 766  ? 2.0943 1.3333 1.3342 0.0446  -0.3551 -0.1167 766  ARG B CA  
20158 C C   . ARG C 766  ? 2.0940 1.3572 1.3450 0.0843  -0.3640 -0.1036 766  ARG B C   
20159 O O   . ARG C 766  ? 2.1011 1.3572 1.3448 0.1131  -0.3836 -0.1008 766  ARG B O   
20160 C CB  . ARG C 766  ? 2.0595 1.2913 1.3042 0.0545  -0.3661 -0.1303 766  ARG B CB  
20161 C CG  . ARG C 766  ? 2.0508 1.2746 1.3002 0.0195  -0.3529 -0.1464 766  ARG B CG  
20162 C CD  . ARG C 766  ? 2.1038 1.2752 1.3084 -0.0105 -0.3639 -0.1446 766  ARG B CD  
20163 N NE  . ARG C 766  ? 2.1546 1.3211 1.3657 -0.0460 -0.3488 -0.1610 766  ARG B NE  
20164 C CZ  . ARG C 766  ? 2.2372 1.3630 1.4186 -0.0704 -0.3582 -0.1663 766  ARG B CZ  
20165 N NH1 . ARG C 766  ? 2.3007 1.3841 1.4422 -0.0617 -0.3844 -0.1564 766  ARG B NH1 
20166 N NH2 . ARG C 766  ? 2.2455 1.3728 1.4378 -0.1037 -0.3414 -0.1819 766  ARG B NH2 
20167 N N   . SER C 767  ? 2.1038 1.3945 1.3713 0.0856  -0.3495 -0.0959 767  SER B N   
20168 C CA  . SER C 767  ? 2.1353 1.4492 1.4127 0.1199  -0.3565 -0.0829 767  SER B CA  
20169 C C   . SER C 767  ? 2.1493 1.4663 1.4198 0.1062  -0.3496 -0.0687 767  SER B C   
20170 O O   . SER C 767  ? 2.1409 1.4651 1.4182 0.0807  -0.3302 -0.0714 767  SER B O   
20171 C CB  . SER C 767  ? 2.1386 1.4952 1.4540 0.1489  -0.3471 -0.0893 767  SER B CB  
20172 O OG  . SER C 767  ? 2.1277 1.5103 1.4680 0.1351  -0.3239 -0.0932 767  SER B OG  
20173 N N   . TYR C 768  ? 2.1851 1.4966 1.4425 0.1234  -0.3661 -0.0542 768  TYR B N   
20174 C CA  . TYR C 768  ? 2.2207 1.5324 1.4693 0.1104  -0.3639 -0.0397 768  TYR B CA  
20175 C C   . TYR C 768  ? 2.1153 1.4726 1.3966 0.1309  -0.3509 -0.0339 768  TYR B C   
20176 O O   . TYR C 768  ? 2.1126 1.4970 1.4168 0.1625  -0.3506 -0.0373 768  TYR B O   
20177 C CB  . TYR C 768  ? 2.3559 1.6410 1.5778 0.1195  -0.3897 -0.0268 768  TYR B CB  
20178 C CG  . TYR C 768  ? 2.4529 1.7374 1.6656 0.1078  -0.3923 -0.0108 768  TYR B CG  
20179 C CD1 . TYR C 768  ? 2.5294 1.7769 1.7089 0.0700  -0.3943 -0.0068 768  TYR B CD1 
20180 C CD2 . TYR C 768  ? 2.4605 1.7802 1.6962 0.1338  -0.3933 0.0001  768  TYR B CD2 
20181 C CE1 . TYR C 768  ? 2.5725 1.8177 1.7419 0.0587  -0.3987 0.0078  768  TYR B CE1 
20182 C CE2 . TYR C 768  ? 2.5053 1.8256 1.7346 0.1225  -0.3971 0.0145  768  TYR B CE2 
20183 C CZ  . TYR C 768  ? 2.5571 1.8397 1.7530 0.0853  -0.4007 0.0183  768  TYR B CZ  
20184 O OH  . TYR C 768  ? 2.5759 1.8580 1.7642 0.0735  -0.4061 0.0327  768  TYR B OH  
20185 N N   . PHE C 769  ? 2.0226 1.3863 1.3034 0.1123  -0.3407 -0.0251 769  PHE B N   
20186 C CA  . PHE C 769  ? 1.9370 1.3406 1.2451 0.1296  -0.3299 -0.0174 769  PHE B CA  
20187 C C   . PHE C 769  ? 1.9283 1.3287 1.2247 0.1227  -0.3380 -0.0006 769  PHE B C   
20188 O O   . PHE C 769  ? 1.9582 1.3390 1.2362 0.0902  -0.3331 0.0024  769  PHE B O   
20189 C CB  . PHE C 769  ? 1.9030 1.3242 1.2300 0.1126  -0.3043 -0.0255 769  PHE B CB  
20190 C CG  . PHE C 769  ? 1.8601 1.2870 1.2031 0.1163  -0.2953 -0.0430 769  PHE B CG  
20191 C CD1 . PHE C 769  ? 1.8289 1.2818 1.1953 0.1499  -0.2968 -0.0469 769  PHE B CD1 
20192 C CD2 . PHE C 769  ? 1.8618 1.2681 1.1962 0.0851  -0.2853 -0.0558 769  PHE B CD2 
20193 C CE1 . PHE C 769  ? 1.8391 1.2965 1.2204 0.1527  -0.2910 -0.0628 769  PHE B CE1 
20194 C CE2 . PHE C 769  ? 1.8008 1.2146 1.1533 0.0874  -0.2778 -0.0722 769  PHE B CE2 
20195 C CZ  . PHE C 769  ? 1.8616 1.3005 1.2379 0.1212  -0.2818 -0.0757 769  PHE B CZ  
20196 N N   . PRO C 770  ? 1.9236 1.3451 1.2319 0.1529  -0.3495 0.0099  770  PRO B N   
20197 C CA  . PRO C 770  ? 1.9773 1.4020 1.2810 0.1551  -0.3620 0.0264  770  PRO B CA  
20198 C C   . PRO C 770  ? 2.0286 1.4637 1.3356 0.1312  -0.3486 0.0344  770  PRO B C   
20199 O O   . PRO C 770  ? 2.0309 1.4891 1.3573 0.1289  -0.3276 0.0299  770  PRO B O   
20200 C CB  . PRO C 770  ? 1.9449 1.4065 1.2752 0.1957  -0.3654 0.0307  770  PRO B CB  
20201 C CG  . PRO C 770  ? 1.9378 1.3979 1.2720 0.2154  -0.3652 0.0172  770  PRO B CG  
20202 C CD  . PRO C 770  ? 1.9166 1.3645 1.2473 0.1898  -0.3494 0.0047  770  PRO B CD  
20203 N N   . GLU C 771  ? 2.0801 1.4970 1.3677 0.1144  -0.3618 0.0461  771  GLU B N   
20204 C CA  . GLU C 771  ? 2.1177 1.5439 1.4072 0.0926  -0.3513 0.0546  771  GLU B CA  
20205 C C   . GLU C 771  ? 2.0620 1.5367 1.3883 0.1168  -0.3390 0.0593  771  GLU B C   
20206 O O   . GLU C 771  ? 2.0274 1.5256 1.3722 0.1501  -0.3471 0.0623  771  GLU B O   
20207 C CB  . GLU C 771  ? 2.2363 1.6419 1.5042 0.0798  -0.3728 0.0688  771  GLU B CB  
20208 C CG  . GLU C 771  ? 2.3174 1.7292 1.5835 0.0546  -0.3644 0.0783  771  GLU B CG  
20209 C CD  . GLU C 771  ? 2.4098 1.7983 1.6524 0.0403  -0.3885 0.0923  771  GLU B CD  
20210 O OE1 . GLU C 771  ? 2.4440 1.8052 1.6588 0.0048  -0.3862 0.0950  771  GLU B OE1 
20211 O OE2 . GLU C 771  ? 2.4464 1.8433 1.6980 0.0650  -0.4102 0.1003  771  GLU B OE2 
20212 N N   . SER C 772  ? 2.0289 1.5163 1.3638 0.0996  -0.3189 0.0593  772  SER B N   
20213 C CA  . SER C 772  ? 1.9663 1.4956 1.3323 0.1172  -0.3054 0.0644  772  SER B CA  
20214 C C   . SER C 772  ? 1.9221 1.4700 1.2960 0.1193  -0.3149 0.0815  772  SER B C   
20215 O O   . SER C 772  ? 1.9386 1.4657 1.2936 0.1051  -0.3323 0.0893  772  SER B O   
20216 C CB  . SER C 772  ? 1.9513 1.4840 1.3231 0.0986  -0.2806 0.0568  772  SER B CB  
20217 O OG  . SER C 772  ? 1.9440 1.4717 1.3202 0.1035  -0.2703 0.0408  772  SER B OG  
20218 N N   . TRP C 773  ? 1.8782 1.4643 1.2795 0.1356  -0.3040 0.0873  773  TRP B N   
20219 C CA  . TRP C 773  ? 1.8922 1.5029 1.3073 0.1404  -0.3121 0.1030  773  TRP B CA  
20220 C C   . TRP C 773  ? 1.9212 1.5681 1.3613 0.1461  -0.2938 0.1086  773  TRP B C   
20221 O O   . TRP C 773  ? 1.9454 1.5982 1.3924 0.1502  -0.2758 0.1005  773  TRP B O   
20222 C CB  . TRP C 773  ? 1.8788 1.5036 1.3048 0.1715  -0.3304 0.1069  773  TRP B CB  
20223 C CG  . TRP C 773  ? 1.8706 1.5153 1.3127 0.2040  -0.3225 0.0987  773  TRP B CG  
20224 C CD1 . TRP C 773  ? 1.8699 1.4957 1.3016 0.2116  -0.3207 0.0848  773  TRP B CD1 
20225 C CD2 . TRP C 773  ? 1.8516 1.5379 1.3212 0.2324  -0.3157 0.1037  773  TRP B CD2 
20226 N NE1 . TRP C 773  ? 1.8638 1.5154 1.3134 0.2435  -0.3145 0.0810  773  TRP B NE1 
20227 C CE2 . TRP C 773  ? 1.8543 1.5426 1.3260 0.2567  -0.3105 0.0924  773  TRP B CE2 
20228 C CE3 . TRP C 773  ? 1.8462 1.5683 1.3384 0.2386  -0.3132 0.1165  773  TRP B CE3 
20229 C CZ2 . TRP C 773  ? 1.8366 1.5589 1.3285 0.2868  -0.3027 0.0937  773  TRP B CZ2 
20230 C CZ3 . TRP C 773  ? 1.8275 1.5853 1.3419 0.2679  -0.3040 0.1175  773  TRP B CZ3 
20231 C CH2 . TRP C 773  ? 1.8246 1.5811 1.3370 0.2917  -0.2987 0.1063  773  TRP B CH2 
20232 N N   . LEU C 774  ? 1.9192 1.5900 1.3735 0.1468  -0.2995 0.1227  774  LEU B N   
20233 C CA  . LEU C 774  ? 1.9140 1.6142 1.3876 0.1448  -0.2827 0.1298  774  LEU B CA  
20234 C C   . LEU C 774  ? 1.8927 1.5715 1.3510 0.1119  -0.2685 0.1269  774  LEU B C   
20235 O O   . LEU C 774  ? 1.8521 1.5451 1.3213 0.1110  -0.2503 0.1269  774  LEU B O   
20236 C CB  . LEU C 774  ? 1.9374 1.6662 1.4315 0.1748  -0.2688 0.1259  774  LEU B CB  
20237 C CG  . LEU C 774  ? 1.9657 1.7367 1.4863 0.1966  -0.2704 0.1374  774  LEU B CG  
20238 C CD1 . LEU C 774  ? 1.9569 1.7533 1.4926 0.2195  -0.2527 0.1352  774  LEU B CD1 
20239 C CD2 . LEU C 774  ? 1.9939 1.7760 1.5208 0.1735  -0.2706 0.1507  774  LEU B CD2 
20240 N N   . TRP C 775  ? 1.9153 1.5579 1.3464 0.0851  -0.2772 0.1243  775  TRP B N   
20241 C CA  . TRP C 775  ? 1.9084 1.5237 1.3190 0.0513  -0.2646 0.1193  775  TRP B CA  
20242 C C   . TRP C 775  ? 1.9291 1.5509 1.3398 0.0296  -0.2639 0.1318  775  TRP B C   
20243 O O   . TRP C 775  ? 1.9330 1.5266 1.3202 -0.0019 -0.2599 0.1300  775  TRP B O   
20244 C CB  . TRP C 775  ? 1.9003 1.4728 1.2783 0.0308  -0.2742 0.1115  775  TRP B CB  
20245 C CG  . TRP C 775  ? 1.9182 1.4600 1.2728 -0.0029 -0.2591 0.1028  775  TRP B CG  
20246 C CD1 . TRP C 775  ? 1.9677 1.4839 1.2962 -0.0360 -0.2629 0.1077  775  TRP B CD1 
20247 C CD2 . TRP C 775  ? 1.9022 1.4350 1.2572 -0.0068 -0.2380 0.0866  775  TRP B CD2 
20248 N NE1 . TRP C 775  ? 1.9787 1.4703 1.2900 -0.0605 -0.2436 0.0952  775  TRP B NE1 
20249 C CE2 . TRP C 775  ? 1.9323 1.4351 1.2618 -0.0427 -0.2281 0.0819  775  TRP B CE2 
20250 C CE3 . TRP C 775  ? 1.8840 1.4315 1.2588 0.0166  -0.2270 0.0753  775  TRP B CE3 
20251 C CZ2 . TRP C 775  ? 1.9194 1.4091 1.2460 -0.0548 -0.2066 0.0657  775  TRP B CZ2 
20252 C CZ3 . TRP C 775  ? 1.8826 1.4170 1.2553 0.0045  -0.2078 0.0600  775  TRP B CZ3 
20253 C CH2 . TRP C 775  ? 1.8987 1.4056 1.2491 -0.0305 -0.1971 0.0549  775  TRP B CH2 
20254 N N   . GLU C 776  ? 1.9494 1.6084 1.3863 0.0461  -0.2669 0.1439  776  GLU B N   
20255 C CA  . GLU C 776  ? 2.0067 1.6781 1.4489 0.0279  -0.2671 0.1568  776  GLU B CA  
20256 C C   . GLU C 776  ? 1.9874 1.6656 1.4357 0.0190  -0.2437 0.1555  776  GLU B C   
20257 O O   . GLU C 776  ? 1.9537 1.6433 1.4143 0.0378  -0.2288 0.1485  776  GLU B O   
20258 C CB  . GLU C 776  ? 2.0516 1.7631 1.5226 0.0491  -0.2802 0.1701  776  GLU B CB  
20259 C CG  . GLU C 776  ? 2.0894 1.8275 1.5823 0.0878  -0.2792 0.1664  776  GLU B CG  
20260 C CD  . GLU C 776  ? 2.1588 1.9280 1.6748 0.1070  -0.2974 0.1769  776  GLU B CD  
20261 O OE1 . GLU C 776  ? 2.1680 1.9444 1.6914 0.1347  -0.3057 0.1724  776  GLU B OE1 
20262 O OE2 . GLU C 776  ? 2.2010 1.9873 1.7286 0.0942  -0.3040 0.1891  776  GLU B OE2 
20263 N N   . VAL C 777  ? 2.0142 1.6828 1.4522 -0.0097 -0.2416 0.1622  777  VAL B N   
20264 C CA  . VAL C 777  ? 2.0003 1.6791 1.4470 -0.0171 -0.2225 0.1645  777  VAL B CA  
20265 C C   . VAL C 777  ? 2.0826 1.8039 1.5582 -0.0040 -0.2269 0.1799  777  VAL B C   
20266 O O   . VAL C 777  ? 2.1110 1.8500 1.5977 0.0051  -0.2451 0.1881  777  VAL B O   
20267 C CB  . VAL C 777  ? 1.8892 1.5359 1.3096 -0.0550 -0.2178 0.1638  777  VAL B CB  
20268 C CG1 . VAL C 777  ? 1.8379 1.4995 1.2695 -0.0634 -0.2050 0.1718  777  VAL B CG1 
20269 C CG2 . VAL C 777  ? 1.8762 1.4862 1.2732 -0.0668 -0.2048 0.1464  777  VAL B CG2 
20270 N N   . HIS C 778  ? 2.1341 1.8718 1.6224 -0.0028 -0.2104 0.1838  778  HIS B N   
20271 C CA  . HIS C 778  ? 2.2200 1.9984 1.7352 0.0064  -0.2121 0.1984  778  HIS B CA  
20272 C C   . HIS C 778  ? 2.3605 2.1397 1.8760 -0.0094 -0.1954 0.2033  778  HIS B C   
20273 O O   . HIS C 778  ? 2.3667 2.1210 1.8676 -0.0156 -0.1803 0.1938  778  HIS B O   
20274 C CB  . HIS C 778  ? 2.1509 1.9617 1.6894 0.0435  -0.2086 0.1977  778  HIS B CB  
20275 C CG  . HIS C 778  ? 2.1285 1.9542 1.6776 0.0623  -0.2276 0.1989  778  HIS B CG  
20276 N ND1 . HIS C 778  ? 2.1166 1.9832 1.6937 0.0767  -0.2355 0.2100  778  HIS B ND1 
20277 C CD2 . HIS C 778  ? 2.1212 1.9262 1.6574 0.0704  -0.2398 0.1898  778  HIS B CD2 
20278 C CE1 . HIS C 778  ? 2.1114 1.9810 1.6926 0.0939  -0.2525 0.2074  778  HIS B CE1 
20279 N NE2 . HIS C 778  ? 2.1134 1.9444 1.6685 0.0901  -0.2558 0.1956  778  HIS B NE2 
20280 N N   . LEU C 779  ? 2.5133 2.3213 2.0467 -0.0156 -0.1985 0.2179  779  LEU B N   
20281 C CA  . LEU C 779  ? 2.6461 2.4573 2.1812 -0.0292 -0.1831 0.2243  779  LEU B CA  
20282 C C   . LEU C 779  ? 2.7258 2.5750 2.2859 -0.0052 -0.1718 0.2311  779  LEU B C   
20283 O O   . LEU C 779  ? 2.7518 2.6377 2.3353 -0.0026 -0.1769 0.2435  779  LEU B O   
20284 C CB  . LEU C 779  ? 2.6829 2.4972 2.2178 -0.0588 -0.1929 0.2364  779  LEU B CB  
20285 C CG  . LEU C 779  ? 2.6974 2.5141 2.2337 -0.0713 -0.1762 0.2428  779  LEU B CG  
20286 C CD1 . LEU C 779  ? 2.7132 2.4837 2.2197 -0.0865 -0.1630 0.2309  779  LEU B CD1 
20287 C CD2 . LEU C 779  ? 2.7209 2.5536 2.2663 -0.0960 -0.1855 0.2575  779  LEU B CD2 
20288 N N   . VAL C 780  ? 2.7836 2.6241 2.3389 0.0116  -0.1565 0.2230  780  VAL B N   
20289 C CA  . VAL C 780  ? 2.8347 2.7073 2.4084 0.0356  -0.1459 0.2288  780  VAL B CA  
20290 C C   . VAL C 780  ? 2.8321 2.7017 2.4023 0.0237  -0.1298 0.2359  780  VAL B C   
20291 O O   . VAL C 780  ? 2.8019 2.6427 2.3557 0.0228  -0.1185 0.2281  780  VAL B O   
20292 C CB  . VAL C 780  ? 2.9192 2.7884 2.4910 0.0665  -0.1420 0.2170  780  VAL B CB  
20293 C CG1 . VAL C 780  ? 2.9670 2.8653 2.5522 0.0894  -0.1302 0.2233  780  VAL B CG1 
20294 C CG2 . VAL C 780  ? 2.9493 2.8240 2.5258 0.0798  -0.1586 0.2115  780  VAL B CG2 
20295 N N   . PRO C 781  ? 2.8394 2.7390 2.4261 0.0144  -0.1292 0.2507  781  PRO B N   
20296 C CA  . PRO C 781  ? 2.8606 2.7602 2.4445 0.0038  -0.1141 0.2594  781  PRO B CA  
20297 C C   . PRO C 781  ? 2.8395 2.7597 2.4312 0.0325  -0.1021 0.2608  781  PRO B C   
20298 O O   . PRO C 781  ? 2.8510 2.8114 2.4639 0.0416  -0.1007 0.2707  781  PRO B O   
20299 C CB  . PRO C 781  ? 2.8846 2.8144 2.4872 -0.0161 -0.1204 0.2745  781  PRO B CB  
20300 C CG  . PRO C 781  ? 2.8959 2.8319 2.5061 -0.0195 -0.1408 0.2722  781  PRO B CG  
20301 C CD  . PRO C 781  ? 2.8737 2.8063 2.4822 0.0098  -0.1439 0.2601  781  PRO B CD  
20302 N N   . ARG C 782  ? 2.8234 2.7166 2.3983 0.0468  -0.0940 0.2505  782  ARG B N   
20303 C CA  . ARG C 782  ? 2.8220 2.7274 2.3978 0.0728  -0.0829 0.2516  782  ARG B CA  
20304 C C   . ARG C 782  ? 2.7583 2.6981 2.3510 0.1013  -0.0879 0.2503  782  ARG B C   
20305 O O   . ARG C 782  ? 2.7603 2.7066 2.3499 0.1252  -0.0801 0.2487  782  ARG B O   
20306 C CB  . ARG C 782  ? 2.9007 2.8170 2.4766 0.0615  -0.0700 0.2664  782  ARG B CB  
20307 C CG  . ARG C 782  ? 3.0008 2.8801 2.5577 0.0352  -0.0642 0.2679  782  ARG B CG  
20308 C CD  . ARG C 782  ? 3.0965 2.9833 2.6504 0.0261  -0.0513 0.2826  782  ARG B CD  
20309 N NE  . ARG C 782  ? 3.1592 3.0857 2.7343 0.0114  -0.0524 0.2969  782  ARG B NE  
20310 C CZ  . ARG C 782  ? 3.2187 3.1606 2.7961 0.0006  -0.0414 0.3112  782  ARG B CZ  
20311 N NH1 . ARG C 782  ? 3.2498 3.1669 2.8057 0.0029  -0.0293 0.3141  782  ARG B NH1 
20312 N NH2 . ARG C 782  ? 3.2305 3.2123 2.8319 -0.0130 -0.0432 0.3229  782  ARG B NH2 
20313 N N   . ARG C 783  ? 2.7057 2.6650 2.3143 0.0990  -0.1014 0.2508  783  ARG B N   
20314 C CA  . ARG C 783  ? 2.6486 2.6401 2.2749 0.1257  -0.1075 0.2491  783  ARG B CA  
20315 C C   . ARG C 783  ? 2.5817 2.5799 2.2197 0.1195  -0.1264 0.2473  783  ARG B C   
20316 O O   . ARG C 783  ? 2.5872 2.5812 2.2271 0.0927  -0.1335 0.2532  783  ARG B O   
20317 C CB  . ARG C 783  ? 2.6665 2.7020 2.3127 0.1332  -0.0975 0.2617  783  ARG B CB  
20318 C CG  . ARG C 783  ? 2.6846 2.7210 2.3197 0.1510  -0.0807 0.2628  783  ARG B CG  
20319 C CD  . ARG C 783  ? 2.7092 2.7829 2.3597 0.1450  -0.0679 0.2777  783  ARG B CD  
20320 N NE  . ARG C 783  ? 2.7429 2.7980 2.3723 0.1399  -0.0520 0.2832  783  ARG B NE  
20321 C CZ  . ARG C 783  ? 2.7580 2.8286 2.3911 0.1225  -0.0399 0.2971  783  ARG B CZ  
20322 N NH1 . ARG C 783  ? 2.7542 2.8630 2.4150 0.1082  -0.0416 0.3066  783  ARG B NH1 
20323 N NH2 . ARG C 783  ? 2.7724 2.8194 2.3817 0.1190  -0.0270 0.3017  783  ARG B NH2 
20324 N N   . LYS C 784  ? 2.5147 2.5209 2.1583 0.1442  -0.1355 0.2392  784  LYS B N   
20325 C CA  . LYS C 784  ? 2.4585 2.4759 2.1156 0.1445  -0.1547 0.2387  784  LYS B CA  
20326 C C   . LYS C 784  ? 2.4222 2.4417 2.0796 0.1765  -0.1607 0.2280  784  LYS B C   
20327 O O   . LYS C 784  ? 2.4277 2.4209 2.0661 0.1876  -0.1564 0.2172  784  LYS B O   
20328 C CB  . LYS C 784  ? 2.4456 2.4274 2.0860 0.1174  -0.1675 0.2353  784  LYS B CB  
20329 C CG  . LYS C 784  ? 2.4262 2.4182 2.0788 0.1139  -0.1897 0.2377  784  LYS B CG  
20330 C CD  . LYS C 784  ? 2.4136 2.3681 2.0450 0.0831  -0.2021 0.2359  784  LYS B CD  
20331 C CE  . LYS C 784  ? 2.3907 2.3542 2.0327 0.0784  -0.2264 0.2404  784  LYS B CE  
20332 N NZ  . LYS C 784  ? 2.3869 2.3112 2.0034 0.0471  -0.2390 0.2393  784  LYS B NZ  
20333 N N   . GLN C 785  ? 2.3910 2.4419 2.0710 0.1914  -0.1713 0.2305  785  GLN B N   
20334 C CA  . GLN C 785  ? 2.3553 2.4114 2.0373 0.2237  -0.1768 0.2210  785  GLN B CA  
20335 C C   . GLN C 785  ? 2.3117 2.3705 2.0046 0.2254  -0.1997 0.2198  785  GLN B C   
20336 O O   . GLN C 785  ? 2.2944 2.3791 2.0097 0.2150  -0.2077 0.2294  785  GLN B O   
20337 C CB  . GLN C 785  ? 2.3693 2.4667 2.0702 0.2473  -0.1630 0.2251  785  GLN B CB  
20338 C CG  . GLN C 785  ? 2.3981 2.5077 2.1058 0.2808  -0.1697 0.2163  785  GLN B CG  
20339 C CD  . GLN C 785  ? 2.4298 2.5844 2.1585 0.3012  -0.1553 0.2209  785  GLN B CD  
20340 O OE1 . GLN C 785  ? 2.4445 2.6332 2.1963 0.2895  -0.1484 0.2322  785  GLN B OE1 
20341 N NE2 . GLN C 785  ? 2.4456 2.6005 2.1658 0.3310  -0.1500 0.2117  785  GLN B NE2 
20342 N N   . LEU C 786  ? 2.3018 2.3336 1.9791 0.2381  -0.2114 0.2082  786  LEU B N   
20343 C CA  . LEU C 786  ? 2.3104 2.3330 1.9901 0.2342  -0.2352 0.2075  786  LEU B CA  
20344 C C   . LEU C 786  ? 2.3400 2.3546 2.0158 0.2630  -0.2467 0.1967  786  LEU B C   
20345 O O   . LEU C 786  ? 2.3700 2.3456 2.0212 0.2601  -0.2549 0.1872  786  LEU B O   
20346 C CB  . LEU C 786  ? 2.2835 2.2639 1.9381 0.2017  -0.2434 0.2065  786  LEU B CB  
20347 C CG  . LEU C 786  ? 2.2346 2.1759 1.8599 0.1946  -0.2324 0.1958  786  LEU B CG  
20348 C CD1 . LEU C 786  ? 2.2264 2.1277 1.8278 0.1628  -0.2407 0.1938  786  LEU B CD1 
20349 C CD2 . LEU C 786  ? 2.2180 2.1703 1.8453 0.1932  -0.2095 0.1988  786  LEU B CD2 
20350 N N   . GLN C 787  ? 2.3398 2.3916 2.0407 0.2898  -0.2472 0.1980  787  GLN B N   
20351 C CA  . GLN C 787  ? 2.3423 2.3889 2.0409 0.3201  -0.2573 0.1876  787  GLN B CA  
20352 C C   . GLN C 787  ? 2.3076 2.3173 1.9899 0.3135  -0.2826 0.1827  787  GLN B C   
20353 O O   . GLN C 787  ? 2.2959 2.2894 1.9724 0.2862  -0.2944 0.1887  787  GLN B O   
20354 C CB  . GLN C 787  ? 2.3971 2.4925 2.1295 0.3471  -0.2556 0.1905  787  GLN B CB  
20355 C CG  . GLN C 787  ? 2.4595 2.5863 2.2235 0.3361  -0.2674 0.2018  787  GLN B CG  
20356 C CD  . GLN C 787  ? 2.5127 2.6951 2.3148 0.3603  -0.2586 0.2046  787  GLN B CD  
20357 O OE1 . GLN C 787  ? 2.5408 2.7498 2.3729 0.3663  -0.2737 0.2084  787  GLN B OE1 
20358 N NE2 . GLN C 787  ? 2.5253 2.7253 2.3261 0.3744  -0.2343 0.2023  787  GLN B NE2 
20359 N N   . PHE C 788  ? 2.2774 2.2715 1.9494 0.3382  -0.2904 0.1716  788  PHE B N   
20360 C CA  . PHE C 788  ? 2.2338 2.1911 1.8878 0.3374  -0.3141 0.1657  788  PHE B CA  
20361 C C   . PHE C 788  ? 2.2049 2.1504 1.8479 0.3681  -0.3144 0.1525  788  PHE B C   
20362 O O   . PHE C 788  ? 2.2227 2.1745 1.8612 0.3796  -0.2958 0.1472  788  PHE B O   
20363 C CB  . PHE C 788  ? 2.2051 2.1181 1.8288 0.3033  -0.3172 0.1646  788  PHE B CB  
20364 C CG  . PHE C 788  ? 2.1570 2.0520 1.7617 0.2979  -0.2975 0.1566  788  PHE B CG  
20365 C CD1 . PHE C 788  ? 2.1460 2.0137 1.7309 0.3112  -0.2989 0.1434  788  PHE B CD1 
20366 C CD2 . PHE C 788  ? 2.1209 2.0248 1.7276 0.2790  -0.2789 0.1621  788  PHE B CD2 
20367 C CE1 . PHE C 788  ? 2.1092 1.9619 1.6800 0.3067  -0.2826 0.1357  788  PHE B CE1 
20368 C CE2 . PHE C 788  ? 2.0915 1.9780 1.6825 0.2754  -0.2627 0.1543  788  PHE B CE2 
20369 C CZ  . PHE C 788  ? 2.0853 1.9476 1.6598 0.2895  -0.2649 0.1411  788  PHE B CZ  
20370 N N   . ALA C 789  ? 2.1487 2.0761 1.7861 0.3820  -0.3359 0.1472  789  ALA B N   
20371 C CA  . ALA C 789  ? 2.0990 2.0083 1.7210 0.4079  -0.3371 0.1339  789  ALA B CA  
20372 C C   . ALA C 789  ? 2.0642 1.9212 1.6509 0.3894  -0.3441 0.1258  789  ALA B C   
20373 O O   . ALA C 789  ? 2.0651 1.8944 1.6382 0.3659  -0.3594 0.1292  789  ALA B O   
20374 C CB  . ALA C 789  ? 2.1153 2.0334 1.7506 0.4370  -0.3550 0.1309  789  ALA B CB  
20375 N N   . LEU C 790  ? 2.0474 1.8906 1.6186 0.3987  -0.3329 0.1151  790  LEU B N   
20376 C CA  . LEU C 790  ? 2.0508 1.8489 1.5925 0.3794  -0.3369 0.1067  790  LEU B CA  
20377 C C   . LEU C 790  ? 2.1127 1.8762 1.6362 0.3878  -0.3597 0.0992  790  LEU B C   
20378 O O   . LEU C 790  ? 2.0883 1.8620 1.6205 0.4161  -0.3699 0.0972  790  LEU B O   
20379 C CB  . LEU C 790  ? 2.0078 1.8036 1.5417 0.3815  -0.3174 0.0984  790  LEU B CB  
20380 C CG  . LEU C 790  ? 1.9574 1.7916 1.5088 0.4034  -0.2989 0.1006  790  LEU B CG  
20381 C CD1 . LEU C 790  ? 1.9724 1.8112 1.5225 0.4391  -0.3031 0.0917  790  LEU B CD1 
20382 C CD2 . LEU C 790  ? 1.9155 1.7464 1.4606 0.3921  -0.2803 0.0979  790  LEU B CD2 
20383 N N   . PRO C 791  ? 2.2038 1.9251 1.7010 0.3627  -0.3672 0.0948  791  PRO B N   
20384 C CA  . PRO C 791  ? 2.3134 1.9958 1.7891 0.3607  -0.3913 0.0912  791  PRO B CA  
20385 C C   . PRO C 791  ? 2.4273 2.0982 1.8953 0.3903  -0.3982 0.0794  791  PRO B C   
20386 O O   . PRO C 791  ? 2.4638 2.1367 1.9290 0.3992  -0.3845 0.0701  791  PRO B O   
20387 C CB  . PRO C 791  ? 2.2993 1.9427 1.7479 0.3254  -0.3891 0.0871  791  PRO B CB  
20388 C CG  . PRO C 791  ? 2.2489 1.9133 1.7085 0.3082  -0.3656 0.0901  791  PRO B CG  
20389 C CD  . PRO C 791  ? 2.2047 1.9114 1.6897 0.3364  -0.3514 0.0910  791  PRO B CD  
20390 N N   . ASP C 792  ? 2.5062 2.1627 1.9698 0.4053  -0.4206 0.0796  792  ASP B N   
20391 C CA  . ASP C 792  ? 2.6043 2.2404 2.0548 0.4306  -0.4304 0.0676  792  ASP B CA  
20392 C C   . ASP C 792  ? 2.5584 2.1521 1.9787 0.4096  -0.4299 0.0576  792  ASP B C   
20393 O O   . ASP C 792  ? 2.5591 2.1128 1.9557 0.3896  -0.4462 0.0579  792  ASP B O   
20394 C CB  . ASP C 792  ? 2.7939 2.4131 2.2410 0.4447  -0.4577 0.0703  792  ASP B CB  
20395 C CG  . ASP C 792  ? 2.9798 2.5798 2.4152 0.4757  -0.4685 0.0578  792  ASP B CG  
20396 O OD1 . ASP C 792  ? 3.0804 2.6683 2.5020 0.4790  -0.4588 0.0467  792  ASP B OD1 
20397 O OD2 . ASP C 792  ? 3.0623 2.6587 2.5026 0.4971  -0.4879 0.0589  792  ASP B OD2 
20398 N N   . SER C 793  ? 2.4955 2.0976 1.9169 0.4131  -0.4118 0.0489  793  SER B N   
20399 C CA  . SER C 793  ? 2.4360 2.0020 1.8337 0.3962  -0.4116 0.0376  793  SER B CA  
20400 C C   . SER C 793  ? 2.3329 1.9133 1.7367 0.4048  -0.3932 0.0279  793  SER B C   
20401 O O   . SER C 793  ? 2.3075 1.9189 1.7290 0.4028  -0.3746 0.0322  793  SER B O   
20402 C CB  . SER C 793  ? 2.4202 1.9633 1.8044 0.3551  -0.4102 0.0415  793  SER B CB  
20403 O OG  . SER C 793  ? 2.3998 1.9153 1.7667 0.3391  -0.4058 0.0294  793  SER B OG  
20404 N N   . LEU C 794  ? 2.2682 1.8230 1.6556 0.4132  -0.4002 0.0150  794  LEU B N   
20405 C CA  . LEU C 794  ? 2.1797 1.7407 1.5694 0.4196  -0.3874 0.0041  794  LEU B CA  
20406 C C   . LEU C 794  ? 2.1549 1.7147 1.5479 0.3876  -0.3726 0.0031  794  LEU B C   
20407 O O   . LEU C 794  ? 2.1993 1.7292 1.5777 0.3659  -0.3765 -0.0049 794  LEU B O   
20408 C CB  . LEU C 794  ? 2.1789 1.7051 1.5475 0.4268  -0.4015 -0.0097 794  LEU B CB  
20409 C CG  . LEU C 794  ? 2.2127 1.7347 1.5740 0.4628  -0.4134 -0.0163 794  LEU B CG  
20410 C CD1 . LEU C 794  ? 2.2196 1.7599 1.5906 0.4848  -0.4198 -0.0066 794  LEU B CD1 
20411 C CD2 . LEU C 794  ? 2.2545 1.7300 1.5894 0.4578  -0.4320 -0.0275 794  LEU B CD2 
20412 N N   . THR C 795  ? 2.0907 1.6823 1.5026 0.3845  -0.3551 0.0104  795  THR B N   
20413 C CA  . THR C 795  ? 2.0285 1.6207 1.4457 0.3566  -0.3397 0.0089  795  THR B CA  
20414 C C   . THR C 795  ? 1.9599 1.5871 1.3971 0.3675  -0.3210 0.0124  795  THR B C   
20415 O O   . THR C 795  ? 1.9183 1.5721 1.3663 0.3847  -0.3178 0.0222  795  THR B O   
20416 C CB  . THR C 795  ? 2.7395 2.3197 2.1508 0.3241  -0.3405 0.0178  795  THR B CB  
20417 O OG1 . THR C 795  ? 2.7476 2.3374 2.1613 0.3337  -0.3513 0.0301  795  THR B OG1 
20418 C CG2 . THR C 795  ? 2.7602 2.2993 2.1486 0.2995  -0.3505 0.0098  795  THR B CG2 
20419 N N   . THR C 796  ? 1.9511 1.5781 1.3935 0.3581  -0.3092 0.0043  796  THR B N   
20420 C CA  . THR C 796  ? 1.9237 1.5786 1.3824 0.3639  -0.2922 0.0091  796  THR B CA  
20421 C C   . THR C 796  ? 1.9433 1.6029 1.4088 0.3357  -0.2809 0.0175  796  THR B C   
20422 O O   . THR C 796  ? 1.9677 1.6150 1.4337 0.3129  -0.2733 0.0109  796  THR B O   
20423 C CB  . THR C 796  ? 1.8852 1.5390 1.3485 0.3694  -0.2857 -0.0029 796  THR B CB  
20424 O OG1 . THR C 796  ? 1.9057 1.5551 1.3611 0.3963  -0.2964 -0.0108 796  THR B OG1 
20425 C CG2 . THR C 796  ? 1.8492 1.5283 1.3265 0.3746  -0.2696 0.0040  796  THR B CG2 
20426 N N   . TRP C 797  ? 1.9412 1.6193 1.4124 0.3373  -0.2795 0.0315  797  TRP B N   
20427 C CA  . TRP C 797  ? 1.9095 1.5901 1.3844 0.3099  -0.2713 0.0406  797  TRP B CA  
20428 C C   . TRP C 797  ? 1.8267 1.5221 1.3137 0.3059  -0.2528 0.0410  797  TRP B C   
20429 O O   . TRP C 797  ? 1.8116 1.5323 1.3088 0.3224  -0.2455 0.0489  797  TRP B O   
20430 C CB  . TRP C 797  ? 1.9514 1.6509 1.4323 0.3144  -0.2764 0.0556  797  TRP B CB  
20431 C CG  . TRP C 797  ? 2.0304 1.7140 1.5005 0.3149  -0.2961 0.0574  797  TRP B CG  
20432 C CD1 . TRP C 797  ? 2.0761 1.7737 1.5514 0.3389  -0.3074 0.0627  797  TRP B CD1 
20433 C CD2 . TRP C 797  ? 2.0923 1.7412 1.5433 0.2902  -0.3070 0.0538  797  TRP B CD2 
20434 N NE1 . TRP C 797  ? 2.1285 1.8012 1.5900 0.3319  -0.3265 0.0629  797  TRP B NE1 
20435 C CE2 . TRP C 797  ? 2.1385 1.7797 1.5829 0.3012  -0.3268 0.0580  797  TRP B CE2 
20436 C CE3 . TRP C 797  ? 2.1100 1.7330 1.5484 0.2598  -0.3015 0.0470  797  TRP B CE3 
20437 C CZ2 . TRP C 797  ? 2.1764 1.7819 1.5988 0.2821  -0.3425 0.0569  797  TRP B CZ2 
20438 C CZ3 . TRP C 797  ? 2.1550 1.7446 1.5716 0.2398  -0.3150 0.0455  797  TRP B CZ3 
20439 C CH2 . TRP C 797  ? 2.1834 1.7629 1.5906 0.2506  -0.3360 0.0510  797  TRP B CH2 
20440 N N   . GLU C 798  ? 1.7807 1.4599 1.2664 0.2844  -0.2449 0.0323  798  GLU B N   
20441 C CA  . GLU C 798  ? 1.7430 1.4341 1.2401 0.2782  -0.2282 0.0343  798  GLU B CA  
20442 C C   . GLU C 798  ? 1.7283 1.4234 1.2254 0.2554  -0.2225 0.0468  798  GLU B C   
20443 O O   . GLU C 798  ? 1.7281 1.4035 1.2161 0.2281  -0.2225 0.0446  798  GLU B O   
20444 C CB  . GLU C 798  ? 1.7419 1.4172 1.2417 0.2653  -0.2206 0.0195  798  GLU B CB  
20445 C CG  . GLU C 798  ? 1.7464 1.4288 1.2561 0.2535  -0.2042 0.0223  798  GLU B CG  
20446 C CD  . GLU C 798  ? 1.7777 1.4487 1.2952 0.2454  -0.1963 0.0066  798  GLU B CD  
20447 O OE1 . GLU C 798  ? 1.7997 1.4622 1.3174 0.2530  -0.2037 -0.0060 798  GLU B OE1 
20448 O OE2 . GLU C 798  ? 1.7811 1.4520 1.3057 0.2315  -0.1830 0.0063  798  GLU B OE2 
20449 N N   . ILE C 799  ? 1.7352 1.4547 1.2411 0.2651  -0.2176 0.0598  799  ILE B N   
20450 C CA  . ILE C 799  ? 1.7488 1.4736 1.2556 0.2436  -0.2138 0.0722  799  ILE B CA  
20451 C C   . ILE C 799  ? 1.7725 1.5005 1.2855 0.2310  -0.1966 0.0741  799  ILE B C   
20452 O O   . ILE C 799  ? 1.7574 1.5059 1.2793 0.2435  -0.1886 0.0821  799  ILE B O   
20453 C CB  . ILE C 799  ? 1.5941 1.3430 1.1075 0.2577  -0.2223 0.0860  799  ILE B CB  
20454 C CG1 . ILE C 799  ? 1.5910 1.3558 1.1120 0.2416  -0.2155 0.1004  799  ILE B CG1 
20455 C CG2 . ILE C 799  ? 1.5876 1.3584 1.1092 0.2910  -0.2207 0.0861  799  ILE B CG2 
20456 C CD1 . ILE C 799  ? 1.5885 1.3854 1.1232 0.2603  -0.2203 0.1125  799  ILE B CD1 
20457 N N   . GLN C 800  ? 1.7989 1.5043 1.3054 0.2062  -0.1907 0.0657  800  GLN B N   
20458 C CA  . GLN C 800  ? 1.8235 1.5258 1.3339 0.1909  -0.1750 0.0656  800  GLN B CA  
20459 C C   . GLN C 800  ? 1.8249 1.5315 1.3323 0.1699  -0.1724 0.0798  800  GLN B C   
20460 O O   . GLN C 800  ? 1.8266 1.5361 1.3288 0.1640  -0.1837 0.0882  800  GLN B O   
20461 C CB  . GLN C 800  ? 1.8387 1.5159 1.3449 0.1728  -0.1686 0.0491  800  GLN B CB  
20462 C CG  . GLN C 800  ? 1.8763 1.5306 1.3657 0.1466  -0.1749 0.0457  800  GLN B CG  
20463 C CD  . GLN C 800  ? 1.8959 1.5324 1.3811 0.1454  -0.1784 0.0288  800  GLN B CD  
20464 O OE1 . GLN C 800  ? 1.9080 1.5521 1.4007 0.1695  -0.1847 0.0231  800  GLN B OE1 
20465 N NE2 . GLN C 800  ? 1.8958 1.5079 1.3675 0.1163  -0.1743 0.0209  800  GLN B NE2 
20466 N N   . GLY C 801  ? 1.8210 1.5272 1.3316 0.1589  -0.1587 0.0824  801  GLY B N   
20467 C CA  . GLY C 801  ? 1.8267 1.5367 1.3343 0.1385  -0.1559 0.0958  801  GLY B CA  
20468 C C   . GLY C 801  ? 1.8270 1.5273 1.3346 0.1236  -0.1401 0.0947  801  GLY B C   
20469 O O   . GLY C 801  ? 1.8080 1.5218 1.3236 0.1350  -0.1328 0.1015  801  GLY B O   
20470 N N   . ILE C 802  ? 1.8747 1.5493 1.3711 0.0976  -0.1347 0.0859  802  ILE B N   
20471 C CA  . ILE C 802  ? 1.8896 1.5505 1.3836 0.0808  -0.1200 0.0834  802  ILE B CA  
20472 C C   . ILE C 802  ? 1.8923 1.5602 1.3821 0.0649  -0.1197 0.1003  802  ILE B C   
20473 O O   . ILE C 802  ? 1.9469 1.6253 1.4338 0.0597  -0.1315 0.1113  802  ILE B O   
20474 C CB  . ILE C 802  ? 1.9109 1.5424 1.3925 0.0562  -0.1141 0.0680  802  ILE B CB  
20475 C CG1 . ILE C 802  ? 1.9349 1.5488 1.4018 0.0249  -0.1067 0.0720  802  ILE B CG1 
20476 C CG2 . ILE C 802  ? 1.9316 1.5557 1.4022 0.0505  -0.1268 0.0647  802  ILE B CG2 
20477 C CD1 . ILE C 802  ? 1.9455 1.5441 1.4150 0.0179  -0.0895 0.0615  802  ILE B CD1 
20478 N N   . GLY C 803  ? 1.8451 1.5066 1.3352 0.0570  -0.1073 0.1022  803  GLY B N   
20479 C CA  . GLY C 803  ? 1.8327 1.4958 1.3167 0.0367  -0.1061 0.1165  803  GLY B CA  
20480 C C   . GLY C 803  ? 1.8676 1.5026 1.3399 0.0124  -0.0930 0.1100  803  GLY B C   
20481 O O   . GLY C 803  ? 1.8432 1.4644 1.3187 0.0186  -0.0822 0.0971  803  GLY B O   
20482 N N   . ILE C 804  ? 1.9304 1.5557 1.3893 -0.0152 -0.0945 0.1181  804  ILE B N   
20483 C CA  . ILE C 804  ? 1.9326 1.5308 1.3789 -0.0376 -0.0817 0.1128  804  ILE B CA  
20484 C C   . ILE C 804  ? 1.9657 1.5670 1.4060 -0.0559 -0.0831 0.1293  804  ILE B C   
20485 O O   . ILE C 804  ? 1.9178 1.5316 1.3555 -0.0664 -0.0956 0.1414  804  ILE B O   
20486 C CB  . ILE C 804  ? 1.8750 1.4421 1.3027 -0.0608 -0.0774 0.0971  804  ILE B CB  
20487 C CG1 . ILE C 804  ? 1.8478 1.4120 1.2597 -0.0800 -0.0915 0.1039  804  ILE B CG1 
20488 C CG2 . ILE C 804  ? 1.8261 1.3899 1.2625 -0.0441 -0.0732 0.0792  804  ILE B CG2 
20489 C CD1 . ILE C 804  ? 1.8409 1.3765 1.2339 -0.0972 -0.0882 0.0873  804  ILE B CD1 
20490 N N   . SER C 805  ? 2.0698 1.6594 1.5091 -0.0587 -0.0709 0.1293  805  SER B N   
20491 C CA  . SER C 805  ? 2.1211 1.7092 1.5539 -0.0771 -0.0695 0.1436  805  SER B CA  
20492 C C   . SER C 805  ? 2.2261 1.7824 1.6480 -0.0879 -0.0547 0.1350  805  SER B C   
20493 O O   . SER C 805  ? 2.2103 1.7454 1.6292 -0.0854 -0.0458 0.1170  805  SER B O   
20494 C CB  . SER C 805  ? 2.1411 1.7636 1.5912 -0.0592 -0.0736 0.1612  805  SER B CB  
20495 O OG  . SER C 805  ? 2.1324 1.7810 1.5888 -0.0634 -0.0878 0.1737  805  SER B OG  
20496 N N   . ASN C 806  ? 2.3033 1.8565 1.7203 -0.1001 -0.0519 0.1475  806  ASN B N   
20497 C CA  . ASN C 806  ? 2.4391 1.9569 1.8412 -0.1156 -0.0394 0.1402  806  ASN B CA  
20498 C C   . ASN C 806  ? 2.4740 1.9810 1.8850 -0.0922 -0.0286 0.1294  806  ASN B C   
20499 O O   . ASN C 806  ? 2.4867 1.9635 1.8880 -0.1004 -0.0181 0.1216  806  ASN B O   
20500 C CB  . ASN C 806  ? 2.5263 2.0419 1.9191 -0.1372 -0.0409 0.1572  806  ASN B CB  
20501 C CG  . ASN C 806  ? 2.6137 2.1284 1.9931 -0.1665 -0.0513 0.1636  806  ASN B CG  
20502 O OD1 . ASN C 806  ? 2.6248 2.1683 2.0134 -0.1695 -0.0628 0.1802  806  ASN B OD1 
20503 N ND2 . ASN C 806  ? 2.6630 2.1446 2.0207 -0.1880 -0.0475 0.1498  806  ASN B ND2 
20504 N N   . THR C 807  ? 2.4692 1.9998 1.8985 -0.0624 -0.0321 0.1286  807  THR B N   
20505 C CA  . THR C 807  ? 2.4553 1.9767 1.8941 -0.0384 -0.0250 0.1177  807  THR B CA  
20506 C C   . THR C 807  ? 2.3935 1.9036 1.8376 -0.0336 -0.0210 0.0947  807  THR B C   
20507 O O   . THR C 807  ? 2.4308 1.9217 1.8798 -0.0250 -0.0122 0.0800  807  THR B O   
20508 C CB  . THR C 807  ? 2.4736 2.0246 1.9269 -0.0091 -0.0312 0.1289  807  THR B CB  
20509 O OG1 . THR C 807  ? 2.4693 2.0488 1.9311 -0.0016 -0.0413 0.1316  807  THR B OG1 
20510 C CG2 . THR C 807  ? 2.4816 2.0402 1.9293 -0.0153 -0.0313 0.1499  807  THR B CG2 
20511 N N   . GLY C 808  ? 2.2845 1.8063 1.7279 -0.0398 -0.0278 0.0919  808  GLY B N   
20512 C CA  . GLY C 808  ? 2.1977 1.7141 1.6467 -0.0355 -0.0252 0.0719  808  GLY B CA  
20513 C C   . GLY C 808  ? 2.1421 1.6845 1.5999 -0.0214 -0.0375 0.0740  808  GLY B C   
20514 O O   . GLY C 808  ? 2.1071 1.6699 1.5634 -0.0216 -0.0485 0.0903  808  GLY B O   
20515 N N   . ILE C 809  ? 2.1189 1.6608 1.5872 -0.0090 -0.0357 0.0569  809  ILE B N   
20516 C CA  . ILE C 809  ? 2.0704 1.6326 1.5465 0.0055  -0.0470 0.0564  809  ILE B CA  
20517 C C   . ILE C 809  ? 2.0587 1.6418 1.5538 0.0404  -0.0520 0.0582  809  ILE B C   
20518 O O   . ILE C 809  ? 2.0923 1.6686 1.5991 0.0544  -0.0454 0.0470  809  ILE B O   
20519 C CB  . ILE C 809  ? 2.0273 1.5756 1.5027 -0.0029 -0.0423 0.0358  809  ILE B CB  
20520 C CG1 . ILE C 809  ? 1.9801 1.5472 1.4666 0.0175  -0.0533 0.0328  809  ILE B CG1 
20521 C CG2 . ILE C 809  ? 2.0127 1.5460 1.4998 0.0017  -0.0279 0.0175  809  ILE B CG2 
20522 C CD1 . ILE C 809  ? 1.9660 1.5217 1.4564 0.0126  -0.0475 0.0113  809  ILE B CD1 
20523 N N   . CYS C 810  ? 2.0164 1.6241 1.5145 0.0548  -0.0641 0.0712  810  CYS B N   
20524 C CA  . CYS C 810  ? 1.9690 1.5961 1.4810 0.0877  -0.0695 0.0734  810  CYS B CA  
20525 C C   . CYS C 810  ? 1.9688 1.6156 1.4843 0.1019  -0.0823 0.0751  810  CYS B C   
20526 O O   . CYS C 810  ? 1.9463 1.6125 1.4601 0.1060  -0.0899 0.0902  810  CYS B O   
20527 C CB  . CYS C 810  ? 1.9501 1.5882 1.4616 0.0970  -0.0683 0.0909  810  CYS B CB  
20528 S SG  . CYS C 810  ? 2.3413 1.9997 1.8630 0.1362  -0.0741 0.0950  810  CYS B SG  
20529 N N   . VAL C 811  ? 1.9835 1.6254 1.5052 0.1096  -0.0844 0.0588  811  VAL B N   
20530 C CA  . VAL C 811  ? 1.9803 1.6369 1.5056 0.1272  -0.0966 0.0576  811  VAL B CA  
20531 C C   . VAL C 811  ? 1.9684 1.6452 1.5010 0.1572  -0.1014 0.0665  811  VAL B C   
20532 O O   . VAL C 811  ? 1.9778 1.6520 1.5163 0.1704  -0.0962 0.0644  811  VAL B O   
20533 C CB  . VAL C 811  ? 1.9682 1.6150 1.5013 0.1320  -0.0963 0.0374  811  VAL B CB  
20534 C CG1 . VAL C 811  ? 1.9851 1.6435 1.5187 0.1475  -0.1099 0.0365  811  VAL B CG1 
20535 C CG2 . VAL C 811  ? 1.9729 1.5976 1.4989 0.1024  -0.0875 0.0255  811  VAL B CG2 
20536 N N   . ALA C 812  ? 1.9408 1.6363 1.4718 0.1686  -0.1116 0.0760  812  ALA B N   
20537 C CA  . ALA C 812  ? 1.9304 1.6449 1.4654 0.1963  -0.1147 0.0841  812  ALA B CA  
20538 C C   . ALA C 812  ? 1.8910 1.6081 1.4303 0.2197  -0.1233 0.0727  812  ALA B C   
20539 O O   . ALA C 812  ? 1.9003 1.6082 1.4400 0.2141  -0.1286 0.0607  812  ALA B O   
20540 C CB  . ALA C 812  ? 1.9372 1.6739 1.4702 0.1973  -0.1186 0.1016  812  ALA B CB  
20541 N N   . ASP C 813  ? 1.8781 1.6065 1.4184 0.2450  -0.1247 0.0769  813  ASP B N   
20542 C CA  . ASP C 813  ? 1.8509 1.5820 1.3930 0.2691  -0.1338 0.0673  813  ASP B CA  
20543 C C   . ASP C 813  ? 1.7848 1.5266 1.3236 0.2709  -0.1436 0.0701  813  ASP B C   
20544 O O   . ASP C 813  ? 1.7685 1.5268 1.3050 0.2706  -0.1439 0.0839  813  ASP B O   
20545 C CB  . ASP C 813  ? 1.9044 1.6436 1.4431 0.2941  -0.1331 0.0736  813  ASP B CB  
20546 C CG  . ASP C 813  ? 1.9500 1.6746 1.4906 0.2920  -0.1251 0.0718  813  ASP B CG  
20547 O OD1 . ASP C 813  ? 1.9516 1.6622 1.5008 0.2942  -0.1269 0.0564  813  ASP B OD1 
20548 O OD2 . ASP C 813  ? 1.9602 1.6873 1.4947 0.2880  -0.1174 0.0855  813  ASP B OD2 
20549 N N   . THR C 814  ? 1.7621 1.4938 1.3018 0.2715  -0.1517 0.0563  814  THR B N   
20550 C CA  . THR C 814  ? 1.7419 1.4765 1.2767 0.2716  -0.1628 0.0565  814  THR B CA  
20551 C C   . THR C 814  ? 1.7517 1.5070 1.2841 0.2960  -0.1686 0.0663  814  THR B C   
20552 O O   . THR C 814  ? 1.7440 1.5105 1.2768 0.3112  -0.1630 0.0726  814  THR B O   
20553 C CB  . THR C 814  ? 1.7418 1.4620 1.2770 0.2758  -0.1707 0.0393  814  THR B CB  
20554 O OG1 . THR C 814  ? 1.7380 1.4624 1.2667 0.2886  -0.1837 0.0401  814  THR B OG1 
20555 C CG2 . THR C 814  ? 1.7320 1.4517 1.2738 0.2959  -0.1697 0.0303  814  THR B CG2 
20556 N N   . VAL C 815  ? 1.7700 1.5293 1.2991 0.3000  -0.1795 0.0674  815  VAL B N   
20557 C CA  . VAL C 815  ? 1.8012 1.5789 1.3288 0.3271  -0.1851 0.0726  815  VAL B CA  
20558 C C   . VAL C 815  ? 1.8183 1.5890 1.3406 0.3362  -0.2002 0.0652  815  VAL B C   
20559 O O   . VAL C 815  ? 1.8471 1.6219 1.3693 0.3301  -0.2073 0.0712  815  VAL B O   
20560 C CB  . VAL C 815  ? 1.8163 1.6191 1.3490 0.3268  -0.1796 0.0897  815  VAL B CB  
20561 C CG1 . VAL C 815  ? 1.8186 1.6402 1.3516 0.3518  -0.1868 0.0928  815  VAL B CG1 
20562 C CG2 . VAL C 815  ? 1.8224 1.6336 1.3565 0.3276  -0.1654 0.0975  815  VAL B CG2 
20563 N N   . LYS C 816  ? 1.8117 1.5704 1.3294 0.3510  -0.2062 0.0520  816  LYS B N   
20564 C CA  . LYS C 816  ? 1.8392 1.5870 1.3495 0.3602  -0.2211 0.0437  816  LYS B CA  
20565 C C   . LYS C 816  ? 1.8991 1.6659 1.4083 0.3798  -0.2263 0.0529  816  LYS B C   
20566 O O   . LYS C 816  ? 1.8905 1.6789 1.4033 0.3948  -0.2181 0.0612  816  LYS B O   
20567 C CB  . LYS C 816  ? 2.1811 1.9163 1.6871 0.3761  -0.2265 0.0288  816  LYS B CB  
20568 C CG  . LYS C 816  ? 2.4101 2.1256 1.9206 0.3572  -0.2247 0.0154  816  LYS B CG  
20569 C CD  . LYS C 816  ? 2.3839 2.1045 1.9044 0.3519  -0.2111 0.0164  816  LYS B CD  
20570 C CE  . LYS C 816  ? 2.3442 2.0493 1.8738 0.3368  -0.2084 0.0015  816  LYS B CE  
20571 N NZ  . LYS C 816  ? 2.3098 2.0193 1.8495 0.3358  -0.1966 0.0028  816  LYS B NZ  
20572 N N   . ALA C 817  ? 1.9985 1.7568 1.5030 0.3796  -0.2397 0.0512  817  ALA B N   
20573 C CA  . ALA C 817  ? 2.0792 1.8555 1.5858 0.3991  -0.2458 0.0584  817  ALA B CA  
20574 C C   . ALA C 817  ? 2.0951 1.8522 1.5912 0.4085  -0.2636 0.0497  817  ALA B C   
20575 O O   . ALA C 817  ? 2.1239 1.8785 1.6203 0.4028  -0.2740 0.0545  817  ALA B O   
20576 C CB  . ALA C 817  ? 2.1175 1.9109 1.6351 0.3837  -0.2428 0.0727  817  ALA B CB  
20577 N N   . LYS C 818  ? 2.0932 1.8351 1.5792 0.4227  -0.2684 0.0369  818  LYS B N   
20578 C CA  . LYS C 818  ? 2.1153 1.8358 1.5889 0.4323  -0.2856 0.0277  818  LYS B CA  
20579 C C   . LYS C 818  ? 2.1016 1.8374 1.5771 0.4550  -0.2925 0.0336  818  LYS B C   
20580 O O   . LYS C 818  ? 2.0653 1.8261 1.5466 0.4766  -0.2839 0.0376  818  LYS B O   
20581 C CB  . LYS C 818  ? 2.1808 1.8865 1.6443 0.4472  -0.2893 0.0134  818  LYS B CB  
20582 C CG  . LYS C 818  ? 2.2547 1.9733 1.7127 0.4819  -0.2899 0.0115  818  LYS B CG  
20583 C CD  . LYS C 818  ? 2.3364 2.0339 1.7806 0.4950  -0.2989 -0.0037 818  LYS B CD  
20584 C CE  . LYS C 818  ? 2.3989 2.1093 1.8352 0.5268  -0.2956 -0.0053 818  LYS B CE  
20585 N NZ  . LYS C 818  ? 2.4278 2.1191 1.8508 0.5380  -0.3036 -0.0194 818  LYS B NZ  
20586 N N   . VAL C 819  ? 2.1152 1.8357 1.5859 0.4496  -0.3077 0.0342  819  VAL B N   
20587 C CA  . VAL C 819  ? 2.1202 1.8503 1.5929 0.4739  -0.3177 0.0365  819  VAL B CA  
20588 C C   . VAL C 819  ? 2.1572 1.8564 1.6109 0.4871  -0.3335 0.0233  819  VAL B C   
20589 O O   . VAL C 819  ? 2.1587 1.8294 1.5997 0.4707  -0.3383 0.0148  819  VAL B O   
20590 C CB  . VAL C 819  ? 2.1048 1.8389 1.5863 0.4606  -0.3265 0.0474  819  VAL B CB  
20591 C CG1 . VAL C 819  ? 2.0711 1.8401 1.5731 0.4514  -0.3113 0.0608  819  VAL B CG1 
20592 C CG2 . VAL C 819  ? 2.0974 1.7952 1.5641 0.4302  -0.3378 0.0453  819  VAL B CG2 
20593 N N   . PHE C 820  ? 2.2030 1.9081 1.6552 0.5164  -0.3410 0.0209  820  PHE B N   
20594 C CA  . PHE C 820  ? 2.3005 1.9744 1.7329 0.5305  -0.3569 0.0081  820  PHE B CA  
20595 C C   . PHE C 820  ? 2.3088 1.9932 1.7405 0.5670  -0.3618 0.0047  820  PHE B C   
20596 O O   . PHE C 820  ? 2.2709 1.9865 1.7123 0.5862  -0.3475 0.0071  820  PHE B O   
20597 C CB  . PHE C 820  ? 2.4077 2.0659 1.8281 0.5268  -0.3525 -0.0031 820  PHE B CB  
20598 C CG  . PHE C 820  ? 2.5864 2.2228 1.9881 0.5497  -0.3645 -0.0164 820  PHE B CG  
20599 C CD1 . PHE C 820  ? 2.6648 2.3156 2.0630 0.5770  -0.3571 -0.0213 820  PHE B CD1 
20600 C CD2 . PHE C 820  ? 2.6772 2.2763 2.0623 0.5435  -0.3836 -0.0237 820  PHE B CD2 
20601 C CE1 . PHE C 820  ? 2.7430 2.3716 2.1217 0.5980  -0.3687 -0.0340 820  PHE B CE1 
20602 C CE2 . PHE C 820  ? 2.7477 2.3243 2.1143 0.5640  -0.3955 -0.0361 820  PHE B CE2 
20603 C CZ  . PHE C 820  ? 2.7761 2.3676 2.1396 0.5917  -0.3883 -0.0416 820  PHE B CZ  
20604 N N   . LYS C 821  ? 2.3803 2.0367 1.7991 0.5758  -0.3818 -0.0013 821  LYS B N   
20605 C CA  . LYS C 821  ? 2.4395 2.0995 1.8556 0.6110  -0.3887 -0.0069 821  LYS B CA  
20606 C C   . LYS C 821  ? 2.5235 2.1562 1.9150 0.6270  -0.3945 -0.0224 821  LYS B C   
20607 O O   . LYS C 821  ? 2.5241 2.1211 1.8980 0.6105  -0.4056 -0.0294 821  LYS B O   
20608 C CB  . LYS C 821  ? 2.4203 2.0643 1.8373 0.6131  -0.4090 -0.0040 821  LYS B CB  
20609 C CG  . LYS C 821  ? 2.3995 2.0446 1.8153 0.6505  -0.4180 -0.0110 821  LYS B CG  
20610 C CD  . LYS C 821  ? 2.3503 2.0361 1.7966 0.6646  -0.4138 -0.0012 821  LYS B CD  
20611 C CE  . LYS C 821  ? 2.3543 2.0308 1.8002 0.6968  -0.4303 -0.0082 821  LYS B CE  
20612 N NZ  . LYS C 821  ? 2.3340 2.0546 1.8146 0.7142  -0.4260 -0.0007 821  LYS B NZ  
20613 N N   . ASP C 822  ? 2.1634 1.7532 1.9165 0.2706  -0.1435 -0.2626 822  ASP B N   
20614 C CA  . ASP C 822  ? 2.2089 1.8170 1.9827 0.2932  -0.1313 -0.2604 822  ASP B CA  
20615 C C   . ASP C 822  ? 2.1962 1.8094 1.9838 0.3070  -0.1522 -0.2553 822  ASP B C   
20616 O O   . ASP C 822  ? 2.1580 1.7544 1.9284 0.3165  -0.1414 -0.2459 822  ASP B O   
20617 C CB  . ASP C 822  ? 2.2816 1.9322 2.0996 0.3022  -0.1280 -0.2710 822  ASP B CB  
20618 C CG  . ASP C 822  ? 2.4088 2.0554 2.2132 0.2967  -0.0972 -0.2745 822  ASP B CG  
20619 O OD1 . ASP C 822  ? 2.4805 2.0944 2.2437 0.2805  -0.0835 -0.2712 822  ASP B OD1 
20620 O OD2 . ASP C 822  ? 2.4290 2.1037 2.2627 0.3084  -0.0866 -0.2806 822  ASP B OD2 
20621 N N   . VAL C 823  ? 2.2151 1.8534 2.0357 0.3084  -0.1816 -0.2614 823  VAL B N   
20622 C CA  . VAL C 823  ? 2.1997 1.8411 2.0314 0.3187  -0.2058 -0.2576 823  VAL B CA  
20623 C C   . VAL C 823  ? 2.2608 1.8940 2.0889 0.3046  -0.2356 -0.2593 823  VAL B C   
20624 O O   . VAL C 823  ? 2.2918 1.9416 2.1379 0.2943  -0.2466 -0.2669 823  VAL B O   
20625 C CB  . VAL C 823  ? 2.1178 1.7994 1.9968 0.3381  -0.2148 -0.2629 823  VAL B CB  
20626 C CG1 . VAL C 823  ? 2.0757 1.7599 1.9652 0.3456  -0.2440 -0.2603 823  VAL B CG1 
20627 C CG2 . VAL C 823  ? 2.0961 1.7816 1.9755 0.3530  -0.1893 -0.2591 823  VAL B CG2 
20628 N N   . PHE C 824  ? 2.2459 1.8533 2.0510 0.3041  -0.2489 -0.2519 824  PHE B N   
20629 C CA  . PHE C 824  ? 2.2409 1.8341 2.0363 0.2903  -0.2777 -0.2523 824  PHE B CA  
20630 C C   . PHE C 824  ? 2.1766 1.7566 1.9646 0.2989  -0.2962 -0.2462 824  PHE B C   
20631 O O   . PHE C 824  ? 2.1443 1.7085 1.9144 0.3083  -0.2816 -0.2385 824  PHE B O   
20632 C CB  . PHE C 824  ? 2.3108 1.8638 2.0596 0.2671  -0.2682 -0.2491 824  PHE B CB  
20633 C CG  . PHE C 824  ? 2.3818 1.8914 2.0830 0.2657  -0.2479 -0.2386 824  PHE B CG  
20634 C CD1 . PHE C 824  ? 2.4401 1.9129 2.1078 0.2568  -0.2620 -0.2323 824  PHE B CD1 
20635 C CD2 . PHE C 824  ? 2.4036 1.9086 2.0939 0.2733  -0.2146 -0.2347 824  PHE B CD2 
20636 C CE1 . PHE C 824  ? 2.4849 1.9174 2.1098 0.2558  -0.2421 -0.2223 824  PHE B CE1 
20637 C CE2 . PHE C 824  ? 2.4504 1.9167 2.0994 0.2727  -0.1952 -0.2242 824  PHE B CE2 
20638 C CZ  . PHE C 824  ? 2.4844 1.9146 2.1011 0.2640  -0.2084 -0.2179 824  PHE B CZ  
20639 N N   . LEU C 825  ? 2.1258 1.7134 1.9288 0.2959  -0.3286 -0.2493 825  LEU B N   
20640 C CA  . LEU C 825  ? 2.0553 1.6279 1.8483 0.3021  -0.3479 -0.2442 825  LEU B CA  
20641 C C   . LEU C 825  ? 2.0871 1.6167 1.8381 0.2829  -0.3617 -0.2399 825  LEU B C   
20642 O O   . LEU C 825  ? 2.1223 1.6449 1.8664 0.2650  -0.3716 -0.2432 825  LEU B O   
20643 C CB  . LEU C 825  ? 1.9377 1.5464 1.7754 0.3153  -0.3753 -0.2499 825  LEU B CB  
20644 C CG  . LEU C 825  ? 1.8439 1.4317 1.6659 0.3147  -0.4023 -0.2461 825  LEU B CG  
20645 C CD1 . LEU C 825  ? 1.7889 1.3640 1.5964 0.3289  -0.3932 -0.2388 825  LEU B CD1 
20646 C CD2 . LEU C 825  ? 1.8051 1.4233 1.6666 0.3204  -0.4338 -0.2526 825  LEU B CD2 
20647 N N   . GLU C 826  ? 2.0780 1.5785 1.8008 0.2865  -0.3626 -0.2324 826  GLU B N   
20648 C CA  . GLU C 826  ? 2.1061 1.5650 1.7902 0.2711  -0.3793 -0.2283 826  GLU B CA  
20649 C C   . GLU C 826  ? 2.0842 1.5475 1.7794 0.2828  -0.4053 -0.2275 826  GLU B C   
20650 O O   . GLU C 826  ? 2.0316 1.5121 1.7436 0.3016  -0.3994 -0.2254 826  GLU B O   
20651 C CB  . GLU C 826  ? 2.1599 1.5723 1.7927 0.2634  -0.3524 -0.2191 826  GLU B CB  
20652 C CG  . GLU C 826  ? 2.1808 1.5938 1.8131 0.2818  -0.3356 -0.2120 826  GLU B CG  
20653 C CD  . GLU C 826  ? 2.2529 1.6180 1.8351 0.2747  -0.3124 -0.2016 826  GLU B CD  
20654 O OE1 . GLU C 826  ? 2.2569 1.6122 1.8313 0.2854  -0.3097 -0.1945 826  GLU B OE1 
20655 O OE2 . GLU C 826  ? 2.3056 1.6424 1.8560 0.2584  -0.2967 -0.2003 826  GLU B OE2 
20656 N N   . MET C 827  ? 2.0999 1.5473 1.7849 0.2713  -0.4347 -0.2290 827  MET B N   
20657 C CA  . MET C 827  ? 2.0715 1.5161 1.7597 0.2800  -0.4603 -0.2281 827  MET B CA  
20658 C C   . MET C 827  ? 2.0808 1.4710 1.7159 0.2659  -0.4641 -0.2216 827  MET B C   
20659 O O   . MET C 827  ? 2.1385 1.4997 1.7450 0.2454  -0.4670 -0.2213 827  MET B O   
20660 C CB  . MET C 827  ? 2.0698 1.5402 1.7911 0.2786  -0.4942 -0.2353 827  MET B CB  
20661 C CG  . MET C 827  ? 2.0261 1.5491 1.8009 0.2912  -0.4926 -0.2422 827  MET B CG  
20662 S SD  . MET C 827  ? 1.8338 1.3853 1.6381 0.3195  -0.4914 -0.2419 827  MET B SD  
20663 C CE  . MET C 827  ? 1.3738 0.8999 1.1584 0.3201  -0.5236 -0.2392 827  MET B CE  
20664 N N   . ASN C 828  ? 2.0371 1.4118 1.6576 0.2757  -0.4646 -0.2163 828  ASN B N   
20665 C CA  . ASN C 828  ? 2.0905 1.4124 1.6609 0.2625  -0.4698 -0.2106 828  ASN B CA  
20666 C C   . ASN C 828  ? 1.9618 1.2745 1.5305 0.2582  -0.5088 -0.2140 828  ASN B C   
20667 O O   . ASN C 828  ? 1.9565 1.2764 1.5346 0.2718  -0.5224 -0.2135 828  ASN B O   
20668 C CB  . ASN C 828  ? 2.1575 1.4597 1.7055 0.2722  -0.4467 -0.2017 828  ASN B CB  
20669 C CG  . ASN C 828  ? 2.3099 1.5525 1.8001 0.2554  -0.4365 -0.1946 828  ASN B CG  
20670 O OD1 . ASN C 828  ? 2.3730 1.5920 1.8377 0.2403  -0.4197 -0.1931 828  ASN B OD1 
20671 N ND2 . ASN C 828  ? 2.3571 1.5735 1.8250 0.2577  -0.4460 -0.1902 828  ASN B ND2 
20672 N N   . ILE C 829  ? 1.9295 1.2255 1.4851 0.2389  -0.5269 -0.2171 829  ILE B N   
20673 C CA  . ILE C 829  ? 1.8344 1.1160 1.3832 0.2320  -0.5637 -0.2195 829  ILE B CA  
20674 C C   . ILE C 829  ? 1.8037 1.0246 1.2938 0.2195  -0.5610 -0.2131 829  ILE B C   
20675 O O   . ILE C 829  ? 1.8429 1.0307 1.2965 0.2092  -0.5340 -0.2077 829  ILE B O   
20676 C CB  . ILE C 829  ? 1.8010 1.0900 1.3609 0.2154  -0.5847 -0.2244 829  ILE B CB  
20677 C CG1 . ILE C 829  ? 1.7484 1.0915 1.3594 0.2244  -0.5755 -0.2296 829  ILE B CG1 
20678 C CG2 . ILE C 829  ? 1.7873 1.0790 1.3585 0.2145  -0.6255 -0.2278 829  ILE B CG2 
20679 C CD1 . ILE C 829  ? 1.6857 1.0788 1.3496 0.2483  -0.5884 -0.2341 829  ILE B CD1 
20680 N N   . PRO C 830  ? 1.7341 0.9390 1.2139 0.2209  -0.5878 -0.2136 830  PRO B N   
20681 C CA  . PRO C 830  ? 1.8353 0.9817 1.2598 0.2097  -0.5878 -0.2082 830  PRO B CA  
20682 C C   . PRO C 830  ? 2.0697 1.1769 1.4598 0.1839  -0.6035 -0.2089 830  PRO B C   
20683 O O   . PRO C 830  ? 2.2066 1.3365 1.6204 0.1762  -0.6186 -0.2135 830  PRO B O   
20684 C CB  . PRO C 830  ? 1.7130 0.8654 1.1478 0.2215  -0.6166 -0.2105 830  PRO B CB  
20685 C CG  . PRO C 830  ? 1.6267 0.8396 1.1213 0.2387  -0.6303 -0.2167 830  PRO B CG  
20686 C CD  . PRO C 830  ? 1.6404 0.8798 1.1593 0.2324  -0.6209 -0.2196 830  PRO B CD  
20687 N N   . TYR C 831  ? 2.1226 1.1704 1.4568 0.1699  -0.6005 -0.2040 831  TYR B N   
20688 C CA  . TYR C 831  ? 2.1763 1.1839 1.4762 0.1453  -0.6222 -0.2048 831  TYR B CA  
20689 C C   . TYR C 831  ? 2.1146 1.1489 1.4468 0.1506  -0.6638 -0.2110 831  TYR B C   
20690 O O   . TYR C 831  ? 2.1101 1.1784 1.4774 0.1479  -0.6820 -0.2156 831  TYR B O   
20691 C CB  . TYR C 831  ? 2.2844 1.2224 1.5191 0.1318  -0.6146 -0.1990 831  TYR B CB  
20692 C CG  . TYR C 831  ? 2.3732 1.2594 1.5623 0.1035  -0.6331 -0.1987 831  TYR B CG  
20693 C CD1 . TYR C 831  ? 2.4282 1.2624 1.5732 0.0930  -0.6511 -0.1974 831  TYR B CD1 
20694 C CD2 . TYR C 831  ? 2.4074 1.2949 1.5956 0.0864  -0.6326 -0.1996 831  TYR B CD2 
20695 C CE1 . TYR C 831  ? 2.4924 1.2763 1.5931 0.0665  -0.6682 -0.1968 831  TYR B CE1 
20696 C CE2 . TYR C 831  ? 2.4713 1.3097 1.6157 0.0594  -0.6503 -0.1986 831  TYR B CE2 
20697 C CZ  . TYR C 831  ? 2.5242 1.3100 1.6244 0.0495  -0.6682 -0.1972 831  TYR B CZ  
20698 O OH  . TYR C 831  ? 2.5949 1.3278 1.6482 0.0215  -0.6869 -0.1959 831  TYR B OH  
20699 N N   . SER C 832  ? 2.0905 1.1122 1.4137 0.1595  -0.6783 -0.2110 832  SER B N   
20700 C CA  . SER C 832  ? 2.1131 1.1469 1.4549 0.1603  -0.7196 -0.2161 832  SER B CA  
20701 C C   . SER C 832  ? 2.0725 1.1347 1.4420 0.1844  -0.7290 -0.2183 832  SER B C   
20702 O O   . SER C 832  ? 2.0575 1.1112 1.4144 0.1954  -0.7071 -0.2145 832  SER B O   
20703 C CB  . SER C 832  ? 2.2199 1.1904 1.5061 0.1371  -0.7398 -0.2146 832  SER B CB  
20704 O OG  . SER C 832  ? 2.2661 1.1912 1.5073 0.1378  -0.7247 -0.2102 832  SER B OG  
20705 N N   . VAL C 833  ? 2.0222 1.1172 1.4289 0.1918  -0.7621 -0.2237 833  VAL B N   
20706 C CA  . VAL C 833  ? 1.9424 1.0638 1.3754 0.2138  -0.7767 -0.2264 833  VAL B CA  
20707 C C   . VAL C 833  ? 1.9418 1.0484 1.3686 0.2083  -0.8181 -0.2298 833  VAL B C   
20708 O O   . VAL C 833  ? 1.9447 1.0549 1.3810 0.1955  -0.8401 -0.2318 833  VAL B O   
20709 C CB  . VAL C 833  ? 1.8957 1.0841 1.3931 0.2338  -0.7752 -0.2303 833  VAL B CB  
20710 C CG1 . VAL C 833  ? 1.8530 1.0627 1.3666 0.2576  -0.7666 -0.2301 833  VAL B CG1 
20711 C CG2 . VAL C 833  ? 1.8798 1.0884 1.3925 0.2297  -0.7466 -0.2292 833  VAL B CG2 
20712 N N   . VAL C 834  ? 1.9249 1.0161 1.3367 0.2180  -0.8295 -0.2302 834  VAL B N   
20713 C CA  . VAL C 834  ? 1.9420 1.0235 1.3517 0.2166  -0.8696 -0.2339 834  VAL B CA  
20714 C C   . VAL C 834  ? 1.9357 1.0765 1.4069 0.2351  -0.8902 -0.2387 834  VAL B C   
20715 O O   . VAL C 834  ? 1.9021 1.0880 1.4128 0.2545  -0.8733 -0.2395 834  VAL B O   
20716 C CB  . VAL C 834  ? 1.9305 0.9760 1.3033 0.2216  -0.8744 -0.2331 834  VAL B CB  
20717 C CG1 . VAL C 834  ? 1.9340 0.9824 1.3158 0.2272  -0.9147 -0.2377 834  VAL B CG1 
20718 C CG2 . VAL C 834  ? 1.9682 0.9469 1.2761 0.2000  -0.8622 -0.2287 834  VAL B CG2 
20719 N N   . ARG C 835  ? 1.9951 1.1345 1.4738 0.2290  -0.9267 -0.2415 835  ARG B N   
20720 C CA  . ARG C 835  ? 2.0102 1.2018 1.5454 0.2465  -0.9486 -0.2454 835  ARG B CA  
20721 C C   . ARG C 835  ? 2.0050 1.2121 1.5511 0.2709  -0.9487 -0.2473 835  ARG B C   
20722 O O   . ARG C 835  ? 2.0152 1.1842 1.5221 0.2701  -0.9568 -0.2469 835  ARG B O   
20723 C CB  . ARG C 835  ? 2.0771 1.2578 1.6128 0.2340  -0.9894 -0.2468 835  ARG B CB  
20724 C CG  . ARG C 835  ? 2.0971 1.3061 1.6666 0.2533  -1.0190 -0.2503 835  ARG B CG  
20725 C CD  . ARG C 835  ? 2.1284 1.3486 1.7215 0.2443  -1.0559 -0.2508 835  ARG B CD  
20726 N NE  . ARG C 835  ? 2.1727 1.3415 1.7215 0.2267  -1.0867 -0.2502 835  ARG B NE  
20727 C CZ  . ARG C 835  ? 2.1927 1.3058 1.6828 0.2189  -1.0860 -0.2499 835  ARG B CZ  
20728 N NH1 . ARG C 835  ? 2.1744 1.2743 1.6411 0.2268  -1.0557 -0.2495 835  ARG B NH1 
20729 N NH2 . ARG C 835  ? 2.2294 1.2987 1.6837 0.2025  -1.1165 -0.2496 835  ARG B NH2 
20730 N N   . GLY C 836  ? 1.9712 1.2325 1.5689 0.2918  -0.9391 -0.2491 836  GLY B N   
20731 C CA  . GLY C 836  ? 1.9697 1.2492 1.5812 0.3154  -0.9392 -0.2506 836  GLY B CA  
20732 C C   . GLY C 836  ? 1.9607 1.2225 1.5435 0.3209  -0.9100 -0.2474 836  GLY B C   
20733 O O   . GLY C 836  ? 1.9416 1.2005 1.5173 0.3349  -0.9146 -0.2477 836  GLY B O   
20734 N N   . GLU C 837  ? 1.9905 1.2390 1.5555 0.3092  -0.8809 -0.2437 837  GLU B N   
20735 C CA  . GLU C 837  ? 1.9851 1.2250 1.5319 0.3146  -0.8479 -0.2392 837  GLU B CA  
20736 C C   . GLU C 837  ? 1.9968 1.2900 1.5932 0.3287  -0.8273 -0.2399 837  GLU B C   
20737 O O   . GLU C 837  ? 2.0108 1.3249 1.6324 0.3220  -0.8274 -0.2419 837  GLU B O   
20738 C CB  . GLU C 837  ? 1.9770 1.1731 1.4794 0.2929  -0.8287 -0.2347 837  GLU B CB  
20739 C CG  . GLU C 837  ? 1.9434 1.0898 1.3928 0.2875  -0.8193 -0.2302 837  GLU B CG  
20740 C CD  . GLU C 837  ? 1.8517 0.9470 1.2530 0.2634  -0.8057 -0.2261 837  GLU B CD  
20741 O OE1 . GLU C 837  ? 1.8541 0.9569 1.2641 0.2530  -0.7940 -0.2257 837  GLU B OE1 
20742 O OE2 . GLU C 837  ? 1.8543 0.9004 1.2077 0.2545  -0.8059 -0.2234 837  GLU B OE2 
20743 N N   . GLN C 838  ? 1.9926 1.3077 1.6035 0.3472  -0.8110 -0.2384 838  GLN B N   
20744 C CA  . GLN C 838  ? 1.9662 1.3298 1.6224 0.3610  -0.7907 -0.2392 838  GLN B CA  
20745 C C   . GLN C 838  ? 1.9554 1.3140 1.5999 0.3555  -0.7537 -0.2341 838  GLN B C   
20746 O O   . GLN C 838  ? 1.9289 1.2715 1.5507 0.3592  -0.7361 -0.2288 838  GLN B O   
20747 C CB  . GLN C 838  ? 1.9529 1.3435 1.6324 0.3841  -0.7942 -0.2402 838  GLN B CB  
20748 C CG  . GLN C 838  ? 1.9558 1.3908 1.6759 0.3991  -0.7709 -0.2403 838  GLN B CG  
20749 C CD  . GLN C 838  ? 2.1163 1.5637 1.8419 0.4189  -0.7670 -0.2386 838  GLN B CD  
20750 O OE1 . GLN C 838  ? 2.1138 1.5830 1.8642 0.4334  -0.7843 -0.2424 838  GLN B OE1 
20751 N NE2 . GLN C 838  ? 2.1038 1.5361 1.8055 0.4192  -0.7443 -0.2322 838  GLN B NE2 
20752 N N   . ILE C 839  ? 1.9919 1.3647 1.6527 0.3467  -0.7420 -0.2353 839  ILE B N   
20753 C CA  . ILE C 839  ? 2.0243 1.3821 1.6649 0.3366  -0.7095 -0.2304 839  ILE B CA  
20754 C C   . ILE C 839  ? 2.0109 1.4084 1.6856 0.3497  -0.6814 -0.2298 839  ILE B C   
20755 O O   . ILE C 839  ? 2.0203 1.4586 1.7384 0.3596  -0.6868 -0.2348 839  ILE B O   
20756 C CB  . ILE C 839  ? 2.0384 1.3755 1.6632 0.3141  -0.7130 -0.2313 839  ILE B CB  
20757 C CG1 . ILE C 839  ? 2.0625 1.3669 1.6498 0.3010  -0.6818 -0.2252 839  ILE B CG1 
20758 C CG2 . ILE C 839  ? 2.0264 1.4064 1.6975 0.3158  -0.7170 -0.2365 839  ILE B CG2 
20759 C CD1 . ILE C 839  ? 2.0887 1.3400 1.6230 0.2920  -0.6819 -0.2201 839  ILE B CD1 
20760 N N   . GLN C 840  ? 2.0094 1.3943 1.6647 0.3497  -0.6514 -0.2234 840  GLN B N   
20761 C CA  . GLN C 840  ? 1.9746 1.3927 1.6579 0.3602  -0.6236 -0.2223 840  GLN B CA  
20762 C C   . GLN C 840  ? 1.9169 1.3294 1.5933 0.3464  -0.6000 -0.2212 840  GLN B C   
20763 O O   . GLN C 840  ? 1.9053 1.2844 1.5456 0.3360  -0.5809 -0.2151 840  GLN B O   
20764 C CB  . GLN C 840  ? 2.0493 1.4654 1.7235 0.3725  -0.6053 -0.2154 840  GLN B CB  
20765 C CG  . GLN C 840  ? 2.1131 1.5735 1.8285 0.3915  -0.5971 -0.2171 840  GLN B CG  
20766 C CD  . GLN C 840  ? 2.1939 1.6595 1.9077 0.3958  -0.5630 -0.2103 840  GLN B CD  
20767 O OE1 . GLN C 840  ? 2.2052 1.6946 1.9389 0.4110  -0.5551 -0.2085 840  GLN B OE1 
20768 N NE2 . GLN C 840  ? 2.2299 1.6715 1.9186 0.3820  -0.5426 -0.2061 840  GLN B NE2 
20769 N N   . LEU C 841  ? 1.8590 1.3046 1.5708 0.3469  -0.6007 -0.2270 841  LEU B N   
20770 C CA  . LEU C 841  ? 1.8293 1.2713 1.5364 0.3325  -0.5830 -0.2274 841  LEU B CA  
20771 C C   . LEU C 841  ? 1.7767 1.2401 1.4986 0.3406  -0.5492 -0.2253 841  LEU B C   
20772 O O   . LEU C 841  ? 1.7240 1.2270 1.4860 0.3500  -0.5458 -0.2303 841  LEU B O   
20773 C CB  . LEU C 841  ? 1.7998 1.2660 1.5376 0.3269  -0.6039 -0.2348 841  LEU B CB  
20774 C CG  . LEU C 841  ? 1.7808 1.2145 1.4918 0.3072  -0.6285 -0.2353 841  LEU B CG  
20775 C CD1 . LEU C 841  ? 1.7570 1.2186 1.5017 0.3004  -0.6450 -0.2413 841  LEU B CD1 
20776 C CD2 . LEU C 841  ? 1.7835 1.1707 1.4439 0.2890  -0.6081 -0.2295 841  LEU B CD2 
20777 N N   . LYS C 842  ? 1.7992 1.2352 1.4885 0.3364  -0.5235 -0.2179 842  LYS B N   
20778 C CA  . LYS C 842  ? 1.7916 1.2454 1.4926 0.3443  -0.4911 -0.2149 842  LYS B CA  
20779 C C   . LYS C 842  ? 1.8217 1.2767 1.5219 0.3319  -0.4723 -0.2170 842  LYS B C   
20780 O O   . LYS C 842  ? 1.8531 1.2997 1.5481 0.3169  -0.4852 -0.2211 842  LYS B O   
20781 C CB  . LYS C 842  ? 1.7825 1.2111 1.4539 0.3478  -0.4704 -0.2048 842  LYS B CB  
20782 C CG  . LYS C 842  ? 1.7742 1.2021 1.4454 0.3601  -0.4862 -0.2020 842  LYS B CG  
20783 C CD  . LYS C 842  ? 1.7955 1.1987 1.4381 0.3618  -0.4643 -0.1910 842  LYS B CD  
20784 C CE  . LYS C 842  ? 1.8185 1.2068 1.4470 0.3674  -0.4822 -0.1875 842  LYS B CE  
20785 N NZ  . LYS C 842  ? 1.8518 1.2141 1.4517 0.3670  -0.4594 -0.1758 842  LYS B NZ  
20786 N N   . GLY C 843  ? 1.8516 1.3171 1.5566 0.3383  -0.4418 -0.2135 843  GLY B N   
20787 C CA  . GLY C 843  ? 1.8802 1.3512 1.5873 0.3296  -0.4203 -0.2156 843  GLY B CA  
20788 C C   . GLY C 843  ? 1.9276 1.4217 1.6525 0.3440  -0.3922 -0.2129 843  GLY B C   
20789 O O   . GLY C 843  ? 1.8875 1.4006 1.6311 0.3607  -0.3946 -0.2111 843  GLY B O   
20790 N N   . THR C 844  ? 1.9774 1.4681 1.6942 0.3372  -0.3658 -0.2122 844  THR B N   
20791 C CA  . THR C 844  ? 2.0135 1.5260 1.7473 0.3501  -0.3391 -0.2099 844  THR B CA  
20792 C C   . THR C 844  ? 1.9907 1.5260 1.7449 0.3453  -0.3276 -0.2178 844  THR B C   
20793 O O   . THR C 844  ? 2.0005 1.5216 1.7404 0.3284  -0.3304 -0.2212 844  THR B O   
20794 C CB  . THR C 844  ? 1.7793 1.2624 1.4798 0.3518  -0.3124 -0.1974 844  THR B CB  
20795 O OG1 . THR C 844  ? 1.7907 1.2494 1.4630 0.3388  -0.2872 -0.1945 844  THR B OG1 
20796 C CG2 . THR C 844  ? 1.7043 1.1564 1.3773 0.3498  -0.3270 -0.1906 844  THR B CG2 
20797 N N   . VAL C 845  ? 1.9732 1.5437 1.7613 0.3592  -0.3171 -0.2212 845  VAL B N   
20798 C CA  . VAL C 845  ? 1.9838 1.5779 1.7941 0.3553  -0.3076 -0.2296 845  VAL B CA  
20799 C C   . VAL C 845  ? 1.9779 1.5698 1.7790 0.3571  -0.2725 -0.2263 845  VAL B C   
20800 O O   . VAL C 845  ? 1.9413 1.5421 1.7497 0.3713  -0.2586 -0.2214 845  VAL B O   
20801 C CB  . VAL C 845  ? 1.5082 1.1456 1.3674 0.3673  -0.3245 -0.2389 845  VAL B CB  
20802 C CG1 . VAL C 845  ? 1.4780 1.1332 1.3555 0.3875  -0.3200 -0.2360 845  VAL B CG1 
20803 C CG2 . VAL C 845  ? 1.4987 1.1585 1.3792 0.3617  -0.3135 -0.2475 845  VAL B CG2 
20804 N N   . TYR C 846  ? 2.0284 1.6071 1.8120 0.3420  -0.2586 -0.2285 846  TYR B N   
20805 C CA  . TYR C 846  ? 2.0446 1.6091 1.8069 0.3409  -0.2243 -0.2233 846  TYR B CA  
20806 C C   . TYR C 846  ? 2.1193 1.7142 1.9088 0.3472  -0.2067 -0.2299 846  TYR B C   
20807 O O   . TYR C 846  ? 2.1072 1.7175 1.9118 0.3389  -0.2105 -0.2392 846  TYR B O   
20808 C CB  . TYR C 846  ? 2.0016 1.5232 1.7171 0.3214  -0.2135 -0.2187 846  TYR B CB  
20809 C CG  . TYR C 846  ? 1.9434 1.4298 1.6268 0.3193  -0.2206 -0.2090 846  TYR B CG  
20810 C CD1 . TYR C 846  ? 1.9378 1.3891 1.5876 0.3015  -0.2322 -0.2078 846  TYR B CD1 
20811 C CD2 . TYR C 846  ? 1.8964 1.3852 1.5839 0.3350  -0.2170 -0.2011 846  TYR B CD2 
20812 C CE1 . TYR C 846  ? 1.9285 1.3467 1.5489 0.3000  -0.2382 -0.1993 846  TYR B CE1 
20813 C CE2 . TYR C 846  ? 1.8774 1.3359 1.5377 0.3335  -0.2232 -0.1923 846  TYR B CE2 
20814 C CZ  . TYR C 846  ? 1.8908 1.3139 1.5178 0.3164  -0.2332 -0.1918 846  TYR B CZ  
20815 O OH  . TYR C 846  ? 1.8976 1.2899 1.4975 0.3155  -0.2385 -0.1834 846  TYR B OH  
20816 N N   . ASN C 847  ? 2.2046 1.8083 2.0012 0.3621  -0.1887 -0.2248 847  ASN B N   
20817 C CA  . ASN C 847  ? 2.2898 1.9146 2.1039 0.3685  -0.1665 -0.2291 847  ASN B CA  
20818 C C   . ASN C 847  ? 2.3519 1.9499 2.1320 0.3636  -0.1348 -0.2213 847  ASN B C   
20819 O O   . ASN C 847  ? 2.3264 1.9038 2.0854 0.3684  -0.1246 -0.2097 847  ASN B O   
20820 C CB  . ASN C 847  ? 2.3114 1.9639 2.1567 0.3883  -0.1683 -0.2286 847  ASN B CB  
20821 C CG  . ASN C 847  ? 2.3539 2.0352 2.2273 0.3938  -0.1556 -0.2377 847  ASN B CG  
20822 O OD1 . ASN C 847  ? 2.3882 2.0636 2.2499 0.3871  -0.1326 -0.2396 847  ASN B OD1 
20823 N ND2 . ASN C 847  ? 2.3490 2.0596 2.2579 0.4059  -0.1699 -0.2436 847  ASN B ND2 
20824 N N   . TYR C 848  ? 2.4387 2.0376 2.2144 0.3542  -0.1190 -0.2276 848  TYR B N   
20825 C CA  . TYR C 848  ? 2.5202 2.0918 2.2614 0.3478  -0.0885 -0.2215 848  TYR B CA  
20826 C C   . TYR C 848  ? 2.5505 2.1430 2.3080 0.3519  -0.0678 -0.2283 848  TYR B C   
20827 O O   . TYR C 848  ? 2.5658 2.1412 2.2997 0.3493  -0.0398 -0.2243 848  TYR B O   
20828 C CB  . TYR C 848  ? 2.5607 2.1001 2.2665 0.3270  -0.0904 -0.2217 848  TYR B CB  
20829 C CG  . TYR C 848  ? 2.5666 2.0699 2.2391 0.3230  -0.0954 -0.2107 848  TYR B CG  
20830 C CD1 . TYR C 848  ? 2.5355 2.0392 2.2127 0.3377  -0.0969 -0.2013 848  TYR B CD1 
20831 C CD2 . TYR C 848  ? 2.5912 2.0579 2.2252 0.3038  -0.0972 -0.2092 848  TYR B CD2 
20832 C CE1 . TYR C 848  ? 2.5437 2.0141 2.1906 0.3340  -0.1000 -0.1913 848  TYR B CE1 
20833 C CE2 . TYR C 848  ? 2.5977 2.0286 2.1994 0.2999  -0.1000 -0.1993 848  TYR B CE2 
20834 C CZ  . TYR C 848  ? 2.5865 2.0202 2.1957 0.3154  -0.1010 -0.1906 848  TYR B CZ  
20835 O OH  . TYR C 848  ? 2.6247 2.0228 2.2022 0.3115  -0.1031 -0.1808 848  TYR B OH  
20836 N N   . ARG C 849  ? 2.5681 2.1967 2.3657 0.3586  -0.0815 -0.2385 849  ARG B N   
20837 C CA  . ARG C 849  ? 2.5979 2.2494 2.4163 0.3660  -0.0639 -0.2450 849  ARG B CA  
20838 C C   . ARG C 849  ? 2.5790 2.2281 2.3950 0.3818  -0.0475 -0.2349 849  ARG B C   
20839 O O   . ARG C 849  ? 2.5516 2.1961 2.3671 0.3900  -0.0587 -0.2261 849  ARG B O   
20840 C CB  . ARG C 849  ? 2.6323 2.3213 2.4951 0.3714  -0.0843 -0.2569 849  ARG B CB  
20841 C CG  . ARG C 849  ? 2.6943 2.4082 2.5819 0.3796  -0.0684 -0.2649 849  ARG B CG  
20842 C CD  . ARG C 849  ? 2.7867 2.4917 2.6567 0.3676  -0.0442 -0.2700 849  ARG B CD  
20843 N NE  . ARG C 849  ? 2.8264 2.5560 2.7219 0.3747  -0.0313 -0.2792 849  ARG B NE  
20844 C CZ  . ARG C 849  ? 2.8687 2.5926 2.7509 0.3692  -0.0058 -0.2831 849  ARG B CZ  
20845 N NH1 . ARG C 849  ? 2.9080 2.6021 2.7509 0.3568  0.0103  -0.2782 849  ARG B NH1 
20846 N NH2 . ARG C 849  ? 2.8587 2.6048 2.7651 0.3761  0.0043  -0.2920 849  ARG B NH2 
20847 N N   . THR C 850  ? 2.5958 2.2470 2.4090 0.3852  -0.0213 -0.2356 850  THR B N   
20848 C CA  . THR C 850  ? 2.5765 2.2240 2.3856 0.3987  -0.0037 -0.2250 850  THR B CA  
20849 C C   . THR C 850  ? 2.5509 2.2236 2.3924 0.4147  -0.0193 -0.2244 850  THR B C   
20850 O O   . THR C 850  ? 2.5556 2.2232 2.3935 0.4249  -0.0171 -0.2127 850  THR B O   
20851 C CB  . THR C 850  ? 2.5624 2.2086 2.3638 0.3989  0.0263  -0.2274 850  THR B CB  
20852 O OG1 . THR C 850  ? 2.5467 2.2171 2.3727 0.3962  0.0232  -0.2426 850  THR B OG1 
20853 C CG2 . THR C 850  ? 2.5862 2.1992 2.3466 0.3859  0.0471  -0.2227 850  THR B CG2 
20854 N N   . SER C 851  ? 2.5270 2.2265 2.3997 0.4166  -0.0343 -0.2369 851  SER B N   
20855 C CA  . SER C 851  ? 2.5214 2.2433 2.4241 0.4304  -0.0518 -0.2379 851  SER B CA  
20856 C C   . SER C 851  ? 2.5286 2.2537 2.4399 0.4291  -0.0824 -0.2386 851  SER B C   
20857 O O   . SER C 851  ? 2.5148 2.2270 2.4118 0.4166  -0.0911 -0.2399 851  SER B O   
20858 C CB  . SER C 851  ? 2.5391 2.2873 2.4714 0.4349  -0.0484 -0.2509 851  SER B CB  
20859 O OG  . SER C 851  ? 2.5754 2.3334 2.5181 0.4237  -0.0557 -0.2631 851  SER B OG  
20860 N N   . GLY C 852  ? 2.5363 2.2764 2.4687 0.4416  -0.0989 -0.2374 852  GLY B N   
20861 C CA  . GLY C 852  ? 2.5229 2.2673 2.4651 0.4419  -0.1283 -0.2386 852  GLY B CA  
20862 C C   . GLY C 852  ? 2.4493 2.2169 2.4205 0.4394  -0.1424 -0.2527 852  GLY B C   
20863 O O   . GLY C 852  ? 2.4514 2.2313 2.4342 0.4368  -0.1285 -0.2613 852  GLY B O   
20864 N N   . MET C 853  ? 2.3689 2.1428 2.3522 0.4402  -0.1697 -0.2547 853  MET B N   
20865 C CA  . MET C 853  ? 2.2994 2.0987 2.3157 0.4405  -0.1852 -0.2668 853  MET B CA  
20866 C C   . MET C 853  ? 2.2331 2.0399 2.2645 0.4466  -0.2157 -0.2669 853  MET B C   
20867 O O   . MET C 853  ? 2.2181 2.0094 2.2327 0.4497  -0.2264 -0.2581 853  MET B O   
20868 C CB  . MET C 853  ? 2.3201 2.1190 2.3337 0.4241  -0.1821 -0.2739 853  MET B CB  
20869 C CG  . MET C 853  ? 2.3502 2.1277 2.3400 0.4105  -0.1970 -0.2697 853  MET B CG  
20870 S SD  . MET C 853  ? 2.6987 2.4693 2.6759 0.3895  -0.1865 -0.2760 853  MET B SD  
20871 C CE  . MET C 853  ? 2.8540 2.6020 2.7977 0.3882  -0.1493 -0.2694 853  MET B CE  
20872 N N   . GLN C 854  ? 2.1957 2.0268 2.2597 0.4487  -0.2291 -0.2768 854  GLN B N   
20873 C CA  . GLN C 854  ? 2.1674 2.0071 2.2479 0.4548  -0.2577 -0.2778 854  GLN B CA  
20874 C C   . GLN C 854  ? 2.1493 1.9869 2.2295 0.4408  -0.2760 -0.2809 854  GLN B C   
20875 O O   . GLN C 854  ? 2.1535 2.0004 2.2430 0.4304  -0.2697 -0.2876 854  GLN B O   
20876 C CB  . GLN C 854  ? 2.1581 2.0259 2.2766 0.4681  -0.2610 -0.2857 854  GLN B CB  
20877 C CG  . GLN C 854  ? 2.1516 2.0210 2.2702 0.4794  -0.2399 -0.2841 854  GLN B CG  
20878 C CD  . GLN C 854  ? 2.1402 2.0325 2.2925 0.4931  -0.2432 -0.2912 854  GLN B CD  
20879 O OE1 . GLN C 854  ? 2.1396 2.0501 2.3193 0.4943  -0.2587 -0.2983 854  GLN B OE1 
20880 N NE2 . GLN C 854  ? 2.1257 2.0161 2.2756 0.5034  -0.2284 -0.2889 854  GLN B NE2 
20881 N N   . PHE C 855  ? 2.1201 1.9439 2.1876 0.4396  -0.2985 -0.2757 855  PHE B N   
20882 C CA  . PHE C 855  ? 2.0886 1.9112 2.1589 0.4278  -0.3215 -0.2786 855  PHE B CA  
20883 C C   . PHE C 855  ? 2.0870 1.9258 2.1837 0.4377  -0.3501 -0.2812 855  PHE B C   
20884 O O   . PHE C 855  ? 2.0933 1.9492 2.2124 0.4536  -0.3502 -0.2832 855  PHE B O   
20885 C CB  . PHE C 855  ? 2.0451 1.8330 2.0735 0.4134  -0.3239 -0.2710 855  PHE B CB  
20886 C CG  . PHE C 855  ? 1.9835 1.7497 1.9878 0.4204  -0.3300 -0.2616 855  PHE B CG  
20887 C CD1 . PHE C 855  ? 1.9684 1.7278 1.9705 0.4214  -0.3578 -0.2600 855  PHE B CD1 
20888 C CD2 . PHE C 855  ? 1.9556 1.7074 1.9384 0.4251  -0.3078 -0.2539 855  PHE B CD2 
20889 C CE1 . PHE C 855  ? 1.9538 1.6925 1.9323 0.4269  -0.3630 -0.2514 855  PHE B CE1 
20890 C CE2 . PHE C 855  ? 1.9398 1.6724 1.9012 0.4307  -0.3133 -0.2445 855  PHE B CE2 
20891 C CZ  . PHE C 855  ? 1.9356 1.6615 1.8944 0.4313  -0.3406 -0.2435 855  PHE B CZ  
20892 N N   . CYS C 856  ? 2.0968 1.9281 2.1891 0.4279  -0.3739 -0.2810 856  CYS B N   
20893 C CA  . CYS C 856  ? 2.0973 1.9419 2.2128 0.4362  -0.4028 -0.2831 856  CYS B CA  
20894 C C   . CYS C 856  ? 2.1407 1.9719 2.2446 0.4208  -0.4265 -0.2822 856  CYS B C   
20895 O O   . CYS C 856  ? 2.1479 1.9971 2.2761 0.4134  -0.4369 -0.2876 856  CYS B O   
20896 C CB  . CYS C 856  ? 2.0753 1.9572 2.2386 0.4460  -0.4032 -0.2917 856  CYS B CB  
20897 S SG  . CYS C 856  ? 2.5438 2.4470 2.7431 0.4563  -0.4373 -0.2950 856  CYS B SG  
20898 N N   . VAL C 857  ? 2.1673 1.9665 2.2342 0.4154  -0.4351 -0.2752 857  VAL B N   
20899 C CA  . VAL C 857  ? 2.1792 1.9590 2.2280 0.3988  -0.4562 -0.2738 857  VAL B CA  
20900 C C   . VAL C 857  ? 2.1776 1.9668 2.2456 0.4049  -0.4893 -0.2754 857  VAL B C   
20901 O O   . VAL C 857  ? 2.1807 1.9681 2.2483 0.4191  -0.4979 -0.2731 857  VAL B O   
20902 C CB  . VAL C 857  ? 2.1695 1.9072 2.1675 0.3890  -0.4505 -0.2656 857  VAL B CB  
20903 C CG1 . VAL C 857  ? 2.1717 1.8965 2.1478 0.3798  -0.4194 -0.2635 857  VAL B CG1 
20904 C CG2 . VAL C 857  ? 2.1500 1.8785 2.1374 0.4040  -0.4525 -0.2601 857  VAL B CG2 
20905 N N   . LYS C 858  ? 2.1734 1.9718 2.2571 0.3938  -0.5083 -0.2788 858  LYS B N   
20906 C CA  . LYS C 858  ? 2.1885 1.9964 2.2921 0.3990  -0.5406 -0.2800 858  LYS B CA  
20907 C C   . LYS C 858  ? 2.1817 1.9672 2.2643 0.3791  -0.5633 -0.2779 858  LYS B C   
20908 O O   . LYS C 858  ? 2.1965 1.9773 2.2718 0.3612  -0.5578 -0.2786 858  LYS B O   
20909 C CB  . LYS C 858  ? 2.2287 2.0807 2.3878 0.4111  -0.5455 -0.2866 858  LYS B CB  
20910 C CG  . LYS C 858  ? 2.2894 2.1629 2.4719 0.3989  -0.5363 -0.2912 858  LYS B CG  
20911 C CD  . LYS C 858  ? 2.3167 2.2342 2.5563 0.4117  -0.5414 -0.2972 858  LYS B CD  
20912 C CE  . LYS C 858  ? 2.3552 2.2936 2.6183 0.3970  -0.5369 -0.3011 858  LYS B CE  
20913 N NZ  . LYS C 858  ? 2.3503 2.3323 2.6701 0.4097  -0.5359 -0.3069 858  LYS B NZ  
20914 N N   . MET C 859  ? 2.1480 1.9174 2.2183 0.3817  -0.5889 -0.2752 859  MET B N   
20915 C CA  . MET C 859  ? 2.1215 1.8647 2.1676 0.3634  -0.6131 -0.2727 859  MET B CA  
20916 C C   . MET C 859  ? 2.1009 1.8690 2.1848 0.3641  -0.6441 -0.2757 859  MET B C   
20917 O O   . MET C 859  ? 2.0793 1.8743 2.1979 0.3827  -0.6537 -0.2782 859  MET B O   
20918 C CB  . MET C 859  ? 2.1057 1.8097 2.1081 0.3638  -0.6207 -0.2673 859  MET B CB  
20919 C CG  . MET C 859  ? 2.1094 1.8025 2.1088 0.3615  -0.6565 -0.2667 859  MET B CG  
20920 S SD  . MET C 859  ? 1.6112 1.2638 1.5645 0.3672  -0.6612 -0.2613 859  MET B SD  
20921 C CE  . MET C 859  ? 2.5793 2.1811 2.4744 0.3413  -0.6508 -0.2561 859  MET B CE  
20922 N N   . SER C 860  ? 2.1220 1.8796 2.1979 0.3435  -0.6597 -0.2748 860  SER B N   
20923 C CA  . SER C 860  ? 2.1368 1.9202 2.2511 0.3415  -0.6886 -0.2767 860  SER B CA  
20924 C C   . SER C 860  ? 2.1576 1.9225 2.2603 0.3416  -0.7233 -0.2740 860  SER B C   
20925 O O   . SER C 860  ? 2.1926 1.9174 2.2517 0.3244  -0.7348 -0.2703 860  SER B O   
20926 C CB  . SER C 860  ? 2.1715 1.9563 2.2868 0.3182  -0.6894 -0.2767 860  SER B CB  
20927 O OG  . SER C 860  ? 2.2121 1.9953 2.3353 0.3068  -0.7244 -0.2747 860  SER B OG  
20928 N N   . ALA C 861  ? 2.1243 1.9177 2.2657 0.3608  -0.7395 -0.2760 861  ALA B N   
20929 C CA  . ALA C 861  ? 2.1076 1.8882 2.2438 0.3635  -0.7733 -0.2740 861  ALA B CA  
20930 C C   . ALA C 861  ? 2.0971 1.8708 2.2334 0.3423  -0.8012 -0.2718 861  ALA B C   
20931 O O   . ALA C 861  ? 2.0651 1.8744 2.2480 0.3429  -0.8143 -0.2729 861  ALA B O   
20932 C CB  . ALA C 861  ? 2.0701 1.8864 2.2525 0.3892  -0.7827 -0.2766 861  ALA B CB  
20933 N N   . VAL C 862  ? 2.1258 1.8529 2.2098 0.3233  -0.8102 -0.2682 862  VAL B N   
20934 C CA  . VAL C 862  ? 2.1695 1.8840 2.2475 0.3017  -0.8386 -0.2655 862  VAL B CA  
20935 C C   . VAL C 862  ? 2.1558 1.8563 2.2286 0.3057  -0.8742 -0.2637 862  VAL B C   
20936 O O   . VAL C 862  ? 2.1837 1.8551 2.2229 0.3134  -0.8752 -0.2632 862  VAL B O   
20937 C CB  . VAL C 862  ? 2.2136 1.8826 2.2363 0.2753  -0.8291 -0.2623 862  VAL B CB  
20938 C CG1 . VAL C 862  ? 2.2597 1.9136 2.2748 0.2522  -0.8614 -0.2590 862  VAL B CG1 
20939 C CG2 . VAL C 862  ? 2.2058 1.8886 2.2337 0.2704  -0.7947 -0.2640 862  VAL B CG2 
20940 N N   . GLU C 863  ? 2.1051 1.8252 2.2098 0.2992  -0.9036 -0.2623 863  GLU B N   
20941 C CA  . GLU C 863  ? 2.0718 1.7943 2.1903 0.3085  -0.9384 -0.2612 863  GLU B CA  
20942 C C   . GLU C 863  ? 2.0215 1.7019 2.0934 0.3147  -0.9467 -0.2608 863  GLU B C   
20943 O O   . GLU C 863  ? 1.9853 1.6788 2.0746 0.3366  -0.9549 -0.2624 863  GLU B O   
20944 C CB  . GLU C 863  ? 2.1281 1.8502 2.2567 0.2880  -0.9718 -0.2572 863  GLU B CB  
20945 C CG  . GLU C 863  ? 2.3327 2.1125 2.5338 0.2964  -0.9857 -0.2569 863  GLU B CG  
20946 C CD  . GLU C 863  ? 2.3448 2.1426 2.5778 0.3161  -1.0145 -0.2562 863  GLU B CD  
20947 O OE1 . GLU C 863  ? 2.3307 2.1243 2.5569 0.3380  -1.0072 -0.2591 863  GLU B OE1 
20948 O OE2 . GLU C 863  ? 2.3581 2.1745 2.6231 0.3098  -1.0444 -0.2524 863  GLU B OE2 
20949 N N   . GLY C 864  ? 2.0419 1.6706 2.0536 0.2952  -0.9443 -0.2585 864  GLY B N   
20950 C CA  . GLY C 864  ? 2.0477 1.6333 2.0143 0.2963  -0.9589 -0.2575 864  GLY B CA  
20951 C C   . GLY C 864  ? 2.0244 1.5930 1.9625 0.3100  -0.9322 -0.2588 864  GLY B C   
20952 O O   . GLY C 864  ? 2.0433 1.5717 1.9376 0.3088  -0.9395 -0.2577 864  GLY B O   
20953 N N   . ILE C 865  ? 1.9524 1.5520 1.9160 0.3230  -0.9016 -0.2608 865  ILE B N   
20954 C CA  . ILE C 865  ? 1.8965 1.4805 1.8327 0.3331  -0.8732 -0.2608 865  ILE B CA  
20955 C C   . ILE C 865  ? 1.8726 1.4934 1.8456 0.3610  -0.8624 -0.2636 865  ILE B C   
20956 O O   . ILE C 865  ? 1.8192 1.4827 1.8385 0.3705  -0.8511 -0.2661 865  ILE B O   
20957 C CB  . ILE C 865  ? 1.8606 1.4363 1.7790 0.3204  -0.8403 -0.2597 865  ILE B CB  
20958 C CG1 . ILE C 865  ? 1.8739 1.4181 1.7618 0.2918  -0.8499 -0.2570 865  ILE B CG1 
20959 C CG2 . ILE C 865  ? 1.8514 1.4000 1.7313 0.3265  -0.8152 -0.2577 865  ILE B CG2 
20960 C CD1 . ILE C 865  ? 1.8812 1.4088 1.7424 0.2783  -0.8173 -0.2553 865  ILE B CD1 
20961 N N   . CYS C 866  ? 1.9192 1.5208 1.8688 0.3732  -0.8656 -0.2631 866  CYS B N   
20962 C CA  . CYS C 866  ? 1.9629 1.5912 1.9378 0.3986  -0.8555 -0.2650 866  CYS B CA  
20963 C C   . CYS C 866  ? 2.0481 1.6872 2.0240 0.4041  -0.8179 -0.2647 866  CYS B C   
20964 O O   . CYS C 866  ? 2.0161 1.6324 1.9613 0.3895  -0.7987 -0.2623 866  CYS B O   
20965 C CB  . CYS C 866  ? 1.9433 1.5436 1.8868 0.4075  -0.8691 -0.2639 866  CYS B CB  
20966 S SG  . CYS C 866  ? 1.9788 1.5931 1.9491 0.4200  -0.9075 -0.2660 866  CYS B SG  
20967 N N   . THR C 867  ? 2.1607 1.8330 2.1709 0.4253  -0.8074 -0.2669 867  THR B N   
20968 C CA  . THR C 867  ? 2.2712 1.9576 2.2876 0.4324  -0.7732 -0.2668 867  THR B CA  
20969 C C   . THR C 867  ? 2.3958 2.1116 2.4439 0.4569  -0.7677 -0.2690 867  THR B C   
20970 O O   . THR C 867  ? 2.4246 2.1542 2.4953 0.4689  -0.7893 -0.2708 867  THR B O   
20971 C CB  . THR C 867  ? 2.1632 1.8695 2.2007 0.4207  -0.7559 -0.2685 867  THR B CB  
20972 O OG1 . THR C 867  ? 2.1587 1.8714 2.2124 0.4081  -0.7798 -0.2696 867  THR B OG1 
20973 C CG2 . THR C 867  ? 2.1541 1.8309 2.1508 0.4051  -0.7323 -0.2651 867  THR B CG2 
20974 N N   . SER C 868  ? 2.5520 2.2757 2.6002 0.4641  -0.7382 -0.2683 868  SER B N   
20975 C CA  . SER C 868  ? 2.6899 2.4338 2.7585 0.4860  -0.7292 -0.2694 868  SER B CA  
20976 C C   . SER C 868  ? 2.8444 2.6314 2.9673 0.4973  -0.7250 -0.2742 868  SER B C   
20977 O O   . SER C 868  ? 2.8323 2.6356 2.9751 0.5162  -0.7233 -0.2756 868  SER B O   
20978 C CB  . SER C 868  ? 2.6915 2.4241 2.7361 0.4883  -0.7002 -0.2658 868  SER B CB  
20979 O OG  . SER C 868  ? 2.7183 2.4122 2.7150 0.4765  -0.7012 -0.2607 868  SER B OG  
20980 N N   . GLU C 869  ? 3.0157 2.8196 3.1611 0.4854  -0.7223 -0.2766 869  GLU B N   
20981 C CA  . GLU C 869  ? 3.1451 2.9904 3.3439 0.4947  -0.7195 -0.2810 869  GLU B CA  
20982 C C   . GLU C 869  ? 3.2478 3.1057 3.4731 0.4993  -0.7516 -0.2819 869  GLU B C   
20983 O O   . GLU C 869  ? 3.2691 3.1047 3.4724 0.4882  -0.7756 -0.2797 869  GLU B O   
20984 C CB  . GLU C 869  ? 3.1794 3.0391 3.3922 0.4797  -0.7021 -0.2829 869  GLU B CB  
20985 C CG  . GLU C 869  ? 3.1686 3.0718 3.4368 0.4887  -0.6941 -0.2875 869  GLU B CG  
20986 C CD  . GLU C 869  ? 3.1739 3.0975 3.4766 0.4835  -0.7205 -0.2884 869  GLU B CD  
20987 O OE1 . GLU C 869  ? 3.1949 3.0978 3.4761 0.4680  -0.7423 -0.2857 869  GLU B OE1 
20988 O OE2 . GLU C 869  ? 3.1532 3.1130 3.5048 0.4947  -0.7194 -0.2914 869  GLU B OE2 
20989 N N   . SER C 870  ? 3.2986 3.1908 3.5703 0.5160  -0.7516 -0.2849 870  SER B N   
20990 C CA  . SER C 870  ? 3.3617 3.2684 3.6625 0.5241  -0.7806 -0.2850 870  SER B CA  
20991 C C   . SER C 870  ? 3.3960 3.3060 3.7069 0.5051  -0.8020 -0.2840 870  SER B C   
20992 O O   . SER C 870  ? 3.4044 3.3310 3.7331 0.4927  -0.7910 -0.2852 870  SER B O   
20993 C CB  . SER C 870  ? 3.3675 3.3124 3.7198 0.5446  -0.7719 -0.2880 870  SER B CB  
20994 O OG  . SER C 870  ? 3.3746 3.3482 3.7603 0.5383  -0.7539 -0.2907 870  SER B OG  
20995 N N   . LYS C 882  ? 2.7913 2.6866 3.0203 0.4652  -0.5951 -0.2895 882  LYS B N   
20996 C CA  . LYS C 882  ? 2.7797 2.6917 3.0264 0.4836  -0.5747 -0.2917 882  LYS B CA  
20997 C C   . LYS C 882  ? 2.7579 2.6627 2.9862 0.4786  -0.5421 -0.2913 882  LYS B C   
20998 O O   . LYS C 882  ? 2.7585 2.6351 2.9475 0.4665  -0.5355 -0.2868 882  LYS B O   
20999 C CB  . LYS C 882  ? 2.8075 2.7067 3.0405 0.5000  -0.5847 -0.2886 882  LYS B CB  
21000 C CG  . LYS C 882  ? 2.8319 2.6940 3.0142 0.4947  -0.5815 -0.2821 882  LYS B CG  
21001 C CD  . LYS C 882  ? 2.8420 2.6928 3.0120 0.5103  -0.5932 -0.2791 882  LYS B CD  
21002 C CE  . LYS C 882  ? 2.8658 2.7142 3.0416 0.5122  -0.6265 -0.2795 882  LYS B CE  
21003 N NZ  . LYS C 882  ? 2.8647 2.6984 3.0236 0.5260  -0.6388 -0.2766 882  LYS B NZ  
21004 N N   . CYS C 883  ? 2.7200 2.6488 2.9759 0.4881  -0.5214 -0.2957 883  CYS B N   
21005 C CA  . CYS C 883  ? 2.6900 2.6139 2.9315 0.4835  -0.4903 -0.2958 883  CYS B CA  
21006 C C   . CYS C 883  ? 2.6507 2.5570 2.8659 0.4939  -0.4751 -0.2911 883  CYS B C   
21007 O O   . CYS C 883  ? 2.6325 2.5517 2.8626 0.5063  -0.4581 -0.2934 883  CYS B O   
21008 C CB  . CYS C 883  ? 2.6843 2.6397 2.9645 0.4864  -0.4733 -0.3030 883  CYS B CB  
21009 S SG  . CYS C 883  ? 3.3761 3.3237 3.6363 0.4776  -0.4368 -0.3036 883  CYS B SG  
21010 N N   . VAL C 884  ? 2.6255 2.5015 2.8010 0.4880  -0.4808 -0.2842 884  VAL B N   
21011 C CA  . VAL C 884  ? 2.6111 2.4688 2.7591 0.4950  -0.4671 -0.2780 884  VAL B CA  
21012 C C   . VAL C 884  ? 2.6192 2.4706 2.7521 0.4873  -0.4371 -0.2764 884  VAL B C   
21013 O O   . VAL C 884  ? 2.6363 2.4642 2.7373 0.4745  -0.4315 -0.2713 884  VAL B O   
21014 C CB  . VAL C 884  ? 2.1519 1.9792 2.2636 0.4911  -0.4843 -0.2707 884  VAL B CB  
21015 C CG1 . VAL C 884  ? 2.1488 1.9804 2.2728 0.5004  -0.5133 -0.2721 884  VAL B CG1 
21016 C CG2 . VAL C 884  ? 2.1800 1.9867 2.2664 0.4712  -0.4868 -0.2686 884  VAL B CG2 
21017 N N   . ARG C 885  ? 2.6211 2.4918 2.7755 0.4952  -0.4171 -0.2805 885  ARG B N   
21018 C CA  . ARG C 885  ? 2.6161 2.4835 2.7598 0.4877  -0.3887 -0.2802 885  ARG B CA  
21019 C C   . ARG C 885  ? 2.5902 2.4381 2.7047 0.4917  -0.3718 -0.2719 885  ARG B C   
21020 O O   . ARG C 885  ? 2.5720 2.4234 2.6908 0.5052  -0.3683 -0.2699 885  ARG B O   
21021 C CB  . ARG C 885  ? 2.6054 2.5004 2.7833 0.4916  -0.3733 -0.2889 885  ARG B CB  
21022 C CG  . ARG C 885  ? 2.5914 2.5012 2.7914 0.5098  -0.3707 -0.2913 885  ARG B CG  
21023 C CD  . ARG C 885  ? 2.5912 2.5219 2.8169 0.5119  -0.3489 -0.2990 885  ARG B CD  
21024 N NE  . ARG C 885  ? 2.6095 2.5598 2.8613 0.5025  -0.3537 -0.3063 885  ARG B NE  
21025 C CZ  . ARG C 885  ? 2.6207 2.5891 2.8940 0.5001  -0.3354 -0.3134 885  ARG B CZ  
21026 N NH1 . ARG C 885  ? 2.6209 2.5885 2.8912 0.5067  -0.3111 -0.3147 885  ARG B NH1 
21027 N NH2 . ARG C 885  ? 2.6258 2.6124 2.9229 0.4906  -0.3418 -0.3191 885  ARG B NH2 
21028 N N   . GLN C 886  ? 2.6060 2.4326 2.6903 0.4792  -0.3611 -0.2664 886  GLN B N   
21029 C CA  . GLN C 886  ? 2.6116 2.4178 2.6666 0.4811  -0.3468 -0.2567 886  GLN B CA  
21030 C C   . GLN C 886  ? 2.5756 2.3826 2.6260 0.4774  -0.3164 -0.2565 886  GLN B C   
21031 O O   . GLN C 886  ? 2.5690 2.3929 2.6394 0.4742  -0.3070 -0.2648 886  GLN B O   
21032 C CB  . GLN C 886  ? 2.7149 2.4930 2.7367 0.4702  -0.3565 -0.2495 886  GLN B CB  
21033 C CG  . GLN C 886  ? 2.7888 2.5469 2.7839 0.4747  -0.3504 -0.2383 886  GLN B CG  
21034 C CD  . GLN C 886  ? 2.8406 2.5989 2.8385 0.4859  -0.3723 -0.2358 886  GLN B CD  
21035 O OE1 . GLN C 886  ? 2.8780 2.6201 2.8545 0.4891  -0.3720 -0.2264 886  GLN B OE1 
21036 N NE2 . GLN C 886  ? 2.8372 2.6135 2.8612 0.4919  -0.3912 -0.2439 886  GLN B NE2 
21037 N N   . LYS C 887  ? 2.5395 2.3279 2.5636 0.4775  -0.3011 -0.2467 887  LYS B N   
21038 C CA  . LYS C 887  ? 2.5164 2.3027 2.5328 0.4745  -0.2718 -0.2451 887  LYS B CA  
21039 C C   . LYS C 887  ? 2.4993 2.2575 2.4797 0.4644  -0.2606 -0.2353 887  LYS B C   
21040 O O   . LYS C 887  ? 2.4482 2.1905 2.4101 0.4676  -0.2652 -0.2253 887  LYS B O   
21041 C CB  . LYS C 887  ? 2.5178 2.3121 2.5419 0.4881  -0.2594 -0.2417 887  LYS B CB  
21042 C CG  . LYS C 887  ? 2.5140 2.3290 2.5670 0.5009  -0.2725 -0.2483 887  LYS B CG  
21043 C CD  . LYS C 887  ? 2.5189 2.3266 2.5658 0.5083  -0.2957 -0.2426 887  LYS B CD  
21044 C CE  . LYS C 887  ? 2.5095 2.3346 2.5821 0.5215  -0.3074 -0.2485 887  LYS B CE  
21045 N NZ  . LYS C 887  ? 2.4945 2.3222 2.5689 0.5313  -0.2919 -0.2455 887  LYS B NZ  
21046 N N   . VAL C 888  ? 2.5215 2.2725 2.4913 0.4520  -0.2455 -0.2378 888  VAL B N   
21047 C CA  . VAL C 888  ? 2.5332 2.2554 2.4674 0.4423  -0.2310 -0.2286 888  VAL B CA  
21048 C C   . VAL C 888  ? 2.5746 2.2939 2.5006 0.4453  -0.2010 -0.2234 888  VAL B C   
21049 O O   . VAL C 888  ? 2.6143 2.3436 2.5488 0.4423  -0.1848 -0.2301 888  VAL B O   
21050 C CB  . VAL C 888  ? 2.5068 2.2168 2.4272 0.4252  -0.2303 -0.2332 888  VAL B CB  
21051 C CG1 . VAL C 888  ? 2.5005 2.1895 2.4017 0.4170  -0.2522 -0.2298 888  VAL B CG1 
21052 C CG2 . VAL C 888  ? 2.4804 2.2163 2.4306 0.4227  -0.2340 -0.2462 888  VAL B CG2 
21053 N N   . GLU C 889  ? 2.5997 2.3049 2.5086 0.4508  -0.1935 -0.2109 889  GLU B N   
21054 C CA  . GLU C 889  ? 2.6714 2.3716 2.5706 0.4537  -0.1652 -0.2038 889  GLU B CA  
21055 C C   . GLU C 889  ? 2.6565 2.3395 2.5337 0.4406  -0.1444 -0.2045 889  GLU B C   
21056 O O   . GLU C 889  ? 2.6382 2.3013 2.4948 0.4290  -0.1504 -0.2038 889  GLU B O   
21057 C CB  . GLU C 889  ? 2.7992 2.4868 2.6842 0.4609  -0.1629 -0.1886 889  GLU B CB  
21058 C CG  . GLU C 889  ? 2.9600 2.6205 2.8172 0.4532  -0.1696 -0.1800 889  GLU B CG  
21059 C CD  . GLU C 889  ? 3.0693 2.7300 2.9307 0.4526  -0.2009 -0.1839 889  GLU B CD  
21060 O OE1 . GLU C 889  ? 3.0958 2.7786 2.9828 0.4595  -0.2180 -0.1922 889  GLU B OE1 
21061 O OE2 . GLU C 889  ? 3.1210 2.7581 2.9589 0.4454  -0.2079 -0.1783 889  GLU B OE2 
21062 N N   . GLY C 890  ? 2.6641 2.3528 2.5437 0.4419  -0.1201 -0.2061 890  GLY B N   
21063 C CA  . GLY C 890  ? 2.6413 2.3160 2.5018 0.4298  -0.0998 -0.2087 890  GLY B CA  
21064 C C   . GLY C 890  ? 2.5729 2.2142 2.3965 0.4216  -0.0890 -0.1975 890  GLY B C   
21065 O O   . GLY C 890  ? 2.5538 2.1842 2.3669 0.4283  -0.0847 -0.1847 890  GLY B O   
21066 N N   . SER C 891  ? 2.5140 2.1383 2.3176 0.4066  -0.0843 -0.2018 891  SER B N   
21067 C CA  . SER C 891  ? 2.4690 2.0568 2.2333 0.3970  -0.0719 -0.1920 891  SER B CA  
21068 C C   . SER C 891  ? 2.4479 2.0203 2.2012 0.3986  -0.0891 -0.1830 891  SER B C   
21069 O O   . SER C 891  ? 2.4675 2.0145 2.1949 0.3984  -0.0750 -0.1704 891  SER B O   
21070 C CB  . SER C 891  ? 2.4505 2.0265 2.1988 0.4016  -0.0392 -0.1823 891  SER B CB  
21071 O OG  . SER C 891  ? 2.4508 2.0390 2.2068 0.3998  -0.0228 -0.1910 891  SER B OG  
21072 N N   . SER C 892  ? 2.3959 1.9833 2.1688 0.4002  -0.1189 -0.1894 892  SER B N   
21073 C CA  . SER C 892  ? 2.3737 1.9491 2.1388 0.4024  -0.1383 -0.1824 892  SER B CA  
21074 C C   . SER C 892  ? 2.3648 1.9414 2.1349 0.3940  -0.1680 -0.1916 892  SER B C   
21075 O O   . SER C 892  ? 2.3494 1.9238 2.1161 0.3817  -0.1697 -0.2001 892  SER B O   
21076 C CB  . SER C 892  ? 2.3411 1.9375 2.1294 0.4192  -0.1454 -0.1773 892  SER B CB  
21077 O OG  . SER C 892  ? 2.3359 1.9305 2.1196 0.4268  -0.1200 -0.1669 892  SER B OG  
21078 N N   . SER C 893  ? 2.3652 1.9454 2.1432 0.4003  -0.1917 -0.1896 893  SER B N   
21079 C CA  . SER C 893  ? 2.3743 1.9554 2.1575 0.3939  -0.2219 -0.1972 893  SER B CA  
21080 C C   . SER C 893  ? 2.3656 1.9599 2.1662 0.4057  -0.2465 -0.1963 893  SER B C   
21081 O O   . SER C 893  ? 2.3755 1.9603 2.1660 0.4129  -0.2438 -0.1862 893  SER B O   
21082 C CB  . SER C 893  ? 2.3849 1.9273 2.1297 0.3782  -0.2242 -0.1931 893  SER B CB  
21083 O OG  . SER C 893  ? 2.3827 1.9254 2.1324 0.3713  -0.2544 -0.2003 893  SER B OG  
21084 N N   . HIS C 894  ? 2.3924 2.0082 2.2189 0.4073  -0.2705 -0.2066 894  HIS B N   
21085 C CA  . HIS C 894  ? 2.4981 2.1255 2.3401 0.4182  -0.2953 -0.2068 894  HIS B CA  
21086 C C   . HIS C 894  ? 2.2917 1.9027 2.1213 0.4097  -0.3226 -0.2089 894  HIS B C   
21087 O O   . HIS C 894  ? 2.2701 1.8866 2.1086 0.4012  -0.3361 -0.2174 894  HIS B O   
21088 C CB  . HIS C 894  ? 2.9483 2.6124 2.8304 0.4294  -0.3032 -0.2160 894  HIS B CB  
21089 C CG  . HIS C 894  ? 3.5381 3.2148 3.4329 0.4457  -0.3061 -0.2115 894  HIS B CG  
21090 N ND1 . HIS C 894  ? 3.8354 3.5341 3.7570 0.4564  -0.3257 -0.2175 894  HIS B ND1 
21091 C CD2 . HIS C 894  ? 3.8056 3.4746 3.6884 0.4526  -0.2917 -0.2005 894  HIS B CD2 
21092 C CE1 . HIS C 894  ? 4.0831 3.7856 4.0066 0.4684  -0.3233 -0.2109 894  HIS B CE1 
21093 N NE2 . HIS C 894  ? 3.9665 3.6523 3.8678 0.4661  -0.3033 -0.2004 894  HIS B NE2 
21094 N N   . LEU C 895  ? 2.1925 1.7837 2.0024 0.4121  -0.3314 -0.2008 895  LEU B N   
21095 C CA  . LEU C 895  ? 2.1197 1.6933 1.9160 0.4051  -0.3584 -0.2024 895  LEU B CA  
21096 C C   . LEU C 895  ? 2.0002 1.5993 1.8273 0.4087  -0.3844 -0.2132 895  LEU B C   
21097 O O   . LEU C 895  ? 1.9760 1.6055 1.8348 0.4219  -0.3861 -0.2173 895  LEU B O   
21098 C CB  . LEU C 895  ? 2.1566 1.7158 1.9377 0.4123  -0.3661 -0.1936 895  LEU B CB  
21099 C CG  . LEU C 895  ? 2.2119 1.7299 1.9513 0.4005  -0.3598 -0.1852 895  LEU B CG  
21100 C CD1 . LEU C 895  ? 2.2152 1.7255 1.9437 0.4094  -0.3463 -0.1729 895  LEU B CD1 
21101 C CD2 . LEU C 895  ? 2.2313 1.7294 1.9555 0.3916  -0.3890 -0.1891 895  LEU B CD2 
21102 N N   . VAL C 896  ? 1.8975 1.4827 1.7148 0.3967  -0.4047 -0.2173 896  VAL B N   
21103 C CA  . VAL C 896  ? 1.7812 1.3883 1.6269 0.3999  -0.4320 -0.2261 896  VAL B CA  
21104 C C   . VAL C 896  ? 1.7681 1.3493 1.5908 0.3947  -0.4572 -0.2239 896  VAL B C   
21105 O O   . VAL C 896  ? 1.7988 1.3446 1.5837 0.3847  -0.4514 -0.2172 896  VAL B O   
21106 C CB  . VAL C 896  ? 1.7225 1.3396 1.5811 0.3876  -0.4339 -0.2338 896  VAL B CB  
21107 C CG1 . VAL C 896  ? 1.7037 1.3530 1.6020 0.3950  -0.4574 -0.2423 896  VAL B CG1 
21108 C CG2 . VAL C 896  ? 1.6936 1.3217 1.5583 0.3864  -0.4037 -0.2345 896  VAL B CG2 
21109 N N   . THR C 897  ? 1.7043 1.3015 1.5487 0.4020  -0.4845 -0.2292 897  THR B N   
21110 C CA  . THR C 897  ? 1.6699 1.2437 1.4945 0.3964  -0.5116 -0.2286 897  THR B CA  
21111 C C   . THR C 897  ? 1.6820 1.2804 1.5390 0.4020  -0.5399 -0.2366 897  THR B C   
21112 O O   . THR C 897  ? 1.6781 1.3119 1.5731 0.4139  -0.5380 -0.2415 897  THR B O   
21113 C CB  . THR C 897  ? 1.6260 1.1840 1.4314 0.4055  -0.5146 -0.2217 897  THR B CB  
21114 O OG1 . THR C 897  ? 1.6206 1.1921 1.4438 0.4162  -0.5419 -0.2259 897  THR B OG1 
21115 C CG2 . THR C 897  ? 1.5972 1.1678 1.4091 0.4170  -0.4888 -0.2163 897  THR B CG2 
21116 N N   . PHE C 898  ? 1.7025 1.2802 1.5433 0.3931  -0.5659 -0.2374 898  PHE B N   
21117 C CA  . PHE C 898  ? 1.6816 1.2772 1.5485 0.3984  -0.5963 -0.2434 898  PHE B CA  
21118 C C   . PHE C 898  ? 1.6740 1.2362 1.5088 0.3936  -0.6198 -0.2407 898  PHE B C   
21119 O O   . PHE C 898  ? 1.6880 1.2129 1.4829 0.3792  -0.6160 -0.2362 898  PHE B O   
21120 C CB  . PHE C 898  ? 1.6756 1.2844 1.5620 0.3862  -0.6054 -0.2489 898  PHE B CB  
21121 C CG  . PHE C 898  ? 1.6493 1.2873 1.5636 0.3876  -0.5819 -0.2521 898  PHE B CG  
21122 C CD1 . PHE C 898  ? 1.6275 1.3059 1.5891 0.3976  -0.5883 -0.2584 898  PHE B CD1 
21123 C CD2 . PHE C 898  ? 1.6553 1.2791 1.5478 0.3787  -0.5530 -0.2486 898  PHE B CD2 
21124 C CE1 . PHE C 898  ? 1.6214 1.3253 1.6075 0.3983  -0.5667 -0.2618 898  PHE B CE1 
21125 C CE2 . PHE C 898  ? 1.6490 1.2980 1.5650 0.3796  -0.5317 -0.2520 898  PHE B CE2 
21126 C CZ  . PHE C 898  ? 1.6353 1.3244 1.5980 0.3891  -0.5387 -0.2588 898  PHE B CZ  
21127 N N   . THR C 899  ? 1.6631 1.2369 1.5139 0.4057  -0.6436 -0.2434 899  THR B N   
21128 C CA  . THR C 899  ? 1.6463 1.1903 1.4699 0.4003  -0.6699 -0.2424 899  THR B CA  
21129 C C   . THR C 899  ? 1.6091 1.1647 1.4545 0.3947  -0.6981 -0.2481 899  THR B C   
21130 O O   . THR C 899  ? 1.5691 1.1626 1.4578 0.4043  -0.7016 -0.2528 899  THR B O   
21131 C CB  . THR C 899  ? 1.6892 1.2305 1.5063 0.4166  -0.6765 -0.2400 899  THR B CB  
21132 O OG1 . THR C 899  ? 1.6687 1.2469 1.5267 0.4345  -0.6852 -0.2446 899  THR B OG1 
21133 C CG2 . THR C 899  ? 1.6028 1.1338 1.3998 0.4198  -0.6472 -0.2328 899  THR B CG2 
21134 N N   . VAL C 900  ? 1.6387 1.1607 1.4535 0.3780  -0.7164 -0.2472 900  VAL B N   
21135 C CA  . VAL C 900  ? 1.6288 1.1548 1.4577 0.3698  -0.7469 -0.2511 900  VAL B CA  
21136 C C   . VAL C 900  ? 1.6290 1.1169 1.4222 0.3635  -0.7731 -0.2497 900  VAL B C   
21137 O O   . VAL C 900  ? 1.6205 1.0804 1.3796 0.3659  -0.7672 -0.2461 900  VAL B O   
21138 C CB  . VAL C 900  ? 1.4279 0.9480 1.2534 0.3482  -0.7434 -0.2515 900  VAL B CB  
21139 C CG1 . VAL C 900  ? 1.4165 0.9841 1.2934 0.3537  -0.7365 -0.2557 900  VAL B CG1 
21140 C CG2 . VAL C 900  ? 1.4295 0.9145 1.2115 0.3339  -0.7163 -0.2466 900  VAL B CG2 
21141 N N   . LEU C 901  ? 1.6440 1.1304 1.4448 0.3551  -0.8025 -0.2523 901  LEU B N   
21142 C CA  . LEU C 901  ? 1.7192 1.1681 1.4856 0.3484  -0.8295 -0.2515 901  LEU B CA  
21143 C C   . LEU C 901  ? 1.8204 1.2701 1.5988 0.3367  -0.8617 -0.2537 901  LEU B C   
21144 O O   . LEU C 901  ? 1.8159 1.2986 1.6350 0.3490  -0.8817 -0.2568 901  LEU B O   
21145 C CB  . LEU C 901  ? 1.6875 1.1407 1.4559 0.3688  -0.8379 -0.2520 901  LEU B CB  
21146 C CG  . LEU C 901  ? 1.6959 1.1292 1.4505 0.3692  -0.8733 -0.2536 901  LEU B CG  
21147 C CD1 . LEU C 901  ? 1.6989 1.1045 1.4181 0.3767  -0.8712 -0.2514 901  LEU B CD1 
21148 C CD2 . LEU C 901  ? 1.6832 1.1586 1.4884 0.3851  -0.8931 -0.2576 901  LEU B CD2 
21149 N N   . PRO C 902  ? 1.8465 1.2586 1.5886 0.3125  -0.8666 -0.2515 902  PRO B N   
21150 C CA  . PRO C 902  ? 1.8952 1.3104 1.6506 0.2985  -0.8945 -0.2525 902  PRO B CA  
21151 C C   . PRO C 902  ? 1.9336 1.3227 1.6697 0.2968  -0.9301 -0.2529 902  PRO B C   
21152 O O   . PRO C 902  ? 1.9552 1.3033 1.6461 0.2947  -0.9302 -0.2515 902  PRO B O   
21153 C CB  . PRO C 902  ? 1.9086 1.2891 1.6262 0.2726  -0.8808 -0.2494 902  PRO B CB  
21154 C CG  . PRO C 902  ? 1.8576 1.2189 1.5446 0.2757  -0.8438 -0.2466 902  PRO B CG  
21155 C CD  . PRO C 902  ? 1.8497 1.2147 1.5377 0.2964  -0.8463 -0.2473 902  PRO B CD  
21156 N N   . LEU C 903  ? 1.9664 1.3800 1.7378 0.2985  -0.9597 -0.2546 903  LEU B N   
21157 C CA  . LEU C 903  ? 2.0190 1.4071 1.7728 0.2943  -0.9967 -0.2547 903  LEU B CA  
21158 C C   . LEU C 903  ? 2.0624 1.4294 1.8028 0.2679  -1.0180 -0.2524 903  LEU B C   
21159 O O   . LEU C 903  ? 2.1080 1.4326 1.8104 0.2540  -1.0425 -0.2513 903  LEU B O   
21160 C CB  . LEU C 903  ? 1.9916 1.4205 1.7938 0.3177  -1.0177 -0.2574 903  LEU B CB  
21161 C CG  . LEU C 903  ? 1.9289 1.3931 1.7612 0.3458  -0.9988 -0.2598 903  LEU B CG  
21162 C CD1 . LEU C 903  ? 1.9362 1.3665 1.7234 0.3514  -0.9851 -0.2593 903  LEU B CD1 
21163 C CD2 . LEU C 903  ? 1.8883 1.3948 1.7600 0.3517  -0.9689 -0.2604 903  LEU B CD2 
21164 N N   . GLU C 904  ? 2.0674 1.4636 1.8385 0.2602  -1.0083 -0.2517 904  GLU B N   
21165 C CA  . GLU C 904  ? 2.1485 1.5265 1.9075 0.2339  -1.0262 -0.2489 904  GLU B CA  
21166 C C   . GLU C 904  ? 2.1778 1.5038 1.8766 0.2106  -1.0051 -0.2461 904  GLU B C   
21167 O O   . GLU C 904  ? 2.1168 1.4497 1.8133 0.2115  -0.9700 -0.2460 904  GLU B O   
21168 C CB  . GLU C 904  ? 2.2229 1.6557 2.0426 0.2350  -1.0280 -0.2490 904  GLU B CB  
21169 C CG  . GLU C 904  ? 2.2624 1.7450 2.1420 0.2586  -1.0482 -0.2510 904  GLU B CG  
21170 C CD  . GLU C 904  ? 2.3319 1.8549 2.2631 0.2520  -1.0666 -0.2492 904  GLU B CD  
21171 O OE1 . GLU C 904  ? 2.3789 1.8991 2.3050 0.2312  -1.0579 -0.2470 904  GLU B OE1 
21172 O OE2 . GLU C 904  ? 2.3424 1.8995 2.3190 0.2675  -1.0894 -0.2494 904  GLU B OE2 
21173 N N   . ILE C 905  ? 2.1921 1.4644 1.8411 0.1901  -1.0266 -0.2438 905  ILE B N   
21174 C CA  . ILE C 905  ? 2.1299 1.3432 1.7140 0.1675  -1.0094 -0.2408 905  ILE B CA  
21175 C C   . ILE C 905  ? 2.0975 1.3163 1.6855 0.1479  -0.9978 -0.2383 905  ILE B C   
21176 O O   . ILE C 905  ? 1.9281 1.1859 1.5612 0.1458  -1.0148 -0.2383 905  ILE B O   
21177 C CB  . ILE C 905  ? 1.9040 1.0561 1.4332 0.1498  -1.0379 -0.2391 905  ILE B CB  
21178 C CG1 . ILE C 905  ? 1.9061 1.0637 1.4448 0.1698  -1.0601 -0.2422 905  ILE B CG1 
21179 C CG2 . ILE C 905  ? 1.8900 0.9784 1.3493 0.1332  -1.0141 -0.2365 905  ILE B CG2 
21180 C CD1 . ILE C 905  ? 1.9281 1.0264 1.4044 0.1664  -1.0565 -0.2421 905  ILE B CD1 
21181 N N   . GLY C 906  ? 2.1836 1.3649 1.7258 0.1347  -0.9675 -0.2360 906  GLY B N   
21182 C CA  . GLY C 906  ? 2.2970 1.4723 1.8297 0.1135  -0.9530 -0.2333 906  GLY B CA  
21183 C C   . GLY C 906  ? 2.2910 1.5278 1.8809 0.1253  -0.9333 -0.2353 906  GLY B C   
21184 O O   . GLY C 906  ? 2.2854 1.5172 1.8624 0.1162  -0.9043 -0.2340 906  GLY B O   
21185 N N   . LEU C 907  ? 2.3188 1.6117 1.9704 0.1460  -0.9490 -0.2386 907  LEU B N   
21186 C CA  . LEU C 907  ? 2.3229 1.6791 2.0361 0.1601  -0.9341 -0.2412 907  LEU B CA  
21187 C C   . LEU C 907  ? 2.3367 1.6956 2.0406 0.1656  -0.8900 -0.2418 907  LEU B C   
21188 O O   . LEU C 907  ? 2.3271 1.6590 1.9975 0.1730  -0.8699 -0.2413 907  LEU B O   
21189 C CB  . LEU C 907  ? 2.3094 1.7138 2.0768 0.1891  -0.9466 -0.2449 907  LEU B CB  
21190 C CG  . LEU C 907  ? 2.3420 1.8075 2.1687 0.2068  -0.9257 -0.2480 907  LEU B CG  
21191 C CD1 . LEU C 907  ? 2.3670 1.8583 2.2231 0.1907  -0.9311 -0.2469 907  LEU B CD1 
21192 C CD2 . LEU C 907  ? 2.3613 1.8666 2.2350 0.2338  -0.9403 -0.2511 907  LEU B CD2 
21193 N N   . HIS C 908  ? 2.3789 1.7724 2.1146 0.1627  -0.8747 -0.2428 908  HIS B N   
21194 C CA  . HIS C 908  ? 2.4265 1.8159 2.1465 0.1636  -0.8336 -0.2428 908  HIS B CA  
21195 C C   . HIS C 908  ? 2.3790 1.8305 2.1599 0.1795  -0.8183 -0.2467 908  HIS B C   
21196 O O   . HIS C 908  ? 2.3755 1.8716 2.2093 0.1943  -0.8370 -0.2495 908  HIS B O   
21197 C CB  . HIS C 908  ? 2.4852 1.8310 2.1567 0.1335  -0.8248 -0.2389 908  HIS B CB  
21198 C CG  . HIS C 908  ? 2.4852 1.7793 2.1112 0.1107  -0.8543 -0.2351 908  HIS B CG  
21199 N ND1 . HIS C 908  ? 2.4512 1.7579 2.1010 0.1071  -0.8950 -0.2351 908  HIS B ND1 
21200 C CD2 . HIS C 908  ? 2.4959 1.7242 2.0533 0.0896  -0.8485 -0.2309 908  HIS B CD2 
21201 C CE1 . HIS C 908  ? 2.4870 1.7373 2.0839 0.0845  -0.9140 -0.2313 908  HIS B CE1 
21202 N NE2 . HIS C 908  ? 2.5123 1.7134 2.0517 0.0734  -0.8860 -0.2289 908  HIS B NE2 
21203 N N   . ASN C 909  ? 2.3421 1.7942 2.1137 0.1764  -0.7835 -0.2468 909  ASN B N   
21204 C CA  . ASN C 909  ? 2.3054 1.8107 2.1283 0.1872  -0.7659 -0.2506 909  ASN B CA  
21205 C C   . ASN C 909  ? 2.1997 1.7456 2.0637 0.2181  -0.7539 -0.2545 909  ASN B C   
21206 O O   . ASN C 909  ? 2.1651 1.7310 2.0574 0.2337  -0.7760 -0.2561 909  ASN B O   
21207 C CB  . ASN C 909  ? 2.3676 1.9060 2.2319 0.1767  -0.7906 -0.2515 909  ASN B CB  
21208 C CG  . ASN C 909  ? 2.3983 1.9946 2.3205 0.1900  -0.7739 -0.2560 909  ASN B CG  
21209 O OD1 . ASN C 909  ? 2.4017 2.0428 2.3789 0.1998  -0.7928 -0.2581 909  ASN B OD1 
21210 N ND2 . ASN C 909  ? 2.4189 2.0139 2.3289 0.1910  -0.7374 -0.2573 909  ASN B ND2 
21211 N N   . ILE C 910  ? 2.1446 1.7004 2.0096 0.2262  -0.7183 -0.2558 910  ILE B N   
21212 C CA  . ILE C 910  ? 2.0343 1.6291 1.9377 0.2530  -0.7026 -0.2594 910  ILE B CA  
21213 C C   . ILE C 910  ? 2.0408 1.6552 1.9563 0.2515  -0.6697 -0.2615 910  ILE B C   
21214 O O   . ILE C 910  ? 2.1208 1.7038 1.9953 0.2402  -0.6455 -0.2587 910  ILE B O   
21215 C CB  . ILE C 910  ? 1.9208 1.4903 1.7942 0.2666  -0.6921 -0.2570 910  ILE B CB  
21216 C CG1 . ILE C 910  ? 1.8702 1.4231 1.7345 0.2698  -0.7251 -0.2558 910  ILE B CG1 
21217 C CG2 . ILE C 910  ? 1.8643 1.4697 1.7710 0.2912  -0.6708 -0.2598 910  ILE B CG2 
21218 C CD1 . ILE C 910  ? 1.8295 1.3629 1.6701 0.2848  -0.7175 -0.2538 910  ILE B CD1 
21219 N N   . ASN C 911  ? 1.9627 1.6274 1.9335 0.2618  -0.6690 -0.2662 911  ASN B N   
21220 C CA  . ASN C 911  ? 1.8865 1.5734 1.8729 0.2627  -0.6380 -0.2692 911  ASN B CA  
21221 C C   . ASN C 911  ? 1.8928 1.5858 1.8799 0.2849  -0.6118 -0.2700 911  ASN B C   
21222 O O   . ASN C 911  ? 1.8739 1.5787 1.8779 0.3039  -0.6220 -0.2705 911  ASN B O   
21223 C CB  . ASN C 911  ? 1.8543 1.5929 1.9009 0.2660  -0.6465 -0.2740 911  ASN B CB  
21224 C CG  . ASN C 911  ? 1.8953 1.6323 1.9460 0.2426  -0.6736 -0.2723 911  ASN B CG  
21225 O OD1 . ASN C 911  ? 1.9335 1.6731 1.9969 0.2422  -0.7066 -0.2707 911  ASN B OD1 
21226 N ND2 . ASN C 911  ? 1.8711 1.6064 1.9137 0.2237  -0.6600 -0.2726 911  ASN B ND2 
21227 N N   . PHE C 912  ? 1.9209 1.6045 1.8883 0.2821  -0.5786 -0.2695 912  PHE B N   
21228 C CA  . PHE C 912  ? 1.8996 1.5924 1.8714 0.3022  -0.5530 -0.2698 912  PHE B CA  
21229 C C   . PHE C 912  ? 1.9340 1.6569 1.9326 0.3044  -0.5279 -0.2745 912  PHE B C   
21230 O O   . PHE C 912  ? 1.9767 1.6931 1.9644 0.2866  -0.5192 -0.2751 912  PHE B O   
21231 C CB  . PHE C 912  ? 1.8464 1.4944 1.7641 0.2982  -0.5349 -0.2634 912  PHE B CB  
21232 C CG  . PHE C 912  ? 1.7772 1.4000 1.6726 0.3032  -0.5542 -0.2593 912  PHE B CG  
21233 C CD1 . PHE C 912  ? 1.7153 1.3584 1.6352 0.3245  -0.5632 -0.2604 912  PHE B CD1 
21234 C CD2 . PHE C 912  ? 1.7857 1.3625 1.6337 0.2859  -0.5631 -0.2544 912  PHE B CD2 
21235 C CE1 . PHE C 912  ? 1.6941 1.3134 1.5921 0.3285  -0.5812 -0.2568 912  PHE B CE1 
21236 C CE2 . PHE C 912  ? 1.7610 1.3136 1.5877 0.2903  -0.5809 -0.2511 912  PHE B CE2 
21237 C CZ  . PHE C 912  ? 1.7113 1.2861 1.5635 0.3115  -0.5900 -0.2524 912  PHE B CZ  
21238 N N   . SER C 913  ? 1.9320 1.6860 1.9638 0.3257  -0.5161 -0.2779 913  SER B N   
21239 C CA  . SER C 913  ? 1.9640 1.7487 2.0250 0.3294  -0.4933 -0.2832 913  SER B CA  
21240 C C   . SER C 913  ? 2.0151 1.8019 2.0726 0.3467  -0.4657 -0.2826 913  SER B C   
21241 O O   . SER C 913  ? 2.0018 1.7816 2.0532 0.3608  -0.4705 -0.2794 913  SER B O   
21242 C CB  . SER C 913  ? 1.9213 1.7508 2.0396 0.3381  -0.5109 -0.2891 913  SER B CB  
21243 O OG  . SER C 913  ? 1.8949 1.7554 2.0444 0.3428  -0.4892 -0.2949 913  SER B OG  
21244 N N   . LEU C 914  ? 2.0900 1.8853 2.1498 0.3451  -0.4373 -0.2852 914  LEU B N   
21245 C CA  . LEU C 914  ? 2.1216 1.9268 2.1883 0.3630  -0.4134 -0.2856 914  LEU B CA  
21246 C C   . LEU C 914  ? 2.2327 2.0707 2.3335 0.3671  -0.3947 -0.2930 914  LEU B C   
21247 O O   . LEU C 914  ? 2.2663 2.1129 2.3752 0.3528  -0.3928 -0.2969 914  LEU B O   
21248 C CB  . LEU C 914  ? 2.0531 1.8231 2.0735 0.3605  -0.3915 -0.2784 914  LEU B CB  
21249 C CG  . LEU C 914  ? 1.9964 1.7387 1.9795 0.3411  -0.3730 -0.2758 914  LEU B CG  
21250 C CD1 . LEU C 914  ? 1.9657 1.7292 1.9690 0.3314  -0.3629 -0.2829 914  LEU B CD1 
21251 C CD2 . LEU C 914  ? 1.9622 1.6831 1.9152 0.3472  -0.3448 -0.2694 914  LEU B CD2 
21252 N N   . GLU C 915  ? 2.2994 2.1541 2.4188 0.3859  -0.3810 -0.2947 915  GLU B N   
21253 C CA  . GLU C 915  ? 2.3747 2.2606 2.5287 0.3921  -0.3643 -0.3023 915  GLU B CA  
21254 C C   . GLU C 915  ? 2.4488 2.3287 2.5889 0.3998  -0.3325 -0.3015 915  GLU B C   
21255 O O   . GLU C 915  ? 2.4035 2.2754 2.5346 0.4135  -0.3284 -0.2971 915  GLU B O   
21256 C CB  . GLU C 915  ? 2.3906 2.3095 2.5915 0.4083  -0.3806 -0.3071 915  GLU B CB  
21257 C CG  . GLU C 915  ? 2.4321 2.3696 2.6615 0.4004  -0.4073 -0.3101 915  GLU B CG  
21258 C CD  . GLU C 915  ? 2.4748 2.4013 2.6984 0.4034  -0.4380 -0.3054 915  GLU B CD  
21259 O OE1 . GLU C 915  ? 2.4722 2.3926 2.6907 0.4191  -0.4410 -0.3025 915  GLU B OE1 
21260 O OE2 . GLU C 915  ? 2.5141 2.4377 2.7377 0.3895  -0.4598 -0.3044 915  GLU B OE2 
21261 N N   . THR C 916  ? 2.5527 2.4362 2.6910 0.3903  -0.3109 -0.3056 916  THR B N   
21262 C CA  . THR C 916  ? 2.6481 2.5276 2.7755 0.3962  -0.2800 -0.3057 916  THR B CA  
21263 C C   . THR C 916  ? 2.7623 2.6702 2.9217 0.3960  -0.2663 -0.3154 916  THR B C   
21264 O O   . THR C 916  ? 2.7709 2.6924 2.9469 0.3841  -0.2750 -0.3203 916  THR B O   
21265 C CB  . THR C 916  ? 2.6380 2.4833 2.7180 0.3828  -0.2621 -0.2994 916  THR B CB  
21266 O OG1 . THR C 916  ? 2.6307 2.4491 2.6815 0.3837  -0.2734 -0.2901 916  THR B OG1 
21267 C CG2 . THR C 916  ? 2.6206 2.4629 2.6909 0.3892  -0.2301 -0.2993 916  THR B CG2 
21268 N N   . TRP C 917  ? 2.8623 2.7783 3.0299 0.4089  -0.2454 -0.3178 917  TRP B N   
21269 C CA  . TRP C 917  ? 2.9714 2.9127 3.1688 0.4111  -0.2298 -0.3273 917  TRP B CA  
21270 C C   . TRP C 917  ? 3.0310 2.9773 3.2294 0.3918  -0.2263 -0.3323 917  TRP B C   
21271 O O   . TRP C 917  ? 3.0147 2.9891 3.2498 0.3902  -0.2325 -0.3397 917  TRP B O   
21272 C CB  . TRP C 917  ? 3.0257 2.9583 3.2083 0.4193  -0.2007 -0.3269 917  TRP B CB  
21273 C CG  . TRP C 917  ? 3.0714 3.0287 3.2877 0.4314  -0.1889 -0.3352 917  TRP B CG  
21274 C CD1 . TRP C 917  ? 3.0980 3.0656 3.3232 0.4269  -0.1669 -0.3432 917  TRP B CD1 
21275 C CD2 . TRP C 917  ? 3.0882 3.0602 3.3309 0.4497  -0.1973 -0.3365 917  TRP B CD2 
21276 N NE1 . TRP C 917  ? 3.0946 3.0821 3.3508 0.4413  -0.1610 -0.3495 917  TRP B NE1 
21277 C CE2 . TRP C 917  ? 3.0846 3.0745 3.3515 0.4555  -0.1791 -0.3453 917  TRP B CE2 
21278 C CE3 . TRP C 917  ? 3.0864 3.0562 3.3328 0.4614  -0.2180 -0.3310 917  TRP B CE3 
21279 C CZ2 . TRP C 917  ? 3.0731 3.0772 3.3667 0.4724  -0.1805 -0.3485 917  TRP B CZ2 
21280 C CZ3 . TRP C 917  ? 3.0749 3.0592 3.3472 0.4782  -0.2197 -0.3341 917  TRP B CZ3 
21281 C CH2 . TRP C 917  ? 3.0676 3.0682 3.3629 0.4836  -0.2008 -0.3427 917  TRP B CH2 
21282 N N   . PHE C 918  ? 3.1246 3.0431 3.2823 0.3769  -0.2159 -0.3278 918  PHE B N   
21283 C CA  . PHE C 918  ? 3.1920 3.1101 3.3434 0.3568  -0.2110 -0.3318 918  PHE B CA  
21284 C C   . PHE C 918  ? 3.1322 3.0311 3.2610 0.3396  -0.2321 -0.3264 918  PHE B C   
21285 O O   . PHE C 918  ? 3.1607 3.0502 3.2728 0.3205  -0.2276 -0.3276 918  PHE B O   
21286 C CB  . PHE C 918  ? 3.3029 3.2040 3.4247 0.3510  -0.1783 -0.3326 918  PHE B CB  
21287 C CG  . PHE C 918  ? 3.3849 3.2485 3.4588 0.3497  -0.1675 -0.3227 918  PHE B CG  
21288 C CD1 . PHE C 918  ? 3.4412 3.2756 3.4765 0.3314  -0.1676 -0.3177 918  PHE B CD1 
21289 C CD2 . PHE C 918  ? 3.3861 3.2429 3.4534 0.3665  -0.1567 -0.3179 918  PHE B CD2 
21290 C CE1 . PHE C 918  ? 3.4672 3.2667 3.4594 0.3308  -0.1559 -0.3081 918  PHE B CE1 
21291 C CE2 . PHE C 918  ? 3.4107 3.2350 3.4369 0.3656  -0.1462 -0.3078 918  PHE B CE2 
21292 C CZ  . PHE C 918  ? 3.4468 3.2426 3.4361 0.3483  -0.1451 -0.3030 918  PHE B CZ  
21293 N N   . GLY C 919  ? 3.0273 2.9186 3.1539 0.3456  -0.2551 -0.3205 919  GLY B N   
21294 C CA  . GLY C 919  ? 2.9513 2.8223 3.0558 0.3295  -0.2767 -0.3154 919  GLY B CA  
21295 C C   . GLY C 919  ? 2.8492 2.7277 2.9722 0.3370  -0.3090 -0.3128 919  GLY B C   
21296 O O   . GLY C 919  ? 2.8236 2.7020 2.9504 0.3541  -0.3125 -0.3099 919  GLY B O   
21297 N N   . LYS C 920  ? 2.7904 2.6746 2.9236 0.3233  -0.3330 -0.3134 920  LYS B N   
21298 C CA  . LYS C 920  ? 2.6923 2.5783 2.8368 0.3266  -0.3658 -0.3102 920  LYS B CA  
21299 C C   . LYS C 920  ? 2.6498 2.5089 2.7634 0.3035  -0.3833 -0.3056 920  LYS B C   
21300 O O   . LYS C 920  ? 2.6805 2.5490 2.8036 0.2870  -0.3893 -0.3083 920  LYS B O   
21301 C CB  . LYS C 920  ? 2.6456 2.5751 2.8483 0.3371  -0.3825 -0.3162 920  LYS B CB  
21302 C CG  . LYS C 920  ? 2.6109 2.5431 2.8266 0.3406  -0.4172 -0.3129 920  LYS B CG  
21303 C CD  . LYS C 920  ? 2.5536 2.5276 2.8265 0.3574  -0.4287 -0.3179 920  LYS B CD  
21304 C CE  . LYS C 920  ? 2.5239 2.4983 2.8072 0.3643  -0.4615 -0.3142 920  LYS B CE  
21305 N NZ  . LYS C 920  ? 2.4819 2.4920 2.8157 0.3853  -0.4686 -0.3181 920  LYS B NZ  
21306 N N   . GLU C 921  ? 2.5548 2.3794 2.6309 0.3020  -0.3919 -0.2985 921  GLU B N   
21307 C CA  . GLU C 921  ? 2.4972 2.2843 2.5297 0.2794  -0.4004 -0.2932 921  GLU B CA  
21308 C C   . GLU C 921  ? 2.3769 2.1513 2.4043 0.2785  -0.4337 -0.2889 921  GLU B C   
21309 O O   . GLU C 921  ? 2.3433 2.1196 2.3773 0.2960  -0.4412 -0.2871 921  GLU B O   
21310 C CB  . GLU C 921  ? 2.5517 2.2995 2.5326 0.2761  -0.3727 -0.2878 921  GLU B CB  
21311 C CG  . GLU C 921  ? 2.6492 2.3534 2.5789 0.2520  -0.3733 -0.2825 921  GLU B CG  
21312 C CD  . GLU C 921  ? 2.7195 2.4211 2.6377 0.2349  -0.3540 -0.2855 921  GLU B CD  
21313 O OE1 . GLU C 921  ? 2.7264 2.4657 2.6848 0.2372  -0.3516 -0.2927 921  GLU B OE1 
21314 O OE2 . GLU C 921  ? 2.7683 2.4287 2.6361 0.2190  -0.3407 -0.2806 921  GLU B OE2 
21315 N N   . ILE C 922  ? 2.2942 2.0538 2.3078 0.2575  -0.4540 -0.2870 922  ILE B N   
21316 C CA  . ILE C 922  ? 2.1759 1.9205 2.1819 0.2546  -0.4869 -0.2829 922  ILE B CA  
21317 C C   . ILE C 922  ? 2.1320 1.8234 2.0785 0.2339  -0.4915 -0.2762 922  ILE B C   
21318 O O   . ILE C 922  ? 2.1431 1.8171 2.0671 0.2113  -0.4902 -0.2753 922  ILE B O   
21319 C CB  . ILE C 922  ? 2.1393 1.9164 2.1896 0.2507  -0.5178 -0.2858 922  ILE B CB  
21320 C CG1 . ILE C 922  ? 2.0750 1.8974 2.1814 0.2762  -0.5231 -0.2905 922  ILE B CG1 
21321 C CG2 . ILE C 922  ? 2.1552 1.9050 2.1830 0.2401  -0.5496 -0.2807 922  ILE B CG2 
21322 C CD1 . ILE C 922  ? 2.0539 1.9009 2.1993 0.2779  -0.5592 -0.2909 922  ILE B CD1 
21323 N N   . LEU C 923  ? 2.0867 1.7514 2.0073 0.2417  -0.4972 -0.2715 923  LEU B N   
21324 C CA  . LEU C 923  ? 2.0834 1.6943 1.9460 0.2253  -0.5005 -0.2648 923  LEU B CA  
21325 C C   . LEU C 923  ? 2.0903 1.6924 1.9538 0.2219  -0.5383 -0.2630 923  LEU B C   
21326 O O   . LEU C 923  ? 2.0769 1.6977 1.9660 0.2408  -0.5523 -0.2641 923  LEU B O   
21327 C CB  . LEU C 923  ? 2.0634 1.6486 1.8939 0.2370  -0.4750 -0.2602 923  LEU B CB  
21328 C CG  . LEU C 923  ? 2.0768 1.6126 1.8574 0.2321  -0.4801 -0.2529 923  LEU B CG  
21329 C CD1 . LEU C 923  ? 2.1242 1.6149 1.8573 0.2044  -0.4856 -0.2492 923  LEU B CD1 
21330 C CD2 . LEU C 923  ? 2.0525 1.5727 1.8109 0.2447  -0.4494 -0.2482 923  LEU B CD2 
21331 N N   . VAL C 924  ? 2.0885 1.6614 1.9234 0.1976  -0.5554 -0.2603 924  VAL B N   
21332 C CA  . VAL C 924  ? 2.0437 1.6002 1.8711 0.1921  -0.5915 -0.2578 924  VAL B CA  
21333 C C   . VAL C 924  ? 2.0161 1.5115 1.7793 0.1806  -0.5911 -0.2514 924  VAL B C   
21334 O O   . VAL C 924  ? 1.9950 1.4530 1.7124 0.1663  -0.5683 -0.2479 924  VAL B O   
21335 C CB  . VAL C 924  ? 2.0652 1.6354 1.9131 0.1742  -0.6213 -0.2588 924  VAL B CB  
21336 C CG1 . VAL C 924  ? 2.0535 1.6304 1.9201 0.1809  -0.6585 -0.2583 924  VAL B CG1 
21337 C CG2 . VAL C 924  ? 2.0435 1.6669 1.9457 0.1791  -0.6143 -0.2643 924  VAL B CG2 
21338 N N   . LYS C 925  ? 1.9720 1.4575 1.7329 0.1868  -0.6169 -0.2500 925  LYS B N   
21339 C CA  . LYS C 925  ? 1.9442 1.3784 1.6528 0.1834  -0.6166 -0.2447 925  LYS B CA  
21340 C C   . LYS C 925  ? 1.9270 1.3489 1.6334 0.1755  -0.6575 -0.2442 925  LYS B C   
21341 O O   . LYS C 925  ? 1.9665 1.4281 1.7201 0.1806  -0.6814 -0.2478 925  LYS B O   
21342 C CB  . LYS C 925  ? 1.8801 1.3280 1.6009 0.2096  -0.6017 -0.2447 925  LYS B CB  
21343 C CG  . LYS C 925  ? 1.8738 1.2780 1.5443 0.2084  -0.5759 -0.2388 925  LYS B CG  
21344 C CD  . LYS C 925  ? 1.8753 1.2727 1.5298 0.2011  -0.5410 -0.2375 925  LYS B CD  
21345 C CE  . LYS C 925  ? 1.9094 1.2529 1.5053 0.1938  -0.5182 -0.2301 925  LYS B CE  
21346 N NZ  . LYS C 925  ? 1.9240 1.2640 1.5073 0.1911  -0.4807 -0.2284 925  LYS B NZ  
21347 N N   . THR C 926  ? 1.8516 1.2194 1.5050 0.1632  -0.6660 -0.2396 926  THR B N   
21348 C CA  . THR C 926  ? 1.7911 1.1445 1.4400 0.1557  -0.7061 -0.2391 926  THR B CA  
21349 C C   . THR C 926  ? 1.7514 1.0618 1.3594 0.1595  -0.7125 -0.2360 926  THR B C   
21350 O O   . THR C 926  ? 1.7755 1.0393 1.3320 0.1513  -0.6916 -0.2316 926  THR B O   
21351 C CB  . THR C 926  ? 2.1703 1.4984 1.7963 0.1255  -0.7246 -0.2370 926  THR B CB  
21352 O OG1 . THR C 926  ? 2.2009 1.4970 1.7856 0.1086  -0.6949 -0.2340 926  THR B OG1 
21353 C CG2 . THR C 926  ? 2.1316 1.5129 1.8165 0.1252  -0.7459 -0.2405 926  THR B CG2 
21354 N N   . LEU C 927  ? 1.7163 1.0416 1.3470 0.1717  -0.7414 -0.2381 927  LEU B N   
21355 C CA  . LEU C 927  ? 1.7382 1.0355 1.3418 0.1819  -0.7448 -0.2363 927  LEU B CA  
21356 C C   . LEU C 927  ? 1.7865 1.0367 1.3503 0.1659  -0.7757 -0.2343 927  LEU B C   
21357 O O   . LEU C 927  ? 1.7968 1.0634 1.3853 0.1681  -0.8096 -0.2367 927  LEU B O   
21358 C CB  . LEU C 927  ? 1.7210 1.0662 1.3746 0.2104  -0.7519 -0.2402 927  LEU B CB  
21359 C CG  . LEU C 927  ? 1.6961 1.0331 1.3383 0.2295  -0.7423 -0.2390 927  LEU B CG  
21360 C CD1 . LEU C 927  ? 1.6372 1.0205 1.3298 0.2537  -0.7590 -0.2432 927  LEU B CD1 
21361 C CD2 . LEU C 927  ? 1.7363 1.0160 1.3235 0.2180  -0.7546 -0.2355 927  LEU B CD2 
21362 N N   . ARG C 928  ? 1.8211 1.0119 1.3232 0.1509  -0.7634 -0.2298 928  ARG B N   
21363 C CA  . ARG C 928  ? 1.8532 0.9922 1.3106 0.1352  -0.7900 -0.2279 928  ARG B CA  
21364 C C   . ARG C 928  ? 1.8369 0.9808 1.3030 0.1540  -0.8082 -0.2298 928  ARG B C   
21365 O O   . ARG C 928  ? 1.8278 0.9660 1.2835 0.1685  -0.7880 -0.2286 928  ARG B O   
21366 C CB  . ARG C 928  ? 1.9091 0.9805 1.2959 0.1152  -0.7682 -0.2224 928  ARG B CB  
21367 C CG  . ARG C 928  ? 1.9916 1.0346 1.3503 0.0863  -0.7698 -0.2200 928  ARG B CG  
21368 C CD  . ARG C 928  ? 2.1133 1.1146 1.4233 0.0745  -0.7304 -0.2150 928  ARG B CD  
21369 N NE  . ARG C 928  ? 2.1874 1.2275 1.5274 0.0942  -0.6948 -0.2154 928  ARG B NE  
21370 C CZ  . ARG C 928  ? 2.2265 1.2832 1.5758 0.0899  -0.6698 -0.2151 928  ARG B CZ  
21371 N NH1 . ARG C 928  ? 2.2744 1.3123 1.6043 0.0652  -0.6751 -0.2141 928  ARG B NH1 
21372 N NH2 . ARG C 928  ? 2.1673 1.2585 1.5440 0.1100  -0.6394 -0.2155 928  ARG B NH2 
21373 N N   . VAL C 929  ? 1.8373 0.9934 1.3241 0.1540  -0.8465 -0.2325 929  VAL B N   
21374 C CA  . VAL C 929  ? 1.8429 0.9973 1.3321 0.1691  -0.8676 -0.2345 929  VAL B CA  
21375 C C   . VAL C 929  ? 1.8676 0.9643 1.3065 0.1493  -0.8954 -0.2329 929  VAL B C   
21376 O O   . VAL C 929  ? 1.8867 0.9659 1.3132 0.1275  -0.9128 -0.2316 929  VAL B O   
21377 C CB  . VAL C 929  ? 1.8297 1.0456 1.3849 0.1888  -0.8894 -0.2390 929  VAL B CB  
21378 C CG1 . VAL C 929  ? 1.8299 1.0415 1.3845 0.2040  -0.9118 -0.2409 929  VAL B CG1 
21379 C CG2 . VAL C 929  ? 1.7917 1.0603 1.3928 0.2078  -0.8607 -0.2407 929  VAL B CG2 
21380 N N   . VAL C 930  ? 1.8928 0.9600 1.3027 0.1565  -0.9002 -0.2329 930  VAL B N   
21381 C CA  . VAL C 930  ? 1.9942 0.9958 1.3445 0.1371  -0.9183 -0.2312 930  VAL B CA  
21382 C C   . VAL C 930  ? 2.0326 1.0316 1.3852 0.1494  -0.9479 -0.2343 930  VAL B C   
21383 O O   . VAL C 930  ? 2.0523 1.0994 1.4512 0.1729  -0.9529 -0.2374 930  VAL B O   
21384 C CB  . VAL C 930  ? 2.0250 0.9761 1.3197 0.1306  -0.8852 -0.2270 930  VAL B CB  
21385 C CG1 . VAL C 930  ? 2.1001 0.9786 1.3293 0.1092  -0.9012 -0.2252 930  VAL B CG1 
21386 C CG2 . VAL C 930  ? 2.0354 0.9889 1.3263 0.1218  -0.8505 -0.2236 930  VAL B CG2 
21387 N N   . PRO C 931  ? 2.2838 0.8372 1.3876 0.1846  -0.9480 -0.1354 931  PRO B N   
21388 C CA  . PRO C 931  ? 2.2741 0.8397 1.4158 0.1704  -0.9571 -0.1383 931  PRO B CA  
21389 C C   . PRO C 931  ? 2.2164 0.8205 1.4248 0.1588  -0.9800 -0.1479 931  PRO B C   
21390 O O   . PRO C 931  ? 2.2404 0.8399 1.4472 0.1693  -1.0045 -0.1584 931  PRO B O   
21391 C CB  . PRO C 931  ? 2.2572 0.8490 1.4152 0.1574  -0.9221 -0.1232 931  PRO B CB  
21392 C CG  . PRO C 931  ? 2.2434 0.8300 1.3623 0.1662  -0.8965 -0.1136 931  PRO B CG  
21393 C CD  . PRO C 931  ? 2.2294 0.8132 1.3437 0.1758  -0.9121 -0.1209 931  PRO B CD  
21394 N N   . GLU C 932  ? 2.1635 0.8047 1.4281 0.1385  -0.9717 -0.1446 932  GLU B N   
21395 C CA  . GLU C 932  ? 2.1481 0.8199 1.4730 0.1258  -0.9954 -0.1560 932  GLU B CA  
21396 C C   . GLU C 932  ? 2.0482 0.7763 1.4458 0.1036  -0.9788 -0.1499 932  GLU B C   
21397 O O   . GLU C 932  ? 1.9961 0.7269 1.4096 0.0889  -0.9678 -0.1461 932  GLU B O   
21398 C CB  . GLU C 932  ? 2.2006 0.8389 1.5112 0.1223  -1.0171 -0.1665 932  GLU B CB  
21399 C CG  . GLU C 932  ? 2.2783 0.8548 1.5128 0.1422  -1.0291 -0.1707 932  GLU B CG  
21400 C CD  . GLU C 932  ? 2.3081 0.8559 1.4946 0.1470  -1.0002 -0.1573 932  GLU B CD  
21401 O OE1 . GLU C 932  ? 2.2713 0.8459 1.4687 0.1434  -0.9700 -0.1438 932  GLU B OE1 
21402 O OE2 . GLU C 932  ? 2.3706 0.8695 1.5081 0.1548  -1.0076 -0.1606 932  GLU B OE2 
21403 N N   . GLY C 933  ? 2.0562 0.8250 1.4945 0.1021  -0.9776 -0.1495 933  GLY B N   
21404 C CA  . GLY C 933  ? 2.0249 0.8462 1.5299 0.0828  -0.9608 -0.1435 933  GLY B CA  
21405 C C   . GLY C 933  ? 1.9935 0.8335 1.4983 0.0781  -0.9237 -0.1260 933  GLY B C   
21406 O O   . GLY C 933  ? 1.9680 0.8037 1.4660 0.0696  -0.9032 -0.1168 933  GLY B O   
21407 N N   . VAL C 934  ? 2.0262 0.8868 1.5374 0.0839  -0.9148 -0.1215 934  VAL B N   
21408 C CA  . VAL C 934  ? 2.0904 0.9550 1.5782 0.0842  -0.8816 -0.1060 934  VAL B CA  
21409 C C   . VAL C 934  ? 2.0432 0.9528 1.5769 0.0695  -0.8565 -0.0952 934  VAL B C   
21410 O O   . VAL C 934  ? 2.0034 0.9341 1.5551 0.0719  -0.8549 -0.0947 934  VAL B O   
21411 C CB  . VAL C 934  ? 2.2080 1.0481 1.6435 0.1031  -0.8809 -0.1053 934  VAL B CB  
21412 C CG1 . VAL C 934  ? 1.8290 0.6817 1.2503 0.0985  -0.8456 -0.0903 934  VAL B CG1 
21413 C CG2 . VAL C 934  ? 2.3063 1.0940 1.6797 0.1188  -0.8956 -0.1116 934  VAL B CG2 
21414 N N   . LYS C 935  ? 2.0414 0.9617 1.5868 0.0560  -0.8355 -0.0858 935  LYS B N   
21415 C CA  . LYS C 935  ? 2.0289 0.9880 1.6136 0.0415  -0.8108 -0.0751 935  LYS B CA  
21416 C C   . LYS C 935  ? 2.0566 1.0119 1.6018 0.0444  -0.7827 -0.0618 935  LYS B C   
21417 O O   . LYS C 935  ? 2.0606 0.9879 1.5589 0.0523  -0.7784 -0.0595 935  LYS B O   
21418 C CB  . LYS C 935  ? 2.0261 0.9992 1.6508 0.0247  -0.8074 -0.0745 935  LYS B CB  
21419 C CG  . LYS C 935  ? 1.7010 0.6962 1.3837 0.0143  -0.8269 -0.0858 935  LYS B CG  
21420 C CD  . LYS C 935  ? 1.7151 0.7139 1.4021 0.0266  -0.8499 -0.0962 935  LYS B CD  
21421 C CE  . LYS C 935  ? 1.7418 0.7844 1.4936 0.0168  -0.8521 -0.0994 935  LYS B CE  
21422 N NZ  . LYS C 935  ? 1.7665 0.8205 1.5618 0.0075  -0.8761 -0.1136 935  LYS B NZ  
21423 N N   . ARG C 936  ? 2.0613 1.0441 1.6236 0.0382  -0.7637 -0.0536 936  ARG B N   
21424 C CA  . ARG C 936  ? 2.0746 1.0602 1.6066 0.0362  -0.7357 -0.0413 936  ARG B CA  
21425 C C   . ARG C 936  ? 2.0806 1.1047 1.6545 0.0194  -0.7134 -0.0310 936  ARG B C   
21426 O O   . ARG C 936  ? 2.0985 1.1456 1.7103 0.0132  -0.7134 -0.0314 936  ARG B O   
21427 C CB  . ARG C 936  ? 2.0850 1.0544 1.5746 0.0471  -0.7320 -0.0412 936  ARG B CB  
21428 C CG  . ARG C 936  ? 2.0851 1.0767 1.5972 0.0431  -0.7245 -0.0386 936  ARG B CG  
21429 C CD  . ARG C 936  ? 2.1703 1.1336 1.6430 0.0597  -0.7365 -0.0454 936  ARG B CD  
21430 N NE  . ARG C 936  ? 2.2245 1.1879 1.6701 0.0579  -0.7138 -0.0377 936  ARG B NE  
21431 C CZ  . ARG C 936  ? 2.2892 1.2225 1.6876 0.0712  -0.7162 -0.0411 936  ARG B CZ  
21432 N NH1 . ARG C 936  ? 2.3164 1.2180 1.6900 0.0891  -0.7417 -0.0520 936  ARG B NH1 
21433 N NH2 . ARG C 936  ? 2.3056 1.2380 1.6786 0.0665  -0.6928 -0.0337 936  ARG B NH2 
21434 N N   . GLU C 937  ? 2.0625 1.0923 1.6285 0.0134  -0.6952 -0.0221 937  GLU B N   
21435 C CA  . GLU C 937  ? 2.1044 1.1667 1.7038 -0.0014 -0.6736 -0.0117 937  GLU B CA  
21436 C C   . GLU C 937  ? 2.1715 1.2454 1.7433 -0.0037 -0.6480 -0.0007 937  GLU B C   
21437 O O   . GLU C 937  ? 2.1457 1.2099 1.6819 0.0016  -0.6398 0.0030  937  GLU B O   
21438 C CB  . GLU C 937  ? 2.1737 1.2346 1.7895 -0.0064 -0.6742 -0.0108 937  GLU B CB  
21439 C CG  . GLU C 937  ? 2.9767 2.0069 2.5488 0.0052  -0.6795 -0.0124 937  GLU B CG  
21440 C CD  . GLU C 937  ? 3.1264 2.1432 2.7132 0.0023  -0.6890 -0.0162 937  GLU B CD  
21441 O OE1 . GLU C 937  ? 3.1398 2.1398 2.7377 0.0031  -0.7123 -0.0279 937  GLU B OE1 
21442 O OE2 . GLU C 937  ? 3.1198 2.1412 2.7037 -0.0003 -0.6733 -0.0079 937  GLU B OE2 
21443 N N   . SER C 938  ? 2.3171 1.4131 1.9063 -0.0123 -0.6351 0.0043  938  SER B N   
21444 C CA  . SER C 938  ? 2.3107 1.4146 1.8708 -0.0154 -0.6139 0.0121  938  SER B CA  
21445 C C   . SER C 938  ? 2.5158 1.6521 2.0984 -0.0298 -0.5909 0.0233  938  SER B C   
21446 O O   . SER C 938  ? 2.5524 1.6996 2.1118 -0.0347 -0.5718 0.0303  938  SER B O   
21447 C CB  . SER C 938  ? 2.1204 1.2206 1.6794 -0.0140 -0.6168 0.0089  938  SER B CB  
21448 O OG  . SER C 938  ? 1.8773 0.9991 1.4876 -0.0224 -0.6186 0.0094  938  SER B OG  
21449 N N   . TYR C 939  ? 2.5590 1.7103 2.1864 -0.0372 -0.5927 0.0244  939  TYR B N   
21450 C CA  . TYR C 939  ? 2.6275 1.8078 2.2818 -0.0511 -0.5726 0.0343  939  TYR B CA  
21451 C C   . TYR C 939  ? 2.5564 1.7518 2.1848 -0.0549 -0.5511 0.0443  939  TYR B C   
21452 O O   . TYR C 939  ? 2.5361 1.7553 2.1800 -0.0661 -0.5336 0.0527  939  TYR B O   
21453 C CB  . TYR C 939  ? 3.2309 2.4188 2.9303 -0.0574 -0.5770 0.0338  939  TYR B CB  
21454 C CG  . TYR C 939  ? 3.3532 2.5304 3.0458 -0.0532 -0.5805 0.0338  939  TYR B CG  
21455 C CD1 . TYR C 939  ? 3.3906 2.5795 3.0696 -0.0544 -0.5631 0.0435  939  TYR B CD1 
21456 C CD2 . TYR C 939  ? 3.4174 2.5731 3.1175 -0.0478 -0.6013 0.0240  939  TYR B CD2 
21457 C CE1 . TYR C 939  ? 3.4271 2.6040 3.0969 -0.0483 -0.5654 0.0440  939  TYR B CE1 
21458 C CE2 . TYR C 939  ? 3.4568 2.5981 3.1466 -0.0438 -0.6035 0.0242  939  TYR B CE2 
21459 C CZ  . TYR C 939  ? 3.4574 2.6083 3.1312 -0.0432 -0.5850 0.0346  939  TYR B CZ  
21460 O OH  . TYR C 939  ? 3.4808 2.6151 3.1409 -0.0370 -0.5861 0.0354  939  TYR B OH  
21461 N N   . SER C 940  ? 2.4795 1.6621 2.0686 -0.0453 -0.5525 0.0429  940  SER B N   
21462 C CA  . SER C 940  ? 2.3798 1.5801 1.9442 -0.0480 -0.5334 0.0508  940  SER B CA  
21463 C C   . SER C 940  ? 2.2506 1.4577 1.7941 -0.0556 -0.5203 0.0528  940  SER B C   
21464 O O   . SER C 940  ? 2.2567 1.4427 1.7837 -0.0519 -0.5283 0.0466  940  SER B O   
21465 C CB  . SER C 940  ? 2.4235 1.6079 1.9534 -0.0347 -0.5386 0.0481  940  SER B CB  
21466 O OG  . SER C 940  ? 2.4421 1.5980 1.9437 -0.0266 -0.5506 0.0398  940  SER B OG  
21467 N N   . GLY C 941  ? 2.1051 1.3405 1.6470 -0.0662 -0.5002 0.0613  941  GLY B N   
21468 C CA  . GLY C 941  ? 1.9901 1.2346 1.5111 -0.0771 -0.4844 0.0641  941  GLY B CA  
21469 C C   . GLY C 941  ? 1.8989 1.1793 1.4296 -0.0890 -0.4654 0.0736  941  GLY B C   
21470 O O   . GLY C 941  ? 1.8760 1.1704 1.4308 -0.0868 -0.4660 0.0779  941  GLY B O   
21471 N N   . VAL C 942  ? 1.8282 1.1219 1.3374 -0.1013 -0.4487 0.0766  942  VAL B N   
21472 C CA  . VAL C 942  ? 1.7148 1.0438 1.2323 -0.1148 -0.4308 0.0852  942  VAL B CA  
21473 C C   . VAL C 942  ? 1.6552 0.9850 1.1583 -0.1307 -0.4171 0.0866  942  VAL B C   
21474 O O   . VAL C 942  ? 1.6944 0.9991 1.1705 -0.1304 -0.4185 0.0811  942  VAL B O   
21475 C CB  . VAL C 942  ? 1.6878 1.0416 1.1825 -0.1148 -0.4208 0.0872  942  VAL B CB  
21476 C CG1 . VAL C 942  ? 1.6703 1.0616 1.1836 -0.1229 -0.4088 0.0958  942  VAL B CG1 
21477 C CG2 . VAL C 942  ? 1.7037 1.0466 1.1917 -0.0969 -0.4330 0.0836  942  VAL B CG2 
21478 N N   . THR C 943  ? 1.5526 0.9078 1.0691 -0.1444 -0.4033 0.0939  943  THR B N   
21479 C CA  . THR C 943  ? 1.5104 0.8701 1.0006 -0.1614 -0.3868 0.0952  943  THR B CA  
21480 C C   . THR C 943  ? 1.4829 0.8782 0.9567 -0.1708 -0.3731 0.0982  943  THR B C   
21481 O O   . THR C 943  ? 1.4814 0.9071 0.9749 -0.1744 -0.3679 0.1046  943  THR B O   
21482 C CB  . THR C 943  ? 1.4484 0.8037 0.9533 -0.1732 -0.3791 0.0996  943  THR B CB  
21483 O OG1 . THR C 943  ? 1.4585 0.7805 0.9696 -0.1645 -0.3904 0.0949  943  THR B OG1 
21484 C CG2 . THR C 943  ? 1.4283 0.7873 0.8992 -0.1914 -0.3610 0.1007  943  THR B CG2 
21485 N N   . LEU C 944  ? 1.4649 0.8563 0.9022 -0.1739 -0.3676 0.0932  944  LEU B N   
21486 C CA  . LEU C 944  ? 1.4362 0.8644 0.8582 -0.1839 -0.3543 0.0946  944  LEU B CA  
21487 C C   . LEU C 944  ? 1.4720 0.9172 0.8908 -0.2065 -0.3381 0.0990  944  LEU B C   
21488 O O   . LEU C 944  ? 1.4882 0.9079 0.8842 -0.2183 -0.3308 0.0968  944  LEU B O   
21489 C CB  . LEU C 944  ? 1.4186 0.8352 0.8016 -0.1834 -0.3508 0.0873  944  LEU B CB  
21490 C CG  . LEU C 944  ? 1.4080 0.8203 0.7947 -0.1613 -0.3644 0.0844  944  LEU B CG  
21491 C CD1 . LEU C 944  ? 1.4123 0.8265 0.7637 -0.1606 -0.3577 0.0787  944  LEU B CD1 
21492 C CD2 . LEU C 944  ? 1.3671 0.8159 0.7854 -0.1543 -0.3668 0.0909  944  LEU B CD2 
21493 N N   . ASP C 945  ? 1.4680 0.9529 0.9075 -0.2110 -0.3332 0.1054  945  ASP B N   
21494 C CA  . ASP C 945  ? 1.4424 0.9474 0.8813 -0.2319 -0.3189 0.1104  945  ASP B CA  
21495 C C   . ASP C 945  ? 1.3950 0.9511 0.8343 -0.2377 -0.3115 0.1125  945  ASP B C   
21496 O O   . ASP C 945  ? 1.3765 0.9568 0.8412 -0.2284 -0.3160 0.1180  945  ASP B O   
21497 C CB  . ASP C 945  ? 1.4416 0.9412 0.9131 -0.2294 -0.3224 0.1173  945  ASP B CB  
21498 C CG  . ASP C 945  ? 1.4546 0.9526 0.9170 -0.2509 -0.3081 0.1211  945  ASP B CG  
21499 O OD1 . ASP C 945  ? 1.4496 0.9649 0.8843 -0.2696 -0.2948 0.1195  945  ASP B OD1 
21500 O OD2 . ASP C 945  ? 1.4444 0.9230 0.9268 -0.2494 -0.3098 0.1252  945  ASP B OD2 
21501 N N   . PRO C 946  ? 1.3814 0.9546 0.7917 -0.2537 -0.2994 0.1081  946  PRO B N   
21502 C CA  . PRO C 946  ? 1.3620 0.9893 0.7759 -0.2547 -0.2952 0.1087  946  PRO B CA  
21503 C C   . PRO C 946  ? 1.3627 1.0240 0.7870 -0.2706 -0.2868 0.1146  946  PRO B C   
21504 O O   . PRO C 946  ? 1.3350 1.0439 0.7719 -0.2679 -0.2862 0.1175  946  PRO B O   
21505 C CB  . PRO C 946  ? 1.3589 0.9901 0.7378 -0.2689 -0.2840 0.1007  946  PRO B CB  
21506 C CG  . PRO C 946  ? 1.3696 0.9463 0.7214 -0.2813 -0.2789 0.0973  946  PRO B CG  
21507 C CD  . PRO C 946  ? 1.3599 0.9093 0.7345 -0.2744 -0.2869 0.1033  946  PRO B CD  
21508 N N   . ARG C 947  ? 1.3659 0.9994 0.7826 -0.2860 -0.2804 0.1163  947  ARG B N   
21509 C CA  . ARG C 947  ? 1.3600 1.0144 0.7736 -0.3073 -0.2693 0.1202  947  ARG B CA  
21510 C C   . ARG C 947  ? 1.3571 0.9955 0.7978 -0.2984 -0.2751 0.1283  947  ARG B C   
21511 O O   . ARG C 947  ? 1.3901 1.0244 0.8268 -0.3143 -0.2665 0.1322  947  ARG B O   
21512 C CB  . ARG C 947  ? 1.4048 1.0305 0.7829 -0.3318 -0.2556 0.1161  947  ARG B CB  
21513 C CG  . ARG C 947  ? 1.4216 1.0647 0.7671 -0.3491 -0.2444 0.1078  947  ARG B CG  
21514 C CD  . ARG C 947  ? 1.4118 1.1062 0.7511 -0.3733 -0.2327 0.1077  947  ARG B CD  
21515 N NE  . ARG C 947  ? 1.4420 1.1166 0.7441 -0.4037 -0.2161 0.1042  947  ARG B NE  
21516 C CZ  . ARG C 947  ? 1.4885 1.1789 0.7602 -0.4262 -0.2029 0.0961  947  ARG B CZ  
21517 N NH1 . ARG C 947  ? 1.4797 1.2097 0.7563 -0.4211 -0.2042 0.0907  947  ARG B NH1 
21518 N NH2 . ARG C 947  ? 1.5293 1.1951 0.7637 -0.4544 -0.1871 0.0931  947  ARG B NH2 
21519 N N   . GLY C 948  ? 1.3212 0.9468 0.7872 -0.2741 -0.2887 0.1304  948  GLY B N   
21520 C CA  . GLY C 948  ? 1.3042 0.9149 0.7977 -0.2655 -0.2934 0.1375  948  GLY B CA  
21521 C C   . GLY C 948  ? 1.3040 0.8789 0.7970 -0.2772 -0.2872 0.1404  948  GLY B C   
21522 O O   . GLY C 948  ? 1.2586 0.8220 0.7757 -0.2708 -0.2896 0.1462  948  GLY B O   
21523 N N   . ILE C 949  ? 1.2930 0.8485 0.7570 -0.2937 -0.2780 0.1363  949  ILE B N   
21524 C CA  . ILE C 949  ? 1.2927 0.8113 0.7509 -0.3032 -0.2711 0.1387  949  ILE B CA  
21525 C C   . ILE C 949  ? 1.3296 0.8238 0.8213 -0.2880 -0.2793 0.1430  949  ILE B C   
21526 O O   . ILE C 949  ? 1.2817 0.7617 0.7792 -0.2954 -0.2718 0.1483  949  ILE B O   
21527 C CB  . ILE C 949  ? 1.3279 0.8120 0.7573 -0.3061 -0.2693 0.1318  949  ILE B CB  
21528 C CG1 . ILE C 949  ? 1.4189 0.9230 0.8143 -0.3207 -0.2610 0.1260  949  ILE B CG1 
21529 C CG2 . ILE C 949  ? 1.3282 0.7758 0.7444 -0.3164 -0.2597 0.1344  949  ILE B CG2 
21530 C CD1 . ILE C 949  ? 1.4332 0.9452 0.8013 -0.3484 -0.2435 0.1274  949  ILE B CD1 
21531 N N   . TYR C 950  ? 1.3581 0.8464 0.8706 -0.2674 -0.2941 0.1402  950  TYR B N   
21532 C CA  . TYR C 950  ? 1.3729 0.8326 0.9145 -0.2538 -0.3033 0.1410  950  TYR B CA  
21533 C C   . TYR C 950  ? 1.3769 0.8485 0.9531 -0.2433 -0.3085 0.1464  950  TYR B C   
21534 O O   . TYR C 950  ? 1.4042 0.8555 1.0078 -0.2340 -0.3151 0.1468  950  TYR B O   
21535 C CB  . TYR C 950  ? 1.2925 0.7255 0.8300 -0.2407 -0.3158 0.1330  950  TYR B CB  
21536 C CG  . TYR C 950  ? 1.3208 0.7245 0.8325 -0.2504 -0.3079 0.1308  950  TYR B CG  
21537 C CD1 . TYR C 950  ? 1.3046 0.6810 0.8325 -0.2465 -0.3091 0.1321  950  TYR B CD1 
21538 C CD2 . TYR C 950  ? 1.3300 0.7349 0.8000 -0.2650 -0.2969 0.1279  950  TYR B CD2 
21539 C CE1 . TYR C 950  ? 1.3245 0.6730 0.8253 -0.2538 -0.3005 0.1309  950  TYR B CE1 
21540 C CE2 . TYR C 950  ? 1.3692 0.7432 0.8095 -0.2745 -0.2875 0.1264  950  TYR B CE2 
21541 C CZ  . TYR C 950  ? 1.3893 0.7341 0.8436 -0.2677 -0.2894 0.1281  950  TYR B CZ  
21542 O OH  . TYR C 950  ? 1.3982 0.7104 0.8172 -0.2754 -0.2791 0.1269  950  TYR B OH  
21543 N N   . GLY C 951  ? 1.3754 0.8800 0.9492 -0.2454 -0.3047 0.1502  951  GLY B N   
21544 C CA  . GLY C 951  ? 1.3992 0.9126 0.9983 -0.2370 -0.3063 0.1565  951  GLY B CA  
21545 C C   . GLY C 951  ? 1.4210 0.9620 1.0206 -0.2235 -0.3132 0.1565  951  GLY B C   
21546 O O   . GLY C 951  ? 1.4174 0.9691 1.0298 -0.2162 -0.3130 0.1620  951  GLY B O   
21547 N N   . THR C 952  ? 1.4347 0.9846 1.0183 -0.2190 -0.3188 0.1502  952  THR B N   
21548 C CA  . THR C 952  ? 1.3966 0.9769 0.9756 -0.2067 -0.3234 0.1498  952  THR B CA  
21549 C C   . THR C 952  ? 1.3634 0.9522 0.9197 -0.2075 -0.3251 0.1425  952  THR B C   
21550 O O   . THR C 952  ? 1.3685 0.9345 0.9114 -0.2161 -0.3239 0.1375  952  THR B O   
21551 C CB  . THR C 952  ? 1.3849 0.9507 0.9838 -0.1852 -0.3350 0.1505  952  THR B CB  
21552 O OG1 . THR C 952  ? 1.3987 0.9838 0.9866 -0.1712 -0.3411 0.1475  952  THR B OG1 
21553 C CG2 . THR C 952  ? 1.3639 0.8892 0.9755 -0.1819 -0.3433 0.1459  952  THR B CG2 
21554 N N   . ILE C 953  ? 1.3497 0.9695 0.9004 -0.1970 -0.3276 0.1420  953  ILE B N   
21555 C CA  . ILE C 953  ? 1.3994 1.0321 0.9278 -0.1991 -0.3266 0.1353  953  ILE B CA  
21556 C C   . ILE C 953  ? 1.5053 1.1139 1.0335 -0.1790 -0.3391 0.1303  953  ILE B C   
21557 O O   . ILE C 953  ? 1.5434 1.1568 1.0822 -0.1595 -0.3469 0.1324  953  ILE B O   
21558 C CB  . ILE C 953  ? 1.4265 1.1141 0.9454 -0.2050 -0.3185 0.1367  953  ILE B CB  
21559 C CG1 . ILE C 953  ? 1.4040 1.1177 0.9228 -0.1841 -0.3245 0.1356  953  ILE B CG1 
21560 C CG2 . ILE C 953  ? 1.4495 1.1557 0.9808 -0.2105 -0.3137 0.1444  953  ILE B CG2 
21561 C CD1 . ILE C 953  ? 1.3755 1.1469 0.8830 -0.1930 -0.3157 0.1343  953  ILE B CD1 
21562 N N   . SER C 954  ? 1.4863 1.0641 0.9999 -0.1838 -0.3410 0.1239  954  SER B N   
21563 C CA  . SER C 954  ? 1.4319 0.9813 0.9409 -0.1670 -0.3532 0.1182  954  SER B CA  
21564 C C   . SER C 954  ? 1.4255 0.9912 0.9065 -0.1684 -0.3483 0.1128  954  SER B C   
21565 O O   . SER C 954  ? 1.4445 0.9984 0.9025 -0.1824 -0.3413 0.1080  954  SER B O   
21566 C CB  . SER C 954  ? 1.3906 0.8944 0.8988 -0.1701 -0.3590 0.1141  954  SER B CB  
21567 O OG  . SER C 954  ? 1.3613 0.8375 0.8885 -0.1527 -0.3744 0.1127  954  SER B OG  
21568 N N   . ARG C 955  ? 1.3870 0.9790 0.8678 -0.1540 -0.3503 0.1134  955  ARG B N   
21569 C CA  . ARG C 955  ? 1.4087 1.0118 0.8639 -0.1532 -0.3459 0.1075  955  ARG B CA  
21570 C C   . ARG C 955  ? 1.4371 1.0220 0.8897 -0.1285 -0.3577 0.1052  955  ARG B C   
21571 O O   . ARG C 955  ? 1.4766 1.0786 0.9124 -0.1217 -0.3542 0.1021  955  ARG B O   
21572 C CB  . ARG C 955  ? 1.3735 1.0339 0.8245 -0.1619 -0.3335 0.1091  955  ARG B CB  
21573 C CG  . ARG C 955  ? 1.3725 1.0508 0.8184 -0.1893 -0.3205 0.1096  955  ARG B CG  
21574 C CD  . ARG C 955  ? 1.3450 1.0834 0.8006 -0.1918 -0.3140 0.1136  955  ARG B CD  
21575 N NE  . ARG C 955  ? 1.2960 1.0612 0.7469 -0.2183 -0.3017 0.1142  955  ARG B NE  
21576 C CZ  . ARG C 955  ? 1.2762 1.0945 0.7372 -0.2208 -0.2977 0.1177  955  ARG B CZ  
21577 N NH1 . ARG C 955  ? 1.2712 1.1159 0.7460 -0.1969 -0.3047 0.1210  955  ARG B NH1 
21578 N NH2 . ARG C 955  ? 1.3055 1.1488 0.7608 -0.2457 -0.2872 0.1177  955  ARG B NH2 
21579 N N   . ARG C 956  ? 1.4212 0.9716 0.8902 -0.1157 -0.3711 0.1066  956  ARG B N   
21580 C CA  . ARG C 956  ? 1.4310 0.9560 0.8955 -0.0936 -0.3836 0.1038  956  ARG B CA  
21581 C C   . ARG C 956  ? 1.5110 0.9958 0.9943 -0.0871 -0.3975 0.1037  956  ARG B C   
21582 O O   . ARG C 956  ? 1.4958 0.9835 1.0030 -0.0931 -0.3969 0.1085  956  ARG B O   
21583 C CB  . ARG C 956  ? 1.3973 0.9527 0.8644 -0.0760 -0.3827 0.1083  956  ARG B CB  
21584 C CG  . ARG C 956  ? 1.4180 0.9872 0.8598 -0.0691 -0.3779 0.1040  956  ARG B CG  
21585 C CD  . ARG C 956  ? 1.4482 1.0533 0.8912 -0.0510 -0.3752 0.1085  956  ARG B CD  
21586 N NE  . ARG C 956  ? 1.4957 1.0693 0.9410 -0.0272 -0.3877 0.1103  956  ARG B NE  
21587 C CZ  . ARG C 956  ? 1.5328 1.1136 0.9652 -0.0054 -0.3883 0.1112  956  ARG B CZ  
21588 N NH1 . ARG C 956  ? 1.5383 1.1605 0.9577 -0.0043 -0.3771 0.1101  956  ARG B NH1 
21589 N NH2 . ARG C 956  ? 1.5473 1.0934 0.9789 0.0149  -0.3994 0.1128  956  ARG B NH2 
21590 N N   . LYS C 957  ? 1.6182 1.0650 1.0895 -0.0758 -0.4095 0.0974  957  LYS B N   
21591 C CA  . LYS C 957  ? 1.6409 1.0513 1.1281 -0.0644 -0.4257 0.0957  957  LYS B CA  
21592 C C   . LYS C 957  ? 1.6333 1.0224 1.0984 -0.0464 -0.4347 0.0909  957  LYS B C   
21593 O O   . LYS C 957  ? 1.5961 0.9809 1.0338 -0.0466 -0.4315 0.0862  957  LYS B O   
21594 C CB  . LYS C 957  ? 1.6840 1.0629 1.1797 -0.0735 -0.4335 0.0910  957  LYS B CB  
21595 C CG  . LYS C 957  ? 1.7480 1.0935 1.2628 -0.0627 -0.4511 0.0879  957  LYS B CG  
21596 C CD  . LYS C 957  ? 1.7939 1.1369 1.3428 -0.0734 -0.4521 0.0902  957  LYS B CD  
21597 C CE  . LYS C 957  ? 1.8462 1.1730 1.4198 -0.0647 -0.4631 0.0903  957  LYS B CE  
21598 N NZ  . LYS C 957  ? 1.8956 1.1860 1.4643 -0.0536 -0.4821 0.0815  957  LYS B NZ  
21599 N N   . GLU C 958  ? 1.6660 1.0403 1.1404 -0.0312 -0.4443 0.0923  958  GLU B N   
21600 C CA  . GLU C 958  ? 1.7711 1.1157 1.2246 -0.0133 -0.4553 0.0875  958  GLU B CA  
21601 C C   . GLU C 958  ? 1.7922 1.0922 1.2557 -0.0120 -0.4734 0.0810  958  GLU B C   
21602 O O   . GLU C 958  ? 1.7978 1.0918 1.2892 -0.0155 -0.4784 0.0828  958  GLU B O   
21603 C CB  . GLU C 958  ? 1.8397 1.1945 1.2927 0.0034  -0.4536 0.0931  958  GLU B CB  
21604 C CG  . GLU C 958  ? 1.9458 1.2861 1.3679 0.0226  -0.4567 0.0905  958  GLU B CG  
21605 C CD  . GLU C 958  ? 2.0312 1.3803 1.4508 0.0410  -0.4540 0.0969  958  GLU B CD  
21606 O OE1 . GLU C 958  ? 2.0429 1.4360 1.4621 0.0438  -0.4406 0.1031  958  GLU B OE1 
21607 O OE2 . GLU C 958  ? 2.0752 1.3868 1.4916 0.0530  -0.4653 0.0955  958  GLU B OE2 
21608 N N   . PHE C 959  ? 1.8140 1.0838 1.2550 -0.0079 -0.4829 0.0730  959  PHE B N   
21609 C CA  . PHE C 959  ? 1.8243 1.0518 1.2699 -0.0020 -0.5031 0.0657  959  PHE B CA  
21610 C C   . PHE C 959  ? 1.9305 1.1339 1.3496 0.0169  -0.5107 0.0631  959  PHE B C   
21611 O O   . PHE C 959  ? 1.9494 1.1537 1.3364 0.0240  -0.5044 0.0622  959  PHE B O   
21612 C CB  . PHE C 959  ? 1.7658 0.9719 1.2003 -0.0077 -0.5103 0.0581  959  PHE B CB  
21613 C CG  . PHE C 959  ? 1.6940 0.9246 1.1323 -0.0240 -0.4960 0.0611  959  PHE B CG  
21614 C CD1 . PHE C 959  ? 1.6892 0.9140 1.1487 -0.0343 -0.5004 0.0593  959  PHE B CD1 
21615 C CD2 . PHE C 959  ? 1.6608 0.9206 1.0809 -0.0292 -0.4776 0.0654  959  PHE B CD2 
21616 C CE1 . PHE C 959  ? 1.6590 0.9020 1.1175 -0.0492 -0.4861 0.0622  959  PHE B CE1 
21617 C CE2 . PHE C 959  ? 1.6376 0.9175 1.0582 -0.0460 -0.4640 0.0676  959  PHE B CE2 
21618 C CZ  . PHE C 959  ? 1.6394 0.9082 1.0771 -0.0557 -0.4681 0.0663  959  PHE B CZ  
21619 N N   . PRO C 960  ? 1.9599 1.1406 1.3906 0.0245  -0.5227 0.0620  960  PRO B N   
21620 C CA  . PRO C 960  ? 2.0650 1.2214 1.4675 0.0429  -0.5281 0.0607  960  PRO B CA  
21621 C C   . PRO C 960  ? 2.1804 1.2888 1.5714 0.0484  -0.5497 0.0504  960  PRO B C   
21622 O O   . PRO C 960  ? 2.1905 1.2883 1.5934 0.0395  -0.5602 0.0441  960  PRO B O   
21623 C CB  . PRO C 960  ? 2.0433 1.2064 1.4634 0.0467  -0.5245 0.0672  960  PRO B CB  
21624 C CG  . PRO C 960  ? 1.8601 1.0469 1.3207 0.0285  -0.5197 0.0706  960  PRO B CG  
21625 C CD  . PRO C 960  ? 1.8965 1.0785 1.3641 0.0168  -0.5265 0.0640  960  PRO B CD  
21626 N N   . TYR C 961  ? 2.2929 1.3723 1.6589 0.0642  -0.5564 0.0487  961  TYR B N   
21627 C CA  . TYR C 961  ? 2.3960 1.4292 1.7543 0.0691  -0.5782 0.0393  961  TYR B CA  
21628 C C   . TYR C 961  ? 2.4437 1.4695 1.8361 0.0611  -0.5868 0.0383  961  TYR B C   
21629 O O   . TYR C 961  ? 2.4549 1.4891 1.8548 0.0633  -0.5775 0.0451  961  TYR B O   
21630 C CB  . TYR C 961  ? 2.4938 1.4979 1.8120 0.0884  -0.5798 0.0391  961  TYR B CB  
21631 C CG  . TYR C 961  ? 2.5631 1.5381 1.8433 0.0973  -0.5878 0.0321  961  TYR B CG  
21632 C CD1 . TYR C 961  ? 2.6213 1.5464 1.8781 0.1071  -0.6070 0.0239  961  TYR B CD1 
21633 C CD2 . TYR C 961  ? 2.5811 1.5756 1.8462 0.0954  -0.5759 0.0332  961  TYR B CD2 
21634 C CE1 . TYR C 961  ? 2.6604 1.5552 1.8790 0.1164  -0.6144 0.0174  961  TYR B CE1 
21635 C CE2 . TYR C 961  ? 2.6335 1.5973 1.8602 0.1038  -0.5818 0.0267  961  TYR B CE2 
21636 C CZ  . TYR C 961  ? 2.6802 1.5935 1.8832 0.1152  -0.6013 0.0190  961  TYR B CZ  
21637 O OH  . TYR C 961  ? 2.7349 1.6141 1.8966 0.1244  -0.6075 0.0124  961  TYR B OH  
21638 N N   . ARG C 962  ? 2.4746 1.4832 1.8858 0.0525  -0.6046 0.0292  962  ARG B N   
21639 C CA  . ARG C 962  ? 2.5417 1.5323 1.9779 0.0463  -0.6166 0.0249  962  ARG B CA  
21640 C C   . ARG C 962  ? 2.5234 1.4759 1.9492 0.0491  -0.6417 0.0119  962  ARG B C   
21641 O O   . ARG C 962  ? 2.4863 1.4423 1.9258 0.0431  -0.6527 0.0053  962  ARG B O   
21642 C CB  . ARG C 962  ? 2.6200 1.6406 2.1055 0.0284  -0.6107 0.0276  962  ARG B CB  
21643 C CG  . ARG C 962  ? 2.7548 1.7568 2.2697 0.0188  -0.6243 0.0207  962  ARG B CG  
21644 C CD  . ARG C 962  ? 2.8418 1.8627 2.3883 0.0079  -0.6096 0.0280  962  ARG B CD  
21645 N NE  . ARG C 962  ? 2.8871 1.9394 2.4756 -0.0078 -0.6047 0.0291  962  ARG B NE  
21646 C CZ  . ARG C 962  ? 2.9232 1.9839 2.5487 -0.0214 -0.5998 0.0302  962  ARG B CZ  
21647 N NH1 . ARG C 962  ? 2.9590 1.9971 2.5836 -0.0223 -0.5992 0.0298  962  ARG B NH1 
21648 N NH2 . ARG C 962  ? 2.9050 1.9936 2.5659 -0.0342 -0.5944 0.0315  962  ARG B NH2 
21649 N N   . ILE C 963  ? 2.5093 1.4242 1.9070 0.0597  -0.6504 0.0085  963  ILE B N   
21650 C CA  . ILE C 963  ? 2.4313 1.3063 1.8148 0.0630  -0.6751 -0.0040 963  ILE B CA  
21651 C C   . ILE C 963  ? 2.4531 1.3203 1.8721 0.0492  -0.6872 -0.0104 963  ILE B C   
21652 O O   . ILE C 963  ? 2.4512 1.3099 1.8724 0.0473  -0.6798 -0.0066 963  ILE B O   
21653 C CB  . ILE C 963  ? 2.3648 1.2006 1.6979 0.0802  -0.6776 -0.0045 963  ILE B CB  
21654 C CG1 . ILE C 963  ? 2.2853 1.1375 1.5882 0.0929  -0.6570 0.0054  963  ILE B CG1 
21655 C CG2 . ILE C 963  ? 2.3775 1.1763 1.6877 0.0856  -0.7016 -0.0168 963  ILE B CG2 
21656 C CD1 . ILE C 963  ? 2.3072 1.1231 1.5605 0.1115  -0.6568 0.0059  963  ILE B CD1 
21657 N N   . PRO C 964  ? 2.4616 1.3332 1.9091 0.0395  -0.7048 -0.0202 964  PRO B N   
21658 C CA  . PRO C 964  ? 2.5129 1.3835 2.0013 0.0238  -0.7177 -0.0284 964  PRO B CA  
21659 C C   . PRO C 964  ? 2.5897 1.4138 2.0530 0.0276  -0.7376 -0.0388 964  PRO B C   
21660 O O   . PRO C 964  ? 2.6320 1.4304 2.0618 0.0395  -0.7530 -0.0454 964  PRO B O   
21661 C CB  . PRO C 964  ? 2.4916 1.3849 2.0116 0.0172  -0.7306 -0.0355 964  PRO B CB  
21662 C CG  . PRO C 964  ? 2.3935 1.3037 1.8909 0.0270  -0.7173 -0.0277 964  PRO B CG  
21663 C CD  . PRO C 964  ? 2.4324 1.3156 1.8765 0.0428  -0.7108 -0.0234 964  PRO B CD  
21664 N N   . LEU C 965  ? 2.6599 1.4695 2.1349 0.0178  -0.7368 -0.0405 965  LEU B N   
21665 C CA  . LEU C 965  ? 2.7856 1.5454 2.2268 0.0222  -0.7526 -0.0491 965  LEU B CA  
21666 C C   . LEU C 965  ? 2.8322 1.5783 2.2831 0.0172  -0.7837 -0.0658 965  LEU B C   
21667 O O   . LEU C 965  ? 2.8883 1.5954 2.3201 0.0154  -0.8001 -0.0756 965  LEU B O   
21668 C CB  . LEU C 965  ? 2.8715 1.6122 2.3143 0.0133  -0.7422 -0.0466 965  LEU B CB  
21669 C CG  . LEU C 965  ? 2.9813 1.7226 2.3983 0.0249  -0.7146 -0.0308 965  LEU B CG  
21670 C CD1 . LEU C 965  ? 3.0377 1.7558 2.4553 0.0158  -0.7050 -0.0293 965  LEU B CD1 
21671 C CD2 . LEU C 965  ? 3.0352 1.7516 2.3935 0.0490  -0.7116 -0.0258 965  LEU B CD2 
21672 N N   . ASP C 966  ? 2.7907 1.5680 2.2686 0.0156  -0.7917 -0.0691 966  ASP B N   
21673 C CA  . ASP C 966  ? 2.7711 1.5401 2.2565 0.0149  -0.8216 -0.0844 966  ASP B CA  
21674 C C   . ASP C 966  ? 2.6852 1.4390 2.1276 0.0348  -0.8297 -0.0851 966  ASP B C   
21675 O O   . ASP C 966  ? 2.6968 1.4459 2.1411 0.0381  -0.8534 -0.0964 966  ASP B O   
21676 C CB  . ASP C 966  ? 2.7777 1.5910 2.3265 -0.0006 -0.8271 -0.0893 966  ASP B CB  
21677 C CG  . ASP C 966  ? 2.7996 1.6204 2.3915 -0.0224 -0.8276 -0.0946 966  ASP B CG  
21678 O OD1 . ASP C 966  ? 2.8398 1.6260 2.4164 -0.0273 -0.8413 -0.1038 966  ASP B OD1 
21679 O OD2 . ASP C 966  ? 2.7746 1.6336 2.4136 -0.0355 -0.8133 -0.0898 966  ASP B OD2 
21680 N N   . LEU C 967  ? 2.5962 1.3425 1.9991 0.0484  -0.8096 -0.0732 967  LEU B N   
21681 C CA  . LEU C 967  ? 2.5313 1.2643 1.8923 0.0659  -0.8122 -0.0728 967  LEU B CA  
21682 C C   . LEU C 967  ? 2.5314 1.2142 1.8491 0.0773  -0.8372 -0.0844 967  LEU B C   
21683 O O   . LEU C 967  ? 2.5641 1.2120 1.8569 0.0790  -0.8407 -0.0863 967  LEU B O   
21684 C CB  . LEU C 967  ? 2.5285 1.2658 1.8573 0.0764  -0.7840 -0.0583 967  LEU B CB  
21685 C CG  . LEU C 967  ? 2.5655 1.2865 1.8465 0.0934  -0.7824 -0.0573 967  LEU B CG  
21686 C CD1 . LEU C 967  ? 2.5581 1.2965 1.8550 0.0919  -0.7922 -0.0627 967  LEU B CD1 
21687 C CD2 . LEU C 967  ? 2.5514 1.2880 1.8112 0.1002  -0.7526 -0.0433 967  LEU B CD2 
21688 N N   . VAL C 968  ? 2.4646 1.1409 1.7701 0.0859  -0.8544 -0.0922 968  VAL B N   
21689 C CA  . VAL C 968  ? 2.4537 1.0805 1.7118 0.0993  -0.8782 -0.1029 968  VAL B CA  
21690 C C   . VAL C 968  ? 2.4683 1.0574 1.6621 0.1164  -0.8638 -0.0955 968  VAL B C   
21691 O O   . VAL C 968  ? 2.4464 1.0447 1.6192 0.1254  -0.8448 -0.0867 968  VAL B O   
21692 C CB  . VAL C 968  ? 2.3975 1.0261 1.6538 0.1071  -0.8981 -0.1119 968  VAL B CB  
21693 C CG1 . VAL C 968  ? 2.3485 1.0080 1.6642 0.0929  -0.9182 -0.1223 968  VAL B CG1 
21694 C CG2 . VAL C 968  ? 2.3759 1.0280 1.6259 0.1130  -0.8762 -0.1017 968  VAL B CG2 
21695 N N   . PRO C 969  ? 2.5207 1.0671 1.6829 0.1202  -0.8719 -0.0992 969  PRO B N   
21696 C CA  . PRO C 969  ? 2.5907 1.0971 1.6912 0.1373  -0.8597 -0.0930 969  PRO B CA  
21697 C C   . PRO C 969  ? 2.6735 1.1639 1.7285 0.1549  -0.8563 -0.0917 969  PRO B C   
21698 O O   . PRO C 969  ? 2.6859 1.1713 1.7387 0.1580  -0.8748 -0.1006 969  PRO B O   
21699 C CB  . PRO C 969  ? 2.6300 1.0850 1.7036 0.1382  -0.8834 -0.1043 969  PRO B CB  
21700 C CG  . PRO C 969  ? 2.5965 1.0755 1.7269 0.1163  -0.8933 -0.1103 969  PRO B CG  
21701 C CD  . PRO C 969  ? 2.5335 1.0686 1.7201 0.1061  -0.8915 -0.1096 969  PRO B CD  
21702 N N   . LYS C 970  ? 2.7719 1.2532 1.7893 0.1669  -0.8321 -0.0809 970  LYS B N   
21703 C CA  . LYS C 970  ? 2.8878 1.3531 1.8584 0.1826  -0.8226 -0.0784 970  LYS B CA  
21704 C C   . LYS C 970  ? 2.8996 1.3948 1.8903 0.1785  -0.8224 -0.0797 970  LYS B C   
21705 O O   . LYS C 970  ? 2.9244 1.3910 1.8783 0.1895  -0.8324 -0.0858 970  LYS B O   
21706 C CB  . LYS C 970  ? 3.0336 1.4336 1.9428 0.1987  -0.8415 -0.0875 970  LYS B CB  
21707 C CG  . LYS C 970  ? 3.1680 1.5330 2.0318 0.2111  -0.8280 -0.0813 970  LYS B CG  
21708 C CD  . LYS C 970  ? 3.3149 1.6179 2.1089 0.2302  -0.8381 -0.0873 970  LYS B CD  
21709 C CE  . LYS C 970  ? 3.4023 1.6634 2.1496 0.2432  -0.8287 -0.0828 970  LYS B CE  
21710 N NZ  . LYS C 970  ? 3.4816 1.6770 2.1600 0.2612  -0.8411 -0.0898 970  LYS B NZ  
21711 N N   . THR C 971  ? 2.8989 1.4480 1.9447 0.1633  -0.8105 -0.0737 971  THR B N   
21712 C CA  . THR C 971  ? 2.9062 1.4871 1.9711 0.1586  -0.8043 -0.0724 971  THR B CA  
21713 C C   . THR C 971  ? 2.8580 1.4880 1.9503 0.1492  -0.7733 -0.0589 971  THR B C   
21714 O O   . THR C 971  ? 2.8439 1.5032 1.9778 0.1376  -0.7671 -0.0541 971  THR B O   
21715 C CB  . THR C 971  ? 2.9185 1.5190 2.0315 0.1479  -0.8268 -0.0814 971  THR B CB  
21716 O OG1 . THR C 971  ? 2.8544 1.5050 2.0266 0.1305  -0.8142 -0.0747 971  THR B OG1 
21717 C CG2 . THR C 971  ? 2.9854 1.5498 2.0921 0.1506  -0.8589 -0.0947 971  THR B CG2 
21718 N N   . GLU C 972  ? 2.8194 1.4566 1.8860 0.1537  -0.7539 -0.0534 972  GLU B N   
21719 C CA  . GLU C 972  ? 2.7543 1.4370 1.8391 0.1456  -0.7237 -0.0410 972  GLU B CA  
21720 C C   . GLU C 972  ? 2.5811 1.3088 1.7200 0.1290  -0.7213 -0.0390 972  GLU B C   
21721 O O   . GLU C 972  ? 2.5363 1.2589 1.6900 0.1266  -0.7399 -0.0471 972  GLU B O   
21722 C CB  . GLU C 972  ? 2.8702 1.5441 1.9085 0.1536  -0.7049 -0.0377 972  GLU B CB  
21723 C CG  . GLU C 972  ? 3.0178 1.6478 2.0160 0.1635  -0.7217 -0.0480 972  GLU B CG  
21724 C CD  . GLU C 972  ? 3.1186 1.7364 2.0686 0.1694  -0.7013 -0.0454 972  GLU B CD  
21725 O OE1 . GLU C 972  ? 3.1108 1.7679 2.0720 0.1601  -0.6745 -0.0365 972  GLU B OE1 
21726 O OE2 . GLU C 972  ? 3.1968 1.7649 2.0967 0.1828  -0.7122 -0.0529 972  GLU B OE2 
21727 N N   . ILE C 973  ? 2.4712 1.2427 1.6390 0.1188  -0.6985 -0.0283 973  ILE B N   
21728 C CA  . ILE C 973  ? 2.3362 1.1496 1.5526 0.1030  -0.6931 -0.0253 973  ILE B CA  
21729 C C   . ILE C 973  ? 2.3768 1.2070 1.5788 0.0996  -0.6750 -0.0213 973  ILE B C   
21730 O O   . ILE C 973  ? 2.4028 1.2516 1.5900 0.0986  -0.6515 -0.0131 973  ILE B O   
21731 C CB  . ILE C 973  ? 2.1580 1.0089 1.4129 0.0927  -0.6783 -0.0161 973  ILE B CB  
21732 C CG1 . ILE C 973  ? 2.1326 0.9637 1.3969 0.0950  -0.6923 -0.0193 973  ILE B CG1 
21733 C CG2 . ILE C 973  ? 2.0611 0.9483 1.3644 0.0770  -0.6756 -0.0143 973  ILE B CG2 
21734 C CD1 . ILE C 973  ? 2.1044 0.9631 1.3928 0.0892  -0.6754 -0.0094 973  ILE B CD1 
21735 N N   . LYS C 974  ? 2.3832 1.2069 1.5891 0.0977  -0.6862 -0.0275 974  LYS B N   
21736 C CA  . LYS C 974  ? 2.3500 1.1841 1.5410 0.0932  -0.6704 -0.0248 974  LYS B CA  
21737 C C   . LYS C 974  ? 2.2370 1.1204 1.4765 0.0758  -0.6554 -0.0169 974  LYS B C   
21738 O O   . LYS C 974  ? 2.2053 1.1064 1.4910 0.0690  -0.6653 -0.0174 974  LYS B O   
21739 C CB  . LYS C 974  ? 2.4362 1.2354 1.6039 0.1021  -0.6897 -0.0350 974  LYS B CB  
21740 C CG  . LYS C 974  ? 2.5143 1.3084 1.6505 0.1006  -0.6744 -0.0338 974  LYS B CG  
21741 C CD  . LYS C 974  ? 2.6371 1.3906 1.7458 0.1137  -0.6963 -0.0443 974  LYS B CD  
21742 C CE  . LYS C 974  ? 2.6857 1.4414 1.7816 0.1093  -0.6838 -0.0430 974  LYS B CE  
21743 N NZ  . LYS C 974  ? 2.7302 1.4446 1.7945 0.1250  -0.7044 -0.0528 974  LYS B NZ  
21744 N N   . ARG C 975  ? 2.1658 1.0707 1.3934 0.0677  -0.6306 -0.0099 975  ARG B N   
21745 C CA  . ARG C 975  ? 2.0479 0.9940 1.3128 0.0513  -0.6160 -0.0031 975  ARG B CA  
21746 C C   . ARG C 975  ? 1.9935 0.9481 1.2291 0.0440  -0.5926 0.0010  975  ARG B C   
21747 O O   . ARG C 975  ? 2.0099 0.9602 1.2103 0.0468  -0.5788 0.0028  975  ARG B O   
21748 C CB  . ARG C 975  ? 1.9994 0.9814 1.3021 0.0436  -0.6068 0.0050  975  ARG B CB  
21749 C CG  . ARG C 975  ? 1.9844 0.9721 1.2623 0.0486  -0.5922 0.0101  975  ARG B CG  
21750 C CD  . ARG C 975  ? 1.9634 0.9656 1.2699 0.0497  -0.5941 0.0145  975  ARG B CD  
21751 N NE  . ARG C 975  ? 1.9607 0.9712 1.2426 0.0570  -0.5791 0.0201  975  ARG B NE  
21752 C CZ  . ARG C 975  ? 1.9194 0.9690 1.2186 0.0517  -0.5614 0.0294  975  ARG B CZ  
21753 N NH1 . ARG C 975  ? 1.8669 0.9475 1.2069 0.0383  -0.5563 0.0343  975  ARG B NH1 
21754 N NH2 . ARG C 975  ? 1.9351 0.9925 1.2102 0.0610  -0.5490 0.0336  975  ARG B NH2 
21755 N N   . ILE C 976  ? 1.9047 0.8710 1.1545 0.0340  -0.5877 0.0020  976  ILE B N   
21756 C CA  . ILE C 976  ? 1.8695 0.8370 1.0882 0.0254  -0.5669 0.0044  976  ILE B CA  
21757 C C   . ILE C 976  ? 1.8093 0.8231 1.0581 0.0068  -0.5458 0.0137  976  ILE B C   
21758 O O   . ILE C 976  ? 1.8159 0.8533 1.1112 0.0008  -0.5505 0.0169  976  ILE B O   
21759 C CB  . ILE C 976  ? 1.8766 0.8174 1.0827 0.0291  -0.5765 -0.0014 976  ILE B CB  
21760 C CG1 . ILE C 976  ? 1.9597 0.8635 1.1574 0.0478  -0.6055 -0.0109 976  ILE B CG1 
21761 C CG2 . ILE C 976  ? 1.8782 0.8010 1.0329 0.0243  -0.5570 -0.0014 976  ILE B CG2 
21762 C CD1 . ILE C 976  ? 1.9900 0.8905 1.2168 0.0515  -0.6249 -0.0158 976  ILE B CD1 
21763 N N   . LEU C 977  ? 1.7390 0.7644 0.9598 -0.0032 -0.5223 0.0173  977  LEU B N   
21764 C CA  . LEU C 977  ? 1.6404 0.7094 0.8821 -0.0220 -0.5008 0.0256  977  LEU B CA  
21765 C C   . LEU C 977  ? 1.6243 0.6842 0.8394 -0.0344 -0.4859 0.0252  977  LEU B C   
21766 O O   . LEU C 977  ? 1.6552 0.6910 0.8224 -0.0340 -0.4767 0.0213  977  LEU B O   
21767 C CB  . LEU C 977  ? 1.6101 0.7044 0.8402 -0.0244 -0.4850 0.0296  977  LEU B CB  
21768 C CG  . LEU C 977  ? 1.5753 0.7198 0.8286 -0.0423 -0.4648 0.0379  977  LEU B CG  
21769 C CD1 . LEU C 977  ? 1.5517 0.7271 0.8387 -0.0368 -0.4678 0.0435  977  LEU B CD1 
21770 C CD2 . LEU C 977  ? 1.6301 0.7835 0.8455 -0.0514 -0.4434 0.0375  977  LEU B CD2 
21771 N N   . SER C 978  ? 1.6172 0.6938 0.8598 -0.0457 -0.4818 0.0292  978  SER B N   
21772 C CA  . SER C 978  ? 1.6836 0.7460 0.8978 -0.0567 -0.4677 0.0289  978  SER B CA  
21773 C C   . SER C 978  ? 1.7776 0.8787 1.0069 -0.0792 -0.4453 0.0368  978  SER B C   
21774 O O   . SER C 978  ? 1.8244 0.9396 1.0863 -0.0856 -0.4457 0.0410  978  SER B O   
21775 C CB  . SER C 978  ? 1.6647 0.6972 0.8834 -0.0471 -0.4838 0.0247  978  SER B CB  
21776 O OG  . SER C 978  ? 1.6437 0.6603 0.8311 -0.0570 -0.4682 0.0253  978  SER B OG  
21777 N N   . VAL C 979  ? 1.7911 0.9085 0.9947 -0.0914 -0.4254 0.0382  979  VAL B N   
21778 C CA  . VAL C 979  ? 1.7308 0.8890 0.9451 -0.1136 -0.4040 0.0448  979  VAL B CA  
21779 C C   . VAL C 979  ? 1.7448 0.8847 0.9236 -0.1302 -0.3865 0.0440  979  VAL B C   
21780 O O   . VAL C 979  ? 1.7938 0.9059 0.9234 -0.1326 -0.3770 0.0387  979  VAL B O   
21781 C CB  . VAL C 979  ? 1.6937 0.8804 0.8953 -0.1185 -0.3913 0.0453  979  VAL B CB  
21782 C CG1 . VAL C 979  ? 1.6322 0.8694 0.8532 -0.1388 -0.3735 0.0519  979  VAL B CG1 
21783 C CG2 . VAL C 979  ? 1.6827 0.8744 0.9038 -0.0990 -0.4074 0.0448  979  VAL B CG2 
21784 N N   . LYS C 980  ? 1.7178 0.8697 0.9169 -0.1420 -0.3806 0.0492  980  LYS B N   
21785 C CA  . LYS C 980  ? 1.7467 0.8793 0.9069 -0.1592 -0.3616 0.0488  980  LYS B CA  
21786 C C   . LYS C 980  ? 1.7299 0.8939 0.9083 -0.1810 -0.3457 0.0560  980  LYS B C   
21787 O O   . LYS C 980  ? 1.7143 0.9050 0.9396 -0.1799 -0.3524 0.0618  980  LYS B O   
21788 C CB  . LYS C 980  ? 1.8016 0.8810 0.9366 -0.1465 -0.3706 0.0445  980  LYS B CB  
21789 C CG  . LYS C 980  ? 1.8138 0.8830 0.9841 -0.1229 -0.3975 0.0429  980  LYS B CG  
21790 C CD  . LYS C 980  ? 1.8173 0.8540 0.9609 -0.1034 -0.4125 0.0350  980  LYS B CD  
21791 C CE  . LYS C 980  ? 1.8344 0.8186 0.9152 -0.1002 -0.4059 0.0291  980  LYS B CE  
21792 N NZ  . LYS C 980  ? 1.8563 0.8129 0.9116 -0.0824 -0.4190 0.0220  980  LYS B NZ  
21793 N N   . GLY C 981  ? 1.7277 0.8854 0.8657 -0.2018 -0.3238 0.0551  981  GLY B N   
21794 C CA  . GLY C 981  ? 1.6826 0.8645 0.8299 -0.2239 -0.3080 0.0612  981  GLY B CA  
21795 C C   . GLY C 981  ? 1.6583 0.8102 0.8109 -0.2182 -0.3127 0.0638  981  GLY B C   
21796 O O   . GLY C 981  ? 1.6993 0.8070 0.8304 -0.2021 -0.3222 0.0594  981  GLY B O   
21797 N N   . LEU C 982  ? 1.5988 0.7755 0.7800 -0.2302 -0.3064 0.0710  982  LEU B N   
21798 C CA  . LEU C 982  ? 1.5938 0.7479 0.7824 -0.2277 -0.3068 0.0748  982  LEU B CA  
21799 C C   . LEU C 982  ? 1.6405 0.7948 0.8780 -0.2049 -0.3291 0.0762  982  LEU B C   
21800 O O   . LEU C 982  ? 1.6492 0.7939 0.8951 -0.1854 -0.3474 0.0711  982  LEU B O   
21801 C CB  . LEU C 982  ? 1.6091 0.7097 0.7392 -0.2296 -0.2963 0.0709  982  LEU B CB  
21802 C CG  . LEU C 982  ? 1.6216 0.7159 0.6982 -0.2548 -0.2723 0.0684  982  LEU B CG  
21803 C CD1 . LEU C 982  ? 1.6501 0.7102 0.6885 -0.2683 -0.2546 0.0707  982  LEU B CD1 
21804 C CD2 . LEU C 982  ? 1.5889 0.7400 0.6911 -0.2738 -0.2643 0.0716  982  LEU B CD2 
21805 N N   . LEU C 983  ? 1.6530 0.8179 0.9218 -0.2087 -0.3269 0.0827  983  LEU B N   
21806 C CA  . LEU C 983  ? 1.6612 0.8303 0.9799 -0.1910 -0.3451 0.0841  983  LEU B CA  
21807 C C   . LEU C 983  ? 1.7693 0.8958 1.0688 -0.1725 -0.3562 0.0783  983  LEU B C   
21808 O O   . LEU C 983  ? 1.7539 0.8784 1.0866 -0.1539 -0.3760 0.0756  983  LEU B O   
21809 C CB  . LEU C 983  ? 1.6086 0.7944 0.9572 -0.2014 -0.3356 0.0924  983  LEU B CB  
21810 C CG  . LEU C 983  ? 1.5670 0.7978 0.9527 -0.2120 -0.3322 0.0985  983  LEU B CG  
21811 C CD1 . LEU C 983  ? 1.5461 0.7997 0.9245 -0.2135 -0.3346 0.0957  983  LEU B CD1 
21812 C CD2 . LEU C 983  ? 1.5818 0.8223 0.9575 -0.2336 -0.3113 0.1056  983  LEU B CD2 
21813 N N   . VAL C 984  ? 1.2356 0.7724 0.8720 -0.1299 -0.1132 0.1263  984  VAL B N   
21814 C CA  . VAL C 984  ? 1.3341 0.8321 0.9380 -0.1264 -0.1120 0.1185  984  VAL B CA  
21815 C C   . VAL C 984  ? 1.4350 0.9195 1.0081 -0.1079 -0.0995 0.1121  984  VAL B C   
21816 O O   . VAL C 984  ? 1.5048 0.9684 1.0483 -0.1082 -0.0892 0.1092  984  VAL B O   
21817 C CB  . VAL C 984  ? 1.2878 0.7914 0.8880 -0.1513 -0.1004 0.1222  984  VAL B CB  
21818 C CG1 . VAL C 984  ? 1.3133 0.8266 0.8944 -0.1595 -0.0759 0.1233  984  VAL B CG1 
21819 C CG2 . VAL C 984  ? 1.3030 0.7706 0.8854 -0.1495 -0.1097 0.1175  984  VAL B CG2 
21820 N N   . GLY C 985  ? 1.4713 0.9690 1.0513 -0.0905 -0.1003 0.1107  985  GLY B N   
21821 C CA  . GLY C 985  ? 1.4794 0.9723 1.0326 -0.0713 -0.0885 0.1046  985  GLY B CA  
21822 C C   . GLY C 985  ? 1.5108 0.9639 1.0387 -0.0454 -0.1007 0.0918  985  GLY B C   
21823 O O   . GLY C 985  ? 1.5111 0.9555 1.0087 -0.0337 -0.0895 0.0868  985  GLY B O   
21824 N N   . GLU C 986  ? 1.4984 0.9291 1.0373 -0.0370 -0.1233 0.0865  986  GLU B N   
21825 C CA  . GLU C 986  ? 1.4985 0.8907 1.0106 -0.0175 -0.1353 0.0733  986  GLU B CA  
21826 C C   . GLU C 986  ? 1.5006 0.8764 0.9904 -0.0282 -0.1312 0.0742  986  GLU B C   
21827 O O   . GLU C 986  ? 1.5491 0.9118 1.0067 -0.0171 -0.1224 0.0691  986  GLU B O   
21828 C CB  . GLU C 986  ? 1.5059 0.8751 1.0333 -0.0125 -0.1610 0.0681  986  GLU B CB  
21829 C CG  . GLU C 986  ? 1.5537 0.8934 1.0599 0.0138  -0.1714 0.0521  986  GLU B CG  
21830 C CD  . GLU C 986  ? 1.5970 0.9534 1.1051 0.0334  -0.1609 0.0493  986  GLU B CD  
21831 O OE1 . GLU C 986  ? 1.6027 0.9484 1.1244 0.0469  -0.1733 0.0448  986  GLU B OE1 
21832 O OE2 . GLU C 986  ? 1.6239 1.0052 1.1198 0.0353  -0.1396 0.0525  986  GLU B OE2 
21833 N N   . ILE C 987  ? 1.4388 0.8174 0.9451 -0.0488 -0.1363 0.0817  987  ILE B N   
21834 C CA  . ILE C 987  ? 1.4393 0.7986 0.9244 -0.0550 -0.1351 0.0820  987  ILE B CA  
21835 C C   . ILE C 987  ? 1.5020 0.8630 0.9614 -0.0574 -0.1114 0.0857  987  ILE B C   
21836 O O   . ILE C 987  ? 1.5409 0.8812 0.9757 -0.0567 -0.1080 0.0859  987  ILE B O   
21837 C CB  . ILE C 987  ? 1.3769 0.7446 0.8826 -0.0766 -0.1395 0.0898  987  ILE B CB  
21838 C CG1 . ILE C 987  ? 1.4497 0.8346 0.9928 -0.0836 -0.1553 0.0932  987  ILE B CG1 
21839 C CG2 . ILE C 987  ? 1.3270 0.6701 0.8144 -0.0740 -0.1491 0.0870  987  ILE B CG2 
21840 C CD1 . ILE C 987  ? 1.4856 0.8761 1.0470 -0.1014 -0.1665 0.0989  987  ILE B CD1 
21841 N N   . LEU C 988  ? 1.5174 0.9048 0.9831 -0.0615 -0.0948 0.0900  988  LEU B N   
21842 C CA  . LEU C 988  ? 1.5537 0.9437 0.9941 -0.0659 -0.0718 0.0945  988  LEU B CA  
21843 C C   . LEU C 988  ? 1.5929 0.9745 1.0050 -0.0418 -0.0680 0.0875  988  LEU B C   
21844 O O   . LEU C 988  ? 1.6443 1.0079 1.0248 -0.0376 -0.0589 0.0885  988  LEU B O   
21845 C CB  . LEU C 988  ? 1.5531 0.9812 1.0125 -0.0848 -0.0549 0.1030  988  LEU B CB  
21846 C CG  . LEU C 988  ? 1.5309 0.9662 1.0045 -0.1133 -0.0492 0.1104  988  LEU B CG  
21847 C CD1 . LEU C 988  ? 1.5390 1.0177 1.0314 -0.1312 -0.0338 0.1175  988  LEU B CD1 
21848 C CD2 . LEU C 988  ? 1.5321 0.9352 0.9747 -0.1204 -0.0389 0.1124  988  LEU B CD2 
21849 N N   . SER C 989  ? 1.5993 0.9940 1.0218 -0.0249 -0.0746 0.0807  989  SER B N   
21850 C CA  . SER C 989  ? 1.6189 1.0093 1.0148 0.0001  -0.0710 0.0720  989  SER B CA  
21851 C C   . SER C 989  ? 1.5884 0.9419 0.9564 0.0141  -0.0840 0.0628  989  SER B C   
21852 O O   . SER C 989  ? 1.5956 0.9419 0.9309 0.0277  -0.0760 0.0596  989  SER B O   
21853 C CB  . SER C 989  ? 1.6432 1.0497 1.0564 0.0182  -0.0781 0.0644  989  SER B CB  
21854 O OG  . SER C 989  ? 1.6927 1.0967 1.0783 0.0437  -0.0738 0.0541  989  SER B OG  
21855 N N   . ALA C 990  ? 1.5612 0.8953 0.9419 0.0097  -0.1040 0.0597  990  ALA B N   
21856 C CA  . ALA C 990  ? 1.6017 0.9067 0.9578 0.0216  -0.1176 0.0514  990  ALA B CA  
21857 C C   . ALA C 990  ? 1.6090 0.9032 0.9365 0.0172  -0.1050 0.0594  990  ALA B C   
21858 O O   . ALA C 990  ? 1.6678 0.9458 0.9650 0.0323  -0.1084 0.0541  990  ALA B O   
21859 C CB  . ALA C 990  ? 1.5941 0.8855 0.9713 0.0156  -0.1422 0.0477  990  ALA B CB  
21860 N N   . VAL C 991  ? 1.5711 0.8729 0.9064 -0.0031 -0.0904 0.0722  991  VAL B N   
21861 C CA  . VAL C 991  ? 1.5989 0.8832 0.9062 -0.0064 -0.0790 0.0804  991  VAL B CA  
21862 C C   . VAL C 991  ? 1.6409 0.9330 0.9248 -0.0066 -0.0544 0.0877  991  VAL B C   
21863 O O   . VAL C 991  ? 1.6731 0.9478 0.9267 -0.0043 -0.0438 0.0947  991  VAL B O   
21864 C CB  . VAL C 991  ? 1.2756 0.5528 0.5983 -0.0266 -0.0802 0.0885  991  VAL B CB  
21865 C CG1 . VAL C 991  ? 1.2770 0.5343 0.5713 -0.0315 -0.0633 0.0987  991  VAL B CG1 
21866 C CG2 . VAL C 991  ? 1.2703 0.5387 0.6056 -0.0218 -0.1053 0.0820  991  VAL B CG2 
21867 N N   . LEU C 992  ? 1.6518 0.9715 0.9486 -0.0080 -0.0456 0.0869  992  LEU B N   
21868 C CA  . LEU C 992  ? 1.7362 1.0694 1.0126 -0.0105 -0.0224 0.0948  992  LEU B CA  
21869 C C   . LEU C 992  ? 1.9404 1.2953 1.2108 0.0108  -0.0216 0.0861  992  LEU B C   
21870 O O   . LEU C 992  ? 2.0090 1.3960 1.2875 0.0056  -0.0069 0.0904  992  LEU B O   
21871 C CB  . LEU C 992  ? 1.6320 0.9870 0.9286 -0.0382 -0.0061 0.1056  992  LEU B CB  
21872 C CG  . LEU C 992  ? 1.5472 0.8894 0.8616 -0.0608 -0.0094 0.1104  992  LEU B CG  
21873 C CD1 . LEU C 992  ? 1.4935 0.8693 0.8356 -0.0844 0.0013  0.1158  992  LEU B CD1 
21874 C CD2 . LEU C 992  ? 1.5798 0.8891 0.8647 -0.0683 0.0015  0.1189  992  LEU B CD2 
21875 N N   . SER C 993  ? 2.0684 1.4081 1.3240 0.0347  -0.0372 0.0733  993  SER B N   
21876 C CA  . SER C 993  ? 2.1915 1.5477 1.4351 0.0583  -0.0362 0.0626  993  SER B CA  
21877 C C   . SER C 993  ? 2.3476 1.6811 1.5577 0.0794  -0.0462 0.0530  993  SER B C   
21878 O O   . SER C 993  ? 2.3884 1.7328 1.5745 0.0988  -0.0406 0.0463  993  SER B O   
21879 C CB  . SER C 993  ? 2.1684 1.5351 1.4426 0.0665  -0.0503 0.0510  993  SER B CB  
21880 O OG  . SER C 993  ? 2.1349 1.5323 1.4385 0.0501  -0.0392 0.0606  993  SER B OG  
21881 N N   . GLN C 994  ? 2.4426 1.7484 1.6516 0.0755  -0.0615 0.0521  994  GLN B N   
21882 C CA  . GLN C 994  ? 2.5613 1.8478 1.7390 0.0919  -0.0716 0.0456  994  GLN B CA  
21883 C C   . GLN C 994  ? 2.5926 1.8637 1.7541 0.0806  -0.0625 0.0620  994  GLN B C   
21884 O O   . GLN C 994  ? 2.5365 1.8010 1.7182 0.0609  -0.0608 0.0714  994  GLN B O   
21885 C CB  . GLN C 994  ? 2.6188 1.8885 1.8101 0.0972  -0.0991 0.0308  994  GLN B CB  
21886 C CG  . GLN C 994  ? 2.6383 1.8999 1.8603 0.0761  -0.1079 0.0383  994  GLN B CG  
21887 C CD  . GLN C 994  ? 2.6826 1.9252 1.8954 0.0772  -0.1250 0.0369  994  GLN B CD  
21888 O OE1 . GLN C 994  ? 2.7265 1.9616 1.9194 0.0932  -0.1386 0.0247  994  GLN B OE1 
21889 N NE2 . GLN C 994  ? 2.6641 1.9016 1.8906 0.0604  -0.1242 0.0489  994  GLN B NE2 
21890 N N   . GLU C 995  ? 2.6864 1.9514 1.8106 0.0938  -0.0564 0.0657  995  GLU B N   
21891 C CA  . GLU C 995  ? 2.7600 2.0048 1.8653 0.0880  -0.0499 0.0814  995  GLU B CA  
21892 C C   . GLU C 995  ? 2.7597 1.9883 1.8651 0.0952  -0.0726 0.0747  995  GLU B C   
21893 O O   . GLU C 995  ? 2.7430 1.9752 1.8587 0.1038  -0.0927 0.0578  995  GLU B O   
21894 C CB  . GLU C 995  ? 2.8436 2.0896 1.9081 0.0993  -0.0333 0.0917  995  GLU B CB  
21895 C CG  . GLU C 995  ? 2.8938 2.1444 1.9528 0.0824  -0.0064 0.1098  995  GLU B CG  
21896 C CD  . GLU C 995  ? 2.9349 2.2186 1.9945 0.0856  0.0056  0.1057  995  GLU B CD  
21897 O OE1 . GLU C 995  ? 2.9494 2.2480 2.0032 0.1065  -0.0049 0.0895  995  GLU B OE1 
21898 O OE2 . GLU C 995  ? 2.9438 2.2393 2.0087 0.0671  0.0256  0.1182  995  GLU B OE2 
21899 N N   . GLY C 996  ? 2.7883 1.9991 1.8813 0.0918  -0.0693 0.0882  996  GLY B N   
21900 C CA  . GLY C 996  ? 2.8197 2.0210 1.9112 0.0994  -0.0894 0.0844  996  GLY B CA  
21901 C C   . GLY C 996  ? 2.8221 2.0273 1.9511 0.0890  -0.1097 0.0732  996  GLY B C   
21902 O O   . GLY C 996  ? 2.8113 2.0265 1.9569 0.0897  -0.1199 0.0588  996  GLY B O   
21903 N N   . ILE C 997  ? 2.8246 2.0215 1.9658 0.0802  -0.1155 0.0803  997  ILE B N   
21904 C CA  . ILE C 997  ? 2.8000 2.0030 1.9775 0.0678  -0.1337 0.0733  997  ILE B CA  
21905 C C   . ILE C 997  ? 2.8502 2.0605 2.0326 0.0765  -0.1585 0.0557  997  ILE B C   
21906 O O   . ILE C 997  ? 2.8914 2.1016 2.0465 0.0932  -0.1657 0.0496  997  ILE B O   
21907 C CB  . ILE C 997  ? 2.7548 1.9510 1.9365 0.0625  -0.1365 0.0835  997  ILE B CB  
21908 C CG1 . ILE C 997  ? 2.7492 1.9480 1.9132 0.0788  -0.1542 0.0804  997  ILE B CG1 
21909 C CG2 . ILE C 997  ? 2.7491 1.9287 1.9116 0.0600  -0.1116 0.0997  997  ILE B CG2 
21910 C CD1 . ILE C 997  ? 2.7493 1.9412 1.9043 0.0823  -0.1512 0.0936  997  ILE B CD1 
21911 N N   . ASN C 998  ? 2.8584 2.0744 2.0747 0.0643  -0.1717 0.0479  998  ASN B N   
21912 C CA  . ASN C 998  ? 2.8822 2.0991 2.1044 0.0697  -0.1939 0.0305  998  ASN B CA  
21913 C C   . ASN C 998  ? 2.7790 1.9993 2.0393 0.0529  -0.2120 0.0280  998  ASN B C   
21914 O O   . ASN C 998  ? 2.7965 2.0227 2.0834 0.0379  -0.2039 0.0366  998  ASN B O   
21915 C CB  . ASN C 998  ? 2.9807 2.1975 2.1957 0.0795  -0.1860 0.0202  998  ASN B CB  
21916 C CG  . ASN C 998  ? 3.0659 2.2780 2.2985 0.0799  -0.2062 0.0031  998  ASN B CG  
21917 O OD1 . ASN C 998  ? 3.1041 2.3098 2.3326 0.0820  -0.2278 -0.0076 998  ASN B OD1 
21918 N ND2 . ASN C 998  ? 3.0840 2.2992 2.3356 0.0779  -0.1992 0.0009  998  ASN B ND2 
21919 N N   . ILE C 999  ? 2.6765 1.8949 1.9387 0.0540  -0.2364 0.0166  999  ILE B N   
21920 C CA  . ILE C 999  ? 2.5314 1.7523 1.8281 0.0373  -0.2562 0.0141  999  ILE B CA  
21921 C C   . ILE C 999  ? 2.4199 1.6336 1.7374 0.0342  -0.2572 0.0068  999  ILE B C   
21922 O O   . ILE C 999  ? 2.4289 1.6348 1.7305 0.0484  -0.2493 -0.0026 999  ILE B O   
21923 C CB  . ILE C 999  ? 3.9451 3.1657 3.2359 0.0371  -0.2831 0.0038  999  ILE B CB  
21924 C CG1 . ILE C 999  ? 3.9568 3.1872 3.2199 0.0472  -0.2823 0.0089  999  ILE B CG1 
21925 C CG2 . ILE C 999  ? 3.9153 3.1433 3.2425 0.0160  -0.3017 0.0074  999  ILE B CG2 
21926 C CD1 . ILE C 999  ? 3.9291 3.1737 3.2051 0.0388  -0.2759 0.0264  999  ILE B CD1 
21927 N N   . LEU C 1000 ? 2.3107 1.5293 1.6637 0.0169  -0.2669 0.0119  1000 LEU B N   
21928 C CA  . LEU C 1000 ? 2.2077 1.4230 1.5830 0.0143  -0.2644 0.0100  1000 LEU B CA  
21929 C C   . LEU C 1000 ? 2.1734 1.3708 1.5589 0.0133  -0.2882 -0.0028 1000 LEU B C   
21930 O O   . LEU C 1000 ? 2.1616 1.3546 1.5713 0.0090  -0.2911 -0.0020 1000 LEU B O   
21931 C CB  . LEU C 1000 ? 2.0817 1.3161 1.4884 -0.0030 -0.2537 0.0265  1000 LEU B CB  
21932 C CG  . LEU C 1000 ? 1.9670 1.2112 1.3629 0.0011  -0.2259 0.0341  1000 LEU B CG  
21933 C CD1 . LEU C 1000 ? 1.8992 1.1628 1.3273 -0.0170 -0.2168 0.0471  1000 LEU B CD1 
21934 C CD2 . LEU C 1000 ? 1.9459 1.1833 1.3236 0.0196  -0.2160 0.0241  1000 LEU B CD2 
21935 N N   . THR C 1001 ? 2.1471 1.3329 1.5124 0.0174  -0.3053 -0.0147 1001 THR B N   
21936 C CA  . THR C 1001 ? 2.1306 1.2936 1.5010 0.0155  -0.3276 -0.0288 1001 THR B CA  
21937 C C   . THR C 1001 ? 2.2248 1.3720 1.5579 0.0306  -0.3364 -0.0486 1001 THR B C   
21938 O O   . THR C 1001 ? 2.2808 1.4363 1.5852 0.0455  -0.3227 -0.0504 1001 THR B O   
21939 C CB  . THR C 1001 ? 2.0383 1.2075 1.4352 -0.0077 -0.3479 -0.0209 1001 THR B CB  
21940 O OG1 . THR C 1001 ? 1.9238 1.1209 1.3414 -0.0196 -0.3360 -0.0011 1001 THR B OG1 
21941 C CG2 . THR C 1001 ? 2.0341 1.1818 1.4548 -0.0157 -0.3623 -0.0245 1001 THR B CG2 
21942 N N   . HIS C 1002 ? 2.2663 1.3900 1.5985 0.0266  -0.3592 -0.0638 1002 HIS B N   
21943 C CA  . HIS C 1002 ? 2.2865 1.3994 1.5837 0.0362  -0.3710 -0.0831 1002 HIS B CA  
21944 C C   . HIS C 1002 ? 2.1037 1.2371 1.3991 0.0212  -0.3860 -0.0772 1002 HIS B C   
21945 O O   . HIS C 1002 ? 2.0995 1.2321 1.3676 0.0257  -0.3980 -0.0911 1002 HIS B O   
21946 C CB  . HIS C 1002 ? 2.4740 1.5487 1.7648 0.0398  -0.3879 -0.1056 1002 HIS B CB  
21947 C CG  . HIS C 1002 ? 2.5933 1.6512 1.8808 0.0604  -0.3725 -0.1131 1002 HIS B CG  
21948 N ND1 . HIS C 1002 ? 2.6159 1.6606 1.9335 0.0568  -0.3713 -0.1063 1002 HIS B ND1 
21949 C CD2 . HIS C 1002 ? 2.6542 1.7105 1.9120 0.0857  -0.3576 -0.1260 1002 HIS B CD2 
21950 C CE1 . HIS C 1002 ? 2.6441 1.6805 1.9509 0.0800  -0.3563 -0.1150 1002 HIS B CE1 
21951 N NE2 . HIS C 1002 ? 2.6661 1.7099 1.9368 0.0974  -0.3476 -0.1272 1002 HIS B NE2 
21952 N N   . LEU C 1003 ? 1.9544 1.1104 1.2782 0.0046  -0.3847 -0.0568 1003 LEU B N   
21953 C CA  . LEU C 1003 ? 1.8750 1.0545 1.2022 -0.0100 -0.4002 -0.0500 1003 LEU B CA  
21954 C C   . LEU C 1003 ? 1.9179 1.1188 1.2134 0.0038  -0.3943 -0.0495 1003 LEU B C   
21955 O O   . LEU C 1003 ? 1.9254 1.1396 1.2138 0.0151  -0.3725 -0.0369 1003 LEU B O   
21956 C CB  . LEU C 1003 ? 1.7289 0.9300 1.0938 -0.0292 -0.3992 -0.0288 1003 LEU B CB  
21957 C CG  . LEU C 1003 ? 1.6171 0.8019 1.0139 -0.0473 -0.4130 -0.0279 1003 LEU B CG  
21958 C CD1 . LEU C 1003 ? 1.5390 0.7489 0.9634 -0.0724 -0.4299 -0.0146 1003 LEU B CD1 
21959 C CD2 . LEU C 1003 ? 1.6497 0.7972 1.0300 -0.0436 -0.4290 -0.0502 1003 LEU B CD2 
21960 N N   . PRO C 1004 ? 1.9034 1.1077 1.1798 0.0016  -0.4146 -0.0625 1004 PRO B N   
21961 C CA  . PRO C 1004 ? 1.9160 1.1413 1.1602 0.0127  -0.4183 -0.0665 1004 PRO B CA  
21962 C C   . PRO C 1004 ? 1.8360 1.0958 1.0822 0.0163  -0.4078 -0.0452 1004 PRO B C   
21963 O O   . PRO C 1004 ? 1.8177 1.0952 1.0923 0.0008  -0.4123 -0.0310 1004 PRO B O   
21964 C CB  . PRO C 1004 ? 1.9342 1.1617 1.1806 -0.0061 -0.4488 -0.0791 1004 PRO B CB  
21965 C CG  . PRO C 1004 ? 1.9062 1.1201 1.1924 -0.0297 -0.4587 -0.0732 1004 PRO B CG  
21966 C CD  . PRO C 1004 ? 1.9070 1.0921 1.1973 -0.0175 -0.4399 -0.0747 1004 PRO B CD  
21967 N N   . LYS C 1005 ? 1.8471 1.1165 1.0615 0.0375  -0.3944 -0.0431 1005 LYS B N   
21968 C CA  . LYS C 1005 ? 1.8727 1.1633 1.0859 0.0463  -0.3775 -0.0218 1005 LYS B CA  
21969 C C   . LYS C 1005 ? 1.8737 1.2006 1.0900 0.0421  -0.3905 -0.0114 1005 LYS B C   
21970 O O   . LYS C 1005 ? 1.8423 1.1837 1.0526 0.0539  -0.3758 0.0053  1005 LYS B O   
21971 C CB  . LYS C 1005 ? 1.9742 1.2589 1.1518 0.0714  -0.3554 -0.0193 1005 LYS B CB  
21972 C CG  . LYS C 1005 ? 2.0755 1.3331 1.2514 0.0776  -0.3359 -0.0233 1005 LYS B CG  
21973 C CD  . LYS C 1005 ? 2.1341 1.3882 1.3284 0.0744  -0.3131 -0.0045 1005 LYS B CD  
21974 C CE  . LYS C 1005 ? 2.2002 1.4626 1.3709 0.0898  -0.2942 0.0122  1005 LYS B CE  
21975 N NZ  . LYS C 1005 ? 2.2001 1.4546 1.3882 0.0834  -0.2727 0.0280  1005 LYS B NZ  
21976 N N   . GLY C 1006 ? 1.9090 1.2513 1.1344 0.0259  -0.4171 -0.0201 1006 GLY B N   
21977 C CA  . GLY C 1006 ? 1.9262 1.3108 1.1493 0.0253  -0.4295 -0.0111 1006 GLY B CA  
21978 C C   . GLY C 1006 ? 1.8488 1.2596 1.0933 0.0243  -0.4212 0.0110  1006 GLY B C   
21979 O O   . GLY C 1006 ? 1.8048 1.2420 1.0348 0.0409  -0.4150 0.0233  1006 GLY B O   
21980 N N   . SER C 1007 ? 1.8076 1.2112 1.0870 0.0054  -0.4215 0.0158  1007 SER B N   
21981 C CA  . SER C 1007 ? 1.7521 1.1812 1.0557 0.0006  -0.4161 0.0339  1007 SER B CA  
21982 C C   . SER C 1007 ? 1.6954 1.1156 0.9835 0.0232  -0.3881 0.0465  1007 SER B C   
21983 O O   . SER C 1007 ? 1.6721 1.0631 0.9370 0.0378  -0.3715 0.0426  1007 SER B O   
21984 C CB  . SER C 1007 ? 1.7544 1.1737 1.0966 -0.0236 -0.4195 0.0358  1007 SER B CB  
21985 O OG  . SER C 1007 ? 1.7455 1.1910 1.1112 -0.0287 -0.4136 0.0520  1007 SER B OG  
21986 N N   . ALA C 1008 ? 1.6751 1.1210 0.9755 0.0255  -0.3830 0.0616  1008 ALA B N   
21987 C CA  . ALA C 1008 ? 1.6815 1.1127 0.9750 0.0404  -0.3564 0.0738  1008 ALA B CA  
21988 C C   . ALA C 1008 ? 1.6371 1.0420 0.9544 0.0245  -0.3452 0.0725  1008 ALA B C   
21989 O O   . ALA C 1008 ? 1.6583 1.0370 0.9664 0.0325  -0.3219 0.0768  1008 ALA B O   
21990 C CB  . ALA C 1008 ? 1.6856 1.1505 0.9884 0.0458  -0.3562 0.0876  1008 ALA B CB  
21991 N N   . GLU C 1009 ? 1.5888 1.0020 0.9363 0.0009  -0.3623 0.0674  1009 GLU B N   
21992 C CA  . GLU C 1009 ? 1.5647 0.9593 0.9375 -0.0146 -0.3539 0.0675  1009 GLU B CA  
21993 C C   . GLU C 1009 ? 1.5680 0.9243 0.9230 -0.0063 -0.3398 0.0588  1009 GLU B C   
21994 O O   . GLU C 1009 ? 1.5752 0.9155 0.9408 -0.0104 -0.3229 0.0620  1009 GLU B O   
21995 C CB  . GLU C 1009 ? 1.5367 0.9457 0.9430 -0.0405 -0.3768 0.0647  1009 GLU B CB  
21996 C CG  . GLU C 1009 ? 1.4635 0.8694 0.9037 -0.0582 -0.3703 0.0708  1009 GLU B CG  
21997 C CD  . GLU C 1009 ? 1.4492 0.8499 0.9133 -0.0798 -0.3909 0.0651  1009 GLU B CD  
21998 O OE1 . GLU C 1009 ? 1.4327 0.8519 0.9040 -0.0922 -0.4146 0.0632  1009 GLU B OE1 
21999 O OE2 . GLU C 1009 ? 1.4470 0.8240 0.9218 -0.0843 -0.3830 0.0630  1009 GLU B OE2 
22000 N N   . ALA C 1010 ? 1.5615 0.9071 0.8895 0.0052  -0.3463 0.0477  1010 ALA B N   
22001 C CA  . ALA C 1010 ? 1.6040 0.9183 0.9173 0.0127  -0.3342 0.0386  1010 ALA B CA  
22002 C C   . ALA C 1010 ? 1.5967 0.8996 0.8842 0.0314  -0.3078 0.0469  1010 ALA B C   
22003 O O   . ALA C 1010 ? 1.5714 0.8530 0.8508 0.0360  -0.2905 0.0452  1010 ALA B O   
22004 C CB  . ALA C 1010 ? 1.6825 0.9892 0.9765 0.0173  -0.3509 0.0218  1010 ALA B CB  
22005 N N   . GLU C 1011 ? 1.6268 0.9449 0.9008 0.0422  -0.3048 0.0572  1011 GLU B N   
22006 C CA  . GLU C 1011 ? 1.6780 0.9819 0.9251 0.0601  -0.2808 0.0670  1011 GLU B CA  
22007 C C   . GLU C 1011 ? 1.6478 0.9420 0.9144 0.0497  -0.2624 0.0765  1011 GLU B C   
22008 O O   . GLU C 1011 ? 1.6707 0.9427 0.9236 0.0544  -0.2403 0.0807  1011 GLU B O   
22009 C CB  . GLU C 1011 ? 1.7146 1.0364 0.9401 0.0777  -0.2836 0.0759  1011 GLU B CB  
22010 C CG  . GLU C 1011 ? 1.7636 1.0736 0.9485 0.0998  -0.2741 0.0764  1011 GLU B CG  
22011 C CD  . GLU C 1011 ? 1.8019 1.1029 0.9783 0.0979  -0.2816 0.0599  1011 GLU B CD  
22012 O OE1 . GLU C 1011 ? 1.8190 1.1365 1.0004 0.0920  -0.3052 0.0477  1011 GLU B OE1 
22013 O OE2 . GLU C 1011 ? 1.8131 1.0911 0.9779 0.1016  -0.2639 0.0586  1011 GLU B OE2 
22014 N N   . LEU C 1012 ? 1.5817 0.8952 0.8801 0.0340  -0.2722 0.0797  1012 LEU B N   
22015 C CA  . LEU C 1012 ? 1.5037 0.8144 0.8235 0.0217  -0.2577 0.0874  1012 LEU B CA  
22016 C C   . LEU C 1012 ? 1.5380 0.8344 0.8740 0.0077  -0.2502 0.0822  1012 LEU B C   
22017 O O   . LEU C 1012 ? 1.5660 0.8466 0.8978 0.0061  -0.2284 0.0869  1012 LEU B O   
22018 C CB  . LEU C 1012 ? 1.3902 0.7319 0.7396 0.0090  -0.2721 0.0915  1012 LEU B CB  
22019 C CG  . LEU C 1012 ? 1.3675 0.7189 0.7032 0.0237  -0.2647 0.1015  1012 LEU B CG  
22020 C CD1 . LEU C 1012 ? 1.3232 0.7121 0.6865 0.0136  -0.2793 0.1056  1012 LEU B CD1 
22021 C CD2 . LEU C 1012 ? 1.3706 0.6940 0.6945 0.0276  -0.2370 0.1078  1012 LEU B CD2 
22022 N N   . MET C 1013 ? 1.5338 0.8354 0.8869 -0.0020 -0.2684 0.0728  1013 MET B N   
22023 C CA  . MET C 1013 ? 1.5197 0.8108 0.8902 -0.0128 -0.2644 0.0679  1013 MET B CA  
22024 C C   . MET C 1013 ? 1.5864 0.8554 0.9324 -0.0009 -0.2445 0.0650  1013 MET B C   
22025 O O   . MET C 1013 ? 1.6040 0.8674 0.9620 -0.0069 -0.2378 0.0620  1013 MET B O   
22026 C CB  . MET C 1013 ? 1.5102 0.8034 0.8946 -0.0199 -0.2886 0.0573  1013 MET B CB  
22027 C CG  . MET C 1013 ? 1.5122 0.8003 0.9240 -0.0330 -0.2885 0.0554  1013 MET B CG  
22028 S SD  . MET C 1013 ? 1.7514 1.0662 1.2051 -0.0564 -0.2941 0.0677  1013 MET B SD  
22029 C CE  . MET C 1013 ? 1.4798 0.8159 0.9285 -0.0560 -0.3139 0.0695  1013 MET B CE  
22030 N N   . SER C 1014 ? 1.6299 0.8896 0.9412 0.0168  -0.2353 0.0669  1014 SER B N   
22031 C CA  . SER C 1014 ? 1.6534 0.8956 0.9381 0.0285  -0.2162 0.0661  1014 SER B CA  
22032 C C   . SER C 1014 ? 1.5722 0.8063 0.8571 0.0219  -0.1909 0.0776  1014 SER B C   
22033 O O   . SER C 1014 ? 1.5394 0.7666 0.8219 0.0191  -0.1750 0.0777  1014 SER B O   
22034 C CB  . SER C 1014 ? 1.7535 0.9912 1.0004 0.0494  -0.2167 0.0664  1014 SER B CB  
22035 O OG  . SER C 1014 ? 1.7908 1.0242 1.0231 0.0556  -0.2034 0.0803  1014 SER B OG  
22036 N N   . VAL C 1015 ? 1.5392 0.7748 0.8249 0.0199  -0.1870 0.0870  1015 VAL B N   
22037 C CA  . VAL C 1015 ? 1.5526 0.7771 0.8375 0.0116  -0.1646 0.0964  1015 VAL B CA  
22038 C C   . VAL C 1015 ? 1.5404 0.7772 0.8610 -0.0107 -0.1624 0.0944  1015 VAL B C   
22039 O O   . VAL C 1015 ? 1.5780 0.8079 0.8986 -0.0205 -0.1429 0.0985  1015 VAL B O   
22040 C CB  . VAL C 1015 ? 1.6447 0.8672 0.9229 0.0167  -0.1629 0.1049  1015 VAL B CB  
22041 C CG1 . VAL C 1015 ? 1.6039 0.8532 0.9129 0.0078  -0.1833 0.1026  1015 VAL B CG1 
22042 C CG2 . VAL C 1015 ? 1.6609 0.8632 0.9316 0.0090  -0.1381 0.1134  1015 VAL B CG2 
22043 N N   . VAL C 1016 ? 1.4469 0.7029 0.7970 -0.0193 -0.1829 0.0888  1016 VAL B N   
22044 C CA  . VAL C 1016 ? 1.3294 0.6018 0.7158 -0.0398 -0.1835 0.0894  1016 VAL B CA  
22045 C C   . VAL C 1016 ? 1.2743 0.5445 0.6643 -0.0471 -0.1659 0.0897  1016 VAL B C   
22046 O O   . VAL C 1016 ? 1.2116 0.4845 0.6076 -0.0600 -0.1496 0.0955  1016 VAL B O   
22047 C CB  . VAL C 1016 ? 1.2780 0.5672 0.6921 -0.0460 -0.2092 0.0842  1016 VAL B CB  
22048 C CG1 . VAL C 1016 ? 1.2334 0.5346 0.6787 -0.0613 -0.2090 0.0843  1016 VAL B CG1 
22049 C CG2 . VAL C 1016 ? 1.2760 0.5821 0.7028 -0.0513 -0.2231 0.0882  1016 VAL B CG2 
22050 N N   . PRO C 1017 ? 1.2965 0.5642 0.6829 -0.0389 -0.1693 0.0827  1017 PRO B N   
22051 C CA  . PRO C 1017 ? 1.3182 0.5919 0.7114 -0.0444 -0.1542 0.0831  1017 PRO B CA  
22052 C C   . PRO C 1017 ? 1.3499 0.6153 0.7210 -0.0468 -0.1280 0.0899  1017 PRO B C   
22053 O O   . PRO C 1017 ? 1.3231 0.6007 0.7050 -0.0581 -0.1140 0.0928  1017 PRO B O   
22054 C CB  . PRO C 1017 ? 1.3111 0.5791 0.6944 -0.0279 -0.1635 0.0727  1017 PRO B CB  
22055 C CG  . PRO C 1017 ? 1.2932 0.5588 0.6843 -0.0249 -0.1887 0.0667  1017 PRO B CG  
22056 C CD  . PRO C 1017 ? 1.3103 0.5727 0.6890 -0.0251 -0.1889 0.0728  1017 PRO B CD  
22057 N N   . VAL C 1018 ? 1.4243 0.6696 0.7641 -0.0365 -0.1213 0.0932  1018 VAL B N   
22058 C CA  . VAL C 1018 ? 1.5345 0.7672 0.8545 -0.0427 -0.0966 0.1016  1018 VAL B CA  
22059 C C   . VAL C 1018 ? 1.5407 0.7769 0.8792 -0.0623 -0.0916 0.1065  1018 VAL B C   
22060 O O   . VAL C 1018 ? 1.5288 0.7725 0.8768 -0.0803 -0.0764 0.1098  1018 VAL B O   
22061 C CB  . VAL C 1018 ? 1.6224 0.8294 0.9014 -0.0250 -0.0895 0.1061  1018 VAL B CB  
22062 C CG1 . VAL C 1018 ? 1.6562 0.8459 0.9136 -0.0336 -0.0631 0.1161  1018 VAL B CG1 
22063 C CG2 . VAL C 1018 ? 1.6633 0.8718 0.9250 -0.0051 -0.0978 0.0991  1018 VAL B CG2 
22064 N N   . PHE C 1019 ? 1.5613 0.7961 0.9056 -0.0592 -0.1050 0.1063  1019 PHE B N   
22065 C CA  . PHE C 1019 ? 1.5494 0.7878 0.9081 -0.0752 -0.0999 0.1096  1019 PHE B CA  
22066 C C   . PHE C 1019 ? 1.4876 0.7527 0.8799 -0.0979 -0.0974 0.1087  1019 PHE B C   
22067 O O   . PHE C 1019 ? 1.5005 0.7642 0.8932 -0.1147 -0.0802 0.1116  1019 PHE B O   
22068 C CB  . PHE C 1019 ? 1.5309 0.7776 0.9004 -0.0698 -0.1180 0.1087  1019 PHE B CB  
22069 C CG  . PHE C 1019 ? 1.4916 0.7525 0.8837 -0.0880 -0.1152 0.1100  1019 PHE B CG  
22070 C CD1 . PHE C 1019 ? 1.4873 0.7295 0.8651 -0.0972 -0.0939 0.1128  1019 PHE B CD1 
22071 C CD2 . PHE C 1019 ? 1.4461 0.7384 0.8726 -0.0973 -0.1330 0.1083  1019 PHE B CD2 
22072 C CE1 . PHE C 1019 ? 1.4648 0.7201 0.8611 -0.1139 -0.0907 0.1118  1019 PHE B CE1 
22073 C CE2 . PHE C 1019 ? 1.4252 0.7347 0.8717 -0.1139 -0.1299 0.1093  1019 PHE B CE2 
22074 C CZ  . PHE C 1019 ? 1.4377 0.7293 0.8688 -0.1218 -0.1087 0.1100  1019 PHE B CZ  
22075 N N   . TYR C 1020 ? 1.4084 0.6974 0.8284 -0.0989 -0.1147 0.1051  1020 TYR B N   
22076 C CA  . TYR C 1020 ? 1.3418 0.6594 0.7943 -0.1181 -0.1132 0.1061  1020 TYR B CA  
22077 C C   . TYR C 1020 ? 1.3162 0.6363 0.7611 -0.1253 -0.0927 0.1080  1020 TYR B C   
22078 O O   . TYR C 1020 ? 1.3095 0.6451 0.7669 -0.1455 -0.0802 0.1109  1020 TYR B O   
22079 C CB  . TYR C 1020 ? 1.3421 0.6797 0.8234 -0.1159 -0.1360 0.1036  1020 TYR B CB  
22080 C CG  . TYR C 1020 ? 1.3672 0.7131 0.8631 -0.1187 -0.1533 0.1044  1020 TYR B CG  
22081 C CD1 . TYR C 1020 ? 1.3875 0.7466 0.8950 -0.1337 -0.1478 0.1080  1020 TYR B CD1 
22082 C CD2 . TYR C 1020 ? 1.4097 0.7518 0.9059 -0.1067 -0.1746 0.1011  1020 TYR B CD2 
22083 C CE1 . TYR C 1020 ? 1.4170 0.7888 0.9374 -0.1353 -0.1628 0.1092  1020 TYR B CE1 
22084 C CE2 . TYR C 1020 ? 1.4323 0.7871 0.9418 -0.1104 -0.1904 0.1030  1020 TYR B CE2 
22085 C CZ  . TYR C 1020 ? 1.4527 0.8239 0.9746 -0.1239 -0.1841 0.1076  1020 TYR B CZ  
22086 O OH  . TYR C 1020 ? 1.4771 0.8667 1.0127 -0.1268 -0.1993 0.1099  1020 TYR B OH  
22087 N N   . VAL C 1021 ? 1.3077 0.6155 0.7309 -0.1098 -0.0886 0.1062  1021 VAL B N   
22088 C CA  . VAL C 1021 ? 1.3115 0.6264 0.7264 -0.1167 -0.0684 0.1091  1021 VAL B CA  
22089 C C   . VAL C 1021 ? 1.3210 0.6199 0.7171 -0.1320 -0.0474 0.1145  1021 VAL B C   
22090 O O   . VAL C 1021 ? 1.3019 0.6178 0.7078 -0.1527 -0.0334 0.1175  1021 VAL B O   
22091 C CB  . VAL C 1021 ? 1.2181 0.5248 0.6099 -0.0957 -0.0665 0.1061  1021 VAL B CB  
22092 C CG1 . VAL C 1021 ? 1.2198 0.5251 0.5895 -0.1022 -0.0418 0.1119  1021 VAL B CG1 
22093 C CG2 . VAL C 1021 ? 1.1981 0.5273 0.6133 -0.0875 -0.0797 0.1006  1021 VAL B CG2 
22094 N N   . PHE C 1022 ? 1.3826 0.6482 0.7511 -0.1225 -0.0454 0.1160  1022 PHE B N   
22095 C CA  . PHE C 1022 ? 1.4641 0.7063 0.8117 -0.1361 -0.0253 0.1211  1022 PHE B CA  
22096 C C   . PHE C 1022 ? 1.4840 0.7385 0.8545 -0.1588 -0.0237 0.1196  1022 PHE B C   
22097 O O   . PHE C 1022 ? 1.5327 0.7789 0.8949 -0.1789 -0.0055 0.1217  1022 PHE B O   
22098 C CB  . PHE C 1022 ? 1.5116 0.7133 0.8241 -0.1179 -0.0237 0.1243  1022 PHE B CB  
22099 C CG  . PHE C 1022 ? 1.5254 0.6941 0.8104 -0.1293 -0.0013 0.1306  1022 PHE B CG  
22100 C CD1 . PHE C 1022 ? 1.5409 0.6924 0.7971 -0.1282 0.0154  0.1376  1022 PHE B CD1 
22101 C CD2 . PHE C 1022 ? 1.5221 0.6768 0.8098 -0.1422 0.0034  0.1294  1022 PHE B CD2 
22102 C CE1 . PHE C 1022 ? 1.5846 0.7018 0.8150 -0.1412 0.0357  0.1444  1022 PHE B CE1 
22103 C CE2 . PHE C 1022 ? 1.5616 0.6801 0.8227 -0.1536 0.0238  0.1341  1022 PHE B CE2 
22104 C CZ  . PHE C 1022 ? 1.5929 0.6908 0.8252 -0.1540 0.0399  0.1422  1022 PHE B CZ  
22105 N N   . HIS C 1023 ? 1.4548 0.7297 0.8529 -0.1570 -0.0427 0.1157  1023 HIS B N   
22106 C CA  . HIS C 1023 ? 1.4120 0.7053 0.8337 -0.1775 -0.0430 0.1140  1023 HIS B CA  
22107 C C   . HIS C 1023 ? 1.3469 0.6782 0.7954 -0.2000 -0.0369 0.1146  1023 HIS B C   
22108 O O   . HIS C 1023 ? 1.3596 0.6964 0.8102 -0.2226 -0.0233 0.1141  1023 HIS B O   
22109 C CB  . HIS C 1023 ? 1.4089 0.7184 0.8531 -0.1693 -0.0656 0.1117  1023 HIS B CB  
22110 C CG  . HIS C 1023 ? 1.4090 0.7414 0.8769 -0.1885 -0.0666 0.1101  1023 HIS B CG  
22111 N ND1 . HIS C 1023 ? 1.4047 0.7777 0.9100 -0.1969 -0.0821 0.1106  1023 HIS B ND1 
22112 C CD2 . HIS C 1023 ? 1.4328 0.7529 0.8908 -0.2010 -0.0537 0.1077  1023 HIS B CD2 
22113 C CE1 . HIS C 1023 ? 1.4012 0.7907 0.9195 -0.2138 -0.0788 0.1090  1023 HIS B CE1 
22114 N NE2 . HIS C 1023 ? 1.4284 0.7856 0.9181 -0.2164 -0.0617 0.1059  1023 HIS B NE2 
22115 N N   . TYR C 1024 ? 1.2804 0.6380 0.7484 -0.1931 -0.0472 0.1153  1024 TYR B N   
22116 C CA  . TYR C 1024 ? 1.2560 0.6515 0.7463 -0.2096 -0.0401 0.1177  1024 TYR B CA  
22117 C C   . TYR C 1024 ? 1.2886 0.6783 0.7571 -0.2209 -0.0167 0.1203  1024 TYR B C   
22118 O O   . TYR C 1024 ? 1.2827 0.7024 0.7653 -0.2431 -0.0060 0.1222  1024 TYR B O   
22119 C CB  . TYR C 1024 ? 1.2668 0.6841 0.7768 -0.1944 -0.0548 0.1181  1024 TYR B CB  
22120 C CG  . TYR C 1024 ? 1.3069 0.7592 0.8306 -0.2033 -0.0442 0.1216  1024 TYR B CG  
22121 C CD1 . TYR C 1024 ? 1.3208 0.8159 0.8811 -0.2137 -0.0512 0.1248  1024 TYR B CD1 
22122 C CD2 . TYR C 1024 ? 1.3416 0.7880 0.8418 -0.2007 -0.0273 0.1229  1024 TYR B CD2 
22123 C CE1 . TYR C 1024 ? 1.3507 0.8830 0.9243 -0.2198 -0.0417 0.1290  1024 TYR B CE1 
22124 C CE2 . TYR C 1024 ? 1.3740 0.8586 0.8874 -0.2079 -0.0176 0.1266  1024 TYR B CE2 
22125 C CZ  . TYR C 1024 ? 1.4017 0.9299 0.9521 -0.2167 -0.0250 0.1295  1024 TYR B CZ  
22126 O OH  . TYR C 1024 ? 1.4619 1.0337 1.0265 -0.2221 -0.0153 0.1342  1024 TYR B OH  
22127 N N   . LEU C 1025 ? 1.3537 0.7087 0.7881 -0.2065 -0.0091 0.1214  1025 LEU B N   
22128 C CA  . LEU C 1025 ? 1.4006 0.7518 0.8136 -0.2177 0.0129  0.1258  1025 LEU B CA  
22129 C C   . LEU C 1025 ? 1.4108 0.7434 0.8108 -0.2435 0.0294  0.1265  1025 LEU B C   
22130 O O   . LEU C 1025 ? 1.3810 0.7307 0.7813 -0.2674 0.0454  0.1291  1025 LEU B O   
22131 C CB  . LEU C 1025 ? 1.4419 0.7607 0.8199 -0.1952 0.0167  0.1283  1025 LEU B CB  
22132 C CG  . LEU C 1025 ? 1.4283 0.7693 0.8075 -0.1782 0.0143  0.1285  1025 LEU B CG  
22133 C CD1 . LEU C 1025 ? 1.4619 0.7701 0.8012 -0.1619 0.0229  0.1320  1025 LEU B CD1 
22134 C CD2 . LEU C 1025 ? 1.4160 0.8016 0.8131 -0.1963 0.0266  0.1319  1025 LEU B CD2 
22135 N N   . GLU C 1026 ? 1.4742 0.7714 0.8616 -0.2379 0.0250  0.1237  1026 GLU B N   
22136 C CA  . GLU C 1026 ? 1.5795 0.8438 0.9460 -0.2561 0.0404  0.1229  1026 GLU B CA  
22137 C C   . GLU C 1026 ? 1.6197 0.9102 1.0134 -0.2786 0.0377  0.1166  1026 GLU B C   
22138 O O   . GLU C 1026 ? 1.6844 0.9778 1.0755 -0.3073 0.0529  0.1148  1026 GLU B O   
22139 C CB  . GLU C 1026 ? 1.6369 0.8504 0.9748 -0.2340 0.0372  0.1231  1026 GLU B CB  
22140 C CG  . GLU C 1026 ? 1.7171 0.8929 1.0361 -0.2484 0.0498  0.1202  1026 GLU B CG  
22141 C CD  . GLU C 1026 ? 1.8025 0.9404 1.0867 -0.2631 0.0733  0.1260  1026 GLU B CD  
22142 O OE1 . GLU C 1026 ? 1.8226 0.9687 1.0983 -0.2608 0.0792  0.1333  1026 GLU B OE1 
22143 O OE2 . GLU C 1026 ? 1.8385 0.9376 1.1029 -0.2767 0.0858  0.1234  1026 GLU B OE2 
22144 N N   . THR C 1027 ? 1.5688 0.8804 0.9883 -0.2676 0.0182  0.1133  1027 THR B N   
22145 C CA  . THR C 1027 ? 1.5283 0.8636 0.9702 -0.2874 0.0158  0.1077  1027 THR B CA  
22146 C C   . THR C 1027 ? 1.5178 0.9090 0.9917 -0.3098 0.0169  0.1088  1027 THR B C   
22147 O O   . THR C 1027 ? 1.5326 0.9509 1.0263 -0.3288 0.0157  0.1048  1027 THR B O   
22148 C CB  . THR C 1027 ? 1.5048 0.8441 0.9612 -0.2711 -0.0036 0.1050  1027 THR B CB  
22149 O OG1 . THR C 1027 ? 1.5315 0.8277 0.9614 -0.2660 0.0025  0.1007  1027 THR B OG1 
22150 C CG2 . THR C 1027 ? 1.4587 0.8487 0.9530 -0.2887 -0.0123 0.1027  1027 THR B CG2 
22151 N N   . GLY C 1028 ? 1.5314 0.9430 1.0096 -0.3073 0.0200  0.1145  1028 GLY B N   
22152 C CA  . GLY C 1028 ? 1.5466 1.0136 1.0527 -0.3283 0.0237  0.1169  1028 GLY B CA  
22153 C C   . GLY C 1028 ? 1.6095 1.0765 1.0967 -0.3420 0.0439  0.1207  1028 GLY B C   
22154 O O   . GLY C 1028 ? 1.5719 1.0833 1.0765 -0.3462 0.0462  0.1257  1028 GLY B O   
22155 N N   . ASN C 1029 ? 1.7070 1.1247 1.1579 -0.3487 0.0588  0.1194  1029 ASN B N   
22156 C CA  . ASN C 1029 ? 1.8116 1.2171 1.2373 -0.3523 0.0753  0.1256  1029 ASN B CA  
22157 C C   . ASN C 1029 ? 1.7549 1.2137 1.2013 -0.3464 0.0737  0.1317  1029 ASN B C   
22158 O O   . ASN C 1029 ? 1.7006 1.2131 1.1727 -0.3656 0.0764  0.1330  1029 ASN B O   
22159 C CB  . ASN C 1029 ? 1.9521 1.3365 1.3549 -0.3863 0.0968  0.1245  1029 ASN B CB  
22160 C CG  . ASN C 1029 ? 2.0454 1.4888 1.4710 -0.4191 0.1054  0.1251  1029 ASN B CG  
22161 O OD1 . ASN C 1029 ? 2.1104 1.5571 1.5202 -0.4417 0.1230  0.1295  1029 ASN B OD1 
22162 N ND2 . ASN C 1029 ? 2.0380 1.5315 1.5010 -0.4230 0.0928  0.1217  1029 ASN B ND2 
22163 N N   . HIS C 1030 ? 1.7773 1.2211 1.2111 -0.3170 0.0686  0.1350  1030 HIS B N   
22164 C CA  . HIS C 1030 ? 1.7519 1.2371 1.1987 -0.3039 0.0673  0.1395  1030 HIS B CA  
22165 C C   . HIS C 1030 ? 1.7565 1.2148 1.1682 -0.2899 0.0783  0.1443  1030 HIS B C   
22166 O O   . HIS C 1030 ? 1.7302 1.2150 1.1443 -0.2736 0.0784  0.1471  1030 HIS B O   
22167 C CB  . HIS C 1030 ? 1.7023 1.2040 1.1761 -0.2772 0.0443  0.1364  1030 HIS B CB  
22168 C CG  . HIS C 1030 ? 1.6395 1.1788 1.1506 -0.2910 0.0342  0.1350  1030 HIS B CG  
22169 N ND1 . HIS C 1030 ? 1.6030 1.1984 1.1383 -0.3116 0.0413  0.1389  1030 HIS B ND1 
22170 C CD2 . HIS C 1030 ? 1.6051 1.1382 1.1334 -0.2872 0.0176  0.1313  1030 HIS B CD2 
22171 C CE1 . HIS C 1030 ? 1.5707 1.1914 1.1360 -0.3195 0.0295  0.1379  1030 HIS B CE1 
22172 N NE2 . HIS C 1030 ? 1.5629 1.1465 1.1246 -0.3053 0.0150  0.1334  1030 HIS B NE2 
22173 N N   . TRP C 1031 ? 1.7584 1.1640 1.1364 -0.2960 0.0882  0.1455  1031 TRP B N   
22174 C CA  . TRP C 1031 ? 1.7507 1.1271 1.0926 -0.2849 0.0994  0.1521  1031 TRP B CA  
22175 C C   . TRP C 1031 ? 1.7641 1.1828 1.1055 -0.2972 0.1148  0.1594  1031 TRP B C   
22176 O O   . TRP C 1031 ? 1.8198 1.2297 1.1361 -0.2845 0.1229  0.1656  1031 TRP B O   
22177 C CB  . TRP C 1031 ? 1.7576 1.0749 1.0657 -0.2982 0.1115  0.1548  1031 TRP B CB  
22178 C CG  . TRP C 1031 ? 1.7265 1.0002 1.0271 -0.2785 0.0981  0.1496  1031 TRP B CG  
22179 C CD1 . TRP C 1031 ? 1.7243 0.9738 1.0276 -0.2901 0.0959  0.1439  1031 TRP B CD1 
22180 C CD2 . TRP C 1031 ? 1.7217 0.9749 1.0108 -0.2432 0.0847  0.1493  1031 TRP B CD2 
22181 N NE1 . TRP C 1031 ? 1.7233 0.9404 1.0181 -0.2630 0.0822  0.1411  1031 TRP B NE1 
22182 C CE2 . TRP C 1031 ? 1.7373 0.9565 1.0234 -0.2350 0.0748  0.1446  1031 TRP B CE2 
22183 C CE3 . TRP C 1031 ? 1.7332 0.9957 1.0133 -0.2176 0.0801  0.1518  1031 TRP B CE3 
22184 C CZ2 . TRP C 1031 ? 1.7717 0.9691 1.0475 -0.2037 0.0601  0.1434  1031 TRP B CZ2 
22185 C CZ3 . TRP C 1031 ? 1.7597 0.9975 1.0282 -0.1874 0.0655  0.1492  1031 TRP B CZ3 
22186 C CH2 . TRP C 1031 ? 1.7821 0.9890 1.0492 -0.1812 0.0554  0.1456  1031 TRP B CH2 
22187 N N   . ASN C 1032 ? 1.7149 1.1841 1.0835 -0.3218 0.1193  0.1593  1032 ASN B N   
22188 C CA  . ASN C 1032 ? 1.7307 1.2485 1.1010 -0.3343 0.1340  0.1669  1032 ASN B CA  
22189 C C   . ASN C 1032 ? 1.6650 1.2275 1.0554 -0.3039 0.1238  0.1661  1032 ASN B C   
22190 O O   . ASN C 1032 ? 1.6509 1.2675 1.0512 -0.3097 0.1333  0.1714  1032 ASN B O   
22191 C CB  . ASN C 1032 ? 1.7408 1.3015 1.1330 -0.3725 0.1425  0.1673  1032 ASN B CB  
22192 C CG  . ASN C 1032 ? 1.6970 1.2946 1.1293 -0.3675 0.1260  0.1611  1032 ASN B CG  
22193 O OD1 . ASN C 1032 ? 1.6754 1.2419 1.1136 -0.3606 0.1126  0.1541  1032 ASN B OD1 
22194 N ND2 . ASN C 1032 ? 1.6824 1.3491 1.1429 -0.3691 0.1263  0.1646  1032 ASN B ND2 
22195 N N   . ILE C 1033 ? 1.6308 1.1721 1.0274 -0.2719 0.1043  0.1591  1033 ILE B N   
22196 C CA  . ILE C 1033 ? 1.6109 1.1831 1.0207 -0.2405 0.0944  0.1567  1033 ILE B CA  
22197 C C   . ILE C 1033 ? 1.6622 1.2360 1.0425 -0.2297 0.1080  0.1620  1033 ILE B C   
22198 O O   . ILE C 1033 ? 1.6574 1.2761 1.0466 -0.2149 0.1104  0.1629  1033 ILE B O   
22199 C CB  . ILE C 1033 ? 1.5812 1.1184 0.9910 -0.2080 0.0727  0.1481  1033 ILE B CB  
22200 C CG1 . ILE C 1033 ? 1.5464 1.0810 0.9853 -0.2134 0.0560  0.1432  1033 ILE B CG1 
22201 C CG2 . ILE C 1033 ? 1.5668 1.1315 0.9843 -0.1768 0.0653  0.1445  1033 ILE B CG2 
22202 C CD1 . ILE C 1033 ? 1.5369 1.0484 0.9805 -0.1823 0.0335  0.1354  1033 ILE B CD1 
22203 N N   . PHE C 1034 ? 1.7113 1.2359 1.0561 -0.2356 0.1169  0.1660  1034 PHE B N   
22204 C CA  . PHE C 1034 ? 1.7554 1.2675 1.0664 -0.2191 0.1261  0.1710  1034 PHE B CA  
22205 C C   . PHE C 1034 ? 1.8490 1.3988 1.1502 -0.2404 0.1483  0.1822  1034 PHE B C   
22206 O O   . PHE C 1034 ? 1.8713 1.4169 1.1667 -0.2757 0.1626  0.1894  1034 PHE B O   
22207 C CB  . PHE C 1034 ? 1.7189 1.1633 0.9954 -0.2144 0.1258  0.1730  1034 PHE B CB  
22208 C CG  . PHE C 1034 ? 1.6469 1.0581 0.9305 -0.1919 0.1038  0.1628  1034 PHE B CG  
22209 C CD1 . PHE C 1034 ? 1.6106 1.0267 0.8967 -0.1578 0.0880  0.1547  1034 PHE B CD1 
22210 C CD2 . PHE C 1034 ? 1.6074 0.9841 0.8948 -0.2056 0.0987  0.1607  1034 PHE B CD2 
22211 C CE1 . PHE C 1034 ? 1.5759 0.9643 0.8692 -0.1405 0.0672  0.1457  1034 PHE B CE1 
22212 C CE2 . PHE C 1034 ? 1.5665 0.9191 0.8617 -0.1860 0.0784  0.1523  1034 PHE B CE2 
22213 C CZ  . PHE C 1034 ? 1.5521 0.9114 0.8509 -0.1550 0.0624  0.1454  1034 PHE B CZ  
22214 N N   . HIS C 1035 ? 1.9313 1.5191 1.2300 -0.2188 0.1511  0.1831  1035 HIS B N   
22215 C CA  . HIS C 1035 ? 2.0875 1.7184 1.3767 -0.2364 0.1720  0.1945  1035 HIS B CA  
22216 C C   . HIS C 1035 ? 2.1700 1.7517 1.4171 -0.2460 0.1846  0.2045  1035 HIS B C   
22217 O O   . HIS C 1035 ? 2.2320 1.8224 1.4660 -0.2785 0.2036  0.2168  1035 HIS B O   
22218 C CB  . HIS C 1035 ? 2.1842 1.8660 1.4797 -0.2047 0.1704  0.1914  1035 HIS B CB  
22219 C CG  . HIS C 1035 ? 2.2397 1.9520 1.5732 -0.1860 0.1538  0.1804  1035 HIS B CG  
22220 N ND1 . HIS C 1035 ? 2.2631 2.0460 1.6250 -0.1899 0.1590  0.1829  1035 HIS B ND1 
22221 C CD2 . HIS C 1035 ? 2.2594 1.9410 1.6074 -0.1649 0.1321  0.1685  1035 HIS B CD2 
22222 C CE1 . HIS C 1035 ? 2.2443 2.0353 1.6357 -0.1700 0.1413  0.1734  1035 HIS B CE1 
22223 N NE2 . HIS C 1035 ? 2.2451 1.9746 1.6287 -0.1560 0.1247  0.1646  1035 HIS B NE2 
22224 N N   . SER C 1036 ? 2.1865 1.7153 1.4125 -0.2189 0.1733  0.1999  1036 SER B N   
22225 C CA  . SER C 1036 ? 2.2294 1.7063 1.4134 -0.2207 0.1828  0.2102  1036 SER B CA  
22226 C C   . SER C 1036 ? 2.2250 1.6493 1.3991 -0.2518 0.1889  0.2155  1036 SER B C   
22227 O O   . SER C 1036 ? 2.2029 1.6392 1.4006 -0.2794 0.1901  0.2125  1036 SER B O   
22228 C CB  . SER C 1036 ? 2.2555 1.6972 1.4221 -0.1810 0.1671  0.2030  1036 SER B CB  
22229 O OG  . SER C 1036 ? 2.2548 1.6570 1.4339 -0.1756 0.1497  0.1932  1036 SER B OG  
22230 N N   . ASP C 1037 ? 2.2430 1.6092 1.3808 -0.2464 0.1930  0.2234  1037 ASP B N   
22231 C CA  . ASP C 1037 ? 2.2224 1.5307 1.3479 -0.2698 0.1977  0.2269  1037 ASP B CA  
22232 C C   . ASP C 1037 ? 2.1099 1.3899 1.2516 -0.2516 0.1770  0.2131  1037 ASP B C   
22233 O O   . ASP C 1037 ? 2.1071 1.3686 1.2397 -0.2183 0.1635  0.2090  1037 ASP B O   
22234 C CB  . ASP C 1037 ? 2.3102 1.5650 1.3899 -0.2693 0.2105  0.2425  1037 ASP B CB  
22235 C CG  . ASP C 1037 ? 2.3132 1.5006 1.3776 -0.2882 0.2148  0.2451  1037 ASP B CG  
22236 O OD1 . ASP C 1037 ? 2.2424 1.4223 1.3309 -0.2929 0.2038  0.2321  1037 ASP B OD1 
22237 O OD2 . ASP C 1037 ? 2.3745 1.5165 1.4020 -0.2976 0.2295  0.2605  1037 ASP B OD2 
22238 N N   . PRO C 1038 ? 2.0235 1.3028 1.1887 -0.2749 0.1745  0.2061  1038 PRO B N   
22239 C CA  . PRO C 1038 ? 1.9611 1.2262 1.1483 -0.2620 0.1549  0.1929  1038 PRO B CA  
22240 C C   . PRO C 1038 ? 1.9681 1.1647 1.1287 -0.2528 0.1526  0.1946  1038 PRO B C   
22241 O O   . PRO C 1038 ? 1.9557 1.1376 1.1231 -0.2279 0.1347  0.1866  1038 PRO B O   
22242 C CB  . PRO C 1038 ? 1.9509 1.2416 1.1669 -0.2965 0.1584  0.1878  1038 PRO B CB  
22243 C CG  . PRO C 1038 ? 1.9789 1.3123 1.1946 -0.3227 0.1767  0.1965  1038 PRO B CG  
22244 C CD  . PRO C 1038 ? 2.0312 1.3333 1.2057 -0.3172 0.1904  0.2100  1038 PRO B CD  
22245 N N   . LEU C 1039 ? 1.9857 1.1408 1.1155 -0.2733 0.1708  0.2055  1039 LEU B N   
22246 C CA  . LEU C 1039 ? 1.9924 1.0786 1.0952 -0.2660 0.1712  0.2082  1039 LEU B CA  
22247 C C   . LEU C 1039 ? 1.9518 1.0166 1.0330 -0.2254 0.1610  0.2123  1039 LEU B C   
22248 O O   . LEU C 1039 ? 1.9199 0.9452 0.9919 -0.2066 0.1516  0.2098  1039 LEU B O   
22249 C CB  . LEU C 1039 ? 2.0617 1.1048 1.1327 -0.2966 0.1943  0.2207  1039 LEU B CB  
22250 C CG  . LEU C 1039 ? 2.1101 1.0791 1.1563 -0.2962 0.1974  0.2216  1039 LEU B CG  
22251 C CD1 . LEU C 1039 ? 2.0634 1.0342 1.1366 -0.2844 0.1792  0.2050  1039 LEU B CD1 
22252 C CD2 . LEU C 1039 ? 2.1622 1.0976 1.1896 -0.3383 0.2190  0.2277  1039 LEU B CD2 
22253 N N   . ILE C 1040 ? 1.9267 1.0224 1.0002 -0.2122 0.1631  0.2182  1040 ILE B N   
22254 C CA  . ILE C 1040 ? 1.9235 1.0080 0.9746 -0.1758 0.1549  0.2222  1040 ILE B CA  
22255 C C   . ILE C 1040 ? 1.8897 1.0108 0.9678 -0.1487 0.1317  0.2069  1040 ILE B C   
22256 O O   . ILE C 1040 ? 1.8936 1.0005 0.9593 -0.1188 0.1188  0.2051  1040 ILE B O   
22257 C CB  . ILE C 1040 ? 1.9180 1.0157 0.9419 -0.1759 0.1707  0.2370  1040 ILE B CB  
22258 C CG1 . ILE C 1040 ? 1.9918 1.0354 0.9710 -0.1607 0.1777  0.2530  1040 ILE B CG1 
22259 C CG2 . ILE C 1040 ? 1.8548 1.0110 0.8941 -0.1549 0.1610  0.2289  1040 ILE B CG2 
22260 C CD1 . ILE C 1040 ? 2.2419 1.2407 1.2137 -0.1353 0.1628  0.2488  1040 ILE B CD1 
22261 N N   . GLU C 1041 ? 1.8745 1.0430 0.9887 -0.1597 0.1265  0.1966  1041 GLU B N   
22262 C CA  . GLU C 1041 ? 1.8758 1.0732 1.0186 -0.1385 0.1043  0.1819  1041 GLU B CA  
22263 C C   . GLU C 1041 ? 1.8760 1.0458 1.0307 -0.1352 0.0897  0.1748  1041 GLU B C   
22264 O O   . GLU C 1041 ? 1.8291 1.0075 0.9987 -0.1142 0.0693  0.1648  1041 GLU B O   
22265 C CB  . GLU C 1041 ? 1.8853 1.1358 1.0645 -0.1535 0.1037  0.1751  1041 GLU B CB  
22266 C CG  . GLU C 1041 ? 1.9223 1.2052 1.1203 -0.1276 0.0861  0.1636  1041 GLU B CG  
22267 C CD  . GLU C 1041 ? 2.0258 1.3290 1.2031 -0.1117 0.0940  0.1672  1041 GLU B CD  
22268 O OE1 . GLU C 1041 ? 2.0475 1.3660 1.2136 -0.1299 0.1141  0.1781  1041 GLU B OE1 
22269 O OE2 . GLU C 1041 ? 2.0853 1.3899 1.2558 -0.0822 0.0805  0.1593  1041 GLU B OE2 
22270 N N   . LYS C 1042 ? 1.9460 1.0842 1.0944 -0.1574 0.1005  0.1796  1042 LYS B N   
22271 C CA  . LYS C 1042 ? 1.9886 1.1002 1.1452 -0.1552 0.0898  0.1736  1042 LYS B CA  
22272 C C   . LYS C 1042 ? 2.0880 1.1547 1.2122 -0.1297 0.0863  0.1796  1042 LYS B C   
22273 O O   . LYS C 1042 ? 2.0843 1.1443 1.2171 -0.1128 0.0697  0.1731  1042 LYS B O   
22274 C CB  . LYS C 1042 ? 2.0273 1.1223 1.1879 -0.1879 0.1032  0.1743  1042 LYS B CB  
22275 C CG  . LYS C 1042 ? 2.0816 1.1397 1.2398 -0.1819 0.0959  0.1700  1042 LYS B CG  
22276 C CD  . LYS C 1042 ? 2.1432 1.1722 1.2954 -0.2120 0.1113  0.1698  1042 LYS B CD  
22277 C CE  . LYS C 1042 ? 2.1016 1.1646 1.2925 -0.2315 0.1034  0.1573  1042 LYS B CE  
22278 N NZ  . LYS C 1042 ? 2.1341 1.1620 1.3144 -0.2567 0.1167  0.1545  1042 LYS B NZ  
22279 N N   . GLN C 1043 ? 2.1761 1.2143 1.2630 -0.1272 0.1023  0.1934  1043 GLN B N   
22280 C CA  . GLN C 1043 ? 2.2242 1.2244 1.2782 -0.0997 0.0994  0.2016  1043 GLN B CA  
22281 C C   . GLN C 1043 ? 2.1471 1.1751 1.2104 -0.0696 0.0775  0.1932  1043 GLN B C   
22282 O O   . GLN C 1043 ? 2.1264 1.1411 1.1876 -0.0496 0.0633  0.1903  1043 GLN B O   
22283 C CB  . GLN C 1043 ? 2.3512 1.3263 1.3646 -0.0999 0.1190  0.2196  1043 GLN B CB  
22284 C CG  . GLN C 1043 ? 2.4626 1.3831 1.4521 -0.1197 0.1381  0.2310  1043 GLN B CG  
22285 C CD  . GLN C 1043 ? 2.5049 1.4037 1.5110 -0.1249 0.1310  0.2206  1043 GLN B CD  
22286 O OE1 . GLN C 1043 ? 2.5149 1.3966 1.5165 -0.0991 0.1185  0.2186  1043 GLN B OE1 
22287 N NE2 . GLN C 1043 ? 2.5037 1.4094 1.5303 -0.1581 0.1385  0.2133  1043 GLN B NE2 
22288 N N   . LYS C 1044 ? 2.0845 1.1527 1.1577 -0.0674 0.0751  0.1887  1044 LYS B N   
22289 C CA  . LYS C 1044 ? 2.0330 1.1271 1.1117 -0.0408 0.0557  0.1791  1044 LYS B CA  
22290 C C   . LYS C 1044 ? 1.9806 1.0816 1.0881 -0.0346 0.0334  0.1663  1044 LYS B C   
22291 O O   . LYS C 1044 ? 1.9941 1.0915 1.0943 -0.0116 0.0176  0.1628  1044 LYS B O   
22292 C CB  . LYS C 1044 ? 2.0067 1.1447 1.0991 -0.0430 0.0570  0.1728  1044 LYS B CB  
22293 C CG  . LYS C 1044 ? 2.4656 1.6092 1.5256 -0.0358 0.0723  0.1834  1044 LYS B CG  
22294 C CD  . LYS C 1044 ? 2.4021 1.5928 1.4780 -0.0427 0.0783  0.1783  1044 LYS B CD  
22295 C CE  . LYS C 1044 ? 2.3720 1.5924 1.4608 -0.0178 0.0589  0.1616  1044 LYS B CE  
22296 N NZ  . LYS C 1044 ? 2.3461 1.6117 1.4504 -0.0204 0.0647  0.1561  1044 LYS B NZ  
22297 N N   . LEU C 1045 ? 1.9183 1.0324 1.0583 -0.0562 0.0321  0.1600  1045 LEU B N   
22298 C CA  . LEU C 1045 ? 1.8426 0.9701 1.0132 -0.0528 0.0108  0.1487  1045 LEU B CA  
22299 C C   . LEU C 1045 ? 1.8286 0.9263 0.9901 -0.0463 0.0064  0.1518  1045 LEU B C   
22300 O O   . LEU C 1045 ? 1.7951 0.9004 0.9671 -0.0317 -0.0132 0.1455  1045 LEU B O   
22301 C CB  . LEU C 1045 ? 1.7665 0.9231 0.9753 -0.0766 0.0103  0.1423  1045 LEU B CB  
22302 C CG  . LEU C 1045 ? 1.7114 0.9023 0.9310 -0.0779 0.0127  0.1389  1045 LEU B CG  
22303 C CD1 . LEU C 1045 ? 1.6876 0.9096 0.9468 -0.0978 0.0091  0.1335  1045 LEU B CD1 
22304 C CD2 . LEU C 1045 ? 1.6727 0.8741 0.8886 -0.0510 -0.0043 0.1310  1045 LEU B CD2 
22305 N N   . LYS C 1046 ? 1.8846 0.9482 1.0260 -0.0569 0.0246  0.1613  1046 LYS B N   
22306 C CA  . LYS C 1046 ? 1.9466 0.9789 1.0742 -0.0454 0.0220  0.1648  1046 LYS B CA  
22307 C C   . LYS C 1046 ? 2.0076 1.0381 1.1141 -0.0137 0.0098  0.1679  1046 LYS B C   
22308 O O   . LYS C 1046 ? 2.0231 1.0615 1.1382 0.0015  -0.0078 0.1632  1046 LYS B O   
22309 C CB  . LYS C 1046 ? 1.9974 0.9833 1.0959 -0.0561 0.0451  0.1762  1046 LYS B CB  
22310 C CG  . LYS C 1046 ? 2.0176 1.0011 1.1314 -0.0897 0.0586  0.1729  1046 LYS B CG  
22311 C CD  . LYS C 1046 ? 2.1210 1.0485 1.2052 -0.0948 0.0758  0.1810  1046 LYS B CD  
22312 C CE  . LYS C 1046 ? 2.1723 1.0873 1.2571 -0.1314 0.0955  0.1810  1046 LYS B CE  
22313 N NZ  . LYS C 1046 ? 2.2481 1.0974 1.2944 -0.1350 0.1144  0.1909  1046 LYS B NZ  
22314 N N   . LYS C 1047 ? 2.0413 1.0665 1.1206 -0.0048 0.0190  0.1757  1047 LYS B N   
22315 C CA  . LYS C 1047 ? 2.0538 1.0807 1.1094 0.0244  0.0091  0.1790  1047 LYS B CA  
22316 C C   . LYS C 1047 ? 1.9320 0.9946 1.0121 0.0355  -0.0167 0.1644  1047 LYS B C   
22317 O O   . LYS C 1047 ? 1.9049 0.9684 0.9854 0.0509  -0.0317 0.1628  1047 LYS B O   
22318 C CB  . LYS C 1047 ? 2.1754 1.2045 1.2055 0.0277  0.0220  0.1866  1047 LYS B CB  
22319 C CG  . LYS C 1047 ? 2.3003 1.3318 1.3008 0.0572  0.0146  0.1914  1047 LYS B CG  
22320 C CD  . LYS C 1047 ? 2.4401 1.4613 1.4073 0.0573  0.0351  0.2058  1047 LYS B CD  
22321 C CE  . LYS C 1047 ? 2.5409 1.5619 1.4733 0.0864  0.0309  0.2141  1047 LYS B CE  
22322 N NZ  . LYS C 1047 ? 2.5506 1.6097 1.4944 0.1029  0.0081  0.1970  1047 LYS B NZ  
22323 N N   . LYS C 1048 ? 1.8657 0.9572 0.9654 0.0275  -0.0214 0.1542  1048 LYS B N   
22324 C CA  . LYS C 1048 ? 1.7748 0.8959 0.8969 0.0357  -0.0454 0.1393  1048 LYS B CA  
22325 C C   . LYS C 1048 ? 1.7089 0.8323 0.8526 0.0342  -0.0611 0.1356  1048 LYS B C   
22326 O O   . LYS C 1048 ? 1.6830 0.8195 0.8307 0.0477  -0.0815 0.1290  1048 LYS B O   
22327 C CB  . LYS C 1048 ? 1.7164 0.8628 0.8671 0.0204  -0.0460 0.1296  1048 LYS B CB  
22328 C CG  . LYS C 1048 ? 1.7080 0.8694 0.8460 0.0306  -0.0437 0.1250  1048 LYS B CG  
22329 C CD  . LYS C 1048 ? 1.6875 0.8749 0.8585 0.0271  -0.0591 0.1101  1048 LYS B CD  
22330 C CE  . LYS C 1048 ? 1.6912 0.8981 0.8658 0.0232  -0.0472 0.1075  1048 LYS B CE  
22331 N NZ  . LYS C 1048 ? 1.6505 0.8778 0.8517 0.0278  -0.0649 0.0921  1048 LYS B NZ  
22332 N N   . LEU C 1049 ? 1.6863 0.7985 0.8428 0.0165  -0.0509 0.1397  1049 LEU B N   
22333 C CA  . LEU C 1049 ? 1.6576 0.7751 0.8362 0.0127  -0.0628 0.1366  1049 LEU B CA  
22334 C C   . LEU C 1049 ? 1.7231 0.8247 0.8783 0.0343  -0.0671 0.1436  1049 LEU B C   
22335 O O   . LEU C 1049 ? 1.7373 0.8560 0.9075 0.0408  -0.0851 0.1393  1049 LEU B O   
22336 C CB  . LEU C 1049 ? 1.5970 0.7050 0.7896 -0.0110 -0.0479 0.1388  1049 LEU B CB  
22337 C CG  . LEU C 1049 ? 1.5011 0.6334 0.7316 -0.0234 -0.0621 0.1311  1049 LEU B CG  
22338 C CD1 . LEU C 1049 ? 1.4198 0.5841 0.6804 -0.0344 -0.0726 0.1227  1049 LEU B CD1 
22339 C CD2 . LEU C 1049 ? 1.4969 0.6135 0.7305 -0.0422 -0.0456 0.1339  1049 LEU B CD2 
22340 N N   . LYS C 1050 ? 1.7553 0.8262 0.8738 0.0457  -0.0505 0.1556  1050 LYS B N   
22341 C CA  . LYS C 1050 ? 1.7889 0.8448 0.8838 0.0690  -0.0534 0.1642  1050 LYS B CA  
22342 C C   . LYS C 1050 ? 1.8382 0.9156 0.9210 0.0912  -0.0705 0.1621  1050 LYS B C   
22343 O O   . LYS C 1050 ? 1.8143 0.9093 0.9023 0.1046  -0.0878 0.1600  1050 LYS B O   
22344 C CB  . LYS C 1050 ? 1.8189 0.8301 0.8774 0.0738  -0.0294 0.1797  1050 LYS B CB  
22345 C CG  . LYS C 1050 ? 1.8337 0.8275 0.8713 0.0984  -0.0312 0.1892  1050 LYS B CG  
22346 C CD  . LYS C 1050 ? 1.8790 0.8232 0.8771 0.1071  -0.0086 0.2063  1050 LYS B CD  
22347 C CE  . LYS C 1050 ? 1.9203 0.8575 0.8982 0.1390  -0.0152 0.2158  1050 LYS B CE  
22348 N NZ  . LYS C 1050 ? 1.9848 0.8719 0.9410 0.1455  0.0023  0.2270  1050 LYS B NZ  
22349 N N   . GLU C 1051 ? 1.9341 1.0132 0.9997 0.0950  -0.0658 0.1624  1051 GLU B N   
22350 C CA  . GLU C 1051 ? 2.0372 1.1341 1.0852 0.1175  -0.0804 0.1606  1051 GLU B CA  
22351 C C   . GLU C 1051 ? 1.9901 1.1198 1.0698 0.1139  -0.1064 0.1455  1051 GLU B C   
22352 O O   . GLU C 1051 ? 2.0056 1.1515 1.0800 0.1294  -0.1228 0.1446  1051 GLU B O   
22353 C CB  . GLU C 1051 ? 2.1609 1.2597 1.1860 0.1226  -0.0724 0.1609  1051 GLU B CB  
22354 C CG  . GLU C 1051 ? 2.2442 1.3680 1.2907 0.1124  -0.0820 0.1439  1051 GLU B CG  
22355 C CD  . GLU C 1051 ? 2.3497 1.4703 1.3774 0.1106  -0.0643 0.1471  1051 GLU B CD  
22356 O OE1 . GLU C 1051 ? 2.3928 1.4932 1.3887 0.1176  -0.0464 0.1633  1051 GLU B OE1 
22357 O OE2 . GLU C 1051 ? 2.3711 1.5101 1.4161 0.1025  -0.0680 0.1343  1051 GLU B OE2 
22358 N N   . GLY C 1052 ? 1.9625 1.1023 1.0759 0.0921  -0.1098 0.1352  1052 GLY B N   
22359 C CA  . GLY C 1052 ? 1.9441 1.1121 1.0891 0.0854  -0.1340 0.1221  1052 GLY B CA  
22360 C C   . GLY C 1052 ? 1.9341 1.1117 1.0939 0.0860  -0.1445 0.1252  1052 GLY B C   
22361 O O   . GLY C 1052 ? 1.9147 1.1182 1.0917 0.0860  -0.1668 0.1178  1052 GLY B O   
22362 N N   . MET C 1053 ? 1.9351 1.0920 1.0873 0.0861  -0.1282 0.1360  1053 MET B N   
22363 C CA  . MET C 1053 ? 1.9543 1.1216 1.1205 0.0878  -0.1358 0.1385  1053 MET B CA  
22364 C C   . MET C 1053 ? 1.9461 1.1247 1.0911 0.1136  -0.1469 0.1442  1053 MET B C   
22365 O O   . MET C 1053 ? 1.9273 1.1359 1.0893 0.1159  -0.1655 0.1412  1053 MET B O   
22366 C CB  . MET C 1053 ? 2.0035 1.1416 1.1652 0.0817  -0.1142 0.1465  1053 MET B CB  
22367 C CG  . MET C 1053 ? 1.9801 1.1359 1.1706 0.0723  -0.1217 0.1433  1053 MET B CG  
22368 S SD  . MET C 1053 ? 3.3299 2.5267 2.5667 0.0484  -0.1433 0.1301  1053 MET B SD  
22369 C CE  . MET C 1053 ? 1.1985 0.4268 0.4610 0.0472  -0.1576 0.1300  1053 MET B CE  
22370 N N   . LEU C 1054 ? 1.9791 1.1365 1.0867 0.1325  -0.1351 0.1537  1054 LEU B N   
22371 C CA  . LEU C 1054 ? 2.0093 1.1787 1.0925 0.1596  -0.1437 0.1613  1054 LEU B CA  
22372 C C   . LEU C 1054 ? 1.9484 1.1574 1.0417 0.1603  -0.1698 0.1493  1054 LEU B C   
22373 O O   . LEU C 1054 ? 1.9312 1.1699 1.0267 0.1716  -0.1868 0.1499  1054 LEU B O   
22374 C CB  . LEU C 1054 ? 2.1008 1.2392 1.1413 0.1777  -0.1249 0.1750  1054 LEU B CB  
22375 C CG  . LEU C 1054 ? 2.1741 1.2649 1.1978 0.1759  -0.0977 0.1879  1054 LEU B CG  
22376 C CD1 . LEU C 1054 ? 2.2322 1.2949 1.2137 0.1914  -0.0809 0.2025  1054 LEU B CD1 
22377 C CD2 . LEU C 1054 ? 2.1983 1.2808 1.2239 0.1868  -0.0957 0.1949  1054 LEU B CD2 
22378 N N   . SER C 1055 ? 1.9137 1.1229 1.0129 0.1476  -0.1726 0.1379  1055 SER B N   
22379 C CA  . SER C 1055 ? 1.8783 1.1162 0.9858 0.1451  -0.1960 0.1235  1055 SER B CA  
22380 C C   . SER C 1055 ? 1.7814 1.0528 0.9110 0.1426  -0.2185 0.1206  1055 SER B C   
22381 O O   . SER C 1055 ? 1.7986 1.0964 0.9219 0.1499  -0.2377 0.1149  1055 SER B O   
22382 C CB  . SER C 1055 ? 1.9301 1.1627 1.0597 0.1240  -0.1968 0.1099  1055 SER B CB  
22383 O OG  . SER C 1055 ? 1.9510 1.2057 1.0951 0.1174  -0.2208 0.0944  1055 SER B OG  
22384 N N   . ILE C 1056 ? 1.7077 0.9813 0.8627 0.1316  -0.2163 0.1242  1056 ILE B N   
22385 C CA  . ILE C 1056 ? 1.6786 0.9898 0.8592 0.1252  -0.2385 0.1211  1056 ILE B CA  
22386 C C   . ILE C 1056 ? 1.6542 0.9870 0.8176 0.1487  -0.2429 0.1322  1056 ILE B C   
22387 O O   . ILE C 1056 ? 1.6333 1.0054 0.8060 0.1493  -0.2645 0.1293  1056 ILE B O   
22388 C CB  . ILE C 1056 ? 1.5019 0.8176 0.7234 0.0994  -0.2397 0.1174  1056 ILE B CB  
22389 C CG1 . ILE C 1056 ? 1.4609 0.8054 0.6995 0.1008  -0.2469 0.1241  1056 ILE B CG1 
22390 C CG2 . ILE C 1056 ? 1.4765 0.7560 0.6982 0.0901  -0.2153 0.1194  1056 ILE B CG2 
22391 C CD1 . ILE C 1056 ? 1.4547 0.7781 0.6783 0.1155  -0.2249 0.1360  1056 ILE B CD1 
22392 N N   . MET C 1057 ? 1.6954 1.0021 0.8313 0.1687  -0.2222 0.1455  1057 MET B N   
22393 C CA  . MET C 1057 ? 1.7982 1.1206 0.9185 0.1941  -0.2223 0.1586  1057 MET B CA  
22394 C C   . MET C 1057 ? 1.8246 1.1963 0.9402 0.2066  -0.2461 0.1579  1057 MET B C   
22395 O O   . MET C 1057 ? 1.8246 1.2278 0.9449 0.2194  -0.2534 0.1654  1057 MET B O   
22396 C CB  . MET C 1057 ? 1.9042 1.1856 0.9856 0.2174  -0.1979 0.1734  1057 MET B CB  
22397 C CG  . MET C 1057 ? 1.9542 1.2332 1.0238 0.2416  -0.1893 0.1882  1057 MET B CG  
22398 S SD  . MET C 1057 ? 2.3734 1.6119 1.4562 0.2300  -0.1675 0.1898  1057 MET B SD  
22399 C CE  . MET C 1057 ? 2.7863 1.9609 1.8390 0.2262  -0.1403 0.1955  1057 MET B CE  
22400 N N   . SER C 1058 ? 1.8337 1.2134 0.9384 0.2036  -0.2575 0.1486  1058 SER B N   
22401 C CA  . SER C 1058 ? 1.7938 1.2195 0.8907 0.2125  -0.2802 0.1458  1058 SER B CA  
22402 C C   . SER C 1058 ? 1.7297 1.2002 0.8618 0.1959  -0.3026 0.1403  1058 SER B C   
22403 O O   . SER C 1058 ? 1.7118 1.2286 0.8417 0.2065  -0.3183 0.1446  1058 SER B O   
22404 C CB  . SER C 1058 ? 1.7810 1.2028 0.8662 0.2043  -0.2892 0.1311  1058 SER B CB  
22405 O OG  . SER C 1058 ? 1.7702 1.1459 0.8422 0.2027  -0.2683 0.1303  1058 SER B OG  
22406 N N   . TYR C 1059 ? 1.6700 1.1294 0.8345 0.1691  -0.3039 0.1318  1059 TYR B N   
22407 C CA  . TYR C 1059 ? 1.6437 1.1422 0.8434 0.1498  -0.3234 0.1280  1059 TYR B CA  
22408 C C   . TYR C 1059 ? 1.7140 1.2214 0.9266 0.1574  -0.3127 0.1402  1059 TYR B C   
22409 O O   . TYR C 1059 ? 1.7238 1.2622 0.9682 0.1405  -0.3247 0.1388  1059 TYR B O   
22410 C CB  . TYR C 1059 ? 1.5667 1.0510 0.7950 0.1178  -0.3311 0.1141  1059 TYR B CB  
22411 C CG  . TYR C 1059 ? 1.5623 1.0289 0.7775 0.1113  -0.3386 0.0999  1059 TYR B CG  
22412 C CD1 . TYR C 1059 ? 1.6019 1.0286 0.7902 0.1235  -0.3196 0.0989  1059 TYR B CD1 
22413 C CD2 . TYR C 1059 ? 1.5791 1.0680 0.8082 0.0923  -0.3644 0.0870  1059 TYR B CD2 
22414 C CE1 . TYR C 1059 ? 1.6589 1.0717 0.8340 0.1195  -0.3259 0.0844  1059 TYR B CE1 
22415 C CE2 . TYR C 1059 ? 1.6536 1.1233 0.8687 0.0875  -0.3715 0.0713  1059 TYR B CE2 
22416 C CZ  . TYR C 1059 ? 1.6908 1.1239 0.8788 0.1024  -0.3521 0.0695  1059 TYR B CZ  
22417 O OH  . TYR C 1059 ? 1.7162 1.1333 0.8896 0.0996  -0.3590 0.0527  1059 TYR B OH  
22418 N N   . ARG C 1060 ? 1.7717 1.2508 0.9595 0.1822  -0.2900 0.1521  1060 ARG B N   
22419 C CA  . ARG C 1060 ? 1.8216 1.3108 1.0179 0.1935  -0.2811 0.1622  1060 ARG B CA  
22420 C C   . ARG C 1060 ? 1.8615 1.3977 1.0456 0.2190  -0.2922 0.1720  1060 ARG B C   
22421 O O   . ARG C 1060 ? 1.8948 1.4249 1.0461 0.2437  -0.2878 0.1794  1060 ARG B O   
22422 C CB  . ARG C 1060 ? 1.8752 1.3085 1.0511 0.2075  -0.2513 0.1702  1060 ARG B CB  
22423 C CG  . ARG C 1060 ? 1.8074 1.2434 0.9988 0.2104  -0.2417 0.1747  1060 ARG B CG  
22424 C CD  . ARG C 1060 ? 1.8539 1.2302 1.0202 0.2251  -0.2124 0.1820  1060 ARG B CD  
22425 N NE  . ARG C 1060 ? 1.9326 1.3084 1.0708 0.2626  -0.2046 0.1960  1060 ARG B NE  
22426 C CZ  . ARG C 1060 ? 2.0081 1.3290 1.1151 0.2823  -0.1804 0.2055  1060 ARG B CZ  
22427 N NH1 . ARG C 1060 ? 2.0595 1.3253 1.1603 0.2651  -0.1620 0.2019  1060 ARG B NH1 
22428 N NH2 . ARG C 1060 ? 2.0163 1.3368 1.0978 0.3188  -0.1743 0.2193  1060 ARG B NH2 
22429 N N   . ASN C 1061 ? 1.8830 1.4703 1.0937 0.2132  -0.3065 0.1731  1061 ASN B N   
22430 C CA  . ASN C 1061 ? 1.9599 1.6007 1.1615 0.2381  -0.3173 0.1833  1061 ASN B CA  
22431 C C   . ASN C 1061 ? 1.9998 1.6246 1.1790 0.2753  -0.2961 0.1983  1061 ASN B C   
22432 O O   . ASN C 1061 ? 2.0057 1.5717 1.1729 0.2806  -0.2725 0.2002  1061 ASN B O   
22433 C CB  . ASN C 1061 ? 1.9751 1.6846 1.2121 0.2177  -0.3424 0.1798  1061 ASN B CB  
22434 C CG  . ASN C 1061 ? 2.0434 1.7892 1.2817 0.2017  -0.3686 0.1719  1061 ASN B CG  
22435 O OD1 . ASN C 1061 ? 2.0673 1.7787 1.2934 0.1910  -0.3696 0.1621  1061 ASN B OD1 
22436 N ND2 . ASN C 1061 ? 2.0640 1.8810 1.3157 0.2004  -0.3896 0.1756  1061 ASN B ND2 
22437 N N   . ALA C 1062 ? 2.0303 1.7069 1.2023 0.3014  -0.3045 0.2091  1062 ALA B N   
22438 C CA  . ALA C 1062 ? 2.0713 1.7339 1.2185 0.3420  -0.2860 0.2242  1062 ALA B CA  
22439 C C   . ALA C 1062 ? 2.0522 1.7092 1.2183 0.3425  -0.2745 0.2239  1062 ALA B C   
22440 O O   . ALA C 1062 ? 2.0989 1.7080 1.2447 0.3656  -0.2514 0.2306  1062 ALA B O   
22441 C CB  . ALA C 1062 ? 2.0975 1.8254 1.2329 0.3706  -0.3002 0.2360  1062 ALA B CB  
22442 N N   . ASP C 1063 ? 1.9928 1.6993 1.1971 0.3162  -0.2910 0.2160  1063 ASP B N   
22443 C CA  . ASP C 1063 ? 1.9618 1.6780 1.1877 0.3146  -0.2835 0.2148  1063 ASP B CA  
22444 C C   . ASP C 1063 ? 1.9058 1.5611 1.1420 0.2882  -0.2679 0.2041  1063 ASP B C   
22445 O O   . ASP C 1063 ? 1.8689 1.5273 1.1236 0.2816  -0.2610 0.2005  1063 ASP B O   
22446 C CB  . ASP C 1063 ? 1.9620 1.7623 1.2250 0.2952  -0.3086 0.2126  1063 ASP B CB  
22447 C CG  . ASP C 1063 ? 1.9887 1.8036 1.2723 0.2550  -0.3301 0.2026  1063 ASP B CG  
22448 O OD1 . ASP C 1063 ? 2.0011 1.7584 1.2734 0.2416  -0.3234 0.1955  1063 ASP B OD1 
22449 O OD2 . ASP C 1063 ? 1.9864 1.8693 1.2965 0.2371  -0.3533 0.2020  1063 ASP B OD2 
22450 N N   . TYR C 1064 ? 1.8861 1.4905 1.1100 0.2735  -0.2626 0.1991  1064 TYR B N   
22451 C CA  . TYR C 1064 ? 1.8486 1.3996 1.0817 0.2472  -0.2488 0.1895  1064 TYR B CA  
22452 C C   . TYR C 1064 ? 1.8122 1.3926 1.0831 0.2070  -0.2677 0.1787  1064 TYR B C   
22453 O O   . TYR C 1064 ? 1.8412 1.3865 1.1237 0.1820  -0.2603 0.1706  1064 TYR B O   
22454 C CB  . TYR C 1064 ? 1.8192 1.3399 1.0493 0.2576  -0.2271 0.1902  1064 TYR B CB  
22455 C CG  . TYR C 1064 ? 1.8365 1.3022 1.0240 0.2914  -0.2054 0.1998  1064 TYR B CG  
22456 C CD1 . TYR C 1064 ? 1.8678 1.2683 1.0324 0.2853  -0.1898 0.1994  1064 TYR B CD1 
22457 C CD2 . TYR C 1064 ? 1.8740 1.3551 1.0430 0.3302  -0.2012 0.2107  1064 TYR B CD2 
22458 C CE1 . TYR C 1064 ? 1.9341 1.2820 1.0581 0.3147  -0.1700 0.2104  1064 TYR B CE1 
22459 C CE2 . TYR C 1064 ? 1.9462 1.3723 1.0738 0.3626  -0.1813 0.2217  1064 TYR B CE2 
22460 C CZ  . TYR C 1064 ? 1.9718 1.3296 1.0767 0.3536  -0.1657 0.2219  1064 TYR B CZ  
22461 O OH  . TYR C 1064 ? 2.0153 1.3158 1.0781 0.3839  -0.1458 0.2348  1064 TYR B OH  
22462 N N   . SER C 1065 ? 1.7571 1.4023 1.0464 0.2006  -0.2924 0.1794  1065 SER B N   
22463 C CA  . SER C 1065 ? 1.7011 1.3707 1.0231 0.1627  -0.3123 0.1705  1065 SER B CA  
22464 C C   . SER C 1065 ? 1.6906 1.3306 0.9988 0.1525  -0.3184 0.1637  1065 SER B C   
22465 O O   . SER C 1065 ? 1.6985 1.3479 0.9827 0.1702  -0.3248 0.1668  1065 SER B O   
22466 C CB  . SER C 1065 ? 1.6841 1.4324 1.0299 0.1561  -0.3372 0.1739  1065 SER B CB  
22467 O OG  . SER C 1065 ? 1.7193 1.4934 1.0490 0.1652  -0.3530 0.1757  1065 SER B OG  
22468 N N   . TYR C 1066 ? 1.6570 1.2634 0.9795 0.1254  -0.3158 0.1545  1066 TYR B N   
22469 C CA  . TYR C 1066 ? 1.6505 1.2333 0.9636 0.1143  -0.3231 0.1461  1066 TYR B CA  
22470 C C   . TYR C 1066 ? 1.6398 1.2686 0.9742 0.0931  -0.3524 0.1407  1066 TYR B C   
22471 O O   . TYR C 1066 ? 1.6243 1.3004 0.9860 0.0808  -0.3658 0.1439  1066 TYR B O   
22472 C CB  . TYR C 1066 ? 1.6192 1.1514 0.9389 0.0958  -0.3092 0.1388  1066 TYR B CB  
22473 C CG  . TYR C 1066 ? 1.6302 1.1178 0.9298 0.1119  -0.2808 0.1440  1066 TYR B CG  
22474 C CD1 . TYR C 1066 ? 1.6442 1.1399 0.9496 0.1207  -0.2701 0.1503  1066 TYR B CD1 
22475 C CD2 . TYR C 1066 ? 1.6653 1.1031 0.9387 0.1182  -0.2646 0.1425  1066 TYR B CD2 
22476 C CE1 . TYR C 1066 ? 1.6957 1.1454 0.9803 0.1342  -0.2441 0.1540  1066 TYR B CE1 
22477 C CE2 . TYR C 1066 ? 1.7109 1.1055 0.9644 0.1303  -0.2384 0.1482  1066 TYR B CE2 
22478 C CZ  . TYR C 1066 ? 1.7382 1.1363 0.9970 0.1378  -0.2284 0.1535  1066 TYR B CZ  
22479 O OH  . TYR C 1066 ? 1.7886 1.1389 1.0259 0.1483  -0.2026 0.1580  1066 TYR B OH  
22480 N N   . SER C 1067 ? 1.6403 1.2554 0.9613 0.0879  -0.3623 0.1321  1067 SER B N   
22481 C CA  . SER C 1067 ? 1.6324 1.2865 0.9677 0.0683  -0.3907 0.1258  1067 SER B CA  
22482 C C   . SER C 1067 ? 1.6495 1.2691 0.9813 0.0507  -0.3986 0.1112  1067 SER B C   
22483 O O   . SER C 1067 ? 1.6697 1.2520 0.9732 0.0649  -0.3871 0.1065  1067 SER B O   
22484 C CB  . SER C 1067 ? 1.6379 1.3371 0.9535 0.0891  -0.4018 0.1316  1067 SER B CB  
22485 O OG  . SER C 1067 ? 1.6230 1.3830 0.9645 0.0719  -0.4247 0.1338  1067 SER B OG  
22486 N N   . VAL C 1068 ? 1.6371 1.2695 0.9974 0.0203  -0.4180 0.1046  1068 VAL B N   
22487 C CA  . VAL C 1068 ? 1.6656 1.2614 1.0275 0.0023  -0.4250 0.0905  1068 VAL B CA  
22488 C C   . VAL C 1068 ? 1.7515 1.3223 1.0769 0.0178  -0.4242 0.0797  1068 VAL B C   
22489 O O   . VAL C 1068 ? 1.7706 1.2960 1.0831 0.0244  -0.4078 0.0744  1068 VAL B O   
22490 C CB  . VAL C 1068 ? 1.6499 1.2727 1.0372 -0.0276 -0.4525 0.0856  1068 VAL B CB  
22491 C CG1 . VAL C 1068 ? 1.6876 1.3628 1.0638 -0.0229 -0.4715 0.0874  1068 VAL B CG1 
22492 C CG2 . VAL C 1068 ? 1.6459 1.2247 1.0310 -0.0428 -0.4597 0.0697  1068 VAL B CG2 
22493 N N   . TRP C 1069 ? 1.7882 1.3914 1.0976 0.0219  -0.4421 0.0760  1069 TRP B N   
22494 C CA  . TRP C 1069 ? 1.8268 1.4141 1.0971 0.0416  -0.4392 0.0678  1069 TRP B CA  
22495 C C   . TRP C 1069 ? 1.8495 1.4688 1.0944 0.0716  -0.4328 0.0805  1069 TRP B C   
22496 O O   . TRP C 1069 ? 1.8418 1.5003 1.0998 0.0763  -0.4344 0.0938  1069 TRP B O   
22497 C CB  . TRP C 1069 ? 1.8276 1.4175 1.0903 0.0251  -0.4636 0.0493  1069 TRP B CB  
22498 C CG  . TRP C 1069 ? 1.7786 1.3503 1.0690 -0.0073 -0.4788 0.0381  1069 TRP B CG  
22499 C CD1 . TRP C 1069 ? 1.7740 1.2951 1.0644 -0.0154 -0.4750 0.0245  1069 TRP B CD1 
22500 C CD2 . TRP C 1069 ? 1.7277 1.3325 1.0485 -0.0353 -0.5008 0.0404  1069 TRP B CD2 
22501 N NE1 . TRP C 1069 ? 1.7469 1.2638 1.0661 -0.0459 -0.4933 0.0188  1069 TRP B NE1 
22502 C CE2 . TRP C 1069 ? 1.7359 1.3033 1.0742 -0.0600 -0.5095 0.0289  1069 TRP B CE2 
22503 C CE3 . TRP C 1069 ? 1.6818 1.3463 1.0172 -0.0415 -0.5138 0.0523  1069 TRP B CE3 
22504 C CZ2 . TRP C 1069 ? 1.7415 1.3259 1.1105 -0.0919 -0.5305 0.0300  1069 TRP B CZ2 
22505 C CZ3 . TRP C 1069 ? 1.6943 1.3805 1.0607 -0.0740 -0.5347 0.0528  1069 TRP B CZ3 
22506 C CH2 . TRP C 1069 ? 1.7312 1.3757 1.1141 -0.0999 -0.5430 0.0422  1069 TRP B CH2 
22507 N N   . LYS C 1070 ? 1.8647 1.4698 1.0729 0.0928  -0.4260 0.0770  1070 LYS B N   
22508 C CA  . LYS C 1070 ? 1.8602 1.4875 1.0411 0.1253  -0.4159 0.0917  1070 LYS B CA  
22509 C C   . LYS C 1070 ? 1.8814 1.5754 1.0646 0.1286  -0.4361 0.0979  1070 LYS B C   
22510 O O   . LYS C 1070 ? 1.8950 1.6177 1.0731 0.1164  -0.4587 0.0865  1070 LYS B O   
22511 C CB  . LYS C 1070 ? 1.8595 1.4597 1.0005 0.1464  -0.4043 0.0882  1070 LYS B CB  
22512 C CG  . LYS C 1070 ? 1.8411 1.3936 0.9695 0.1638  -0.3736 0.0989  1070 LYS B CG  
22513 C CD  . LYS C 1070 ? 1.8741 1.4219 0.9608 0.1960  -0.3596 0.1094  1070 LYS B CD  
22514 C CE  . LYS C 1070 ? 1.8935 1.4179 0.9551 0.1964  -0.3584 0.0956  1070 LYS B CE  
22515 N NZ  . LYS C 1070 ? 1.9211 1.4442 0.9404 0.2270  -0.3456 0.1066  1070 LYS B NZ  
22516 N N   . GLY C 1071 ? 1.8887 1.6081 1.0785 0.1454  -0.4273 0.1156  1071 GLY B N   
22517 C CA  . GLY C 1071 ? 1.9406 1.7286 1.1312 0.1545  -0.4431 0.1246  1071 GLY B CA  
22518 C C   . GLY C 1071 ? 1.9388 1.7680 1.1672 0.1221  -0.4656 0.1204  1071 GLY B C   
22519 O O   . GLY C 1071 ? 1.9977 1.8922 1.2331 0.1222  -0.4823 0.1267  1071 GLY B O   
22520 N N   . GLY C 1072 ? 1.9166 1.7093 1.1695 0.0940  -0.4658 0.1108  1072 GLY B N   
22521 C CA  . GLY C 1072 ? 1.8976 1.7210 1.1883 0.0606  -0.4850 0.1085  1072 GLY B CA  
22522 C C   . GLY C 1072 ? 1.8981 1.7493 1.2130 0.0661  -0.4761 0.1242  1072 GLY B C   
22523 O O   . GLY C 1072 ? 1.8985 1.7168 1.2091 0.0851  -0.4517 0.1316  1072 GLY B O   
22524 N N   . SER C 1073 ? 1.8812 1.7946 1.2210 0.0485  -0.4962 0.1289  1073 SER B N   
22525 C CA  . SER C 1073 ? 1.8487 1.8008 1.2105 0.0555  -0.4898 0.1434  1073 SER B CA  
22526 C C   . SER C 1073 ? 1.8110 1.7115 1.1882 0.0503  -0.4697 0.1435  1073 SER B C   
22527 O O   . SER C 1073 ? 1.7833 1.6385 1.1696 0.0270  -0.4708 0.1329  1073 SER B O   
22528 C CB  . SER C 1073 ? 1.8570 1.8773 1.2493 0.0256  -0.5164 0.1458  1073 SER B CB  
22529 O OG  . SER C 1073 ? 1.8746 1.8795 1.2717 -0.0085 -0.5372 0.1316  1073 SER B OG  
22530 N N   . ALA C 1074 ? 1.7869 1.6944 1.1655 0.0733  -0.4511 0.1549  1074 ALA B N   
22531 C CA  . ALA C 1074 ? 1.7670 1.6268 1.1557 0.0716  -0.4296 0.1548  1074 ALA B CA  
22532 C C   . ALA C 1074 ? 1.6809 1.5442 1.1058 0.0320  -0.4425 0.1498  1074 ALA B C   
22533 O O   . ALA C 1074 ? 1.6873 1.6073 1.1365 0.0123  -0.4631 0.1534  1074 ALA B O   
22534 C CB  . ALA C 1074 ? 1.7743 1.6559 1.1644 0.0965  -0.4139 0.1665  1074 ALA B CB  
22535 N N   . SER C 1075 ? 1.6459 1.4505 1.0743 0.0199  -0.4310 0.1424  1075 SER B N   
22536 C CA  . SER C 1075 ? 1.6223 1.4269 1.0858 -0.0149 -0.4403 0.1400  1075 SER B CA  
22537 C C   . SER C 1075 ? 1.5950 1.3874 1.0717 -0.0112 -0.4195 0.1453  1075 SER B C   
22538 O O   . SER C 1075 ? 1.5910 1.3344 1.0488 0.0057  -0.3964 0.1431  1075 SER B O   
22539 C CB  . SER C 1075 ? 1.6475 1.3992 1.1091 -0.0334 -0.4442 0.1276  1075 SER B CB  
22540 O OG  . SER C 1075 ? 1.6433 1.3531 1.1148 -0.0380 -0.4253 0.1268  1075 SER B OG  
22541 N N   . THR C 1076 ? 1.5690 1.4079 1.0778 -0.0289 -0.4284 0.1522  1076 THR B N   
22542 C CA  . THR C 1076 ? 1.5054 1.3438 1.0308 -0.0296 -0.4120 0.1565  1076 THR B CA  
22543 C C   . THR C 1076 ? 1.5005 1.2817 1.0313 -0.0453 -0.4017 0.1495  1076 THR B C   
22544 O O   . THR C 1076 ? 1.5073 1.2599 1.0350 -0.0377 -0.3799 0.1489  1076 THR B O   
22545 C CB  . THR C 1076 ? 1.4523 1.3532 1.0140 -0.0530 -0.4283 0.1644  1076 THR B CB  
22546 O OG1 . THR C 1076 ? 1.4580 1.3960 1.0217 -0.0336 -0.4166 0.1714  1076 THR B OG1 
22547 C CG2 . THR C 1076 ? 1.4065 1.2879 0.9961 -0.0837 -0.4293 0.1633  1076 THR B CG2 
22548 N N   . TRP C 1077 ? 1.4932 1.2576 1.0303 -0.0664 -0.4176 0.1437  1077 TRP B N   
22549 C CA  . TRP C 1077 ? 1.4904 1.2067 1.0360 -0.0826 -0.4114 0.1377  1077 TRP B CA  
22550 C C   . TRP C 1077 ? 1.4647 1.1235 0.9801 -0.0615 -0.3882 0.1309  1077 TRP B C   
22551 O O   . TRP C 1077 ? 1.4274 1.0598 0.9469 -0.0624 -0.3692 0.1308  1077 TRP B O   
22552 C CB  . TRP C 1077 ? 1.5306 1.2397 1.0857 -0.1061 -0.4348 0.1322  1077 TRP B CB  
22553 C CG  . TRP C 1077 ? 1.5744 1.2427 1.1436 -0.1234 -0.4315 0.1280  1077 TRP B CG  
22554 C CD1 . TRP C 1077 ? 1.5838 1.2637 1.1859 -0.1455 -0.4331 0.1349  1077 TRP B CD1 
22555 C CD2 . TRP C 1077 ? 1.6225 1.2358 1.1736 -0.1187 -0.4260 0.1168  1077 TRP B CD2 
22556 N NE1 . TRP C 1077 ? 1.6110 1.2463 1.2170 -0.1539 -0.4291 0.1294  1077 TRP B NE1 
22557 C CE2 . TRP C 1077 ? 1.6307 1.2248 1.2057 -0.1374 -0.4245 0.1177  1077 TRP B CE2 
22558 C CE3 . TRP C 1077 ? 1.6529 1.2346 1.1695 -0.0994 -0.4218 0.1065  1077 TRP B CE3 
22559 C CZ2 . TRP C 1077 ? 1.6294 1.1742 1.1953 -0.1361 -0.4189 0.1084  1077 TRP B CZ2 
22560 C CZ3 . TRP C 1077 ? 1.6743 1.2075 1.1817 -0.0994 -0.4162 0.0965  1077 TRP B CZ3 
22561 C CH2 . TRP C 1077 ? 1.6506 1.1661 1.1827 -0.1169 -0.4147 0.0973  1077 TRP B CH2 
22562 N N   . LEU C 1078 ? 1.4669 1.1097 0.9518 -0.0437 -0.3900 0.1258  1078 LEU B N   
22563 C CA  . LEU C 1078 ? 1.4608 1.0507 0.9163 -0.0261 -0.3700 0.1201  1078 LEU B CA  
22564 C C   . LEU C 1078 ? 1.4806 1.0605 0.9210 -0.0043 -0.3454 0.1263  1078 LEU B C   
22565 O O   . LEU C 1078 ? 1.4966 1.0339 0.9249 0.0008  -0.3246 0.1242  1078 LEU B O   
22566 C CB  . LEU C 1078 ? 1.4344 1.0133 0.8607 -0.0133 -0.3788 0.1133  1078 LEU B CB  
22567 C CG  . LEU C 1078 ? 1.3854 0.9098 0.7874 -0.0036 -0.3624 0.1058  1078 LEU B CG  
22568 C CD1 . LEU C 1078 ? 1.3584 0.8661 0.7552 -0.0136 -0.3780 0.0933  1078 LEU B CD1 
22569 C CD2 . LEU C 1078 ? 1.4026 0.9151 0.7686 0.0273  -0.3456 0.1106  1078 LEU B CD2 
22570 N N   . THR C 1079 ? 1.4835 1.1033 0.9252 0.0078  -0.3479 0.1340  1079 THR B N   
22571 C CA  . THR C 1079 ? 1.5011 1.1098 0.9297 0.0284  -0.3250 0.1392  1079 THR B CA  
22572 C C   . THR C 1079 ? 1.4847 1.0748 0.9333 0.0111  -0.3105 0.1375  1079 THR B C   
22573 O O   . THR C 1079 ? 1.5068 1.0549 0.9381 0.0201  -0.2875 0.1362  1079 THR B O   
22574 C CB  . THR C 1079 ? 1.6407 1.3019 1.0710 0.0451  -0.3312 0.1475  1079 THR B CB  
22575 O OG1 . THR C 1079 ? 1.6614 1.3400 1.0703 0.0627  -0.3430 0.1496  1079 THR B OG1 
22576 C CG2 . THR C 1079 ? 1.6394 1.2818 1.0535 0.0685  -0.3068 0.1514  1079 THR B CG2 
22577 N N   . ALA C 1080 ? 1.4088 1.0310 0.8932 -0.0154 -0.3243 0.1381  1080 ALA B N   
22578 C CA  . ALA C 1080 ? 1.3729 0.9841 0.8774 -0.0329 -0.3123 0.1369  1080 ALA B CA  
22579 C C   . ALA C 1080 ? 1.3567 0.9139 0.8485 -0.0366 -0.2994 0.1307  1080 ALA B C   
22580 O O   . ALA C 1080 ? 1.3607 0.8846 0.8375 -0.0294 -0.2768 0.1291  1080 ALA B O   
22581 C CB  . ALA C 1080 ? 1.3403 0.9932 0.8842 -0.0613 -0.3312 0.1402  1080 ALA B CB  
22582 N N   . PHE C 1081 ? 1.3478 0.8971 0.8444 -0.0476 -0.3142 0.1268  1081 PHE B N   
22583 C CA  . PHE C 1081 ? 1.3277 0.8336 0.8168 -0.0526 -0.3052 0.1205  1081 PHE B CA  
22584 C C   . PHE C 1081 ? 1.3082 0.7730 0.7600 -0.0303 -0.2832 0.1187  1081 PHE B C   
22585 O O   . PHE C 1081 ? 1.2683 0.7004 0.7140 -0.0337 -0.2668 0.1159  1081 PHE B O   
22586 C CB  . PHE C 1081 ? 1.3581 0.8615 0.8501 -0.0606 -0.3262 0.1150  1081 PHE B CB  
22587 C CG  . PHE C 1081 ? 1.4004 0.8643 0.8870 -0.0645 -0.3188 0.1080  1081 PHE B CG  
22588 C CD1 . PHE C 1081 ? 1.3867 0.8491 0.9011 -0.0846 -0.3195 0.1083  1081 PHE B CD1 
22589 C CD2 . PHE C 1081 ? 1.4620 0.8942 0.9159 -0.0468 -0.3113 0.1019  1081 PHE B CD2 
22590 C CE1 . PHE C 1081 ? 1.4146 0.8447 0.9242 -0.0855 -0.3123 0.1022  1081 PHE B CE1 
22591 C CE2 . PHE C 1081 ? 1.4897 0.8907 0.9387 -0.0489 -0.3041 0.0953  1081 PHE B CE2 
22592 C CZ  . PHE C 1081 ? 1.4625 0.8627 0.9395 -0.0676 -0.3045 0.0952  1081 PHE B CZ  
22593 N N   . ALA C 1082 ? 1.3374 0.8060 0.7640 -0.0074 -0.2831 0.1216  1082 ALA B N   
22594 C CA  . ALA C 1082 ? 1.3672 0.7970 0.7568 0.0150  -0.2621 0.1228  1082 ALA B CA  
22595 C C   . ALA C 1082 ? 1.3621 0.7751 0.7504 0.0155  -0.2394 0.1258  1082 ALA B C   
22596 O O   . ALA C 1082 ? 1.3722 0.7476 0.7483 0.0127  -0.2205 0.1241  1082 ALA B O   
22597 C CB  . ALA C 1082 ? 1.3968 0.8390 0.7615 0.0404  -0.2682 0.1272  1082 ALA B CB  
22598 N N   . LEU C 1083 ? 1.3322 0.7750 0.7329 0.0178  -0.2415 0.1295  1083 LEU B N   
22599 C CA  . LEU C 1083 ? 1.3059 0.7395 0.7127 0.0119  -0.2236 0.1293  1083 LEU B CA  
22600 C C   . LEU C 1083 ? 1.3009 0.7200 0.7261 -0.0143 -0.2158 0.1246  1083 LEU B C   
22601 O O   . LEU C 1083 ? 1.3368 0.7178 0.7458 -0.0148 -0.1944 0.1229  1083 LEU B O   
22602 C CB  . LEU C 1083 ? 1.2303 0.7135 0.6608 0.0094  -0.2344 0.1318  1083 LEU B CB  
22603 C CG  . LEU C 1083 ? 1.2263 0.7153 0.6314 0.0407  -0.2327 0.1370  1083 LEU B CG  
22604 C CD1 . LEU C 1083 ? 1.2094 0.7604 0.6389 0.0398  -0.2495 0.1404  1083 LEU B CD1 
22605 C CD2 . LEU C 1083 ? 1.2263 0.6698 0.6028 0.0579  -0.2059 0.1369  1083 LEU B CD2 
22606 N N   . ARG C 1084 ? 1.2535 0.7037 0.7124 -0.0360 -0.2329 0.1235  1084 ARG B N   
22607 C CA  . ARG C 1084 ? 1.2559 0.6971 0.7336 -0.0589 -0.2275 0.1205  1084 ARG B CA  
22608 C C   . ARG C 1084 ? 1.3121 0.7072 0.7649 -0.0541 -0.2109 0.1174  1084 ARG B C   
22609 O O   . ARG C 1084 ? 1.3303 0.7075 0.7818 -0.0637 -0.1926 0.1160  1084 ARG B O   
22610 C CB  . ARG C 1084 ? 1.2544 0.7238 0.7636 -0.0771 -0.2504 0.1209  1084 ARG B CB  
22611 C CG  . ARG C 1084 ? 1.2138 0.6617 0.7301 -0.0898 -0.2473 0.1175  1084 ARG B CG  
22612 C CD  . ARG C 1084 ? 1.2062 0.6778 0.7574 -0.1134 -0.2489 0.1201  1084 ARG B CD  
22613 N NE  . ARG C 1084 ? 1.2789 0.7331 0.8366 -0.1231 -0.2421 0.1179  1084 ARG B NE  
22614 C CZ  . ARG C 1084 ? 1.3452 0.8109 0.9280 -0.1359 -0.2568 0.1195  1084 ARG B CZ  
22615 N NH1 . ARG C 1084 ? 1.3733 0.8647 0.9757 -0.1430 -0.2795 0.1234  1084 ARG B NH1 
22616 N NH2 . ARG C 1084 ? 1.3445 0.7969 0.9328 -0.1418 -0.2491 0.1182  1084 ARG B NH2 
22617 N N   . VAL C 1085 ? 1.3626 0.7416 0.7955 -0.0407 -0.2170 0.1163  1085 VAL B N   
22618 C CA  . VAL C 1085 ? 1.4205 0.7615 0.8313 -0.0372 -0.2016 0.1139  1085 VAL B CA  
22619 C C   . VAL C 1085 ? 1.4524 0.7581 0.8287 -0.0224 -0.1781 0.1172  1085 VAL B C   
22620 O O   . VAL C 1085 ? 1.4396 0.7163 0.8019 -0.0263 -0.1601 0.1169  1085 VAL B O   
22621 C CB  . VAL C 1085 ? 1.3079 0.6429 0.7077 -0.0286 -0.2148 0.1100  1085 VAL B CB  
22622 C CG1 . VAL C 1085 ? 1.3245 0.6261 0.7033 -0.0255 -0.1976 0.1078  1085 VAL B CG1 
22623 C CG2 . VAL C 1085 ? 1.2565 0.6179 0.6888 -0.0447 -0.2377 0.1063  1085 VAL B CG2 
22624 N N   . LEU C 1086 ? 1.4977 0.8069 0.8606 -0.0053 -0.1787 0.1212  1086 LEU B N   
22625 C CA  . LEU C 1086 ? 1.5803 0.8533 0.9100 0.0109  -0.1576 0.1256  1086 LEU B CA  
22626 C C   . LEU C 1086 ? 1.5806 0.8423 0.9188 -0.0055 -0.1404 0.1234  1086 LEU B C   
22627 O O   . LEU C 1086 ? 1.6168 0.8390 0.9333 -0.0077 -0.1191 0.1242  1086 LEU B O   
22628 C CB  . LEU C 1086 ? 1.6476 0.9331 0.9637 0.0359  -0.1645 0.1308  1086 LEU B CB  
22629 C CG  . LEU C 1086 ? 1.7227 1.0015 1.0083 0.0637  -0.1696 0.1366  1086 LEU B CG  
22630 C CD1 . LEU C 1086 ? 1.7568 0.9837 1.0025 0.0786  -0.1470 0.1426  1086 LEU B CD1 
22631 C CD2 . LEU C 1086 ? 1.7299 1.0322 1.0250 0.0593  -0.1904 0.1327  1086 LEU B CD2 
22632 N N   . GLY C 1087 ? 1.5287 0.8268 0.8976 -0.0180 -0.1499 0.1207  1087 GLY B N   
22633 C CA  . GLY C 1087 ? 1.4993 0.7947 0.8785 -0.0345 -0.1358 0.1169  1087 GLY B CA  
22634 C C   . GLY C 1087 ? 1.4711 0.7500 0.8550 -0.0563 -0.1241 0.1142  1087 GLY B C   
22635 O O   . GLY C 1087 ? 1.5082 0.7533 0.8740 -0.0623 -0.1030 0.1128  1087 GLY B O   
22636 N N   . GLN C 1088 ? 1.3980 0.7006 0.8052 -0.0677 -0.1380 0.1137  1088 GLN B N   
22637 C CA  . GLN C 1088 ? 1.4115 0.7038 0.8229 -0.0838 -0.1289 0.1122  1088 GLN B CA  
22638 C C   . GLN C 1088 ? 1.5047 0.7512 0.8797 -0.0764 -0.1080 0.1139  1088 GLN B C   
22639 O O   . GLN C 1088 ? 1.5082 0.7408 0.8803 -0.0929 -0.0904 0.1127  1088 GLN B O   
22640 C CB  . GLN C 1088 ? 1.3876 0.7016 0.8183 -0.0856 -0.1483 0.1118  1088 GLN B CB  
22641 C CG  . GLN C 1088 ? 1.3677 0.7239 0.8330 -0.0948 -0.1688 0.1122  1088 GLN B CG  
22642 C CD  . GLN C 1088 ? 1.3543 0.7286 0.8434 -0.1033 -0.1861 0.1118  1088 GLN B CD  
22643 O OE1 . GLN C 1088 ? 1.3319 0.7295 0.8371 -0.1027 -0.2073 0.1129  1088 GLN B OE1 
22644 N NE2 . GLN C 1088 ? 1.3595 0.7237 0.8512 -0.1114 -0.1772 0.1103  1088 GLN B NE2 
22645 N N   . VAL C 1089 ? 1.5696 0.7954 0.9165 -0.0532 -0.1100 0.1175  1089 VAL B N   
22646 C CA  . VAL C 1089 ? 1.6101 0.7963 0.9230 -0.0463 -0.0919 0.1213  1089 VAL B CA  
22647 C C   . VAL C 1089 ? 1.6804 0.8270 0.9638 -0.0403 -0.0718 0.1251  1089 VAL B C   
22648 O O   . VAL C 1089 ? 1.7031 0.8132 0.9587 -0.0402 -0.0535 0.1296  1089 VAL B O   
22649 C CB  . VAL C 1089 ? 1.5481 0.7306 0.8424 -0.0250 -0.1020 0.1238  1089 VAL B CB  
22650 C CG1 . VAL C 1089 ? 1.5451 0.6987 0.8127 -0.0238 -0.0848 0.1274  1089 VAL B CG1 
22651 C CG2 . VAL C 1089 ? 1.5109 0.7291 0.8340 -0.0299 -0.1245 0.1181  1089 VAL B CG2 
22652 N N   . ASN C 1090 ? 1.7405 0.8941 1.0300 -0.0359 -0.0749 0.1235  1090 ASN B N   
22653 C CA  . ASN C 1090 ? 1.8296 0.9432 1.0927 -0.0304 -0.0561 0.1250  1090 ASN B CA  
22654 C C   . ASN C 1090 ? 1.8699 0.9623 1.1324 -0.0578 -0.0360 0.1209  1090 ASN B C   
22655 O O   . ASN C 1090 ? 1.9134 0.9587 1.1456 -0.0566 -0.0166 0.1232  1090 ASN B O   
22656 C CB  . ASN C 1090 ? 1.8460 0.9781 1.1188 -0.0195 -0.0644 0.1222  1090 ASN B CB  
22657 C CG  . ASN C 1090 ? 1.9261 1.0120 1.1663 -0.0054 -0.0464 0.1239  1090 ASN B CG  
22658 O OD1 . ASN C 1090 ? 1.9520 0.9901 1.1665 -0.0122 -0.0261 0.1258  1090 ASN B OD1 
22659 N ND2 . ASN C 1090 ? 1.9583 1.0571 1.1982 0.0150  -0.0535 0.1238  1090 ASN B ND2 
22660 N N   . LYS C 1091 ? 1.8635 0.9910 1.1591 -0.0832 -0.0409 0.1152  1091 LYS B N   
22661 C CA  . LYS C 1091 ? 1.9022 1.0184 1.1992 -0.1115 -0.0231 0.1113  1091 LYS B CA  
22662 C C   . LYS C 1091 ? 1.8792 0.9510 1.1419 -0.1107 -0.0050 0.1180  1091 LYS B C   
22663 O O   . LYS C 1091 ? 1.9223 0.9546 1.1622 -0.1207 0.0144  0.1177  1091 LYS B O   
22664 C CB  . LYS C 1091 ? 1.9656 1.1285 1.3002 -0.1346 -0.0314 0.1082  1091 LYS B CB  
22665 C CG  . LYS C 1091 ? 2.0313 1.2361 1.4011 -0.1505 -0.0407 0.1016  1091 LYS B CG  
22666 C CD  . LYS C 1091 ? 2.0864 1.3170 1.4789 -0.1806 -0.0344 0.0992  1091 LYS B CD  
22667 C CE  . LYS C 1091 ? 2.1804 1.3723 1.5454 -0.1959 -0.0096 0.0982  1091 LYS B CE  
22668 N NZ  . LYS C 1091 ? 2.1968 1.4130 1.5807 -0.2285 -0.0007 0.0921  1091 LYS B NZ  
22669 N N   . TYR C 1092 ? 1.8272 0.9057 1.0856 -0.0995 -0.0115 0.1237  1092 TYR B N   
22670 C CA  . TYR C 1092 ? 1.8480 0.8957 1.0781 -0.1013 0.0047  0.1309  1092 TYR B CA  
22671 C C   . TYR C 1092 ? 1.9462 0.9569 1.1380 -0.0724 0.0079  0.1407  1092 TYR B C   
22672 O O   . TYR C 1092 ? 2.0147 0.9916 1.1769 -0.0737 0.0245  0.1488  1092 TYR B O   
22673 C CB  . TYR C 1092 ? 1.7696 0.8518 1.0193 -0.1106 -0.0011 0.1303  1092 TYR B CB  
22674 C CG  . TYR C 1092 ? 1.7123 0.8351 1.0006 -0.1353 -0.0059 0.1229  1092 TYR B CG  
22675 C CD1 . TYR C 1092 ? 1.7204 0.8379 1.0116 -0.1620 0.0097  0.1199  1092 TYR B CD1 
22676 C CD2 . TYR C 1092 ? 1.6795 0.8459 1.0009 -0.1326 -0.0264 0.1192  1092 TYR B CD2 
22677 C CE1 . TYR C 1092 ? 1.7075 0.8674 1.0344 -0.1845 0.0051  0.1141  1092 TYR B CE1 
22678 C CE2 . TYR C 1092 ? 1.6531 0.8578 1.0101 -0.1542 -0.0310 0.1147  1092 TYR B CE2 
22679 C CZ  . TYR C 1092 ? 1.6662 0.8704 1.0264 -0.1797 -0.0151 0.1125  1092 TYR B CZ  
22680 O OH  . TYR C 1092 ? 1.6300 0.8771 1.0256 -0.2012 -0.0195 0.1089  1092 TYR B OH  
22681 N N   . VAL C 1093 ? 1.9522 0.9722 1.1442 -0.0469 -0.0080 0.1413  1093 VAL B N   
22682 C CA  . VAL C 1093 ? 1.9851 0.9727 1.1404 -0.0178 -0.0051 0.1515  1093 VAL B CA  
22683 C C   . VAL C 1093 ? 1.9599 0.9446 1.1126 0.0028  -0.0126 0.1511  1093 VAL B C   
22684 O O   . VAL C 1093 ? 1.9259 0.9512 1.1013 0.0124  -0.0332 0.1469  1093 VAL B O   
22685 C CB  . VAL C 1093 ? 1.9939 1.0033 1.1460 -0.0017 -0.0182 0.1548  1093 VAL B CB  
22686 C CG1 . VAL C 1093 ? 2.0563 1.0369 1.1702 0.0285  -0.0152 0.1665  1093 VAL B CG1 
22687 C CG2 . VAL C 1093 ? 1.9791 0.9947 1.1335 -0.0197 -0.0098 0.1547  1093 VAL B CG2 
22688 N N   . GLU C 1094 ? 1.9694 0.9065 1.0943 0.0092  0.0043  0.1554  1094 GLU B N   
22689 C CA  . GLU C 1094 ? 1.9671 0.9014 1.0907 0.0274  0.0002  0.1532  1094 GLU B CA  
22690 C C   . GLU C 1094 ? 1.9411 0.9017 1.0618 0.0591  -0.0180 0.1595  1094 GLU B C   
22691 O O   . GLU C 1094 ? 1.9967 0.9437 1.0935 0.0749  -0.0168 0.1696  1094 GLU B O   
22692 C CB  . GLU C 1094 ? 2.0699 0.9381 1.1557 0.0345  0.0227  0.1585  1094 GLU B CB  
22693 C CG  . GLU C 1094 ? 2.1390 0.9987 1.2214 0.0529  0.0223  0.1542  1094 GLU B CG  
22694 C CD  . GLU C 1094 ? 2.2739 1.0577 1.3133 0.0634  0.0454  0.1600  1094 GLU B CD  
22695 O OE1 . GLU C 1094 ? 2.3294 1.0675 1.3416 0.0549  0.0613  0.1691  1094 GLU B OE1 
22696 O OE2 . GLU C 1094 ? 2.3153 1.0841 1.3471 0.0806  0.0480  0.1558  1094 GLU B OE2 
22697 N N   . GLN C 1095 ? 1.8767 0.8803 1.0224 0.0669  -0.0358 0.1538  1095 GLN B N   
22698 C CA  . GLN C 1095 ? 1.8818 0.9129 1.0233 0.0957  -0.0531 0.1600  1095 GLN B CA  
22699 C C   . GLN C 1095 ? 1.9676 0.9829 1.0908 0.1230  -0.0483 0.1646  1095 GLN B C   
22700 O O   . GLN C 1095 ? 1.9952 0.9882 1.1177 0.1165  -0.0361 0.1592  1095 GLN B O   
22701 C CB  . GLN C 1095 ? 1.8120 0.9064 0.9927 0.0859  -0.0784 0.1526  1095 GLN B CB  
22702 C CG  . GLN C 1095 ? 1.8200 0.9261 1.0203 0.0586  -0.0813 0.1468  1095 GLN B CG  
22703 C CD  . GLN C 1095 ? 2.2177 1.3102 1.3953 0.0674  -0.0804 0.1525  1095 GLN B CD  
22704 O OE1 . GLN C 1095 ? 2.2233 1.3388 1.3976 0.0842  -0.0965 0.1545  1095 GLN B OE1 
22705 N NE2 . GLN C 1095 ? 2.2244 1.2841 1.3873 0.0543  -0.0620 0.1546  1095 GLN B NE2 
22706 N N   . ASN C 1096 ? 2.0398 1.0652 1.1457 0.1547  -0.0570 0.1745  1096 ASN B N   
22707 C CA  . ASN C 1096 ? 2.1164 1.1255 1.1995 0.1879  -0.0516 0.1819  1096 ASN B CA  
22708 C C   . ASN C 1096 ? 2.1156 1.1609 1.2259 0.1866  -0.0596 0.1722  1096 ASN B C   
22709 O O   . ASN C 1096 ? 2.0638 1.1706 1.2065 0.1800  -0.0809 0.1673  1096 ASN B O   
22710 C CB  . ASN C 1096 ? 2.1757 1.2089 1.2432 0.2191  -0.0647 0.1939  1096 ASN B CB  
22711 C CG  . ASN C 1096 ? 2.2545 1.2912 1.3059 0.2565  -0.0647 0.2020  1096 ASN B CG  
22712 O OD1 . ASN C 1096 ? 2.3447 1.3473 1.3595 0.2858  -0.0548 0.2164  1096 ASN B OD1 
22713 N ND2 . ASN C 1096 ? 2.2338 1.3153 1.3123 0.2572  -0.0762 0.1941  1096 ASN B ND2 
22714 N N   . GLN C 1097 ? 2.1859 1.1943 1.2830 0.1924  -0.0431 0.1691  1097 GLN B N   
22715 C CA  . GLN C 1097 ? 2.1745 1.2221 1.2992 0.1887  -0.0503 0.1582  1097 GLN B CA  
22716 C C   . GLN C 1097 ? 2.2059 1.3101 1.3392 0.2184  -0.0688 0.1637  1097 GLN B C   
22717 O O   . GLN C 1097 ? 2.1300 1.2996 1.2987 0.2063  -0.0893 0.1593  1097 GLN B O   
22718 C CB  . GLN C 1097 ? 2.2071 1.2035 1.3139 0.1900  -0.0288 0.1512  1097 GLN B CB  
22719 C CG  . GLN C 1097 ? 2.1525 1.1924 1.2914 0.1768  -0.0350 0.1370  1097 GLN B CG  
22720 C CD  . GLN C 1097 ? 2.2040 1.1964 1.3219 0.1846  -0.0150 0.1283  1097 GLN B CD  
22721 O OE1 . GLN C 1097 ? 2.2641 1.1828 1.3429 0.1961  0.0047  0.1325  1097 GLN B OE1 
22722 N NE2 . GLN C 1097 ? 2.1843 1.2177 1.3270 0.1781  -0.0200 0.1159  1097 GLN B NE2 
22723 N N   . ASN C 1098 ? 2.2998 1.3788 1.3999 0.2571  -0.0614 0.1748  1098 ASN B N   
22724 C CA  . ASN C 1098 ? 2.3387 1.4716 1.4419 0.2900  -0.0771 0.1824  1098 ASN B CA  
22725 C C   . ASN C 1098 ? 2.1008 1.3069 1.2334 0.2792  -0.1045 0.1838  1098 ASN B C   
22726 O O   . ASN C 1098 ? 2.0406 1.3125 1.1999 0.2816  -0.1218 0.1813  1098 ASN B O   
22727 C CB  . ASN C 1098 ? 2.4318 1.5208 1.4900 0.3324  -0.0649 0.1983  1098 ASN B CB  
22728 C CG  . ASN C 1098 ? 2.4794 1.6278 1.5385 0.3688  -0.0809 0.2084  1098 ASN B CG  
22729 O OD1 . ASN C 1098 ? 2.5014 1.6702 1.5508 0.3819  -0.0914 0.2198  1098 ASN B OD1 
22730 N ND2 . ASN C 1098 ? 2.4936 1.6740 1.5640 0.3850  -0.0829 0.2039  1098 ASN B ND2 
22731 N N   . SER C 1099 ? 2.0964 1.2909 1.2231 0.2667  -0.1083 0.1872  1099 SER B N   
22732 C CA  . SER C 1099 ? 2.0126 1.2655 1.1664 0.2506  -0.1329 0.1848  1099 SER B CA  
22733 C C   . SER C 1099 ? 1.9230 1.2171 1.1199 0.2190  -0.1439 0.1724  1099 SER B C   
22734 O O   . SER C 1099 ? 1.9202 1.2752 1.1408 0.2214  -0.1615 0.1717  1099 SER B O   
22735 C CB  . SER C 1099 ? 1.9958 1.2208 1.1388 0.2352  -0.1313 0.1856  1099 SER B CB  
22736 O OG  . SER C 1099 ? 1.9364 1.2083 1.1108 0.2105  -0.1530 0.1779  1099 SER B OG  
22737 N N   . ILE C 1100 ? 1.8432 1.1063 1.0500 0.1893  -0.1331 0.1636  1100 ILE B N   
22738 C CA  . ILE C 1100 ? 1.7287 1.0308 0.9769 0.1568  -0.1441 0.1534  1100 ILE B CA  
22739 C C   . ILE C 1100 ? 1.7389 1.0857 1.0067 0.1632  -0.1500 0.1507  1100 ILE B C   
22740 O O   . ILE C 1100 ? 1.6974 1.0989 1.0014 0.1432  -0.1673 0.1468  1100 ILE B O   
22741 C CB  . ILE C 1100 ? 1.6503 0.9121 0.9029 0.1278  -0.1279 0.1453  1100 ILE B CB  
22742 C CG1 . ILE C 1100 ? 1.5839 0.8270 0.8335 0.1120  -0.1291 0.1458  1100 ILE B CG1 
22743 C CG2 . ILE C 1100 ? 1.5965 0.9008 0.8896 0.1003  -0.1368 0.1365  1100 ILE B CG2 
22744 C CD1 . ILE C 1100 ? 1.5050 0.7978 0.7907 0.0900  -0.1519 0.1414  1100 ILE B CD1 
22745 N N   . CYS C 1101 ? 1.7930 1.1159 1.0364 0.1912  -0.1351 0.1532  1101 CYS B N   
22746 C CA  . CYS C 1101 ? 1.7836 1.1500 1.0420 0.2024  -0.1390 0.1503  1101 CYS B CA  
22747 C C   . CYS C 1101 ? 1.7470 1.1882 1.0236 0.2136  -0.1639 0.1575  1101 CYS B C   
22748 O O   . CYS C 1101 ? 1.6776 1.1792 0.9901 0.1946  -0.1801 0.1541  1101 CYS B O   
22749 C CB  . CYS C 1101 ? 1.8546 1.1766 1.0778 0.2372  -0.1183 0.1521  1101 CYS B CB  
22750 S SG  . CYS C 1101 ? 2.1914 1.4482 1.4034 0.2209  -0.0916 0.1384  1101 CYS B SG  
22751 N N   . ASN C 1102 ? 1.7683 1.2060 1.0195 0.2430  -0.1670 0.1683  1102 ASN B N   
22752 C CA  . ASN C 1102 ? 1.7279 1.2355 0.9910 0.2553  -0.1901 0.1759  1102 ASN B CA  
22753 C C   . ASN C 1102 ? 1.6793 1.2276 0.9730 0.2216  -0.2133 0.1729  1102 ASN B C   
22754 O O   . ASN C 1102 ? 1.6407 1.2582 0.9592 0.2165  -0.2344 0.1751  1102 ASN B O   
22755 C CB  . ASN C 1102 ? 1.7551 1.2437 0.9810 0.2922  -0.1864 0.1881  1102 ASN B CB  
22756 C CG  . ASN C 1102 ? 1.7834 1.2492 0.9823 0.3318  -0.1690 0.1937  1102 ASN B CG  
22757 O OD1 . ASN C 1102 ? 1.7869 1.2846 1.0001 0.3387  -0.1684 0.1898  1102 ASN B OD1 
22758 N ND2 . ASN C 1102 ? 1.8145 1.2248 0.9733 0.3593  -0.1543 0.2032  1102 ASN B ND2 
22759 N N   . SER C 1103 ? 1.6786 1.1837 0.9696 0.1990  -0.2094 0.1683  1103 SER B N   
22760 C CA  . SER C 1103 ? 1.6442 1.1775 0.9634 0.1666  -0.2293 0.1637  1103 SER B CA  
22761 C C   . SER C 1103 ? 1.6181 1.1934 0.9771 0.1405  -0.2375 0.1583  1103 SER B C   
22762 O O   . SER C 1103 ? 1.5863 1.2181 0.9725 0.1252  -0.2601 0.1594  1103 SER B O   
22763 C CB  . SER C 1103 ? 1.6404 1.1176 0.9497 0.1488  -0.2201 0.1587  1103 SER B CB  
22764 O OG  . SER C 1103 ? 1.6724 1.1095 0.9438 0.1715  -0.2107 0.1644  1103 SER B OG  
22765 N N   . LEU C 1104 ? 1.6430 1.1911 1.0038 0.1347  -0.2191 0.1529  1104 LEU B N   
22766 C CA  . LEU C 1104 ? 1.6193 1.2067 1.0146 0.1126  -0.2233 0.1481  1104 LEU B CA  
22767 C C   . LEU C 1104 ? 1.6680 1.3210 1.0750 0.1293  -0.2343 0.1530  1104 LEU B C   
22768 O O   . LEU C 1104 ? 1.6385 1.3526 1.0790 0.1094  -0.2537 0.1547  1104 LEU B O   
22769 C CB  . LEU C 1104 ? 1.5974 1.1397 0.9844 0.1083  -0.1991 0.1403  1104 LEU B CB  
22770 C CG  . LEU C 1104 ? 1.5597 1.0641 0.9549 0.0772  -0.1905 0.1336  1104 LEU B CG  
22771 C CD1 . LEU C 1104 ? 1.5818 1.0418 0.9624 0.0764  -0.1654 0.1258  1104 LEU B CD1 
22772 C CD2 . LEU C 1104 ? 1.4920 1.0460 0.9297 0.0444  -0.2086 0.1324  1104 LEU B CD2 
22773 N N   . LEU C 1105 ? 1.7526 1.3921 1.1309 0.1663  -0.2213 0.1562  1105 LEU B N   
22774 C CA  . LEU C 1105 ? 1.7682 1.4675 1.1511 0.1910  -0.2278 0.1613  1105 LEU B CA  
22775 C C   . LEU C 1105 ? 1.7663 1.5324 1.1632 0.1919  -0.2538 0.1704  1105 LEU B C   
22776 O O   . LEU C 1105 ? 1.7716 1.6020 1.1783 0.2073  -0.2631 0.1759  1105 LEU B O   
22777 C CB  . LEU C 1105 ? 1.8226 1.4819 1.1658 0.2350  -0.2076 0.1640  1105 LEU B CB  
22778 C CG  . LEU C 1105 ? 1.8682 1.4808 1.1987 0.2412  -0.1830 0.1544  1105 LEU B CG  
22779 C CD1 . LEU C 1105 ? 1.9338 1.4632 1.2173 0.2711  -0.1599 0.1564  1105 LEU B CD1 
22780 C CD2 . LEU C 1105 ? 1.8639 1.5347 1.2094 0.2551  -0.1844 0.1519  1105 LEU B CD2 
22781 N N   . TRP C 1106 ? 1.7508 1.5031 1.1475 0.1753  -0.2654 0.1713  1106 TRP B N   
22782 C CA  . TRP C 1106 ? 1.7343 1.5441 1.1423 0.1716  -0.2906 0.1778  1106 TRP B CA  
22783 C C   . TRP C 1106 ? 1.6998 1.5635 1.1505 0.1333  -0.3108 0.1763  1106 TRP B C   
22784 O O   . TRP C 1106 ? 1.6857 1.6220 1.1553 0.1320  -0.3284 0.1826  1106 TRP B O   
22785 C CB  . TRP C 1106 ? 1.7575 1.5265 1.1449 0.1697  -0.2941 0.1774  1106 TRP B CB  
22786 C CG  . TRP C 1106 ? 1.7327 1.5540 1.1283 0.1631  -0.3201 0.1815  1106 TRP B CG  
22787 C CD1 . TRP C 1106 ? 1.7325 1.5918 1.1117 0.1905  -0.3282 0.1898  1106 TRP B CD1 
22788 C CD2 . TRP C 1106 ? 1.7173 1.5569 1.1378 0.1263  -0.3415 0.1770  1106 TRP B CD2 
22789 N NE1 . TRP C 1106 ? 1.7142 1.6166 1.1067 0.1706  -0.3537 0.1898  1106 TRP B NE1 
22790 C CE2 . TRP C 1106 ? 1.7109 1.5988 1.1283 0.1310  -0.3623 0.1817  1106 TRP B CE2 
22791 C CE3 . TRP C 1106 ? 1.7240 1.5433 1.1687 0.0902  -0.3450 0.1699  1106 TRP B CE3 
22792 C CZ2 . TRP C 1106 ? 1.7271 1.6389 1.1633 0.0992  -0.3866 0.1779  1106 TRP B CZ2 
22793 C CZ3 . TRP C 1106 ? 1.7213 1.5628 1.1849 0.0613  -0.3688 0.1675  1106 TRP B CZ3 
22794 C CH2 . TRP C 1106 ? 1.7214 1.6063 1.1800 0.0651  -0.3894 0.1708  1106 TRP B CH2 
22795 N N   . LEU C 1107 ? 1.6822 1.5121 1.1484 0.1020  -0.3083 0.1694  1107 LEU B N   
22796 C CA  . LEU C 1107 ? 1.6611 1.5348 1.1668 0.0646  -0.3275 0.1697  1107 LEU B CA  
22797 C C   . LEU C 1107 ? 1.7082 1.6424 1.2361 0.0652  -0.3285 0.1734  1107 LEU B C   
22798 O O   . LEU C 1107 ? 1.7030 1.7069 1.2548 0.0537  -0.3489 0.1803  1107 LEU B O   
22799 C CB  . LEU C 1107 ? 1.5884 1.4153 1.1060 0.0357  -0.3209 0.1627  1107 LEU B CB  
22800 C CG  . LEU C 1107 ? 1.5508 1.3236 1.0541 0.0277  -0.3218 0.1581  1107 LEU B CG  
22801 C CD1 . LEU C 1107 ? 1.5709 1.2770 1.0442 0.0451  -0.2952 0.1532  1107 LEU B CD1 
22802 C CD2 . LEU C 1107 ? 1.5070 1.2781 1.0400 -0.0092 -0.3323 0.1555  1107 LEU B CD2 
22803 N N   . VAL C 1108 ? 1.7601 1.6673 1.2784 0.0786  -0.3060 0.1683  1108 VAL B N   
22804 C CA  . VAL C 1108 ? 1.7720 1.7289 1.3118 0.0756  -0.3037 0.1684  1108 VAL B CA  
22805 C C   . VAL C 1108 ? 1.8102 1.8327 1.3479 0.1042  -0.3093 0.1755  1108 VAL B C   
22806 O O   . VAL C 1108 ? 1.8009 1.8935 1.3665 0.0933  -0.3195 0.1796  1108 VAL B O   
22807 C CB  . VAL C 1108 ? 1.7757 1.6815 1.3036 0.0800  -0.2776 0.1583  1108 VAL B CB  
22808 C CG1 . VAL C 1108 ? 1.8227 1.6558 1.3074 0.1111  -0.2573 0.1545  1108 VAL B CG1 
22809 C CG2 . VAL C 1108 ? 1.7694 1.7257 1.3090 0.0894  -0.2725 0.1569  1108 VAL B CG2 
22810 N N   . GLU C 1109 ? 1.8617 1.8664 1.3670 0.1411  -0.3029 0.1782  1109 GLU B N   
22811 C CA  . GLU C 1109 ? 1.8963 1.9666 1.3988 0.1719  -0.3077 0.1858  1109 GLU B CA  
22812 C C   . GLU C 1109 ? 1.8950 2.0412 1.4168 0.1602  -0.3360 0.1963  1109 GLU B C   
22813 O O   . GLU C 1109 ? 1.8932 2.1173 1.4274 0.1721  -0.3448 0.2036  1109 GLU B O   
22814 C CB  . GLU C 1109 ? 1.9561 1.9820 1.4159 0.2199  -0.2890 0.1864  1109 GLU B CB  
22815 C CG  . GLU C 1109 ? 1.9796 1.9331 1.4178 0.2334  -0.2607 0.1761  1109 GLU B CG  
22816 C CD  . GLU C 1109 ? 2.0186 1.9317 1.4151 0.2828  -0.2426 0.1786  1109 GLU B CD  
22817 O OE1 . GLU C 1109 ? 2.0418 1.8691 1.4092 0.2902  -0.2233 0.1738  1109 GLU B OE1 
22818 O OE2 . GLU C 1109 ? 2.0265 1.9950 1.4193 0.3144  -0.2476 0.1865  1109 GLU B OE2 
22819 N N   . ASN C 1110 ? 1.8866 2.0116 1.4103 0.1366  -0.3501 0.1967  1110 ASN B N   
22820 C CA  . ASN C 1110 ? 1.8658 2.0546 1.4035 0.1234  -0.3772 0.2049  1110 ASN B CA  
22821 C C   . ASN C 1110 ? 1.8172 2.0294 1.3909 0.0734  -0.3981 0.2052  1110 ASN B C   
22822 O O   . ASN C 1110 ? 1.7985 2.0818 1.3937 0.0560  -0.4209 0.2131  1110 ASN B O   
22823 C CB  . ASN C 1110 ? 1.9040 2.0582 1.4105 0.1404  -0.3799 0.2053  1110 ASN B CB  
22824 C CG  . ASN C 1110 ? 1.9598 2.0867 1.4287 0.1909  -0.3595 0.2077  1110 ASN B CG  
22825 O OD1 . ASN C 1110 ? 1.9911 2.0383 1.4327 0.2041  -0.3403 0.2025  1110 ASN B OD1 
22826 N ND2 . ASN C 1110 ? 1.9709 2.1647 1.4381 0.2194  -0.3633 0.2167  1110 ASN B ND2 
22827 N N   . TYR C 1111 ? 1.7932 1.9471 1.3737 0.0501  -0.3901 0.1977  1111 TYR B N   
22828 C CA  . TYR C 1111 ? 1.7758 1.9315 1.3829 0.0064  -0.4091 0.1979  1111 TYR B CA  
22829 C C   . TYR C 1111 ? 1.7590 1.9198 1.3971 -0.0228 -0.4066 0.1978  1111 TYR B C   
22830 O O   . TYR C 1111 ? 1.7391 1.8655 1.3901 -0.0522 -0.4120 0.1952  1111 TYR B O   
22831 C CB  . TYR C 1111 ? 1.7768 1.8594 1.3626 0.0028  -0.4081 0.1902  1111 TYR B CB  
22832 C CG  . TYR C 1111 ? 1.7921 1.8888 1.3556 0.0203  -0.4194 0.1922  1111 TYR B CG  
22833 C CD1 . TYR C 1111 ? 1.7956 1.9223 1.3713 -0.0055 -0.4457 0.1938  1111 TYR B CD1 
22834 C CD2 . TYR C 1111 ? 1.8115 1.8935 1.3415 0.0620  -0.4044 0.1929  1111 TYR B CD2 
22835 C CE1 . TYR C 1111 ? 1.8112 1.9566 1.3667 0.0085  -0.4571 0.1948  1111 TYR B CE1 
22836 C CE2 . TYR C 1111 ? 1.8292 1.9305 1.3392 0.0783  -0.4154 0.1960  1111 TYR B CE2 
22837 C CZ  . TYR C 1111 ? 1.8330 1.9684 1.3564 0.0506  -0.4420 0.1963  1111 TYR B CZ  
22838 O OH  . TYR C 1111 ? 1.8620 2.0215 1.3660 0.0637  -0.4543 0.1983  1111 TYR B OH  
22839 N N   . GLN C 1112 ? 1.7696 1.9769 1.4191 -0.0133 -0.3988 0.2010  1112 GLN B N   
22840 C CA  . GLN C 1112 ? 1.7559 1.9835 1.4355 -0.0395 -0.3974 0.2024  1112 GLN B CA  
22841 C C   . GLN C 1112 ? 1.7928 2.1180 1.4983 -0.0458 -0.4121 0.2137  1112 GLN B C   
22842 O O   . GLN C 1112 ? 1.8185 2.1836 1.5145 -0.0155 -0.4043 0.2148  1112 GLN B O   
22843 C CB  . GLN C 1112 ? 1.7320 1.9184 1.3974 -0.0210 -0.3694 0.1927  1112 GLN B CB  
22844 C CG  . GLN C 1112 ? 1.6693 1.8823 1.3642 -0.0457 -0.3662 0.1932  1112 GLN B CG  
22845 C CD  . GLN C 1112 ? 1.6559 1.8153 1.3338 -0.0328 -0.3388 0.1808  1112 GLN B CD  
22846 O OE1 . GLN C 1112 ? 1.6814 1.8179 1.3305 0.0018  -0.3214 0.1739  1112 GLN B OE1 
22847 N NE2 . GLN C 1112 ? 1.6125 1.7514 1.3077 -0.0609 -0.3349 0.1782  1112 GLN B NE2 
22848 N N   . LEU C 1113 ? 1.8053 2.1687 1.5430 -0.0848 -0.4334 0.2228  1113 LEU B N   
22849 C CA  . LEU C 1113 ? 1.8066 2.2670 1.5715 -0.0975 -0.4504 0.2359  1113 LEU B CA  
22850 C C   . LEU C 1113 ? 1.8254 2.3296 1.6041 -0.0903 -0.4367 0.2367  1113 LEU B C   
22851 O O   . LEU C 1113 ? 1.8134 2.2701 1.5855 -0.0850 -0.4168 0.2272  1113 LEU B O   
22852 C CB  . LEU C 1113 ? 1.7696 2.2485 1.5643 -0.1447 -0.4757 0.2460  1113 LEU B CB  
22853 C CG  . LEU C 1113 ? 1.7567 2.1986 1.5385 -0.1547 -0.4920 0.2439  1113 LEU B CG  
22854 C CD1 . LEU C 1113 ? 1.7400 2.1444 1.5410 -0.1959 -0.5053 0.2461  1113 LEU B CD1 
22855 C CD2 . LEU C 1113 ? 1.7545 2.2711 1.5393 -0.1547 -0.5123 0.2529  1113 LEU B CD2 
22856 N N   . ASP C 1114 ? 1.8509 2.4493 1.6480 -0.0906 -0.4476 0.2477  1114 ASP B N   
22857 C CA  . ASP C 1114 ? 1.8631 2.5174 1.6742 -0.0831 -0.4368 0.2489  1114 ASP B CA  
22858 C C   . ASP C 1114 ? 1.8157 2.4781 1.6580 -0.1225 -0.4406 0.2541  1114 ASP B C   
22859 O O   . ASP C 1114 ? 1.7999 2.5380 1.6665 -0.1330 -0.4439 0.2625  1114 ASP B O   
22860 C CB  . ASP C 1114 ? 1.9187 2.6792 1.7420 -0.0730 -0.4488 0.2606  1114 ASP B CB  
22861 C CG  . ASP C 1114 ? 1.9993 2.7659 1.7924 -0.0195 -0.4321 0.2530  1114 ASP B CG  
22862 O OD1 . ASP C 1114 ? 2.0316 2.7396 1.8020 0.0071  -0.4075 0.2389  1114 ASP B OD1 
22863 O OD2 . ASP C 1114 ? 2.0286 2.8579 1.8198 -0.0043 -0.4435 0.2615  1114 ASP B OD2 
22864 N N   . ASN C 1115 ? 1.7845 2.3713 1.6257 -0.1434 -0.4401 0.2498  1115 ASN B N   
22865 C CA  . ASN C 1115 ? 1.7190 2.2993 1.5852 -0.1759 -0.4399 0.2536  1115 ASN B CA  
22866 C C   . ASN C 1115 ? 1.6501 2.1369 1.4960 -0.1679 -0.4196 0.2385  1115 ASN B C   
22867 O O   . ASN C 1115 ? 1.5978 2.0709 1.4584 -0.1873 -0.4136 0.2382  1115 ASN B O   
22868 C CB  . ASN C 1115 ? 1.7386 2.3365 1.6334 -0.2197 -0.4664 0.2695  1115 ASN B CB  
22869 C CG  . ASN C 1115 ? 1.7726 2.2974 1.6513 -0.2254 -0.4754 0.2649  1115 ASN B CG  
22870 O OD1 . ASN C 1115 ? 1.7687 2.2930 1.6650 -0.2584 -0.4961 0.2749  1115 ASN B OD1 
22871 N ND2 . ASN C 1115 ? 1.7938 2.2558 1.6380 -0.1933 -0.4596 0.2498  1115 ASN B ND2 
22872 N N   . GLY C 1116 ? 1.6352 2.0616 1.4469 -0.1389 -0.4089 0.2268  1116 GLY B N   
22873 C CA  . GLY C 1116 ? 1.6117 1.9493 1.4016 -0.1313 -0.3900 0.2133  1116 GLY B CA  
22874 C C   . GLY C 1116 ? 1.5445 1.8210 1.3297 -0.1472 -0.3996 0.2132  1116 GLY B C   
22875 O O   . GLY C 1116 ? 1.5695 1.7737 1.3339 -0.1384 -0.3843 0.2024  1116 GLY B O   
22876 N N   . SER C 1117 ? 1.4960 1.8004 1.2996 -0.1712 -0.4244 0.2245  1117 SER B N   
22877 C CA  . SER C 1117 ? 1.4895 1.7348 1.2861 -0.1843 -0.4344 0.2224  1117 SER B CA  
22878 C C   . SER C 1117 ? 1.5325 1.7488 1.2955 -0.1562 -0.4336 0.2150  1117 SER B C   
22879 O O   . SER C 1117 ? 1.5662 1.8209 1.3173 -0.1310 -0.4309 0.2156  1117 SER B O   
22880 C CB  . SER C 1117 ? 1.4661 1.7433 1.2931 -0.2228 -0.4614 0.2362  1117 SER B CB  
22881 O OG  . SER C 1117 ? 1.4685 1.8037 1.2993 -0.2247 -0.4805 0.2441  1117 SER B OG  
22882 N N   . PHE C 1118 ? 1.5251 1.6761 1.2721 -0.1585 -0.4353 0.2083  1118 PHE B N   
22883 C CA  . PHE C 1118 ? 1.5194 1.6399 1.2326 -0.1315 -0.4329 0.2011  1118 PHE B CA  
22884 C C   . PHE C 1118 ? 1.5143 1.6474 1.2291 -0.1470 -0.4585 0.2043  1118 PHE B C   
22885 O O   . PHE C 1118 ? 1.5064 1.6198 1.2362 -0.1760 -0.4721 0.2055  1118 PHE B O   
22886 C CB  . PHE C 1118 ? 1.5451 1.5818 1.2329 -0.1182 -0.4127 0.1892  1118 PHE B CB  
22887 C CG  . PHE C 1118 ? 1.5614 1.5793 1.2308 -0.0909 -0.3860 0.1832  1118 PHE B CG  
22888 C CD1 . PHE C 1118 ? 1.5365 1.5875 1.2240 -0.0958 -0.3772 0.1853  1118 PHE B CD1 
22889 C CD2 . PHE C 1118 ? 1.5983 1.5643 1.2307 -0.0607 -0.3695 0.1755  1118 PHE B CD2 
22890 C CE1 . PHE C 1118 ? 1.5427 1.5719 1.2110 -0.0714 -0.3526 0.1777  1118 PHE B CE1 
22891 C CE2 . PHE C 1118 ? 1.6001 1.5424 1.2137 -0.0369 -0.3448 0.1700  1118 PHE B CE2 
22892 C CZ  . PHE C 1118 ? 1.5713 1.5436 1.2023 -0.0425 -0.3365 0.1701  1118 PHE B CZ  
22893 N N   . LYS C 1119 ? 1.5242 1.6904 1.2231 -0.1277 -0.4654 0.2056  1119 LYS B N   
22894 C CA  . LYS C 1119 ? 1.5264 1.7038 1.2235 -0.1430 -0.4896 0.2066  1119 LYS B CA  
22895 C C   . LYS C 1119 ? 1.5425 1.6518 1.2061 -0.1264 -0.4838 0.1946  1119 LYS B C   
22896 O O   . LYS C 1119 ? 1.5405 1.6193 1.1770 -0.0933 -0.4635 0.1893  1119 LYS B O   
22897 C CB  . LYS C 1119 ? 1.6584 1.9191 1.3589 -0.1364 -0.5044 0.2156  1119 LYS B CB  
22898 C CG  . LYS C 1119 ? 1.7617 2.0508 1.4421 -0.0924 -0.4871 0.2165  1119 LYS B CG  
22899 C CD  . LYS C 1119 ? 2.1255 2.4923 1.8030 -0.0828 -0.5041 0.2244  1119 LYS B CD  
22900 C CE  . LYS C 1119 ? 2.0921 2.5543 1.7962 -0.0858 -0.5100 0.2372  1119 LYS B CE  
22901 N NZ  . LYS C 1119 ? 2.0883 2.5765 1.7762 -0.0401 -0.4904 0.2382  1119 LYS B NZ  
22902 N N   . GLU C 1120 ? 1.5700 1.6536 1.2340 -0.1492 -0.5013 0.1902  1120 GLU B N   
22903 C CA  . GLU C 1120 ? 1.6458 1.6768 1.2761 -0.1321 -0.4982 0.1786  1120 GLU B CA  
22904 C C   . GLU C 1120 ? 1.6783 1.7590 1.2935 -0.1185 -0.5112 0.1809  1120 GLU B C   
22905 O O   . GLU C 1120 ? 1.6905 1.8366 1.3256 -0.1372 -0.5311 0.1893  1120 GLU B O   
22906 C CB  . GLU C 1120 ? 1.6541 1.6318 1.2867 -0.1577 -0.5096 0.1700  1120 GLU B CB  
22907 C CG  . GLU C 1120 ? 1.7031 1.6341 1.3006 -0.1429 -0.5103 0.1568  1120 GLU B CG  
22908 C CD  . GLU C 1120 ? 1.6973 1.5878 1.2626 -0.1051 -0.4838 0.1515  1120 GLU B CD  
22909 O OE1 . GLU C 1120 ? 1.6933 1.5227 1.2495 -0.1019 -0.4692 0.1441  1120 GLU B OE1 
22910 O OE2 . GLU C 1120 ? 1.6943 1.6147 1.2425 -0.0784 -0.4779 0.1558  1120 GLU B OE2 
22911 N N   . ASN C 1121 ? 1.7101 1.7634 1.2903 -0.0859 -0.4993 0.1748  1121 ASN B N   
22912 C CA  . ASN C 1121 ? 1.7423 1.8408 1.3037 -0.0669 -0.5088 0.1774  1121 ASN B CA  
22913 C C   . ASN C 1121 ? 1.8060 1.8990 1.3575 -0.0856 -0.5315 0.1692  1121 ASN B C   
22914 O O   . ASN C 1121 ? 1.8121 1.9619 1.3787 -0.1085 -0.5554 0.1733  1121 ASN B O   
22915 C CB  . ASN C 1121 ? 1.7317 1.8004 1.2582 -0.0221 -0.4849 0.1763  1121 ASN B CB  
22916 C CG  . ASN C 1121 ? 1.6987 1.8081 1.2017 0.0013  -0.4934 0.1794  1121 ASN B CG  
22917 O OD1 . ASN C 1121 ? 1.6897 1.8744 1.2043 0.0042  -0.5045 0.1891  1121 ASN B OD1 
22918 N ND2 . ASN C 1121 ? 1.6808 1.7452 1.1506 0.0191  -0.4876 0.1722  1121 ASN B ND2 
22919 N N   . SER C 1122 ? 1.8643 1.8899 1.3895 -0.0765 -0.5236 0.1571  1122 SER B N   
22920 C CA  . SER C 1122 ? 1.9037 1.9154 1.4144 -0.0910 -0.5426 0.1458  1122 SER B CA  
22921 C C   . SER C 1122 ? 1.9493 1.9520 1.4864 -0.1353 -0.5633 0.1416  1122 SER B C   
22922 O O   . SER C 1122 ? 1.9360 1.9446 1.5035 -0.1546 -0.5627 0.1491  1122 SER B O   
22923 C CB  . SER C 1122 ? 1.8980 1.8376 1.3760 -0.0707 -0.5269 0.1337  1122 SER B CB  
22924 O OG  . SER C 1122 ? 1.8660 1.7466 1.3556 -0.0893 -0.5218 0.1262  1122 SER B OG  
22925 N N   . GLN C 1123 ? 1.9951 1.9816 1.5192 -0.1512 -0.5816 0.1295  1123 GLN B N   
22926 C CA  . GLN C 1123 ? 2.0322 2.0045 1.5774 -0.1930 -0.6028 0.1248  1123 GLN B CA  
22927 C C   . GLN C 1123 ? 1.9606 1.8514 1.5062 -0.1986 -0.5922 0.1150  1123 GLN B C   
22928 O O   . GLN C 1123 ? 1.9654 1.8346 1.5299 -0.2306 -0.6066 0.1127  1123 GLN B O   
22929 C CB  . GLN C 1123 ? 2.1733 2.1648 1.7041 -0.2106 -0.6290 0.1146  1123 GLN B CB  
22930 C CG  . GLN C 1123 ? 2.2803 2.3609 1.8124 -0.2068 -0.6409 0.1253  1123 GLN B CG  
22931 C CD  . GLN C 1123 ? 2.4130 2.5251 1.9423 -0.2385 -0.6717 0.1180  1123 GLN B CD  
22932 O OE1 . GLN C 1123 ? 2.4529 2.5523 2.0013 -0.2786 -0.6902 0.1155  1123 GLN B OE1 
22933 N NE2 . GLN C 1123 ? 2.4723 2.6275 1.9775 -0.2213 -0.6775 0.1154  1123 GLN B NE2 
22934 N N   . TYR C 1124 ? 1.8728 1.7196 1.3981 -0.1676 -0.5671 0.1106  1124 TYR B N   
22935 C CA  . TYR C 1124 ? 1.7918 1.5653 1.3133 -0.1694 -0.5566 0.1002  1124 TYR B CA  
22936 C C   . TYR C 1124 ? 1.7361 1.5001 1.2934 -0.1971 -0.5602 0.1074  1124 TYR B C   
22937 O O   . TYR C 1124 ? 1.6952 1.4817 1.2732 -0.1950 -0.5483 0.1203  1124 TYR B O   
22938 C CB  . TYR C 1124 ? 1.7157 1.4557 1.2175 -0.1352 -0.5266 0.0998  1124 TYR B CB  
22939 C CG  . TYR C 1124 ? 1.6606 1.3314 1.1567 -0.1344 -0.5142 0.0894  1124 TYR B CG  
22940 C CD1 . TYR C 1124 ? 1.6698 1.2992 1.1363 -0.1249 -0.5149 0.0733  1124 TYR B CD1 
22941 C CD2 . TYR C 1124 ? 1.6054 1.2566 1.1250 -0.1419 -0.5013 0.0956  1124 TYR B CD2 
22942 C CE1 . TYR C 1124 ? 1.6454 1.2156 1.1064 -0.1217 -0.5026 0.0639  1124 TYR B CE1 
22943 C CE2 . TYR C 1124 ? 1.5750 1.1685 1.0900 -0.1397 -0.4894 0.0871  1124 TYR B CE2 
22944 C CZ  . TYR C 1124 ? 1.5712 1.1246 1.0572 -0.1289 -0.4898 0.0715  1124 TYR B CZ  
22945 O OH  . TYR C 1124 ? 1.4954 0.9971 0.9771 -0.1246 -0.4772 0.0635  1124 TYR B OH  
22946 N N   . GLN C 1125 ? 1.7474 1.4776 1.3107 -0.2227 -0.5770 0.0988  1125 GLN B N   
22947 C CA  . GLN C 1125 ? 1.7293 1.4388 1.3233 -0.2467 -0.5797 0.1054  1125 GLN B CA  
22948 C C   . GLN C 1125 ? 1.6345 1.2799 1.2184 -0.2301 -0.5594 0.0970  1125 GLN B C   
22949 O O   . GLN C 1125 ? 1.6209 1.2200 1.1815 -0.2238 -0.5614 0.0808  1125 GLN B O   
22950 C CB  . GLN C 1125 ? 1.8473 1.5456 1.4501 -0.2812 -0.6079 0.1005  1125 GLN B CB  
22951 C CG  . GLN C 1125 ? 1.9443 1.7104 1.5624 -0.3054 -0.6301 0.1111  1125 GLN B CG  
22952 C CD  . GLN C 1125 ? 1.9899 1.8026 1.6459 -0.3213 -0.6290 0.1330  1125 GLN B CD  
22953 O OE1 . GLN C 1125 ? 1.9770 1.7996 1.6406 -0.3016 -0.6071 0.1411  1125 GLN B OE1 
22954 N NE2 . GLN C 1125 ? 2.0233 1.8654 1.7026 -0.3586 -0.6530 0.1424  1125 GLN B NE2 
22955 N N   . PRO C 1126 ? 1.5963 1.2416 1.1972 -0.2234 -0.5399 0.1073  1126 PRO B N   
22956 C CA  . PRO C 1126 ? 1.5912 1.1820 1.1811 -0.2066 -0.5192 0.0997  1126 PRO B CA  
22957 C C   . PRO C 1126 ? 1.6419 1.1976 1.2526 -0.2280 -0.5274 0.0997  1126 PRO B C   
22958 O O   . PRO C 1126 ? 1.6889 1.1929 1.2840 -0.2215 -0.5258 0.0863  1126 PRO B O   
22959 C CB  . PRO C 1126 ? 1.5442 1.1564 1.1430 -0.1924 -0.4957 0.1111  1126 PRO B CB  
22960 C CG  . PRO C 1126 ? 1.5349 1.2138 1.1503 -0.2009 -0.5053 0.1242  1126 PRO B CG  
22961 C CD  . PRO C 1126 ? 1.5484 1.2440 1.1771 -0.2298 -0.5346 0.1250  1126 PRO B CD  
22962 N N   . ILE C 1127 ? 1.6402 1.2249 1.2854 -0.2516 -0.5356 0.1153  1127 ILE B N   
22963 C CA  . ILE C 1127 ? 1.6665 1.2224 1.3342 -0.2746 -0.5469 0.1191  1127 ILE B CA  
22964 C C   . ILE C 1127 ? 1.6940 1.2722 1.3771 -0.3066 -0.5759 0.1252  1127 ILE B C   
22965 O O   . ILE C 1127 ? 1.6756 1.3071 1.3617 -0.3140 -0.5854 0.1315  1127 ILE B O   
22966 C CB  . ILE C 1127 ? 1.7029 1.2679 1.4006 -0.2791 -0.5324 0.1346  1127 ILE B CB  
22967 C CG1 . ILE C 1127 ? 1.6651 1.2844 1.3711 -0.2709 -0.5179 0.1453  1127 ILE B CG1 
22968 C CG2 . ILE C 1127 ? 1.7072 1.2224 1.3956 -0.2610 -0.5131 0.1266  1127 ILE B CG2 
22969 C CD1 . ILE C 1127 ? 1.6757 1.3522 1.3863 -0.2812 -0.5335 0.1521  1127 ILE B CD1 
22970 N N   . LYS C 1128 ? 1.7419 1.2779 1.4335 -0.3251 -0.5896 0.1234  1128 LYS B N   
22971 C CA  . LYS C 1128 ? 1.7921 1.3444 1.5053 -0.3608 -0.6154 0.1341  1128 LYS B CA  
22972 C C   . LYS C 1128 ? 1.8406 1.4000 1.5888 -0.3741 -0.6108 0.1541  1128 LYS B C   
22973 O O   . LYS C 1128 ? 1.8624 1.3739 1.6127 -0.3662 -0.6017 0.1520  1128 LYS B O   
22974 C CB  . LYS C 1128 ? 1.8218 1.3130 1.5184 -0.3719 -0.6335 0.1181  1128 LYS B CB  
22975 C CG  . LYS C 1128 ? 1.8275 1.3114 1.5470 -0.4104 -0.6583 0.1297  1128 LYS B CG  
22976 C CD  . LYS C 1128 ? 1.8259 1.3543 1.5452 -0.4374 -0.6822 0.1317  1128 LYS B CD  
22977 C CE  . LYS C 1128 ? 1.7632 1.3773 1.5079 -0.4461 -0.6803 0.1535  1128 LYS B CE  
22978 N NZ  . LYS C 1128 ? 1.7650 1.4212 1.5216 -0.4837 -0.7075 0.1627  1128 LYS B NZ  
22979 N N   . LEU C 1129 ? 1.8658 1.4881 1.6410 -0.3924 -0.6161 0.1739  1129 LEU B N   
22980 C CA  . LEU C 1129 ? 1.8793 1.5138 1.6887 -0.4076 -0.6134 0.1946  1129 LEU B CA  
22981 C C   . LEU C 1129 ? 1.9762 1.6057 1.8056 -0.4456 -0.6403 0.2074  1129 LEU B C   
22982 O O   . LEU C 1129 ? 2.0258 1.6589 1.8457 -0.4630 -0.6607 0.2021  1129 LEU B O   
22983 C CB  . LEU C 1129 ? 1.7983 1.5047 1.6265 -0.4039 -0.6003 0.2094  1129 LEU B CB  
22984 C CG  . LEU C 1129 ? 1.7488 1.4705 1.5584 -0.3702 -0.5751 0.1997  1129 LEU B CG  
22985 C CD1 . LEU C 1129 ? 1.6924 1.4807 1.5242 -0.3716 -0.5649 0.2153  1129 LEU B CD1 
22986 C CD2 . LEU C 1129 ? 1.7403 1.4048 1.5344 -0.3461 -0.5545 0.1877  1129 LEU B CD2 
22987 N N   . GLN C 1130 ? 1.9767 1.5975 1.8329 -0.4594 -0.6408 0.2249  1130 GLN B N   
22988 C CA  . GLN C 1130 ? 2.0084 1.6248 1.8844 -0.4967 -0.6657 0.2405  1130 GLN B CA  
22989 C C   . GLN C 1130 ? 1.9075 1.6089 1.8096 -0.5199 -0.6736 0.2621  1130 GLN B C   
22990 O O   . GLN C 1130 ? 1.8251 1.5821 1.7343 -0.5050 -0.6572 0.2668  1130 GLN B O   
22991 C CB  . GLN C 1130 ? 2.1027 1.6753 1.9966 -0.5012 -0.6636 0.2529  1130 GLN B CB  
22992 C CG  . GLN C 1130 ? 2.1722 1.6868 2.0487 -0.4676 -0.6436 0.2369  1130 GLN B CG  
22993 C CD  . GLN C 1130 ? 2.2411 1.7078 2.1335 -0.4730 -0.6461 0.2490  1130 GLN B CD  
22994 O OE1 . GLN C 1130 ? 2.2970 1.7425 2.2010 -0.5010 -0.6674 0.2611  1130 GLN B OE1 
22995 N NE2 . GLN C 1130 ? 2.2251 1.6754 2.1181 -0.4467 -0.6244 0.2470  1130 GLN B NE2 
22996 N N   . GLY C 1131 ? 1.9159 1.6274 1.8314 -0.5567 -0.6987 0.2749  1131 GLY B N   
22997 C CA  . GLY C 1131 ? 1.9127 1.7090 1.8547 -0.5814 -0.7075 0.2975  1131 GLY B CA  
22998 C C   . GLY C 1131 ? 1.9601 1.7811 1.9000 -0.6139 -0.7341 0.2994  1131 GLY B C   
22999 O O   . GLY C 1131 ? 2.0455 1.8170 1.9608 -0.6177 -0.7466 0.2809  1131 GLY B O   
23000 N N   . THR C 1132 ? 1.9319 1.8336 1.8979 -0.6386 -0.7431 0.3219  1132 THR B N   
23001 C CA  . THR C 1132 ? 1.9272 1.8714 1.8945 -0.6711 -0.7675 0.3266  1132 THR B CA  
23002 C C   . THR C 1132 ? 1.8767 1.8734 1.8250 -0.6469 -0.7602 0.3112  1132 THR B C   
23003 O O   . THR C 1132 ? 1.8285 1.8404 1.7704 -0.6105 -0.7367 0.3042  1132 THR B O   
23004 C CB  . THR C 1132 ? 1.9261 1.9454 1.9301 -0.7053 -0.7782 0.3588  1132 THR B CB  
23005 O OG1 . THR C 1132 ? 1.9156 1.9171 1.9418 -0.7047 -0.7678 0.3763  1132 THR B OG1 
23006 C CG2 . THR C 1132 ? 1.9970 2.0126 2.0059 -0.7536 -0.8092 0.3684  1132 THR B CG2 
23007 N N   . LEU C 1133 ? 1.9134 1.9393 1.8522 -0.6665 -0.7798 0.3066  1133 LEU B N   
23008 C CA  . LEU C 1133 ? 1.9381 2.0154 1.8584 -0.6397 -0.7720 0.2934  1133 LEU B CA  
23009 C C   . LEU C 1133 ? 1.9335 2.0874 1.8691 -0.6154 -0.7518 0.3049  1133 LEU B C   
23010 O O   . LEU C 1133 ? 1.9658 2.1288 1.8818 -0.5772 -0.7339 0.2908  1133 LEU B O   
23011 C CB  . LEU C 1133 ? 1.9501 2.0708 1.8640 -0.6678 -0.7971 0.2919  1133 LEU B CB  
23012 C CG  . LEU C 1133 ? 1.9666 2.0125 1.8457 -0.6655 -0.8065 0.2649  1133 LEU B CG  
23013 C CD1 . LEU C 1133 ? 2.0050 1.9656 1.8866 -0.6960 -0.8213 0.2650  1133 LEU B CD1 
23014 C CD2 . LEU C 1133 ? 1.9633 2.0640 1.8283 -0.6789 -0.8249 0.2576  1133 LEU B CD2 
23015 N N   . PRO C 1134 ? 1.9172 2.1250 1.8865 -0.6373 -0.7544 0.3304  1134 PRO B N   
23016 C CA  . PRO C 1134 ? 1.8830 2.1617 1.8693 -0.6173 -0.7354 0.3420  1134 PRO B CA  
23017 C C   . PRO C 1134 ? 1.8999 2.1302 1.8839 -0.5868 -0.7092 0.3358  1134 PRO B C   
23018 O O   . PRO C 1134 ? 1.8672 2.1115 1.8382 -0.5497 -0.6874 0.3249  1134 PRO B O   
23019 C CB  . PRO C 1134 ? 1.8698 2.2076 1.8928 -0.6582 -0.7506 0.3716  1134 PRO B CB  
23020 C CG  . PRO C 1134 ? 1.9163 2.2360 1.9383 -0.6989 -0.7793 0.3748  1134 PRO B CG  
23021 C CD  . PRO C 1134 ? 1.9429 2.1569 1.9352 -0.6870 -0.7792 0.3506  1134 PRO B CD  
23022 N N   . VAL C 1135 ? 1.9344 2.1100 1.9312 -0.6033 -0.7116 0.3441  1135 VAL B N   
23023 C CA  . VAL C 1135 ? 1.9005 2.0248 1.8950 -0.5783 -0.6891 0.3383  1135 VAL B CA  
23024 C C   . VAL C 1135 ? 1.8899 1.9696 1.8500 -0.5378 -0.6710 0.3112  1135 VAL B C   
23025 O O   . VAL C 1135 ? 1.8537 1.9523 1.8085 -0.5081 -0.6484 0.3056  1135 VAL B O   
23026 C CB  . VAL C 1135 ? 1.9218 1.9697 1.9223 -0.5973 -0.6984 0.3432  1135 VAL B CB  
23027 C CG1 . VAL C 1135 ? 1.9099 1.8891 1.8948 -0.5649 -0.6764 0.3276  1135 VAL B CG1 
23028 C CG2 . VAL C 1135 ? 1.9183 2.0034 1.9552 -0.6300 -0.7079 0.3735  1135 VAL B CG2 
23029 N N   . GLU C 1136 ? 1.9180 1.9384 1.8536 -0.5378 -0.6814 0.2943  1136 GLU B N   
23030 C CA  . GLU C 1136 ? 1.9085 1.8859 1.8095 -0.5016 -0.6665 0.2693  1136 GLU B CA  
23031 C C   . GLU C 1136 ? 1.8993 1.9350 1.7923 -0.4726 -0.6493 0.2659  1136 GLU B C   
23032 O O   . GLU C 1136 ? 1.8933 1.9133 1.7784 -0.4436 -0.6252 0.2592  1136 GLU B O   
23033 C CB  . GLU C 1136 ? 1.9245 1.8652 1.8010 -0.5100 -0.6850 0.2534  1136 GLU B CB  
23034 C CG  . GLU C 1136 ? 1.9199 1.8261 1.7601 -0.4730 -0.6705 0.2292  1136 GLU B CG  
23035 C CD  . GLU C 1136 ? 1.9612 1.7959 1.7767 -0.4778 -0.6831 0.2105  1136 GLU B CD  
23036 O OE1 . GLU C 1136 ? 1.9701 1.7979 1.7932 -0.5123 -0.7076 0.2148  1136 GLU B OE1 
23037 O OE2 . GLU C 1136 ? 1.9794 1.7651 1.7672 -0.4478 -0.6685 0.1914  1136 GLU B OE2 
23038 N N   . ALA C 1137 ? 1.8975 2.0008 1.7923 -0.4805 -0.6615 0.2709  1137 ALA B N   
23039 C CA  . ALA C 1137 ? 1.8876 2.0455 1.7726 -0.4499 -0.6459 0.2677  1137 ALA B CA  
23040 C C   . ALA C 1137 ? 1.8490 2.0298 1.7497 -0.4350 -0.6235 0.2757  1137 ALA B C   
23041 O O   . ALA C 1137 ? 1.8260 2.0019 1.7095 -0.4004 -0.6011 0.2655  1137 ALA B O   
23042 C CB  . ALA C 1137 ? 1.8949 2.1366 1.7880 -0.4648 -0.6637 0.2775  1137 ALA B CB  
23043 N N   . ARG C 1138 ? 1.8351 2.0398 1.7675 -0.4621 -0.6297 0.2942  1138 ARG B N   
23044 C CA  . ARG C 1138 ? 1.8137 2.0373 1.7612 -0.4515 -0.6096 0.3010  1138 ARG B CA  
23045 C C   . ARG C 1138 ? 1.7567 1.9017 1.6848 -0.4268 -0.5890 0.2849  1138 ARG B C   
23046 O O   . ARG C 1138 ? 1.7320 1.8726 1.6421 -0.3952 -0.5675 0.2732  1138 ARG B O   
23047 C CB  . ARG C 1138 ? 1.8610 2.1148 1.8449 -0.4873 -0.6217 0.3244  1138 ARG B CB  
23048 C CG  . ARG C 1138 ? 1.8825 2.1683 1.8845 -0.4802 -0.6030 0.3329  1138 ARG B CG  
23049 C CD  . ARG C 1138 ? 1.9132 2.2737 1.9508 -0.5122 -0.6162 0.3588  1138 ARG B CD  
23050 N NE  . ARG C 1138 ? 1.9322 2.3340 1.9835 -0.5015 -0.5970 0.3639  1138 ARG B NE  
23051 C CZ  . ARG C 1138 ? 1.9456 2.4272 2.0247 -0.5194 -0.6013 0.3835  1138 ARG B CZ  
23052 N NH1 . ARG C 1138 ? 1.9623 2.4936 2.0600 -0.5507 -0.6245 0.4022  1138 ARG B NH1 
23053 N NH2 . ARG C 1138 ? 1.9294 2.4429 2.0169 -0.5073 -0.5825 0.3843  1138 ARG B NH2 
23054 N N   . GLU C 1139 ? 1.7324 1.8147 1.6630 -0.4413 -0.5960 0.2846  1139 GLU B N   
23055 C CA  . GLU C 1139 ? 1.6948 1.7035 1.6088 -0.4210 -0.5789 0.2706  1139 GLU B CA  
23056 C C   . GLU C 1139 ? 1.6927 1.6754 1.5714 -0.3865 -0.5638 0.2497  1139 GLU B C   
23057 O O   . GLU C 1139 ? 1.6881 1.6573 1.5557 -0.3618 -0.5402 0.2418  1139 GLU B O   
23058 C CB  . GLU C 1139 ? 1.6815 1.6249 1.5931 -0.4378 -0.5946 0.2683  1139 GLU B CB  
23059 C CG  . GLU C 1139 ? 1.6496 1.5856 1.5903 -0.4631 -0.6020 0.2864  1139 GLU B CG  
23060 C CD  . GLU C 1139 ? 1.6125 1.5235 1.5575 -0.4469 -0.5800 0.2857  1139 GLU B CD  
23061 O OE1 . GLU C 1139 ? 1.6382 1.4873 1.5798 -0.4459 -0.5800 0.2821  1139 GLU B OE1 
23062 O OE2 . GLU C 1139 ? 1.5605 1.5149 1.5116 -0.4350 -0.5627 0.2881  1139 GLU B OE2 
23063 N N   . ASN C 1140 ? 1.7249 1.6989 1.5850 -0.3868 -0.5782 0.2411  1140 ASN B N   
23064 C CA  . ASN C 1140 ? 1.7352 1.6832 1.5602 -0.3559 -0.5673 0.2227  1140 ASN B CA  
23065 C C   . ASN C 1140 ? 1.6513 1.6363 1.4699 -0.3288 -0.5456 0.2221  1140 ASN B C   
23066 O O   . ASN C 1140 ? 1.6406 1.5881 1.4360 -0.3010 -0.5248 0.2099  1140 ASN B O   
23067 C CB  . ASN C 1140 ? 1.8310 1.7969 1.6436 -0.3643 -0.5887 0.2187  1140 ASN B CB  
23068 C CG  . ASN C 1140 ? 1.9437 1.8715 1.7186 -0.3360 -0.5812 0.1995  1140 ASN B CG  
23069 O OD1 . ASN C 1140 ? 2.0065 1.9534 1.7672 -0.3372 -0.5955 0.1946  1140 ASN B OD1 
23070 N ND2 . ASN C 1140 ? 1.9604 1.8371 1.7184 -0.3110 -0.5587 0.1891  1140 ASN B ND2 
23071 N N   . SER C 1141 ? 1.5954 1.6536 1.4343 -0.3377 -0.5502 0.2356  1141 SER B N   
23072 C CA  . SER C 1141 ? 1.5369 1.6336 1.3705 -0.3120 -0.5306 0.2351  1141 SER B CA  
23073 C C   . SER C 1141 ? 1.4654 1.5299 1.2998 -0.3003 -0.5060 0.2313  1141 SER B C   
23074 O O   . SER C 1141 ? 1.4411 1.4808 1.2514 -0.2711 -0.4851 0.2199  1141 SER B O   
23075 C CB  . SER C 1141 ? 1.5406 1.7259 1.3994 -0.3259 -0.5409 0.2510  1141 SER B CB  
23076 O OG  . SER C 1141 ? 1.5407 1.7620 1.3904 -0.2971 -0.5223 0.2482  1141 SER B OG  
23077 N N   . LEU C 1142 ? 1.4119 1.4783 1.2737 -0.3239 -0.5089 0.2418  1142 LEU B N   
23078 C CA  . LEU C 1142 ? 1.3512 1.3897 1.2154 -0.3166 -0.4874 0.2387  1142 LEU B CA  
23079 C C   . LEU C 1142 ? 1.3593 1.3263 1.1913 -0.2937 -0.4741 0.2214  1142 LEU B C   
23080 O O   . LEU C 1142 ? 1.3462 1.2991 1.1580 -0.2688 -0.4523 0.2116  1142 LEU B O   
23081 C CB  . LEU C 1142 ? 1.2961 1.3275 1.1894 -0.3450 -0.4960 0.2514  1142 LEU B CB  
23082 C CG  . LEU C 1142 ? 1.2073 1.2750 1.1259 -0.3546 -0.4853 0.2621  1142 LEU B CG  
23083 C CD1 . LEU C 1142 ? 1.1852 1.2579 1.1346 -0.3857 -0.5015 0.2800  1142 LEU B CD1 
23084 C CD2 . LEU C 1142 ? 1.1629 1.1963 1.0677 -0.3351 -0.4588 0.2501  1142 LEU B CD2 
23085 N N   . TYR C 1143 ? 1.3725 1.2946 1.1981 -0.3021 -0.4877 0.2175  1143 TYR B N   
23086 C CA  . TYR C 1143 ? 1.3710 1.2241 1.1689 -0.2832 -0.4757 0.2020  1143 TYR B CA  
23087 C C   . TYR C 1143 ? 1.3537 1.1981 1.1190 -0.2517 -0.4588 0.1901  1143 TYR B C   
23088 O O   . TYR C 1143 ? 1.3296 1.1357 1.0779 -0.2342 -0.4376 0.1814  1143 TYR B O   
23089 C CB  . TYR C 1143 ? 1.3729 1.1824 1.1632 -0.2930 -0.4940 0.1966  1143 TYR B CB  
23090 C CG  . TYR C 1143 ? 1.3799 1.1276 1.1372 -0.2690 -0.4807 0.1793  1143 TYR B CG  
23091 C CD1 . TYR C 1143 ? 1.3757 1.0770 1.1330 -0.2663 -0.4692 0.1753  1143 TYR B CD1 
23092 C CD2 . TYR C 1143 ? 1.4003 1.1412 1.1264 -0.2481 -0.4790 0.1683  1143 TYR B CD2 
23093 C CE1 . TYR C 1143 ? 1.3988 1.0493 1.1263 -0.2446 -0.4565 0.1603  1143 TYR B CE1 
23094 C CE2 . TYR C 1143 ? 1.4054 1.0934 1.1010 -0.2266 -0.4666 0.1538  1143 TYR B CE2 
23095 C CZ  . TYR C 1143 ? 1.4114 1.0549 1.1080 -0.2254 -0.4553 0.1498  1143 TYR B CZ  
23096 O OH  . TYR C 1143 ? 1.4177 1.0139 1.0845 -0.2046 -0.4426 0.1363  1143 TYR B OH  
23097 N N   . LEU C 1144 ? 1.3571 1.2388 1.1139 -0.2447 -0.4681 0.1910  1144 LEU B N   
23098 C CA  . LEU C 1144 ? 1.3687 1.2461 1.0954 -0.2130 -0.4522 0.1826  1144 LEU B CA  
23099 C C   . LEU C 1144 ? 1.3648 1.2586 1.0944 -0.2009 -0.4298 0.1842  1144 LEU B C   
23100 O O   . LEU C 1144 ? 1.3855 1.2377 1.0947 -0.1826 -0.4081 0.1756  1144 LEU B O   
23101 C CB  . LEU C 1144 ? 1.3537 1.2753 1.0726 -0.2071 -0.4674 0.1850  1144 LEU B CB  
23102 C CG  . LEU C 1144 ? 1.3409 1.2465 1.0233 -0.1723 -0.4541 0.1762  1144 LEU B CG  
23103 C CD1 . LEU C 1144 ? 1.3613 1.2125 1.0194 -0.1677 -0.4586 0.1651  1144 LEU B CD1 
23104 C CD2 . LEU C 1144 ? 1.3282 1.2979 1.0092 -0.1627 -0.4642 0.1825  1144 LEU B CD2 
23105 N N   . THR C 1145 ? 1.3364 1.2911 1.0909 -0.2123 -0.4351 0.1948  1145 THR B N   
23106 C CA  . THR C 1145 ? 1.3231 1.2975 1.0788 -0.2003 -0.4148 0.1944  1145 THR B CA  
23107 C C   . THR C 1145 ? 1.3186 1.2458 1.0731 -0.2024 -0.3953 0.1884  1145 THR B C   
23108 O O   . THR C 1145 ? 1.3234 1.2265 1.0573 -0.1825 -0.3731 0.1799  1145 THR B O   
23109 C CB  . THR C 1145 ? 1.3517 1.4040 1.1380 -0.2159 -0.4248 0.2072  1145 THR B CB  
23110 O OG1 . THR C 1145 ? 1.3389 1.4365 1.1254 -0.2147 -0.4431 0.2128  1145 THR B OG1 
23111 C CG2 . THR C 1145 ? 1.3530 1.4265 1.1346 -0.1984 -0.4037 0.2035  1145 THR B CG2 
23112 N N   . ALA C 1146 ? 1.3138 1.2256 1.0885 -0.2257 -0.4032 0.1930  1146 ALA B N   
23113 C CA  . ALA C 1146 ? 1.3461 1.2173 1.1190 -0.2267 -0.3852 0.1877  1146 ALA B CA  
23114 C C   . ALA C 1146 ? 1.3907 1.2011 1.1274 -0.2032 -0.3691 0.1742  1146 ALA B C   
23115 O O   . ALA C 1146 ? 1.3737 1.1639 1.0952 -0.1908 -0.3468 0.1673  1146 ALA B O   
23116 C CB  . ALA C 1146 ? 1.3527 1.2148 1.1504 -0.2513 -0.3976 0.1955  1146 ALA B CB  
23117 N N   . PHE C 1147 ? 1.4241 1.2067 1.1467 -0.1987 -0.3812 0.1707  1147 PHE B N   
23118 C CA  . PHE C 1147 ? 1.4326 1.1612 1.1205 -0.1772 -0.3699 0.1593  1147 PHE B CA  
23119 C C   . PHE C 1147 ? 1.4343 1.1597 1.0947 -0.1510 -0.3521 0.1544  1147 PHE B C   
23120 O O   . PHE C 1147 ? 1.4473 1.1346 1.0876 -0.1386 -0.3305 0.1479  1147 PHE B O   
23121 C CB  . PHE C 1147 ? 1.4488 1.1669 1.1271 -0.1768 -0.3904 0.1569  1147 PHE B CB  
23122 C CG  . PHE C 1147 ? 1.4513 1.1146 1.0965 -0.1583 -0.3818 0.1455  1147 PHE B CG  
23123 C CD1 . PHE C 1147 ? 1.4304 1.0636 1.0739 -0.1659 -0.3944 0.1405  1147 PHE B CD1 
23124 C CD2 . PHE C 1147 ? 1.4743 1.1163 1.0896 -0.1335 -0.3614 0.1401  1147 PHE B CD2 
23125 C CE1 . PHE C 1147 ? 1.4415 1.0303 1.0554 -0.1491 -0.3867 0.1299  1147 PHE B CE1 
23126 C CE2 . PHE C 1147 ? 1.4882 1.0850 1.0742 -0.1180 -0.3539 0.1316  1147 PHE B CE2 
23127 C CZ  . PHE C 1147 ? 1.4742 1.0472 1.0599 -0.1257 -0.3666 0.1262  1147 PHE B CZ  
23128 N N   . THR C 1148 ? 1.4246 1.1894 1.0829 -0.1422 -0.3615 0.1582  1148 THR B N   
23129 C CA  . THR C 1148 ? 1.4558 1.2183 1.0875 -0.1142 -0.3457 0.1550  1148 THR B CA  
23130 C C   . THR C 1148 ? 1.3795 1.1436 1.0146 -0.1124 -0.3242 0.1533  1148 THR B C   
23131 O O   . THR C 1148 ? 1.3933 1.1314 1.0015 -0.0901 -0.3047 0.1479  1148 THR B O   
23132 C CB  . THR C 1148 ? 1.3725 1.1812 1.0002 -0.1021 -0.3612 0.1600  1148 THR B CB  
23133 O OG1 . THR C 1148 ? 1.3975 1.2282 1.0154 -0.0808 -0.3476 0.1608  1148 THR B OG1 
23134 C CG2 . THR C 1148 ? 1.3367 1.1992 0.9978 -0.1284 -0.3866 0.1689  1148 THR B CG2 
23135 N N   . VAL C 1149 ? 1.3320 1.1230 0.9982 -0.1365 -0.3271 0.1575  1149 VAL B N   
23136 C CA  . VAL C 1149 ? 1.3138 1.1012 0.9803 -0.1367 -0.3060 0.1533  1149 VAL B CA  
23137 C C   . VAL C 1149 ? 1.2989 1.0231 0.9449 -0.1337 -0.2872 0.1451  1149 VAL B C   
23138 O O   . VAL C 1149 ? 1.3070 0.9972 0.9239 -0.1146 -0.2680 0.1383  1149 VAL B O   
23139 C CB  . VAL C 1149 ? 1.0826 0.9218 0.7871 -0.1625 -0.3127 0.1603  1149 VAL B CB  
23140 C CG1 . VAL C 1149 ? 1.0877 0.9094 0.7937 -0.1709 -0.2921 0.1544  1149 VAL B CG1 
23141 C CG2 . VAL C 1149 ? 1.0279 0.9299 0.7431 -0.1574 -0.3200 0.1655  1149 VAL B CG2 
23142 N N   . ILE C 1150 ? 1.2573 0.9659 0.9175 -0.1515 -0.2933 0.1467  1150 ILE B N   
23143 C CA  . ILE C 1150 ? 1.2140 0.8708 0.8584 -0.1507 -0.2775 0.1403  1150 ILE B CA  
23144 C C   . ILE C 1150 ? 1.2347 0.8468 0.8391 -0.1252 -0.2636 0.1337  1150 ILE B C   
23145 O O   . ILE C 1150 ? 1.2666 0.8413 0.8529 -0.1217 -0.2434 0.1283  1150 ILE B O   
23146 C CB  . ILE C 1150 ? 1.1743 0.8174 0.8304 -0.1622 -0.2917 0.1427  1150 ILE B CB  
23147 C CG1 . ILE C 1150 ? 1.1731 0.8629 0.8645 -0.1822 -0.3149 0.1526  1150 ILE B CG1 
23148 C CG2 . ILE C 1150 ? 1.1116 0.7225 0.7663 -0.1693 -0.2765 0.1390  1150 ILE B CG2 
23149 C CD1 . ILE C 1150 ? 1.1798 0.8610 0.8922 -0.1999 -0.3251 0.1568  1150 ILE B CD1 
23150 N N   . GLY C 1151 ? 1.2432 0.8611 0.8338 -0.1085 -0.2749 0.1352  1151 GLY B N   
23151 C CA  . GLY C 1151 ? 1.2848 0.8648 0.8369 -0.0820 -0.2628 0.1314  1151 GLY B CA  
23152 C C   . GLY C 1151 ? 1.3395 0.9132 0.8742 -0.0666 -0.2435 0.1293  1151 GLY B C   
23153 O O   . GLY C 1151 ? 1.3566 0.8844 0.8662 -0.0585 -0.2223 0.1248  1151 GLY B O   
23154 N N   . ILE C 1152 ? 1.3381 0.9571 0.8850 -0.0625 -0.2505 0.1324  1152 ILE B N   
23155 C CA  . ILE C 1152 ? 1.3798 0.9936 0.9091 -0.0445 -0.2332 0.1292  1152 ILE B CA  
23156 C C   . ILE C 1152 ? 1.4297 1.0209 0.9617 -0.0601 -0.2141 0.1226  1152 ILE B C   
23157 O O   . ILE C 1152 ? 1.4644 1.0119 0.9687 -0.0484 -0.1929 0.1168  1152 ILE B O   
23158 C CB  . ILE C 1152 ? 1.3101 0.9867 0.8588 -0.0415 -0.2449 0.1333  1152 ILE B CB  
23159 C CG1 . ILE C 1152 ? 1.2375 0.9458 0.7877 -0.0314 -0.2667 0.1407  1152 ILE B CG1 
23160 C CG2 . ILE C 1152 ? 0.9414 0.6087 0.4699 -0.0203 -0.2251 0.1278  1152 ILE B CG2 
23161 C CD1 . ILE C 1152 ? 1.1619 0.9432 0.7411 -0.0395 -0.2852 0.1475  1152 ILE B CD1 
23162 N N   . ARG C 1153 ? 1.4202 1.0429 0.9861 -0.0878 -0.2228 0.1241  1153 ARG B N   
23163 C CA  . ARG C 1153 ? 1.4410 1.0509 1.0152 -0.1080 -0.2085 0.1190  1153 ARG B CA  
23164 C C   . ARG C 1153 ? 1.4347 0.9839 0.9830 -0.1056 -0.1921 0.1146  1153 ARG B C   
23165 O O   . ARG C 1153 ? 1.4817 1.0010 1.0133 -0.1067 -0.1715 0.1078  1153 ARG B O   
23166 C CB  . ARG C 1153 ? 1.4826 1.1328 1.0965 -0.1358 -0.2243 0.1250  1153 ARG B CB  
23167 C CG  . ARG C 1153 ? 1.5372 1.2511 1.1803 -0.1463 -0.2351 0.1294  1153 ARG B CG  
23168 C CD  . ARG C 1153 ? 1.5978 1.3149 1.2337 -0.1459 -0.2158 0.1205  1153 ARG B CD  
23169 N NE  . ARG C 1153 ? 1.5858 1.3661 1.2527 -0.1617 -0.2235 0.1239  1153 ARG B NE  
23170 C CZ  . ARG C 1153 ? 1.5997 1.3968 1.2615 -0.1576 -0.2112 0.1158  1153 ARG B CZ  
23171 N NH1 . ARG C 1153 ? 1.6224 1.3728 1.2491 -0.1383 -0.1912 0.1042  1153 ARG B NH1 
23172 N NH2 . ARG C 1153 ? 1.5936 1.4527 1.2839 -0.1723 -0.2188 0.1194  1153 ARG B NH2 
23173 N N   . LYS C 1154 ? 1.3994 0.9310 0.9435 -0.1032 -0.2010 0.1180  1154 LYS B N   
23174 C CA  . LYS C 1154 ? 1.4158 0.8986 0.9403 -0.1046 -0.1866 0.1150  1154 LYS B CA  
23175 C C   . LYS C 1154 ? 1.4876 0.9223 0.9719 -0.0846 -0.1662 0.1115  1154 LYS B C   
23176 O O   . LYS C 1154 ? 1.4987 0.8953 0.9667 -0.0905 -0.1480 0.1082  1154 LYS B O   
23177 C CB  . LYS C 1154 ? 1.3962 0.8712 0.9208 -0.1017 -0.2009 0.1181  1154 LYS B CB  
23178 C CG  . LYS C 1154 ? 1.3694 0.8627 0.9249 -0.1242 -0.2112 0.1199  1154 LYS B CG  
23179 C CD  . LYS C 1154 ? 1.3848 0.8491 0.9336 -0.1337 -0.1934 0.1167  1154 LYS B CD  
23180 C CE  . LYS C 1154 ? 1.3615 0.8432 0.9392 -0.1506 -0.2049 0.1196  1154 LYS B CE  
23181 N NZ  . LYS C 1154 ? 1.3811 0.8299 0.9436 -0.1484 -0.1937 0.1168  1154 LYS B NZ  
23182 N N   . ALA C 1155 ? 1.5498 0.9880 1.0184 -0.0609 -0.1697 0.1135  1155 ALA B N   
23183 C CA  . ALA C 1155 ? 1.6347 1.0259 1.0625 -0.0357 -0.1541 0.1135  1155 ALA B CA  
23184 C C   . ALA C 1155 ? 1.7390 1.1278 1.1555 -0.0234 -0.1424 0.1099  1155 ALA B C   
23185 O O   . ALA C 1155 ? 1.8043 1.1483 1.1859 -0.0028 -0.1268 0.1099  1155 ALA B O   
23186 C CB  . ALA C 1155 ? 1.6213 1.0159 1.0353 -0.0127 -0.1678 0.1197  1155 ALA B CB  
23187 N N   . PHE C 1156 ? 1.7611 1.1976 1.2060 -0.0350 -0.1500 0.1072  1156 PHE B N   
23188 C CA  . PHE C 1156 ? 1.8110 1.2556 1.2478 -0.0205 -0.1418 0.1027  1156 PHE B CA  
23189 C C   . PHE C 1156 ? 1.8408 1.2234 1.2440 -0.0149 -0.1154 0.0952  1156 PHE B C   
23190 O O   . PHE C 1156 ? 1.8686 1.2324 1.2480 0.0094  -0.1055 0.0927  1156 PHE B O   
23191 C CB  . PHE C 1156 ? 1.8033 1.3072 1.2767 -0.0409 -0.1504 0.0995  1156 PHE B CB  
23192 C CG  . PHE C 1156 ? 1.8455 1.3526 1.3094 -0.0308 -0.1373 0.0908  1156 PHE B CG  
23193 C CD1 . PHE C 1156 ? 1.8575 1.3959 1.3181 -0.0048 -0.1438 0.0930  1156 PHE B CD1 
23194 C CD2 . PHE C 1156 ? 1.8631 1.3442 1.3209 -0.0474 -0.1187 0.0796  1156 PHE B CD2 
23195 C CE1 . PHE C 1156 ? 1.8822 1.4227 1.3325 0.0073  -0.1313 0.0837  1156 PHE B CE1 
23196 C CE2 . PHE C 1156 ? 1.8893 1.3701 1.3361 -0.0380 -0.1067 0.0692  1156 PHE B CE2 
23197 C CZ  . PHE C 1156 ? 1.9016 1.4111 1.3443 -0.0094 -0.1127 0.0709  1156 PHE B CZ  
23198 N N   . ASP C 1157 ? 1.8189 1.1689 1.2191 -0.0371 -0.1040 0.0920  1157 ASP B N   
23199 C CA  . ASP C 1157 ? 1.8677 1.1631 1.2404 -0.0410 -0.0794 0.0838  1157 ASP B CA  
23200 C C   . ASP C 1157 ? 1.9166 1.1467 1.2432 -0.0126 -0.0640 0.0868  1157 ASP B C   
23201 O O   . ASP C 1157 ? 1.9476 1.1318 1.2495 -0.0123 -0.0442 0.0794  1157 ASP B O   
23202 C CB  . ASP C 1157 ? 1.9119 1.1976 1.2954 -0.0748 -0.0713 0.0802  1157 ASP B CB  
23203 C CG  . ASP C 1157 ? 1.9651 1.2850 1.3734 -0.1007 -0.0687 0.0703  1157 ASP B CG  
23204 O OD1 . ASP C 1157 ? 2.0018 1.3350 1.4083 -0.0908 -0.0669 0.0636  1157 ASP B OD1 
23205 O OD2 . ASP C 1157 ? 1.9631 1.2990 1.3919 -0.1296 -0.0683 0.0692  1157 ASP B OD2 
23206 N N   . ILE C 1158 ? 1.9060 1.1308 1.2197 0.0105  -0.0727 0.0976  1158 ILE B N   
23207 C CA  . ILE C 1158 ? 1.9018 1.0671 1.1717 0.0387  -0.0586 0.1032  1158 ILE B CA  
23208 C C   . ILE C 1158 ? 1.9428 1.1205 1.2024 0.0722  -0.0620 0.1050  1158 ILE B C   
23209 O O   . ILE C 1158 ? 2.0268 1.1605 1.2507 0.1012  -0.0515 0.1109  1158 ILE B O   
23210 C CB  . ILE C 1158 ? 1.7947 0.9517 1.0530 0.0506  -0.0661 0.1147  1158 ILE B CB  
23211 C CG1 . ILE C 1158 ? 1.6928 0.8909 0.9848 0.0249  -0.0821 0.1145  1158 ILE B CG1 
23212 C CG2 . ILE C 1158 ? 1.8339 0.9176 1.0505 0.0576  -0.0444 0.1193  1158 ILE B CG2 
23213 C CD1 . ILE C 1158 ? 1.6562 0.8712 0.9469 0.0392  -0.0984 0.1229  1158 ILE B CD1 
23214 N N   . CYS C 1159 ? 1.9067 1.1484 1.1982 0.0691  -0.0773 0.1014  1159 CYS B N   
23215 C CA  . CYS C 1159 ? 1.9252 1.1910 1.2108 0.1007  -0.0815 0.1029  1159 CYS B CA  
23216 C C   . CYS C 1159 ? 1.9743 1.2972 1.2913 0.0884  -0.0883 0.0937  1159 CYS B C   
23217 O O   . CYS C 1159 ? 1.9637 1.3460 1.2982 0.1026  -0.1043 0.0980  1159 CYS B O   
23218 C CB  . CYS C 1159 ? 1.8788 1.1811 1.1674 0.1225  -0.1009 0.1157  1159 CYS B CB  
23219 S SG  . CYS C 1159 ? 2.6734 1.9829 1.9367 0.1731  -0.0998 0.1224  1159 CYS B SG  
23220 N N   . PRO C 1160 ? 1.9943 1.3040 1.3186 0.0613  -0.0764 0.0815  1160 PRO B N   
23221 C CA  . PRO C 1160 ? 1.9896 1.3526 1.3379 0.0552  -0.0807 0.0726  1160 PRO B CA  
23222 C C   . PRO C 1160 ? 1.9720 1.3409 1.3013 0.0956  -0.0785 0.0729  1160 PRO B C   
23223 O O   . PRO C 1160 ? 2.0093 1.3154 1.3000 0.1193  -0.0602 0.0696  1160 PRO B O   
23224 C CB  . PRO C 1160 ? 2.0250 1.3489 1.3651 0.0307  -0.0610 0.0578  1160 PRO B CB  
23225 C CG  . PRO C 1160 ? 2.0832 1.3249 1.3870 0.0324  -0.0439 0.0599  1160 PRO B CG  
23226 C CD  . PRO C 1160 ? 2.0523 1.3054 1.3629 0.0363  -0.0585 0.0749  1160 PRO B CD  
23227 N N   . LEU C 1161 ? 1.9313 1.3757 1.2872 0.1038  -0.0972 0.0781  1161 LEU B N   
23228 C CA  . LEU C 1161 ? 1.9494 1.4122 1.2904 0.1452  -0.0990 0.0824  1161 LEU B CA  
23229 C C   . LEU C 1161 ? 1.9533 1.4994 1.3271 0.1407  -0.1111 0.0790  1161 LEU B C   
23230 O O   . LEU C 1161 ? 1.9259 1.5357 1.3368 0.1177  -0.1313 0.0859  1161 LEU B O   
23231 C CB  . LEU C 1161 ? 1.8914 1.3704 1.2307 0.1619  -0.1147 0.0987  1161 LEU B CB  
23232 C CG  . LEU C 1161 ? 1.8661 1.3449 1.1789 0.2096  -0.1131 0.1064  1161 LEU B CG  
23233 C CD1 . LEU C 1161 ? 1.8587 1.3281 1.1549 0.2345  -0.0970 0.0955  1161 LEU B CD1 
23234 C CD2 . LEU C 1161 ? 1.8780 1.2857 1.1537 0.2269  -0.1033 0.1145  1161 LEU B CD2 
23235 N N   . VAL C 1162 ? 1.9992 1.5447 1.3588 0.1624  -0.0986 0.0685  1162 VAL B N   
23236 C CA  . VAL C 1162 ? 2.0038 1.6289 1.3939 0.1554  -0.1074 0.0634  1162 VAL B CA  
23237 C C   . VAL C 1162 ? 1.9487 1.6547 1.3724 0.1506  -0.1340 0.0796  1162 VAL B C   
23238 O O   . VAL C 1162 ? 1.8884 1.6503 1.3498 0.1175  -0.1486 0.0824  1162 VAL B O   
23239 C CB  . VAL C 1162 ? 2.0898 1.7184 1.4580 0.1945  -0.0953 0.0543  1162 VAL B CB  
23240 C CG1 . VAL C 1162 ? 2.1243 1.7275 1.4852 0.1804  -0.0771 0.0328  1162 VAL B CG1 
23241 C CG2 . VAL C 1162 ? 2.1750 1.7400 1.4998 0.2384  -0.0841 0.0599  1162 VAL B CG2 
23242 N N   . LYS C 1163 ? 1.9857 1.6948 1.3942 0.1826  -0.1403 0.0912  1163 LYS B N   
23243 C CA  . LYS C 1163 ? 1.9575 1.7492 1.3943 0.1825  -0.1652 0.1054  1163 LYS B CA  
23244 C C   . LYS C 1163 ? 1.9176 1.7299 1.3860 0.1409  -0.1835 0.1126  1163 LYS B C   
23245 O O   . LYS C 1163 ? 1.8784 1.7664 1.3806 0.1250  -0.2043 0.1209  1163 LYS B O   
23246 C CB  . LYS C 1163 ? 1.9813 1.7681 1.3936 0.2223  -0.1684 0.1167  1163 LYS B CB  
23247 C CG  . LYS C 1163 ? 1.9413 1.8259 1.3771 0.2343  -0.1886 0.1274  1163 LYS B CG  
23248 C CD  . LYS C 1163 ? 1.9582 1.8439 1.3714 0.2711  -0.1934 0.1396  1163 LYS B CD  
23249 C CE  . LYS C 1163 ? 1.9170 1.9072 1.3572 0.2760  -0.2162 0.1513  1163 LYS B CE  
23250 N NZ  . LYS C 1163 ? 1.9192 1.9169 1.3498 0.2880  -0.2299 0.1648  1163 LYS B NZ  
23251 N N   . ILE C 1164 ? 1.9405 1.6855 1.3975 0.1231  -0.1757 0.1098  1164 ILE B N   
23252 C CA  . ILE C 1164 ? 1.9245 1.6833 1.4082 0.0884  -0.1925 0.1165  1164 ILE B CA  
23253 C C   . ILE C 1164 ? 1.9290 1.6971 1.4393 0.0502  -0.1908 0.1098  1164 ILE B C   
23254 O O   . ILE C 1164 ? 1.9031 1.6864 1.4387 0.0206  -0.2047 0.1154  1164 ILE B O   
23255 C CB  . ILE C 1164 ? 1.6465 1.3424 1.1067 0.0920  -0.1907 0.1209  1164 ILE B CB  
23256 C CG1 . ILE C 1164 ? 1.6387 1.2791 1.0974 0.0640  -0.1792 0.1141  1164 ILE B CG1 
23257 C CG2 . ILE C 1164 ? 1.6867 1.3382 1.1044 0.1346  -0.1776 0.1228  1164 ILE B CG2 
23258 C CD1 . ILE C 1164 ? 1.6638 1.2488 1.0987 0.0699  -0.1767 0.1185  1164 ILE B CD1 
23259 N N   . ASP C 1165 ? 1.9633 1.7231 1.4672 0.0515  -0.1740 0.0975  1165 ASP B N   
23260 C CA  . ASP C 1165 ? 1.9654 1.7476 1.4962 0.0163  -0.1729 0.0913  1165 ASP B CA  
23261 C C   . ASP C 1165 ? 1.9053 1.7808 1.4739 0.0054  -0.1920 0.0987  1165 ASP B C   
23262 O O   . ASP C 1165 ? 1.8625 1.7740 1.4644 -0.0269 -0.2059 0.1056  1165 ASP B O   
23263 C CB  . ASP C 1165 ? 2.0166 1.7592 1.5258 0.0196  -0.1486 0.0739  1165 ASP B CB  
23264 C CG  . ASP C 1165 ? 1.9950 1.7673 1.5316 -0.0168 -0.1476 0.0672  1165 ASP B CG  
23265 O OD1 . ASP C 1165 ? 1.9574 1.7306 1.5150 -0.0473 -0.1552 0.0730  1165 ASP B OD1 
23266 O OD2 . ASP C 1165 ? 2.0178 1.8132 1.5536 -0.0132 -0.1387 0.0558  1165 ASP B OD2 
23267 N N   . THR C 1166 ? 1.9202 1.8346 1.4826 0.0338  -0.1921 0.0983  1166 THR B N   
23268 C CA  . THR C 1166 ? 1.8821 1.8904 1.4766 0.0299  -0.2119 0.1087  1166 THR B CA  
23269 C C   . THR C 1166 ? 1.8393 1.8751 1.4591 0.0080  -0.2363 0.1249  1166 THR B C   
23270 O O   . THR C 1166 ? 1.8126 1.8983 1.4681 -0.0239 -0.2511 0.1325  1166 THR B O   
23271 C CB  . THR C 1166 ? 1.9145 1.9513 1.4917 0.0717  -0.2112 0.1104  1166 THR B CB  
23272 O OG1 . THR C 1166 ? 1.9516 1.9715 1.5074 0.0933  -0.1900 0.0947  1166 THR B OG1 
23273 C CG2 . THR C 1166 ? 1.8758 2.0142 1.4872 0.0652  -0.2344 0.1244  1166 THR B CG2 
23274 N N   . ALA C 1167 ? 1.8254 1.8275 1.4255 0.0254  -0.2406 0.1303  1167 ALA B N   
23275 C CA  . ALA C 1167 ? 1.7469 1.7661 1.3653 0.0067  -0.2631 0.1430  1167 ALA B CA  
23276 C C   . ALA C 1167 ? 1.6667 1.6668 1.3070 -0.0323 -0.2674 0.1435  1167 ALA B C   
23277 O O   . ALA C 1167 ? 1.6039 1.6505 1.2766 -0.0589 -0.2876 0.1539  1167 ALA B O   
23278 C CB  . ALA C 1167 ? 1.7836 1.7538 1.3712 0.0308  -0.2621 0.1448  1167 ALA B CB  
23279 N N   . LEU C 1168 ? 1.6342 1.5668 1.2566 -0.0356 -0.2484 0.1332  1168 LEU B N   
23280 C CA  . LEU C 1168 ? 1.5970 1.5098 1.2375 -0.0687 -0.2507 0.1338  1168 LEU B CA  
23281 C C   . LEU C 1168 ? 1.6325 1.6101 1.3116 -0.0967 -0.2607 0.1389  1168 LEU B C   
23282 O O   . LEU C 1168 ? 1.6351 1.6268 1.3407 -0.1244 -0.2746 0.1475  1168 LEU B O   
23283 C CB  . LEU C 1168 ? 1.5570 1.3999 1.1734 -0.0684 -0.2267 0.1214  1168 LEU B CB  
23284 C CG  . LEU C 1168 ? 1.5383 1.3254 1.1412 -0.0707 -0.2279 0.1237  1168 LEU B CG  
23285 C CD1 . LEU C 1168 ? 1.5633 1.2878 1.1475 -0.0777 -0.2061 0.1138  1168 LEU B CD1 
23286 C CD2 . LEU C 1168 ? 1.4856 1.3042 1.1210 -0.0966 -0.2505 0.1342  1168 LEU B CD2 
23287 N N   . ILE C 1169 ? 1.6552 1.6722 1.3362 -0.0878 -0.2531 0.1339  1169 ILE B N   
23288 C CA  . ILE C 1169 ? 1.6036 1.6876 1.3188 -0.1118 -0.2603 0.1385  1169 ILE B CA  
23289 C C   . ILE C 1169 ? 1.5731 1.7289 1.3172 -0.1212 -0.2859 0.1553  1169 ILE B C   
23290 O O   . ILE C 1169 ? 1.5485 1.7286 1.3223 -0.1512 -0.3012 0.1668  1169 ILE B O   
23291 C CB  . ILE C 1169 ? 1.5815 1.6828 1.2856 -0.0973 -0.2426 0.1253  1169 ILE B CB  
23292 C CG1 . ILE C 1169 ? 1.5661 1.6217 1.2619 -0.1124 -0.2233 0.1119  1169 ILE B CG1 
23293 C CG2 . ILE C 1169 ? 1.5566 1.7513 1.2915 -0.1064 -0.2552 0.1334  1169 ILE B CG2 
23294 C CD1 . ILE C 1169 ? 1.5864 1.6009 1.2470 -0.0882 -0.1992 0.0930  1169 ILE B CD1 
23295 N N   . LYS C 1170 ? 1.6071 1.7953 1.3417 -0.0957 -0.2905 0.1576  1170 LYS B N   
23296 C CA  . LYS C 1170 ? 1.6173 1.8751 1.3766 -0.1046 -0.3151 0.1738  1170 LYS B CA  
23297 C C   . LYS C 1170 ? 1.5610 1.7973 1.3350 -0.1310 -0.3330 0.1840  1170 LYS B C   
23298 O O   . LYS C 1170 ? 1.5061 1.7933 1.3109 -0.1567 -0.3535 0.1983  1170 LYS B O   
23299 C CB  . LYS C 1170 ? 1.7262 1.9978 1.4641 -0.0698 -0.3171 0.1743  1170 LYS B CB  
23300 C CG  . LYS C 1170 ? 1.8312 2.1294 1.5539 -0.0383 -0.3012 0.1653  1170 LYS B CG  
23301 C CD  . LYS C 1170 ? 1.8881 2.2671 1.6417 -0.0558 -0.3055 0.1693  1170 LYS B CD  
23302 C CE  . LYS C 1170 ? 1.9204 2.3893 1.7036 -0.0683 -0.3308 0.1880  1170 LYS B CE  
23303 N NZ  . LYS C 1170 ? 1.9089 2.4613 1.7241 -0.0882 -0.3358 0.1945  1170 LYS B NZ  
23304 N N   . ALA C 1171 ? 1.5746 1.7332 1.3249 -0.1240 -0.3246 0.1765  1171 ALA B N   
23305 C CA  . ALA C 1171 ? 1.5818 1.7092 1.3414 -0.1456 -0.3384 0.1827  1171 ALA B CA  
23306 C C   . ALA C 1171 ? 1.5650 1.6945 1.3513 -0.1775 -0.3390 0.1864  1171 ALA B C   
23307 O O   . ALA C 1171 ? 1.5452 1.7093 1.3608 -0.2035 -0.3584 0.1996  1171 ALA B O   
23308 C CB  . ALA C 1171 ? 1.6252 1.6735 1.3510 -0.1275 -0.3267 0.1729  1171 ALA B CB  
23309 N N   . ASP C 1172 ? 1.5769 1.6691 1.3524 -0.1757 -0.3179 0.1754  1172 ASP B N   
23310 C CA  . ASP C 1172 ? 1.5747 1.6720 1.3737 -0.2035 -0.3160 0.1784  1172 ASP B CA  
23311 C C   . ASP C 1172 ? 1.5415 1.7188 1.3774 -0.2256 -0.3317 0.1926  1172 ASP B C   
23312 O O   . ASP C 1172 ? 1.5101 1.7008 1.3732 -0.2527 -0.3429 0.2042  1172 ASP B O   
23313 C CB  . ASP C 1172 ? 1.6040 1.6752 1.3865 -0.1967 -0.2905 0.1635  1172 ASP B CB  
23314 C CG  . ASP C 1172 ? 1.6468 1.6481 1.4142 -0.2005 -0.2780 0.1562  1172 ASP B CG  
23315 O OD1 . ASP C 1172 ? 1.6568 1.6270 1.4242 -0.2046 -0.2880 0.1615  1172 ASP B OD1 
23316 O OD2 . ASP C 1172 ? 1.6838 1.6628 1.4387 -0.2001 -0.2579 0.1445  1172 ASP B OD2 
23317 N N   . ASN C 1173 ? 1.5709 1.8020 1.4068 -0.2124 -0.3319 0.1925  1173 ASN B N   
23318 C CA  . ASN C 1173 ? 1.5638 1.8796 1.4323 -0.2303 -0.3451 0.2060  1173 ASN B CA  
23319 C C   . ASN C 1173 ? 1.5297 1.8692 1.4234 -0.2539 -0.3717 0.2251  1173 ASN B C   
23320 O O   . ASN C 1173 ? 1.5107 1.8729 1.4332 -0.2828 -0.3815 0.2381  1173 ASN B O   
23321 C CB  . ASN C 1173 ? 1.6355 2.0035 1.4951 -0.2063 -0.3410 0.2018  1173 ASN B CB  
23322 C CG  . ASN C 1173 ? 1.7134 2.1005 1.5686 -0.1994 -0.3209 0.1892  1173 ASN B CG  
23323 O OD1 . ASN C 1173 ? 1.7422 2.1970 1.6057 -0.1923 -0.3217 0.1906  1173 ASN B OD1 
23324 N ND2 . ASN C 1173 ? 1.7315 2.0617 1.5731 -0.2020 -0.3030 0.1762  1173 ASN B ND2 
23325 N N   . PHE C 1174 ? 1.5186 1.8504 1.4004 -0.2420 -0.3833 0.2270  1174 PHE B N   
23326 C CA  . PHE C 1174 ? 1.4805 1.8278 1.3818 -0.2648 -0.4091 0.2428  1174 PHE B CA  
23327 C C   . PHE C 1174 ? 1.4496 1.7563 1.3661 -0.2909 -0.4150 0.2489  1174 PHE B C   
23328 O O   . PHE C 1174 ? 1.4434 1.7834 1.3889 -0.3192 -0.4331 0.2659  1174 PHE B O   
23329 C CB  . PHE C 1174 ? 1.4949 1.8137 1.3722 -0.2463 -0.4162 0.2381  1174 PHE B CB  
23330 C CG  . PHE C 1174 ? 1.4763 1.7969 1.3679 -0.2701 -0.4420 0.2503  1174 PHE B CG  
23331 C CD1 . PHE C 1174 ? 1.4624 1.8539 1.3738 -0.2848 -0.4624 0.2647  1174 PHE B CD1 
23332 C CD2 . PHE C 1174 ? 1.4812 1.7320 1.3647 -0.2776 -0.4457 0.2465  1174 PHE B CD2 
23333 C CE1 . PHE C 1174 ? 1.4711 1.8597 1.3934 -0.3090 -0.4865 0.2748  1174 PHE B CE1 
23334 C CE2 . PHE C 1174 ? 1.4865 1.7330 1.3801 -0.2990 -0.4693 0.2553  1174 PHE B CE2 
23335 C CZ  . PHE C 1174 ? 1.4795 1.7928 1.3921 -0.3158 -0.4900 0.2693  1174 PHE B CZ  
23336 N N   . LEU C 1175 ? 1.4202 1.6565 1.3172 -0.2811 -0.3993 0.2361  1175 LEU B N   
23337 C CA  . LEU C 1175 ? 1.4146 1.6098 1.3233 -0.3009 -0.4037 0.2410  1175 LEU B CA  
23338 C C   . LEU C 1175 ? 1.3884 1.6235 1.3284 -0.3253 -0.4037 0.2529  1175 LEU B C   
23339 O O   . LEU C 1175 ? 1.3720 1.6163 1.3368 -0.3498 -0.4203 0.2689  1175 LEU B O   
23340 C CB  . LEU C 1175 ? 1.4331 1.5508 1.3131 -0.2836 -0.3855 0.2248  1175 LEU B CB  
23341 C CG  . LEU C 1175 ? 1.4583 1.5292 1.3079 -0.2624 -0.3871 0.2153  1175 LEU B CG  
23342 C CD1 . LEU C 1175 ? 1.4768 1.4778 1.2988 -0.2462 -0.3665 0.2006  1175 LEU B CD1 
23343 C CD2 . LEU C 1175 ? 1.4602 1.5234 1.3195 -0.2775 -0.4116 0.2243  1175 LEU B CD2 
23344 N N   . LEU C 1176 ? 1.3891 1.6471 1.3270 -0.3184 -0.3853 0.2453  1176 LEU B N   
23345 C CA  . LEU C 1176 ? 1.3726 1.6826 1.3397 -0.3403 -0.3856 0.2566  1176 LEU B CA  
23346 C C   . LEU C 1176 ? 1.4173 1.7958 1.4139 -0.3608 -0.4084 0.2779  1176 LEU B C   
23347 O O   . LEU C 1176 ? 1.4226 1.8193 1.4470 -0.3870 -0.4215 0.2962  1176 LEU B O   
23348 C CB  . LEU C 1176 ? 1.3032 1.6419 1.2605 -0.3275 -0.3653 0.2434  1176 LEU B CB  
23349 C CG  . LEU C 1176 ? 1.2726 1.5497 1.2025 -0.3125 -0.3415 0.2234  1176 LEU B CG  
23350 C CD1 . LEU C 1176 ? 1.2617 1.5732 1.1853 -0.3050 -0.3241 0.2114  1176 LEU B CD1 
23351 C CD2 . LEU C 1176 ? 1.2496 1.4978 1.1925 -0.3311 -0.3407 0.2289  1176 LEU B CD2 
23352 N N   . GLU C 1177 ? 1.4524 1.8698 1.4419 -0.3482 -0.4127 0.2762  1177 GLU B N   
23353 C CA  . GLU C 1177 ? 1.4729 1.9670 1.4882 -0.3657 -0.4322 0.2953  1177 GLU B CA  
23354 C C   . GLU C 1177 ? 1.4792 1.9594 1.5062 -0.3857 -0.4571 0.3105  1177 GLU B C   
23355 O O   . GLU C 1177 ? 1.4918 2.0325 1.5431 -0.4072 -0.4753 0.3295  1177 GLU B O   
23356 C CB  . GLU C 1177 ? 1.5354 2.0778 1.5379 -0.3429 -0.4282 0.2879  1177 GLU B CB  
23357 C CG  . GLU C 1177 ? 1.5915 2.1818 1.5937 -0.3316 -0.4102 0.2795  1177 GLU B CG  
23358 C CD  . GLU C 1177 ? 1.6605 2.3275 1.6646 -0.3189 -0.4146 0.2823  1177 GLU B CD  
23359 O OE1 . GLU C 1177 ? 1.6656 2.4075 1.6892 -0.3278 -0.4140 0.2894  1177 GLU B OE1 
23360 O OE2 . GLU C 1177 ? 1.7027 2.3593 1.6890 -0.2995 -0.4191 0.2779  1177 GLU B OE2 
23361 N N   . ASN C 1178 ? 1.4699 1.8720 1.4794 -0.3801 -0.4582 0.3024  1178 ASN B N   
23362 C CA  . ASN C 1178 ? 1.4514 1.8331 1.4654 -0.3958 -0.4816 0.3121  1178 ASN B CA  
23363 C C   . ASN C 1178 ? 1.4393 1.7465 1.4521 -0.4060 -0.4871 0.3126  1178 ASN B C   
23364 O O   . ASN C 1178 ? 1.4620 1.7448 1.4741 -0.4174 -0.5059 0.3172  1178 ASN B O   
23365 C CB  . ASN C 1178 ? 1.4514 1.8286 1.4409 -0.3756 -0.4855 0.3015  1178 ASN B CB  
23366 C CG  . ASN C 1178 ? 1.4198 1.8709 1.4263 -0.3908 -0.5057 0.3165  1178 ASN B CG  
23367 O OD1 . ASN C 1178 ? 1.4115 1.8708 1.4369 -0.4201 -0.5276 0.3324  1178 ASN B OD1 
23368 N ND2 . ASN C 1178 ? 1.4082 1.9134 1.4072 -0.3708 -0.4985 0.3119  1178 ASN B ND2 
23369 N N   . THR C 1179 ? 1.3940 1.6669 1.4058 -0.4020 -0.4711 0.3074  1179 THR B N   
23370 C CA  . THR C 1179 ? 1.3756 1.5849 1.3885 -0.4097 -0.4749 0.3091  1179 THR B CA  
23371 C C   . THR C 1179 ? 1.3340 1.5681 1.3809 -0.4408 -0.4915 0.3336  1179 THR B C   
23372 O O   . THR C 1179 ? 1.3212 1.5269 1.3740 -0.4559 -0.5105 0.3426  1179 THR B O   
23373 C CB  . THR C 1179 ? 1.1715 1.3433 1.1724 -0.3942 -0.4504 0.2958  1179 THR B CB  
23374 O OG1 . THR C 1179 ? 1.2101 1.3662 1.1809 -0.3669 -0.4325 0.2753  1179 THR B OG1 
23375 C CG2 . THR C 1179 ? 1.1353 1.2381 1.1323 -0.3953 -0.4516 0.2943  1179 THR B CG2 
23376 N N   . LEU C 1180 ? 1.3163 1.6057 1.3846 -0.4503 -0.4845 0.3443  1180 LEU B N   
23377 C CA  . LEU C 1180 ? 1.3130 1.6000 1.4048 -0.4675 -0.4858 0.3604  1180 LEU B CA  
23378 C C   . LEU C 1180 ? 1.3814 1.6704 1.4985 -0.4955 -0.5093 0.3856  1180 LEU B C   
23379 O O   . LEU C 1180 ? 1.4115 1.6642 1.5374 -0.5009 -0.5098 0.3937  1180 LEU B O   
23380 C CB  . LEU C 1180 ? 1.2256 1.5656 1.3298 -0.4679 -0.4691 0.3623  1180 LEU B CB  
23381 C CG  . LEU C 1180 ? 1.1807 1.4663 1.2686 -0.4514 -0.4488 0.3461  1180 LEU B CG  
23382 C CD1 . LEU C 1180 ? 1.1424 1.4717 1.2395 -0.4528 -0.4314 0.3451  1180 LEU B CD1 
23383 C CD2 . LEU C 1180 ? 1.1703 1.3998 1.2643 -0.4581 -0.4582 0.3553  1180 LEU B CD2 
23384 N N   . PRO C 1181 ? 1.3949 1.7274 1.5237 -0.5135 -0.5285 0.3992  1181 PRO B N   
23385 C CA  . PRO C 1181 ? 1.3899 1.7008 1.5343 -0.5394 -0.5525 0.4192  1181 PRO B CA  
23386 C C   . PRO C 1181 ? 1.4281 1.6526 1.5455 -0.5255 -0.5553 0.4008  1181 PRO B C   
23387 O O   . PRO C 1181 ? 1.4336 1.6492 1.5380 -0.5272 -0.5679 0.3942  1181 PRO B O   
23388 C CB  . PRO C 1181 ? 1.3690 1.7457 1.5248 -0.5583 -0.5696 0.4319  1181 PRO B CB  
23389 C CG  . PRO C 1181 ? 1.3371 1.7859 1.4938 -0.5454 -0.5537 0.4257  1181 PRO B CG  
23390 C CD  . PRO C 1181 ? 1.3498 1.7543 1.4797 -0.5125 -0.5293 0.3985  1181 PRO B CD  
23391 N N   . ALA C 1182 ? 1.4356 1.6020 1.5441 -0.5107 -0.5427 0.3919  1182 ALA B N   
23392 C CA  . ALA C 1182 ? 1.4360 1.5247 1.5147 -0.4896 -0.5379 0.3694  1182 ALA B CA  
23393 C C   . ALA C 1182 ? 1.5102 1.5514 1.5849 -0.5040 -0.5615 0.3731  1182 ALA B C   
23394 O O   . ALA C 1182 ? 1.5409 1.5724 1.6358 -0.5259 -0.5764 0.3932  1182 ALA B O   
23395 C CB  . ALA C 1182 ? 1.3824 1.4297 1.4565 -0.4733 -0.5195 0.3624  1182 ALA B CB  
23396 N N   . GLN C 1183 ? 1.4979 1.5098 1.5458 -0.4920 -0.5648 0.3538  1183 GLN B N   
23397 C CA  . GLN C 1183 ? 1.4981 1.4676 1.5383 -0.5061 -0.5872 0.3532  1183 GLN B CA  
23398 C C   . GLN C 1183 ? 1.4719 1.3533 1.4911 -0.4906 -0.5846 0.3375  1183 GLN B C   
23399 O O   . GLN C 1183 ? 1.5154 1.3517 1.5377 -0.5058 -0.6017 0.3436  1183 GLN B O   
23400 C CB  . GLN C 1183 ? 1.5347 1.5325 1.5595 -0.5051 -0.5954 0.3431  1183 GLN B CB  
23401 C CG  . GLN C 1183 ? 1.6108 1.5834 1.6328 -0.5287 -0.6220 0.3461  1183 GLN B CG  
23402 C CD  . GLN C 1183 ? 1.6357 1.6249 1.6885 -0.5645 -0.6406 0.3739  1183 GLN B CD  
23403 O OE1 . GLN C 1183 ? 1.6176 1.6508 1.6956 -0.5717 -0.6340 0.3926  1183 GLN B OE1 
23404 N NE2 . GLN C 1183 ? 1.6735 1.6275 1.7238 -0.5882 -0.6640 0.3772  1183 GLN B NE2 
23405 N N   . SER C 1184 ? 1.4056 1.2618 1.4026 -0.4604 -0.5630 0.3173  1184 SER B N   
23406 C CA  . SER C 1184 ? 1.4136 1.1962 1.3946 -0.4431 -0.5557 0.3047  1184 SER B CA  
23407 C C   . SER C 1184 ? 1.3777 1.1571 1.3542 -0.4197 -0.5287 0.2972  1184 SER B C   
23408 O O   . SER C 1184 ? 1.3556 1.1674 1.3234 -0.4065 -0.5124 0.2887  1184 SER B O   
23409 C CB  . SER C 1184 ? 1.4547 1.1881 1.4024 -0.4292 -0.5601 0.2817  1184 SER B CB  
23410 O OG  . SER C 1184 ? 1.4673 1.1535 1.3943 -0.4015 -0.5411 0.2647  1184 SER B OG  
23411 N N   . THR C 1185 ? 1.3702 1.1085 1.3510 -0.4141 -0.5242 0.2998  1185 THR B N   
23412 C CA  . THR C 1185 ? 1.3275 1.0562 1.3011 -0.3922 -0.4996 0.2909  1185 THR B CA  
23413 C C   . THR C 1185 ? 1.3228 1.0340 1.2633 -0.3677 -0.4832 0.2664  1185 THR B C   
23414 O O   . THR C 1185 ? 1.2659 1.0026 1.2025 -0.3573 -0.4632 0.2614  1185 THR B O   
23415 C CB  . THR C 1185 ? 1.3361 1.0106 1.3103 -0.3847 -0.5001 0.2920  1185 THR B CB  
23416 O OG1 . THR C 1185 ? 1.3301 1.0212 1.3357 -0.4051 -0.5124 0.3174  1185 THR B OG1 
23417 C CG2 . THR C 1185 ? 1.3046 0.9712 1.2691 -0.3621 -0.4746 0.2815  1185 THR B CG2 
23418 N N   . PHE C 1186 ? 1.3789 1.0453 1.2947 -0.3595 -0.4922 0.2515  1186 PHE B N   
23419 C CA  . PHE C 1186 ? 1.3741 1.0276 1.2575 -0.3382 -0.4806 0.2307  1186 PHE B CA  
23420 C C   . PHE C 1186 ? 1.3873 1.0964 1.2707 -0.3388 -0.4747 0.2319  1186 PHE B C   
23421 O O   . PHE C 1186 ? 1.4008 1.1180 1.2719 -0.3226 -0.4536 0.2237  1186 PHE B O   
23422 C CB  . PHE C 1186 ? 1.3766 0.9884 1.2371 -0.3354 -0.4967 0.2176  1186 PHE B CB  
23423 C CG  . PHE C 1186 ? 1.3464 0.9489 1.1736 -0.3134 -0.4859 0.1987  1186 PHE B CG  
23424 C CD1 . PHE C 1186 ? 1.3568 0.9133 1.1585 -0.2901 -0.4713 0.1825  1186 PHE B CD1 
23425 C CD2 . PHE C 1186 ? 1.3223 0.9648 1.1438 -0.3147 -0.4895 0.1983  1186 PHE B CD2 
23426 C CE1 . PHE C 1186 ? 1.3557 0.9040 1.1263 -0.2699 -0.4608 0.1673  1186 PHE B CE1 
23427 C CE2 . PHE C 1186 ? 1.3340 0.9672 1.1243 -0.2925 -0.4791 0.1829  1186 PHE B CE2 
23428 C CZ  . PHE C 1186 ? 1.3457 0.9309 1.1105 -0.2708 -0.4647 0.1680  1186 PHE B CZ  
23429 N N   . THR C 1187 ? 1.3713 1.1173 1.2666 -0.3569 -0.4932 0.2415  1187 THR B N   
23430 C CA  . THR C 1187 ? 1.3337 1.1396 1.2323 -0.3569 -0.4884 0.2446  1187 THR B CA  
23431 C C   . THR C 1187 ? 1.2861 1.1254 1.1987 -0.3545 -0.4685 0.2502  1187 THR B C   
23432 O O   . THR C 1187 ? 1.2886 1.1427 1.1865 -0.3381 -0.4509 0.2407  1187 THR B O   
23433 C CB  . THR C 1187 ? 1.3101 1.1655 1.2313 -0.3830 -0.5111 0.2611  1187 THR B CB  
23434 O OG1 . THR C 1187 ? 1.3271 1.1503 1.2399 -0.3930 -0.5328 0.2582  1187 THR B OG1 
23435 C CG2 . THR C 1187 ? 1.2933 1.2074 1.2109 -0.3765 -0.5064 0.2602  1187 THR B CG2 
23436 N N   . LEU C 1188 ? 1.2308 1.0807 1.1707 -0.3708 -0.4715 0.2657  1188 LEU B N   
23437 C CA  . LEU C 1188 ? 1.2031 1.0915 1.1594 -0.3731 -0.4554 0.2726  1188 LEU B CA  
23438 C C   . LEU C 1188 ? 1.1950 1.0544 1.1284 -0.3505 -0.4304 0.2554  1188 LEU B C   
23439 O O   . LEU C 1188 ? 1.1853 1.0698 1.1104 -0.3418 -0.4143 0.2483  1188 LEU B O   
23440 C CB  . LEU C 1188 ? 1.2023 1.0932 1.1873 -0.3903 -0.4624 0.2910  1188 LEU B CB  
23441 C CG  . LEU C 1188 ? 1.1158 1.0592 1.1250 -0.3998 -0.4515 0.3036  1188 LEU B CG  
23442 C CD1 . LEU C 1188 ? 1.0748 1.0903 1.1026 -0.4163 -0.4595 0.3162  1188 LEU B CD1 
23443 C CD2 . LEU C 1188 ? 1.0929 1.0215 1.1234 -0.4101 -0.4578 0.3198  1188 LEU B CD2 
23444 N N   . ALA C 1189 ? 1.2304 1.0353 1.1528 -0.3411 -0.4274 0.2487  1189 ALA B N   
23445 C CA  . ALA C 1189 ? 1.2457 1.0215 1.1479 -0.3221 -0.4040 0.2344  1189 ALA B CA  
23446 C C   . ALA C 1189 ? 1.2717 1.0416 1.1436 -0.3038 -0.3895 0.2180  1189 ALA B C   
23447 O O   . ALA C 1189 ? 1.2447 1.0189 1.1080 -0.2962 -0.3683 0.2112  1189 ALA B O   
23448 C CB  . ALA C 1189 ? 1.2871 1.0044 1.1780 -0.3122 -0.4058 0.2283  1189 ALA B CB  
23449 N N   . ILE C 1190 ? 1.2909 1.0503 1.1457 -0.2969 -0.4007 0.2118  1190 ILE B N   
23450 C CA  . ILE C 1190 ? 1.3057 1.0617 1.1323 -0.2778 -0.3874 0.1989  1190 ILE B CA  
23451 C C   . ILE C 1190 ? 1.3100 1.1210 1.1491 -0.2834 -0.3810 0.2044  1190 ILE B C   
23452 O O   . ILE C 1190 ? 1.2935 1.1055 1.1220 -0.2744 -0.3598 0.1972  1190 ILE B O   
23453 C CB  . ILE C 1190 ? 1.3265 1.0652 1.1320 -0.2680 -0.4009 0.1920  1190 ILE B CB  
23454 C CG1 . ILE C 1190 ? 1.3372 1.0183 1.1254 -0.2594 -0.4036 0.1828  1190 ILE B CG1 
23455 C CG2 . ILE C 1190 ? 1.3209 1.0612 1.0984 -0.2465 -0.3867 0.1818  1190 ILE B CG2 
23456 C CD1 . ILE C 1190 ? 1.3579 1.0169 1.1163 -0.2440 -0.4096 0.1714  1190 ILE B CD1 
23457 N N   . SER C 1191 ? 1.2910 1.1480 1.1530 -0.2997 -0.3990 0.2172  1191 SER B N   
23458 C CA  . SER C 1191 ? 1.2480 1.1634 1.1249 -0.3059 -0.3939 0.2232  1191 SER B CA  
23459 C C   . SER C 1191 ? 1.2067 1.1236 1.0875 -0.3066 -0.3727 0.2203  1191 SER B C   
23460 O O   . SER C 1191 ? 1.1952 1.1224 1.0626 -0.2959 -0.3555 0.2111  1191 SER B O   
23461 C CB  . SER C 1191 ? 1.2151 1.1810 1.1248 -0.3304 -0.4151 0.2419  1191 SER B CB  
23462 O OG  . SER C 1191 ? 1.2063 1.2298 1.1207 -0.3295 -0.4138 0.2443  1191 SER B OG  
23463 N N   . ALA C 1192 ? 1.1943 1.0991 1.0919 -0.3186 -0.3738 0.2275  1192 ALA B N   
23464 C CA  . ALA C 1192 ? 1.1711 1.0807 1.0734 -0.3213 -0.3547 0.2253  1192 ALA B CA  
23465 C C   . ALA C 1192 ? 1.2184 1.0864 1.0872 -0.3015 -0.3320 0.2066  1192 ALA B C   
23466 O O   . ALA C 1192 ? 1.2484 1.1321 1.1081 -0.2976 -0.3159 0.1989  1192 ALA B O   
23467 C CB  . ALA C 1192 ? 1.1247 1.0233 1.0475 -0.3330 -0.3602 0.2363  1192 ALA B CB  
23468 N N   . TYR C 1193 ? 1.2498 1.0641 1.0991 -0.2891 -0.3306 0.1994  1193 TYR B N   
23469 C CA  . TYR C 1193 ? 1.2801 1.0540 1.0981 -0.2723 -0.3088 0.1842  1193 TYR B CA  
23470 C C   . TYR C 1193 ? 1.2852 1.0633 1.0803 -0.2587 -0.2992 0.1748  1193 TYR B C   
23471 O O   . TYR C 1193 ? 1.3180 1.0773 1.0924 -0.2505 -0.2782 0.1644  1193 TYR B O   
23472 C CB  . TYR C 1193 ? 1.2971 1.0162 1.0951 -0.2588 -0.3107 0.1778  1193 TYR B CB  
23473 C CG  . TYR C 1193 ? 1.3080 0.9879 1.0716 -0.2415 -0.2888 0.1640  1193 TYR B CG  
23474 C CD1 . TYR C 1193 ? 1.3182 0.9921 1.0796 -0.2454 -0.2689 0.1605  1193 TYR B CD1 
23475 C CD2 . TYR C 1193 ? 1.3021 0.9547 1.0355 -0.2225 -0.2880 0.1556  1193 TYR B CD2 
23476 C CE1 . TYR C 1193 ? 1.3357 0.9740 1.0655 -0.2328 -0.2485 0.1494  1193 TYR B CE1 
23477 C CE2 . TYR C 1193 ? 1.3274 0.9437 1.0289 -0.2075 -0.2674 0.1454  1193 TYR B CE2 
23478 C CZ  . TYR C 1193 ? 1.3354 0.9432 1.0352 -0.2137 -0.2476 0.1424  1193 TYR B CZ  
23479 O OH  . TYR C 1193 ? 1.3258 0.8973 0.9943 -0.2023 -0.2267 0.1337  1193 TYR B OH  
23480 N N   . ALA C 1194 ? 1.2432 1.0466 1.0421 -0.2566 -0.3144 0.1790  1194 ALA B N   
23481 C CA  . ALA C 1194 ? 1.2263 1.0320 1.0020 -0.2390 -0.3064 0.1710  1194 ALA B CA  
23482 C C   . ALA C 1194 ? 1.2022 1.0447 0.9845 -0.2434 -0.2936 0.1690  1194 ALA B C   
23483 O O   . ALA C 1194 ? 1.2194 1.0465 0.9766 -0.2275 -0.2770 0.1582  1194 ALA B O   
23484 C CB  . ALA C 1194 ? 1.2405 1.0671 1.0178 -0.2343 -0.3270 0.1763  1194 ALA B CB  
23485 N N   . LEU C 1195 ? 1.1504 1.0410 0.9654 -0.2646 -0.3015 0.1794  1195 LEU B N   
23486 C CA  . LEU C 1195 ? 1.1227 1.0548 0.9461 -0.2711 -0.2906 0.1772  1195 LEU B CA  
23487 C C   . LEU C 1195 ? 1.1499 1.0522 0.9623 -0.2742 -0.2690 0.1674  1195 LEU B C   
23488 O O   . LEU C 1195 ? 1.1634 1.0530 0.9544 -0.2655 -0.2503 0.1545  1195 LEU B O   
23489 C CB  . LEU C 1195 ? 1.0595 1.0552 0.9217 -0.2940 -0.3068 0.1934  1195 LEU B CB  
23490 C CG  . LEU C 1195 ? 1.0628 1.0861 0.9366 -0.2950 -0.3303 0.2049  1195 LEU B CG  
23491 C CD1 . LEU C 1195 ? 1.0446 1.1133 0.9561 -0.3205 -0.3489 0.2244  1195 LEU B CD1 
23492 C CD2 . LEU C 1195 ? 1.0639 1.1201 0.9266 -0.2799 -0.3289 0.2000  1195 LEU B CD2 
23493 N N   . SER C 1196 ? 1.1548 1.0432 0.9802 -0.2859 -0.2718 0.1736  1196 SER B N   
23494 C CA  . SER C 1196 ? 1.1917 1.0503 1.0069 -0.2891 -0.2532 0.1660  1196 SER B CA  
23495 C C   . SER C 1196 ? 1.2532 1.0687 1.0304 -0.2727 -0.2320 0.1493  1196 SER B C   
23496 O O   . SER C 1196 ? 1.2233 1.0274 0.9906 -0.2789 -0.2131 0.1407  1196 SER B O   
23497 C CB  . SER C 1196 ? 1.1915 1.0191 1.0112 -0.2894 -0.2607 0.1721  1196 SER B CB  
23498 O OG  . SER C 1196 ? 1.2254 1.0132 1.0250 -0.2848 -0.2422 0.1627  1196 SER B OG  
23499 N N   . LEU C 1197 ? 1.3743 1.1660 1.1293 -0.2523 -0.2353 0.1454  1197 LEU B N   
23500 C CA  . LEU C 1197 ? 1.5242 1.2709 1.2415 -0.2342 -0.2163 0.1321  1197 LEU B CA  
23501 C C   . LEU C 1197 ? 1.6016 1.3699 1.3102 -0.2250 -0.2109 0.1258  1197 LEU B C   
23502 O O   . LEU C 1197 ? 1.6261 1.3720 1.3096 -0.2024 -0.2083 0.1214  1197 LEU B O   
23503 C CB  . LEU C 1197 ? 1.5858 1.2871 1.2791 -0.2139 -0.2208 0.1316  1197 LEU B CB  
23504 C CG  . LEU C 1197 ? 1.6222 1.3041 1.3232 -0.2185 -0.2300 0.1372  1197 LEU B CG  
23505 C CD1 . LEU C 1197 ? 1.6789 1.3198 1.3522 -0.1969 -0.2332 0.1343  1197 LEU B CD1 
23506 C CD2 . LEU C 1197 ? 1.6317 1.2963 1.3333 -0.2306 -0.2146 0.1344  1197 LEU B CD2 
23507 N N   . GLY C 1198 ? 1.6501 1.4641 1.3790 -0.2411 -0.2089 0.1256  1198 GLY B N   
23508 C CA  . GLY C 1198 ? 1.7206 1.5600 1.4426 -0.2319 -0.2039 0.1187  1198 GLY B CA  
23509 C C   . GLY C 1198 ? 1.7389 1.6172 1.4777 -0.2530 -0.1958 0.1144  1198 GLY B C   
23510 O O   . GLY C 1198 ? 1.7703 1.6235 1.4994 -0.2640 -0.1792 0.1056  1198 GLY B O   
23511 N N   . ASP C 1199 ? 1.6878 1.6310 1.4517 -0.2598 -0.2075 0.1210  1199 ASP B N   
23512 C CA  . ASP C 1199 ? 1.6198 1.6130 1.4063 -0.2828 -0.2042 0.1207  1199 ASP B CA  
23513 C C   . ASP C 1199 ? 1.4757 1.5011 1.2980 -0.3051 -0.2199 0.1388  1199 ASP B C   
23514 O O   . ASP C 1199 ? 1.4428 1.5040 1.2881 -0.3077 -0.2400 0.1543  1199 ASP B O   
23515 C CB  . ASP C 1199 ? 1.6692 1.7214 1.4648 -0.2790 -0.2082 0.1193  1199 ASP B CB  
23516 C CG  . ASP C 1199 ? 1.6977 1.8128 1.5219 -0.3045 -0.2094 0.1230  1199 ASP B CG  
23517 O OD1 . ASP C 1199 ? 1.6889 1.7937 1.5177 -0.3226 -0.2011 0.1211  1199 ASP B OD1 
23518 O OD2 . ASP C 1199 ? 1.7214 1.9000 1.5636 -0.3063 -0.2187 0.1288  1199 ASP B OD2 
23519 N N   . LYS C 1200 ? 1.3731 1.3862 1.1996 -0.3211 -0.2107 0.1374  1200 LYS B N   
23520 C CA  . LYS C 1200 ? 1.2946 1.3325 1.1529 -0.3387 -0.2241 0.1551  1200 LYS B CA  
23521 C C   . LYS C 1200 ? 1.3130 1.4183 1.1988 -0.3613 -0.2243 0.1605  1200 LYS B C   
23522 O O   . LYS C 1200 ? 1.3506 1.4710 1.2546 -0.3782 -0.2237 0.1683  1200 LYS B O   
23523 C CB  . LYS C 1200 ? 1.2575 1.2439 1.1050 -0.3390 -0.2160 0.1532  1200 LYS B CB  
23524 C CG  . LYS C 1200 ? 1.3088 1.2494 1.1219 -0.3329 -0.1924 0.1337  1200 LYS B CG  
23525 C CD  . LYS C 1200 ? 1.3830 1.2614 1.1756 -0.3232 -0.1861 0.1314  1200 LYS B CD  
23526 C CE  . LYS C 1200 ? 1.3969 1.2779 1.2005 -0.3403 -0.1786 0.1346  1200 LYS B CE  
23527 N NZ  . LYS C 1200 ? 1.4403 1.2614 1.2127 -0.3329 -0.1617 0.1245  1200 LYS B NZ  
23528 N N   . THR C 1201 ? 1.2632 1.4134 1.1522 -0.3607 -0.2250 0.1567  1201 THR B N   
23529 C CA  . THR C 1201 ? 1.1898 1.4128 1.1069 -0.3819 -0.2280 0.1640  1201 THR B CA  
23530 C C   . THR C 1201 ? 1.1781 1.4619 1.1146 -0.3816 -0.2437 0.1754  1201 THR B C   
23531 O O   . THR C 1201 ? 1.1446 1.4949 1.1079 -0.3993 -0.2497 0.1862  1201 THR B O   
23532 C CB  . THR C 1201 ? 1.1605 1.3914 1.0619 -0.3886 -0.2073 0.1437  1201 THR B CB  
23533 O OG1 . THR C 1201 ? 1.1824 1.3888 1.0536 -0.3683 -0.1973 0.1251  1201 THR B OG1 
23534 C CG2 . THR C 1201 ? 1.1404 1.3288 1.0297 -0.3976 -0.1923 0.1357  1201 THR B CG2 
23535 N N   . HIS C 1202 ? 1.2400 1.5061 1.1633 -0.3619 -0.2503 0.1739  1202 HIS B N   
23536 C CA  . HIS C 1202 ? 1.2578 1.5856 1.2025 -0.3637 -0.2675 0.1881  1202 HIS B CA  
23537 C C   . HIS C 1202 ? 1.2783 1.6428 1.2601 -0.3872 -0.2848 0.2133  1202 HIS B C   
23538 O O   . HIS C 1202 ? 1.2789 1.6033 1.2652 -0.3904 -0.2914 0.2222  1202 HIS B O   
23539 C CB  . HIS C 1202 ? 1.2642 1.5693 1.1964 -0.3434 -0.2780 0.1900  1202 HIS B CB  
23540 C CG  . HIS C 1202 ? 1.2516 1.6268 1.2022 -0.3444 -0.2924 0.2014  1202 HIS B CG  
23541 N ND1 . HIS C 1202 ? 1.2901 1.6746 1.2225 -0.3218 -0.2898 0.1918  1202 HIS B ND1 
23542 C CD2 . HIS C 1202 ? 1.2297 1.6728 1.2152 -0.3653 -0.3092 0.2228  1202 HIS B CD2 
23543 C CE1 . HIS C 1202 ? 1.2621 1.7205 1.2181 -0.3290 -0.3046 0.2062  1202 HIS B CE1 
23544 N NE2 . HIS C 1202 ? 1.2368 1.7312 1.2251 -0.3566 -0.3165 0.2255  1202 HIS B NE2 
23545 N N   . PRO C 1203 ? 1.2855 1.7268 1.2932 -0.4028 -0.2918 0.2249  1203 PRO B N   
23546 C CA  . PRO C 1203 ? 1.2771 1.7641 1.3216 -0.4268 -0.3069 0.2509  1203 PRO B CA  
23547 C C   . PRO C 1203 ? 1.2382 1.6971 1.2931 -0.4270 -0.3271 0.2691  1203 PRO B C   
23548 O O   . PRO C 1203 ? 1.2576 1.6934 1.3260 -0.4367 -0.3344 0.2827  1203 PRO B O   
23549 C CB  . PRO C 1203 ? 1.2752 1.8487 1.3382 -0.4354 -0.3131 0.2589  1203 PRO B CB  
23550 C CG  . PRO C 1203 ? 1.2897 1.8627 1.3240 -0.4185 -0.2936 0.2308  1203 PRO B CG  
23551 C CD  . PRO C 1203 ? 1.2951 1.7856 1.2961 -0.3953 -0.2853 0.2137  1203 PRO B CD  
23552 N N   . GLN C 1204 ? 1.1801 1.6418 1.2268 -0.4152 -0.3359 0.2682  1204 GLN B N   
23553 C CA  . GLN C 1204 ? 1.1233 1.5563 1.1735 -0.4138 -0.3548 0.2806  1204 GLN B CA  
23554 C C   . GLN C 1204 ? 1.0833 1.4326 1.1167 -0.4050 -0.3519 0.2741  1204 GLN B C   
23555 O O   . GLN C 1204 ? 1.0418 1.3732 1.0906 -0.4157 -0.3664 0.2900  1204 GLN B O   
23556 C CB  . GLN C 1204 ? 1.1352 1.5824 1.1707 -0.3972 -0.3582 0.2732  1204 GLN B CB  
23557 C CG  . GLN C 1204 ? 1.1153 1.5403 1.1512 -0.3957 -0.3773 0.2831  1204 GLN B CG  
23558 C CD  . GLN C 1204 ? 1.0739 1.5316 1.1434 -0.4222 -0.3992 0.3103  1204 GLN B CD  
23559 O OE1 . GLN C 1204 ? 1.0166 1.5203 1.1107 -0.4410 -0.4002 0.3241  1204 GLN B OE1 
23560 N NE2 . GLN C 1204 ? 1.1006 1.5340 1.1707 -0.4250 -0.4174 0.3189  1204 GLN B NE2 
23561 N N   . PHE C 1205 ? 1.0764 1.3745 1.0778 -0.3856 -0.3332 0.2511  1205 PHE B N   
23562 C CA  . PHE C 1205 ? 1.0643 1.2897 1.0499 -0.3779 -0.3280 0.2447  1205 PHE B CA  
23563 C C   . PHE C 1205 ? 1.0595 1.2896 1.0688 -0.3959 -0.3312 0.2590  1205 PHE B C   
23564 O O   . PHE C 1205 ? 1.0694 1.2653 1.0849 -0.3975 -0.3429 0.2690  1205 PHE B O   
23565 C CB  . PHE C 1205 ? 1.0044 1.1833 0.9549 -0.3598 -0.3040 0.2200  1205 PHE B CB  
23566 C CG  . PHE C 1205 ? 0.9709 1.0841 0.9068 -0.3548 -0.2957 0.2141  1205 PHE B CG  
23567 C CD1 . PHE C 1205 ? 0.9915 1.0552 0.9166 -0.3439 -0.3054 0.2156  1205 PHE B CD1 
23568 C CD2 . PHE C 1205 ? 0.9152 1.0195 0.8467 -0.3608 -0.2777 0.2058  1205 PHE B CD2 
23569 C CE1 . PHE C 1205 ? 0.9994 1.0077 0.9105 -0.3380 -0.2968 0.2096  1205 PHE B CE1 
23570 C CE2 . PHE C 1205 ? 0.9166 0.9678 0.8352 -0.3563 -0.2694 0.2010  1205 PHE B CE2 
23571 C CZ  . PHE C 1205 ? 0.9628 0.9669 0.8715 -0.3441 -0.2786 0.2031  1205 PHE B CZ  
23572 N N   . ARG C 1206 ? 1.0389 1.3126 1.0612 -0.4085 -0.3210 0.2599  1206 ARG B N   
23573 C CA  . ARG C 1206 ? 1.0455 1.3324 1.0912 -0.4244 -0.3227 0.2746  1206 ARG B CA  
23574 C C   . ARG C 1206 ? 1.0030 1.3111 1.0791 -0.4380 -0.3467 0.3023  1206 ARG B C   
23575 O O   . ARG C 1206 ? 0.9774 1.2704 1.0680 -0.4442 -0.3518 0.3157  1206 ARG B O   
23576 C CB  . ARG C 1206 ? 1.0630 1.4055 1.1185 -0.4373 -0.3094 0.2716  1206 ARG B CB  
23577 C CG  . ARG C 1206 ? 1.1459 1.4659 1.1711 -0.4278 -0.2855 0.2441  1206 ARG B CG  
23578 C CD  . ARG C 1206 ? 1.2143 1.5586 1.2473 -0.4423 -0.2720 0.2419  1206 ARG B CD  
23579 N NE  . ARG C 1206 ? 1.2935 1.6269 1.3000 -0.4397 -0.2494 0.2159  1206 ARG B NE  
23580 C CZ  . ARG C 1206 ? 1.3213 1.6979 1.3238 -0.4441 -0.2419 0.2045  1206 ARG B CZ  
23581 N NH1 . ARG C 1206 ? 1.3019 1.7412 1.3258 -0.4501 -0.2550 0.2173  1206 ARG B NH1 
23582 N NH2 . ARG C 1206 ? 1.3420 1.6984 1.3178 -0.4425 -0.2212 0.1798  1206 ARG B NH2 
23583 N N   . SER C 1207 ? 0.9870 1.3303 1.0719 -0.4424 -0.3610 0.3109  1207 SER B N   
23584 C CA  . SER C 1207 ? 0.9563 1.3161 1.0667 -0.4571 -0.3850 0.3368  1207 SER B CA  
23585 C C   . SER C 1207 ? 0.9550 1.2408 1.0523 -0.4472 -0.3941 0.3348  1207 SER B C   
23586 O O   . SER C 1207 ? 0.9587 1.2221 1.0705 -0.4548 -0.4048 0.3504  1207 SER B O   
23587 C CB  . SER C 1207 ? 0.9536 1.3679 1.0718 -0.4630 -0.3967 0.3434  1207 SER B CB  
23588 O OG  . SER C 1207 ? 0.9434 1.3928 1.0915 -0.4844 -0.4188 0.3721  1207 SER B OG  
23589 N N   . ILE C 1208 ? 0.9252 1.1725 0.9935 -0.4288 -0.3891 0.3150  1208 ILE B N   
23590 C CA  . ILE C 1208 ? 0.8693 1.0506 0.9215 -0.4183 -0.3979 0.3103  1208 ILE B CA  
23591 C C   . ILE C 1208 ? 0.8064 0.9349 0.8530 -0.4120 -0.3895 0.3067  1208 ILE B C   
23592 O O   . ILE C 1208 ? 0.7769 0.8692 0.8294 -0.4144 -0.4027 0.3161  1208 ILE B O   
23593 C CB  . ILE C 1208 ? 0.8577 1.0121 0.8777 -0.3975 -0.3910 0.2893  1208 ILE B CB  
23594 C CG1 . ILE C 1208 ? 0.8071 1.0190 0.8263 -0.3957 -0.3854 0.2849  1208 ILE B CG1 
23595 C CG2 . ILE C 1208 ? 0.8979 1.0216 0.9118 -0.3958 -0.4104 0.2924  1208 ILE B CG2 
23596 C CD1 . ILE C 1208 ? 0.7948 1.0023 0.7962 -0.3822 -0.3928 0.2777  1208 ILE B CD1 
23597 N N   . VAL C 1209 ? 0.7832 0.9086 0.8179 -0.4043 -0.3675 0.2928  1209 VAL B N   
23598 C CA  . VAL C 1209 ? 0.8368 0.9256 0.8685 -0.3995 -0.3576 0.2904  1209 VAL B CA  
23599 C C   . VAL C 1209 ? 0.9105 1.0235 0.9743 -0.4150 -0.3684 0.3141  1209 VAL B C   
23600 O O   . VAL C 1209 ? 0.9256 1.0010 0.9906 -0.4097 -0.3694 0.3180  1209 VAL B O   
23601 C CB  . VAL C 1209 ? 0.8311 0.9283 0.8500 -0.3956 -0.3334 0.2750  1209 VAL B CB  
23602 C CG1 . VAL C 1209 ? 0.8508 0.9134 0.8660 -0.3904 -0.3233 0.2729  1209 VAL B CG1 
23603 C CG2 . VAL C 1209 ? 0.8380 0.9119 0.8247 -0.3801 -0.3214 0.2532  1209 VAL B CG2 
23604 N N   . SER C 1210 ? 0.9638 1.1418 1.0530 -0.4328 -0.3755 0.3303  1210 SER B N   
23605 C CA  . SER C 1210 ? 1.0194 1.2230 1.1403 -0.4486 -0.3895 0.3574  1210 SER B CA  
23606 C C   . SER C 1210 ? 1.0773 1.2358 1.2001 -0.4488 -0.4109 0.3679  1210 SER B C   
23607 O O   . SER C 1210 ? 1.1155 1.2302 1.2403 -0.4433 -0.4150 0.3738  1210 SER B O   
23608 C CB  . SER C 1210 ? 1.0181 1.3015 1.1641 -0.4683 -0.3956 0.3740  1210 SER B CB  
23609 O OG  . SER C 1210 ? 1.0388 1.3365 1.2128 -0.4837 -0.4154 0.4032  1210 SER B OG  
23610 N N   . ALA C 1211 ? 1.0785 1.2477 1.1993 -0.4545 -0.4242 0.3690  1211 ALA B N   
23611 C CA  . ALA C 1211 ? 1.1010 1.2269 1.2196 -0.4568 -0.4445 0.3751  1211 ALA B CA  
23612 C C   . ALA C 1211 ? 1.1203 1.1704 1.2203 -0.4392 -0.4405 0.3633  1211 ALA B C   
23613 O O   . ALA C 1211 ? 1.1089 1.1297 1.2202 -0.4421 -0.4505 0.3769  1211 ALA B O   
23614 C CB  . ALA C 1211 ? 1.1190 1.2503 1.2216 -0.4541 -0.4502 0.3635  1211 ALA B CB  
23615 N N   . LEU C 1212 ? 1.1313 1.1508 1.2019 -0.4197 -0.4250 0.3382  1212 LEU B N   
23616 C CA  . LEU C 1212 ? 1.1657 1.1153 1.2139 -0.4010 -0.4205 0.3240  1212 LEU B CA  
23617 C C   . LEU C 1212 ? 1.1524 1.0904 1.2135 -0.3985 -0.4147 0.3333  1212 LEU B C   
23618 O O   . LEU C 1212 ? 1.1830 1.0722 1.2421 -0.3917 -0.4232 0.3361  1212 LEU B O   
23619 C CB  . LEU C 1212 ? 1.1454 1.0748 1.1618 -0.3817 -0.4008 0.2983  1212 LEU B CB  
23620 C CG  . LEU C 1212 ? 1.1418 1.0091 1.1350 -0.3618 -0.3906 0.2834  1212 LEU B CG  
23621 C CD1 . LEU C 1212 ? 1.1684 0.9865 1.1566 -0.3586 -0.4091 0.2849  1212 LEU B CD1 
23622 C CD2 . LEU C 1212 ? 1.1485 0.9976 1.1100 -0.3455 -0.3738 0.2612  1212 LEU B CD2 
23623 N N   . LYS C 1213 ? 1.0917 1.0768 1.1656 -0.4034 -0.4002 0.3376  1213 LYS B N   
23624 C CA  . LYS C 1213 ? 1.0706 1.0506 1.1520 -0.3973 -0.3896 0.3422  1213 LYS B CA  
23625 C C   . LYS C 1213 ? 1.1188 1.1035 1.2280 -0.4071 -0.4066 0.3688  1213 LYS B C   
23626 O O   . LYS C 1213 ? 1.1133 1.0785 1.2287 -0.3982 -0.4039 0.3756  1213 LYS B O   
23627 C CB  . LYS C 1213 ? 0.9719 1.0053 1.0584 -0.4026 -0.3701 0.3385  1213 LYS B CB  
23628 C CG  . LYS C 1213 ? 0.9534 0.9782 1.0382 -0.3929 -0.3543 0.3354  1213 LYS B CG  
23629 C CD  . LYS C 1213 ? 0.9565 1.0061 1.0272 -0.3936 -0.3317 0.3178  1213 LYS B CD  
23630 C CE  . LYS C 1213 ? 0.9603 1.0308 1.0389 -0.3932 -0.3166 0.3203  1213 LYS B CE  
23631 N NZ  . LYS C 1213 ? 0.9600 1.0247 1.0132 -0.3898 -0.2943 0.2970  1213 LYS B NZ  
23632 N N   . ARG C 1214 ? 1.1771 1.1886 1.3026 -0.4252 -0.4243 0.3845  1214 ARG B N   
23633 C CA  . ARG C 1214 ? 1.3001 1.3152 1.4516 -0.4377 -0.4422 0.4122  1214 ARG B CA  
23634 C C   . ARG C 1214 ? 1.3634 1.3028 1.5011 -0.4294 -0.4571 0.4084  1214 ARG B C   
23635 O O   . ARG C 1214 ? 1.3934 1.3049 1.5433 -0.4299 -0.4683 0.4252  1214 ARG B O   
23636 C CB  . ARG C 1214 ? 1.4160 1.4920 1.5886 -0.4623 -0.4548 0.4304  1214 ARG B CB  
23637 C CG  . ARG C 1214 ? 1.5840 1.6522 1.7777 -0.4793 -0.4789 0.4581  1214 ARG B CG  
23638 C CD  . ARG C 1214 ? 1.6786 1.8211 1.8956 -0.5049 -0.4887 0.4784  1214 ARG B CD  
23639 N NE  . ARG C 1214 ? 1.7421 1.9160 1.9452 -0.5057 -0.4831 0.4597  1214 ARG B NE  
23640 C CZ  . ARG C 1214 ? 1.7660 2.0156 1.9837 -0.5208 -0.4829 0.4682  1214 ARG B CZ  
23641 N NH1 . ARG C 1214 ? 1.7757 2.0798 2.0226 -0.5383 -0.4882 0.4958  1214 ARG B NH1 
23642 N NH2 . ARG C 1214 ? 1.7640 2.0368 1.9666 -0.5170 -0.4770 0.4497  1214 ARG B NH2 
23643 N N   . GLU C 1215 ? 1.3814 1.2851 1.4918 -0.4205 -0.4570 0.3855  1215 GLU B N   
23644 C CA  . GLU C 1215 ? 1.3860 1.2223 1.4823 -0.4160 -0.4733 0.3804  1215 GLU B CA  
23645 C C   . GLU C 1215 ? 1.3606 1.1352 1.4430 -0.3932 -0.4670 0.3709  1215 GLU B C   
23646 O O   . GLU C 1215 ? 1.4070 1.1272 1.4849 -0.3911 -0.4821 0.3731  1215 GLU B O   
23647 C CB  . GLU C 1215 ? 1.3735 1.1987 1.4466 -0.4156 -0.4777 0.3613  1215 GLU B CB  
23648 C CG  . GLU C 1215 ? 1.3711 1.2408 1.4615 -0.4411 -0.4952 0.3774  1215 GLU B CG  
23649 C CD  . GLU C 1215 ? 1.4292 1.2724 1.5354 -0.4581 -0.5188 0.3982  1215 GLU B CD  
23650 O OE1 . GLU C 1215 ? 1.4792 1.2550 1.5734 -0.4467 -0.5235 0.3921  1215 GLU B OE1 
23651 O OE2 . GLU C 1215 ? 1.4268 1.3147 1.5563 -0.4828 -0.5324 0.4205  1215 GLU B OE2 
23652 N N   . ALA C 1216 ? 1.2630 1.0489 1.3393 -0.3773 -0.4449 0.3610  1216 ALA B N   
23653 C CA  . ALA C 1216 ? 1.2140 0.9497 1.2724 -0.3524 -0.4343 0.3472  1216 ALA B CA  
23654 C C   . ALA C 1216 ? 1.2282 0.9330 1.3003 -0.3457 -0.4431 0.3634  1216 ALA B C   
23655 O O   . ALA C 1216 ? 1.2496 0.9732 1.3474 -0.3620 -0.4572 0.3884  1216 ALA B O   
23656 C CB  . ALA C 1216 ? 1.1667 0.9330 1.2191 -0.3424 -0.4092 0.3367  1216 ALA B CB  
23657 N N   . LEU C 1217 ? 1.2026 0.8605 1.2569 -0.3207 -0.4345 0.3496  1217 LEU B N   
23658 C CA  . LEU C 1217 ? 1.2081 0.8307 1.2713 -0.3074 -0.4405 0.3619  1217 LEU B CA  
23659 C C   . LEU C 1217 ? 1.1931 0.8160 1.2492 -0.2818 -0.4195 0.3534  1217 LEU B C   
23660 O O   . LEU C 1217 ? 1.1295 0.7631 1.1671 -0.2735 -0.4018 0.3339  1217 LEU B O   
23661 C CB  . LEU C 1217 ? 1.2412 0.7885 1.2868 -0.3020 -0.4588 0.3532  1217 LEU B CB  
23662 C CG  . LEU C 1217 ? 1.2381 0.7801 1.2768 -0.3239 -0.4754 0.3485  1217 LEU B CG  
23663 C CD1 . LEU C 1217 ? 1.2586 0.7440 1.2621 -0.3098 -0.4770 0.3197  1217 LEU B CD1 
23664 C CD2 . LEU C 1217 ? 1.2604 0.7945 1.3205 -0.3472 -0.4998 0.3733  1217 LEU B CD2 
23665 N N   . VAL C 1218 ? 1.2345 0.8449 1.3043 -0.2687 -0.4215 0.3688  1218 VAL B N   
23666 C CA  . VAL C 1218 ? 1.2516 0.8840 1.3226 -0.2480 -0.4013 0.3671  1218 VAL B CA  
23667 C C   . VAL C 1218 ? 1.2722 0.8548 1.3404 -0.2218 -0.4053 0.3703  1218 VAL B C   
23668 O O   . VAL C 1218 ? 1.2639 0.8130 1.3420 -0.2242 -0.4233 0.3856  1218 VAL B O   
23669 C CB  . VAL C 1218 ? 1.2939 0.9978 1.3963 -0.2613 -0.3962 0.3916  1218 VAL B CB  
23670 C CG1 . VAL C 1218 ? 1.2535 1.0175 1.3541 -0.2742 -0.3783 0.3815  1218 VAL B CG1 
23671 C CG2 . VAL C 1218 ? 1.3618 1.0717 1.4856 -0.2844 -0.4176 0.4148  1218 VAL B CG2 
23672 N N   . LYS C 1219 ? 1.3543 0.9316 1.4080 -0.1964 -0.3881 0.3561  1219 LYS B N   
23673 C CA  . LYS C 1219 ? 1.5222 1.0520 1.5701 -0.1666 -0.3901 0.3563  1219 LYS B CA  
23674 C C   . LYS C 1219 ? 1.5993 1.1836 1.6671 -0.1527 -0.3742 0.3719  1219 LYS B C   
23675 O O   . LYS C 1219 ? 1.5967 1.2311 1.6622 -0.1533 -0.3545 0.3639  1219 LYS B O   
23676 C CB  . LYS C 1219 ? 1.6502 1.1224 1.6609 -0.1444 -0.3851 0.3247  1219 LYS B CB  
23677 C CG  . LYS C 1219 ? 2.4614 1.8490 2.4528 -0.1395 -0.4062 0.3136  1219 LYS B CG  
23678 C CD  . LYS C 1219 ? 2.3005 1.6526 2.2563 -0.1386 -0.4055 0.2820  1219 LYS B CD  
23679 C CE  . LYS C 1219 ? 2.1280 1.4182 2.0523 -0.1063 -0.4029 0.2576  1219 LYS B CE  
23680 N NZ  . LYS C 1219 ? 2.1166 1.3870 2.0077 -0.1072 -0.4000 0.2292  1219 LYS B NZ  
23681 N N   . GLY C 1220 ? 1.6641 1.2388 1.7513 -0.1413 -0.3833 0.3951  1220 GLY B N   
23682 C CA  . GLY C 1220 ? 1.6556 1.2806 1.7633 -0.1245 -0.3708 0.4135  1220 GLY B CA  
23683 C C   . GLY C 1220 ? 1.6466 1.3581 1.7842 -0.1502 -0.3660 0.4357  1220 GLY B C   
23684 O O   . GLY C 1220 ? 1.6135 1.3561 1.7502 -0.1775 -0.3640 0.4286  1220 GLY B O   
23685 N N   . ASN C 1221 ? 1.6548 1.4070 1.8186 -0.1408 -0.3643 0.4627  1221 ASN B N   
23686 C CA  . ASN C 1221 ? 1.6142 1.4542 1.8064 -0.1652 -0.3598 0.4839  1221 ASN B CA  
23687 C C   . ASN C 1221 ? 1.5314 1.4446 1.7322 -0.1560 -0.3380 0.4852  1221 ASN B C   
23688 O O   . ASN C 1221 ? 1.5482 1.4680 1.7568 -0.1281 -0.3333 0.4970  1221 ASN B O   
23689 C CB  . ASN C 1221 ? 1.6583 1.5074 1.8791 -0.1722 -0.3767 0.5198  1221 ASN B CB  
23690 C CG  . ASN C 1221 ? 1.6105 1.5552 1.8596 -0.1965 -0.3715 0.5408  1221 ASN B CG  
23691 O OD1 . ASN C 1221 ? 1.5960 1.5902 1.8673 -0.1861 -0.3671 0.5648  1221 ASN B OD1 
23692 N ND2 . ASN C 1221 ? 1.5815 1.5559 1.8286 -0.2277 -0.3710 0.5307  1221 ASN B ND2 
23693 N N   . PRO C 1222 ? 1.4232 1.3945 1.6235 -0.1799 -0.3250 0.4744  1222 PRO B N   
23694 C CA  . PRO C 1222 ? 1.3743 1.3497 1.5685 -0.2120 -0.3294 0.4636  1222 PRO B CA  
23695 C C   . PRO C 1222 ? 1.3818 1.2863 1.5418 -0.2064 -0.3299 0.4329  1222 PRO B C   
23696 O O   . PRO C 1222 ? 1.4465 1.2984 1.5897 -0.1788 -0.3289 0.4223  1222 PRO B O   
23697 C CB  . PRO C 1222 ? 1.3175 1.3734 1.5171 -0.2296 -0.3103 0.4582  1222 PRO B CB  
23698 C CG  . PRO C 1222 ? 1.3236 1.4209 1.5339 -0.2087 -0.2970 0.4680  1222 PRO B CG  
23699 C CD  . PRO C 1222 ? 1.3806 1.4130 1.5813 -0.1739 -0.3027 0.4680  1222 PRO B CD  
23700 N N   . PRO C 1223 ? 1.3225 1.2280 1.4716 -0.2304 -0.3309 0.4185  1223 PRO B N   
23701 C CA  . PRO C 1223 ? 1.2541 1.1012 1.3698 -0.2239 -0.3288 0.3895  1223 PRO B CA  
23702 C C   . PRO C 1223 ? 1.1821 1.0250 1.2795 -0.2015 -0.3096 0.3726  1223 PRO B C   
23703 O O   . PRO C 1223 ? 1.1032 1.0043 1.2056 -0.2085 -0.2920 0.3716  1223 PRO B O   
23704 C CB  . PRO C 1223 ? 1.2096 1.0897 1.3201 -0.2513 -0.3233 0.3787  1223 PRO B CB  
23705 C CG  . PRO C 1223 ? 1.2279 1.1512 1.3665 -0.2728 -0.3348 0.4020  1223 PRO B CG  
23706 C CD  . PRO C 1223 ? 1.2801 1.2402 1.4447 -0.2622 -0.3333 0.4270  1223 PRO B CD  
23707 N N   . ILE C 1224 ? 1.2015 0.9792 1.2784 -0.1760 -0.3133 0.3601  1224 ILE B N   
23708 C CA  . ILE C 1224 ? 1.1853 0.9484 1.2354 -0.1581 -0.2961 0.3370  1224 ILE B CA  
23709 C C   . ILE C 1224 ? 1.1991 0.9102 1.2179 -0.1619 -0.2991 0.3123  1224 ILE B C   
23710 O O   . ILE C 1224 ? 1.1949 0.9105 1.1918 -0.1601 -0.2825 0.2936  1224 ILE B O   
23711 C CB  . ILE C 1224 ? 1.1807 0.9192 1.2270 -0.1237 -0.2934 0.3378  1224 ILE B CB  
23712 C CG1 . ILE C 1224 ? 1.2039 1.0020 1.2828 -0.1205 -0.2903 0.3648  1224 ILE B CG1 
23713 C CG2 . ILE C 1224 ? 1.1437 0.8775 1.1624 -0.1085 -0.2740 0.3144  1224 ILE B CG2 
23714 C CD1 . ILE C 1224 ? 1.2443 1.0556 1.3224 -0.0883 -0.2772 0.3659  1224 ILE B CD1 
23715 N N   . TYR C 1225 ? 1.1822 0.8487 1.1997 -0.1688 -0.3200 0.3138  1225 TYR B N   
23716 C CA  . TYR C 1225 ? 1.1700 0.7928 1.1611 -0.1749 -0.3263 0.2934  1225 TYR B CA  
23717 C C   . TYR C 1225 ? 1.1272 0.7627 1.1323 -0.2026 -0.3416 0.3038  1225 TYR B C   
23718 O O   . TYR C 1225 ? 1.1418 0.7809 1.1700 -0.2101 -0.3565 0.3243  1225 TYR B O   
23719 C CB  . TYR C 1225 ? 1.2386 0.7867 1.2098 -0.1539 -0.3396 0.2819  1225 TYR B CB  
23720 C CG  . TYR C 1225 ? 1.2756 0.8033 1.2296 -0.1225 -0.3267 0.2694  1225 TYR B CG  
23721 C CD1 . TYR C 1225 ? 1.2751 0.8108 1.2052 -0.1151 -0.3079 0.2503  1225 TYR B CD1 
23722 C CD2 . TYR C 1225 ? 1.3280 0.8296 1.2891 -0.0995 -0.3328 0.2775  1225 TYR B CD2 
23723 C CE1 . TYR C 1225 ? 1.3133 0.8371 1.2280 -0.0862 -0.2954 0.2398  1225 TYR B CE1 
23724 C CE2 . TYR C 1225 ? 1.3689 0.8564 1.3142 -0.0682 -0.3203 0.2658  1225 TYR B CE2 
23725 C CZ  . TYR C 1225 ? 1.3520 0.8536 1.2747 -0.0621 -0.3015 0.2470  1225 TYR B CZ  
23726 O OH  . TYR C 1225 ? 1.3667 0.8597 1.2740 -0.0312 -0.2889 0.2362  1225 TYR B OH  
23727 N N   . ARG C 1226 ? 1.1174 0.7575 1.1072 -0.2164 -0.3382 0.2901  1226 ARG B N   
23728 C CA  . ARG C 1226 ? 1.1753 0.8205 1.1727 -0.2394 -0.3540 0.2959  1226 ARG B CA  
23729 C C   . ARG C 1226 ? 1.2270 0.8251 1.1932 -0.2352 -0.3589 0.2738  1226 ARG B C   
23730 O O   . ARG C 1226 ? 1.2554 0.8352 1.1960 -0.2195 -0.3447 0.2550  1226 ARG B O   
23731 C CB  . ARG C 1226 ? 1.1901 0.9002 1.2001 -0.2607 -0.3431 0.3010  1226 ARG B CB  
23732 C CG  . ARG C 1226 ? 1.2037 0.9297 1.2213 -0.2837 -0.3571 0.3062  1226 ARG B CG  
23733 C CD  . ARG C 1226 ? 1.1477 0.9380 1.1759 -0.3024 -0.3450 0.3091  1226 ARG B CD  
23734 N NE  . ARG C 1226 ? 1.1095 0.9431 1.1526 -0.3017 -0.3295 0.3172  1226 ARG B NE  
23735 C CZ  . ARG C 1226 ? 1.0314 0.9046 1.1050 -0.3092 -0.3347 0.3406  1226 ARG B CZ  
23736 N NH1 . ARG C 1226 ? 0.9953 0.8683 1.0888 -0.3193 -0.3555 0.3601  1226 ARG B NH1 
23737 N NH2 . ARG C 1226 ? 0.9797 0.8950 1.0634 -0.3076 -0.3190 0.3453  1226 ARG B NH2 
23738 N N   . PHE C 1227 ? 1.2291 0.8116 1.1974 -0.2496 -0.3787 0.2769  1227 PHE B N   
23739 C CA  . PHE C 1227 ? 1.2129 0.7644 1.1543 -0.2500 -0.3847 0.2582  1227 PHE B CA  
23740 C C   . PHE C 1227 ? 1.1996 0.7583 1.1560 -0.2723 -0.4066 0.2705  1227 PHE B C   
23741 O O   . PHE C 1227 ? 1.2020 0.7713 1.1846 -0.2829 -0.4182 0.2916  1227 PHE B O   
23742 C CB  . PHE C 1227 ? 1.2695 0.7560 1.1859 -0.2290 -0.3906 0.2421  1227 PHE B CB  
23743 C CG  . PHE C 1227 ? 1.3209 0.7746 1.2511 -0.2249 -0.4063 0.2541  1227 PHE B CG  
23744 C CD1 . PHE C 1227 ? 1.3388 0.7615 1.2717 -0.2381 -0.4302 0.2586  1227 PHE B CD1 
23745 C CD2 . PHE C 1227 ? 1.3214 0.7768 1.2622 -0.2082 -0.3970 0.2620  1227 PHE B CD2 
23746 C CE1 . PHE C 1227 ? 1.3521 0.7386 1.2961 -0.2349 -0.4444 0.2701  1227 PHE B CE1 
23747 C CE2 . PHE C 1227 ? 1.3335 0.7558 1.2857 -0.2017 -0.4106 0.2736  1227 PHE B CE2 
23748 C CZ  . PHE C 1227 ? 1.3575 0.7417 1.3106 -0.2153 -0.4344 0.2777  1227 PHE B CZ  
23749 N N   . TRP C 1228 ? 1.2002 0.7548 1.1407 -0.2796 -0.4127 0.2594  1228 TRP B N   
23750 C CA  . TRP C 1228 ? 1.2258 0.7828 1.1779 -0.3007 -0.4362 0.2700  1228 TRP B CA  
23751 C C   . TRP C 1228 ? 1.4939 0.9906 1.4252 -0.2966 -0.4543 0.2575  1228 TRP B C   
23752 O O   . TRP C 1228 ? 1.5125 0.9702 1.4150 -0.2772 -0.4480 0.2366  1228 TRP B O   
23753 C CB  . TRP C 1228 ? 1.1787 0.7871 1.1351 -0.3169 -0.4346 0.2717  1228 TRP B CB  
23754 C CG  . TRP C 1228 ? 1.1476 0.8161 1.1226 -0.3238 -0.4183 0.2816  1228 TRP B CG  
23755 C CD1 . TRP C 1228 ? 1.1380 0.8632 1.1362 -0.3447 -0.4229 0.2972  1228 TRP B CD1 
23756 C CD2 . TRP C 1228 ? 1.1117 0.7920 1.0823 -0.3112 -0.3949 0.2756  1228 TRP B CD2 
23757 N NE1 . TRP C 1228 ? 1.0965 0.8656 1.1038 -0.3454 -0.4039 0.2995  1228 TRP B NE1 
23758 C CE2 . TRP C 1228 ? 1.0905 0.8327 1.0814 -0.3262 -0.3868 0.2866  1228 TRP B CE2 
23759 C CE3 . TRP C 1228 ? 1.0919 0.7396 1.0433 -0.2898 -0.3801 0.2619  1228 TRP B CE3 
23760 C CZ2 . TRP C 1228 ? 1.0661 0.8355 1.0580 -0.3223 -0.3651 0.2836  1228 TRP B CZ2 
23761 C CZ3 . TRP C 1228 ? 1.0746 0.7520 1.0285 -0.2862 -0.3585 0.2608  1228 TRP B CZ3 
23762 C CH2 . TRP C 1228 ? 1.0572 0.7936 1.0308 -0.3032 -0.3514 0.2712  1228 TRP B CH2 
23763 N N   . LYS C 1229 ? 1.5181 1.0087 1.4641 -0.3165 -0.4769 0.2710  1229 LYS B N   
23764 C CA  . LYS C 1229 ? 1.5908 1.0279 1.5190 -0.3185 -0.4962 0.2603  1229 LYS B CA  
23765 C C   . LYS C 1229 ? 1.6899 1.1582 1.6138 -0.3361 -0.5055 0.2576  1229 LYS B C   
23766 O O   . LYS C 1229 ? 1.6587 1.1856 1.6011 -0.3496 -0.5016 0.2704  1229 LYS B O   
23767 C CB  . LYS C 1229 ? 1.6034 1.0166 1.5524 -0.3331 -0.5155 0.2798  1229 LYS B CB  
23768 C CG  . LYS C 1229 ? 1.6740 1.0101 1.6045 -0.3191 -0.5251 0.2677  1229 LYS B CG  
23769 C CD  . LYS C 1229 ? 2.1351 1.4451 2.0884 -0.3303 -0.5407 0.2909  1229 LYS B CD  
23770 C CE  . LYS C 1229 ? 2.1004 1.3966 2.0604 -0.3623 -0.5680 0.3013  1229 LYS B CE  
23771 N NZ  . LYS C 1229 ? 2.0863 1.3257 2.0157 -0.3643 -0.5832 0.2774  1229 LYS B NZ  
23772 N N   . ASP C 1230 ? 1.8220 1.2550 1.7216 -0.3354 -0.5177 0.2408  1230 ASP B N   
23773 C CA  . ASP C 1230 ? 1.9188 1.3839 1.8109 -0.3479 -0.5255 0.2363  1230 ASP B CA  
23774 C C   . ASP C 1230 ? 1.9787 1.4848 1.8979 -0.3800 -0.5444 0.2582  1230 ASP B C   
23775 O O   . ASP C 1230 ? 1.9431 1.5081 1.8717 -0.3886 -0.5409 0.2647  1230 ASP B O   
23776 C CB  . ASP C 1230 ? 2.0003 1.4188 1.8599 -0.3403 -0.5357 0.2136  1230 ASP B CB  
23777 C CG  . ASP C 1230 ? 2.0445 1.4973 1.8990 -0.3559 -0.5483 0.2119  1230 ASP B CG  
23778 O OD1 . ASP C 1230 ? 2.0301 1.5430 1.8999 -0.3634 -0.5420 0.2233  1230 ASP B OD1 
23779 O OD2 . ASP C 1230 ? 2.1026 1.5255 1.9375 -0.3604 -0.5642 0.1989  1230 ASP B OD2 
23780 N N   . ASN C 1231 ? 2.1275 1.6003 2.0571 -0.3969 -0.5648 0.2687  1231 ASN B N   
23781 C CA  . ASN C 1231 ? 2.2277 1.7344 2.1866 -0.4293 -0.5828 0.2945  1231 ASN B CA  
23782 C C   . ASN C 1231 ? 2.2597 1.8397 2.2464 -0.4357 -0.5706 0.3141  1231 ASN B C   
23783 O O   . ASN C 1231 ? 2.2286 1.8308 2.2108 -0.4162 -0.5483 0.3065  1231 ASN B O   
23784 C CB  . ASN C 1231 ? 2.3240 1.7785 2.2942 -0.4371 -0.5957 0.3076  1231 ASN B CB  
23785 C CG  . ASN C 1231 ? 2.3621 1.8298 2.3542 -0.4260 -0.5805 0.3244  1231 ASN B CG  
23786 O OD1 . ASN C 1231 ? 2.3894 1.8219 2.3699 -0.3994 -0.5662 0.3133  1231 ASN B OD1 
23787 N ND2 . ASN C 1231 ? 2.3478 1.8719 2.3715 -0.4466 -0.5834 0.3516  1231 ASN B ND2 
23788 N N   . LEU C 1232 ? 2.3300 1.9466 2.3450 -0.4640 -0.5851 0.3398  1232 LEU B N   
23789 C CA  . LEU C 1232 ? 2.3104 1.9978 2.3534 -0.4720 -0.5753 0.3601  1232 LEU B CA  
23790 C C   . LEU C 1232 ? 2.4500 2.1443 2.5233 -0.4963 -0.5904 0.3908  1232 LEU B C   
23791 O O   . LEU C 1232 ? 2.5001 2.2071 2.5835 -0.5238 -0.6110 0.4044  1232 LEU B O   
23792 C CB  . LEU C 1232 ? 2.1772 1.9316 2.2223 -0.4828 -0.5761 0.3595  1232 LEU B CB  
23793 C CG  . LEU C 1232 ? 2.0078 1.8406 2.0842 -0.5002 -0.5740 0.3836  1232 LEU B CG  
23794 C CD1 . LEU C 1232 ? 1.9226 1.7915 1.9953 -0.4798 -0.5481 0.3733  1232 LEU B CD1 
23795 C CD2 . LEU C 1232 ? 1.9577 1.8400 2.0412 -0.5237 -0.5905 0.3916  1232 LEU B CD2 
23796 N N   . GLN C 1233 ? 2.4977 2.1851 2.5851 -0.4865 -0.5804 0.4029  1233 GLN B N   
23797 C CA  . GLN C 1233 ? 2.5970 2.2892 2.7131 -0.5058 -0.5927 0.4347  1233 GLN B CA  
23798 C C   . GLN C 1233 ? 2.7866 2.4270 2.9032 -0.5283 -0.6196 0.4457  1233 GLN B C   
23799 O O   . GLN C 1233 ? 2.7671 2.4204 2.9086 -0.5506 -0.6323 0.4755  1233 GLN B O   
23800 C CB  . GLN C 1233 ? 2.6545 2.4379 2.8000 -0.5241 -0.5894 0.4579  1233 GLN B CB  
23801 C CG  . GLN C 1233 ? 2.7546 2.5908 2.9009 -0.5443 -0.5984 0.4569  1233 GLN B CG  
23802 C CD  . GLN C 1233 ? 2.7947 2.7238 2.9685 -0.5603 -0.5943 0.4779  1233 GLN B CD  
23803 O OE1 . GLN C 1233 ? 2.8312 2.7848 3.0315 -0.5773 -0.6013 0.5070  1233 GLN B OE1 
23804 N NE2 . GLN C 1233 ? 2.7809 2.7622 2.9472 -0.5544 -0.5831 0.4635  1233 GLN B NE2 
23805 N N   . HIS C 1234 ? 2.8624 2.4452 2.9508 -0.5239 -0.6283 0.4219  1234 HIS B N   
23806 C CA  . HIS C 1234 ? 2.9331 2.4555 3.0160 -0.5444 -0.6532 0.4265  1234 HIS B CA  
23807 C C   . HIS C 1234 ? 3.0433 2.4810 3.1152 -0.5239 -0.6523 0.4213  1234 HIS B C   
23808 O O   . HIS C 1234 ? 3.0855 2.4560 3.1478 -0.5349 -0.6707 0.4208  1234 HIS B O   
23809 C CB  . HIS C 1234 ? 2.9070 2.4147 2.9642 -0.5512 -0.6638 0.4021  1234 HIS B CB  
23810 C CG  . HIS C 1234 ? 2.8291 2.4204 2.8962 -0.5695 -0.6658 0.4073  1234 HIS B CG  
23811 N ND1 . HIS C 1234 ? 2.8050 2.4528 2.9010 -0.6022 -0.6786 0.4372  1234 HIS B ND1 
23812 C CD2 . HIS C 1234 ? 2.7802 2.4104 2.8321 -0.5579 -0.6560 0.3875  1234 HIS B CD2 
23813 C CE1 . HIS C 1234 ? 2.7601 2.4801 2.8585 -0.6093 -0.6766 0.4343  1234 HIS B CE1 
23814 N NE2 . HIS C 1234 ? 2.7468 2.4557 2.8184 -0.5820 -0.6629 0.4045  1234 HIS B NE2 
23815 N N   . LYS C 1235 ? 3.0921 2.5344 3.1632 -0.4930 -0.6299 0.4152  1235 LYS B N   
23816 C CA  . LYS C 1235 ? 3.2097 2.5974 3.2811 -0.4712 -0.6247 0.4198  1235 LYS B CA  
23817 C C   . LYS C 1235 ? 3.4019 2.6960 3.4574 -0.4734 -0.6435 0.4150  1235 LYS B C   
23818 O O   . LYS C 1235 ? 3.4563 2.7183 3.5263 -0.4765 -0.6513 0.4376  1235 LYS B O   
23819 C CB  . LYS C 1235 ? 3.1513 2.5873 3.2581 -0.4791 -0.6212 0.4552  1235 LYS B CB  
23820 C CG  . LYS C 1235 ? 3.0412 2.5691 3.1636 -0.4773 -0.6023 0.4593  1235 LYS B CG  
23821 C CD  . LYS C 1235 ? 2.9807 2.5074 3.0907 -0.4421 -0.5771 0.4401  1235 LYS B CD  
23822 C CE  . LYS C 1235 ? 2.8830 2.4960 3.0073 -0.4428 -0.5588 0.4438  1235 LYS B CE  
23823 N NZ  . LYS C 1235 ? 2.8369 2.4886 2.9522 -0.4559 -0.5596 0.4303  1235 LYS B NZ  
23824 N N   . ASP C 1236 ? 3.5282 2.7771 3.5532 -0.4716 -0.6508 0.3861  1236 ASP B N   
23825 C CA  . ASP C 1236 ? 3.7052 2.8578 3.7095 -0.4662 -0.6645 0.3748  1236 ASP B CA  
23826 C C   . ASP C 1236 ? 3.7763 2.8933 3.7724 -0.4246 -0.6456 0.3657  1236 ASP B C   
23827 O O   . ASP C 1236 ? 3.8311 2.8747 3.8196 -0.4127 -0.6522 0.3661  1236 ASP B O   
23828 C CB  . ASP C 1236 ? 3.7702 2.8868 3.7417 -0.4717 -0.6752 0.3430  1236 ASP B CB  
23829 C CG  . ASP C 1236 ? 3.8933 2.9138 3.8463 -0.4797 -0.6959 0.3352  1236 ASP B CG  
23830 O OD1 . ASP C 1236 ? 3.9411 2.9058 3.8957 -0.4624 -0.6943 0.3426  1236 ASP B OD1 
23831 O OD2 . ASP C 1236 ? 3.9373 2.9382 3.8736 -0.5030 -0.7138 0.3215  1236 ASP B OD2 
23832 N N   . SER C 1237 ? 3.7762 2.9479 3.7743 -0.4029 -0.6219 0.3583  1237 SER B N   
23833 C CA  . SER C 1237 ? 3.8018 2.9631 3.7971 -0.3653 -0.6009 0.3530  1237 SER B CA  
23834 C C   . SER C 1237 ? 3.8562 2.9434 3.8161 -0.3353 -0.5973 0.3209  1237 SER B C   
23835 O O   . SER C 1237 ? 3.9070 2.9768 3.8631 -0.3031 -0.5822 0.3168  1237 SER B O   
23836 C CB  . SER C 1237 ? 3.8164 2.9769 3.8395 -0.3630 -0.6017 0.3853  1237 SER B CB  
23837 O OG  . SER C 1237 ? 3.7893 2.9587 3.8127 -0.3278 -0.5797 0.3816  1237 SER B OG  
23838 N N   . SER C 1238 ? 3.8229 2.8704 3.7569 -0.3457 -0.6112 0.2984  1238 SER B N   
23839 C CA  . SER C 1238 ? 3.7974 2.7852 3.6947 -0.3177 -0.6064 0.2642  1238 SER B CA  
23840 C C   . SER C 1238 ? 3.6659 2.7013 3.5515 -0.2949 -0.5820 0.2465  1238 SER B C   
23841 O O   . SER C 1238 ? 3.5694 2.6274 3.4394 -0.3027 -0.5819 0.2302  1238 SER B O   
23842 C CB  . SER C 1238 ? 3.9294 2.8676 3.8015 -0.3374 -0.6284 0.2445  1238 SER B CB  
23843 O OG  . SER C 1238 ? 3.9466 2.9419 3.8203 -0.3621 -0.6329 0.2429  1238 SER B OG  
23844 N N   . VAL C 1239 ? 3.4472 2.4998 3.3411 -0.2677 -0.5614 0.2515  1239 VAL B N   
23845 C CA  . VAL C 1239 ? 3.3482 2.4323 3.2273 -0.2431 -0.5373 0.2334  1239 VAL B CA  
23846 C C   . VAL C 1239 ? 3.3475 2.3684 3.1980 -0.2089 -0.5316 0.2095  1239 VAL B C   
23847 O O   . VAL C 1239 ? 3.3053 2.3421 3.1517 -0.1811 -0.5104 0.2037  1239 VAL B O   
23848 C CB  . VAL C 1239 ? 3.3162 2.4672 3.2229 -0.2373 -0.5174 0.2540  1239 VAL B CB  
23849 C CG1 . VAL C 1239 ? 3.3057 2.5115 3.2440 -0.2702 -0.5260 0.2813  1239 VAL B CG1 
23850 C CG2 . VAL C 1239 ? 3.3772 2.5049 3.2941 -0.2135 -0.5112 0.2650  1239 VAL B CG2 
23851 N N   . PRO C 1240 ? 3.4088 2.3597 3.2378 -0.2121 -0.5506 0.1942  1240 PRO B N   
23852 C CA  . PRO C 1240 ? 3.4631 2.3386 3.2716 -0.1846 -0.5529 0.1786  1240 PRO B CA  
23853 C C   . PRO C 1240 ? 3.3703 2.2507 3.1601 -0.1450 -0.5290 0.1595  1240 PRO B C   
23854 O O   . PRO C 1240 ? 3.4345 2.2800 3.1902 -0.1295 -0.5280 0.1298  1240 PRO B O   
23855 C CB  . PRO C 1240 ? 3.5557 2.3742 3.3347 -0.1992 -0.5739 0.1549  1240 PRO B CB  
23856 C CG  . PRO C 1240 ? 3.5150 2.3897 3.2910 -0.2199 -0.5731 0.1498  1240 PRO B CG  
23857 C CD  . PRO C 1240 ? 3.4476 2.3919 3.2620 -0.2391 -0.5681 0.1822  1240 PRO B CD  
23858 N N   . ASN C 1241 ? 3.1909 2.1175 3.0024 -0.1299 -0.5101 0.1768  1241 ASN B N   
23859 C CA  . ASN C 1241 ? 3.0468 1.9844 2.8432 -0.0940 -0.4869 0.1616  1241 ASN B CA  
23860 C C   . ASN C 1241 ? 2.7558 1.7067 2.5228 -0.0917 -0.4786 0.1353  1241 ASN B C   
23861 O O   . ASN C 1241 ? 2.7279 1.6607 2.4687 -0.0627 -0.4664 0.1132  1241 ASN B O   
23862 C CB  . ASN C 1241 ? 3.2326 2.1006 3.0112 -0.0611 -0.4890 0.1484  1241 ASN B CB  
23863 C CG  . ASN C 1241 ? 3.3526 2.2046 3.1584 -0.0559 -0.4946 0.1756  1241 ASN B CG  
23864 O OD1 . ASN C 1241 ? 3.3378 2.2470 3.1767 -0.0660 -0.4881 0.2041  1241 ASN B OD1 
23865 N ND2 . ASN C 1241 ? 3.4570 2.2298 3.2475 -0.0387 -0.5066 0.1664  1241 ASN B ND2 
23866 N N   . THR C 1242 ? 2.5211 1.5044 2.2915 -0.1210 -0.4851 0.1381  1242 THR B N   
23867 C CA  . THR C 1242 ? 2.2982 1.2906 2.0395 -0.1185 -0.4791 0.1147  1242 THR B CA  
23868 C C   . THR C 1242 ? 1.9739 1.0272 1.7257 -0.1424 -0.4752 0.1239  1242 THR B C   
23869 O O   . THR C 1242 ? 1.8927 0.9618 1.6629 -0.1716 -0.4905 0.1387  1242 THR B O   
23870 C CB  . THR C 1242 ? 2.3913 1.3238 2.1035 -0.1227 -0.4990 0.0918  1242 THR B CB  
23871 O OG1 . THR C 1242 ? 2.4299 1.3500 2.1594 -0.1554 -0.5228 0.1064  1242 THR B OG1 
23872 C CG2 . THR C 1242 ? 2.4567 1.3247 2.1466 -0.0918 -0.4989 0.0728  1242 THR B CG2 
23873 N N   . GLY C 1243 ? 1.7997 0.8854 1.5376 -0.1283 -0.4543 0.1142  1243 GLY B N   
23874 C CA  . GLY C 1243 ? 1.6371 0.7755 1.3786 -0.1443 -0.4468 0.1192  1243 GLY B CA  
23875 C C   . GLY C 1243 ? 1.5763 0.7012 1.2945 -0.1552 -0.4605 0.1037  1243 GLY B C   
23876 O O   . GLY C 1243 ? 1.6100 0.6860 1.3116 -0.1551 -0.4779 0.0900  1243 GLY B O   
23877 N N   . THR C 1244 ? 1.4601 0.6282 1.1757 -0.1639 -0.4527 0.1053  1244 THR B N   
23878 C CA  . THR C 1244 ? 1.4491 0.6185 1.1517 -0.1794 -0.4682 0.0980  1244 THR B CA  
23879 C C   . THR C 1244 ? 1.5071 0.7229 1.2038 -0.1801 -0.4540 0.0991  1244 THR B C   
23880 O O   . THR C 1244 ? 1.4885 0.7452 1.2057 -0.1853 -0.4408 0.1143  1244 THR B O   
23881 C CB  . THR C 1244 ? 1.3851 0.5671 1.1155 -0.2096 -0.4889 0.1163  1244 THR B CB  
23882 O OG1 . THR C 1244 ? 1.4181 0.5464 1.1428 -0.2154 -0.5104 0.1096  1244 THR B OG1 
23883 C CG2 . THR C 1244 ? 1.3498 0.5706 1.0781 -0.2270 -0.4955 0.1180  1244 THR B CG2 
23884 N N   . ALA C 1245 ? 1.5972 0.8062 1.2651 -0.1752 -0.4575 0.0831  1245 ALA B N   
23885 C CA  . ALA C 1245 ? 1.5972 0.8458 1.2563 -0.1752 -0.4466 0.0842  1245 ALA B CA  
23886 C C   . ALA C 1245 ? 1.5715 0.8699 1.2613 -0.1961 -0.4469 0.1053  1245 ALA B C   
23887 O O   . ALA C 1245 ? 1.5113 0.8411 1.2038 -0.1913 -0.4276 0.1110  1245 ALA B O   
23888 C CB  . ALA C 1245 ? 1.6230 0.8624 1.2549 -0.1754 -0.4603 0.0695  1245 ALA B CB  
23889 N N   . ARG C 1246 ? 1.6163 0.9217 1.3277 -0.2198 -0.4686 0.1162  1246 ARG B N   
23890 C CA  . ARG C 1246 ? 1.5907 0.9474 1.3318 -0.2407 -0.4708 0.1364  1246 ARG B CA  
23891 C C   . ARG C 1246 ? 1.5378 0.9098 1.3087 -0.2450 -0.4612 0.1533  1246 ARG B C   
23892 O O   . ARG C 1246 ? 1.4823 0.8998 1.2704 -0.2517 -0.4501 0.1655  1246 ARG B O   
23893 C CB  . ARG C 1246 ? 1.6098 0.9761 1.3626 -0.2663 -0.4973 0.1435  1246 ARG B CB  
23894 C CG  . ARG C 1246 ? 1.5831 1.0115 1.3572 -0.2830 -0.4976 0.1598  1246 ARG B CG  
23895 C CD  . ARG C 1246 ? 1.6465 1.0905 1.4304 -0.3084 -0.5234 0.1667  1246 ARG B CD  
23896 N NE  . ARG C 1246 ? 1.7685 1.1915 1.5226 -0.3033 -0.5342 0.1485  1246 ARG B NE  
23897 C CZ  . ARG C 1246 ? 1.8369 1.2972 1.5841 -0.3094 -0.5419 0.1476  1246 ARG B CZ  
23898 N NH1 . ARG C 1246 ? 1.8285 1.3477 1.5966 -0.3201 -0.5398 0.1635  1246 ARG B NH1 
23899 N NH2 . ARG C 1246 ? 1.8861 1.3279 1.6051 -0.3041 -0.5518 0.1307  1246 ARG B NH2 
23900 N N   . MET C 1247 ? 1.5303 0.8649 1.3064 -0.2403 -0.4654 0.1537  1247 MET B N   
23901 C CA  . MET C 1247 ? 1.4666 0.8154 1.2671 -0.2387 -0.4538 0.1684  1247 MET B CA  
23902 C C   . MET C 1247 ? 1.4304 0.8068 1.2245 -0.2244 -0.4267 0.1653  1247 MET B C   
23903 O O   . MET C 1247 ? 1.3839 0.8066 1.1974 -0.2351 -0.4176 0.1783  1247 MET B O   
23904 C CB  . MET C 1247 ? 1.4767 0.7757 1.2738 -0.2249 -0.4572 0.1639  1247 MET B CB  
23905 C CG  . MET C 1247 ? 1.4452 0.7600 1.2724 -0.2274 -0.4522 0.1836  1247 MET B CG  
23906 S SD  . MET C 1247 ? 1.6563 0.9084 1.4862 -0.2264 -0.4736 0.1852  1247 MET B SD  
23907 C CE  . MET C 1247 ? 1.4377 0.6771 1.2598 -0.2527 -0.5006 0.1810  1247 MET B CE  
23908 N N   . VAL C 1248 ? 1.4460 0.7937 1.2120 -0.2011 -0.4137 0.1477  1248 VAL B N   
23909 C CA  . VAL C 1248 ? 1.4059 0.7744 1.1614 -0.1884 -0.3877 0.1438  1248 VAL B CA  
23910 C C   . VAL C 1248 ? 1.3140 0.7185 1.0667 -0.1981 -0.3822 0.1460  1248 VAL B C   
23911 O O   . VAL C 1248 ? 1.2735 0.7059 1.0294 -0.1978 -0.3632 0.1497  1248 VAL B O   
23912 C CB  . VAL C 1248 ? 1.1098 0.4430 0.8306 -0.1623 -0.3753 0.1240  1248 VAL B CB  
23913 C CG1 . VAL C 1248 ? 1.0421 0.3983 0.7499 -0.1541 -0.3494 0.1214  1248 VAL B CG1 
23914 C CG2 . VAL C 1248 ? 1.1476 0.4498 0.8709 -0.1477 -0.3758 0.1212  1248 VAL B CG2 
23915 N N   . GLU C 1249 ? 1.3095 0.7141 1.0559 -0.2067 -0.3988 0.1434  1249 GLU B N   
23916 C CA  . GLU C 1249 ? 1.3278 0.7680 1.0716 -0.2125 -0.3933 0.1460  1249 GLU B CA  
23917 C C   . GLU C 1249 ? 1.2996 0.7859 1.0762 -0.2311 -0.3915 0.1638  1249 GLU B C   
23918 O O   . GLU C 1249 ? 1.2888 0.8011 1.0666 -0.2300 -0.3731 0.1658  1249 GLU B O   
23919 C CB  . GLU C 1249 ? 1.3928 0.8327 1.1252 -0.2178 -0.4119 0.1412  1249 GLU B CB  
23920 C CG  . GLU C 1249 ? 1.4292 0.9123 1.1638 -0.2233 -0.4071 0.1467  1249 GLU B CG  
23921 C CD  . GLU C 1249 ? 1.5199 0.9948 1.2232 -0.2098 -0.4078 0.1345  1249 GLU B CD  
23922 O OE1 . GLU C 1249 ? 1.6041 1.0413 1.2851 -0.1984 -0.4126 0.1217  1249 GLU B OE1 
23923 O OE2 . GLU C 1249 ? 1.5179 1.0242 1.2179 -0.2090 -0.4034 0.1375  1249 GLU B OE2 
23924 N N   . THR C 1250 ? 1.2932 0.7895 1.0955 -0.2492 -0.4109 0.1767  1250 THR B N   
23925 C CA  . THR C 1250 ? 1.2299 0.7768 1.0637 -0.2686 -0.4117 0.1949  1250 THR B CA  
23926 C C   . THR C 1250 ? 1.1186 0.6826 0.9654 -0.2658 -0.3918 0.2008  1250 THR B C   
23927 O O   . THR C 1250 ? 1.0349 0.6386 0.8895 -0.2717 -0.3790 0.2050  1250 THR B O   
23928 C CB  . THR C 1250 ? 1.2731 0.8269 1.1332 -0.2901 -0.4363 0.2107  1250 THR B CB  
23929 O OG1 . THR C 1250 ? 1.3155 0.8418 1.1874 -0.2878 -0.4385 0.2168  1250 THR B OG1 
23930 C CG2 . THR C 1250 ? 1.2680 0.8006 1.1138 -0.2948 -0.4572 0.2034  1250 THR B CG2 
23931 N N   . THR C 1251 ? 1.1052 0.6400 0.9530 -0.2563 -0.3891 0.2001  1251 THR B N   
23932 C CA  . THR C 1251 ? 1.1040 0.6593 0.9647 -0.2539 -0.3712 0.2064  1251 THR B CA  
23933 C C   . THR C 1251 ? 1.0980 0.6619 0.9376 -0.2441 -0.3468 0.1943  1251 THR B C   
23934 O O   . THR C 1251 ? 1.0894 0.6880 0.9405 -0.2508 -0.3319 0.1998  1251 THR B O   
23935 C CB  . THR C 1251 ? 1.1287 0.6535 0.9947 -0.2426 -0.3729 0.2088  1251 THR B CB  
23936 O OG1 . THR C 1251 ? 1.1722 0.6664 1.0106 -0.2204 -0.3580 0.1920  1251 THR B OG1 
23937 C CG2 . THR C 1251 ? 1.1341 0.6244 1.0043 -0.2466 -0.3976 0.2121  1251 THR B CG2 
23938 N N   . ALA C 1252 ? 1.1190 0.6521 0.9268 -0.2297 -0.3431 0.1784  1252 ALA B N   
23939 C CA  . ALA C 1252 ? 1.1312 0.6711 0.9186 -0.2229 -0.3212 0.1694  1252 ALA B CA  
23940 C C   . ALA C 1252 ? 1.1255 0.7047 0.9220 -0.2368 -0.3201 0.1748  1252 ALA B C   
23941 O O   . ALA C 1252 ? 1.0868 0.6865 0.8820 -0.2400 -0.3020 0.1741  1252 ALA B O   
23942 C CB  . ALA C 1252 ? 1.1750 0.6754 0.9258 -0.2039 -0.3177 0.1533  1252 ALA B CB  
23943 N N   . TYR C 1253 ? 1.1632 0.7545 0.9685 -0.2457 -0.3392 0.1799  1253 TYR B N   
23944 C CA  . TYR C 1253 ? 1.1786 0.8134 0.9949 -0.2578 -0.3385 0.1858  1253 TYR B CA  
23945 C C   . TYR C 1253 ? 1.1530 0.8317 0.9995 -0.2746 -0.3332 0.1987  1253 TYR B C   
23946 O O   . TYR C 1253 ? 1.1673 0.8749 1.0136 -0.2790 -0.3201 0.1972  1253 TYR B O   
23947 C CB  . TYR C 1253 ? 1.2155 0.8627 1.0384 -0.2656 -0.3610 0.1908  1253 TYR B CB  
23948 C CG  . TYR C 1253 ? 1.2615 0.8847 1.0531 -0.2501 -0.3619 0.1778  1253 TYR B CG  
23949 C CD1 . TYR C 1253 ? 1.2617 0.8901 1.0327 -0.2388 -0.3451 0.1700  1253 TYR B CD1 
23950 C CD2 . TYR C 1253 ? 1.2874 0.8810 1.0685 -0.2460 -0.3792 0.1731  1253 TYR B CD2 
23951 C CE1 . TYR C 1253 ? 1.2707 0.8788 1.0128 -0.2229 -0.3458 0.1602  1253 TYR B CE1 
23952 C CE2 . TYR C 1253 ? 1.3001 0.8765 1.0522 -0.2316 -0.3802 0.1618  1253 TYR B CE2 
23953 C CZ  . TYR C 1253 ? 1.2934 0.8783 1.0266 -0.2193 -0.3635 0.1564  1253 TYR B CZ  
23954 O OH  . TYR C 1253 ? 1.3386 0.9067 1.0424 -0.2031 -0.3648 0.1469  1253 TYR B OH  
23955 N N   . ALA C 1254 ? 1.0901 0.7740 0.9615 -0.2835 -0.3438 0.2113  1254 ALA B N   
23956 C CA  . ALA C 1254 ? 0.9888 0.7136 0.8874 -0.2969 -0.3369 0.2239  1254 ALA B CA  
23957 C C   . ALA C 1254 ? 0.9623 0.6846 0.8484 -0.2896 -0.3120 0.2149  1254 ALA B C   
23958 O O   . ALA C 1254 ? 0.8978 0.6506 0.7841 -0.2971 -0.2981 0.2124  1254 ALA B O   
23959 C CB  . ALA C 1254 ? 0.9454 0.6687 0.8696 -0.3035 -0.3520 0.2399  1254 ALA B CB  
23960 N N   . LEU C 1255 ? 1.0153 0.7011 0.8890 -0.2753 -0.3064 0.2090  1255 LEU B N   
23961 C CA  . LEU C 1255 ? 1.0765 0.7597 0.9366 -0.2690 -0.2828 0.2007  1255 LEU B CA  
23962 C C   . LEU C 1255 ? 1.0511 0.7360 0.8883 -0.2692 -0.2660 0.1887  1255 LEU B C   
23963 O O   . LEU C 1255 ? 0.9967 0.6981 0.8315 -0.2750 -0.2471 0.1857  1255 LEU B O   
23964 C CB  . LEU C 1255 ? 1.1495 0.7878 0.9897 -0.2492 -0.2788 0.1919  1255 LEU B CB  
23965 C CG  . LEU C 1255 ? 1.1519 0.7878 0.9733 -0.2436 -0.2536 0.1827  1255 LEU B CG  
23966 C CD1 . LEU C 1255 ? 1.1214 0.8023 0.9666 -0.2571 -0.2426 0.1924  1255 LEU B CD1 
23967 C CD2 . LEU C 1255 ? 1.1692 0.7634 0.9665 -0.2226 -0.2482 0.1727  1255 LEU B CD2 
23968 N N   . LEU C 1256 ? 1.0952 0.7616 0.9144 -0.2625 -0.2727 0.1817  1256 LEU B N   
23969 C CA  . LEU C 1256 ? 1.1685 0.8280 0.9623 -0.2584 -0.2570 0.1705  1256 LEU B CA  
23970 C C   . LEU C 1256 ? 1.1826 0.8864 0.9918 -0.2739 -0.2546 0.1745  1256 LEU B C   
23971 O O   . LEU C 1256 ? 1.2064 0.9145 1.0031 -0.2770 -0.2358 0.1670  1256 LEU B O   
23972 C CB  . LEU C 1256 ? 1.2156 0.8407 0.9823 -0.2421 -0.2637 0.1620  1256 LEU B CB  
23973 C CG  . LEU C 1256 ? 1.2481 0.8259 0.9826 -0.2231 -0.2548 0.1512  1256 LEU B CG  
23974 C CD1 . LEU C 1256 ? 1.2976 0.8563 1.0080 -0.2101 -0.2608 0.1448  1256 LEU B CD1 
23975 C CD2 . LEU C 1256 ? 1.2185 0.7858 0.9358 -0.2215 -0.2294 0.1451  1256 LEU B CD2 
23976 N N   . THR C 1257 ? 1.1612 0.8971 0.9961 -0.2842 -0.2735 0.1860  1257 THR B N   
23977 C CA  . THR C 1257 ? 1.0834 0.8707 0.9376 -0.3001 -0.2736 0.1919  1257 THR B CA  
23978 C C   . THR C 1257 ? 1.0434 0.8586 0.9121 -0.3133 -0.2594 0.1948  1257 THR B C   
23979 O O   . THR C 1257 ? 1.0085 0.8345 0.8667 -0.3180 -0.2419 0.1857  1257 THR B O   
23980 C CB  . THR C 1257 ? 0.9932 0.8137 0.8765 -0.3114 -0.2972 0.2076  1257 THR B CB  
23981 O OG1 . THR C 1257 ? 1.0109 0.8057 0.8813 -0.3011 -0.3119 0.2050  1257 THR B OG1 
23982 C CG2 . THR C 1257 ? 0.9314 0.8069 0.8299 -0.3248 -0.2966 0.2119  1257 THR B CG2 
23983 N N   . SER C 1258 ? 1.0275 0.8519 0.9187 -0.3185 -0.2669 0.2069  1258 SER B N   
23984 C CA  . SER C 1258 ? 1.0548 0.9059 0.9592 -0.3287 -0.2538 0.2106  1258 SER B CA  
23985 C C   . SER C 1258 ? 1.0716 0.9025 0.9497 -0.3251 -0.2293 0.1952  1258 SER B C   
23986 O O   . SER C 1258 ? 1.0261 0.8873 0.9063 -0.3388 -0.2158 0.1914  1258 SER B O   
23987 C CB  . SER C 1258 ? 1.0702 0.9193 0.9949 -0.3264 -0.2641 0.2243  1258 SER B CB  
23988 O OG  . SER C 1258 ? 1.0612 0.9346 1.0125 -0.3352 -0.2850 0.2408  1258 SER B OG  
23989 N N   . LEU C 1259 ? 1.1083 0.8896 0.9612 -0.3084 -0.2239 0.1866  1259 LEU B N   
23990 C CA  . LEU C 1259 ? 1.0935 0.8544 0.9208 -0.3064 -0.2011 0.1741  1259 LEU B CA  
23991 C C   . LEU C 1259 ? 1.0976 0.8631 0.9088 -0.3142 -0.1885 0.1634  1259 LEU B C   
23992 O O   . LEU C 1259 ? 1.0871 0.8528 0.8855 -0.3231 -0.1689 0.1553  1259 LEU B O   
23993 C CB  . LEU C 1259 ? 1.0589 0.7660 0.8585 -0.2859 -0.1985 0.1666  1259 LEU B CB  
23994 C CG  . LEU C 1259 ? 1.0088 0.7144 0.8169 -0.2805 -0.1967 0.1717  1259 LEU B CG  
23995 C CD1 . LEU C 1259 ? 1.0510 0.7071 0.8319 -0.2594 -0.1955 0.1638  1259 LEU B CD1 
23996 C CD2 . LEU C 1259 ? 0.9536 0.6878 0.7657 -0.2943 -0.1770 0.1714  1259 LEU B CD2 
23997 N N   . ASN C 1260 ? 1.0976 0.8679 0.9095 -0.3113 -0.2000 0.1634  1260 ASN B N   
23998 C CA  . ASN C 1260 ? 1.1228 0.8990 0.9206 -0.3154 -0.1898 0.1535  1260 ASN B CA  
23999 C C   . ASN C 1260 ? 1.1334 0.9626 0.9524 -0.3375 -0.1840 0.1554  1260 ASN B C   
24000 O O   . ASN C 1260 ? 1.1854 1.0130 0.9891 -0.3463 -0.1656 0.1438  1260 ASN B O   
24001 C CB  . ASN C 1260 ? 1.1002 0.8725 0.8932 -0.3037 -0.2037 0.1535  1260 ASN B CB  
24002 C CG  . ASN C 1260 ? 1.1456 0.8665 0.9005 -0.2842 -0.1946 0.1417  1260 ASN B CG  
24003 O OD1 . ASN C 1260 ? 1.2012 0.8988 0.9326 -0.2843 -0.1748 0.1312  1260 ASN B OD1 
24004 N ND2 . ASN C 1260 ? 1.1367 0.8394 0.8846 -0.2685 -0.2089 0.1440  1260 ASN B ND2 
24005 N N   . LEU C 1261 ? 1.0692 0.9442 0.9224 -0.3474 -0.1995 0.1701  1261 LEU B N   
24006 C CA  . LEU C 1261 ? 0.9890 0.9230 0.8660 -0.3685 -0.1969 0.1748  1261 LEU B CA  
24007 C C   . LEU C 1261 ? 0.9745 0.9252 0.8612 -0.3803 -0.1858 0.1779  1261 LEU B C   
24008 O O   . LEU C 1261 ? 0.9337 0.9364 0.8489 -0.3949 -0.1904 0.1896  1261 LEU B O   
24009 C CB  . LEU C 1261 ? 0.9233 0.9011 0.8328 -0.3739 -0.2187 0.1922  1261 LEU B CB  
24010 C CG  . LEU C 1261 ? 0.8940 0.8608 0.7987 -0.3625 -0.2338 0.1933  1261 LEU B CG  
24011 C CD1 . LEU C 1261 ? 0.8568 0.8688 0.7960 -0.3721 -0.2559 0.2136  1261 LEU B CD1 
24012 C CD2 . LEU C 1261 ? 0.8633 0.8287 0.7456 -0.3582 -0.2232 0.1776  1261 LEU B CD2 
24013 N N   . LYS C 1262 ? 0.9994 0.9084 0.8618 -0.3737 -0.1712 0.1683  1262 LYS B N   
24014 C CA  . LYS C 1262 ? 0.9731 0.8951 0.8415 -0.3821 -0.1602 0.1711  1262 LYS B CA  
24015 C C   . LYS C 1262 ? 0.8882 0.8581 0.7938 -0.3880 -0.1728 0.1902  1262 LYS B C   
24016 O O   . LYS C 1262 ? 0.8499 0.8589 0.7691 -0.4018 -0.1646 0.1943  1262 LYS B O   
24017 C CB  . LYS C 1262 ? 1.0294 0.9636 0.8836 -0.4005 -0.1394 0.1576  1262 LYS B CB  
24018 C CG  . LYS C 1262 ? 1.1681 1.0574 0.9884 -0.3940 -0.1307 0.1406  1262 LYS B CG  
24019 C CD  . LYS C 1262 ? 1.3019 1.1527 1.0893 -0.3991 -0.1080 0.1259  1262 LYS B CD  
24020 C CE  . LYS C 1262 ? 1.3845 1.1693 1.1367 -0.3784 -0.1045 0.1167  1262 LYS B CE  
24021 N NZ  . LYS C 1262 ? 1.3966 1.1623 1.1544 -0.3552 -0.1222 0.1268  1262 LYS B NZ  
24022 N N   . ASP C 1263 ? 0.8676 0.8313 0.7878 -0.3768 -0.1930 0.2023  1263 ASP B N   
24023 C CA  . ASP C 1263 ? 0.8465 0.8478 0.8015 -0.3803 -0.2084 0.2230  1263 ASP B CA  
24024 C C   . ASP C 1263 ? 0.8596 0.8579 0.8215 -0.3729 -0.2046 0.2303  1263 ASP B C   
24025 O O   . ASP C 1263 ? 0.8757 0.8830 0.8601 -0.3670 -0.2186 0.2470  1263 ASP B O   
24026 C CB  . ASP C 1263 ? 0.8819 0.8615 0.8434 -0.3695 -0.2304 0.2316  1263 ASP B CB  
24027 C CG  . ASP C 1263 ? 1.2207 1.2514 1.2184 -0.3817 -0.2476 0.2528  1263 ASP B CG  
24028 O OD1 . ASP C 1263 ? 1.1895 1.2645 1.2100 -0.3916 -0.2448 0.2652  1263 ASP B OD1 
24029 O OD2 . ASP C 1263 ? 1.1983 1.2265 1.2009 -0.3815 -0.2637 0.2579  1263 ASP B OD2 
24030 N N   . ILE C 1264 ? 0.8257 0.8144 0.7687 -0.3742 -0.1851 0.2184  1264 ILE B N   
24031 C CA  . ILE C 1264 ? 0.8218 0.8010 0.7631 -0.3635 -0.1779 0.2212  1264 ILE B CA  
24032 C C   . ILE C 1264 ? 0.8749 0.8711 0.8426 -0.3529 -0.1896 0.2398  1264 ILE B C   
24033 O O   . ILE C 1264 ? 0.9237 0.8809 0.8828 -0.3324 -0.1931 0.2397  1264 ILE B O   
24034 C CB  . ILE C 1264 ? 0.7742 0.7802 0.7080 -0.3789 -0.1569 0.2134  1264 ILE B CB  
24035 C CG1 . ILE C 1264 ? 0.7583 0.7295 0.6596 -0.3848 -0.1446 0.1938  1264 ILE B CG1 
24036 C CG2 . ILE C 1264 ? 0.6107 0.6118 0.5423 -0.3669 -0.1488 0.2165  1264 ILE B CG2 
24037 C CD1 . ILE C 1264 ? 0.7836 0.7672 0.6706 -0.4015 -0.1234 0.1834  1264 ILE B CD1 
24038 N N   . ASN C 1265 ? 0.8979 0.9517 0.8965 -0.3654 -0.1949 0.2558  1265 ASN B N   
24039 C CA  . ASN C 1265 ? 0.9485 1.0138 0.9709 -0.3526 -0.2058 0.2750  1265 ASN B CA  
24040 C C   . ASN C 1265 ? 0.9759 0.9967 1.0012 -0.3372 -0.2269 0.2821  1265 ASN B C   
24041 O O   . ASN C 1265 ? 1.0022 0.9926 1.0272 -0.3171 -0.2323 0.2867  1265 ASN B O   
24042 C CB  . ASN C 1265 ? 0.9838 1.1231 1.0394 -0.3683 -0.2076 0.2936  1265 ASN B CB  
24043 C CG  . ASN C 1265 ? 1.0254 1.2055 1.0841 -0.3723 -0.1901 0.2936  1265 ASN B CG  
24044 O OD1 . ASN C 1265 ? 1.0781 1.2494 1.1390 -0.3539 -0.1883 0.2995  1265 ASN B OD1 
24045 N ND2 . ASN C 1265 ? 1.0042 1.2301 1.0622 -0.3966 -0.1771 0.2862  1265 ASN B ND2 
24046 N N   . TYR C 1266 ? 0.9763 0.9945 1.0037 -0.3470 -0.2386 0.2823  1266 TYR B N   
24047 C CA  . TYR C 1266 ? 0.9922 0.9759 1.0251 -0.3383 -0.2606 0.2908  1266 TYR B CA  
24048 C C   . TYR C 1266 ? 1.0654 0.9837 1.0744 -0.3156 -0.2617 0.2794  1266 TYR B C   
24049 O O   . TYR C 1266 ? 1.1194 1.0084 1.1351 -0.3024 -0.2760 0.2882  1266 TYR B O   
24050 C CB  . TYR C 1266 ? 0.9355 0.9173 0.9617 -0.3497 -0.2680 0.2845  1266 TYR B CB  
24051 C CG  . TYR C 1266 ? 0.8949 0.8556 0.9312 -0.3477 -0.2916 0.2959  1266 TYR B CG  
24052 C CD1 . TYR C 1266 ? 0.8836 0.8596 0.9477 -0.3494 -0.3060 0.3186  1266 TYR B CD1 
24053 C CD2 . TYR C 1266 ? 0.8821 0.8091 0.8999 -0.3451 -0.2995 0.2849  1266 TYR B CD2 
24054 C CE1 . TYR C 1266 ? 0.9157 0.8708 0.9884 -0.3511 -0.3278 0.3297  1266 TYR B CE1 
24055 C CE2 . TYR C 1266 ? 0.8797 0.7909 0.9070 -0.3467 -0.3218 0.2955  1266 TYR B CE2 
24056 C CZ  . TYR C 1266 ? 0.9082 0.8322 0.9628 -0.3510 -0.3358 0.3177  1266 TYR B CZ  
24057 O OH  . TYR C 1266 ? 0.9291 0.8367 0.9938 -0.3560 -0.3582 0.3299  1266 TYR B OH  
24058 N N   . VAL C 1267 ? 1.0380 0.9344 1.0179 -0.3121 -0.2456 0.2595  1267 VAL B N   
24059 C CA  . VAL C 1267 ? 0.9937 0.8294 0.9429 -0.2942 -0.2448 0.2437  1267 VAL B CA  
24060 C C   . VAL C 1267 ? 0.9902 0.8042 0.9330 -0.2745 -0.2389 0.2425  1267 VAL B C   
24061 O O   . VAL C 1267 ? 1.0193 0.7849 0.9474 -0.2567 -0.2471 0.2364  1267 VAL B O   
24062 C CB  . VAL C 1267 ? 0.9570 0.7844 0.8791 -0.3001 -0.2287 0.2259  1267 VAL B CB  
24063 C CG1 . VAL C 1267 ? 0.9695 0.7652 0.8640 -0.2862 -0.2121 0.2127  1267 VAL B CG1 
24064 C CG2 . VAL C 1267 ? 0.9613 0.7657 0.8720 -0.3008 -0.2404 0.2201  1267 VAL B CG2 
24065 N N   . ASN C 1268 ? 1.0108 0.8639 0.9655 -0.2772 -0.2257 0.2484  1268 ASN B N   
24066 C CA  . ASN C 1268 ? 1.1156 0.9547 1.0649 -0.2565 -0.2192 0.2478  1268 ASN B CA  
24067 C C   . ASN C 1268 ? 1.1959 0.9876 1.1445 -0.2340 -0.2365 0.2506  1268 ASN B C   
24068 O O   . ASN C 1268 ? 1.2640 1.0092 1.1864 -0.2169 -0.2346 0.2364  1268 ASN B O   
24069 C CB  . ASN C 1268 ? 1.1950 1.0935 1.1673 -0.2620 -0.2087 0.2606  1268 ASN B CB  
24070 C CG  . ASN C 1268 ? 1.2459 1.1850 1.2122 -0.2838 -0.1888 0.2532  1268 ASN B CG  
24071 O OD1 . ASN C 1268 ? 1.2763 1.1893 1.2142 -0.2860 -0.1765 0.2364  1268 ASN B OD1 
24072 N ND2 . ASN C 1268 ? 1.2556 1.2585 1.2481 -0.3006 -0.1857 0.2662  1268 ASN B ND2 
24073 N N   . PRO C 1269 ? 1.1839 0.9847 1.1592 -0.2347 -0.2536 0.2685  1269 PRO B N   
24074 C CA  . PRO C 1269 ? 1.2082 0.9606 1.1833 -0.2146 -0.2704 0.2718  1269 PRO B CA  
24075 C C   . PRO C 1269 ? 1.1616 0.8579 1.1132 -0.2121 -0.2825 0.2574  1269 PRO B C   
24076 O O   . PRO C 1269 ? 1.1908 0.8362 1.1296 -0.1938 -0.2924 0.2510  1269 PRO B O   
24077 C CB  . PRO C 1269 ? 1.2214 0.9993 1.2302 -0.2254 -0.2867 0.2959  1269 PRO B CB  
24078 C CG  . PRO C 1269 ? 1.2219 1.0684 1.2496 -0.2487 -0.2772 0.3051  1269 PRO B CG  
24079 C CD  . PRO C 1269 ? 1.2056 1.0546 1.2089 -0.2577 -0.2608 0.2849  1269 PRO B CD  
24080 N N   . VAL C 1270 ? 1.0957 0.8033 1.0416 -0.2304 -0.2821 0.2521  1270 VAL B N   
24081 C CA  . VAL C 1270 ? 1.0496 0.7125 0.9695 -0.2270 -0.2891 0.2366  1270 VAL B CA  
24082 C C   . VAL C 1270 ? 1.0254 0.6541 0.9127 -0.2071 -0.2751 0.2176  1270 VAL B C   
24083 O O   . VAL C 1270 ? 1.0500 0.6317 0.9208 -0.1899 -0.2838 0.2088  1270 VAL B O   
24084 C CB  . VAL C 1270 ? 1.0272 0.7156 0.9468 -0.2475 -0.2879 0.2349  1270 VAL B CB  
24085 C CG1 . VAL C 1270 ? 1.0119 0.6667 0.8971 -0.2405 -0.2817 0.2153  1270 VAL B CG1 
24086 C CG2 . VAL C 1270 ? 1.0245 0.7239 0.9666 -0.2621 -0.3095 0.2494  1270 VAL B CG2 
24087 N N   . ILE C 1271 ? 0.9654 0.6167 0.8419 -0.2098 -0.2536 0.2111  1271 ILE B N   
24088 C CA  . ILE C 1271 ? 0.9712 0.5913 0.8168 -0.1914 -0.2408 0.1953  1271 ILE B CA  
24089 C C   . ILE C 1271 ? 0.9762 0.5853 0.8244 -0.1694 -0.2401 0.1969  1271 ILE B C   
24090 O O   . ILE C 1271 ? 1.0337 0.6067 0.8571 -0.1501 -0.2374 0.1838  1271 ILE B O   
24091 C CB  . ILE C 1271 ? 0.9716 0.6075 0.7977 -0.1993 -0.2173 0.1862  1271 ILE B CB  
24092 C CG1 . ILE C 1271 ? 0.9452 0.6203 0.7813 -0.2010 -0.1995 0.1916  1271 ILE B CG1 
24093 C CG2 . ILE C 1271 ? 0.9724 0.6241 0.7996 -0.2203 -0.2169 0.1861  1271 ILE B CG2 
24094 C CD1 . ILE C 1271 ? 0.9739 0.6286 0.7928 -0.1772 -0.1914 0.1845  1271 ILE B CD1 
24095 N N   . LYS C 1272 ? 0.9614 0.6014 0.8382 -0.1698 -0.2425 0.2126  1272 LYS B N   
24096 C CA  . LYS C 1272 ? 1.0591 0.6829 0.9348 -0.1438 -0.2420 0.2125  1272 LYS B CA  
24097 C C   . LYS C 1272 ? 1.1376 0.6970 0.9960 -0.1275 -0.2601 0.2020  1272 LYS B C   
24098 O O   . LYS C 1272 ? 1.1872 0.7158 1.0261 -0.1032 -0.2568 0.1903  1272 LYS B O   
24099 C CB  . LYS C 1272 ? 1.0744 0.7379 0.9846 -0.1435 -0.2446 0.2334  1272 LYS B CB  
24100 C CG  . LYS C 1272 ? 1.0963 0.7362 1.0094 -0.1144 -0.2499 0.2364  1272 LYS B CG  
24101 C CD  . LYS C 1272 ? 1.0807 0.7524 0.9916 -0.0971 -0.2302 0.2356  1272 LYS B CD  
24102 C CE  . LYS C 1272 ? 1.1341 0.7920 1.0573 -0.0697 -0.2381 0.2447  1272 LYS B CE  
24103 N NZ  . LYS C 1272 ? 1.1811 0.8596 1.0962 -0.0443 -0.2205 0.2402  1272 LYS B NZ  
24104 N N   . TRP C 1273 ? 1.1330 0.6754 0.9976 -0.1421 -0.2787 0.2053  1273 TRP B N   
24105 C CA  . TRP C 1273 ? 1.1249 0.6099 0.9765 -0.1328 -0.2988 0.1970  1273 TRP B CA  
24106 C C   . TRP C 1273 ? 1.0910 0.5432 0.9076 -0.1290 -0.2976 0.1762  1273 TRP B C   
24107 O O   . TRP C 1273 ? 1.1419 0.5477 0.9379 -0.1118 -0.3056 0.1628  1273 TRP B O   
24108 C CB  . TRP C 1273 ? 1.1087 0.5960 0.9858 -0.1519 -0.3203 0.2132  1273 TRP B CB  
24109 C CG  . TRP C 1273 ? 1.1400 0.5757 1.0069 -0.1533 -0.3433 0.2069  1273 TRP B CG  
24110 C CD1 . TRP C 1273 ? 1.1907 0.5877 1.0651 -0.1468 -0.3615 0.2125  1273 TRP B CD1 
24111 C CD2 . TRP C 1273 ? 1.1364 0.5569 0.9854 -0.1641 -0.3513 0.1955  1273 TRP B CD2 
24112 N NE1 . TRP C 1273 ? 1.1993 0.5572 1.0606 -0.1556 -0.3807 0.2038  1273 TRP B NE1 
24113 C CE2 . TRP C 1273 ? 1.1808 0.5559 1.0268 -0.1656 -0.3748 0.1936  1273 TRP B CE2 
24114 C CE3 . TRP C 1273 ? 1.1194 0.5587 0.9531 -0.1720 -0.3411 0.1866  1273 TRP B CE3 
24115 C CZ2 . TRP C 1273 ? 1.2081 0.5637 1.0380 -0.1756 -0.3880 0.1834  1273 TRP B CZ2 
24116 C CZ3 . TRP C 1273 ? 1.1464 0.5651 0.9642 -0.1787 -0.3540 0.1775  1273 TRP B CZ3 
24117 C CH2 . TRP C 1273 ? 1.1860 0.5665 1.0025 -0.1810 -0.3772 0.1759  1273 TRP B CH2 
24118 N N   . LEU C 1274 ? 1.0167 0.4913 0.8250 -0.1431 -0.2875 0.1730  1274 LEU B N   
24119 C CA  . LEU C 1274 ? 1.0809 0.5275 0.8537 -0.1339 -0.2816 0.1545  1274 LEU B CA  
24120 C C   . LEU C 1274 ? 1.1629 0.5988 0.9138 -0.1108 -0.2645 0.1434  1274 LEU B C   
24121 O O   . LEU C 1274 ? 1.2220 0.6195 0.9513 -0.0919 -0.2698 0.1302  1274 LEU B O   
24122 C CB  . LEU C 1274 ? 1.1165 0.5843 0.8825 -0.1509 -0.2737 0.1538  1274 LEU B CB  
24123 C CG  . LEU C 1274 ? 1.1632 0.6315 0.9393 -0.1674 -0.2929 0.1587  1274 LEU B CG  
24124 C CD1 . LEU C 1274 ? 1.1646 0.6486 0.9289 -0.1782 -0.2849 0.1555  1274 LEU B CD1 
24125 C CD2 . LEU C 1274 ? 1.2147 0.6379 0.9751 -0.1570 -0.3115 0.1489  1274 LEU B CD2 
24126 N N   . SER C 1275 ? 1.1407 0.6133 0.8972 -0.1127 -0.2440 0.1486  1275 SER B N   
24127 C CA  . SER C 1275 ? 1.2065 0.6778 0.9439 -0.0929 -0.2266 0.1400  1275 SER B CA  
24128 C C   . SER C 1275 ? 1.2344 0.6850 0.9739 -0.0683 -0.2336 0.1374  1275 SER B C   
24129 O O   . SER C 1275 ? 1.2233 0.6903 0.9593 -0.0522 -0.2186 0.1362  1275 SER B O   
24130 C CB  . SER C 1275 ? 1.3010 0.8238 1.0510 -0.1040 -0.2052 0.1494  1275 SER B CB  
24131 O OG  . SER C 1275 ? 1.3778 0.9026 1.1009 -0.1021 -0.1855 0.1405  1275 SER B OG  
24132 N N   . GLU C 1276 ? 1.2912 0.7068 1.0363 -0.0655 -0.2560 0.1367  1276 GLU B N   
24133 C CA  . GLU C 1276 ? 1.3789 0.7638 1.1252 -0.0423 -0.2659 0.1335  1276 GLU B CA  
24134 C C   . GLU C 1276 ? 1.4063 0.7397 1.1416 -0.0437 -0.2892 0.1242  1276 GLU B C   
24135 O O   . GLU C 1276 ? 1.4610 0.7601 1.2002 -0.0314 -0.3035 0.1230  1276 GLU B O   
24136 C CB  . GLU C 1276 ? 1.4197 0.8289 1.2025 -0.0455 -0.2710 0.1537  1276 GLU B CB  
24137 C CG  . GLU C 1276 ? 1.4329 0.8909 1.2292 -0.0361 -0.2510 0.1631  1276 GLU B CG  
24138 C CD  . GLU C 1276 ? 1.4234 0.8902 1.2482 -0.0258 -0.2584 0.1796  1276 GLU B CD  
24139 O OE1 . GLU C 1276 ? 1.4222 0.8558 1.2577 -0.0299 -0.2794 0.1855  1276 GLU B OE1 
24140 O OE2 . GLU C 1276 ? 1.4050 0.9125 1.2407 -0.0136 -0.2432 0.1873  1276 GLU B OE2 
24141 N N   . GLU C 1277 ? 1.3791 0.7088 1.1018 -0.0600 -0.2934 0.1189  1277 GLU B N   
24142 C CA  . GLU C 1277 ? 1.4154 0.7047 1.1262 -0.0657 -0.3152 0.1100  1277 GLU B CA  
24143 C C   . GLU C 1277 ? 1.4374 0.7044 1.1095 -0.0537 -0.3102 0.0895  1277 GLU B C   
24144 O O   . GLU C 1277 ? 1.4650 0.6904 1.1154 -0.0373 -0.3197 0.0733  1277 GLU B O   
24145 C CB  . GLU C 1277 ? 1.3967 0.7087 1.1275 -0.0948 -0.3257 0.1232  1277 GLU B CB  
24146 C CG  . GLU C 1277 ? 1.4286 0.7079 1.1607 -0.1059 -0.3524 0.1216  1277 GLU B CG  
24147 C CD  . GLU C 1277 ? 1.4729 0.7203 1.2183 -0.0986 -0.3667 0.1259  1277 GLU B CD  
24148 O OE1 . GLU C 1277 ? 1.5022 0.7143 1.2457 -0.1069 -0.3888 0.1230  1277 GLU B OE1 
24149 O OE2 . GLU C 1277 ? 1.4802 0.7369 1.2368 -0.0842 -0.3557 0.1324  1277 GLU B OE2 
24150 N N   . GLN C 1278 ? 1.4405 0.7353 1.1038 -0.0620 -0.2952 0.0907  1278 GLN B N   
24151 C CA  . GLN C 1278 ? 1.5031 0.7860 1.1301 -0.0499 -0.2848 0.0755  1278 GLN B CA  
24152 C C   . GLN C 1278 ? 1.5733 0.8329 1.1798 -0.0220 -0.2792 0.0613  1278 GLN B C   
24153 O O   . GLN C 1278 ? 1.5767 0.8464 1.1978 -0.0114 -0.2722 0.0664  1278 GLN B O   
24154 C CB  . GLN C 1278 ? 1.5663 0.8842 1.1892 -0.0588 -0.2625 0.0822  1278 GLN B CB  
24155 C CG  . GLN C 1278 ? 1.9392 1.2848 1.5834 -0.0850 -0.2649 0.0959  1278 GLN B CG  
24156 C CD  . GLN C 1278 ? 1.3588 0.6901 1.0006 -0.0957 -0.2859 0.0939  1278 GLN B CD  
24157 O OE1 . GLN C 1278 ? 1.3162 0.6592 0.9501 -0.1045 -0.2819 0.0954  1278 GLN B OE1 
24158 N NE2 . GLN C 1278 ? 1.3787 0.6855 1.0272 -0.0949 -0.3079 0.0909  1278 GLN B NE2 
24159 N N   . ARG C 1279 ? 1.5907 0.8213 1.1637 -0.0090 -0.2832 0.0436  1279 ARG B N   
24160 C CA  . ARG C 1279 ? 1.5944 0.7982 1.1457 0.0180  -0.2822 0.0270  1279 ARG B CA  
24161 C C   . ARG C 1279 ? 1.5112 0.7352 1.0396 0.0311  -0.2583 0.0230  1279 ARG B C   
24162 O O   . ARG C 1279 ? 1.4671 0.7151 0.9937 0.0177  -0.2466 0.0315  1279 ARG B O   
24163 C CB  . ARG C 1279 ? 1.6793 0.8405 1.2068 0.0224  -0.3027 0.0090  1279 ARG B CB  
24164 C CG  . ARG C 1279 ? 1.7301 0.8721 1.2791 0.0040  -0.3273 0.0143  1279 ARG B CG  
24165 C CD  . ARG C 1279 ? 1.8368 0.9291 1.3754 0.0165  -0.3456 -0.0019 1279 ARG B CD  
24166 N NE  . ARG C 1279 ? 1.9193 0.9876 1.4184 0.0381  -0.3437 -0.0259 1279 ARG B NE  
24167 C CZ  . ARG C 1279 ? 1.9775 0.9990 1.4587 0.0484  -0.3602 -0.0454 1279 ARG B CZ  
24168 N NH1 . ARG C 1279 ? 1.9754 0.9658 1.4749 0.0379  -0.3799 -0.0423 1279 ARG B NH1 
24169 N NH2 . ARG C 1279 ? 2.0301 1.0353 1.4740 0.0682  -0.3571 -0.0679 1279 ARG B NH2 
24170 N N   . TYR C 1280 ? 1.5218 0.7357 1.0318 0.0570  -0.2510 0.0103  1280 TYR B N   
24171 C CA  . TYR C 1280 ? 1.5279 0.7627 1.0134 0.0699  -0.2280 0.0065  1280 TYR B CA  
24172 C C   . TYR C 1280 ? 1.3075 0.5423 0.7669 0.0612  -0.2239 0.0045  1280 TYR B C   
24173 O O   . TYR C 1280 ? 1.3050 0.5129 0.7466 0.0620  -0.2395 -0.0066 1280 TYR B O   
24174 C CB  . TYR C 1280 ? 1.5504 0.7674 1.0142 0.1009  -0.2264 -0.0114 1280 TYR B CB  
24175 C CG  . TYR C 1280 ? 1.5561 0.7865 0.9864 0.1154  -0.2082 -0.0194 1280 TYR B CG  
24176 C CD1 . TYR C 1280 ? 1.6393 0.8488 1.0400 0.1425  -0.2101 -0.0402 1280 TYR B CD1 
24177 C CD2 . TYR C 1280 ? 1.5045 0.7668 0.9310 0.1021  -0.1893 -0.0066 1280 TYR B CD2 
24178 C CE1 . TYR C 1280 ? 1.6600 0.8853 1.0289 0.1565  -0.1933 -0.0468 1280 TYR B CE1 
24179 C CE2 . TYR C 1280 ? 1.5516 0.8252 0.9460 0.1148  -0.1726 -0.0121 1280 TYR B CE2 
24180 C CZ  . TYR C 1280 ? 1.6302 0.8877 0.9965 0.1421  -0.1747 -0.0316 1280 TYR B CZ  
24181 O OH  . TYR C 1280 ? 1.6799 0.9523 1.0144 0.1548  -0.1582 -0.0359 1280 TYR B OH  
24182 N N   . GLY C 1281 ? 1.2841 0.5487 0.7408 0.0524  -0.2033 0.0158  1281 GLY B N   
24183 C CA  . GLY C 1281 ? 1.3216 0.5829 0.7556 0.0444  -0.2000 0.0167  1281 GLY B CA  
24184 C C   . GLY C 1281 ? 1.3657 0.6323 0.8166 0.0198  -0.2064 0.0289  1281 GLY B C   
24185 O O   . GLY C 1281 ? 1.4158 0.6984 0.8624 0.0094  -0.1907 0.0387  1281 GLY B O   
24186 N N   . GLY C 1282 ? 1.4338 0.6870 0.9022 0.0101  -0.2286 0.0283  1282 GLY B N   
24187 C CA  . GLY C 1282 ? 1.4872 0.7518 0.9740 -0.0127 -0.2345 0.0404  1282 GLY B CA  
24188 C C   . GLY C 1282 ? 1.6458 0.9008 1.1573 -0.0239 -0.2595 0.0414  1282 GLY B C   
24189 O O   . GLY C 1282 ? 1.6341 0.8713 1.1524 -0.0157 -0.2713 0.0346  1282 GLY B O   
24190 N N   . GLY C 1283 ? 1.7961 1.0615 1.3195 -0.0421 -0.2677 0.0499  1283 GLY B N   
24191 C CA  . GLY C 1283 ? 1.9046 1.1720 1.4579 -0.0584 -0.2885 0.0565  1283 GLY B CA  
24192 C C   . GLY C 1283 ? 1.9549 1.1943 1.5108 -0.0579 -0.3142 0.0479  1283 GLY B C   
24193 O O   . GLY C 1283 ? 1.8903 1.1345 1.4671 -0.0755 -0.3314 0.0554  1283 GLY B O   
24194 N N   . PHE C 1284 ? 2.0824 1.2928 1.6171 -0.0386 -0.3164 0.0324  1284 PHE B N   
24195 C CA  . PHE C 1284 ? 2.2583 1.4338 1.7828 -0.0360 -0.3399 0.0184  1284 PHE B CA  
24196 C C   . PHE C 1284 ? 2.1311 1.3053 1.6635 -0.0565 -0.3632 0.0209  1284 PHE B C   
24197 O O   . PHE C 1284 ? 2.1899 1.3508 1.6973 -0.0535 -0.3738 0.0080  1284 PHE B O   
24198 C CB  . PHE C 1284 ? 2.5504 1.7002 2.0865 -0.0273 -0.3467 0.0143  1284 PHE B CB  
24199 C CG  . PHE C 1284 ? 2.8814 1.9867 2.3935 -0.0162 -0.3642 -0.0070 1284 PHE B CG  
24200 C CD1 . PHE C 1284 ? 3.0393 2.1316 2.5141 0.0048  -0.3571 -0.0261 1284 PHE B CD1 
24201 C CD2 . PHE C 1284 ? 3.0328 2.1085 2.5587 -0.0277 -0.3876 -0.0081 1284 PHE B CD2 
24202 C CE1 . PHE C 1284 ? 3.2074 2.2592 2.6586 0.0145  -0.3733 -0.0480 1284 PHE B CE1 
24203 C CE2 . PHE C 1284 ? 3.1923 2.2229 2.6944 -0.0195 -0.4040 -0.0297 1284 PHE B CE2 
24204 C CZ  . PHE C 1284 ? 3.2859 2.3051 2.7503 0.0019  -0.3969 -0.0507 1284 PHE B CZ  
24205 N N   . TYR C 1285 ? 1.9562 1.1458 1.5221 -0.0773 -0.3725 0.0368  1285 TYR B N   
24206 C CA  . TYR C 1285 ? 1.8406 1.0266 1.4120 -0.0961 -0.3969 0.0373  1285 TYR B CA  
24207 C C   . TYR C 1285 ? 1.7672 0.9790 1.3243 -0.1001 -0.3947 0.0381  1285 TYR B C   
24208 O O   . TYR C 1285 ? 1.7861 1.0309 1.3559 -0.1065 -0.3820 0.0515  1285 TYR B O   
24209 C CB  . TYR C 1285 ? 1.7587 0.9568 1.3687 -0.1184 -0.4089 0.0553  1285 TYR B CB  
24210 C CG  . TYR C 1285 ? 1.7485 0.9207 1.3721 -0.1111 -0.4098 0.0566  1285 TYR B CG  
24211 C CD1 . TYR C 1285 ? 1.7764 0.9038 1.3776 -0.0926 -0.4142 0.0381  1285 TYR B CD1 
24212 C CD2 . TYR C 1285 ? 1.7114 0.9055 1.3690 -0.1208 -0.4054 0.0762  1285 TYR B CD2 
24213 C CE1 . TYR C 1285 ? 1.7843 0.8872 1.3964 -0.0819 -0.4138 0.0393  1285 TYR B CE1 
24214 C CE2 . TYR C 1285 ? 1.7010 0.8738 1.3708 -0.1110 -0.4054 0.0791  1285 TYR B CE2 
24215 C CZ  . TYR C 1285 ? 1.7415 0.8674 1.3883 -0.0907 -0.4094 0.0608  1285 TYR B CZ  
24216 O OH  . TYR C 1285 ? 1.7621 0.8654 1.4200 -0.0779 -0.4092 0.0637  1285 TYR B OH  
24217 N N   . SER C 1286 ? 1.6797 0.8771 1.2091 -0.0951 -0.4061 0.0234  1286 SER B N   
24218 C CA  . SER C 1286 ? 1.5981 0.8226 1.1153 -0.0986 -0.4073 0.0259  1286 SER B CA  
24219 C C   . SER C 1286 ? 1.4993 0.7516 1.0137 -0.0910 -0.3824 0.0364  1286 SER B C   
24220 O O   . SER C 1286 ? 1.4898 0.7369 0.9986 -0.0783 -0.3617 0.0364  1286 SER B O   
24221 C CB  . SER C 1286 ? 1.5626 0.8061 1.1014 -0.1237 -0.4300 0.0348  1286 SER B CB  
24222 O OG  . SER C 1286 ? 1.5127 0.7949 1.0524 -0.1283 -0.4269 0.0444  1286 SER B OG  
24223 N N   . THR C 1287 ? 1.4968 0.7784 1.0137 -0.0988 -0.3846 0.0450  1287 THR B N   
24224 C CA  . THR C 1287 ? 1.5239 0.8236 1.0304 -0.0895 -0.3628 0.0520  1287 THR B CA  
24225 C C   . THR C 1287 ? 1.5966 0.9247 1.1341 -0.1050 -0.3566 0.0680  1287 THR B C   
24226 O O   . THR C 1287 ? 1.6234 0.9544 1.1679 -0.1035 -0.3369 0.0736  1287 THR B O   
24227 C CB  . THR C 1287 ? 1.4982 0.8140 0.9851 -0.0847 -0.3690 0.0513  1287 THR B CB  
24228 O OG1 . THR C 1287 ? 1.4850 0.8154 0.9874 -0.1019 -0.3947 0.0525  1287 THR B OG1 
24229 C CG2 . THR C 1287 ? 1.5401 0.8352 0.9888 -0.0644 -0.3662 0.0376  1287 THR B CG2 
24230 N N   . GLN C 1288 ? 1.6300 0.9823 1.1856 -0.1210 -0.3740 0.0751  1288 GLN B N   
24231 C CA  . GLN C 1288 ? 1.6214 1.0091 1.2018 -0.1343 -0.3696 0.0895  1288 GLN B CA  
24232 C C   . GLN C 1288 ? 1.6561 1.0485 1.2640 -0.1445 -0.3601 0.0980  1288 GLN B C   
24233 O O   . GLN C 1288 ? 1.6712 1.0838 1.2875 -0.1473 -0.3439 0.1057  1288 GLN B O   
24234 C CB  . GLN C 1288 ? 1.6092 1.0242 1.2062 -0.1509 -0.3929 0.0954  1288 GLN B CB  
24235 C CG  . GLN C 1288 ? 1.6248 1.0557 1.1996 -0.1409 -0.3962 0.0928  1288 GLN B CG  
24236 C CD  . GLN C 1288 ? 1.6036 1.0574 1.1747 -0.1324 -0.3770 0.1004  1288 GLN B CD  
24237 O OE1 . GLN C 1288 ? 1.6010 1.0795 1.1971 -0.1444 -0.3722 0.1106  1288 GLN B OE1 
24238 N NE2 . GLN C 1288 ? 1.5843 1.0296 1.1234 -0.1115 -0.3665 0.0955  1288 GLN B NE2 
24239 N N   . ASP C 1289 ? 1.6480 1.0221 1.2693 -0.1499 -0.3700 0.0965  1289 ASP B N   
24240 C CA  . ASP C 1289 ? 1.6261 1.0062 1.2710 -0.1560 -0.3594 0.1050  1289 ASP B CA  
24241 C C   . ASP C 1289 ? 1.6264 0.9955 1.2513 -0.1393 -0.3337 0.0994  1289 ASP B C   
24242 O O   . ASP C 1289 ? 1.6452 1.0350 1.2795 -0.1439 -0.3163 0.1069  1289 ASP B O   
24243 C CB  . ASP C 1289 ? 1.6505 1.0065 1.3080 -0.1589 -0.3733 0.1036  1289 ASP B CB  
24244 C CG  . ASP C 1289 ? 1.6940 1.0103 1.3220 -0.1409 -0.3759 0.0866  1289 ASP B CG  
24245 O OD1 . ASP C 1289 ? 1.6948 1.0043 1.3038 -0.1393 -0.3879 0.0782  1289 ASP B OD1 
24246 O OD2 . ASP C 1289 ? 1.7253 1.0216 1.3482 -0.1278 -0.3653 0.0815  1289 ASP B OD2 
24247 N N   . THR C 1290 ? 1.5594 0.8975 1.1558 -0.1213 -0.3312 0.0862  1290 THR B N   
24248 C CA  . THR C 1290 ? 1.4762 0.8048 1.0550 -0.1067 -0.3077 0.0820  1290 THR B CA  
24249 C C   . THR C 1290 ? 1.3705 0.7164 0.9409 -0.1075 -0.2867 0.0878  1290 THR B C   
24250 O O   . THR C 1290 ? 1.3416 0.6898 0.9098 -0.1052 -0.2665 0.0896  1290 THR B O   
24251 C CB  . THR C 1290 ? 1.4952 0.7920 1.0414 -0.0862 -0.3078 0.0666  1290 THR B CB  
24252 O OG1 . THR C 1290 ? 1.5287 0.8049 1.0837 -0.0850 -0.3240 0.0603  1290 THR B OG1 
24253 C CG2 . THR C 1290 ? 1.4642 0.7573 0.9933 -0.0727 -0.2820 0.0646  1290 THR B CG2 
24254 N N   . ILE C 1291 ? 1.3059 0.6642 0.8714 -0.1111 -0.2909 0.0908  1291 ILE B N   
24255 C CA  . ILE C 1291 ? 1.2669 0.6356 0.8238 -0.1110 -0.2704 0.0957  1291 ILE B CA  
24256 C C   . ILE C 1291 ? 1.2490 0.6451 0.8371 -0.1295 -0.2645 0.1055  1291 ILE B C   
24257 O O   . ILE C 1291 ? 1.2826 0.6824 0.8681 -0.1321 -0.2441 0.1077  1291 ILE B O   
24258 C CB  . ILE C 1291 ? 1.1824 0.5564 0.7224 -0.1053 -0.2736 0.0963  1291 ILE B CB  
24259 C CG1 . ILE C 1291 ? 1.0984 0.4777 0.6303 -0.1056 -0.2517 0.1012  1291 ILE B CG1 
24260 C CG2 . ILE C 1291 ? 1.1568 0.5548 0.7193 -0.1174 -0.2965 0.1006  1291 ILE B CG2 
24261 C CD1 . ILE C 1291 ? 1.0630 0.4526 0.5844 -0.0998 -0.2554 0.1038  1291 ILE B CD1 
24262 N N   . ASN C 1292 ? 1.1982 0.6148 0.8155 -0.1436 -0.2828 0.1117  1292 ASN B N   
24263 C CA  . ASN C 1292 ? 1.1408 0.5896 0.7891 -0.1619 -0.2797 0.1221  1292 ASN B CA  
24264 C C   . ASN C 1292 ? 1.1505 0.5995 0.8120 -0.1648 -0.2702 0.1244  1292 ASN B C   
24265 O O   . ASN C 1292 ? 1.1776 0.6394 0.8411 -0.1700 -0.2514 0.1268  1292 ASN B O   
24266 C CB  . ASN C 1292 ? 1.1115 0.5832 0.7856 -0.1758 -0.3026 0.1296  1292 ASN B CB  
24267 C CG  . ASN C 1292 ? 1.1257 0.6092 0.7887 -0.1736 -0.3089 0.1290  1292 ASN B CG  
24268 O OD1 . ASN C 1292 ? 1.1013 0.5885 0.7491 -0.1675 -0.2929 0.1274  1292 ASN B OD1 
24269 N ND2 . ASN C 1292 ? 1.1265 0.6151 0.7955 -0.1777 -0.3319 0.1301  1292 ASN B ND2 
24270 N N   . ALA C 1293 ? 1.1418 0.5755 0.8101 -0.1604 -0.2826 0.1228  1293 ALA B N   
24271 C CA  . ALA C 1293 ? 1.1697 0.6029 0.8482 -0.1580 -0.2736 0.1247  1293 ALA B CA  
24272 C C   . ALA C 1293 ? 1.1963 0.6227 0.8521 -0.1482 -0.2487 0.1190  1293 ALA B C   
24273 O O   . ALA C 1293 ? 1.1749 0.6202 0.8432 -0.1537 -0.2348 0.1240  1293 ALA B O   
24274 C CB  . ALA C 1293 ? 1.2267 0.6338 0.9062 -0.1482 -0.2892 0.1203  1293 ALA B CB  
24275 N N   . ILE C 1294 ? 1.2523 0.6544 0.8746 -0.1345 -0.2427 0.1097  1294 ILE B N   
24276 C CA  . ILE C 1294 ? 1.3018 0.6991 0.9028 -0.1286 -0.2181 0.1070  1294 ILE B CA  
24277 C C   . ILE C 1294 ? 1.3134 0.7335 0.9219 -0.1452 -0.2034 0.1135  1294 ILE B C   
24278 O O   . ILE C 1294 ? 1.3248 0.7607 0.9404 -0.1534 -0.1871 0.1168  1294 ILE B O   
24279 C CB  . ILE C 1294 ? 1.3012 0.6691 0.8628 -0.1110 -0.2123 0.0980  1294 ILE B CB  
24280 C CG1 . ILE C 1294 ? 1.2929 0.6382 0.8415 -0.0933 -0.2221 0.0886  1294 ILE B CG1 
24281 C CG2 . ILE C 1294 ? 1.2855 0.6520 0.8281 -0.1111 -0.1859 0.0991  1294 ILE B CG2 
24282 C CD1 . ILE C 1294 ? 1.2813 0.6191 0.8103 -0.0810 -0.2034 0.0844  1294 ILE B CD1 
24283 N N   . GLU C 1295 ? 1.2940 0.7176 0.9008 -0.1501 -0.2092 0.1148  1295 GLU B N   
24284 C CA  . GLU C 1295 ? 1.2636 0.7054 0.8752 -0.1642 -0.1957 0.1186  1295 GLU B CA  
24285 C C   . GLU C 1295 ? 1.1645 0.6400 0.8086 -0.1818 -0.1935 0.1257  1295 GLU B C   
24286 O O   . GLU C 1295 ? 1.1554 0.6416 0.7987 -0.1914 -0.1749 0.1264  1295 GLU B O   
24287 C CB  . GLU C 1295 ? 1.3280 0.7784 0.9422 -0.1669 -0.2066 0.1201  1295 GLU B CB  
24288 C CG  . GLU C 1295 ? 1.3982 0.8584 1.0087 -0.1769 -0.1899 0.1208  1295 GLU B CG  
24289 C CD  . GLU C 1295 ? 1.4538 0.9227 1.0629 -0.1754 -0.1978 0.1213  1295 GLU B CD  
24290 O OE1 . GLU C 1295 ? 1.4405 0.8903 1.0289 -0.1590 -0.2051 0.1185  1295 GLU B OE1 
24291 O OE2 . GLU C 1295 ? 1.4862 0.9847 1.1147 -0.1902 -0.1964 0.1244  1295 GLU B OE2 
24292 N N   . GLY C 1296 ? 1.1167 0.6099 0.7891 -0.1870 -0.2125 0.1316  1296 GLY B N   
24293 C CA  . GLY C 1296 ? 1.0995 0.6268 0.8042 -0.2014 -0.2123 0.1406  1296 GLY B CA  
24294 C C   . GLY C 1296 ? 1.0960 0.6259 0.7976 -0.1990 -0.1951 0.1400  1296 GLY B C   
24295 O O   . GLY C 1296 ? 1.0894 0.6384 0.7915 -0.2112 -0.1774 0.1409  1296 GLY B O   
24296 N N   . LEU C 1297 ? 1.0988 0.6106 0.7963 -0.1835 -0.2002 0.1377  1297 LEU B N   
24297 C CA  . LEU C 1297 ? 1.1134 0.6277 0.8035 -0.1770 -0.1836 0.1361  1297 LEU B CA  
24298 C C   . LEU C 1297 ? 1.1551 0.6716 0.8242 -0.1844 -0.1592 0.1327  1297 LEU B C   
24299 O O   . LEU C 1297 ? 1.1322 0.6726 0.8076 -0.1917 -0.1441 0.1359  1297 LEU B O   
24300 C CB  . LEU C 1297 ? 1.1031 0.5838 0.7747 -0.1535 -0.1899 0.1283  1297 LEU B CB  
24301 C CG  . LEU C 1297 ? 1.0739 0.5668 0.7722 -0.1489 -0.2008 0.1345  1297 LEU B CG  
24302 C CD1 . LEU C 1297 ? 1.0562 0.5301 0.7653 -0.1461 -0.2266 0.1352  1297 LEU B CD1 
24303 C CD2 . LEU C 1297 ? 1.0946 0.5782 0.7786 -0.1296 -0.1905 0.1288  1297 LEU B CD2 
24304 N N   . THR C 1298 ? 1.2253 0.7165 0.8685 -0.1824 -0.1551 0.1269  1298 THR B N   
24305 C CA  . THR C 1298 ? 1.2418 0.7265 0.8617 -0.1891 -0.1319 0.1241  1298 THR B CA  
24306 C C   . THR C 1298 ? 1.2311 0.7469 0.8698 -0.2131 -0.1251 0.1282  1298 THR B C   
24307 O O   . THR C 1298 ? 1.1827 0.7248 0.8305 -0.2272 -0.1111 0.1311  1298 THR B O   
24308 C CB  . THR C 1298 ? 1.2307 0.6765 0.8152 -0.1785 -0.1281 0.1181  1298 THR B CB  
24309 O OG1 . THR C 1298 ? 1.2734 0.6960 0.8469 -0.1576 -0.1436 0.1141  1298 THR B OG1 
24310 C CG2 . THR C 1298 ? 1.2200 0.6499 0.7759 -0.1792 -0.1047 0.1163  1298 THR B CG2 
24311 N N   . GLU C 1299 ? 1.2328 0.7494 0.8782 -0.2173 -0.1364 0.1283  1299 GLU B N   
24312 C CA  . GLU C 1299 ? 1.2509 0.7917 0.9080 -0.2376 -0.1309 0.1294  1299 GLU B CA  
24313 C C   . GLU C 1299 ? 1.2215 0.8104 0.9107 -0.2566 -0.1284 0.1362  1299 GLU B C   
24314 O O   . GLU C 1299 ? 1.2418 0.8502 0.9323 -0.2760 -0.1141 0.1346  1299 GLU B O   
24315 C CB  . GLU C 1299 ? 1.2675 0.8086 0.9311 -0.2346 -0.1478 0.1297  1299 GLU B CB  
24316 C CG  . GLU C 1299 ? 1.3395 0.8852 0.9959 -0.2463 -0.1381 0.1257  1299 GLU B CG  
24317 C CD  . GLU C 1299 ? 1.4353 0.9363 1.0518 -0.2354 -0.1240 0.1182  1299 GLU B CD  
24318 O OE1 . GLU C 1299 ? 1.4774 0.9530 1.0776 -0.2163 -0.1332 0.1169  1299 GLU B OE1 
24319 O OE2 . GLU C 1299 ? 1.4566 0.9481 1.0577 -0.2467 -0.1041 0.1139  1299 GLU B OE2 
24320 N N   . TYR C 1300 ? 1.1422 0.7488 0.8556 -0.2507 -0.1422 0.1436  1300 TYR B N   
24321 C CA  . TYR C 1300 ? 1.0794 0.7315 0.8222 -0.2632 -0.1402 0.1522  1300 TYR B CA  
24322 C C   . TYR C 1300 ? 1.0368 0.6979 0.7710 -0.2659 -0.1208 0.1512  1300 TYR B C   
24323 O O   . TYR C 1300 ? 0.9679 0.6706 0.7198 -0.2828 -0.1128 0.1560  1300 TYR B O   
24324 C CB  . TYR C 1300 ? 1.1069 0.7679 0.8753 -0.2525 -0.1608 0.1614  1300 TYR B CB  
24325 C CG  . TYR C 1300 ? 1.0914 0.7929 0.8865 -0.2567 -0.1584 0.1718  1300 TYR B CG  
24326 C CD1 . TYR C 1300 ? 1.0772 0.8223 0.9059 -0.2704 -0.1676 0.1838  1300 TYR B CD1 
24327 C CD2 . TYR C 1300 ? 1.0747 0.7744 0.8614 -0.2456 -0.1469 0.1705  1300 TYR B CD2 
24328 C CE1 . TYR C 1300 ? 1.0708 0.8556 0.9238 -0.2725 -0.1655 0.1949  1300 TYR B CE1 
24329 C CE2 . TYR C 1300 ? 1.0712 0.8118 0.8822 -0.2470 -0.1445 0.1806  1300 TYR B CE2 
24330 C CZ  . TYR C 1300 ? 1.0816 0.8643 0.9258 -0.2601 -0.1539 0.1932  1300 TYR B CZ  
24331 O OH  . TYR C 1300 ? 1.0926 0.9197 0.9616 -0.2599 -0.1514 0.2051  1300 TYR B OH  
24332 N N   . SER C 1301 ? 1.1096 0.7374 0.8176 -0.2495 -0.1136 0.1457  1301 SER B N   
24333 C CA  . SER C 1301 ? 1.1480 0.7915 0.8496 -0.2524 -0.0954 0.1463  1301 SER B CA  
24334 C C   . SER C 1301 ? 1.1033 0.7446 0.7864 -0.2732 -0.0762 0.1413  1301 SER B C   
24335 O O   . SER C 1301 ? 1.0488 0.7109 0.7285 -0.2860 -0.0592 0.1421  1301 SER B O   
24336 C CB  . SER C 1301 ? 1.2378 0.8506 0.9170 -0.2279 -0.0935 0.1423  1301 SER B CB  
24337 O OG  . SER C 1301 ? 1.2629 0.8974 0.9625 -0.2144 -0.1007 0.1479  1301 SER B OG  
24338 N N   . LEU C 1302 ? 1.1375 0.7524 0.8084 -0.2761 -0.0797 0.1360  1302 LEU B N   
24339 C CA  . LEU C 1302 ? 1.2093 0.8151 0.8631 -0.2954 -0.0647 0.1300  1302 LEU B CA  
24340 C C   . LEU C 1302 ? 1.2142 0.8652 0.8938 -0.3202 -0.0644 0.1316  1302 LEU B C   
24341 O O   . LEU C 1302 ? 1.2860 0.9526 0.9606 -0.3425 -0.0477 0.1287  1302 LEU B O   
24342 C CB  . LEU C 1302 ? 1.2679 0.8293 0.8996 -0.2832 -0.0707 0.1241  1302 LEU B CB  
24343 C CG  . LEU C 1302 ? 1.3305 0.8452 0.9260 -0.2665 -0.0618 0.1209  1302 LEU B CG  
24344 C CD1 . LEU C 1302 ? 1.3422 0.8179 0.9184 -0.2489 -0.0713 0.1172  1302 LEU B CD1 
24345 C CD2 . LEU C 1302 ? 1.3642 0.8708 0.9387 -0.2857 -0.0376 0.1182  1302 LEU B CD2 
24346 N N   . LEU C 1303 ? 1.1194 0.7912 0.8248 -0.3176 -0.0829 0.1361  1303 LEU B N   
24347 C CA  . LEU C 1303 ? 1.0244 0.7469 0.7583 -0.3391 -0.0859 0.1396  1303 LEU B CA  
24348 C C   . LEU C 1303 ? 0.9282 0.7055 0.6882 -0.3526 -0.0813 0.1481  1303 LEU B C   
24349 O O   . LEU C 1303 ? 0.9076 0.7202 0.6755 -0.3764 -0.0719 0.1464  1303 LEU B O   
24350 C CB  . LEU C 1303 ? 1.0123 0.7435 0.7664 -0.3315 -0.1077 0.1446  1303 LEU B CB  
24351 C CG  . LEU C 1303 ? 0.9405 0.7258 0.7312 -0.3445 -0.1202 0.1540  1303 LEU B CG  
24352 C CD1 . LEU C 1303 ? 0.8792 0.7092 0.6957 -0.3513 -0.1192 0.1648  1303 LEU B CD1 
24353 C CD2 . LEU C 1303 ? 0.9552 0.7596 0.7442 -0.3643 -0.1132 0.1465  1303 LEU B CD2 
24354 N N   . VAL C 1304 ? 0.9173 0.7028 0.6901 -0.3366 -0.0884 0.1568  1304 VAL B N   
24355 C CA  . VAL C 1304 ? 0.9406 0.7776 0.7358 -0.3440 -0.0829 0.1659  1304 VAL B CA  
24356 C C   . VAL C 1304 ? 0.9603 0.7901 0.7333 -0.3460 -0.0630 0.1614  1304 VAL B C   
24357 O O   . VAL C 1304 ? 1.0433 0.8261 0.7901 -0.3292 -0.0601 0.1560  1304 VAL B O   
24358 C CB  . VAL C 1304 ? 0.9748 0.8188 0.7916 -0.3210 -0.0993 0.1773  1304 VAL B CB  
24359 C CG1 . VAL C 1304 ? 1.0048 0.8969 0.8393 -0.3221 -0.0914 0.1864  1304 VAL B CG1 
24360 C CG2 . VAL C 1304 ? 0.9352 0.7915 0.7782 -0.3199 -0.1205 0.1859  1304 VAL B CG2 
24361 N N   . LYS C 1305 ? 1.7300 0.8790 0.8759 -0.3706 -0.1765 0.1298  1305 LYS B N   
24362 C CA  . LYS C 1305 ? 1.7914 0.9295 0.8877 -0.3834 -0.1694 0.1216  1305 LYS B CA  
24363 C C   . LYS C 1305 ? 1.8161 0.9780 0.9302 -0.3707 -0.1854 0.1147  1305 LYS B C   
24364 O O   . LYS C 1305 ? 1.8019 1.0025 0.9678 -0.3589 -0.2004 0.1166  1305 LYS B O   
24365 C CB  . LYS C 1305 ? 1.8297 0.9848 0.8954 -0.4169 -0.1511 0.1216  1305 LYS B CB  
24366 C CG  . LYS C 1305 ? 1.9123 1.0309 0.9098 -0.4336 -0.1355 0.1143  1305 LYS B CG  
24367 C CD  . LYS C 1305 ? 2.2121 1.3107 1.1621 -0.4647 -0.1117 0.1166  1305 LYS B CD  
24368 C CE  . LYS C 1305 ? 2.3258 1.3679 1.2503 -0.4571 -0.1024 0.1226  1305 LYS B CE  
24369 N NZ  . LYS C 1305 ? 2.3492 1.3748 1.2292 -0.4886 -0.0796 0.1252  1305 LYS B NZ  
24370 N N   . GLN C 1306 ? 1.8664 1.0014 0.9344 -0.3728 -0.1811 0.1068  1306 GLN B N   
24371 C CA  . GLN C 1306 ? 1.8613 1.0151 0.9406 -0.3609 -0.1947 0.1001  1306 GLN B CA  
24372 C C   . GLN C 1306 ? 1.8360 1.0474 0.9339 -0.3787 -0.1919 0.0998  1306 GLN B C   
24373 O O   . GLN C 1306 ? 1.8699 1.1040 0.9722 -0.3984 -0.1813 0.1045  1306 GLN B O   
24374 C CB  . GLN C 1306 ? 2.3943 1.5019 1.4146 -0.3596 -0.1888 0.0916  1306 GLN B CB  
24375 C CG  . GLN C 1306 ? 3.0323 2.1085 2.0603 -0.3259 -0.2086 0.0881  1306 GLN B CG  
24376 C CD  . GLN C 1306 ? 2.1767 1.2116 1.1483 -0.3221 -0.2051 0.0791  1306 GLN B CD  
24377 O OE1 . GLN C 1306 ? 2.1634 1.2175 1.1292 -0.3269 -0.2056 0.0736  1306 GLN B OE1 
24378 N NE2 . GLN C 1306 ? 2.2251 1.2022 1.1550 -0.3112 -0.2018 0.0777  1306 GLN B NE2 
24379 N N   . LEU C 1307 ? 1.8017 1.0379 0.9108 -0.3711 -0.2013 0.0945  1307 LEU B N   
24380 C CA  . LEU C 1307 ? 1.7620 1.0533 0.8815 -0.3888 -0.1961 0.0934  1307 LEU B CA  
24381 C C   . LEU C 1307 ? 1.7676 1.0668 0.8668 -0.3889 -0.1957 0.0849  1307 LEU B C   
24382 O O   . LEU C 1307 ? 1.7504 1.0644 0.8769 -0.3674 -0.2116 0.0833  1307 LEU B O   
24383 C CB  . LEU C 1307 ? 1.7367 1.0779 0.9169 -0.3772 -0.2102 0.0996  1307 LEU B CB  
24384 C CG  . LEU C 1307 ? 1.7256 1.0687 0.9460 -0.3672 -0.2175 0.1085  1307 LEU B CG  
24385 C CD1 . LEU C 1307 ? 1.7517 1.0560 0.9880 -0.3404 -0.2320 0.1088  1307 LEU B CD1 
24386 C CD2 . LEU C 1307 ? 1.6740 1.0734 0.9398 -0.3627 -0.2264 0.1123  1307 LEU B CD2 
24387 N N   . ARG C 1308 ? 1.7658 1.0549 0.8158 -0.4147 -0.1761 0.0793  1308 ARG B N   
24388 C CA  . ARG C 1308 ? 1.7222 1.0193 0.7463 -0.4214 -0.1700 0.0706  1308 ARG B CA  
24389 C C   . ARG C 1308 ? 1.6347 0.9728 0.7013 -0.4001 -0.1871 0.0700  1308 ARG B C   
24390 O O   . ARG C 1308 ? 1.5479 0.9440 0.6526 -0.4030 -0.1909 0.0732  1308 ARG B O   
24391 C CB  . ARG C 1308 ? 1.7260 1.0516 0.7236 -0.4585 -0.1484 0.0669  1308 ARG B CB  
24392 C CG  . ARG C 1308 ? 1.7192 1.0896 0.7180 -0.4674 -0.1442 0.0600  1308 ARG B CG  
24393 C CD  . ARG C 1308 ? 1.7791 1.1476 0.7286 -0.5051 -0.1192 0.0528  1308 ARG B CD  
24394 N NE  . ARG C 1308 ? 1.8119 1.2045 0.7487 -0.5125 -0.1119 0.0439  1308 ARG B NE  
24395 C CZ  . ARG C 1308 ? 1.8036 1.2619 0.7831 -0.5052 -0.1205 0.0436  1308 ARG B CZ  
24396 N NH1 . ARG C 1308 ? 1.7417 1.2448 0.7760 -0.4906 -0.1367 0.0518  1308 ARG B NH1 
24397 N NH2 . ARG C 1308 ? 1.8336 1.3109 0.7991 -0.5114 -0.1121 0.0352  1308 ARG B NH2 
24398 N N   . LEU C 1309 ? 1.6425 0.9467 0.6991 -0.3775 -0.1974 0.0659  1309 LEU B N   
24399 C CA  . LEU C 1309 ? 1.6233 0.9540 0.7104 -0.3556 -0.2131 0.0645  1309 LEU B CA  
24400 C C   . LEU C 1309 ? 1.6258 0.9976 0.7030 -0.3693 -0.2024 0.0587  1309 LEU B C   
24401 O O   . LEU C 1309 ? 1.6448 0.9981 0.6749 -0.3879 -0.1850 0.0516  1309 LEU B O   
24402 C CB  . LEU C 1309 ? 1.6126 0.8895 0.6824 -0.3302 -0.2257 0.0606  1309 LEU B CB  
24403 C CG  . LEU C 1309 ? 1.5892 0.8391 0.6867 -0.3057 -0.2450 0.0652  1309 LEU B CG  
24404 C CD1 . LEU C 1309 ? 1.6243 0.8140 0.6840 -0.2901 -0.2501 0.0595  1309 LEU B CD1 
24405 C CD2 . LEU C 1309 ? 1.5309 0.8162 0.6828 -0.2848 -0.2648 0.0687  1309 LEU B CD2 
24406 N N   . SER C 1310 ? 1.5277 0.9539 0.6481 -0.3591 -0.2121 0.0615  1310 SER B N   
24407 C CA  . SER C 1310 ? 1.5301 0.9975 0.6457 -0.3664 -0.2040 0.0561  1310 SER B CA  
24408 C C   . SER C 1310 ? 1.5783 1.0952 0.7415 -0.3451 -0.2189 0.0600  1310 SER B C   
24409 O O   . SER C 1310 ? 1.4782 1.0550 0.6584 -0.3548 -0.2130 0.0601  1310 SER B O   
24410 C CB  . SER C 1310 ? 1.5758 1.0777 0.6731 -0.4023 -0.1825 0.0529  1310 SER B CB  
24411 O OG  . SER C 1310 ? 1.5709 1.1364 0.6859 -0.4064 -0.1788 0.0500  1310 SER B OG  
24412 N N   . MET C 1311 ? 1.5788 1.0697 0.7619 -0.3158 -0.2383 0.0631  1311 MET B N   
24413 C CA  . MET C 1311 ? 1.6011 1.1211 0.8149 -0.2918 -0.2518 0.0648  1311 MET B CA  
24414 C C   . MET C 1311 ? 1.6268 1.1483 0.8165 -0.2870 -0.2464 0.0576  1311 MET B C   
24415 O O   . MET C 1311 ? 1.6595 1.1625 0.8082 -0.3044 -0.2306 0.0506  1311 MET B O   
24416 C CB  . MET C 1311 ? 1.4566 0.9409 0.6919 -0.2646 -0.2729 0.0685  1311 MET B CB  
24417 C CG  . MET C 1311 ? 1.4257 0.9279 0.7001 -0.2619 -0.2808 0.0767  1311 MET B CG  
24418 S SD  . MET C 1311 ? 1.6556 1.0999 0.9398 -0.2452 -0.2973 0.0786  1311 MET B SD  
24419 C CE  . MET C 1311 ? 1.7186 1.1367 0.9728 -0.2714 -0.2809 0.0784  1311 MET B CE  
24420 N N   . ASP C 1312 ? 1.6735 1.2138 0.8872 -0.2625 -0.2590 0.0594  1312 ASP B N   
24421 C CA  . ASP C 1312 ? 1.7010 1.2529 0.8996 -0.2543 -0.2545 0.0540  1312 ASP B CA  
24422 C C   . ASP C 1312 ? 1.6593 1.1953 0.8768 -0.2210 -0.2746 0.0568  1312 ASP B C   
24423 O O   . ASP C 1312 ? 1.6269 1.2029 0.8666 -0.2066 -0.2784 0.0595  1312 ASP B O   
24424 C CB  . ASP C 1312 ? 1.7575 1.3831 0.9723 -0.2664 -0.2425 0.0543  1312 ASP B CB  
24425 C CG  . ASP C 1312 ? 1.8604 1.4977 1.0472 -0.2734 -0.2274 0.0463  1312 ASP B CG  
24426 O OD1 . ASP C 1312 ? 1.9069 1.4963 1.0667 -0.2594 -0.2303 0.0420  1312 ASP B OD1 
24427 O OD2 . ASP C 1312 ? 1.8786 1.5733 1.0701 -0.2933 -0.2125 0.0440  1312 ASP B OD2 
24428 N N   . ILE C 1313 ? 1.6532 1.1301 0.8611 -0.2087 -0.2877 0.0560  1313 ILE B N   
24429 C CA  . ILE C 1313 ? 1.6296 1.0871 0.8595 -0.1804 -0.3090 0.0589  1313 ILE B CA  
24430 C C   . ILE C 1313 ? 1.6949 1.1524 0.9144 -0.1612 -0.3123 0.0559  1313 ILE B C   
24431 O O   . ILE C 1313 ? 1.7880 1.2426 0.9750 -0.1674 -0.2994 0.0500  1313 ILE B O   
24432 C CB  . ILE C 1313 ? 1.5992 0.9954 0.8167 -0.1732 -0.3213 0.0567  1313 ILE B CB  
24433 C CG1 . ILE C 1313 ? 1.6046 0.9911 0.8124 -0.1960 -0.3109 0.0572  1313 ILE B CG1 
24434 C CG2 . ILE C 1313 ? 1.5738 0.9617 0.8274 -0.1521 -0.3427 0.0612  1313 ILE B CG2 
24435 C CD1 . ILE C 1313 ? 1.6080 0.9789 0.8450 -0.1900 -0.3245 0.0621  1313 ILE B CD1 
24436 N N   . ASP C 1314 ? 1.6421 1.1001 0.8870 -0.1378 -0.3289 0.0599  1314 ASP B N   
24437 C CA  . ASP C 1314 ? 1.6270 1.0805 0.8607 -0.1171 -0.3329 0.0578  1314 ASP B CA  
24438 C C   . ASP C 1314 ? 1.6173 1.0365 0.8657 -0.0931 -0.3550 0.0597  1314 ASP B C   
24439 O O   . ASP C 1314 ? 1.5919 1.0311 0.8738 -0.0848 -0.3636 0.0660  1314 ASP B O   
24440 C CB  . ASP C 1314 ? 1.6327 1.1491 0.8832 -0.1144 -0.3233 0.0615  1314 ASP B CB  
24441 C CG  . ASP C 1314 ? 1.6737 1.1841 0.9239 -0.0862 -0.3327 0.0624  1314 ASP B CG  
24442 O OD1 . ASP C 1314 ? 1.6560 1.1565 0.9287 -0.0686 -0.3485 0.0673  1314 ASP B OD1 
24443 O OD2 . ASP C 1314 ? 1.7343 1.2467 0.9592 -0.0820 -0.3232 0.0580  1314 ASP B OD2 
24444 N N   . VAL C 1315 ? 1.6289 0.9943 0.8494 -0.0822 -0.3642 0.0537  1315 VAL B N   
24445 C CA  . VAL C 1315 ? 1.6146 0.9437 0.8440 -0.0599 -0.3861 0.0537  1315 VAL B CA  
24446 C C   . VAL C 1315 ? 1.6440 0.9769 0.8602 -0.0403 -0.3862 0.0532  1315 VAL B C   
24447 O O   . VAL C 1315 ? 1.6705 1.0083 0.8573 -0.0430 -0.3722 0.0496  1315 VAL B O   
24448 C CB  . VAL C 1315 ? 1.6215 0.8916 0.8293 -0.0587 -0.3977 0.0473  1315 VAL B CB  
24449 C CG1 . VAL C 1315 ? 1.6026 0.8462 0.7612 -0.0629 -0.3861 0.0403  1315 VAL B CG1 
24450 C CG2 . VAL C 1315 ? 1.5743 0.8090 0.7934 -0.0378 -0.4218 0.0461  1315 VAL B CG2 
24451 N N   . SER C 1316 ? 1.6770 1.0093 0.9140 -0.0216 -0.3997 0.0572  1316 SER B N   
24452 C CA  . SER C 1316 ? 1.7463 1.0909 0.9741 -0.0026 -0.3972 0.0588  1316 SER B CA  
24453 C C   . SER C 1316 ? 1.8115 1.1328 1.0519 0.0195  -0.4155 0.0616  1316 SER B C   
24454 O O   . SER C 1316 ? 1.8029 1.1259 1.0736 0.0179  -0.4251 0.0653  1316 SER B O   
24455 C CB  . SER C 1316 ? 1.7353 1.1474 0.9789 -0.0090 -0.3794 0.0644  1316 SER B CB  
24456 O OG  . SER C 1316 ? 1.7647 1.1892 0.9894 0.0065  -0.3717 0.0639  1316 SER B OG  
24457 N N   . TYR C 1317 ? 1.8863 1.1838 1.1017 0.0394  -0.4191 0.0595  1317 TYR B N   
24458 C CA  . TYR C 1317 ? 1.9497 1.2194 1.1710 0.0596  -0.4357 0.0614  1317 TYR B CA  
24459 C C   . TYR C 1317 ? 1.9426 1.2551 1.1833 0.0700  -0.4286 0.0699  1317 TYR B C   
24460 O O   . TYR C 1317 ? 1.9366 1.2867 1.1685 0.0747  -0.4131 0.0723  1317 TYR B O   
24461 C CB  . TYR C 1317 ? 2.0487 1.2715 1.2309 0.0776  -0.4422 0.0560  1317 TYR B CB  
24462 C CG  . TYR C 1317 ? 2.1293 1.3029 1.2890 0.0717  -0.4524 0.0475  1317 TYR B CG  
24463 C CD1 . TYR C 1317 ? 2.1802 1.3493 1.3098 0.0631  -0.4396 0.0427  1317 TYR B CD1 
24464 C CD2 . TYR C 1317 ? 2.1672 1.2991 1.3352 0.0746  -0.4745 0.0438  1317 TYR B CD2 
24465 C CE1 . TYR C 1317 ? 2.2457 1.3658 1.3500 0.0597  -0.4491 0.0349  1317 TYR B CE1 
24466 C CE2 . TYR C 1317 ? 2.2340 1.3221 1.3811 0.0715  -0.4855 0.0357  1317 TYR B CE2 
24467 C CZ  . TYR C 1317 ? 2.2745 1.3546 1.3878 0.0652  -0.4730 0.0315  1317 TYR B CZ  
24468 O OH  . TYR C 1317 ? 2.3129 1.3451 1.4007 0.0645  -0.4843 0.0235  1317 TYR B OH  
24469 N N   . LYS C 1318 ? 1.9392 1.2453 1.2046 0.0747  -0.4397 0.0741  1318 LYS B N   
24470 C CA  . LYS C 1318 ? 1.9423 1.2829 1.2225 0.0869  -0.4337 0.0824  1318 LYS B CA  
24471 C C   . LYS C 1318 ? 2.0304 1.3782 1.2851 0.1101  -0.4263 0.0846  1318 LYS B C   
24472 O O   . LYS C 1318 ? 2.0097 1.4088 1.2720 0.1151  -0.4129 0.0904  1318 LYS B O   
24473 C CB  . LYS C 1318 ? 1.9285 1.2454 1.2296 0.0913  -0.4473 0.0854  1318 LYS B CB  
24474 C CG  . LYS C 1318 ? 1.9583 1.2883 1.2583 0.1124  -0.4437 0.0929  1318 LYS B CG  
24475 C CD  . LYS C 1318 ? 1.9601 1.3142 1.2917 0.1067  -0.4420 0.0999  1318 LYS B CD  
24476 C CE  . LYS C 1318 ? 1.9776 1.2872 1.3244 0.1008  -0.4572 0.0976  1318 LYS B CE  
24477 N NZ  . LYS C 1318 ? 1.9584 1.2876 1.3321 0.0967  -0.4536 0.1047  1318 LYS B NZ  
24478 N N   . HIS C 1319 ? 2.1463 1.4442 1.3705 0.1252  -0.4350 0.0800  1319 HIS B N   
24479 C CA  . HIS C 1319 ? 2.2389 1.5395 1.4353 0.1485  -0.4269 0.0820  1319 HIS B CA  
24480 C C   . HIS C 1319 ? 2.3966 1.6873 1.5611 0.1478  -0.4187 0.0757  1319 HIS B C   
24481 O O   . HIS C 1319 ? 2.4102 1.7346 1.5629 0.1571  -0.4030 0.0778  1319 HIS B O   
24482 C CB  . HIS C 1319 ? 2.2028 1.4537 1.3833 0.1706  -0.4402 0.0832  1319 HIS B CB  
24483 C CG  . HIS C 1319 ? 2.1661 1.4133 1.3736 0.1689  -0.4491 0.0877  1319 HIS B CG  
24484 N ND1 . HIS C 1319 ? 2.1591 1.3699 1.3813 0.1553  -0.4653 0.0832  1319 HIS B ND1 
24485 C CD2 . HIS C 1319 ? 2.1648 1.4401 1.3867 0.1789  -0.4434 0.0962  1319 HIS B CD2 
24486 C CE1 . HIS C 1319 ? 2.1508 1.3664 1.3957 0.1556  -0.4681 0.0885  1319 HIS B CE1 
24487 N NE2 . HIS C 1319 ? 2.1566 1.4087 1.3997 0.1702  -0.4550 0.0965  1319 HIS B NE2 
24488 N N   . LYS C 1320 ? 2.5495 1.7939 1.6991 0.1376  -0.4290 0.0679  1320 LYS B N   
24489 C CA  . LYS C 1320 ? 2.7268 1.9567 1.8429 0.1347  -0.4203 0.0614  1320 LYS B CA  
24490 C C   . LYS C 1320 ? 2.7948 2.0807 1.9215 0.1143  -0.4000 0.0614  1320 LYS B C   
24491 O O   . LYS C 1320 ? 2.7865 2.1079 1.9451 0.0967  -0.3979 0.0642  1320 LYS B O   
24492 C CB  . LYS C 1320 ? 2.8033 1.9712 1.9008 0.1284  -0.4368 0.0530  1320 LYS B CB  
24493 C CG  . LYS C 1320 ? 2.8851 2.0366 1.9473 0.1213  -0.4264 0.0461  1320 LYS B CG  
24494 C CD  . LYS C 1320 ? 2.9746 2.1134 1.9993 0.1411  -0.4165 0.0455  1320 LYS B CD  
24495 C CE  . LYS C 1320 ? 3.0274 2.1468 2.0140 0.1333  -0.4040 0.0384  1320 LYS B CE  
24496 N NZ  . LYS C 1320 ? 3.0749 2.1727 2.0217 0.1536  -0.3951 0.0372  1320 LYS B NZ  
24497 N N   . GLY C 1321 ? 2.8512 2.1432 1.9494 0.1155  -0.3845 0.0580  1321 GLY B N   
24498 C CA  . GLY C 1321 ? 2.8296 2.1693 1.9321 0.0938  -0.3641 0.0561  1321 GLY B CA  
24499 C C   . GLY C 1321 ? 2.7910 2.1261 1.9070 0.0673  -0.3676 0.0532  1321 GLY B C   
24500 O O   . GLY C 1321 ? 2.8386 2.1265 1.9545 0.0666  -0.3857 0.0508  1321 GLY B O   
24501 N N   . ALA C 1322 ? 2.7033 2.0887 1.8309 0.0454  -0.3500 0.0530  1322 ALA B N   
24502 C CA  . ALA C 1322 ? 2.5818 1.9653 1.7201 0.0198  -0.3505 0.0509  1322 ALA B CA  
24503 C C   . ALA C 1322 ? 2.5944 1.9125 1.6969 0.0146  -0.3563 0.0430  1322 ALA B C   
24504 O O   . ALA C 1322 ? 2.5662 1.8608 1.6310 0.0173  -0.3470 0.0375  1322 ALA B O   
24505 C CB  . ALA C 1322 ? 2.5570 2.0037 1.7065 -0.0040 -0.3285 0.0511  1322 ALA B CB  
24506 N N   . LEU C 1323 ? 2.5590 1.8471 1.6726 0.0084  -0.3716 0.0423  1323 LEU B N   
24507 C CA  . LEU C 1323 ? 2.4866 1.7235 1.5692 -0.0005 -0.3744 0.0352  1323 LEU B CA  
24508 C C   . LEU C 1323 ? 2.5648 1.8332 1.6499 -0.0290 -0.3558 0.0346  1323 LEU B C   
24509 O O   . LEU C 1323 ? 2.6069 1.9355 1.7128 -0.0400 -0.3407 0.0385  1323 LEU B O   
24510 C CB  . LEU C 1323 ? 2.2872 1.4803 1.3816 0.0082  -0.3999 0.0344  1323 LEU B CB  
24511 C CG  . LEU C 1323 ? 1.9671 1.1206 1.0511 -0.0021 -0.4084 0.0296  1323 LEU B CG  
24512 C CD1 . LEU C 1323 ? 1.9565 1.0716 0.9890 -0.0064 -0.3983 0.0222  1323 LEU B CD1 
24513 C CD2 . LEU C 1323 ? 1.8957 1.0100 0.9923 0.0136  -0.4357 0.0281  1323 LEU B CD2 
24514 N N   . HIS C 1324 ? 2.5349 1.7625 1.5966 -0.0404 -0.3569 0.0294  1324 HIS B N   
24515 C CA  . HIS C 1324 ? 2.4949 1.7396 1.5457 -0.0677 -0.3371 0.0275  1324 HIS B CA  
24516 C C   . HIS C 1324 ? 2.4457 1.7442 1.5386 -0.0858 -0.3322 0.0338  1324 HIS B C   
24517 O O   . HIS C 1324 ? 2.3897 1.7031 1.5210 -0.0774 -0.3467 0.0397  1324 HIS B O   
24518 C CB  . HIS C 1324 ? 2.5636 1.7446 1.5756 -0.0721 -0.3407 0.0210  1324 HIS B CB  
24519 C CG  . HIS C 1324 ? 2.6194 1.7813 1.6542 -0.0716 -0.3587 0.0231  1324 HIS B CG  
24520 N ND1 . HIS C 1324 ? 2.6444 1.8258 1.6941 -0.0926 -0.3507 0.0257  1324 HIS B ND1 
24521 C CD2 . HIS C 1324 ? 2.6657 1.7912 1.7108 -0.0530 -0.3839 0.0225  1324 HIS B CD2 
24522 C CE1 . HIS C 1324 ? 2.6581 1.8168 1.7272 -0.0860 -0.3693 0.0271  1324 HIS B CE1 
24523 N NE2 . HIS C 1324 ? 2.6749 1.8016 1.7433 -0.0626 -0.3899 0.0248  1324 HIS B NE2 
24524 N N   . ASN C 1325 ? 2.4690 1.7934 1.5513 -0.1115 -0.3110 0.0321  1325 ASN B N   
24525 C CA  . ASN C 1325 ? 2.4645 1.8404 1.5800 -0.1312 -0.3035 0.0373  1325 ASN B CA  
24526 C C   . ASN C 1325 ? 2.4104 1.7894 1.4984 -0.1609 -0.2817 0.0328  1325 ASN B C   
24527 O O   . ASN C 1325 ? 2.4046 1.8008 1.4694 -0.1717 -0.2630 0.0282  1325 ASN B O   
24528 C CB  . ASN C 1325 ? 2.5321 1.9763 1.6808 -0.1266 -0.2988 0.0426  1325 ASN B CB  
24529 C CG  . ASN C 1325 ? 2.6012 2.0681 1.7281 -0.1258 -0.2824 0.0383  1325 ASN B CG  
24530 O OD1 . ASN C 1325 ? 2.6310 2.0791 1.7468 -0.1028 -0.2887 0.0373  1325 ASN B OD1 
24531 N ND2 . ASN C 1325 ? 2.6069 2.1158 1.7283 -0.1513 -0.2607 0.0355  1325 ASN B ND2 
24532 N N   . TYR C 1326 ? 2.3806 1.7437 1.4709 -0.1751 -0.2829 0.0342  1326 TYR B N   
24533 C CA  . TYR C 1326 ? 2.4025 1.7487 1.4551 -0.2015 -0.2632 0.0290  1326 TYR B CA  
24534 C C   . TYR C 1326 ? 2.2749 1.6497 1.3435 -0.2267 -0.2541 0.0326  1326 TYR B C   
24535 O O   . TYR C 1326 ? 2.2306 1.6050 1.3287 -0.2222 -0.2671 0.0385  1326 TYR B O   
24536 C CB  . TYR C 1326 ? 2.5599 1.8291 1.5725 -0.1933 -0.2705 0.0243  1326 TYR B CB  
24537 C CG  . TYR C 1326 ? 2.6476 1.8931 1.6868 -0.1781 -0.2935 0.0289  1326 TYR B CG  
24538 C CD1 . TYR C 1326 ? 2.6909 1.9100 1.7220 -0.1893 -0.2926 0.0296  1326 TYR B CD1 
24539 C CD2 . TYR C 1326 ? 2.6734 1.9228 1.7454 -0.1529 -0.3152 0.0322  1326 TYR B CD2 
24540 C CE1 . TYR C 1326 ? 2.7132 1.9143 1.7717 -0.1752 -0.3130 0.0333  1326 TYR B CE1 
24541 C CE2 . TYR C 1326 ? 2.6950 1.9250 1.7932 -0.1408 -0.3355 0.0353  1326 TYR B CE2 
24542 C CZ  . TYR C 1326 ? 2.7135 1.9216 1.8070 -0.1518 -0.3345 0.0359  1326 TYR B CZ  
24543 O OH  . TYR C 1326 ? 2.7129 1.9055 1.8359 -0.1393 -0.3543 0.0386  1326 TYR B OH  
24544 N N   . LYS C 1327 ? 2.1888 1.5843 1.2339 -0.2544 -0.2305 0.0283  1327 LYS B N   
24545 C CA  . LYS C 1327 ? 2.0863 1.4997 1.1340 -0.2821 -0.2189 0.0301  1327 LYS B CA  
24546 C C   . LYS C 1327 ? 1.9928 1.3419 1.0156 -0.2838 -0.2231 0.0302  1327 LYS B C   
24547 O O   . LYS C 1327 ? 2.0073 1.3029 0.9801 -0.2883 -0.2143 0.0240  1327 LYS B O   
24548 C CB  . LYS C 1327 ? 2.1376 1.5821 1.1598 -0.3130 -0.1920 0.0236  1327 LYS B CB  
24549 C CG  . LYS C 1327 ? 2.1750 1.6526 1.2066 -0.3430 -0.1805 0.0258  1327 LYS B CG  
24550 C CD  . LYS C 1327 ? 2.1966 1.7484 1.2401 -0.3668 -0.1631 0.0227  1327 LYS B CD  
24551 C CE  . LYS C 1327 ? 2.1474 1.7426 1.2158 -0.3891 -0.1599 0.0273  1327 LYS B CE  
24552 N NZ  . LYS C 1327 ? 2.0770 1.7023 1.1983 -0.3677 -0.1809 0.0374  1327 LYS B NZ  
24553 N N   . MET C 1328 ? 1.8800 1.2351 0.9380 -0.2785 -0.2364 0.0375  1328 MET B N   
24554 C CA  . MET C 1328 ? 1.7768 1.0830 0.8211 -0.2802 -0.2402 0.0391  1328 MET B CA  
24555 C C   . MET C 1328 ? 1.7841 1.0991 0.8100 -0.3125 -0.2198 0.0393  1328 MET B C   
24556 O O   . MET C 1328 ? 1.7587 1.1306 0.8072 -0.3298 -0.2110 0.0416  1328 MET B O   
24557 C CB  . MET C 1328 ? 1.6380 0.9519 0.7317 -0.2614 -0.2619 0.0467  1328 MET B CB  
24558 C CG  . MET C 1328 ? 1.5971 0.8736 0.6856 -0.2639 -0.2646 0.0494  1328 MET B CG  
24559 S SD  . MET C 1328 ? 1.5594 0.8229 0.6946 -0.2331 -0.2938 0.0542  1328 MET B SD  
24560 C CE  . MET C 1328 ? 2.2246 1.4173 1.3165 -0.2127 -0.3043 0.0462  1328 MET B CE  
24561 N N   . THR C 1329 ? 1.8328 1.0907 0.8164 -0.3196 -0.2126 0.0368  1329 THR B N   
24562 C CA  . THR C 1329 ? 1.8527 1.1060 0.8050 -0.3518 -0.1903 0.0357  1329 THR B CA  
24563 C C   . THR C 1329 ? 1.8694 1.0548 0.7867 -0.3480 -0.1903 0.0361  1329 THR B C   
24564 O O   . THR C 1329 ? 1.8886 1.0339 0.8046 -0.3212 -0.2071 0.0360  1329 THR B O   
24565 C CB  . THR C 1329 ? 1.8992 1.1536 0.8061 -0.3752 -0.1669 0.0270  1329 THR B CB  
24566 O OG1 . THR C 1329 ? 1.9473 1.1522 0.8173 -0.3581 -0.1692 0.0208  1329 THR B OG1 
24567 C CG2 . THR C 1329 ? 1.8818 1.2141 0.8244 -0.3852 -0.1627 0.0268  1329 THR B CG2 
24568 N N   . ASP C 1330 ? 1.8885 1.0589 0.7761 -0.3732 -0.1723 0.0364  1330 ASP B N   
24569 C CA  . ASP C 1330 ? 1.9534 1.0565 0.8072 -0.3639 -0.1737 0.0372  1330 ASP B CA  
24570 C C   . ASP C 1330 ? 2.0460 1.0866 0.8371 -0.3570 -0.1671 0.0289  1330 ASP B C   
24571 O O   . ASP C 1330 ? 2.1120 1.0911 0.8675 -0.3447 -0.1691 0.0284  1330 ASP B O   
24572 C CB  . ASP C 1330 ? 1.9885 1.0823 0.8235 -0.3888 -0.1571 0.0407  1330 ASP B CB  
24573 C CG  . ASP C 1330 ? 1.9501 1.1082 0.8397 -0.4005 -0.1597 0.0479  1330 ASP B CG  
24574 O OD1 . ASP C 1330 ? 1.8760 1.0536 0.8184 -0.3799 -0.1793 0.0549  1330 ASP B OD1 
24575 O OD2 . ASP C 1330 ? 1.9798 1.1669 0.8560 -0.4317 -0.1411 0.0459  1330 ASP B OD2 
24576 N N   . LYS C 1331 ? 2.0559 1.1116 0.8322 -0.3636 -0.1589 0.0224  1331 LYS B N   
24577 C CA  . LYS C 1331 ? 2.1123 1.1076 0.8266 -0.3575 -0.1512 0.0143  1331 LYS B CA  
24578 C C   . LYS C 1331 ? 2.1204 1.0821 0.8449 -0.3181 -0.1776 0.0146  1331 LYS B C   
24579 O O   . LYS C 1331 ? 2.1534 1.0545 0.8456 -0.3025 -0.1835 0.0142  1331 LYS B O   
24580 C CB  . LYS C 1331 ? 2.1188 1.1457 0.8210 -0.3752 -0.1351 0.0075  1331 LYS B CB  
24581 C CG  . LYS C 1331 ? 2.1011 1.1682 0.7986 -0.4151 -0.1109 0.0063  1331 LYS B CG  
24582 C CD  . LYS C 1331 ? 2.1480 1.1566 0.7891 -0.4330 -0.0939 0.0055  1331 LYS B CD  
24583 C CE  . LYS C 1331 ? 2.1800 1.2151 0.7984 -0.4771 -0.0658 0.0014  1331 LYS B CE  
24584 N NZ  . LYS C 1331 ? 2.2525 1.2155 0.7863 -0.4959 -0.0404 -0.0063 1331 LYS B NZ  
24585 N N   . ASN C 1332 ? 2.0828 1.0848 0.8515 -0.3020 -0.1936 0.0153  1332 ASN B N   
24586 C CA  . ASN C 1332 ? 2.1045 1.0911 0.9003 -0.2665 -0.2222 0.0169  1332 ASN B CA  
24587 C C   . ASN C 1332 ? 2.0814 1.1198 0.9499 -0.2585 -0.2402 0.0251  1332 ASN B C   
24588 O O   . ASN C 1332 ? 2.0569 1.1559 0.9636 -0.2692 -0.2371 0.0281  1332 ASN B O   
24589 C CB  . ASN C 1332 ? 2.1345 1.1306 0.9306 -0.2536 -0.2277 0.0123  1332 ASN B CB  
24590 C CG  . ASN C 1332 ? 2.0903 1.1623 0.9483 -0.2550 -0.2337 0.0169  1332 ASN B CG  
24591 O OD1 . ASN C 1332 ? 2.0457 1.1670 0.9162 -0.2802 -0.2168 0.0183  1332 ASN B OD1 
24592 N ND2 . ASN C 1332 ? 2.0769 1.1578 0.9725 -0.2276 -0.2580 0.0191  1332 ASN B ND2 
24593 N N   . PHE C 1333 ? 2.0754 1.0922 0.9645 -0.2390 -0.2591 0.0287  1333 PHE B N   
24594 C CA  . PHE C 1333 ? 2.0017 1.0640 0.9602 -0.2270 -0.2785 0.0352  1333 PHE B CA  
24595 C C   . PHE C 1333 ? 2.0582 1.0893 1.0284 -0.1955 -0.3047 0.0333  1333 PHE B C   
24596 O O   . PHE C 1333 ? 2.0699 1.1300 1.0876 -0.1812 -0.3226 0.0357  1333 PHE B O   
24597 C CB  . PHE C 1333 ? 1.8506 0.9394 0.8420 -0.2406 -0.2744 0.0429  1333 PHE B CB  
24598 C CG  . PHE C 1333 ? 1.8008 0.8428 0.7569 -0.2456 -0.2660 0.0433  1333 PHE B CG  
24599 C CD1 . PHE C 1333 ? 1.7376 0.7602 0.7161 -0.2272 -0.2821 0.0465  1333 PHE B CD1 
24600 C CD2 . PHE C 1333 ? 1.8313 0.8499 0.7318 -0.2695 -0.2408 0.0405  1333 PHE B CD2 
24601 C CE1 . PHE C 1333 ? 1.7705 0.7506 0.7155 -0.2299 -0.2734 0.0474  1333 PHE B CE1 
24602 C CE2 . PHE C 1333 ? 1.7817 0.7531 0.6453 -0.2729 -0.2320 0.0413  1333 PHE B CE2 
24603 C CZ  . PHE C 1333 ? 1.7743 0.7270 0.6600 -0.2520 -0.2483 0.0451  1333 PHE B CZ  
24604 N N   . LEU C 1334 ? 2.0741 1.0447 0.9980 -0.1846 -0.3068 0.0285  1334 LEU B N   
24605 C CA  . LEU C 1334 ? 2.0273 0.9671 0.9600 -0.1543 -0.3332 0.0257  1334 LEU B CA  
24606 C C   . LEU C 1334 ? 2.1127 1.0311 1.0158 -0.1416 -0.3384 0.0188  1334 LEU B C   
24607 O O   . LEU C 1334 ? 2.1925 1.0577 1.0565 -0.1234 -0.3478 0.0130  1334 LEU B O   
24608 C CB  . LEU C 1334 ? 1.9449 0.8322 0.8468 -0.1435 -0.3369 0.0241  1334 LEU B CB  
24609 C CG  . LEU C 1334 ? 1.8709 0.7406 0.7438 -0.1613 -0.3161 0.0272  1334 LEU B CG  
24610 C CD1 . LEU C 1334 ? 1.8038 0.7029 0.7301 -0.1620 -0.3227 0.0347  1334 LEU B CD1 
24611 C CD2 . LEU C 1334 ? 1.8739 0.7548 0.7117 -0.1928 -0.2862 0.0268  1334 LEU B CD2 
24612 N N   . GLY C 1335 ? 2.1563 1.1164 1.0771 -0.1502 -0.3320 0.0197  1335 GLY B N   
24613 C CA  . GLY C 1335 ? 2.2461 1.1953 1.1513 -0.1359 -0.3391 0.0146  1335 GLY B CA  
24614 C C   . GLY C 1335 ? 2.3371 1.2569 1.2513 -0.1052 -0.3683 0.0112  1335 GLY B C   
24615 O O   . GLY C 1335 ? 2.3259 1.2346 1.2641 -0.0918 -0.3874 0.0121  1335 GLY B O   
24616 N N   . ARG C 1336 ? 2.4061 1.3135 1.2990 -0.0946 -0.3711 0.0067  1336 ARG B N   
24617 C CA  . ARG C 1336 ? 2.5019 1.3771 1.3928 -0.0671 -0.3969 0.0022  1336 ARG B CA  
24618 C C   . ARG C 1336 ? 2.3626 1.2780 1.3206 -0.0583 -0.4174 0.0068  1336 ARG B C   
24619 O O   . ARG C 1336 ? 2.3157 1.2844 1.3130 -0.0723 -0.4081 0.0132  1336 ARG B O   
24620 C CB  . ARG C 1336 ? 2.7051 1.5705 1.5629 -0.0634 -0.3890 -0.0019 1336 ARG B CB  
24621 C CG  . ARG C 1336 ? 2.8178 1.7428 1.6980 -0.0836 -0.3679 0.0028  1336 ARG B CG  
24622 C CD  . ARG C 1336 ? 2.9525 1.8855 1.8273 -0.0731 -0.3683 0.0010  1336 ARG B CD  
24623 N NE  . ARG C 1336 ? 3.0258 2.0236 1.9316 -0.0887 -0.3519 0.0061  1336 ARG B NE  
24624 C CZ  . ARG C 1336 ? 3.1170 2.1314 2.0117 -0.0870 -0.3413 0.0048  1336 ARG B CZ  
24625 N NH1 . ARG C 1336 ? 3.1857 2.1530 2.0374 -0.0712 -0.3446 -0.0012 1336 ARG B NH1 
24626 N NH2 . ARG C 1336 ? 3.1090 2.1870 2.0345 -0.1001 -0.3274 0.0095  1336 ARG B NH2 
24627 N N   . PRO C 1337 ? 2.2615 1.1516 1.2320 -0.0359 -0.4451 0.0033  1337 PRO B N   
24628 C CA  . PRO C 1337 ? 2.1557 1.0767 1.1801 -0.0265 -0.4639 0.0059  1337 PRO B CA  
24629 C C   . PRO C 1337 ? 2.0904 1.0101 1.0987 -0.0184 -0.4635 0.0040  1337 PRO B C   
24630 O O   . PRO C 1337 ? 2.1056 1.0067 1.0665 -0.0223 -0.4470 0.0012  1337 PRO B O   
24631 C CB  . PRO C 1337 ? 2.1652 1.0553 1.2001 -0.0073 -0.4921 0.0010  1337 PRO B CB  
24632 C CG  . PRO C 1337 ? 2.2267 1.0898 1.2339 -0.0108 -0.4854 -0.0004 1337 PRO B CG  
24633 C CD  . PRO C 1337 ? 2.2828 1.1257 1.2308 -0.0222 -0.4595 -0.0017 1337 PRO B CD  
24634 N N   . VAL C 1338 ? 2.0822 1.0204 1.1276 -0.0079 -0.4795 0.0056  1338 VAL B N   
24635 C CA  . VAL C 1338 ? 2.1457 1.0853 1.1780 0.0010  -0.4782 0.0049  1338 VAL B CA  
24636 C C   . VAL C 1338 ? 2.2224 1.1591 1.2863 0.0177  -0.5038 0.0041  1338 VAL B C   
24637 O O   . VAL C 1338 ? 2.2180 1.1882 1.3322 0.0134  -0.5098 0.0090  1338 VAL B O   
24638 C CB  . VAL C 1338 ? 2.6399 1.6336 1.6873 -0.0147 -0.4540 0.0119  1338 VAL B CB  
24639 C CG1 . VAL C 1338 ? 2.6141 1.6329 1.6892 -0.0037 -0.4613 0.0154  1338 VAL B CG1 
24640 C CG2 . VAL C 1338 ? 2.6760 1.6600 1.6733 -0.0236 -0.4304 0.0091  1338 VAL B CG2 
24641 N N   . GLU C 1339 ? 2.3021 1.1962 1.3349 0.0360  -0.5186 -0.0024 1339 GLU B N   
24642 C CA  . GLU C 1339 ? 2.3471 1.2353 1.4058 0.0504  -0.5426 -0.0039 1339 GLU B CA  
24643 C C   . GLU C 1339 ? 2.3311 1.2461 1.3982 0.0521  -0.5327 0.0014  1339 GLU B C   
24644 O O   . GLU C 1339 ? 2.3262 1.2336 1.3567 0.0553  -0.5186 0.0011  1339 GLU B O   
24645 C CB  . GLU C 1339 ? 2.4763 1.3068 1.4983 0.0696  -0.5646 -0.0133 1339 GLU B CB  
24646 C CG  . GLU C 1339 ? 2.5500 1.3648 1.5903 0.0734  -0.5869 -0.0184 1339 GLU B CG  
24647 C CD  . GLU C 1339 ? 2.6517 1.4077 1.6451 0.0914  -0.6057 -0.0284 1339 GLU B CD  
24648 O OE1 . GLU C 1339 ? 2.6973 1.4276 1.6772 0.1056  -0.6218 -0.0329 1339 GLU B OE1 
24649 O OE2 . GLU C 1339 ? 2.6758 1.4092 1.6438 0.0921  -0.6044 -0.0317 1339 GLU B OE2 
24650 N N   . VAL C 1340 ? 2.3205 1.2680 1.4356 0.0499  -0.5386 0.0065  1340 VAL B N   
24651 C CA  . VAL C 1340 ? 2.3452 1.3228 1.4708 0.0520  -0.5278 0.0128  1340 VAL B CA  
24652 C C   . VAL C 1340 ? 2.3883 1.3276 1.4931 0.0715  -0.5446 0.0082  1340 VAL B C   
24653 O O   . VAL C 1340 ? 2.4202 1.3416 1.5444 0.0779  -0.5668 0.0049  1340 VAL B O   
24654 C CB  . VAL C 1340 ? 2.3238 1.3439 1.5038 0.0437  -0.5279 0.0199  1340 VAL B CB  
24655 C CG1 . VAL C 1340 ? 2.3357 1.3740 1.5227 0.0530  -0.5238 0.0252  1340 VAL B CG1 
24656 C CG2 . VAL C 1340 ? 2.2956 1.3568 1.4931 0.0238  -0.5082 0.0255  1340 VAL B CG2 
24657 N N   . LEU C 1341 ? 2.4106 1.3358 1.4746 0.0805  -0.5340 0.0075  1341 LEU B N   
24658 C CA  . LEU C 1341 ? 2.4812 1.3607 1.5158 0.1001  -0.5499 0.0024  1341 LEU B CA  
24659 C C   . LEU C 1341 ? 2.5124 1.4072 1.5693 0.1086  -0.5534 0.0076  1341 LEU B C   
24660 O O   . LEU C 1341 ? 2.5225 1.3952 1.5931 0.1157  -0.5749 0.0046  1341 LEU B O   
24661 C CB  . LEU C 1341 ? 2.4953 1.3463 1.4727 0.1082  -0.5370 -0.0008 1341 LEU B CB  
24662 C CG  . LEU C 1341 ? 2.7706 1.5640 1.6977 0.1149  -0.5453 -0.0101 1341 LEU B CG  
24663 C CD1 . LEU C 1341 ? 2.7834 1.5353 1.7137 0.1250  -0.5778 -0.0176 1341 LEU B CD1 
24664 C CD2 . LEU C 1341 ? 2.7615 1.5619 1.6734 0.0994  -0.5276 -0.0109 1341 LEU B CD2 
24665 N N   . LEU C 1342 ? 2.5355 1.4690 1.5957 0.1076  -0.5319 0.0151  1342 LEU B N   
24666 C CA  . LEU C 1342 ? 2.5429 1.4785 1.6040 0.1221  -0.5325 0.0194  1342 LEU B CA  
24667 C C   . LEU C 1342 ? 2.5121 1.4590 1.6157 0.1207  -0.5455 0.0226  1342 LEU B C   
24668 O O   . LEU C 1342 ? 2.4679 1.4335 1.6079 0.1064  -0.5502 0.0231  1342 LEU B O   
24669 C CB  . LEU C 1342 ? 2.5181 1.4948 1.5710 0.1236  -0.5063 0.0262  1342 LEU B CB  
24670 C CG  . LEU C 1342 ? 2.4967 1.4728 1.5185 0.1150  -0.4901 0.0225  1342 LEU B CG  
24671 C CD1 . LEU C 1342 ? 2.4778 1.4989 1.4928 0.1142  -0.4632 0.0277  1342 LEU B CD1 
24672 C CD2 . LEU C 1342 ? 2.5283 1.4395 1.5005 0.1261  -0.5011 0.0136  1342 LEU B CD2 
24673 N N   . ASN C 1343 ? 2.5503 1.4799 1.6449 0.1361  -0.5510 0.0244  1343 ASN B N   
24674 C CA  . ASN C 1343 ? 2.5992 1.5316 1.7260 0.1362  -0.5617 0.0272  1343 ASN B CA  
24675 C C   . ASN C 1343 ? 2.5653 1.5498 1.7178 0.1344  -0.5429 0.0379  1343 ASN B C   
24676 O O   . ASN C 1343 ? 2.5722 1.5562 1.7117 0.1496  -0.5369 0.0429  1343 ASN B O   
24677 C CB  . ASN C 1343 ? 2.7322 1.6124 1.8318 0.1533  -0.5778 0.0230  1343 ASN B CB  
24678 C CG  . ASN C 1343 ? 2.8601 1.6901 1.9452 0.1529  -0.6027 0.0115  1343 ASN B CG  
24679 O OD1 . ASN C 1343 ? 2.9113 1.7122 2.0039 0.1545  -0.6222 0.0068  1343 ASN B OD1 
24680 N ND2 . ASN C 1343 ? 2.9045 1.7248 1.9685 0.1504  -0.6020 0.0065  1343 ASN B ND2 
24681 N N   . ASP C 1344 ? 2.5151 1.5427 1.7017 0.1170  -0.5339 0.0415  1344 ASP B N   
24682 C CA  . ASP C 1344 ? 2.4421 1.5228 1.6516 0.1142  -0.5157 0.0513  1344 ASP B CA  
24683 C C   . ASP C 1344 ? 2.3893 1.4989 1.6411 0.0941  -0.5153 0.0534  1344 ASP B C   
24684 O O   . ASP C 1344 ? 2.4141 1.5091 1.6741 0.0824  -0.5248 0.0476  1344 ASP B O   
24685 C CB  . ASP C 1344 ? 2.3687 1.4823 1.5581 0.1153  -0.4948 0.0540  1344 ASP B CB  
24686 C CG  . ASP C 1344 ? 2.2695 1.4245 1.4646 0.1257  -0.4794 0.0630  1344 ASP B CG  
24687 O OD1 . ASP C 1344 ? 2.2336 1.3976 1.4522 0.1284  -0.4826 0.0683  1344 ASP B OD1 
24688 O OD2 . ASP C 1344 ? 2.2313 1.4098 1.4067 0.1317  -0.4637 0.0646  1344 ASP B OD2 
24689 N N   . ASP C 1345 ? 2.3253 1.4747 1.6028 0.0913  -0.5044 0.0618  1345 ASP B N   
24690 C CA  . ASP C 1345 ? 2.2589 1.4383 1.5734 0.0720  -0.5007 0.0645  1345 ASP B CA  
24691 C C   . ASP C 1345 ? 1.8871 1.0984 1.1954 0.0585  -0.4856 0.0645  1345 ASP B C   
24692 O O   . ASP C 1345 ? 1.8960 1.1328 1.1858 0.0632  -0.4710 0.0670  1345 ASP B O   
24693 C CB  . ASP C 1345 ? 2.2292 1.4385 1.5684 0.0738  -0.4930 0.0735  1345 ASP B CB  
24694 C CG  . ASP C 1345 ? 2.3466 1.5221 1.6794 0.0903  -0.5031 0.0742  1345 ASP B CG  
24695 O OD1 . ASP C 1345 ? 2.3437 1.5263 1.6993 0.0885  -0.5020 0.0792  1345 ASP B OD1 
24696 O OD2 . ASP C 1345 ? 2.3839 1.5229 1.6859 0.1049  -0.5110 0.0699  1345 ASP B OD2 
24697 N N   . LEU C 1346 ? 1.8498 1.0587 1.1717 0.0416  -0.4886 0.0612  1346 LEU B N   
24698 C CA  . LEU C 1346 ? 1.7957 1.0291 1.1091 0.0266  -0.4738 0.0608  1346 LEU B CA  
24699 C C   . LEU C 1346 ? 1.7886 1.0733 1.1304 0.0120  -0.4590 0.0685  1346 LEU B C   
24700 O O   . LEU C 1346 ? 1.8119 1.1052 1.1837 0.0110  -0.4630 0.0730  1346 LEU B O   
24701 C CB  . LEU C 1346 ? 1.7455 0.9476 1.0545 0.0172  -0.4835 0.0538  1346 LEU B CB  
24702 C CG  . LEU C 1346 ? 1.7170 0.9327 1.0043 0.0039  -0.4673 0.0523  1346 LEU B CG  
24703 C CD1 . LEU C 1346 ? 1.7417 0.9525 0.9907 0.0139  -0.4587 0.0500  1346 LEU B CD1 
24704 C CD2 . LEU C 1346 ? 1.7209 0.9032 0.9999 -0.0031 -0.4760 0.0459  1346 LEU B CD2 
24705 N N   . ILE C 1347 ? 1.7378 1.0549 1.0690 -0.0003 -0.4416 0.0694  1347 ILE B N   
24706 C CA  . ILE C 1347 ? 1.6251 0.9897 0.9800 -0.0169 -0.4279 0.0757  1347 ILE B CA  
24707 C C   . ILE C 1347 ? 1.5422 0.9247 0.8855 -0.0384 -0.4131 0.0737  1347 ILE B C   
24708 O O   . ILE C 1347 ? 1.5226 0.9341 0.8488 -0.0424 -0.3984 0.0734  1347 ILE B O   
24709 C CB  . ILE C 1347 ? 1.6109 1.0229 0.9723 -0.0095 -0.4167 0.0825  1347 ILE B CB  
24710 C CG1 . ILE C 1347 ? 1.6336 1.0293 0.9880 0.0155  -0.4252 0.0839  1347 ILE B CG1 
24711 C CG2 . ILE C 1347 ? 1.5829 1.0293 0.9763 -0.0204 -0.4116 0.0896  1347 ILE B CG2 
24712 C CD1 . ILE C 1347 ? 1.6434 1.0877 1.0029 0.0253  -0.4138 0.0909  1347 ILE B CD1 
24713 N N   . VAL C 1348 ? 1.4946 0.8616 0.8478 -0.0525 -0.4159 0.0724  1348 VAL B N   
24714 C CA  . VAL C 1348 ? 1.4858 0.8702 0.8314 -0.0750 -0.4008 0.0721  1348 VAL B CA  
24715 C C   . VAL C 1348 ? 1.5797 1.0207 0.9466 -0.0858 -0.3872 0.0795  1348 VAL B C   
24716 O O   . VAL C 1348 ? 1.5875 1.0422 0.9822 -0.0783 -0.3928 0.0853  1348 VAL B O   
24717 C CB  . VAL C 1348 ? 1.4540 0.8072 0.8090 -0.0836 -0.4087 0.0704  1348 VAL B CB  
24718 C CG1 . VAL C 1348 ? 1.4528 0.8086 0.7879 -0.1049 -0.3935 0.0687  1348 VAL B CG1 
24719 C CG2 . VAL C 1348 ? 1.4741 0.7767 0.8175 -0.0685 -0.4270 0.0638  1348 VAL B CG2 
24720 N N   . SER C 1349 ? 1.5578 1.0304 0.9107 -0.1032 -0.3697 0.0790  1349 SER B N   
24721 C CA  . SER C 1349 ? 1.5389 1.0691 0.9103 -0.1114 -0.3584 0.0851  1349 SER B CA  
24722 C C   . SER C 1349 ? 1.5853 1.1514 0.9421 -0.1355 -0.3390 0.0832  1349 SER B C   
24723 O O   . SER C 1349 ? 1.5788 1.1877 0.9309 -0.1355 -0.3291 0.0829  1349 SER B O   
24724 C CB  . SER C 1349 ? 1.5040 1.0604 0.8822 -0.0904 -0.3609 0.0881  1349 SER B CB  
24725 O OG  . SER C 1349 ? 1.5202 1.0642 0.8708 -0.0806 -0.3592 0.0826  1349 SER B OG  
24726 N N   . THR C 1350 ? 1.6435 1.1929 0.9936 -0.1559 -0.3336 0.0820  1350 THR B N   
24727 C CA  . THR C 1350 ? 1.6554 1.2333 0.9917 -0.1830 -0.3152 0.0805  1350 THR B CA  
24728 C C   . THR C 1350 ? 1.5935 1.2383 0.9477 -0.1910 -0.3057 0.0847  1350 THR B C   
24729 O O   . THR C 1350 ? 1.5348 1.2026 0.9182 -0.1808 -0.3127 0.0916  1350 THR B O   
24730 C CB  . THR C 1350 ? 1.7537 1.3059 1.0893 -0.2007 -0.3128 0.0818  1350 THR B CB  
24731 O OG1 . THR C 1350 ? 1.7945 1.3603 1.1045 -0.2276 -0.2943 0.0782  1350 THR B OG1 
24732 C CG2 . THR C 1350 ? 1.7237 1.2974 1.0956 -0.2004 -0.3175 0.0901  1350 THR B CG2 
24733 N N   . GLY C 1351 ? 1.5933 1.2674 0.9277 -0.2106 -0.2893 0.0799  1351 GLY B N   
24734 C CA  . GLY C 1351 ? 1.5513 1.2927 0.8995 -0.2222 -0.2794 0.0820  1351 GLY B CA  
24735 C C   . GLY C 1351 ? 1.5105 1.2644 0.8737 -0.2393 -0.2772 0.0872  1351 GLY B C   
24736 O O   . GLY C 1351 ? 1.4710 1.1893 0.8462 -0.2330 -0.2869 0.0918  1351 GLY B O   
24737 N N   . PHE C 1352 ? 1.4903 1.2955 0.8535 -0.2608 -0.2646 0.0862  1352 PHE B N   
24738 C CA  . PHE C 1352 ? 1.4552 1.2654 0.8253 -0.2801 -0.2610 0.0904  1352 PHE B CA  
24739 C C   . PHE C 1352 ? 1.4776 1.2306 0.8197 -0.2987 -0.2546 0.0869  1352 PHE B C   
24740 O O   . PHE C 1352 ? 1.4953 1.1977 0.8402 -0.2856 -0.2646 0.0893  1352 PHE B O   
24741 C CB  . PHE C 1352 ? 1.4150 1.2938 0.7921 -0.2988 -0.2510 0.0901  1352 PHE B CB  
24742 C CG  . PHE C 1352 ? 1.3899 1.2666 0.7669 -0.3215 -0.2460 0.0936  1352 PHE B CG  
24743 C CD1 . PHE C 1352 ? 1.3596 1.2015 0.7517 -0.3115 -0.2553 0.1013  1352 PHE B CD1 
24744 C CD2 . PHE C 1352 ? 1.3818 1.2885 0.7422 -0.3535 -0.2312 0.0889  1352 PHE B CD2 
24745 C CE1 . PHE C 1352 ? 1.3286 1.1644 0.7184 -0.3313 -0.2498 0.1047  1352 PHE B CE1 
24746 C CE2 . PHE C 1352 ? 1.3494 1.2490 0.7058 -0.3741 -0.2264 0.0921  1352 PHE B CE2 
24747 C CZ  . PHE C 1352 ? 1.3304 1.1937 0.7010 -0.3621 -0.2355 0.1004  1352 PHE B CZ  
24748 N N   . GLY C 1353 ? 1.4563 1.2161 0.7705 -0.3282 -0.2379 0.0811  1353 GLY B N   
24749 C CA  . GLY C 1353 ? 1.4952 1.1967 0.7752 -0.3441 -0.2301 0.0774  1353 GLY B CA  
24750 C C   . GLY C 1353 ? 1.4853 1.1528 0.7694 -0.3496 -0.2325 0.0834  1353 GLY B C   
24751 O O   . GLY C 1353 ? 1.4611 1.1584 0.7682 -0.3537 -0.2340 0.0895  1353 GLY B O   
24752 N N   . SER C 1354 ? 1.5269 1.1316 0.7880 -0.3478 -0.2331 0.0817  1354 SER B N   
24753 C CA  . SER C 1354 ? 1.5169 1.0858 0.7729 -0.3569 -0.2308 0.0860  1354 SER B CA  
24754 C C   . SER C 1354 ? 1.5165 1.0178 0.7526 -0.3451 -0.2360 0.0841  1354 SER B C   
24755 O O   . SER C 1354 ? 1.5386 1.0138 0.7473 -0.3401 -0.2350 0.0774  1354 SER B O   
24756 C CB  . SER C 1354 ? 1.5471 1.1246 0.7715 -0.3913 -0.2108 0.0832  1354 SER B CB  
24757 O OG  . SER C 1354 ? 1.5927 1.1196 0.7699 -0.4021 -0.1998 0.0766  1354 SER B OG  
24758 N N   . GLY C 1355 ? 1.5302 1.0032 0.7779 -0.3411 -0.2405 0.0897  1355 GLY B N   
24759 C CA  . GLY C 1355 ? 1.5661 0.9795 0.7998 -0.3278 -0.2471 0.0883  1355 GLY B CA  
24760 C C   . GLY C 1355 ? 1.5642 0.9698 0.8392 -0.2991 -0.2683 0.0919  1355 GLY B C   
24761 O O   . GLY C 1355 ? 1.6044 1.0455 0.9187 -0.2913 -0.2761 0.0971  1355 GLY B O   
24762 N N   . LEU C 1356 ? 1.5016 0.8604 0.7665 -0.2833 -0.2778 0.0886  1356 LEU B N   
24763 C CA  . LEU C 1356 ? 1.5363 0.8869 0.8399 -0.2584 -0.2981 0.0907  1356 LEU B CA  
24764 C C   . LEU C 1356 ? 1.6200 0.9352 0.9086 -0.2384 -0.3115 0.0836  1356 LEU B C   
24765 O O   . LEU C 1356 ? 1.7429 1.0145 1.0030 -0.2356 -0.3113 0.0799  1356 LEU B O   
24766 C CB  . LEU C 1356 ? 1.4874 0.8179 0.8078 -0.2583 -0.2990 0.0957  1356 LEU B CB  
24767 C CG  . LEU C 1356 ? 1.4262 0.7902 0.7860 -0.2631 -0.2978 0.1039  1356 LEU B CG  
24768 C CD1 . LEU C 1356 ? 1.3909 0.7332 0.7532 -0.2702 -0.2909 0.1086  1356 LEU B CD1 
24769 C CD2 . LEU C 1356 ? 1.3864 0.7593 0.7870 -0.2415 -0.3163 0.1048  1356 LEU B CD2 
24770 N N   . ALA C 1357 ? 1.5906 0.9221 0.8955 -0.2232 -0.3234 0.0818  1357 ALA B N   
24771 C CA  . ALA C 1357 ? 1.5257 0.8229 0.8137 -0.2042 -0.3367 0.0748  1357 ALA B CA  
24772 C C   . ALA C 1357 ? 1.4634 0.7534 0.7906 -0.1819 -0.3589 0.0756  1357 ALA B C   
24773 O O   . ALA C 1357 ? 1.4211 0.7417 0.7818 -0.1765 -0.3646 0.0795  1357 ALA B O   
24774 C CB  . ALA C 1357 ? 1.4733 0.7854 0.7382 -0.2042 -0.3316 0.0704  1357 ALA B CB  
24775 N N   . THR C 1358 ? 1.4635 0.7127 0.7848 -0.1693 -0.3711 0.0714  1358 THR B N   
24776 C CA  . THR C 1358 ? 1.4540 0.6945 0.8107 -0.1498 -0.3930 0.0703  1358 THR B CA  
24777 C C   . THR C 1358 ? 1.4694 0.6958 0.8158 -0.1318 -0.4080 0.0641  1358 THR B C   
24778 O O   . THR C 1358 ? 1.5008 0.6911 0.8126 -0.1233 -0.4133 0.0573  1358 THR B O   
24779 C CB  . THR C 1358 ? 1.6754 0.8853 1.0408 -0.1433 -0.4019 0.0688  1358 THR B CB  
24780 O OG1 . THR C 1358 ? 1.6955 0.8663 1.0132 -0.1419 -0.3982 0.0634  1358 THR B OG1 
24781 C CG2 . THR C 1358 ? 1.6405 0.8694 1.0341 -0.1563 -0.3917 0.0764  1358 THR B CG2 
24782 N N   . VAL C 1359 ? 1.4502 0.7022 0.8242 -0.1252 -0.4145 0.0666  1359 VAL B N   
24783 C CA  . VAL C 1359 ? 1.4626 0.6997 0.8350 -0.1063 -0.4313 0.0616  1359 VAL B CA  
24784 C C   . VAL C 1359 ? 1.5523 0.7685 0.9547 -0.0925 -0.4533 0.0585  1359 VAL B C   
24785 O O   . VAL C 1359 ? 1.5092 0.7435 0.9528 -0.0939 -0.4571 0.0628  1359 VAL B O   
24786 C CB  . VAL C 1359 ? 1.4453 0.7167 0.8337 -0.1034 -0.4288 0.0660  1359 VAL B CB  
24787 C CG1 . VAL C 1359 ? 1.4621 0.7131 0.8451 -0.0837 -0.4454 0.0610  1359 VAL B CG1 
24788 C CG2 . VAL C 1359 ? 1.4445 0.7445 0.8091 -0.1162 -0.4086 0.0683  1359 VAL B CG2 
24789 N N   . HIS C 1360 ? 1.5640 0.7423 0.9454 -0.0798 -0.4676 0.0506  1360 HIS B N   
24790 C CA  . HIS C 1360 ? 1.5975 0.7586 1.0046 -0.0647 -0.4916 0.0457  1360 HIS B CA  
24791 C C   . HIS C 1360 ? 1.6176 0.7574 1.0015 -0.0495 -0.5043 0.0397  1360 HIS B C   
24792 O O   . HIS C 1360 ? 1.6696 0.7947 1.0098 -0.0476 -0.4970 0.0371  1360 HIS B O   
24793 C CB  . HIS C 1360 ? 1.6484 0.7821 1.0535 -0.0592 -0.5025 0.0403  1360 HIS B CB  
24794 C CG  . HIS C 1360 ? 1.6380 0.7873 1.0688 -0.0710 -0.4929 0.0456  1360 HIS B CG  
24795 N ND1 . HIS C 1360 ? 1.6258 0.7815 1.0343 -0.0856 -0.4712 0.0506  1360 HIS B ND1 
24796 C CD2 . HIS C 1360 ? 1.6264 0.7848 1.1019 -0.0707 -0.5013 0.0464  1360 HIS B CD2 
24797 C CE1 . HIS C 1360 ? 1.6219 0.7882 1.0588 -0.0928 -0.4667 0.0548  1360 HIS B CE1 
24798 N NE2 . HIS C 1360 ? 1.6242 0.7934 1.1030 -0.0837 -0.4843 0.0525  1360 HIS B NE2 
24799 N N   . VAL C 1361 ? 1.5775 0.7119 0.9881 -0.0389 -0.5231 0.0368  1361 VAL B N   
24800 C CA  . VAL C 1361 ? 1.6126 0.7261 1.0013 -0.0244 -0.5350 0.0317  1361 VAL B CA  
24801 C C   . VAL C 1361 ? 1.6323 0.7236 1.0413 -0.0128 -0.5609 0.0244  1361 VAL B C   
24802 O O   . VAL C 1361 ? 1.6409 0.7423 1.0825 -0.0121 -0.5686 0.0255  1361 VAL B O   
24803 C CB  . VAL C 1361 ? 1.5275 0.6666 0.9191 -0.0254 -0.5239 0.0381  1361 VAL B CB  
24804 C CG1 . VAL C 1361 ? 1.5353 0.6627 0.9403 -0.0130 -0.5405 0.0355  1361 VAL B CG1 
24805 C CG2 . VAL C 1361 ? 1.5446 0.6817 0.8918 -0.0243 -0.5102 0.0381  1361 VAL B CG2 
24806 N N   . THR C 1362 ? 1.6579 0.7173 1.0449 -0.0038 -0.5743 0.0164  1362 THR B N   
24807 C CA  . THR C 1362 ? 1.6652 0.7088 1.0761 0.0049  -0.5995 0.0085  1362 THR B CA  
24808 C C   . THR C 1362 ? 1.6542 0.6675 1.0432 0.0199  -0.6184 0.0010  1362 THR B C   
24809 O O   . THR C 1362 ? 1.6695 0.6519 1.0116 0.0302  -0.6215 -0.0036 1362 THR B O   
24810 C CB  . THR C 1362 ? 1.6903 0.7213 1.0957 0.0069  -0.6041 0.0046  1362 THR B CB  
24811 O OG1 . THR C 1362 ? 1.6949 0.7210 1.1331 0.0141  -0.6283 -0.0030 1362 THR B OG1 
24812 C CG2 . THR C 1362 ? 1.7476 0.7435 1.0928 0.0162  -0.6021 0.0004  1362 THR B CG2 
24813 N N   . THR C 1363 ? 1.6755 0.6959 1.0963 0.0200  -0.6292 0.0003  1363 THR B N   
24814 C CA  . THR C 1363 ? 1.7644 0.7594 1.1649 0.0317  -0.6424 -0.0045 1363 THR B CA  
24815 C C   . THR C 1363 ? 1.8645 0.8360 1.2784 0.0397  -0.6720 -0.0158 1363 THR B C   
24816 O O   . THR C 1363 ? 1.8598 0.8471 1.3198 0.0325  -0.6807 -0.0174 1363 THR B O   
24817 C CB  . THR C 1363 ? 2.4795 1.4936 1.8947 0.0274  -0.6311 0.0031  1363 THR B CB  
24818 O OG1 . THR C 1363 ? 2.4730 1.4823 1.9201 0.0271  -0.6477 -0.0012 1363 THR B OG1 
24819 C CG2 . THR C 1363 ? 2.4463 1.5009 1.8846 0.0132  -0.6073 0.0138  1363 THR B CG2 
24820 N N   . VAL C 1364 ? 1.9221 0.8557 1.2943 0.0542  -0.6869 -0.0239 1364 VAL B N   
24821 C CA  . VAL C 1364 ? 1.9229 0.8317 1.3000 0.0634  -0.7170 -0.0359 1364 VAL B CA  
24822 C C   . VAL C 1364 ? 1.9852 0.8708 1.3511 0.0695  -0.7297 -0.0400 1364 VAL B C   
24823 O O   . VAL C 1364 ? 2.0316 0.8999 1.3586 0.0761  -0.7200 -0.0364 1364 VAL B O   
24824 C CB  . VAL C 1364 ? 1.9108 0.7859 1.2428 0.0775  -0.7273 -0.0428 1364 VAL B CB  
24825 C CG1 . VAL C 1364 ? 1.9577 0.7982 1.2763 0.0904  -0.7576 -0.0549 1364 VAL B CG1 
24826 C CG2 . VAL C 1364 ? 1.8813 0.7718 1.2311 0.0746  -0.7262 -0.0432 1364 VAL B CG2 
24827 N N   . VAL C 1365 ? 1.9950 0.8789 1.3932 0.0672  -0.7513 -0.0479 1365 VAL B N   
24828 C CA  . VAL C 1365 ? 2.0368 0.8931 1.4194 0.0725  -0.7640 -0.0526 1365 VAL B CA  
24829 C C   . VAL C 1365 ? 2.1439 0.9855 1.5447 0.0745  -0.7961 -0.0666 1365 VAL B C   
24830 O O   . VAL C 1365 ? 2.1621 1.0275 1.6031 0.0684  -0.8048 -0.0708 1365 VAL B O   
24831 C CB  . VAL C 1365 ? 1.9528 0.8284 1.3572 0.0621  -0.7467 -0.0436 1365 VAL B CB  
24832 C CG1 . VAL C 1365 ? 1.9157 0.8104 1.3764 0.0481  -0.7564 -0.0475 1365 VAL B CG1 
24833 C CG2 . VAL C 1365 ? 1.9699 0.8125 1.3310 0.0728  -0.7459 -0.0428 1365 VAL B CG2 
24834 N N   . HIS C 1366 ? 2.1922 0.9951 1.5619 0.0837  -0.8139 -0.0744 1366 HIS B N   
24835 C CA  . HIS C 1366 ? 2.2034 0.9932 1.5899 0.0841  -0.8457 -0.0887 1366 HIS B CA  
24836 C C   . HIS C 1366 ? 2.1681 0.9558 1.5775 0.0727  -0.8497 -0.0907 1366 HIS B C   
24837 O O   . HIS C 1366 ? 2.1749 0.9378 1.5514 0.0765  -0.8408 -0.0862 1366 HIS B O   
24838 C CB  . HIS C 1366 ? 2.2995 1.0410 1.6303 0.1025  -0.8664 -0.0980 1366 HIS B CB  
24839 C CG  . HIS C 1366 ? 2.3404 1.0727 1.6381 0.1157  -0.8643 -0.0976 1366 HIS B CG  
24840 N ND1 . HIS C 1366 ? 2.3307 1.0792 1.6171 0.1145  -0.8357 -0.0858 1366 HIS B ND1 
24841 C CD2 . HIS C 1366 ? 2.3890 1.0944 1.6583 0.1307  -0.8867 -0.1078 1366 HIS B CD2 
24842 C CE1 . HIS C 1366 ? 2.3630 1.0930 1.6147 0.1271  -0.8393 -0.0888 1366 HIS B CE1 
24843 N NE2 . HIS C 1366 ? 2.4059 1.1087 1.6456 0.1383  -0.8701 -0.1018 1366 HIS B NE2 
24844 N N   . LYS C 1367 ? 2.1274 0.9397 1.5912 0.0589  -0.8622 -0.0977 1367 LYS B N   
24845 C CA  . LYS C 1367 ? 2.1694 0.9738 1.6516 0.0464  -0.8675 -0.1016 1367 LYS B CA  
24846 C C   . LYS C 1367 ? 2.1893 0.9730 1.6752 0.0459  -0.9015 -0.1188 1367 LYS B C   
24847 O O   . LYS C 1367 ? 2.1925 0.9768 1.6777 0.0547  -0.9223 -0.1279 1367 LYS B O   
24848 C CB  . LYS C 1367 ? 2.1751 1.0200 1.7146 0.0266  -0.8500 -0.0954 1367 LYS B CB  
24849 C CG  . LYS C 1367 ? 2.1689 1.0583 1.7596 0.0191  -0.8494 -0.0960 1367 LYS B CG  
24850 C CD  . LYS C 1367 ? 2.1488 1.0714 1.7822 0.0019  -0.8245 -0.0860 1367 LYS B CD  
24851 C CE  . LYS C 1367 ? 2.1486 1.0650 1.7483 0.0065  -0.7964 -0.0706 1367 LYS B CE  
24852 N NZ  . LYS C 1367 ? 2.1331 1.0646 1.7617 -0.0086 -0.7773 -0.0632 1367 LYS B NZ  
24853 N N   . THR C 1368 ? 1.8929 1.0151 1.7056 0.0782  -0.7762 0.0725  1368 THR B N   
24854 C CA  . THR C 1368 ? 1.8987 0.9948 1.7091 0.0714  -0.7882 0.0529  1368 THR B CA  
24855 C C   . THR C 1368 ? 1.8906 0.9732 1.7163 0.0395  -0.7933 0.0608  1368 THR B C   
24856 O O   . THR C 1368 ? 1.9359 0.9996 1.7640 0.0292  -0.8039 0.0455  1368 THR B O   
24857 C CB  . THR C 1368 ? 1.9316 0.9796 1.7283 0.0909  -0.8000 0.0381  1368 THR B CB  
24858 O OG1 . THR C 1368 ? 1.9739 0.9788 1.7758 0.0784  -0.8070 0.0492  1368 THR B OG1 
24859 C CG2 . THR C 1368 ? 1.9173 0.9762 1.7010 0.1230  -0.7935 0.0374  1368 THR B CG2 
24860 N N   . SER C 1369 ? 1.8638 0.9575 1.7002 0.0240  -0.7857 0.0846  1369 SER B N   
24861 C CA  . SER C 1369 ? 1.8904 0.9655 1.7416 -0.0046 -0.7899 0.0952  1369 SER B CA  
24862 C C   . SER C 1369 ? 1.8670 0.9718 1.7294 -0.0229 -0.7788 0.1195  1369 SER B C   
24863 O O   . SER C 1369 ? 1.8050 0.9345 1.6636 -0.0138 -0.7689 0.1331  1369 SER B O   
24864 C CB  . SER C 1369 ? 1.9484 0.9680 1.7982 -0.0039 -0.7986 0.0992  1369 SER B CB  
24865 O OG  . SER C 1369 ? 1.9977 0.9854 1.8343 0.0149  -0.8095 0.0769  1369 SER B OG  
24866 N N   . THR C 1370 ? 1.9397 1.0411 1.8165 -0.0490 -0.7811 0.1244  1370 THR B N   
24867 C CA  . THR C 1370 ? 1.9840 1.1080 1.8709 -0.0673 -0.7714 0.1479  1370 THR B CA  
24868 C C   . THR C 1370 ? 2.1482 1.2333 2.0439 -0.0812 -0.7740 0.1651  1370 THR B C   
24869 O O   . THR C 1370 ? 2.1632 1.2584 2.0625 -0.0895 -0.7654 0.1883  1370 THR B O   
24870 C CB  . THR C 1370 ? 1.9011 1.0577 1.7982 -0.0858 -0.7692 0.1437  1370 THR B CB  
24871 O OG1 . THR C 1370 ? 1.8242 1.0202 1.7108 -0.0716 -0.7629 0.1336  1370 THR B OG1 
24872 C CG2 . THR C 1370 ? 1.8817 1.0549 1.7901 -0.1066 -0.7604 0.1686  1370 THR B CG2 
24873 N N   . SER C 1371 ? 2.2884 1.3274 2.1859 -0.0827 -0.7857 0.1540  1371 SER B N   
24874 C CA  . SER C 1371 ? 2.4212 1.4185 2.3283 -0.0981 -0.7882 0.1694  1371 SER B CA  
24875 C C   . SER C 1371 ? 2.4839 1.4864 2.3883 -0.0970 -0.7769 0.1982  1371 SER B C   
24876 O O   . SER C 1371 ? 2.5126 1.5094 2.4293 -0.1170 -0.7722 0.2178  1371 SER B O   
24877 C CB  . SER C 1371 ? 2.5163 1.4585 2.4150 -0.0864 -0.8001 0.1559  1371 SER B CB  
24878 O OG  . SER C 1371 ? 2.5465 1.4815 2.4264 -0.0584 -0.7976 0.1580  1371 SER B OG  
24879 N N   . GLU C 1372 ? 2.5135 1.5280 2.4021 -0.0728 -0.7726 0.2006  1372 GLU B N   
24880 C CA  . GLU C 1372 ? 2.5414 1.5663 2.4249 -0.0674 -0.7631 0.2252  1372 GLU B CA  
24881 C C   . GLU C 1372 ? 2.4046 1.4686 2.2970 -0.0855 -0.7530 0.2419  1372 GLU B C   
24882 O O   . GLU C 1372 ? 2.4104 1.4620 2.3099 -0.1006 -0.7488 0.2622  1372 GLU B O   
24883 C CB  . GLU C 1372 ? 2.6708 1.7152 2.5392 -0.0392 -0.7609 0.2204  1372 GLU B CB  
24884 C CG  . GLU C 1372 ? 2.7699 1.8531 2.6361 -0.0311 -0.7602 0.2004  1372 GLU B CG  
24885 C CD  . GLU C 1372 ? 2.8484 1.9628 2.7046 -0.0081 -0.7544 0.2007  1372 GLU B CD  
24886 O OE1 . GLU C 1372 ? 2.9045 2.0058 2.7540 0.0066  -0.7542 0.2112  1372 GLU B OE1 
24887 O OE2 . GLU C 1372 ? 2.8384 1.9911 2.6943 -0.0047 -0.7500 0.1905  1372 GLU B OE2 
24888 N N   . GLU C 1373 ? 2.2599 1.3695 2.1508 -0.0832 -0.7488 0.2331  1373 GLU B N   
24889 C CA  . GLU C 1373 ? 2.1032 1.2545 1.9970 -0.0945 -0.7385 0.2473  1373 GLU B CA  
24890 C C   . GLU C 1373 ? 2.0608 1.2089 1.9684 -0.1201 -0.7348 0.2640  1373 GLU B C   
24891 O O   . GLU C 1373 ? 2.0750 1.1911 1.9944 -0.1338 -0.7406 0.2627  1373 GLU B O   
24892 C CB  . GLU C 1373 ? 1.9938 1.1861 1.8855 -0.0914 -0.7362 0.2302  1373 GLU B CB  
24893 C CG  . GLU C 1373 ? 1.9124 1.1140 1.7920 -0.0662 -0.7374 0.2152  1373 GLU B CG  
24894 C CD  . GLU C 1373 ? 1.8017 1.0380 1.6786 -0.0625 -0.7348 0.1974  1373 GLU B CD  
24895 O OE1 . GLU C 1373 ? 1.7557 1.0065 1.6397 -0.0790 -0.7339 0.1943  1373 GLU B OE1 
24896 O OE2 . GLU C 1373 ? 1.7452 0.9947 1.6133 -0.0424 -0.7333 0.1871  1373 GLU B OE2 
24897 N N   . VAL C 1374 ? 1.9747 1.1567 1.8808 -0.1263 -0.7249 0.2798  1374 VAL B N   
24898 C CA  . VAL C 1374 ? 1.9193 1.1038 1.8369 -0.1480 -0.7191 0.2987  1374 VAL B CA  
24899 C C   . VAL C 1374 ? 1.8831 1.0994 1.8109 -0.1635 -0.7173 0.2904  1374 VAL B C   
24900 O O   . VAL C 1374 ? 1.8596 1.1147 1.7790 -0.1586 -0.7115 0.2874  1374 VAL B O   
24901 C CB  . VAL C 1374 ? 1.8797 1.0825 1.7872 -0.1444 -0.7089 0.3224  1374 VAL B CB  
24902 C CG1 . VAL C 1374 ? 1.8926 1.0840 1.8107 -0.1633 -0.7031 0.3453  1374 VAL B CG1 
24903 C CG2 . VAL C 1374 ? 1.8713 1.0592 1.7640 -0.1226 -0.7103 0.3269  1374 VAL B CG2 
24904 N N   . CYS C 1375 ? 1.8781 1.0789 1.8243 -0.1825 -0.7220 0.2874  1375 CYS B N   
24905 C CA  . CYS C 1375 ? 1.8398 1.0724 1.7970 -0.1967 -0.7216 0.2782  1375 CYS B CA  
24906 C C   . CYS C 1375 ? 1.8260 1.0838 1.7915 -0.2136 -0.7108 0.3008  1375 CYS B C   
24907 O O   . CYS C 1375 ? 1.8309 1.0700 1.8106 -0.2290 -0.7086 0.3181  1375 CYS B O   
24908 C CB  . CYS C 1375 ? 1.8233 1.0358 1.7961 -0.2066 -0.7343 0.2564  1375 CYS B CB  
24909 S SG  . CYS C 1375 ? 2.8124 2.0384 2.7724 -0.1874 -0.7428 0.2223  1375 CYS B SG  
24910 N N   . SER C 1376 ? 1.8084 1.1083 1.7641 -0.2097 -0.7034 0.3006  1376 SER B N   
24911 C CA  . SER C 1376 ? 1.8140 1.1413 1.7718 -0.2210 -0.6923 0.3213  1376 SER B CA  
24912 C C   . SER C 1376 ? 1.8372 1.1905 1.8111 -0.2368 -0.6936 0.3118  1376 SER B C   
24913 O O   . SER C 1376 ? 1.8589 1.2368 1.8384 -0.2482 -0.6850 0.3275  1376 SER B O   
24914 C CB  . SER C 1376 ? 1.7537 1.1077 1.6880 -0.2051 -0.6838 0.3273  1376 SER B CB  
24915 O OG  . SER C 1376 ? 1.7248 1.0626 1.6456 -0.1860 -0.6881 0.3187  1376 SER B OG  
24916 N N   . PHE C 1377 ? 1.8401 1.1879 1.8205 -0.2359 -0.7047 0.2858  1377 PHE B N   
24917 C CA  . PHE C 1377 ? 1.7969 1.1681 1.7923 -0.2484 -0.7091 0.2716  1377 PHE B CA  
24918 C C   . PHE C 1377 ? 1.8479 1.1894 1.8625 -0.2578 -0.7242 0.2528  1377 PHE B C   
24919 O O   . PHE C 1377 ? 1.8800 1.1933 1.8865 -0.2450 -0.7331 0.2367  1377 PHE B O   
24920 C CB  . PHE C 1377 ? 1.7258 1.1283 1.7032 -0.2330 -0.7079 0.2531  1377 PHE B CB  
24921 C CG  . PHE C 1377 ? 1.7173 1.1568 1.6813 -0.2301 -0.6945 0.2671  1377 PHE B CG  
24922 C CD1 . PHE C 1377 ? 1.7106 1.1787 1.6854 -0.2444 -0.6893 0.2757  1377 PHE B CD1 
24923 C CD2 . PHE C 1377 ? 1.7299 1.1760 1.6703 -0.2129 -0.6872 0.2715  1377 PHE B CD2 
24924 C CE1 . PHE C 1377 ? 1.6962 1.1968 1.6559 -0.2403 -0.6768 0.2885  1377 PHE B CE1 
24925 C CE2 . PHE C 1377 ? 1.7146 1.1923 1.6411 -0.2104 -0.6753 0.2837  1377 PHE B CE2 
24926 C CZ  . PHE C 1377 ? 1.6958 1.1994 1.6306 -0.2236 -0.6700 0.2921  1377 PHE B CZ  
24927 N N   . TYR C 1378 ? 1.8479 1.1961 1.8882 -0.2797 -0.7276 0.2541  1378 TYR B N   
24928 C CA  . TYR C 1378 ? 1.8322 1.1537 1.8921 -0.2904 -0.7434 0.2345  1378 TYR B CA  
24929 C C   . TYR C 1378 ? 1.7971 1.1422 1.8509 -0.2815 -0.7522 0.2052  1378 TYR B C   
24930 O O   . TYR C 1378 ? 1.7474 1.1347 1.8027 -0.2846 -0.7474 0.2043  1378 TYR B O   
24931 C CB  . TYR C 1378 ? 1.8253 1.1454 1.9186 -0.3191 -0.7440 0.2476  1378 TYR B CB  
24932 C CG  . TYR C 1378 ? 1.8138 1.1002 1.9166 -0.3296 -0.7373 0.2747  1378 TYR B CG  
24933 C CD1 . TYR C 1378 ? 1.8323 1.0677 1.9301 -0.3236 -0.7438 0.2721  1378 TYR B CD1 
24934 C CD2 . TYR C 1378 ? 1.7984 1.1038 1.9146 -0.3445 -0.7241 0.3032  1378 TYR B CD2 
24935 C CE1 . TYR C 1378 ? 1.8578 1.0609 1.9623 -0.3318 -0.7369 0.2973  1378 TYR B CE1 
24936 C CE2 . TYR C 1378 ? 1.8167 1.0908 1.9402 -0.3528 -0.7168 0.3291  1378 TYR B CE2 
24937 C CZ  . TYR C 1378 ? 1.8483 1.0707 1.9657 -0.3464 -0.7232 0.3260  1378 TYR B CZ  
24938 O OH  . TYR C 1378 ? 1.8681 1.0580 1.9906 -0.3528 -0.7153 0.3520  1378 TYR B OH  
24939 N N   . LEU C 1379 ? 1.8421 1.1601 1.8874 -0.2688 -0.7645 0.1814  1379 LEU B N   
24940 C CA  . LEU C 1379 ? 1.8752 1.2143 1.9113 -0.2572 -0.7724 0.1536  1379 LEU B CA  
24941 C C   . LEU C 1379 ? 2.0048 1.3211 2.0561 -0.2648 -0.7916 0.1280  1379 LEU B C   
24942 O O   . LEU C 1379 ? 2.0782 1.3518 2.1427 -0.2748 -0.8006 0.1276  1379 LEU B O   
24943 C CB  . LEU C 1379 ? 1.8479 1.1857 1.8535 -0.2288 -0.7686 0.1445  1379 LEU B CB  
24944 C CG  . LEU C 1379 ? 1.8181 1.1836 1.8083 -0.2213 -0.7510 0.1659  1379 LEU B CG  
24945 C CD1 . LEU C 1379 ? 1.7941 1.1592 1.7574 -0.1945 -0.7470 0.1577  1379 LEU B CD1 
24946 C CD2 . LEU C 1379 ? 1.7916 1.2031 1.7856 -0.2293 -0.7445 0.1684  1379 LEU B CD2 
24947 N N   . LYS C 1380 ? 2.0126 1.3570 2.0606 -0.2592 -0.7980 0.1060  1380 LYS B N   
24948 C CA  . LYS C 1380 ? 2.0374 1.3632 2.0926 -0.2599 -0.8175 0.0767  1380 LYS B CA  
24949 C C   . LYS C 1380 ? 2.0037 1.3619 2.0374 -0.2386 -0.8185 0.0552  1380 LYS B C   
24950 O O   . LYS C 1380 ? 1.9509 1.3511 1.9759 -0.2339 -0.8056 0.0642  1380 LYS B O   
24951 C CB  . LYS C 1380 ? 1.8757 1.2005 1.9677 -0.2903 -0.8283 0.0760  1380 LYS B CB  
24952 C CG  . LYS C 1380 ? 1.9291 1.3037 2.0407 -0.3084 -0.8190 0.0919  1380 LYS B CG  
24953 C CD  . LYS C 1380 ? 1.9259 1.2963 2.0793 -0.3407 -0.8299 0.0928  1380 LYS B CD  
24954 C CE  . LYS C 1380 ? 1.6751 1.1019 1.8483 -0.3553 -0.8247 0.1000  1380 LYS B CE  
24955 N NZ  . LYS C 1380 ? 1.6910 1.1222 1.9052 -0.3835 -0.8391 0.0919  1380 LYS B NZ  
24956 N N   . ILE C 1381 ? 2.0013 1.3369 2.0234 -0.2235 -0.8327 0.0277  1381 ILE B N   
24957 C CA  . ILE C 1381 ? 1.9512 1.3123 1.9510 -0.2007 -0.8344 0.0055  1381 ILE B CA  
24958 C C   . ILE C 1381 ? 2.0676 1.3993 2.0656 -0.1937 -0.8559 -0.0261 1381 ILE B C   
24959 O O   . ILE C 1381 ? 2.1538 1.4385 2.1564 -0.1969 -0.8657 -0.0298 1381 ILE B O   
24960 C CB  . ILE C 1381 ? 1.8226 1.1875 1.7913 -0.1736 -0.8199 0.0110  1381 ILE B CB  
24961 C CG1 . ILE C 1381 ? 1.7691 1.1771 1.7190 -0.1569 -0.8125 0.0017  1381 ILE B CG1 
24962 C CG2 . ILE C 1381 ? 1.8002 1.1241 1.7523 -0.1533 -0.8288 -0.0055 1381 ILE B CG2 
24963 C CD1 . ILE C 1381 ? 1.7529 1.1571 1.6732 -0.1274 -0.8051 -0.0053 1381 ILE B CD1 
24964 N N   . ASP C 1382 ? 2.0583 1.4159 2.0484 -0.1834 -0.8636 -0.0490 1382 ASP B N   
24965 C CA  . ASP C 1382 ? 2.1140 1.4461 2.0936 -0.1691 -0.8831 -0.0814 1382 ASP B CA  
24966 C C   . ASP C 1382 ? 2.0985 1.4682 2.0624 -0.1520 -0.8864 -0.1028 1382 ASP B C   
24967 O O   . ASP C 1382 ? 2.0436 1.4584 2.0078 -0.1541 -0.8743 -0.0924 1382 ASP B O   
24968 C CB  . ASP C 1382 ? 2.1935 1.4902 2.2014 -0.1934 -0.9040 -0.0919 1382 ASP B CB  
24969 C CG  . ASP C 1382 ? 2.2308 1.5553 2.2750 -0.2261 -0.9054 -0.0805 1382 ASP B CG  
24970 O OD1 . ASP C 1382 ? 2.2189 1.5553 2.2760 -0.2413 -0.8895 -0.0505 1382 ASP B OD1 
24971 O OD2 . ASP C 1382 ? 2.2706 1.6053 2.3309 -0.2363 -0.9228 -0.1014 1382 ASP B OD2 
24972 N N   . THR C 1383 ? 2.1619 1.5114 2.1095 -0.1329 -0.9022 -0.1325 1383 THR B N   
24973 C CA  . THR C 1383 ? 2.1604 1.5409 2.0907 -0.1140 -0.9077 -0.1558 1383 THR B CA  
24974 C C   . THR C 1383 ? 2.1721 1.5562 2.1239 -0.1298 -0.9317 -0.1792 1383 THR B C   
24975 O O   . THR C 1383 ? 2.1942 1.5391 2.1512 -0.1326 -0.9522 -0.1993 1383 THR B O   
24976 C CB  . THR C 1383 ? 2.1623 1.5269 2.0542 -0.0760 -0.9068 -0.1735 1383 THR B CB  
24977 O OG1 . THR C 1383 ? 2.2086 1.5215 2.0968 -0.0720 -0.9126 -0.1746 1383 THR B OG1 
24978 C CG2 . THR C 1383 ? 2.1062 1.5013 1.9748 -0.0562 -0.8815 -0.1567 1383 THR B CG2 
24979 N N   . GLN C 1384 ? 2.1793 1.6115 2.1433 -0.1398 -0.9289 -0.1764 1384 GLN B N   
24980 C CA  . GLN C 1384 ? 2.2475 1.6949 2.2320 -0.1531 -0.9505 -0.1986 1384 GLN B CA  
24981 C C   . GLN C 1384 ? 2.2778 1.7414 2.2323 -0.1220 -0.9595 -0.2285 1384 GLN B C   
24982 O O   . GLN C 1384 ? 2.2525 1.7294 2.1729 -0.0929 -0.9438 -0.2264 1384 GLN B O   
24983 C CB  . GLN C 1384 ? 2.2544 1.7500 2.2670 -0.1775 -0.9425 -0.1801 1384 GLN B CB  
24984 C CG  . GLN C 1384 ? 2.2956 1.7805 2.3376 -0.2075 -0.9320 -0.1487 1384 GLN B CG  
24985 C CD  . GLN C 1384 ? 2.3134 1.8452 2.3861 -0.2323 -0.9270 -0.1329 1384 GLN B CD  
24986 O OE1 . GLN C 1384 ? 2.2993 1.8780 2.3605 -0.2213 -0.9182 -0.1322 1384 GLN B OE1 
24987 N NE2 . GLN C 1384 ? 2.3385 1.8575 2.4498 -0.2654 -0.9316 -0.1193 1384 GLN B NE2 
24988 N N   . ASP C 1385 ? 2.3365 1.7993 2.3040 -0.1283 -0.9849 -0.2563 1385 ASP B N   
24989 C CA  . ASP C 1385 ? 2.3615 1.8418 2.3013 -0.0991 -0.9957 -0.2863 1385 ASP B CA  
24990 C C   . ASP C 1385 ? 2.3542 1.8941 2.3053 -0.1046 -0.9965 -0.2891 1385 ASP B C   
24991 O O   . ASP C 1385 ? 2.3360 1.9048 2.2571 -0.0759 -0.9921 -0.3008 1385 ASP B O   
24992 C CB  . ASP C 1385 ? 2.4171 1.8546 2.3544 -0.0941 -1.0248 -0.3200 1385 ASP B CB  
24993 C CG  . ASP C 1385 ? 2.4426 1.8263 2.3540 -0.0747 -1.0218 -0.3212 1385 ASP B CG  
24994 O OD1 . ASP C 1385 ? 2.4336 1.8208 2.3066 -0.0402 -1.0081 -0.3224 1385 ASP B OD1 
24995 O OD2 . ASP C 1385 ? 2.4727 1.8109 2.4023 -0.0934 -1.0324 -0.3203 1385 ASP B OD2 
24996 N N   . ILE C 1386 ? 2.3498 1.9084 2.3437 -0.1404 -1.0008 -0.2769 1386 ILE B N   
24997 C CA  . ILE C 1386 ? 2.3239 1.9404 2.3338 -0.1486 -1.0024 -0.2781 1386 ILE B CA  
24998 C C   . ILE C 1386 ? 2.2456 1.9043 2.2293 -0.1293 -0.9746 -0.2578 1386 ILE B C   
24999 O O   . ILE C 1386 ? 2.2104 1.8766 2.1539 -0.0948 -0.9679 -0.2689 1386 ILE B O   
25000 C CB  . ILE C 1386 ? 3.1155 2.7442 3.1795 -0.1927 -1.0081 -0.2626 1386 ILE B CB  
25001 C CG1 . ILE C 1386 ? 3.1565 2.7296 3.2458 -0.2158 -1.0257 -0.2691 1386 ILE B CG1 
25002 C CG2 . ILE C 1386 ? 3.1131 2.7928 3.1994 -0.2017 -1.0229 -0.2780 1386 ILE B CG2 
25003 C CD1 . ILE C 1386 ? 3.1563 2.7373 3.2993 -0.2593 -1.0291 -0.2517 1386 ILE B CD1 
25004 N N   . TYR C 1399 ? 2.9445 2.5613 2.7617 0.0173  -0.9650 -0.3217 1399 TYR B N   
25005 C CA  . TYR C 1399 ? 2.9729 2.5483 2.7590 0.0442  -0.9616 -0.3289 1399 TYR B CA  
25006 C C   . TYR C 1399 ? 2.8004 2.3368 2.6067 0.0220  -0.9564 -0.3085 1399 TYR B C   
25007 O O   . TYR C 1399 ? 2.8248 2.3195 2.6421 0.0134  -0.9755 -0.3220 1399 TYR B O   
25008 C CB  . TYR C 1399 ? 3.1245 2.7203 2.8697 0.0789  -0.9356 -0.3201 1399 TYR B CB  
25009 C CG  . TYR C 1399 ? 3.3039 2.8646 3.0154 0.1101  -0.9276 -0.3247 1399 TYR B CG  
25010 C CD1 . TYR C 1399 ? 3.4187 2.9446 3.1155 0.1281  -0.9489 -0.3536 1399 TYR B CD1 
25011 C CD2 . TYR C 1399 ? 3.3390 2.9032 3.0330 0.1227  -0.8985 -0.3002 1399 TYR B CD2 
25012 C CE1 . TYR C 1399 ? 3.4724 2.9685 3.1379 0.1585  -0.9403 -0.3566 1399 TYR B CE1 
25013 C CE2 . TYR C 1399 ? 3.3882 2.9246 3.0540 0.1512  -0.8901 -0.3032 1399 TYR B CE2 
25014 C CZ  . TYR C 1399 ? 3.4531 2.9562 3.1046 0.1696  -0.9104 -0.3308 1399 TYR B CZ  
25015 O OH  . TYR C 1399 ? 3.4749 2.9524 3.0984 0.1992  -0.9011 -0.3327 1399 TYR B OH  
25016 N N   . LYS C 1400 ? 2.5987 2.1478 2.4088 0.0133  -0.9309 -0.2763 1400 LYS B N   
25017 C CA  . LYS C 1400 ? 2.3980 1.9182 2.2307 -0.0110 -0.9246 -0.2530 1400 LYS B CA  
25018 C C   . LYS C 1400 ? 2.2052 1.7559 2.0451 -0.0234 -0.8987 -0.2191 1400 LYS B C   
25019 O O   . LYS C 1400 ? 2.1566 1.7391 1.9734 -0.0048 -0.8810 -0.2126 1400 LYS B O   
25020 C CB  . LYS C 1400 ? 2.3853 1.8583 2.1978 0.0079  -0.9236 -0.2567 1400 LYS B CB  
25021 C CG  . LYS C 1400 ? 2.3523 1.8290 2.1215 0.0498  -0.9127 -0.2672 1400 LYS B CG  
25022 C CD  . LYS C 1400 ? 2.3440 1.7815 2.0970 0.0661  -0.9046 -0.2612 1400 LYS B CD  
25023 C CE  . LYS C 1400 ? 2.3843 1.7724 2.1365 0.0702  -0.9288 -0.2848 1400 LYS B CE  
25024 N NZ  . LYS C 1400 ? 2.3804 1.7342 2.1122 0.0919  -0.9200 -0.2803 1400 LYS B NZ  
25025 N N   . ARG C 1401 ? 2.0654 1.6047 1.9359 -0.0542 -0.8964 -0.1975 1401 ARG B N   
25026 C CA  . ARG C 1401 ? 1.8935 1.4607 1.7735 -0.0689 -0.8744 -0.1655 1401 ARG B CA  
25027 C C   . ARG C 1401 ? 1.8833 1.4222 1.7853 -0.0925 -0.8687 -0.1409 1401 ARG B C   
25028 O O   . ARG C 1401 ? 1.9106 1.4185 1.8362 -0.1114 -0.8851 -0.1462 1401 ARG B O   
25029 C CB  . ARG C 1401 ? 1.7689 1.3788 1.6704 -0.0871 -0.8788 -0.1646 1401 ARG B CB  
25030 C CG  . ARG C 1401 ? 1.6537 1.2788 1.5815 -0.1156 -0.8660 -0.1334 1401 ARG B CG  
25031 C CD  . ARG C 1401 ? 1.6150 1.2494 1.5837 -0.1469 -0.8829 -0.1361 1401 ARG B CD  
25032 N NE  . ARG C 1401 ? 1.5552 1.2402 1.5343 -0.1568 -0.8726 -0.1215 1401 ARG B NE  
25033 C CZ  . ARG C 1401 ? 1.5339 1.2369 1.5509 -0.1869 -0.8773 -0.1103 1401 ARG B CZ  
25034 N NH1 . ARG C 1401 ? 1.5490 1.2218 1.5986 -0.2123 -0.8919 -0.1113 1401 ARG B NH1 
25035 N NH2 . ARG C 1401 ? 1.5038 1.2544 1.5254 -0.1913 -0.8663 -0.0970 1401 ARG B NH2 
25036 N N   . ILE C 1402 ? 1.8221 1.3711 1.7160 -0.0914 -0.8458 -0.1141 1402 ILE B N   
25037 C CA  . ILE C 1402 ? 1.7795 1.3043 1.6905 -0.1105 -0.8389 -0.0895 1402 ILE B CA  
25038 C C   . ILE C 1402 ? 1.7697 1.3168 1.7092 -0.1403 -0.8331 -0.0661 1402 ILE B C   
25039 O O   . ILE C 1402 ? 1.7381 1.3252 1.6734 -0.1403 -0.8206 -0.0554 1402 ILE B O   
25040 C CB  . ILE C 1402 ? 1.6916 1.2127 1.5795 -0.0936 -0.8182 -0.0725 1402 ILE B CB  
25041 C CG1 . ILE C 1402 ? 1.6852 1.1828 1.5463 -0.0639 -0.8214 -0.0917 1402 ILE B CG1 
25042 C CG2 . ILE C 1402 ? 1.6861 1.1842 1.5915 -0.1128 -0.8129 -0.0483 1402 ILE B CG2 
25043 C CD1 . ILE C 1402 ? 1.6548 1.1496 1.4964 -0.0476 -0.8020 -0.0762 1402 ILE B CD1 
25044 N N   . VAL C 1403 ? 1.8217 1.3413 1.7888 -0.1646 -0.8410 -0.0569 1403 VAL B N   
25045 C CA  . VAL C 1403 ? 1.8499 1.3875 1.8455 -0.1929 -0.8348 -0.0328 1403 VAL B CA  
25046 C C   . VAL C 1403 ? 1.9091 1.4181 1.9097 -0.2023 -0.8240 -0.0068 1403 VAL B C   
25047 O O   . VAL C 1403 ? 1.9591 1.4296 1.9776 -0.2164 -0.8342 -0.0059 1403 VAL B O   
25048 C CB  . VAL C 1403 ? 1.8661 1.4038 1.8971 -0.2182 -0.8544 -0.0441 1403 VAL B CB  
25049 C CG1 . VAL C 1403 ? 1.8574 1.4046 1.9204 -0.2485 -0.8471 -0.0161 1403 VAL B CG1 
25050 C CG2 . VAL C 1403 ? 1.8575 1.4346 1.8859 -0.2108 -0.8628 -0.0651 1403 VAL B CG2 
25051 N N   . ALA C 1404 ? 1.8928 1.4199 1.8760 -0.1934 -0.8036 0.0140  1404 ALA B N   
25052 C CA  . ALA C 1404 ? 1.8899 1.3960 1.8743 -0.1995 -0.7921 0.0397  1404 ALA B CA  
25053 C C   . ALA C 1404 ? 1.8934 1.4206 1.8988 -0.2230 -0.7825 0.0666  1404 ALA B C   
25054 O O   . ALA C 1404 ? 1.8343 1.4026 1.8393 -0.2251 -0.7752 0.0714  1404 ALA B O   
25055 C CB  . ALA C 1404 ? 1.8515 1.3613 1.8045 -0.1752 -0.7768 0.0454  1404 ALA B CB  
25056 N N   . CYS C 1405 ? 1.9372 1.4354 1.9594 -0.2390 -0.7821 0.0844  1405 CYS B N   
25057 C CA  . CYS C 1405 ? 1.9378 1.4506 1.9800 -0.2608 -0.7725 0.1119  1405 CYS B CA  
25058 C C   . CYS C 1405 ? 1.9392 1.4280 1.9739 -0.2596 -0.7611 0.1361  1405 CYS B C   
25059 O O   . CYS C 1405 ? 1.9694 1.4269 1.9888 -0.2451 -0.7631 0.1306  1405 CYS B O   
25060 C CB  . CYS C 1405 ? 1.9741 1.4762 2.0535 -0.2876 -0.7857 0.1101  1405 CYS B CB  
25061 S SG  . CYS C 1405 ? 2.1997 1.7052 2.2896 -0.2878 -0.8084 0.0730  1405 CYS B SG  
25062 N N   . ALA C 1406 ? 1.8922 1.3966 1.9379 -0.2742 -0.7494 0.1630  1406 ALA B N   
25063 C CA  . ALA C 1406 ? 1.8713 1.3551 1.9114 -0.2747 -0.7386 0.1885  1406 ALA B CA  
25064 C C   . ALA C 1406 ? 1.8894 1.3867 1.9508 -0.2963 -0.7298 0.2159  1406 ALA B C   
25065 O O   . ALA C 1406 ? 1.8622 1.3956 1.9359 -0.3064 -0.7274 0.2179  1406 ALA B O   
25066 C CB  . ALA C 1406 ? 1.8002 1.2982 1.8078 -0.2527 -0.7257 0.1938  1406 ALA B CB  
25067 N N   . SER C 1407 ? 1.9402 1.4089 2.0055 -0.3022 -0.7246 0.2372  1407 SER B N   
25068 C CA  . SER C 1407 ? 1.9511 1.4334 2.0275 -0.3162 -0.7118 0.2675  1407 SER B CA  
25069 C C   . SER C 1407 ? 1.9727 1.4366 2.0276 -0.3041 -0.7012 0.2873  1407 SER B C   
25070 O O   . SER C 1407 ? 2.0153 1.4454 2.0588 -0.2926 -0.7065 0.2800  1407 SER B O   
25071 C CB  . SER C 1407 ? 1.9657 1.4293 2.0780 -0.3416 -0.7174 0.2759  1407 SER B CB  
25072 O OG  . SER C 1407 ? 1.9467 1.4143 2.0650 -0.3511 -0.7030 0.3085  1407 SER B OG  
25073 N N   . TYR C 1408 ? 1.9363 1.4230 1.9843 -0.3052 -0.6866 0.3120  1408 TYR B N   
25074 C CA  . TYR C 1408 ? 1.9134 1.3858 1.9393 -0.2928 -0.6771 0.3307  1408 TYR B CA  
25075 C C   . TYR C 1408 ? 1.9278 1.3673 1.9693 -0.3049 -0.6751 0.3524  1408 TYR B C   
25076 O O   . TYR C 1408 ? 1.9496 1.3978 2.0133 -0.3231 -0.6704 0.3686  1408 TYR B O   
25077 C CB  . TYR C 1408 ? 1.9084 1.4174 1.9147 -0.2855 -0.6628 0.3462  1408 TYR B CB  
25078 C CG  . TYR C 1408 ? 1.9502 1.4450 1.9345 -0.2734 -0.6544 0.3652  1408 TYR B CG  
25079 C CD1 . TYR C 1408 ? 1.9805 1.4447 1.9527 -0.2601 -0.6602 0.3573  1408 TYR B CD1 
25080 C CD2 . TYR C 1408 ? 1.9680 1.4806 1.9430 -0.2739 -0.6411 0.3906  1408 TYR B CD2 
25081 C CE1 . TYR C 1408 ? 2.0136 1.4665 1.9668 -0.2486 -0.6540 0.3735  1408 TYR B CE1 
25082 C CE2 . TYR C 1408 ? 2.0025 1.5019 1.9563 -0.2619 -0.6350 0.4067  1408 TYR B CE2 
25083 C CZ  . TYR C 1408 ? 2.0329 1.5029 1.9766 -0.2495 -0.6419 0.3977  1408 TYR B CZ  
25084 O OH  . TYR C 1408 ? 2.0614 1.5197 1.9847 -0.2368 -0.6371 0.4126  1408 TYR B OH  
25085 N N   . LYS C 1409 ? 1.9120 1.3143 1.9423 -0.2943 -0.6783 0.3532  1409 LYS B N   
25086 C CA  . LYS C 1409 ? 1.9360 1.3037 1.9758 -0.3021 -0.6751 0.3752  1409 LYS B CA  
25087 C C   . LYS C 1409 ? 1.9737 1.3528 1.9938 -0.2933 -0.6605 0.4026  1409 LYS B C   
25088 O O   . LYS C 1409 ? 1.9814 1.3579 1.9754 -0.2739 -0.6591 0.4015  1409 LYS B O   
25089 C CB  . LYS C 1409 ? 1.8954 1.2173 1.9288 -0.2918 -0.6850 0.3640  1409 LYS B CB  
25090 C CG  . LYS C 1409 ? 1.8445 1.1500 1.8895 -0.2946 -0.7007 0.3340  1409 LYS B CG  
25091 C CD  . LYS C 1409 ? 1.8246 1.0861 1.8575 -0.2797 -0.7090 0.3240  1409 LYS B CD  
25092 C CE  . LYS C 1409 ? 1.8559 1.0705 1.9043 -0.2918 -0.7110 0.3374  1409 LYS B CE  
25093 N NZ  . LYS C 1409 ? 1.8802 1.0499 1.9169 -0.2771 -0.7201 0.3261  1409 LYS B NZ  
25094 N N   . PRO C 1410 ? 2.0202 1.4130 2.0525 -0.3068 -0.6497 0.4272  1410 PRO B N   
25095 C CA  . PRO C 1410 ? 2.0633 1.4661 2.0727 -0.2955 -0.6366 0.4520  1410 PRO B CA  
25096 C C   . PRO C 1410 ? 2.1917 1.5550 2.1885 -0.2849 -0.6357 0.4656  1410 PRO B C   
25097 O O   . PRO C 1410 ? 2.2148 1.5420 2.2279 -0.2936 -0.6394 0.4698  1410 PRO B O   
25098 C CB  . PRO C 1410 ? 2.0258 1.4503 2.0537 -0.3126 -0.6254 0.4750  1410 PRO B CB  
25099 C CG  . PRO C 1410 ? 1.9998 1.4456 2.0522 -0.3276 -0.6325 0.4562  1410 PRO B CG  
25100 C CD  . PRO C 1410 ? 2.0218 1.4328 2.0849 -0.3296 -0.6481 0.4321  1410 PRO B CD  
25101 N N   . SER C 1411 ? 2.3065 1.6766 2.2735 -0.2653 -0.6315 0.4711  1411 SER B N   
25102 C CA  . SER C 1411 ? 2.4829 1.8221 2.4345 -0.2523 -0.6301 0.4853  1411 SER B CA  
25103 C C   . SER C 1411 ? 2.6540 1.9903 2.6091 -0.2596 -0.6173 0.5177  1411 SER B C   
25104 O O   . SER C 1411 ? 2.6512 2.0181 2.6113 -0.2683 -0.6084 0.5286  1411 SER B O   
25105 C CB  . SER C 1411 ? 2.4709 1.8240 2.3910 -0.2301 -0.6301 0.4804  1411 SER B CB  
25106 O OG  . SER C 1411 ? 2.4595 1.8288 2.3764 -0.2247 -0.6381 0.4524  1411 SER B OG  
25107 N N   . ARG C 1412 ? 2.8469 2.1468 2.7988 -0.2548 -0.6156 0.5337  1412 ARG B N   
25108 C CA  . ARG C 1412 ? 3.0221 2.3153 2.9751 -0.2592 -0.6023 0.5665  1412 ARG B CA  
25109 C C   . ARG C 1412 ? 2.9977 2.3276 2.9282 -0.2495 -0.5920 0.5803  1412 ARG B C   
25110 O O   . ARG C 1412 ? 2.9897 2.3364 2.8960 -0.2335 -0.5958 0.5682  1412 ARG B O   
25111 C CB  . ARG C 1412 ? 3.2172 2.4677 3.1576 -0.2465 -0.6021 0.5802  1412 ARG B CB  
25112 C CG  . ARG C 1412 ? 3.3497 2.6023 3.2567 -0.2204 -0.6064 0.5745  1412 ARG B CG  
25113 C CD  . ARG C 1412 ? 3.5155 2.7338 3.4062 -0.2057 -0.6028 0.5954  1412 ARG B CD  
25114 N NE  . ARG C 1412 ? 3.6005 2.8330 3.4586 -0.1822 -0.6034 0.5975  1412 ARG B NE  
25115 C CZ  . ARG C 1412 ? 3.6989 2.9096 3.5363 -0.1643 -0.6015 0.6138  1412 ARG B CZ  
25116 N NH1 . ARG C 1412 ? 3.7631 2.9348 3.6078 -0.1666 -0.5974 0.6304  1412 ARG B NH1 
25117 N NH2 . ARG C 1412 ? 3.7077 2.9352 3.5172 -0.1440 -0.6038 0.6130  1412 ARG B NH2 
25118 N N   . GLU C 1413 ? 2.9770 2.3185 2.9155 -0.2592 -0.5788 0.6058  1413 GLU B N   
25119 C CA  . GLU C 1413 ? 2.9252 2.2998 2.8415 -0.2498 -0.5680 0.6211  1413 GLU B CA  
25120 C C   . GLU C 1413 ? 2.7141 2.1308 2.6355 -0.2569 -0.5688 0.6050  1413 GLU B C   
25121 O O   . GLU C 1413 ? 2.6725 2.1190 2.5805 -0.2530 -0.5589 0.6178  1413 GLU B O   
25122 C CB  . GLU C 1413 ? 3.0575 2.4278 2.9356 -0.2242 -0.5704 0.6210  1413 GLU B CB  
25123 C CG  . GLU C 1413 ? 3.2108 2.5407 3.0792 -0.2126 -0.5714 0.6339  1413 GLU B CG  
25124 C CD  . GLU C 1413 ? 3.3235 2.6458 3.1829 -0.2088 -0.5566 0.6691  1413 GLU B CD  
25125 O OE1 . GLU C 1413 ? 3.3466 2.6972 3.1900 -0.2036 -0.5474 0.6821  1413 GLU B OE1 
25126 O OE2 . GLU C 1413 ? 3.3829 2.6696 3.2495 -0.2097 -0.5537 0.6842  1413 GLU B OE2 
25127 N N   . GLU C 1414 ? 2.5378 1.9564 2.4764 -0.2656 -0.5805 0.5771  1414 GLU B N   
25128 C CA  . GLU C 1414 ? 2.3179 1.7749 2.2571 -0.2686 -0.5824 0.5588  1414 GLU B CA  
25129 C C   . GLU C 1414 ? 2.2195 1.7024 2.1868 -0.2886 -0.5767 0.5648  1414 GLU B C   
25130 O O   . GLU C 1414 ? 2.2335 1.7019 2.2310 -0.3060 -0.5761 0.5733  1414 GLU B O   
25131 C CB  . GLU C 1414 ? 2.1973 1.6485 2.1381 -0.2655 -0.5970 0.5256  1414 GLU B CB  
25132 C CG  . GLU C 1414 ? 2.0721 1.5379 1.9814 -0.2461 -0.5992 0.5124  1414 GLU B CG  
25133 C CD  . GLU C 1414 ? 1.9955 1.4489 1.9059 -0.2406 -0.6123 0.4833  1414 GLU B CD  
25134 O OE1 . GLU C 1414 ? 1.9798 1.4155 1.9141 -0.2518 -0.6202 0.4717  1414 GLU B OE1 
25135 O OE2 . GLU C 1414 ? 1.9620 1.4227 1.8495 -0.2249 -0.6147 0.4721  1414 GLU B OE2 
25136 N N   . SER C 1415 ? 2.1331 1.6551 2.0904 -0.2857 -0.5727 0.5597  1415 SER B N   
25137 C CA  . SER C 1415 ? 2.0936 1.6485 2.0748 -0.3017 -0.5674 0.5636  1415 SER B CA  
25138 C C   . SER C 1415 ? 2.0870 1.6448 2.0993 -0.3176 -0.5800 0.5377  1415 SER B C   
25139 O O   . SER C 1415 ? 2.1008 1.6475 2.1068 -0.3114 -0.5921 0.5114  1415 SER B O   
25140 C CB  . SER C 1415 ? 2.0508 1.6443 2.0056 -0.2897 -0.5597 0.5650  1415 SER B CB  
25141 O OG  . SER C 1415 ? 2.0285 1.6566 2.0017 -0.3006 -0.5602 0.5542  1415 SER B OG  
25142 N N   . SER C 1416 ? 2.0835 1.6580 2.1296 -0.3377 -0.5772 0.5450  1416 SER B N   
25143 C CA  . SER C 1416 ? 2.0914 1.6692 2.1696 -0.3544 -0.5901 0.5211  1416 SER B CA  
25144 C C   . SER C 1416 ? 2.0586 1.6737 2.1304 -0.3496 -0.5957 0.4966  1416 SER B C   
25145 O O   . SER C 1416 ? 2.0368 1.6603 2.1346 -0.3625 -0.6063 0.4768  1416 SER B O   
25146 C CB  . SER C 1416 ? 2.1205 1.7044 2.2408 -0.3793 -0.5858 0.5376  1416 SER B CB  
25147 O OG  . SER C 1416 ? 2.1133 1.7348 2.2327 -0.3800 -0.5702 0.5616  1416 SER B OG  
25148 N N   . SER C 1417 ? 2.0484 1.6844 2.0852 -0.3308 -0.5886 0.4978  1417 SER B N   
25149 C CA  . SER C 1417 ? 2.0276 1.7012 2.0551 -0.3249 -0.5901 0.4797  1417 SER B CA  
25150 C C   . SER C 1417 ? 1.9865 1.6489 2.0082 -0.3181 -0.6046 0.4463  1417 SER B C   
25151 O O   . SER C 1417 ? 2.0315 1.7198 2.0571 -0.3183 -0.6097 0.4267  1417 SER B O   
25152 C CB  . SER C 1417 ? 2.0187 1.7128 2.0078 -0.3064 -0.5776 0.4918  1417 SER B CB  
25153 O OG  . SER C 1417 ? 2.0304 1.6961 1.9899 -0.2903 -0.5783 0.4916  1417 SER B OG  
25154 N N   . GLY C 1418 ? 1.9220 1.5463 1.9331 -0.3105 -0.6108 0.4402  1418 GLY B N   
25155 C CA  . GLY C 1418 ? 1.8358 1.4476 1.8384 -0.3011 -0.6230 0.4105  1418 GLY B CA  
25156 C C   . GLY C 1418 ? 1.7848 1.3985 1.7493 -0.2790 -0.6191 0.4054  1418 GLY B C   
25157 O O   . GLY C 1418 ? 1.7558 1.3803 1.6988 -0.2709 -0.6079 0.4235  1418 GLY B O   
25158 N N   . SER C 1419 ? 1.7808 1.3844 1.7371 -0.2693 -0.6284 0.3802  1419 SER B N   
25159 C CA  . SER C 1419 ? 1.7280 1.3254 1.6533 -0.2501 -0.6262 0.3753  1419 SER B CA  
25160 C C   . SER C 1419 ? 1.6389 1.2668 1.5369 -0.2387 -0.6157 0.3782  1419 SER B C   
25161 O O   . SER C 1419 ? 1.6164 1.2738 1.5163 -0.2437 -0.6094 0.3837  1419 SER B O   
25162 C CB  . SER C 1419 ? 1.7415 1.3230 1.6659 -0.2418 -0.6375 0.3481  1419 SER B CB  
25163 O OG  . SER C 1419 ? 1.7107 1.2884 1.6083 -0.2243 -0.6344 0.3450  1419 SER B OG  
25164 N N   . SER C 1420 ? 1.5602 1.1795 1.4331 -0.2233 -0.6141 0.3749  1420 SER B N   
25165 C CA  . SER C 1420 ? 1.4947 1.1357 1.3386 -0.2106 -0.6056 0.3737  1420 SER B CA  
25166 C C   . SER C 1420 ? 1.4933 1.1433 1.3327 -0.2031 -0.6099 0.3474  1420 SER B C   
25167 O O   . SER C 1420 ? 1.5295 1.1687 1.3869 -0.2067 -0.6198 0.3310  1420 SER B O   
25168 C CB  . SER C 1420 ? 1.4585 1.0842 1.2801 -0.1985 -0.6033 0.3811  1420 SER B CB  
25169 O OG  . SER C 1420 ? 1.4302 1.0476 1.2449 -0.1878 -0.6089 0.3604  1420 SER B OG  
25170 N N   . HIS C 1421 ? 1.4500 1.1175 1.2639 -0.1916 -0.6022 0.3434  1421 HIS B N   
25171 C CA  . HIS C 1421 ? 1.4171 1.0927 1.2236 -0.1823 -0.6042 0.3198  1421 HIS B CA  
25172 C C   . HIS C 1421 ? 1.3478 0.9982 1.1646 -0.1784 -0.6145 0.3046  1421 HIS B C   
25173 O O   . HIS C 1421 ? 1.3123 0.9445 1.1230 -0.1729 -0.6154 0.3096  1421 HIS B O   
25174 C CB  . HIS C 1421 ? 1.4372 1.1264 1.2125 -0.1696 -0.5936 0.3204  1421 HIS B CB  
25175 C CG  . HIS C 1421 ? 1.4308 1.1173 1.1955 -0.1571 -0.5945 0.3000  1421 HIS B CG  
25176 N ND1 . HIS C 1421 ? 1.4265 1.1136 1.1675 -0.1464 -0.5872 0.3003  1421 HIS B ND1 
25177 C CD2 . HIS C 1421 ? 1.4303 1.1132 1.2051 -0.1533 -0.6014 0.2792  1421 HIS B CD2 
25178 C CE1 . HIS C 1421 ? 1.4267 1.1116 1.1651 -0.1370 -0.5885 0.2816  1421 HIS B CE1 
25179 N NE2 . HIS C 1421 ? 1.4300 1.1123 1.1873 -0.1399 -0.5969 0.2687  1421 HIS B NE2 
25180 N N   . ALA C 1422 ? 1.3485 0.9983 1.1806 -0.1806 -0.6228 0.2861  1422 ALA B N   
25181 C CA  . ALA C 1422 ? 1.3576 0.9819 1.2011 -0.1772 -0.6338 0.2711  1422 ALA B CA  
25182 C C   . ALA C 1422 ? 1.4010 1.0321 1.2429 -0.1685 -0.6384 0.2459  1422 ALA B C   
25183 O O   . ALA C 1422 ? 1.4034 1.0588 1.2412 -0.1682 -0.6353 0.2394  1422 ALA B O   
25184 C CB  . ALA C 1422 ? 1.3841 0.9882 1.2531 -0.1914 -0.6427 0.2769  1422 ALA B CB  
25185 N N   . VAL C 1423 ? 1.4500 1.0597 1.2940 -0.1598 -0.6457 0.2320  1423 VAL B N   
25186 C CA  . VAL C 1423 ? 1.4838 1.0973 1.3237 -0.1484 -0.6499 0.2078  1423 VAL B CA  
25187 C C   . VAL C 1423 ? 1.5516 1.1390 1.4099 -0.1512 -0.6644 0.1948  1423 VAL B C   
25188 O O   . VAL C 1423 ? 1.5416 1.1040 1.4101 -0.1564 -0.6691 0.2039  1423 VAL B O   
25189 C CB  . VAL C 1423 ? 1.1332 0.7489 0.9524 -0.1298 -0.6426 0.2004  1423 VAL B CB  
25190 C CG1 . VAL C 1423 ? 1.1986 0.8242 1.0028 -0.1291 -0.6308 0.2181  1423 VAL B CG1 
25191 C CG2 . VAL C 1423 ? 1.1498 0.7393 0.9748 -0.1215 -0.6505 0.1911  1423 VAL B CG2 
25192 N N   . MET C 1424 ? 1.4969 1.0900 1.3584 -0.1477 -0.6717 0.1740  1424 MET B N   
25193 C CA  . MET C 1424 ? 1.4503 1.0188 1.3228 -0.1448 -0.6861 0.1549  1424 MET B CA  
25194 C C   . MET C 1424 ? 1.4953 1.0658 1.3489 -0.1222 -0.6843 0.1358  1424 MET B C   
25195 O O   . MET C 1424 ? 1.4808 1.0766 1.3178 -0.1123 -0.6751 0.1314  1424 MET B O   
25196 C CB  . MET C 1424 ? 1.3904 0.9654 1.2808 -0.1578 -0.6967 0.1448  1424 MET B CB  
25197 C CG  . MET C 1424 ? 1.3427 0.9398 1.2437 -0.1755 -0.6908 0.1637  1424 MET B CG  
25198 S SD  . MET C 1424 ? 1.4322 1.0425 1.3600 -0.1938 -0.7029 0.1546  1424 MET B SD  
25199 C CE  . MET C 1424 ? 1.3223 0.8892 1.2685 -0.1981 -0.7222 0.1375  1424 MET B CE  
25200 N N   . ASP C 1425 ? 1.5170 1.0602 1.3721 -0.1128 -0.6923 0.1253  1425 ASP B N   
25201 C CA  . ASP C 1425 ? 1.5484 1.0923 1.3860 -0.0901 -0.6886 0.1109  1425 ASP B CA  
25202 C C   . ASP C 1425 ? 1.6082 1.1271 1.4507 -0.0823 -0.7034 0.0896  1425 ASP B C   
25203 O O   . ASP C 1425 ? 1.6580 1.1469 1.5086 -0.0829 -0.7111 0.0908  1425 ASP B O   
25204 C CB  . ASP C 1425 ? 1.5674 1.1050 1.3985 -0.0831 -0.6799 0.1245  1425 ASP B CB  
25205 C CG  . ASP C 1425 ? 1.6060 1.1404 1.4241 -0.0603 -0.6767 0.1113  1425 ASP B CG  
25206 O OD1 . ASP C 1425 ? 1.6066 1.1472 1.4179 -0.0535 -0.6668 0.1212  1425 ASP B OD1 
25207 O OD2 . ASP C 1425 ? 1.6409 1.1670 1.4560 -0.0488 -0.6842 0.0915  1425 ASP B OD2 
25208 N N   . ILE C 1426 ? 1.5810 1.1114 1.4165 -0.0739 -0.7076 0.0700  1426 ILE B N   
25209 C CA  . ILE C 1426 ? 1.5607 1.0690 1.3964 -0.0635 -0.7220 0.0470  1426 ILE B CA  
25210 C C   . ILE C 1426 ? 1.5323 1.0411 1.3468 -0.0359 -0.7164 0.0335  1426 ILE B C   
25211 O O   . ILE C 1426 ? 1.5046 1.0387 1.3030 -0.0236 -0.7070 0.0277  1426 ILE B O   
25212 C CB  . ILE C 1426 ? 1.5498 1.0695 1.3911 -0.0698 -0.7324 0.0314  1426 ILE B CB  
25213 C CG1 . ILE C 1426 ? 1.5305 1.0623 1.3919 -0.0964 -0.7329 0.0477  1426 ILE B CG1 
25214 C CG2 . ILE C 1426 ? 1.5954 1.0844 1.4417 -0.0650 -0.7514 0.0090  1426 ILE B CG2 
25215 C CD1 . ILE C 1426 ? 1.5430 1.0719 1.4223 -0.1097 -0.7496 0.0335  1426 ILE B CD1 
25216 N N   . SER C 1427 ? 1.5387 1.0192 1.3530 -0.0257 -0.7214 0.0299  1427 SER B N   
25217 C CA  . SER C 1427 ? 1.5249 1.0006 1.3218 0.0014  -0.7187 0.0156  1427 SER B CA  
25218 C C   . SER C 1427 ? 1.5225 0.9921 1.3135 0.0098  -0.7322 -0.0099 1427 SER B C   
25219 O O   . SER C 1427 ? 1.5551 1.0058 1.3602 -0.0043 -0.7483 -0.0171 1427 SER B O   
25220 C CB  . SER C 1427 ? 1.4321 0.8775 1.2335 0.0073  -0.7224 0.0202  1427 SER B CB  
25221 O OG  . SER C 1427 ? 1.4457 0.8796 1.2332 0.0336  -0.7233 0.0051  1427 SER B OG  
25222 N N   . LEU C 1428 ? 1.4843 0.9706 1.2551 0.0320  -0.7256 -0.0233 1428 LEU B N   
25223 C CA  . LEU C 1428 ? 1.4876 0.9671 1.2491 0.0445  -0.7391 -0.0493 1428 LEU B CA  
25224 C C   . LEU C 1428 ? 1.5256 0.9781 1.2757 0.0680  -0.7439 -0.0623 1428 LEU B C   
25225 O O   . LEU C 1428 ? 1.5051 0.9610 1.2469 0.0826  -0.7301 -0.0534 1428 LEU B O   
25226 C CB  . LEU C 1428 ? 1.4298 0.9420 1.1729 0.0579  -0.7297 -0.0575 1428 LEU B CB  
25227 C CG  . LEU C 1428 ? 1.3782 0.9175 1.1317 0.0354  -0.7244 -0.0433 1428 LEU B CG  
25228 C CD1 . LEU C 1428 ? 1.3713 0.9438 1.1047 0.0488  -0.7114 -0.0465 1428 LEU B CD1 
25229 C CD2 . LEU C 1428 ? 1.3729 0.9031 1.1477 0.0131  -0.7438 -0.0499 1428 LEU B CD2 
25230 N N   . PRO C 1429 ? 1.5405 0.9655 1.2912 0.0710  -0.7638 -0.0830 1429 PRO B N   
25231 C CA  . PRO C 1429 ? 1.5580 0.9539 1.2945 0.0957  -0.7710 -0.0989 1429 PRO B CA  
25232 C C   . PRO C 1429 ? 1.5461 0.9608 1.2563 0.1272  -0.7593 -0.1092 1429 PRO B C   
25233 O O   . PRO C 1429 ? 1.5055 0.9500 1.2068 0.1300  -0.7518 -0.1117 1429 PRO B O   
25234 C CB  . PRO C 1429 ? 1.5726 0.9415 1.3148 0.0884  -0.7956 -0.1205 1429 PRO B CB  
25235 C CG  . PRO C 1429 ? 1.5681 0.9410 1.3369 0.0538  -0.8004 -0.1071 1429 PRO B CG  
25236 C CD  . PRO C 1429 ? 1.5322 0.9478 1.3017 0.0466  -0.7816 -0.0892 1429 PRO B CD  
25237 N N   . THR C 1430 ? 1.5734 0.9710 1.2707 0.1514  -0.7565 -0.1138 1430 THR B N   
25238 C CA  . THR C 1430 ? 1.5699 0.9869 1.2447 0.1812  -0.7401 -0.1169 1430 THR B CA  
25239 C C   . THR C 1430 ? 1.6301 1.0580 1.2852 0.1964  -0.7456 -0.1388 1430 THR B C   
25240 O O   . THR C 1430 ? 1.6909 1.0956 1.3393 0.2035  -0.7651 -0.1609 1430 THR B O   
25241 C CB  . THR C 1430 ? 1.5702 0.9645 1.2361 0.2054  -0.7386 -0.1195 1430 THR B CB  
25242 O OG1 . THR C 1430 ? 1.5619 0.9313 1.2469 0.1887  -0.7460 -0.1080 1430 THR B OG1 
25243 C CG2 . THR C 1430 ? 1.5321 0.9528 1.1887 0.2244  -0.7144 -0.1072 1430 THR B CG2 
25244 N N   . GLY C 1431 ? 1.6197 1.0826 1.2656 0.2006  -0.7287 -0.1323 1431 GLY B N   
25245 C CA  . GLY C 1431 ? 1.6344 1.1137 1.2611 0.2144  -0.7311 -0.1497 1431 GLY B CA  
25246 C C   . GLY C 1431 ? 1.6423 1.1208 1.2804 0.1935  -0.7515 -0.1619 1431 GLY B C   
25247 O O   . GLY C 1431 ? 1.6285 1.0880 1.2600 0.2021  -0.7711 -0.1850 1431 GLY B O   
25248 N N   . ILE C 1432 ? 1.6945 1.1946 1.3499 0.1666  -0.7470 -0.1464 1432 ILE B N   
25249 C CA  . ILE C 1432 ? 1.7406 1.2449 1.4121 0.1435  -0.7643 -0.1539 1432 ILE B CA  
25250 C C   . ILE C 1432 ? 1.7459 1.2860 1.4244 0.1263  -0.7502 -0.1356 1432 ILE B C   
25251 O O   . ILE C 1432 ? 1.7676 1.3087 1.4703 0.0976  -0.7523 -0.1202 1432 ILE B O   
25252 C CB  . ILE C 1432 ? 1.5404 1.0155 1.2406 0.1159  -0.7801 -0.1486 1432 ILE B CB  
25253 C CG1 . ILE C 1432 ? 1.6314 1.0663 1.3257 0.1311  -0.7903 -0.1598 1432 ILE B CG1 
25254 C CG2 . ILE C 1432 ? 1.5123 0.9911 1.2317 0.0920  -0.7992 -0.1582 1432 ILE B CG2 
25255 C CD1 . ILE C 1432 ? 1.7148 1.1264 1.3996 0.1431  -0.8140 -0.1906 1432 ILE B CD1 
25256 N N   . SER C 1433 ? 1.7177 1.2858 1.3738 0.1447  -0.7351 -0.1365 1433 SER B N   
25257 C CA  . SER C 1433 ? 1.6778 1.2795 1.3348 0.1326  -0.7196 -0.1193 1433 SER B CA  
25258 C C   . SER C 1433 ? 1.6498 1.2624 1.3309 0.1026  -0.7321 -0.1158 1433 SER B C   
25259 O O   . SER C 1433 ? 1.6593 1.2656 1.3490 0.0976  -0.7529 -0.1341 1433 SER B O   
25260 C CB  . SER C 1433 ? 1.6913 1.3178 1.3183 0.1589  -0.7085 -0.1290 1433 SER B CB  
25261 O OG  . SER C 1433 ? 1.7151 1.3326 1.3185 0.1895  -0.6974 -0.1347 1433 SER B OG  
25262 N N   . ALA C 1434 ? 1.6413 1.2709 1.3335 0.0828  -0.7197 -0.0927 1434 ALA B N   
25263 C CA  . ALA C 1434 ? 1.6831 1.3260 1.3982 0.0556  -0.7296 -0.0876 1434 ALA B CA  
25264 C C   . ALA C 1434 ? 1.6877 1.3663 1.3885 0.0628  -0.7235 -0.0914 1434 ALA B C   
25265 O O   . ALA C 1434 ? 1.7070 1.3978 1.3800 0.0870  -0.7088 -0.0938 1434 ALA B O   
25266 C CB  . ALA C 1434 ? 1.6953 1.3369 1.4294 0.0310  -0.7208 -0.0607 1434 ALA B CB  
25267 N N   . ASN C 1435 ? 1.6903 1.3863 1.4103 0.0424  -0.7340 -0.0910 1435 ASN B N   
25268 C CA  . ASN C 1435 ? 1.6800 1.4117 1.3879 0.0499  -0.7314 -0.0971 1435 ASN B CA  
25269 C C   . ASN C 1435 ? 1.6592 1.4180 1.3603 0.0436  -0.7102 -0.0733 1435 ASN B C   
25270 O O   . ASN C 1435 ? 1.6245 1.4026 1.3439 0.0228  -0.7127 -0.0630 1435 ASN B O   
25271 C CB  . ASN C 1435 ? 1.7100 1.4512 1.4417 0.0339  -0.7549 -0.1121 1435 ASN B CB  
25272 C CG  . ASN C 1435 ? 1.7290 1.5071 1.4459 0.0469  -0.7553 -0.1235 1435 ASN B CG  
25273 O OD1 . ASN C 1435 ? 1.7166 1.5127 1.4053 0.0662  -0.7363 -0.1173 1435 ASN B OD1 
25274 N ND2 . ASN C 1435 ? 1.7580 1.5475 1.4942 0.0368  -0.7770 -0.1404 1435 ASN B ND2 
25275 N N   . GLU C 1436 ? 1.6705 1.4308 1.3448 0.0624  -0.6891 -0.0649 1436 GLU B N   
25276 C CA  . GLU C 1436 ? 1.6736 1.4530 1.3388 0.0572  -0.6685 -0.0422 1436 GLU B CA  
25277 C C   . GLU C 1436 ? 1.6544 1.4647 1.3288 0.0437  -0.6722 -0.0381 1436 GLU B C   
25278 O O   . GLU C 1436 ? 1.6342 1.4524 1.3211 0.0239  -0.6658 -0.0176 1436 GLU B O   
25279 C CB  . GLU C 1436 ? 1.7191 1.5047 1.3488 0.0852  -0.6480 -0.0424 1436 GLU B CB  
25280 C CG  . GLU C 1436 ? 1.7375 1.5350 1.3553 0.0808  -0.6253 -0.0188 1436 GLU B CG  
25281 C CD  . GLU C 1436 ? 1.7588 1.5356 1.3733 0.0825  -0.6112 -0.0057 1436 GLU B CD  
25282 O OE1 . GLU C 1436 ? 1.7863 1.5396 1.4138 0.0816  -0.6203 -0.0114 1436 GLU B OE1 
25283 O OE2 . GLU C 1436 ? 1.7355 1.5196 1.3340 0.0850  -0.5913 0.0098  1436 GLU B OE2 
25284 N N   . GLU C 1437 ? 1.6541 1.4825 1.3223 0.0552  -0.6831 -0.0579 1437 GLU B N   
25285 C CA  . GLU C 1437 ? 1.6365 1.4998 1.3104 0.0470  -0.6854 -0.0554 1437 GLU B CA  
25286 C C   . GLU C 1437 ? 1.6430 1.5076 1.3570 0.0143  -0.7000 -0.0475 1437 GLU B C   
25287 O O   . GLU C 1437 ? 1.6410 1.5281 1.3643 -0.0003 -0.6935 -0.0305 1437 GLU B O   
25288 C CB  . GLU C 1437 ? 1.6148 1.4979 1.2742 0.0680  -0.6963 -0.0807 1437 GLU B CB  
25289 C CG  . GLU C 1437 ? 2.2502 2.1168 1.8786 0.1002  -0.6929 -0.0983 1437 GLU B CG  
25290 C CD  . GLU C 1437 ? 2.1903 2.0600 1.7828 0.1217  -0.6652 -0.0856 1437 GLU B CD  
25291 O OE1 . GLU C 1437 ? 2.1635 2.0591 1.7443 0.1224  -0.6523 -0.0737 1437 GLU B OE1 
25292 O OE2 . GLU C 1437 ? 2.1556 2.0021 1.7322 0.1379  -0.6562 -0.0875 1437 GLU B OE2 
25293 N N   . ASP C 1438 ? 1.6784 1.5177 1.4154 0.0036  -0.7188 -0.0592 1438 ASP B N   
25294 C CA  . ASP C 1438 ? 1.6898 1.5262 1.4662 -0.0278 -0.7325 -0.0519 1438 ASP B CA  
25295 C C   . ASP C 1438 ? 1.6419 1.4760 1.4263 -0.0456 -0.7168 -0.0214 1438 ASP B C   
25296 O O   . ASP C 1438 ? 1.6455 1.4979 1.4521 -0.0667 -0.7179 -0.0078 1438 ASP B O   
25297 C CB  . ASP C 1438 ? 1.7305 1.5299 1.5253 -0.0347 -0.7517 -0.0666 1438 ASP B CB  
25298 C CG  . ASP C 1438 ? 1.7521 1.5549 1.5504 -0.0266 -0.7740 -0.0970 1438 ASP B CG  
25299 O OD1 . ASP C 1438 ? 1.7438 1.5814 1.5393 -0.0218 -0.7773 -0.1053 1438 ASP B OD1 
25300 O OD2 . ASP C 1438 ? 1.7702 1.5407 1.5734 -0.0243 -0.7888 -0.1132 1438 ASP B OD2 
25301 N N   . LEU C 1439 ? 1.5830 1.3954 1.3496 -0.0363 -0.7024 -0.0112 1439 LEU B N   
25302 C CA  . LEU C 1439 ? 1.5077 1.3122 1.2793 -0.0507 -0.6888 0.0158  1439 LEU B CA  
25303 C C   . LEU C 1439 ? 1.4913 1.3261 1.2467 -0.0486 -0.6711 0.0326  1439 LEU B C   
25304 O O   . LEU C 1439 ? 1.4803 1.3236 1.2495 -0.0671 -0.6665 0.0528  1439 LEU B O   
25305 C CB  . LEU C 1439 ? 1.4816 1.2567 1.2384 -0.0388 -0.6801 0.0187  1439 LEU B CB  
25306 C CG  . LEU C 1439 ? 1.4720 1.2130 1.2413 -0.0385 -0.6953 0.0047  1439 LEU B CG  
25307 C CD1 . LEU C 1439 ? 1.4608 1.1811 1.2108 -0.0206 -0.6844 0.0056  1439 LEU B CD1 
25308 C CD2 . LEU C 1439 ? 1.4679 1.1917 1.2694 -0.0656 -0.7055 0.0165  1439 LEU B CD2 
25309 N N   . LYS C 1440 ? 1.5019 1.3512 1.2260 -0.0246 -0.6604 0.0245  1440 LYS B N   
25310 C CA  . LYS C 1440 ? 1.5034 1.3821 1.2079 -0.0189 -0.6445 0.0366  1440 LYS B CA  
25311 C C   . LYS C 1440 ? 1.4791 1.3846 1.2079 -0.0374 -0.6539 0.0412  1440 LYS B C   
25312 O O   . LYS C 1440 ? 1.4406 1.3638 1.1679 -0.0456 -0.6430 0.0607  1440 LYS B O   
25313 C CB  . LYS C 1440 ? 1.5783 1.4716 1.2502 0.0098  -0.6380 0.0207  1440 LYS B CB  
25314 C CG  . LYS C 1440 ? 1.6531 1.5267 1.2957 0.0315  -0.6230 0.0189  1440 LYS B CG  
25315 C CD  . LYS C 1440 ? 1.6918 1.5695 1.3111 0.0349  -0.5994 0.0399  1440 LYS B CD  
25316 C CE  . LYS C 1440 ? 1.8426 1.7252 1.4231 0.0638  -0.5825 0.0336  1440 LYS B CE  
25317 N NZ  . LYS C 1440 ? 1.8544 1.7204 1.4244 0.0843  -0.5848 0.0152  1440 LYS B NZ  
25318 N N   . ALA C 1441 ? 1.4965 1.4050 1.2483 -0.0435 -0.6745 0.0228  1441 ALA B N   
25319 C CA  . ALA C 1441 ? 1.5261 1.4622 1.3062 -0.0616 -0.6859 0.0239  1441 ALA B CA  
25320 C C   . ALA C 1441 ? 1.5641 1.4958 1.3697 -0.0883 -0.6827 0.0489  1441 ALA B C   
25321 O O   . ALA C 1441 ? 1.5791 1.5400 1.3975 -0.1000 -0.6802 0.0614  1441 ALA B O   
25322 C CB  . ALA C 1441 ? 1.5325 1.4632 1.3360 -0.0664 -0.7106 -0.0012 1441 ALA B CB  
25323 N N   . LEU C 1442 ? 1.5944 1.4903 1.4073 -0.0968 -0.6827 0.0564  1442 LEU B N   
25324 C CA  . LEU C 1442 ? 1.6164 1.5033 1.4556 -0.1219 -0.6823 0.0782  1442 LEU B CA  
25325 C C   . LEU C 1442 ? 1.6763 1.5724 1.4987 -0.1222 -0.6620 0.1045  1442 LEU B C   
25326 O O   . LEU C 1442 ? 1.7275 1.6396 1.5668 -0.1387 -0.6591 0.1226  1442 LEU B O   
25327 C CB  . LEU C 1442 ? 1.5711 1.4160 1.4227 -0.1290 -0.6905 0.0758  1442 LEU B CB  
25328 C CG  . LEU C 1442 ? 1.5650 1.4054 1.4443 -0.1387 -0.7129 0.0551  1442 LEU B CG  
25329 C CD1 . LEU C 1442 ? 1.5865 1.3848 1.4676 -0.1354 -0.7229 0.0427  1442 LEU B CD1 
25330 C CD2 . LEU C 1442 ? 1.5666 1.4194 1.4830 -0.1670 -0.7189 0.0693  1442 LEU B CD2 
25331 N N   . VAL C 1443 ? 1.7114 1.5974 1.5006 -0.1037 -0.6477 0.1065  1443 VAL B N   
25332 C CA  . VAL C 1443 ? 1.7146 1.6033 1.4850 -0.1031 -0.6291 0.1300  1443 VAL B CA  
25333 C C   . VAL C 1443 ? 1.7463 1.6689 1.4929 -0.0914 -0.6162 0.1351  1443 VAL B C   
25334 O O   . VAL C 1443 ? 1.7314 1.6614 1.4668 -0.0944 -0.6030 0.1558  1443 VAL B O   
25335 C CB  . VAL C 1443 ? 1.7542 1.6147 1.5017 -0.0905 -0.6194 0.1311  1443 VAL B CB  
25336 C CG1 . VAL C 1443 ? 1.7655 1.6004 1.5224 -0.0860 -0.6323 0.1117  1443 VAL B CG1 
25337 C CG2 . VAL C 1443 ? 1.7467 1.6196 1.4567 -0.0686 -0.6034 0.1289  1443 VAL B CG2 
25338 N N   . GLU C 1444 ? 1.7609 1.7030 1.4978 -0.0767 -0.6204 0.1160  1444 GLU B N   
25339 C CA  . GLU C 1444 ? 1.7974 1.7644 1.5021 -0.0584 -0.6060 0.1179  1444 GLU B CA  
25340 C C   . GLU C 1444 ? 1.7604 1.7654 1.4756 -0.0655 -0.6066 0.1258  1444 GLU B C   
25341 O O   . GLU C 1444 ? 1.7262 1.7554 1.4161 -0.0495 -0.5966 0.1258  1444 GLU B O   
25342 C CB  . GLU C 1444 ? 1.9105 1.8784 1.5946 -0.0349 -0.6082 0.0937  1444 GLU B CB  
25343 C CG  . GLU C 1444 ? 1.9955 1.9793 1.6392 -0.0115 -0.5907 0.0947  1444 GLU B CG  
25344 C CD  . GLU C 1444 ? 2.0662 2.0361 1.6849 0.0127  -0.5879 0.0758  1444 GLU B CD  
25345 O OE1 . GLU C 1444 ? 2.0793 2.0186 1.6988 0.0126  -0.5872 0.0743  1444 GLU B OE1 
25346 O OE2 . GLU C 1444 ? 2.0900 2.0803 1.6882 0.0327  -0.5859 0.0632  1444 GLU B OE2 
25347 N N   . GLY C 1445 ? 1.7714 1.7819 1.5240 -0.0891 -0.6176 0.1335  1445 GLY B N   
25348 C CA  . GLY C 1445 ? 1.8067 1.8569 1.5757 -0.0970 -0.6200 0.1396  1445 GLY B CA  
25349 C C   . GLY C 1445 ? 1.8175 1.8730 1.6055 -0.1172 -0.6143 0.1665  1445 GLY B C   
25350 O O   . GLY C 1445 ? 1.8415 1.8681 1.6426 -0.1311 -0.6152 0.1772  1445 GLY B O   
25351 N N   . VAL C 1446 ? 1.8210 1.9143 1.6092 -0.1173 -0.6079 0.1779  1446 VAL B N   
25352 C CA  . VAL C 1446 ? 1.8213 1.9244 1.6272 -0.1348 -0.6014 0.2047  1446 VAL B CA  
25353 C C   . VAL C 1446 ? 1.8039 1.8924 1.6555 -0.1612 -0.6156 0.2072  1446 VAL B C   
25354 O O   . VAL C 1446 ? 1.7946 1.8732 1.6585 -0.1757 -0.6100 0.2296  1446 VAL B O   
25355 C CB  . VAL C 1446 ? 1.8327 1.9853 1.6433 -0.1330 -0.5972 0.2125  1446 VAL B CB  
25356 C CG1 . VAL C 1446 ? 1.8431 2.0039 1.6649 -0.1472 -0.5868 0.2429  1446 VAL B CG1 
25357 C CG2 . VAL C 1446 ? 1.8292 1.9981 1.5948 -0.1051 -0.5850 0.2066  1446 VAL B CG2 
25358 N N   . ASP C 1447 ? 1.8071 1.8935 1.6825 -0.1665 -0.6339 0.1841  1447 ASP B N   
25359 C CA  . ASP C 1447 ? 1.8248 1.8911 1.7415 -0.1906 -0.6484 0.1833  1447 ASP B CA  
25360 C C   . ASP C 1447 ? 1.8163 1.8328 1.7218 -0.1888 -0.6491 0.1806  1447 ASP B C   
25361 O O   . ASP C 1447 ? 1.8284 1.8195 1.7603 -0.2030 -0.6627 0.1732  1447 ASP B O   
25362 C CB  . ASP C 1447 ? 1.8687 1.9515 1.8154 -0.1975 -0.6693 0.1584  1447 ASP B CB  
25363 C CG  . ASP C 1447 ? 1.8969 1.9727 1.8179 -0.1748 -0.6765 0.1292  1447 ASP B CG  
25364 O OD1 . ASP C 1447 ? 1.8899 1.9585 1.7692 -0.1523 -0.6628 0.1296  1447 ASP B OD1 
25365 O OD2 . ASP C 1447 ? 1.9263 2.0032 1.8688 -0.1793 -0.6959 0.1059  1447 ASP B OD2 
25366 N N   . GLN C 1448 ? 1.7906 1.7931 1.6572 -0.1713 -0.6344 0.1868  1448 GLN B N   
25367 C CA  . GLN C 1448 ? 1.7850 1.7454 1.6390 -0.1656 -0.6354 0.1805  1448 GLN B CA  
25368 C C   . GLN C 1448 ? 1.7744 1.7057 1.6588 -0.1866 -0.6438 0.1891  1448 GLN B C   
25369 O O   . GLN C 1448 ? 1.7818 1.7130 1.6770 -0.1999 -0.6371 0.2127  1448 GLN B O   
25370 C CB  . GLN C 1448 ? 1.7827 1.7325 1.5967 -0.1493 -0.6173 0.1919  1448 GLN B CB  
25371 C CG  . GLN C 1448 ? 1.7990 1.7500 1.6086 -0.1573 -0.6043 0.2206  1448 GLN B CG  
25372 C CD  . GLN C 1448 ? 1.8174 1.7498 1.5896 -0.1426 -0.5898 0.2281  1448 GLN B CD  
25373 O OE1 . GLN C 1448 ? 1.8261 1.7304 1.5902 -0.1364 -0.5920 0.2184  1448 GLN B OE1 
25374 N NE2 . GLN C 1448 ? 1.8222 1.7704 1.5716 -0.1370 -0.5751 0.2455  1448 GLN B NE2 
25375 N N   . LEU C 1449 ? 1.7775 1.6834 1.6743 -0.1881 -0.6585 0.1696  1449 LEU B N   
25376 C CA  . LEU C 1449 ? 1.8062 1.6781 1.7280 -0.2050 -0.6670 0.1748  1449 LEU B CA  
25377 C C   . LEU C 1449 ? 1.7530 1.5925 1.6510 -0.1949 -0.6582 0.1823  1449 LEU B C   
25378 O O   . LEU C 1449 ? 1.7366 1.5568 1.6425 -0.2056 -0.6543 0.2014  1449 LEU B O   
25379 C CB  . LEU C 1449 ? 1.8907 1.7489 1.8341 -0.2094 -0.6875 0.1489  1449 LEU B CB  
25380 C CG  . LEU C 1449 ? 1.9625 1.7790 1.9282 -0.2231 -0.6991 0.1473  1449 LEU B CG  
25381 C CD1 . LEU C 1449 ? 1.9844 1.7959 1.9751 -0.2457 -0.6946 0.1743  1449 LEU B CD1 
25382 C CD2 . LEU C 1449 ? 2.0034 1.8132 1.9900 -0.2277 -0.7203 0.1201  1449 LEU B CD2 
25383 N N   . PHE C 1450 ? 1.7229 1.5576 1.5921 -0.1737 -0.6548 0.1672  1450 PHE B N   
25384 C CA  . PHE C 1450 ? 1.6909 1.5018 1.5365 -0.1625 -0.6450 0.1738  1450 PHE B CA  
25385 C C   . PHE C 1450 ? 1.6644 1.4956 1.4770 -0.1480 -0.6277 0.1822  1450 PHE B C   
25386 O O   . PHE C 1450 ? 1.6604 1.5227 1.4666 -0.1442 -0.6237 0.1810  1450 PHE B O   
25387 C CB  . PHE C 1450 ? 1.6668 1.4527 1.5066 -0.1500 -0.6535 0.1518  1450 PHE B CB  
25388 C CG  . PHE C 1450 ? 1.6726 1.4353 1.5417 -0.1630 -0.6708 0.1425  1450 PHE B CG  
25389 C CD1 . PHE C 1450 ? 1.6854 1.4598 1.5743 -0.1697 -0.6850 0.1262  1450 PHE B CD1 
25390 C CD2 . PHE C 1450 ? 1.6679 1.3970 1.5451 -0.1688 -0.6735 0.1501  1450 PHE B CD2 
25391 C CE1 . PHE C 1450 ? 1.7015 1.4513 1.6177 -0.1829 -0.7019 0.1168  1450 PHE B CE1 
25392 C CE2 . PHE C 1450 ? 1.6979 1.4021 1.6007 -0.1806 -0.6893 0.1417  1450 PHE B CE2 
25393 C CZ  . PHE C 1450 ? 1.7060 1.4195 1.6284 -0.1882 -0.7036 0.1248  1450 PHE B CZ  
25394 N N   . THR C 1451 ? 1.6371 1.4508 1.4292 -0.1401 -0.6175 0.1909  1451 THR B N   
25395 C CA  . THR C 1451 ? 1.5835 1.4114 1.3443 -0.1283 -0.6009 0.2006  1451 THR B CA  
25396 C C   . THR C 1451 ? 1.5714 1.3861 1.3090 -0.1099 -0.5959 0.1873  1451 THR B C   
25397 O O   . THR C 1451 ? 1.5496 1.3732 1.2587 -0.0971 -0.5823 0.1898  1451 THR B O   
25398 C CB  . THR C 1451 ? 1.5525 1.3726 1.3088 -0.1366 -0.5920 0.2260  1451 THR B CB  
25399 O OG1 . THR C 1451 ? 1.5369 1.3304 1.2829 -0.1308 -0.5896 0.2266  1451 THR B OG1 
25400 C CG2 . THR C 1451 ? 1.5496 1.3671 1.3371 -0.1570 -0.5999 0.2396  1451 THR B CG2 
25401 N N   . ASP C 1452 ? 1.5801 1.3727 1.3298 -0.1084 -0.6063 0.1734  1452 ASP B N   
25402 C CA  . ASP C 1452 ? 1.5683 1.3491 1.2984 -0.0908 -0.6008 0.1620  1452 ASP B CA  
25403 C C   . ASP C 1452 ? 1.6101 1.3691 1.3522 -0.0859 -0.6127 0.1443  1452 ASP B C   
25404 O O   . ASP C 1452 ? 1.6142 1.3503 1.3726 -0.0944 -0.6199 0.1488  1452 ASP B O   
25405 C CB  . ASP C 1452 ? 1.5212 1.2911 1.2367 -0.0897 -0.5888 0.1780  1452 ASP B CB  
25406 C CG  . ASP C 1452 ? 1.4647 1.2340 1.1547 -0.0715 -0.5773 0.1700  1452 ASP B CG  
25407 O OD1 . ASP C 1452 ? 1.4694 1.2205 1.1611 -0.0656 -0.5783 0.1645  1452 ASP B OD1 
25408 O OD2 . ASP C 1452 ? 1.4164 1.2040 1.0849 -0.0624 -0.5669 0.1695  1452 ASP B OD2 
25409 N N   . TYR C 1453 ? 1.6274 1.3933 1.3583 -0.0700 -0.6141 0.1245  1453 TYR B N   
25410 C CA  . TYR C 1453 ? 1.6401 1.3871 1.3759 -0.0600 -0.6240 0.1055  1453 TYR B CA  
25411 C C   . TYR C 1453 ? 1.6283 1.3698 1.3403 -0.0398 -0.6113 0.1009  1453 TYR B C   
25412 O O   . TYR C 1453 ? 1.6108 1.3655 1.3013 -0.0324 -0.5957 0.1085  1453 TYR B O   
25413 C CB  . TYR C 1453 ? 1.6485 1.4066 1.3897 -0.0554 -0.6367 0.0846  1453 TYR B CB  
25414 C CG  . TYR C 1453 ? 1.6496 1.4235 1.3633 -0.0323 -0.6281 0.0712  1453 TYR B CG  
25415 C CD1 . TYR C 1453 ? 1.6609 1.4600 1.3558 -0.0277 -0.6150 0.0790  1453 TYR B CD1 
25416 C CD2 . TYR C 1453 ? 1.6658 1.4279 1.3701 -0.0135 -0.6320 0.0517  1453 TYR B CD2 
25417 C CE1 . TYR C 1453 ? 1.6853 1.4972 1.3527 -0.0053 -0.6056 0.0681  1453 TYR B CE1 
25418 C CE2 . TYR C 1453 ? 1.6929 1.4688 1.3701 0.0093  -0.6225 0.0407  1453 TYR B CE2 
25419 C CZ  . TYR C 1453 ? 1.6791 1.4798 1.3378 0.0132  -0.6090 0.0492  1453 TYR B CZ  
25420 O OH  . TYR C 1453 ? 1.6465 1.4599 1.2760 0.0368  -0.5982 0.0397  1453 TYR B OH  
25421 N N   . GLN C 1454 ? 1.6242 1.3455 1.3405 -0.0308 -0.6177 0.0888  1454 GLN B N   
25422 C CA  . GLN C 1454 ? 1.6169 1.3340 1.3140 -0.0105 -0.6065 0.0826  1454 GLN B CA  
25423 C C   . GLN C 1454 ? 1.6112 1.3064 1.3170 -0.0012 -0.6174 0.0676  1454 GLN B C   
25424 O O   . GLN C 1454 ? 1.6231 1.2992 1.3490 -0.0128 -0.6288 0.0707  1454 GLN B O   
25425 C CB  . GLN C 1454 ? 1.6086 1.3234 1.2996 -0.0140 -0.5923 0.1011  1454 GLN B CB  
25426 C CG  . GLN C 1454 ? 1.6315 1.3304 1.3430 -0.0315 -0.5995 0.1150  1454 GLN B CG  
25427 C CD  . GLN C 1454 ? 1.6438 1.3383 1.3491 -0.0308 -0.5877 0.1286  1454 GLN B CD  
25428 O OE1 . GLN C 1454 ? 1.6321 1.3259 1.3267 -0.0161 -0.5786 0.1232  1454 GLN B OE1 
25429 N NE2 . GLN C 1454 ? 1.6534 1.3456 1.3660 -0.0465 -0.5879 0.1464  1454 GLN B NE2 
25430 N N   . ILE C 1455 ? 1.6122 1.3090 1.3014 0.0211  -0.6137 0.0516  1455 ILE B N   
25431 C CA  . ILE C 1455 ? 1.6077 1.2836 1.3010 0.0337  -0.6217 0.0382  1455 ILE B CA  
25432 C C   . ILE C 1455 ? 1.6029 1.2750 1.2865 0.0470  -0.6065 0.0443  1455 ILE B C   
25433 O O   . ILE C 1455 ? 1.5883 1.2694 1.2519 0.0670  -0.5944 0.0374  1455 ILE B O   
25434 C CB  . ILE C 1455 ? 1.7104 1.3874 1.3926 0.0525  -0.6300 0.0142  1455 ILE B CB  
25435 C CG1 . ILE C 1455 ? 1.7318 1.4082 1.4298 0.0385  -0.6498 0.0045  1455 ILE B CG1 
25436 C CG2 . ILE C 1455 ? 1.7274 1.3828 1.4080 0.0698  -0.6342 0.0023  1455 ILE B CG2 
25437 C CD1 . ILE C 1455 ? 1.7301 1.4344 1.4224 0.0324  -0.6467 0.0070  1455 ILE B CD1 
25438 N N   . LYS C 1456 ? 1.5956 1.2553 1.2938 0.0361  -0.6069 0.0574  1456 LYS B N   
25439 C CA  . LYS C 1456 ? 1.5876 1.2432 1.2828 0.0474  -0.5957 0.0620  1456 LYS B CA  
25440 C C   . LYS C 1456 ? 1.5517 1.1859 1.2576 0.0563  -0.6070 0.0522  1456 LYS B C   
25441 O O   . LYS C 1456 ? 1.5351 1.1522 1.2565 0.0452  -0.6229 0.0506  1456 LYS B O   
25442 C CB  . LYS C 1456 ? 1.6345 1.2935 1.3367 0.0323  -0.5876 0.0829  1456 LYS B CB  
25443 C CG  . LYS C 1456 ? 1.7026 1.3621 1.4034 0.0434  -0.5754 0.0873  1456 LYS B CG  
25444 C CD  . LYS C 1456 ? 1.7465 1.4106 1.4531 0.0289  -0.5683 0.1065  1456 LYS B CD  
25445 C CE  . LYS C 1456 ? 1.7615 1.4367 1.4596 0.0390  -0.5500 0.1108  1456 LYS B CE  
25446 N NZ  . LYS C 1456 ? 1.7541 1.4440 1.4297 0.0457  -0.5348 0.1094  1456 LYS B NZ  
25447 N N   . ASP C 1457 ? 1.5387 1.1733 1.2351 0.0773  -0.5977 0.0460  1457 ASP B N   
25448 C CA  . ASP C 1457 ? 1.5620 1.1780 1.2662 0.0889  -0.6051 0.0389  1457 ASP B CA  
25449 C C   . ASP C 1457 ? 1.5437 1.1363 1.2580 0.0846  -0.6268 0.0271  1457 ASP B C   
25450 O O   . ASP C 1457 ? 1.5349 1.1088 1.2634 0.0795  -0.6356 0.0310  1457 ASP B O   
25451 C CB  . ASP C 1457 ? 1.5943 1.2095 1.3113 0.0835  -0.5986 0.0547  1457 ASP B CB  
25452 C CG  . ASP C 1457 ? 1.6325 1.2671 1.3403 0.0936  -0.5777 0.0615  1457 ASP B CG  
25453 O OD1 . ASP C 1457 ? 1.6674 1.3111 1.3576 0.1105  -0.5682 0.0519  1457 ASP B OD1 
25454 O OD2 . ASP C 1457 ? 1.6292 1.2696 1.3468 0.0849  -0.5707 0.0761  1457 ASP B OD2 
25455 N N   . GLY C 1458 ? 1.5174 1.1105 1.2238 0.0875  -0.6355 0.0121  1458 GLY B N   
25456 C CA  . GLY C 1458 ? 1.4955 1.0649 1.2096 0.0861  -0.6562 -0.0025 1458 GLY B CA  
25457 C C   . GLY C 1458 ? 1.4607 1.0211 1.1952 0.0582  -0.6683 0.0068  1458 GLY B C   
25458 O O   . GLY C 1458 ? 1.4788 1.0139 1.2249 0.0528  -0.6846 0.0000  1458 GLY B O   
25459 N N   . HIS C 1459 ? 1.4239 1.0039 1.1618 0.0414  -0.6598 0.0227  1459 HIS B N   
25460 C CA  . HIS C 1459 ? 1.4263 1.0009 1.1832 0.0151  -0.6682 0.0351  1459 HIS B CA  
25461 C C   . HIS C 1459 ? 1.3815 0.9809 1.1357 0.0037  -0.6645 0.0390  1459 HIS B C   
25462 O O   . HIS C 1459 ? 1.3436 0.9647 1.0843 0.0078  -0.6489 0.0472  1459 HIS B O   
25463 C CB  . HIS C 1459 ? 1.4498 1.0215 1.2153 0.0051  -0.6604 0.0570  1459 HIS B CB  
25464 C CG  . HIS C 1459 ? 1.5163 1.0652 1.2872 0.0145  -0.6643 0.0563  1459 HIS B CG  
25465 N ND1 . HIS C 1459 ? 1.5552 1.0764 1.3412 0.0053  -0.6785 0.0574  1459 HIS B ND1 
25466 C CD2 . HIS C 1459 ? 1.5334 1.0838 1.2969 0.0327  -0.6551 0.0557  1459 HIS B CD2 
25467 C CE1 . HIS C 1459 ? 1.5675 1.0740 1.3533 0.0188  -0.6784 0.0568  1459 HIS B CE1 
25468 N NE2 . HIS C 1459 ? 1.5507 1.0761 1.3242 0.0353  -0.6644 0.0558  1459 HIS B NE2 
25469 N N   . VAL C 1460 ? 1.4133 1.0097 1.1805 -0.0106 -0.6786 0.0334  1460 VAL B N   
25470 C CA  . VAL C 1460 ? 1.4372 1.0584 1.2067 -0.0250 -0.6753 0.0415  1460 VAL B CA  
25471 C C   . VAL C 1460 ? 1.4836 1.1026 1.2671 -0.0458 -0.6713 0.0655  1460 VAL B C   
25472 O O   . VAL C 1460 ? 1.5203 1.1151 1.3206 -0.0563 -0.6807 0.0706  1460 VAL B O   
25473 C CB  . VAL C 1460 ? 1.4459 1.0685 1.2275 -0.0338 -0.6921 0.0268  1460 VAL B CB  
25474 C CG1 . VAL C 1460 ? 1.4290 1.0754 1.2205 -0.0534 -0.6895 0.0403  1460 VAL B CG1 
25475 C CG2 . VAL C 1460 ? 1.4606 1.0922 1.2237 -0.0116 -0.6946 0.0035  1460 VAL B CG2 
25476 N N   . ILE C 1461 ? 1.4672 1.1093 1.2419 -0.0505 -0.6576 0.0805  1461 ILE B N   
25477 C CA  . ILE C 1461 ? 1.4342 1.0747 1.2163 -0.0657 -0.6514 0.1041  1461 ILE B CA  
25478 C C   . ILE C 1461 ? 1.4392 1.1027 1.2220 -0.0798 -0.6461 0.1174  1461 ILE B C   
25479 O O   . ILE C 1461 ? 1.4079 1.0928 1.1722 -0.0734 -0.6329 0.1220  1461 ILE B O   
25480 C CB  . ILE C 1461 ? 1.3712 1.0117 1.1391 -0.0550 -0.6376 0.1127  1461 ILE B CB  
25481 C CG1 . ILE C 1461 ? 1.3699 0.9843 1.1474 -0.0507 -0.6442 0.1111  1461 ILE B CG1 
25482 C CG2 . ILE C 1461 ? 1.3297 0.9814 1.0947 -0.0668 -0.6275 0.1346  1461 ILE B CG2 
25483 C CD1 . ILE C 1461 ? 1.3592 0.9758 1.1242 -0.0347 -0.6327 0.1115  1461 ILE B CD1 
25484 N N   . LEU C 1462 ? 1.4622 1.1199 1.2665 -0.0987 -0.6559 0.1245  1462 LEU B N   
25485 C CA  . LEU C 1462 ? 1.4440 1.1240 1.2535 -0.1128 -0.6527 0.1369  1462 LEU B CA  
25486 C C   . LEU C 1462 ? 1.4893 1.1667 1.3014 -0.1248 -0.6449 0.1625  1462 LEU B C   
25487 O O   . LEU C 1462 ? 1.5007 1.1550 1.3195 -0.1276 -0.6474 0.1698  1462 LEU B O   
25488 C CB  . LEU C 1462 ? 1.3757 1.0555 1.2091 -0.1261 -0.6680 0.1278  1462 LEU B CB  
25489 C CG  . LEU C 1462 ? 1.2053 0.8928 1.0325 -0.1127 -0.6758 0.1018  1462 LEU B CG  
25490 C CD1 . LEU C 1462 ? 1.2132 0.9018 1.0654 -0.1272 -0.6922 0.0919  1462 LEU B CD1 
25491 C CD2 . LEU C 1462 ? 1.1557 0.8742 0.9598 -0.1005 -0.6629 0.1012  1462 LEU B CD2 
25492 N N   . GLN C 1463 ? 1.4805 1.1819 1.2856 -0.1303 -0.6355 0.1758  1463 GLN B N   
25493 C CA  . GLN C 1463 ? 1.4567 1.1579 1.2592 -0.1390 -0.6271 0.1999  1463 GLN B CA  
25494 C C   . GLN C 1463 ? 1.4224 1.1470 1.2322 -0.1515 -0.6246 0.2118  1463 GLN B C   
25495 O O   . GLN C 1463 ? 1.3902 1.1401 1.1894 -0.1458 -0.6201 0.2055  1463 GLN B O   
25496 C CB  . GLN C 1463 ? 1.4765 1.1844 1.2510 -0.1259 -0.6128 0.2049  1463 GLN B CB  
25497 C CG  . GLN C 1463 ? 1.5017 1.1887 1.2704 -0.1172 -0.6116 0.2038  1463 GLN B CG  
25498 C CD  . GLN C 1463 ? 1.5194 1.2157 1.2632 -0.1085 -0.5971 0.2117  1463 GLN B CD  
25499 O OE1 . GLN C 1463 ? 1.5192 1.2051 1.2570 -0.1006 -0.5942 0.2101  1463 GLN B OE1 
25500 N NE2 . GLN C 1463 ? 1.5307 1.2470 1.2605 -0.1103 -0.5882 0.2202  1463 GLN B NE2 
25501 N N   . LEU C 1464 ? 1.4273 1.1443 1.2546 -0.1674 -0.6268 0.2297  1464 LEU B N   
25502 C CA  . LEU C 1464 ? 1.4304 1.1704 1.2643 -0.1790 -0.6218 0.2460  1464 LEU B CA  
25503 C C   . LEU C 1464 ? 1.4601 1.1899 1.2939 -0.1869 -0.6156 0.2717  1464 LEU B C   
25504 O O   . LEU C 1464 ? 1.4521 1.1559 1.2851 -0.1853 -0.6176 0.2758  1464 LEU B O   
25505 C CB  . LEU C 1464 ? 1.4221 1.1697 1.2864 -0.1936 -0.6332 0.2397  1464 LEU B CB  
25506 C CG  . LEU C 1464 ? 1.4240 1.1476 1.3119 -0.1996 -0.6497 0.2224  1464 LEU B CG  
25507 C CD1 . LEU C 1464 ? 1.4254 1.1121 1.3102 -0.1942 -0.6535 0.2203  1464 LEU B CD1 
25508 C CD2 . LEU C 1464 ? 1.4343 1.1600 1.3556 -0.2214 -0.6571 0.2306  1464 LEU B CD2 
25509 N N   . ASN C 1465 ? 1.5113 1.2625 1.3448 -0.1938 -0.6078 0.2892  1465 ASN B N   
25510 C CA  . ASN C 1465 ? 1.5600 1.3040 1.3892 -0.1988 -0.6005 0.3149  1465 ASN B CA  
25511 C C   . ASN C 1465 ? 1.5952 1.3177 1.4520 -0.2141 -0.6073 0.3271  1465 ASN B C   
25512 O O   . ASN C 1465 ? 1.5989 1.3099 1.4501 -0.2156 -0.6020 0.3473  1465 ASN B O   
25513 C CB  . ASN C 1465 ? 1.5773 1.3511 1.3949 -0.1992 -0.5887 0.3312  1465 ASN B CB  
25514 C CG  . ASN C 1465 ? 1.5619 1.3595 1.3565 -0.1860 -0.5825 0.3186  1465 ASN B CG  
25515 O OD1 . ASN C 1465 ? 1.5374 1.3396 1.3020 -0.1751 -0.5717 0.3257  1465 ASN B OD1 
25516 N ND2 . ASN C 1465 ? 1.5688 1.3805 1.3759 -0.1864 -0.5896 0.2996  1465 ASN B ND2 
25517 N N   . SER C 1466 ? 1.6496 1.3656 1.5346 -0.2247 -0.6188 0.3151  1466 SER B N   
25518 C CA  . SER C 1466 ? 1.6929 1.3876 1.6057 -0.2408 -0.6248 0.3265  1466 SER B CA  
25519 C C   . SER C 1466 ? 1.7075 1.3878 1.6465 -0.2493 -0.6400 0.3061  1466 SER B C   
25520 O O   . SER C 1466 ? 1.6692 1.3652 1.6093 -0.2456 -0.6457 0.2851  1466 SER B O   
25521 C CB  . SER C 1466 ? 1.7423 1.4585 1.6692 -0.2543 -0.6173 0.3490  1466 SER B CB  
25522 O OG  . SER C 1466 ? 1.7923 1.4891 1.7505 -0.2717 -0.6233 0.3580  1466 SER B OG  
25523 N N   . ILE C 1467 ? 1.7318 1.3815 1.6907 -0.2601 -0.6465 0.3124  1467 ILE B N   
25524 C CA  . ILE C 1467 ? 1.7545 1.3871 1.7393 -0.2702 -0.6614 0.2945  1467 ILE B CA  
25525 C C   . ILE C 1467 ? 1.8357 1.4582 1.8530 -0.2926 -0.6634 0.3109  1467 ILE B C   
25526 O O   . ILE C 1467 ? 1.8859 1.4723 1.9164 -0.2990 -0.6707 0.3111  1467 ILE B O   
25527 C CB  . ILE C 1467 ? 1.7266 1.3229 1.7031 -0.2593 -0.6701 0.2794  1467 ILE B CB  
25528 C CG1 . ILE C 1467 ? 1.6307 1.2374 1.5775 -0.2377 -0.6668 0.2645  1467 ILE B CG1 
25529 C CG2 . ILE C 1467 ? 1.7570 1.3350 1.7566 -0.2678 -0.6862 0.2585  1467 ILE B CG2 
25530 C CD1 . ILE C 1467 ? 1.6126 1.1891 1.5544 -0.2264 -0.6762 0.2465  1467 ILE B CD1 
25531 N N   . PRO C 1468 ? 1.8160 1.4708 1.8468 -0.3042 -0.6566 0.3246  1468 PRO B N   
25532 C CA  . PRO C 1468 ? 1.8465 1.5000 1.9078 -0.3255 -0.6538 0.3461  1468 PRO B CA  
25533 C C   . PRO C 1468 ? 1.8763 1.4857 1.9600 -0.3378 -0.6639 0.3447  1468 PRO B C   
25534 O O   . PRO C 1468 ? 1.8626 1.4521 1.9510 -0.3362 -0.6780 0.3198  1468 PRO B O   
25535 C CB  . PRO C 1468 ? 1.8165 1.5077 1.9014 -0.3375 -0.6582 0.3364  1468 PRO B CB  
25536 C CG  . PRO C 1468 ? 1.7839 1.5069 1.8389 -0.3186 -0.6532 0.3254  1468 PRO B CG  
25537 C CD  . PRO C 1468 ? 1.7926 1.4900 1.8140 -0.2979 -0.6531 0.3154  1468 PRO B CD  
25538 N N   . SER C 1469 ? 1.9201 1.5129 2.0156 -0.3485 -0.6563 0.3711  1469 SER B N   
25539 C CA  . SER C 1469 ? 1.9738 1.5234 2.0909 -0.3611 -0.6645 0.3721  1469 SER B CA  
25540 C C   . SER C 1469 ? 2.0069 1.5659 2.1659 -0.3868 -0.6697 0.3729  1469 SER B C   
25541 O O   . SER C 1469 ? 2.0734 1.5991 2.2551 -0.4001 -0.6804 0.3654  1469 SER B O   
25542 C CB  . SER C 1469 ? 1.9911 1.5147 2.0984 -0.3583 -0.6534 0.4004  1469 SER B CB  
25543 O OG  . SER C 1469 ? 1.9874 1.5036 2.0578 -0.3350 -0.6503 0.3979  1469 SER B OG  
25544 N N   . SER C 1470 ? 1.9708 1.5755 2.1403 -0.3938 -0.6621 0.3818  1470 SER B N   
25545 C CA  . SER C 1470 ? 1.9688 1.5917 2.1814 -0.4190 -0.6666 0.3828  1470 SER B CA  
25546 C C   . SER C 1470 ? 1.9637 1.5657 2.1967 -0.4283 -0.6875 0.3519  1470 SER B C   
25547 O O   . SER C 1470 ? 1.9902 1.5721 2.2585 -0.4506 -0.6946 0.3533  1470 SER B O   
25548 C CB  . SER C 1470 ? 1.9707 1.6522 2.1851 -0.4182 -0.6602 0.3844  1470 SER B CB  
25549 O OG  . SER C 1470 ? 1.9663 1.6650 2.1540 -0.3991 -0.6666 0.3584  1470 SER B OG  
25550 N N   . ASP C 1471 ? 1.9180 1.5238 2.1274 -0.4104 -0.6969 0.3241  1471 ASP B N   
25551 C CA  . ASP C 1471 ? 1.9326 1.5199 2.1540 -0.4139 -0.7172 0.2920  1471 ASP B CA  
25552 C C   . ASP C 1471 ? 1.8195 1.3970 2.0021 -0.3867 -0.7216 0.2701  1471 ASP B C   
25553 O O   . ASP C 1471 ? 1.7799 1.3503 1.9319 -0.3693 -0.7105 0.2816  1471 ASP B O   
25554 C CB  . ASP C 1471 ? 2.0020 1.6293 2.2533 -0.4289 -0.7265 0.2777  1471 ASP B CB  
25555 C CG  . ASP C 1471 ? 2.0180 1.7009 2.2526 -0.4164 -0.7165 0.2802  1471 ASP B CG  
25556 O OD1 . ASP C 1471 ? 2.0404 1.7632 2.3021 -0.4308 -0.7166 0.2833  1471 ASP B OD1 
25557 O OD2 . ASP C 1471 ? 2.0113 1.6980 2.2063 -0.3923 -0.7086 0.2789  1471 ASP B OD2 
25558 N N   . PHE C 1472 ? 1.7720 1.3489 1.9565 -0.3828 -0.7379 0.2386  1472 PHE B N   
25559 C CA  . PHE C 1472 ? 1.7034 1.2731 1.8530 -0.3568 -0.7417 0.2173  1472 PHE B CA  
25560 C C   . PHE C 1472 ? 1.6448 1.2616 1.7743 -0.3418 -0.7356 0.2098  1472 PHE B C   
25561 O O   . PHE C 1472 ? 1.6252 1.2825 1.7698 -0.3515 -0.7326 0.2147  1472 PHE B O   
25562 C CB  . PHE C 1472 ? 1.7075 1.2482 1.8642 -0.3563 -0.7621 0.1865  1472 PHE B CB  
25563 C CG  . PHE C 1472 ? 1.7415 1.2276 1.8973 -0.3569 -0.7667 0.1886  1472 PHE B CG  
25564 C CD1 . PHE C 1472 ? 1.7893 1.2510 1.9712 -0.3785 -0.7648 0.2088  1472 PHE B CD1 
25565 C CD2 . PHE C 1472 ? 1.7502 1.2091 1.8784 -0.3347 -0.7717 0.1718  1472 PHE B CD2 
25566 C CE1 . PHE C 1472 ? 1.8364 1.2448 2.0154 -0.3776 -0.7685 0.2115  1472 PHE B CE1 
25567 C CE2 . PHE C 1472 ? 1.7918 1.1997 1.9178 -0.3333 -0.7759 0.1741  1472 PHE B CE2 
25568 C CZ  . PHE C 1472 ? 1.8314 1.2131 1.9818 -0.3544 -0.7745 0.1937  1472 PHE B CZ  
25569 N N   . LEU C 1473 ? 1.6306 1.2415 1.7257 -0.3173 -0.7337 0.1976  1473 LEU B N   
25570 C CA  . LEU C 1473 ? 1.5990 1.2483 1.6713 -0.3005 -0.7282 0.1879  1473 LEU B CA  
25571 C C   . LEU C 1473 ? 1.6475 1.2816 1.7028 -0.2824 -0.7401 0.1572  1473 LEU B C   
25572 O O   . LEU C 1473 ? 1.6500 1.2494 1.6901 -0.2709 -0.7413 0.1534  1473 LEU B O   
25573 C CB  . LEU C 1473 ? 1.5492 1.2094 1.5926 -0.2872 -0.7092 0.2089  1473 LEU B CB  
25574 C CG  . LEU C 1473 ? 1.5165 1.2131 1.5331 -0.2689 -0.7016 0.2004  1473 LEU B CG  
25575 C CD1 . LEU C 1473 ? 1.4993 1.2262 1.5077 -0.2707 -0.6845 0.2261  1473 LEU B CD1 
25576 C CD2 . LEU C 1473 ? 1.5050 1.1845 1.4892 -0.2450 -0.6999 0.1868  1473 LEU B CD2 
25577 N N   . CYS C 1474 ? 1.6450 1.3063 1.7026 -0.2787 -0.7487 0.1358  1474 CYS B N   
25578 C CA  . CYS C 1474 ? 1.6208 1.2680 1.6655 -0.2626 -0.7623 0.1047  1474 CYS B CA  
25579 C C   . CYS C 1474 ? 1.6301 1.3078 1.6448 -0.2389 -0.7565 0.0914  1474 CYS B C   
25580 O O   . CYS C 1474 ? 1.6309 1.3488 1.6475 -0.2405 -0.7525 0.0931  1474 CYS B O   
25581 C CB  . CYS C 1474 ? 1.6041 1.2440 1.6795 -0.2789 -0.7830 0.0855  1474 CYS B CB  
25582 S SG  . CYS C 1474 ? 1.7697 1.3486 1.8617 -0.2916 -0.7933 0.0873  1474 CYS B SG  
25583 N N   . VAL C 1475 ? 1.6432 1.3018 1.6295 -0.2163 -0.7546 0.0801  1475 VAL B N   
25584 C CA  . VAL C 1475 ? 1.6459 1.3261 1.6042 -0.1922 -0.7517 0.0625  1475 VAL B CA  
25585 C C   . VAL C 1475 ? 1.7110 1.3756 1.6745 -0.1867 -0.7719 0.0321  1475 VAL B C   
25586 O O   . VAL C 1475 ? 1.7317 1.3581 1.7074 -0.1933 -0.7836 0.0261  1475 VAL B O   
25587 C CB  . VAL C 1475 ? 1.6042 1.2719 1.5299 -0.1697 -0.7382 0.0663  1475 VAL B CB  
25588 C CG1 . VAL C 1475 ? 1.6240 1.2477 1.5531 -0.1693 -0.7444 0.0651  1475 VAL B CG1 
25589 C CG2 . VAL C 1475 ? 1.5853 1.2667 1.4840 -0.1441 -0.7376 0.0444  1475 VAL B CG2 
25590 N N   . ARG C 1476 ? 1.7058 1.3987 1.6588 -0.1741 -0.7764 0.0129  1476 ARG B N   
25591 C CA  . ARG C 1476 ? 1.7159 1.3948 1.6635 -0.1610 -0.7942 -0.0185 1476 ARG B CA  
25592 C C   . ARG C 1476 ? 1.6366 1.3365 1.5482 -0.1306 -0.7864 -0.0321 1476 ARG B C   
25593 O O   . ARG C 1476 ? 1.5788 1.3125 1.4770 -0.1247 -0.7716 -0.0211 1476 ARG B O   
25594 C CB  . ARG C 1476 ? 1.7733 1.4596 1.7532 -0.1805 -0.8152 -0.0335 1476 ARG B CB  
25595 C CG  . ARG C 1476 ? 1.8179 1.5497 1.8173 -0.1967 -0.8112 -0.0216 1476 ARG B CG  
25596 C CD  . ARG C 1476 ? 1.8994 1.6266 1.9352 -0.2286 -0.8098 0.0024  1476 ARG B CD  
25597 N NE  . ARG C 1476 ? 1.9527 1.7200 1.9885 -0.2337 -0.7921 0.0265  1476 ARG B NE  
25598 C CZ  . ARG C 1476 ? 2.0128 1.7907 2.0769 -0.2583 -0.7867 0.0504  1476 ARG B CZ  
25599 N NH1 . ARG C 1476 ? 2.0513 1.8024 2.1492 -0.2827 -0.7972 0.0546  1476 ARG B NH1 
25600 N NH2 . ARG C 1476 ? 2.0001 1.8150 2.0573 -0.2575 -0.7698 0.0707  1476 ARG B NH2 
25601 N N   . PHE C 1477 ? 1.6349 1.3121 1.5289 -0.1101 -0.7951 -0.0548 1477 PHE B N   
25602 C CA  . PHE C 1477 ? 1.6060 1.2980 1.4643 -0.0790 -0.7871 -0.0680 1477 PHE B CA  
25603 C C   . PHE C 1477 ? 1.6351 1.2994 1.4801 -0.0591 -0.8019 -0.0960 1477 PHE B C   
25604 O O   . PHE C 1477 ? 1.6653 1.2919 1.5215 -0.0655 -0.8129 -0.1004 1477 PHE B O   
25605 C CB  . PHE C 1477 ? 1.5669 1.2617 1.4016 -0.0669 -0.7625 -0.0472 1477 PHE B CB  
25606 C CG  . PHE C 1477 ? 1.5741 1.2306 1.4049 -0.0626 -0.7595 -0.0417 1477 PHE B CG  
25607 C CD1 . PHE C 1477 ? 1.5825 1.2240 1.3880 -0.0357 -0.7567 -0.0552 1477 PHE B CD1 
25608 C CD2 . PHE C 1477 ? 1.5839 1.2211 1.4360 -0.0841 -0.7589 -0.0222 1477 PHE B CD2 
25609 C CE1 . PHE C 1477 ? 1.5856 1.1953 1.3888 -0.0310 -0.7541 -0.0499 1477 PHE B CE1 
25610 C CE2 . PHE C 1477 ? 1.5968 1.2014 1.4450 -0.0788 -0.7566 -0.0173 1477 PHE B CE2 
25611 C CZ  . PHE C 1477 ? 1.5998 1.1913 1.4242 -0.0524 -0.7544 -0.0313 1477 PHE B CZ  
25612 N N   . ARG C 1478 ? 1.6110 1.2930 1.4302 -0.0335 -0.8020 -0.1147 1478 ARG B N   
25613 C CA  . ARG C 1478 ? 1.6308 1.2904 1.4370 -0.0139 -0.8182 -0.1434 1478 ARG B CA  
25614 C C   . ARG C 1478 ? 1.6288 1.2721 1.4025 0.0153  -0.8042 -0.1441 1478 ARG B C   
25615 O O   . ARG C 1478 ? 1.5541 1.2140 1.3112 0.0241  -0.7820 -0.1269 1478 ARG B O   
25616 C CB  . ARG C 1478 ? 1.6504 1.3394 1.4489 -0.0026 -0.8295 -0.1659 1478 ARG B CB  
25617 C CG  . ARG C 1478 ? 1.6583 1.3771 1.4878 -0.0295 -0.8382 -0.1615 1478 ARG B CG  
25618 C CD  . ARG C 1478 ? 1.6916 1.4406 1.5118 -0.0151 -0.8508 -0.1862 1478 ARG B CD  
25619 N NE  . ARG C 1478 ? 1.6686 1.4569 1.4648 0.0014  -0.8317 -0.1770 1478 ARG B NE  
25620 C CZ  . ARG C 1478 ? 1.6733 1.5019 1.4832 -0.0107 -0.8308 -0.1702 1478 ARG B CZ  
25621 N NH1 . ARG C 1478 ? 1.7108 1.5473 1.5606 -0.0401 -0.8479 -0.1717 1478 ARG B NH1 
25622 N NH2 . ARG C 1478 ? 1.6448 1.5055 1.4290 0.0066  -0.8125 -0.1618 1478 ARG B NH2 
25623 N N   . ILE C 1479 ? 1.7294 1.3408 1.4938 0.0307  -0.8173 -0.1645 1479 ILE B N   
25624 C CA  . ILE C 1479 ? 1.8022 1.3938 1.5401 0.0572  -0.8052 -0.1644 1479 ILE B CA  
25625 C C   . ILE C 1479 ? 1.8907 1.4705 1.6023 0.0887  -0.8159 -0.1935 1479 ILE B C   
25626 O O   . ILE C 1479 ? 1.9479 1.5083 1.6679 0.0857  -0.8394 -0.2151 1479 ILE B O   
25627 C CB  . ILE C 1479 ? 1.8430 1.3968 1.5963 0.0448  -0.8071 -0.1532 1479 ILE B CB  
25628 C CG1 . ILE C 1479 ? 1.8758 1.3979 1.6474 0.0327  -0.8338 -0.1720 1479 ILE B CG1 
25629 C CG2 . ILE C 1479 ? 1.8254 1.3885 1.6003 0.0176  -0.7950 -0.1234 1479 ILE B CG2 
25630 C CD1 . ILE C 1479 ? 1.8916 1.3789 1.6839 0.0134  -0.8365 -0.1576 1479 ILE B CD1 
25631 N N   . PHE C 1480 ? 1.9277 1.5179 1.6073 0.1190  -0.7985 -0.1939 1480 PHE B N   
25632 C CA  . PHE C 1480 ? 2.0070 1.5880 1.6580 0.1526  -0.8064 -0.2202 1480 PHE B CA  
25633 C C   . PHE C 1480 ? 2.0162 1.5687 1.6486 0.1764  -0.7983 -0.2208 1480 PHE B C   
25634 O O   . PHE C 1480 ? 1.9880 1.5488 1.6087 0.1871  -0.7748 -0.2032 1480 PHE B O   
25635 C CB  . PHE C 1480 ? 2.4076 2.0244 2.0321 0.1750  -0.7977 -0.2284 1480 PHE B CB  
25636 C CG  . PHE C 1480 ? 2.4245 2.0757 2.0498 0.1651  -0.7749 -0.2038 1480 PHE B CG  
25637 C CD1 . PHE C 1480 ? 2.3918 2.0421 2.0125 0.1655  -0.7504 -0.1792 1480 PHE B CD1 
25638 C CD2 . PHE C 1480 ? 2.4338 2.1189 2.0628 0.1571  -0.7785 -0.2064 1480 PHE B CD2 
25639 C CE1 . PHE C 1480 ? 2.3476 2.0267 1.9666 0.1571  -0.7303 -0.1579 1480 PHE B CE1 
25640 C CE2 . PHE C 1480 ? 2.3828 2.0979 2.0093 0.1500  -0.7576 -0.1842 1480 PHE B CE2 
25641 C CZ  . PHE C 1480 ? 2.3410 2.0514 1.9617 0.1499  -0.7337 -0.1602 1480 PHE B CZ  
25642 N N   . GLU C 1481 ? 2.0335 1.5530 1.6633 0.1853  -0.8185 -0.2420 1481 GLU B N   
25643 C CA  . GLU C 1481 ? 2.0320 1.5225 1.6445 0.2094  -0.8136 -0.2448 1481 GLU B CA  
25644 C C   . GLU C 1481 ? 2.0116 1.5209 1.5906 0.2445  -0.7911 -0.2428 1481 GLU B C   
25645 O O   . GLU C 1481 ? 2.0469 1.5526 1.5985 0.2749  -0.7966 -0.2643 1481 GLU B O   
25646 C CB  . GLU C 1481 ? 2.0764 1.5306 1.6836 0.2194  -0.8407 -0.2735 1481 GLU B CB  
25647 C CG  . GLU C 1481 ? 2.5053 1.9284 2.1451 0.1867  -0.8617 -0.2740 1481 GLU B CG  
25648 C CD  . GLU C 1481 ? 2.5406 1.9206 2.1717 0.1989  -0.8870 -0.3018 1481 GLU B CD  
25649 O OE1 . GLU C 1481 ? 2.5511 1.9236 2.1498 0.2347  -0.8883 -0.3203 1481 GLU B OE1 
25650 O OE2 . GLU C 1481 ? 2.5530 1.9051 2.2090 0.1731  -0.9054 -0.3049 1481 GLU B OE2 
25651 N N   . LEU C 1482 ? 1.9492 1.4770 1.5299 0.2407  -0.7656 -0.2171 1482 LEU B N   
25652 C CA  . LEU C 1482 ? 1.9148 1.4614 1.4664 0.2709  -0.7420 -0.2127 1482 LEU B CA  
25653 C C   . LEU C 1482 ? 1.8971 1.4219 1.4234 0.3069  -0.7427 -0.2280 1482 LEU B C   
25654 O O   . LEU C 1482 ? 1.9048 1.4414 1.4012 0.3378  -0.7344 -0.2385 1482 LEU B O   
25655 C CB  . LEU C 1482 ? 1.8927 1.4550 1.4532 0.2598  -0.7160 -0.1827 1482 LEU B CB  
25656 C CG  . LEU C 1482 ? 1.8978 1.4751 1.4320 0.2892  -0.6895 -0.1754 1482 LEU B CG  
25657 C CD1 . LEU C 1482 ? 1.8619 1.4674 1.4001 0.2753  -0.6670 -0.1517 1482 LEU B CD1 
25658 C CD2 . LEU C 1482 ? 1.9233 1.4798 1.4555 0.3053  -0.6823 -0.1712 1482 LEU B CD2 
25659 N N   . PHE C 1483 ? 1.8810 1.3740 1.4179 0.3041  -0.7517 -0.2287 1483 PHE B N   
25660 C CA  . PHE C 1483 ? 1.8790 1.3473 1.3927 0.3376  -0.7563 -0.2454 1483 PHE B CA  
25661 C C   . PHE C 1483 ? 1.9485 1.3757 1.4754 0.3282  -0.7797 -0.2561 1483 PHE B C   
25662 O O   . PHE C 1483 ? 1.9383 1.3556 1.4939 0.2948  -0.7917 -0.2498 1483 PHE B O   
25663 C CB  . PHE C 1483 ? 1.8184 1.2957 1.3177 0.3617  -0.7286 -0.2296 1483 PHE B CB  
25664 C CG  . PHE C 1483 ? 1.7569 1.2370 1.2817 0.3398  -0.7144 -0.2022 1483 PHE B CG  
25665 C CD1 . PHE C 1483 ? 1.7343 1.1961 1.2880 0.3083  -0.7287 -0.1956 1483 PHE B CD1 
25666 C CD2 . PHE C 1483 ? 1.7031 1.2030 1.2226 0.3515  -0.6867 -0.1833 1483 PHE B CD2 
25667 C CE1 . PHE C 1483 ? 1.6774 1.1416 1.2524 0.2905  -0.7165 -0.1712 1483 PHE B CE1 
25668 C CE2 . PHE C 1483 ? 1.6656 1.1686 1.2084 0.3322  -0.6755 -0.1599 1483 PHE B CE2 
25669 C CZ  . PHE C 1483 ? 1.6448 1.1302 1.2145 0.3023  -0.6908 -0.1541 1483 PHE B CZ  
25670 N N   . GLU C 1484 ? 2.0105 1.4124 1.5150 0.3588  -0.7861 -0.2727 1484 GLU B N   
25671 C CA  . GLU C 1484 ? 2.1134 1.4731 1.6250 0.3532  -0.8108 -0.2874 1484 GLU B CA  
25672 C C   . GLU C 1484 ? 2.0983 1.4409 1.6223 0.3496  -0.8006 -0.2681 1484 GLU B C   
25673 O O   . GLU C 1484 ? 2.1021 1.4461 1.6088 0.3780  -0.7844 -0.2630 1484 GLU B O   
25674 C CB  . GLU C 1484 ? 2.2431 1.5815 1.7213 0.3895  -0.8252 -0.3173 1484 GLU B CB  
25675 C CG  . GLU C 1484 ? 2.3336 1.6950 1.7925 0.4021  -0.8316 -0.3365 1484 GLU B CG  
25676 C CD  . GLU C 1484 ? 2.3677 1.7673 1.8061 0.4250  -0.8027 -0.3241 1484 GLU B CD  
25677 O OE1 . GLU C 1484 ? 2.3629 1.7716 1.8050 0.4285  -0.7781 -0.3005 1484 GLU B OE1 
25678 O OE2 . GLU C 1484 ? 2.3802 1.8005 1.7991 0.4394  -0.8045 -0.3377 1484 GLU B OE2 
25679 N N   . VAL C 1485 ? 2.0719 1.4008 1.6264 0.3152  -0.8088 -0.2562 1485 VAL B N   
25680 C CA  . VAL C 1485 ? 2.0354 1.3466 1.6021 0.3115  -0.8013 -0.2384 1485 VAL B CA  
25681 C C   . VAL C 1485 ? 2.0142 1.2769 1.5789 0.3144  -0.8244 -0.2549 1485 VAL B C   
25682 O O   . VAL C 1485 ? 2.0455 1.2888 1.6136 0.3022  -0.8475 -0.2739 1485 VAL B O   
25683 C CB  . VAL C 1485 ? 2.2401 1.5651 1.8396 0.2744  -0.7928 -0.2111 1485 VAL B CB  
25684 C CG1 . VAL C 1485 ? 2.1807 1.5508 1.7810 0.2727  -0.7675 -0.1920 1485 VAL B CG1 
25685 C CG2 . VAL C 1485 ? 2.2604 1.5734 1.8823 0.2402  -0.8132 -0.2160 1485 VAL B CG2 
25686 N N   . GLY C 1486 ? 2.0125 1.2563 1.5727 0.3301  -0.8176 -0.2469 1486 GLY B N   
25687 C CA  . GLY C 1486 ? 2.0298 1.2247 1.5827 0.3394  -0.8362 -0.2610 1486 GLY B CA  
25688 C C   . GLY C 1486 ? 2.0341 1.2028 1.6153 0.3025  -0.8514 -0.2546 1486 GLY B C   
25689 O O   . GLY C 1486 ? 2.0376 1.2199 1.6390 0.2720  -0.8570 -0.2517 1486 GLY B O   
25690 N N   . PHE C 1487 ? 2.0133 1.1440 1.5956 0.3059  -0.8577 -0.2521 1487 PHE B N   
25691 C CA  . PHE C 1487 ? 2.0244 1.1288 1.6327 0.2720  -0.8693 -0.2430 1487 PHE B CA  
25692 C C   . PHE C 1487 ? 1.9391 1.0822 1.5717 0.2487  -0.8497 -0.2135 1487 PHE B C   
25693 O O   . PHE C 1487 ? 1.9151 1.0742 1.5473 0.2599  -0.8311 -0.1952 1487 PHE B O   
25694 C CB  . PHE C 1487 ? 2.1103 1.1718 1.7120 0.2850  -0.8738 -0.2411 1487 PHE B CB  
25695 C CG  . PHE C 1487 ? 2.1695 1.2164 1.7374 0.3285  -0.8739 -0.2579 1487 PHE B CG  
25696 C CD1 . PHE C 1487 ? 2.2433 1.2369 1.7946 0.3426  -0.8930 -0.2767 1487 PHE B CD1 
25697 C CD2 . PHE C 1487 ? 2.1465 1.2315 1.6985 0.3560  -0.8540 -0.2543 1487 PHE B CD2 
25698 C CE1 . PHE C 1487 ? 2.2733 1.2532 1.7917 0.3846  -0.8926 -0.2916 1487 PHE B CE1 
25699 C CE2 . PHE C 1487 ? 2.1789 1.2514 1.6998 0.3973  -0.8527 -0.2682 1487 PHE B CE2 
25700 C CZ  . PHE C 1487 ? 2.2402 1.2607 1.7437 0.4123  -0.8721 -0.2870 1487 PHE B CZ  
25701 N N   . LEU C 1488 ? 1.8938 1.0544 1.5471 0.2172  -0.8534 -0.2090 1488 LEU B N   
25702 C CA  . LEU C 1488 ? 1.8417 1.0409 1.5139 0.1978  -0.8341 -0.1820 1488 LEU B CA  
25703 C C   . LEU C 1488 ? 1.8492 1.0278 1.5458 0.1705  -0.8369 -0.1630 1488 LEU B C   
25704 O O   . LEU C 1488 ? 1.9012 1.0441 1.6073 0.1542  -0.8557 -0.1717 1488 LEU B O   
25705 C CB  . LEU C 1488 ? 1.7965 1.0343 1.4750 0.1828  -0.8312 -0.1834 1488 LEU B CB  
25706 C CG  . LEU C 1488 ? 1.7952 1.0367 1.4965 0.1482  -0.8440 -0.1846 1488 LEU B CG  
25707 C CD1 . LEU C 1488 ? 1.7922 1.0091 1.5208 0.1168  -0.8506 -0.1686 1488 LEU B CD1 
25708 C CD2 . LEU C 1488 ? 1.7466 1.0387 1.4516 0.1400  -0.8283 -0.1735 1488 LEU B CD2 
25709 N N   . SER C 1489 ? 1.7901 0.9896 1.4958 0.1670  -0.8184 -0.1376 1489 SER B N   
25710 C CA  . SER C 1489 ? 1.7231 0.9116 1.4518 0.1406  -0.8176 -0.1157 1489 SER B CA  
25711 C C   . SER C 1489 ? 1.6922 0.9153 1.4397 0.1117  -0.8107 -0.1015 1489 SER B C   
25712 O O   . SER C 1489 ? 1.6673 0.9274 1.4080 0.1168  -0.8010 -0.1039 1489 SER B O   
25713 C CB  . SER C 1489 ? 1.6778 0.8706 1.4050 0.1542  -0.8029 -0.0972 1489 SER B CB  
25714 O OG  . SER C 1489 ? 1.6173 0.8514 1.3561 0.1418  -0.7851 -0.0757 1489 SER B OG  
25715 N N   . PRO C 1490 ? 1.6516 0.8618 1.4212 0.0825  -0.8152 -0.0866 1490 PRO B N   
25716 C CA  . PRO C 1490 ? 1.6291 0.8658 1.4176 0.0534  -0.8118 -0.0742 1490 PRO B CA  
25717 C C   . PRO C 1490 ? 1.6000 0.8741 1.3909 0.0514  -0.7911 -0.0515 1490 PRO B C   
25718 O O   . PRO C 1490 ? 1.5784 0.8510 1.3662 0.0619  -0.7814 -0.0385 1490 PRO B O   
25719 C CB  . PRO C 1490 ? 1.6302 0.8340 1.4393 0.0278  -0.8217 -0.0634 1490 PRO B CB  
25720 C CG  . PRO C 1490 ? 1.6851 0.8428 1.4845 0.0431  -0.8330 -0.0746 1490 PRO B CG  
25721 C CD  . PRO C 1490 ? 1.6792 0.8471 1.4559 0.0769  -0.8231 -0.0795 1490 PRO B CD  
25722 N N   . ALA C 1491 ? 1.6092 0.9175 1.4054 0.0379  -0.7850 -0.0474 1491 ALA B N   
25723 C CA  . ALA C 1491 ? 1.5898 0.9308 1.3915 0.0285  -0.7676 -0.0245 1491 ALA B CA  
25724 C C   . ALA C 1491 ? 1.6335 0.9635 1.4574 -0.0013 -0.7721 -0.0075 1491 ALA B C   
25725 O O   . ALA C 1491 ? 1.6507 0.9449 1.4845 -0.0109 -0.7866 -0.0122 1491 ALA B O   
25726 C CB  . ALA C 1491 ? 1.5319 0.9114 1.3261 0.0298  -0.7592 -0.0288 1491 ALA B CB  
25727 N N   . THR C 1492 ? 1.6360 0.9960 1.4666 -0.0153 -0.7593 0.0122  1492 THR B N   
25728 C CA  . THR C 1492 ? 1.6451 0.9983 1.4934 -0.0390 -0.7582 0.0343  1492 THR B CA  
25729 C C   . THR C 1492 ? 1.6401 1.0252 1.4971 -0.0587 -0.7517 0.0455  1492 THR B C   
25730 O O   . THR C 1492 ? 1.6365 1.0550 1.4828 -0.0519 -0.7413 0.0441  1492 THR B O   
25731 C CB  . THR C 1492 ? 1.5925 0.9457 1.4377 -0.0320 -0.7472 0.0528  1492 THR B CB  
25732 O OG1 . THR C 1492 ? 1.3758 0.7535 1.2049 -0.0107 -0.7355 0.0485  1492 THR B OG1 
25733 C CG2 . THR C 1492 ? 1.4347 0.7479 1.2807 -0.0241 -0.7564 0.0502  1492 THR B CG2 
25734 N N   . PHE C 1493 ? 1.6506 1.0241 1.5267 -0.0825 -0.7570 0.0574  1493 PHE B N   
25735 C CA  . PHE C 1493 ? 1.5953 0.9974 1.4818 -0.1022 -0.7512 0.0701  1493 PHE B CA  
25736 C C   . PHE C 1493 ? 1.6473 1.0462 1.5418 -0.1150 -0.7429 0.0973  1493 PHE B C   
25737 O O   . PHE C 1493 ? 1.6742 1.0466 1.5844 -0.1301 -0.7497 0.1062  1493 PHE B O   
25738 C CB  . PHE C 1493 ? 1.5351 0.9287 1.4405 -0.1211 -0.7650 0.0612  1493 PHE B CB  
25739 C CG  . PHE C 1493 ? 1.4297 0.8493 1.3499 -0.1432 -0.7592 0.0780  1493 PHE B CG  
25740 C CD1 . PHE C 1493 ? 1.3326 0.7890 1.2417 -0.1398 -0.7438 0.0897  1493 PHE B CD1 
25741 C CD2 . PHE C 1493 ? 1.4439 0.8511 1.3891 -0.1670 -0.7688 0.0816  1493 PHE B CD2 
25742 C CE1 . PHE C 1493 ? 1.3412 0.8219 1.2618 -0.1580 -0.7380 0.1053  1493 PHE B CE1 
25743 C CE2 . PHE C 1493 ? 1.4165 0.8501 1.3763 -0.1864 -0.7626 0.0978  1493 PHE B CE2 
25744 C CZ  . PHE C 1493 ? 1.3846 0.8555 1.3310 -0.1811 -0.7471 0.1098  1493 PHE B CZ  
25745 N N   . THR C 1494 ? 1.6448 1.0699 1.5276 -0.1086 -0.7281 0.1103  1494 THR B N   
25746 C CA  . THR C 1494 ? 1.6270 1.0521 1.5129 -0.1169 -0.7195 0.1356  1494 THR B CA  
25747 C C   . THR C 1494 ? 1.3980 0.8554 1.2860 -0.1313 -0.7096 0.1511  1494 THR B C   
25748 O O   . THR C 1494 ? 1.2737 0.7597 1.1529 -0.1273 -0.7043 0.1435  1494 THR B O   
25749 C CB  . THR C 1494 ? 1.5836 1.0076 1.4551 -0.0975 -0.7125 0.1385  1494 THR B CB  
25750 O OG1 . THR C 1494 ? 1.5676 1.0072 1.4363 -0.1029 -0.7014 0.1606  1494 THR B OG1 
25751 C CG2 . THR C 1494 ? 1.5361 0.9794 1.3918 -0.0778 -0.7081 0.1204  1494 THR B CG2 
25752 N N   . VAL C 1495 ? 1.4709 0.9220 1.3696 -0.1471 -0.7072 0.1727  1495 VAL B N   
25753 C CA  . VAL C 1495 ? 1.5621 1.0417 1.4612 -0.1592 -0.6970 0.1899  1495 VAL B CA  
25754 C C   . VAL C 1495 ? 1.6175 1.0901 1.5160 -0.1646 -0.6899 0.2158  1495 VAL B C   
25755 O O   . VAL C 1495 ? 1.6549 1.1024 1.5670 -0.1750 -0.6947 0.2266  1495 VAL B O   
25756 C CB  . VAL C 1495 ? 1.2710 0.7603 1.1881 -0.1777 -0.7021 0.1884  1495 VAL B CB  
25757 C CG1 . VAL C 1495 ? 1.5557 1.0119 1.4921 -0.1872 -0.7162 0.1803  1495 VAL B CG1 
25758 C CG2 . VAL C 1495 ? 1.2578 0.7642 1.1802 -0.1926 -0.6923 0.2138  1495 VAL B CG2 
25759 N N   . TYR C 1496 ? 1.5967 1.0911 1.4784 -0.1567 -0.6785 0.2250  1496 TYR B N   
25760 C CA  . TYR C 1496 ? 1.5907 1.0838 1.4664 -0.1581 -0.6713 0.2479  1496 TYR B CA  
25761 C C   . TYR C 1496 ? 1.5816 1.1060 1.4480 -0.1640 -0.6600 0.2606  1496 TYR B C   
25762 O O   . TYR C 1496 ? 1.5556 1.1033 1.4183 -0.1642 -0.6571 0.2507  1496 TYR B O   
25763 C CB  . TYR C 1496 ? 1.5612 1.0498 1.4234 -0.1406 -0.6693 0.2450  1496 TYR B CB  
25764 C CG  . TYR C 1496 ? 1.5514 1.0634 1.3995 -0.1276 -0.6637 0.2299  1496 TYR B CG  
25765 C CD1 . TYR C 1496 ? 1.5223 1.0606 1.3644 -0.1314 -0.6575 0.2263  1496 TYR B CD1 
25766 C CD2 . TYR C 1496 ? 1.5558 1.0645 1.3965 -0.1109 -0.6635 0.2204  1496 TYR B CD2 
25767 C CE1 . TYR C 1496 ? 1.4901 1.0474 1.3181 -0.1194 -0.6511 0.2141  1496 TYR B CE1 
25768 C CE2 . TYR C 1496 ? 1.5310 1.0608 1.3596 -0.0996 -0.6566 0.2083  1496 TYR B CE2 
25769 C CZ  . TYR C 1496 ? 1.5018 1.0546 1.3235 -0.1041 -0.6503 0.2054  1496 TYR B CZ  
25770 O OH  . TYR C 1496 ? 1.4854 1.0577 1.2936 -0.0931 -0.6422 0.1944  1496 TYR B OH  
25771 N N   . GLU C 1497 ? 1.5875 1.1116 1.4484 -0.1670 -0.6539 0.2824  1497 GLU B N   
25772 C CA  . GLU C 1497 ? 1.5505 1.1005 1.3988 -0.1703 -0.6429 0.2966  1497 GLU B CA  
25773 C C   . GLU C 1497 ? 1.5283 1.0921 1.3541 -0.1563 -0.6359 0.2941  1497 GLU B C   
25774 O O   . GLU C 1497 ? 1.4935 1.0448 1.3143 -0.1475 -0.6377 0.2957  1497 GLU B O   
25775 C CB  . GLU C 1497 ? 1.5480 1.0880 1.4003 -0.1793 -0.6403 0.3216  1497 GLU B CB  
25776 C CG  . GLU C 1497 ? 1.5267 1.0896 1.3742 -0.1877 -0.6309 0.3377  1497 GLU B CG  
25777 C CD  . GLU C 1497 ? 1.5369 1.0861 1.3955 -0.1986 -0.6296 0.3608  1497 GLU B CD  
25778 O OE1 . GLU C 1497 ? 1.5258 1.0463 1.3969 -0.2007 -0.6365 0.3626  1497 GLU B OE1 
25779 O OE2 . GLU C 1497 ? 1.5582 1.1243 1.4121 -0.2040 -0.6210 0.3778  1497 GLU B OE2 
25780 N N   . TYR C 1498 ? 1.5445 1.1341 1.3571 -0.1544 -0.6279 0.2907  1498 TYR B N   
25781 C CA  . TYR C 1498 ? 1.5522 1.1533 1.3451 -0.1419 -0.6213 0.2848  1498 TYR B CA  
25782 C C   . TYR C 1498 ? 1.5459 1.1398 1.3290 -0.1382 -0.6193 0.2994  1498 TYR B C   
25783 O O   . TYR C 1498 ? 1.5215 1.1089 1.3022 -0.1285 -0.6215 0.2929  1498 TYR B O   
25784 C CB  . TYR C 1498 ? 1.5496 1.1773 1.3267 -0.1409 -0.6114 0.2830  1498 TYR B CB  
25785 C CG  . TYR C 1498 ? 1.5666 1.2036 1.3264 -0.1280 -0.6049 0.2716  1498 TYR B CG  
25786 C CD1 . TYR C 1498 ? 1.5940 1.2255 1.3588 -0.1188 -0.6085 0.2533  1498 TYR B CD1 
25787 C CD2 . TYR C 1498 ? 1.5786 1.2285 1.3170 -0.1249 -0.5948 0.2796  1498 TYR B CD2 
25788 C CE1 . TYR C 1498 ? 1.6028 1.2430 1.3539 -0.1073 -0.6013 0.2442  1498 TYR B CE1 
25789 C CE2 . TYR C 1498 ? 1.5903 1.2469 1.3147 -0.1145 -0.5882 0.2697  1498 TYR B CE2 
25790 C CZ  . TYR C 1498 ? 1.6036 1.2561 1.3357 -0.1060 -0.5910 0.2525  1498 TYR B CZ  
25791 O OH  . TYR C 1498 ? 1.6123 1.2719 1.3326 -0.0958 -0.5832 0.2437  1498 TYR B OH  
25792 N N   . HIS C 1499 ? 1.5391 1.1353 1.3172 -0.1452 -0.6156 0.3190  1499 HIS B N   
25793 C CA  . HIS C 1499 ? 1.5179 1.1094 1.2832 -0.1407 -0.6139 0.3330  1499 HIS B CA  
25794 C C   . HIS C 1499 ? 1.5809 1.1481 1.3574 -0.1398 -0.6221 0.3404  1499 HIS B C   
25795 O O   . HIS C 1499 ? 1.6186 1.1808 1.3854 -0.1330 -0.6230 0.3481  1499 HIS B O   
25796 C CB  . HIS C 1499 ? 1.4580 1.0617 1.2087 -0.1455 -0.6058 0.3509  1499 HIS B CB  
25797 C CG  . HIS C 1499 ? 1.4025 1.0281 1.1350 -0.1423 -0.5970 0.3449  1499 HIS B CG  
25798 N ND1 . HIS C 1499 ? 1.4000 1.0417 1.1251 -0.1475 -0.5896 0.3535  1499 HIS B ND1 
25799 C CD2 . HIS C 1499 ? 1.3851 1.0189 1.1053 -0.1339 -0.5936 0.3314  1499 HIS B CD2 
25800 C CE1 . HIS C 1499 ? 1.3910 1.0484 1.0976 -0.1416 -0.5823 0.3454  1499 HIS B CE1 
25801 N NE2 . HIS C 1499 ? 1.3745 1.0266 1.0781 -0.1338 -0.5842 0.3320  1499 HIS B NE2 
25802 N N   . ARG C 1500 ? 1.5748 1.1260 1.3709 -0.1461 -0.6284 0.3377  1500 ARG B N   
25803 C CA  . ARG C 1500 ? 1.5823 1.1073 1.3880 -0.1431 -0.6362 0.3420  1500 ARG B CA  
25804 C C   . ARG C 1500 ? 1.5513 1.0601 1.3742 -0.1428 -0.6445 0.3249  1500 ARG B C   
25805 O O   . ARG C 1500 ? 1.5976 1.0899 1.4360 -0.1523 -0.6489 0.3275  1500 ARG B O   
25806 C CB  . ARG C 1500 ? 1.6188 1.1307 1.4272 -0.1508 -0.6351 0.3652  1500 ARG B CB  
25807 C CG  . ARG C 1500 ? 1.6431 1.1705 1.4517 -0.1626 -0.6275 0.3769  1500 ARG B CG  
25808 C CD  . ARG C 1500 ? 1.6994 1.2086 1.5293 -0.1754 -0.6303 0.3861  1500 ARG B CD  
25809 N NE  . ARG C 1500 ? 1.7339 1.2345 1.5605 -0.1786 -0.6254 0.4119  1500 ARG B NE  
25810 C CZ  . ARG C 1500 ? 1.7628 1.2451 1.6072 -0.1895 -0.6260 0.4242  1500 ARG B CZ  
25811 N NH1 . ARG C 1500 ? 1.7599 1.2296 1.6270 -0.1990 -0.6328 0.4116  1500 ARG B NH1 
25812 N NH2 . ARG C 1500 ? 1.7911 1.2664 1.6302 -0.1904 -0.6199 0.4490  1500 ARG B NH2 
25813 N N   . PRO C 1501 ? 1.4960 1.0089 1.3160 -0.1315 -0.6466 0.3074  1501 PRO B N   
25814 C CA  . PRO C 1501 ? 1.4956 0.9943 1.3259 -0.1247 -0.6542 0.2889  1501 PRO B CA  
25815 C C   . PRO C 1501 ? 1.5663 1.0338 1.4066 -0.1235 -0.6625 0.2946  1501 PRO B C   
25816 O O   . PRO C 1501 ? 1.5693 1.0213 1.4163 -0.1160 -0.6693 0.2807  1501 PRO B O   
25817 C CB  . PRO C 1501 ? 1.4755 0.9868 1.2961 -0.1102 -0.6518 0.2795  1501 PRO B CB  
25818 C CG  . PRO C 1501 ? 1.4563 0.9919 1.2622 -0.1122 -0.6424 0.2868  1501 PRO B CG  
25819 C CD  . PRO C 1501 ? 1.4552 0.9893 1.2585 -0.1235 -0.6399 0.3063  1501 PRO B CD  
25820 N N   . ASP C 1502 ? 1.6405 1.0982 1.4795 -0.1284 -0.6613 0.3151  1502 ASP B N   
25821 C CA  . ASP C 1502 ? 1.7145 1.1410 1.5601 -0.1254 -0.6679 0.3227  1502 ASP B CA  
25822 C C   . ASP C 1502 ? 1.7905 1.1977 1.6523 -0.1388 -0.6720 0.3206  1502 ASP B C   
25823 O O   . ASP C 1502 ? 1.8451 1.2216 1.7151 -0.1399 -0.6775 0.3256  1502 ASP B O   
25824 C CB  . ASP C 1502 ? 1.7343 1.1567 1.5708 -0.1247 -0.6645 0.3465  1502 ASP B CB  
25825 C CG  . ASP C 1502 ? 1.6805 1.1327 1.5002 -0.1221 -0.6570 0.3528  1502 ASP B CG  
25826 O OD1 . ASP C 1502 ? 1.6232 1.0932 1.4360 -0.1128 -0.6564 0.3405  1502 ASP B OD1 
25827 O OD2 . ASP C 1502 ? 1.6905 1.1472 1.5039 -0.1293 -0.6513 0.3710  1502 ASP B OD2 
25828 N N   . LYS C 1503 ? 1.8205 1.2462 1.6872 -0.1489 -0.6695 0.3127  1503 LYS B N   
25829 C CA  . LYS C 1503 ? 1.9110 1.3241 1.7955 -0.1639 -0.6739 0.3095  1503 LYS B CA  
25830 C C   . LYS C 1503 ? 1.7362 1.1445 1.6286 -0.1615 -0.6824 0.2828  1503 LYS B C   
25831 O O   . LYS C 1503 ? 1.6868 1.1013 1.5910 -0.1735 -0.6849 0.2752  1503 LYS B O   
25832 C CB  . LYS C 1503 ? 1.9485 1.3853 1.8354 -0.1782 -0.6658 0.3227  1503 LYS B CB  
25833 C CG  . LYS C 1503 ? 1.9995 1.4260 1.8881 -0.1862 -0.6605 0.3501  1503 LYS B CG  
25834 C CD  . LYS C 1503 ? 2.0352 1.4514 1.9082 -0.1729 -0.6587 0.3627  1503 LYS B CD  
25835 C CE  . LYS C 1503 ? 2.1104 1.5020 1.9891 -0.1796 -0.6568 0.3865  1503 LYS B CE  
25836 N NZ  . LYS C 1503 ? 2.1544 1.5273 2.0199 -0.1648 -0.6582 0.3968  1503 LYS B NZ  
25837 N N   . GLN C 1504 ? 1.7136 1.1105 1.5996 -0.1452 -0.6873 0.2692  1504 GLN B N   
25838 C CA  . GLN C 1504 ? 1.7395 1.1330 1.6272 -0.1374 -0.6943 0.2439  1504 GLN B CA  
25839 C C   . GLN C 1504 ? 1.7475 1.1055 1.6488 -0.1431 -0.7054 0.2366  1504 GLN B C   
25840 O O   . GLN C 1504 ? 1.3707 0.7007 1.2704 -0.1329 -0.7109 0.2348  1504 GLN B O   
25841 C CB  . GLN C 1504 ? 1.6129 1.0110 1.4879 -0.1159 -0.6934 0.2334  1504 GLN B CB  
25842 C CG  . GLN C 1504 ? 2.1407 1.5755 2.0041 -0.1086 -0.6852 0.2235  1504 GLN B CG  
25843 C CD  . GLN C 1504 ? 1.8481 1.2950 1.7002 -0.0907 -0.6802 0.2212  1504 GLN B CD  
25844 O OE1 . GLN C 1504 ? 1.7530 1.2276 1.5956 -0.0857 -0.6718 0.2168  1504 GLN B OE1 
25845 N NE2 . GLN C 1504 ? 1.8965 1.3228 1.7504 -0.0813 -0.6851 0.2245  1504 GLN B NE2 
25846 N N   . CYS C 1505 ? 1.6898 1.0497 1.6047 -0.1595 -0.7089 0.2325  1505 CYS B N   
25847 C CA  . CYS C 1505 ? 1.6485 0.9789 1.5760 -0.1643 -0.7215 0.2168  1505 CYS B CA  
25848 C C   . CYS C 1505 ? 1.6305 0.9680 1.5502 -0.1502 -0.7275 0.1892  1505 CYS B C   
25849 O O   . CYS C 1505 ? 1.5905 0.9601 1.5055 -0.1490 -0.7235 0.1805  1505 CYS B O   
25850 C CB  . CYS C 1505 ? 1.6677 0.9965 1.6162 -0.1884 -0.7245 0.2221  1505 CYS B CB  
25851 S SG  . CYS C 1505 ? 2.3817 1.6620 2.3469 -0.1962 -0.7411 0.2072  1505 CYS B SG  
25852 N N   . THR C 1506 ? 1.7029 1.0092 1.6196 -0.1380 -0.7365 0.1760  1506 THR B N   
25853 C CA  . THR C 1506 ? 1.7216 1.0326 1.6275 -0.1204 -0.7410 0.1515  1506 THR B CA  
25854 C C   . THR C 1506 ? 1.7675 1.0418 1.6815 -0.1229 -0.7561 0.1348  1506 THR B C   
25855 O O   . THR C 1506 ? 1.8003 1.0388 1.7225 -0.1303 -0.7614 0.1434  1506 THR B O   
25856 C CB  . THR C 1506 ? 1.7470 1.0575 1.6375 -0.0975 -0.7362 0.1516  1506 THR B CB  
25857 O OG1 . THR C 1506 ? 1.7719 1.1105 1.6572 -0.0981 -0.7235 0.1702  1506 THR B OG1 
25858 C CG2 . THR C 1506 ? 1.7265 1.0494 1.6050 -0.0783 -0.7373 0.1288  1506 THR B CG2 
25859 N N   . MET C 1507 ? 1.7692 1.0511 1.6792 -0.1162 -0.7628 0.1109  1507 MET B N   
25860 C CA  . MET C 1507 ? 1.7552 1.0043 1.6710 -0.1178 -0.7791 0.0903  1507 MET B CA  
25861 C C   . MET C 1507 ? 1.7065 0.9607 1.6058 -0.0954 -0.7844 0.0634  1507 MET B C   
25862 O O   . MET C 1507 ? 1.6322 0.9229 1.5239 -0.0895 -0.7783 0.0566  1507 MET B O   
25863 C CB  . MET C 1507 ? 1.7362 0.9911 1.6729 -0.1436 -0.7853 0.0898  1507 MET B CB  
25864 C CG  . MET C 1507 ? 1.7828 0.9985 1.7313 -0.1524 -0.8028 0.0736  1507 MET B CG  
25865 S SD  . MET C 1507 ? 1.6200 0.8637 1.5919 -0.1785 -0.8081 0.0687  1507 MET B SD  
25866 C CE  . MET C 1507 ? 1.4810 0.7793 1.4460 -0.1779 -0.7874 0.0903  1507 MET B CE  
25867 N N   . PHE C 1508 ? 1.7439 0.9606 1.6359 -0.0814 -0.7951 0.0488  1508 PHE B N   
25868 C CA  . PHE C 1508 ? 1.7812 0.9969 1.6580 -0.0609 -0.8025 0.0217  1508 PHE B CA  
25869 C C   . PHE C 1508 ? 1.9074 1.1195 1.7955 -0.0759 -0.8169 0.0036  1508 PHE B C   
25870 O O   . PHE C 1508 ? 1.9975 1.1881 1.9054 -0.0993 -0.8253 0.0088  1508 PHE B O   
25871 C CB  . PHE C 1508 ? 1.7361 0.9089 1.6017 -0.0422 -0.8108 0.0120  1508 PHE B CB  
25872 C CG  . PHE C 1508 ? 1.6390 0.8188 1.4902 -0.0196 -0.7993 0.0211  1508 PHE B CG  
25873 C CD1 . PHE C 1508 ? 1.6007 0.8153 1.4380 -0.0005 -0.7889 0.0157  1508 PHE B CD1 
25874 C CD2 . PHE C 1508 ? 1.6239 0.7739 1.4754 -0.0162 -0.7993 0.0342  1508 PHE B CD2 
25875 C CE1 . PHE C 1508 ? 1.5926 0.8152 1.4197 0.0197  -0.7784 0.0240  1508 PHE B CE1 
25876 C CE2 . PHE C 1508 ? 1.6139 0.7724 1.4539 0.0052  -0.7897 0.0418  1508 PHE B CE2 
25877 C CZ  . PHE C 1508 ? 1.5888 0.7847 1.4181 0.0225  -0.7794 0.0367  1508 PHE B CZ  
25878 N N   . TYR C 1509 ? 1.8873 1.1200 1.7634 -0.0624 -0.8199 -0.0175 1509 TYR B N   
25879 C CA  . TYR C 1509 ? 1.8829 1.1093 1.7669 -0.0716 -0.8368 -0.0398 1509 TYR B CA  
25880 C C   . TYR C 1509 ? 1.9197 1.1515 1.7792 -0.0426 -0.8406 -0.0651 1509 TYR B C   
25881 O O   . TYR C 1509 ? 1.9214 1.1692 1.7618 -0.0196 -0.8275 -0.0620 1509 TYR B O   
25882 C CB  . TYR C 1509 ? 1.7721 1.0376 1.6727 -0.0934 -0.8336 -0.0336 1509 TYR B CB  
25883 C CG  . TYR C 1509 ? 1.6773 0.9879 1.5608 -0.0772 -0.8217 -0.0374 1509 TYR B CG  
25884 C CD1 . TYR C 1509 ? 1.6378 0.9778 1.5240 -0.0818 -0.8261 -0.0501 1509 TYR B CD1 
25885 C CD2 . TYR C 1509 ? 1.6644 0.9874 1.5286 -0.0563 -0.8058 -0.0284 1509 TYR B CD2 
25886 C CE1 . TYR C 1509 ? 1.6097 0.9885 1.4775 -0.0651 -0.8139 -0.0528 1509 TYR B CE1 
25887 C CE2 . TYR C 1509 ? 1.6275 0.9888 1.4754 -0.0414 -0.7936 -0.0310 1509 TYR B CE2 
25888 C CZ  . TYR C 1509 ? 1.6030 0.9909 1.4515 -0.0454 -0.7973 -0.0429 1509 TYR B CZ  
25889 O OH  . TYR C 1509 ? 1.5688 0.9925 1.3992 -0.0296 -0.7841 -0.0446 1509 TYR B OH  
25890 N N   . SER C 1510 ? 1.9313 1.1507 1.7914 -0.0431 -0.8583 -0.0902 1510 SER B N   
25891 C CA  . SER C 1510 ? 1.9322 1.1579 1.7670 -0.0140 -0.8621 -0.1146 1510 SER B CA  
25892 C C   . SER C 1510 ? 1.9389 1.1918 1.7778 -0.0206 -0.8708 -0.1316 1510 SER B C   
25893 O O   . SER C 1510 ? 1.9269 1.1836 1.7904 -0.0481 -0.8797 -0.1299 1510 SER B O   
25894 C CB  . SER C 1510 ? 1.9607 1.1372 1.7816 0.0037  -0.8771 -0.1342 1510 SER B CB  
25895 O OG  . SER C 1510 ? 1.9443 1.1294 1.7360 0.0381  -0.8742 -0.1512 1510 SER B OG  
25896 N N   . THR C 1511 ? 1.9643 1.2374 1.7786 0.0062  -0.8677 -0.1475 1511 THR B N   
25897 C CA  . THR C 1511 ? 1.9595 1.2661 1.7726 0.0054  -0.8721 -0.1616 1511 THR B CA  
25898 C C   . THR C 1511 ? 2.1047 1.3870 1.9085 0.0169  -0.8952 -0.1943 1511 THR B C   
25899 O O   . THR C 1511 ? 2.1262 1.4329 1.9192 0.0278  -0.9002 -0.2122 1511 THR B O   
25900 C CB  . THR C 1511 ? 1.8543 1.1985 1.6437 0.0295  -0.8528 -0.1579 1511 THR B CB  
25901 O OG1 . THR C 1511 ? 1.8212 1.2054 1.6146 0.0215  -0.8515 -0.1607 1511 THR B OG1 
25902 C CG2 . THR C 1511 ? 1.8544 1.1839 1.6128 0.0659  -0.8557 -0.1795 1511 THR B CG2 
25903 N N   . SER C 1512 ? 2.2424 1.4755 2.0485 0.0159  -0.9095 -0.2027 1512 SER B N   
25904 C CA  . SER C 1512 ? 2.3929 1.5966 2.1893 0.0263  -0.9336 -0.2352 1512 SER B CA  
25905 C C   . SER C 1512 ? 2.5738 1.7203 2.3809 0.0143  -0.9497 -0.2395 1512 SER B C   
25906 O O   . SER C 1512 ? 2.5844 1.7080 2.3935 0.0127  -0.9402 -0.2204 1512 SER B O   
25907 C CB  . SER C 1512 ? 2.3954 1.6002 2.1534 0.0682  -0.9303 -0.2529 1512 SER B CB  
25908 O OG  . SER C 1512 ? 2.4061 1.5837 2.1494 0.0866  -0.9209 -0.2436 1512 SER B OG  
25909 N N   . ASN C 1513 ? 2.7413 1.8642 2.5544 0.0067  -0.9746 -0.2654 1513 ASN B N   
25910 C CA  . ASN C 1513 ? 2.9184 1.9838 2.7425 -0.0070 -0.9920 -0.2721 1513 ASN B CA  
25911 C C   . ASN C 1513 ? 3.0459 2.0656 2.8370 0.0258  -1.0035 -0.2951 1513 ASN B C   
25912 O O   . ASN C 1513 ? 3.1180 2.0847 2.9129 0.0184  -1.0179 -0.3020 1513 ASN B O   
25913 C CB  . ASN C 1513 ? 2.9877 2.0491 2.8420 -0.0388 -1.0141 -0.2865 1513 ASN B CB  
25914 C CG  . ASN C 1513 ? 2.9743 2.0943 2.8518 -0.0595 -1.0059 -0.2749 1513 ASN B CG  
25915 O OD1 . ASN C 1513 ? 2.9395 2.0866 2.8291 -0.0714 -0.9850 -0.2450 1513 ASN B OD1 
25916 N ND2 . ASN C 1513 ? 2.9987 2.1388 2.8816 -0.0628 -1.0230 -0.2991 1513 ASN B ND2 
25917 N N   . ILE C 1514 ? 3.0685 2.1074 2.8264 0.0625  -0.9962 -0.3062 1514 ILE B N   
25918 C CA  . ILE C 1514 ? 3.1320 2.1333 2.8552 0.0975  -1.0082 -0.3319 1514 ILE B CA  
25919 C C   . ILE C 1514 ? 3.1703 2.1210 2.8823 0.1090  -1.0060 -0.3239 1514 ILE B C   
25920 O O   . ILE C 1514 ? 3.1377 2.0995 2.8495 0.1136  -0.9846 -0.2978 1514 ILE B O   
25921 C CB  . ILE C 1514 ? 3.2758 2.3126 2.9652 0.1367  -0.9950 -0.3393 1514 ILE B CB  
25922 C CG1 . ILE C 1514 ? 3.2207 2.3138 2.9183 0.1286  -0.9906 -0.3407 1514 ILE B CG1 
25923 C CG2 . ILE C 1514 ? 3.3361 2.3370 2.9903 0.1717  -1.0115 -0.3707 1514 ILE B CG2 
25924 C CD1 . ILE C 1514 ? 3.1792 2.3099 2.8461 0.1641  -0.9723 -0.3413 1514 ILE B CD1 
25925 N N   . LYS C 1515 ? 4.2595 2.2994 2.4208 0.9608  -0.1783 -0.5070 1515 LYS B N   
25926 C CA  . LYS C 1515 ? 4.2414 2.2748 2.5145 0.9353  -0.2619 -0.5312 1515 LYS B CA  
25927 C C   . LYS C 1515 ? 4.1353 2.3118 2.5014 0.9535  -0.2520 -0.5752 1515 LYS B C   
25928 O O   . LYS C 1515 ? 4.1574 2.2669 2.4624 0.9404  -0.2885 -0.6030 1515 LYS B O   
25929 C CB  . LYS C 1515 ? 4.3598 2.1655 2.5285 0.8823  -0.3503 -0.5268 1515 LYS B CB  
25930 C CG  . LYS C 1515 ? 4.4128 2.1118 2.6118 0.8444  -0.4145 -0.4892 1515 LYS B CG  
25931 C CD  . LYS C 1515 ? 4.3531 2.1081 2.7404 0.8299  -0.4927 -0.5026 1515 LYS B CD  
25932 C CE  . LYS C 1515 ? 4.4262 2.0572 2.8328 0.7848  -0.5673 -0.4588 1515 LYS B CE  
25933 N NZ  . LYS C 1515 ? 4.3852 2.0579 2.9890 0.7678  -0.6503 -0.4688 1515 LYS B NZ  
25934 N N   . ILE C 1516 ? 4.2336 2.5478 2.7562 0.9675  -0.1942 -0.5081 1516 ILE B N   
25935 C CA  . ILE C 1516 ? 4.1298 2.6400 2.8096 0.9802  -0.1518 -0.5252 1516 ILE B CA  
25936 C C   . ILE C 1516 ? 4.1001 2.6666 2.9480 0.9660  -0.1983 -0.5636 1516 ILE B C   
25937 O O   . ILE C 1516 ? 4.1771 2.6373 3.0222 0.9496  -0.2695 -0.5744 1516 ILE B O   
25938 C CB  . ILE C 1516 ? 3.0297 1.5697 1.7373 0.9777  -0.1346 -0.4963 1516 ILE B CB  
25939 C CG1 . ILE C 1516 ? 3.1299 1.5261 1.6659 0.9799  -0.1275 -0.4511 1516 ILE B CG1 
25940 C CG2 . ILE C 1516 ? 2.9116 1.6481 1.7116 0.9869  -0.0613 -0.5086 1516 ILE B CG2 
25941 C CD1 . ILE C 1516 ? 3.1364 1.5301 1.6734 0.9742  -0.1231 -0.4193 1516 ILE B CD1 
25942 N N   . GLN C 1517 ? 3.9979 2.7284 2.9938 0.9673  -0.1555 -0.5844 1517 GLN B N   
25943 C CA  . GLN C 1517 ? 3.9421 2.7444 3.1298 0.9535  -0.1813 -0.6222 1517 GLN B CA  
25944 C C   . GLN C 1517 ? 3.8118 2.7767 3.1210 0.9459  -0.1145 -0.6376 1517 GLN B C   
25945 O O   . GLN C 1517 ? 3.7558 2.8001 2.9977 0.9509  -0.0446 -0.6272 1517 GLN B O   
25946 C CB  . GLN C 1517 ? 3.9594 2.7934 3.1655 0.9588  -0.1786 -0.6579 1517 GLN B CB  
25947 C CG  . GLN C 1517 ? 3.9711 2.8609 3.3811 0.9457  -0.2077 -0.6973 1517 GLN B CG  
25948 C CD  . GLN C 1517 ? 4.0960 2.8505 3.5674 0.9290  -0.3153 -0.6846 1517 GLN B CD  
25949 O OE1 . GLN C 1517 ? 4.2002 2.8045 3.5386 0.9205  -0.3701 -0.6469 1517 GLN B OE1 
25950 N NE2 . GLN C 1517 ? 4.0857 2.8878 3.7630 0.9185  -0.3446 -0.7135 1517 GLN B NE2 
25951 N N   . LYS C 1518 ? 3.7582 2.7668 3.2469 0.9279  -0.1372 -0.6614 1518 LYS B N   
25952 C CA  . LYS C 1518 ? 3.6386 2.7848 3.2424 0.9089  -0.0769 -0.6828 1518 LYS B CA  
25953 C C   . LYS C 1518 ? 3.6133 2.8320 3.4485 0.8888  -0.0814 -0.7309 1518 LYS B C   
25954 O O   . LYS C 1518 ? 3.6636 2.8045 3.5860 0.8908  -0.1564 -0.7316 1518 LYS B O   
25955 C CB  . LYS C 1518 ? 3.5765 2.6800 3.1222 0.9040  -0.0925 -0.6481 1518 LYS B CB  
25956 C CG  . LYS C 1518 ? 3.4994 2.5285 2.8337 0.9230  -0.0806 -0.5999 1518 LYS B CG  
25957 C CD  . LYS C 1518 ? 3.4351 2.4042 2.7185 0.9167  -0.1058 -0.5663 1518 LYS B CD  
25958 C CE  . LYS C 1518 ? 3.4500 2.2825 2.5346 0.9349  -0.1191 -0.5158 1518 LYS B CE  
25959 N NZ  . LYS C 1518 ? 3.4954 2.2209 2.5374 0.9231  -0.1707 -0.4823 1518 LYS B NZ  
25960 N N   . VAL C 1519 ? 3.5417 2.9021 3.4787 0.8634  -0.0009 -0.7693 1519 VAL B N   
25961 C CA  . VAL C 1519 ? 3.5000 2.9387 3.6653 0.8402  0.0186  -0.8232 1519 VAL B CA  
25962 C C   . VAL C 1519 ? 3.5011 2.9389 3.8214 0.8231  -0.0147 -0.8337 1519 VAL B C   
25963 O O   . VAL C 1519 ? 3.5667 2.9326 3.9945 0.8326  -0.0920 -0.8277 1519 VAL B O   
25964 C CB  . VAL C 1519 ? 3.4364 3.0162 3.6448 0.8054  0.1286  -0.8647 1519 VAL B CB  
25965 C CG1 . VAL C 1519 ? 3.3990 3.0479 3.8489 0.7774  0.1587  -0.9241 1519 VAL B CG1 
25966 C CG2 . VAL C 1519 ? 3.4307 3.0167 3.5066 0.8200  0.1588  -0.8545 1519 VAL B CG2 
25967 N N   . CYS C 1520 ? 3.4157 2.9343 3.7507 0.7923  0.0417  -0.8493 1520 CYS B N   
25968 C CA  . CYS C 1520 ? 3.3642 2.8747 3.7960 0.7764  0.0089  -0.8524 1520 CYS B CA  
25969 C C   . CYS C 1520 ? 3.2740 2.8481 3.6191 0.7457  0.0637  -0.8552 1520 CYS B C   
25970 O O   . CYS C 1520 ? 3.2066 2.8801 3.6666 0.6998  0.1269  -0.9062 1520 CYS B O   
25971 C CB  . CYS C 1520 ? 3.3333 2.8980 4.0353 0.7556  0.0149  -0.9058 1520 CYS B CB  
25972 S SG  . CYS C 1520 ? 2.9718 2.4248 3.8120 0.7747  -0.1111 -0.8742 1520 CYS B SG  
25973 N N   . GLU C 1521 ? 3.2574 2.7664 3.3968 0.7666  0.0401  -0.8013 1521 GLU B N   
25974 C CA  . GLU C 1521 ? 3.1744 2.7264 3.2090 0.7417  0.0774  -0.7928 1521 GLU B CA  
25975 C C   . GLU C 1521 ? 3.1374 2.6284 3.1540 0.7424  0.0197  -0.7712 1521 GLU B C   
25976 O O   . GLU C 1521 ? 3.1893 2.5837 3.2321 0.7661  -0.0550 -0.7455 1521 GLU B O   
25977 C CB  . GLU C 1521 ? 3.1706 2.6921 2.9990 0.7648  0.0925  -0.7443 1521 GLU B CB  
25978 C CG  . GLU C 1521 ? 3.0898 2.6463 2.9058 0.7734  0.1332  -0.7517 1521 GLU B CG  
25979 C CD  . GLU C 1521 ? 3.0303 2.5987 2.6754 0.7798  0.1697  -0.7119 1521 GLU B CD  
25980 O OE1 . GLU C 1521 ? 3.0205 2.5733 2.5699 0.7766  0.1652  -0.6812 1521 GLU B OE1 
25981 O OE2 . GLU C 1521 ? 2.9942 2.5877 2.6040 0.7876  0.2018  -0.7097 1521 GLU B OE2 
25982 N N   . GLY C 1522 ? 3.0376 2.5807 2.9999 0.7100  0.0514  -0.7788 1522 GLY B N   
25983 C CA  . GLY C 1522 ? 2.9979 2.4885 2.9164 0.7074  0.0023  -0.7582 1522 GLY B CA  
25984 C C   . GLY C 1522 ? 3.0053 2.3633 2.7284 0.7503  -0.0523 -0.6840 1522 GLY B C   
25985 O O   . GLY C 1522 ? 3.0112 2.3271 2.6247 0.7794  -0.0433 -0.6523 1522 GLY B O   
25986 N N   . ALA C 1523 ? 2.9984 2.2858 2.6746 0.7499  -0.1053 -0.6570 1523 ALA B N   
25987 C CA  . ALA C 1523 ? 3.0192 2.1685 2.4999 0.7796  -0.1497 -0.5869 1523 ALA B CA  
25988 C C   . ALA C 1523 ? 3.0004 2.0437 2.4551 0.8109  -0.1861 -0.5556 1523 ALA B C   
25989 O O   . ALA C 1523 ? 3.0578 1.9889 2.3416 0.8331  -0.2002 -0.5047 1523 ALA B O   
25990 C CB  . ALA C 1523 ? 3.0128 2.1830 2.3290 0.7832  -0.1022 -0.5660 1523 ALA B CB  
25991 N N   . ALA C 1524 ? 2.9253 1.9988 2.5495 0.8087  -0.1998 -0.5885 1524 ALA B N   
25992 C CA  . ALA C 1524 ? 2.9476 1.9164 2.5461 0.8308  -0.2430 -0.5631 1524 ALA B CA  
25993 C C   . ALA C 1524 ? 2.9260 1.8975 2.7310 0.8219  -0.2916 -0.5878 1524 ALA B C   
25994 O O   . ALA C 1524 ? 2.9755 1.8556 2.8148 0.8115  -0.3674 -0.5569 1524 ALA B O   
25995 C CB  . ALA C 1524 ? 2.9131 1.9168 2.4342 0.8510  -0.1864 -0.5708 1524 ALA B CB  
25996 N N   . CYS C 1525 ? 2.8603 1.9330 2.8049 0.8225  -0.2490 -0.6392 1525 CYS B N   
25997 C CA  . CYS C 1525 ? 2.8655 1.9414 3.0176 0.8174  -0.2914 -0.6632 1525 CYS B CA  
25998 C C   . CYS C 1525 ? 2.8803 1.9818 3.2043 0.7942  -0.3242 -0.6740 1525 CYS B C   
25999 O O   . CYS C 1525 ? 2.8972 2.0134 3.1631 0.7807  -0.3144 -0.6656 1525 CYS B O   
26000 C CB  . CYS C 1525 ? 2.7937 1.9900 3.0663 0.8175  -0.2207 -0.7228 1525 CYS B CB  
26001 S SG  . CYS C 1525 ? 4.3650 3.6211 4.9569 0.8049  -0.2364 -0.7747 1525 CYS B SG  
26002 N N   . LYS C 1526 ? 2.8871 1.9928 3.4254 0.7895  -0.3650 -0.6920 1526 LYS B N   
26003 C CA  . LYS C 1526 ? 2.9109 2.0402 3.6524 0.7688  -0.4018 -0.7011 1526 LYS B CA  
26004 C C   . LYS C 1526 ? 2.9693 1.9748 3.5816 0.7606  -0.4829 -0.6306 1526 LYS B C   
26005 O O   . LYS C 1526 ? 2.9570 1.9878 3.6556 0.7414  -0.4991 -0.6309 1526 LYS B O   
26006 C CB  . LYS C 1526 ? 2.9029 2.1913 3.7790 0.7456  -0.3073 -0.7737 1526 LYS B CB  
26007 C CG  . LYS C 1526 ? 2.9859 2.2979 3.7076 0.7293  -0.2754 -0.7687 1526 LYS B CG  
26008 C CD  . LYS C 1526 ? 2.9684 2.4294 3.8220 0.6921  -0.1825 -0.8482 1526 LYS B CD  
26009 C CE  . LYS C 1526 ? 3.0138 2.4853 3.7745 0.6676  -0.1823 -0.8447 1526 LYS B CE  
26010 N NZ  . LYS C 1526 ? 3.0728 2.4738 3.9068 0.6681  -0.2701 -0.8076 1526 LYS B NZ  
26011 N N   . CYS C 1527 ? 3.0337 1.8985 3.4306 0.7705  -0.5307 -0.5703 1527 CYS B N   
26012 C CA  . CYS C 1527 ? 3.1118 1.8416 3.3533 0.7555  -0.5989 -0.4988 1527 CYS B CA  
26013 C C   . CYS C 1527 ? 3.1651 1.7249 3.1757 0.7580  -0.6425 -0.4397 1527 CYS B C   
26014 O O   . CYS C 1527 ? 3.2486 1.6740 3.0912 0.7397  -0.6898 -0.3763 1527 CYS B O   
26015 C CB  . CYS C 1527 ? 3.1163 1.9069 3.2482 0.7520  -0.5430 -0.5067 1527 CYS B CB  
26016 S SG  . CYS C 1527 ? 4.3218 3.0946 4.5277 0.7214  -0.6022 -0.4787 1527 CYS B SG  
26017 N N   . VAL C 1528 ? 3.1161 1.6754 3.1064 0.7758  -0.6219 -0.4616 1528 VAL B N   
26018 C CA  . VAL C 1528 ? 3.1846 1.5681 2.9903 0.7678  -0.6757 -0.4125 1528 VAL B CA  
26019 C C   . VAL C 1528 ? 3.2209 1.5583 3.1595 0.7573  -0.7440 -0.4194 1528 VAL B C   
26020 O O   . VAL C 1528 ? 3.3204 1.5041 3.2384 0.7214  -0.8443 -0.3667 1528 VAL B O   
26021 C CB  . VAL C 1528 ? 3.1221 1.4992 2.7127 0.7930  -0.6010 -0.4185 1528 VAL B CB  
26022 C CG1 . VAL C 1528 ? 3.2065 1.3905 2.6102 0.7765  -0.6533 -0.3741 1528 VAL B CG1 
26023 C CG2 . VAL C 1528 ? 3.1076 1.5099 2.5674 0.7990  -0.5484 -0.4024 1528 VAL B CG2 
26024 N N   . GLU C 1529 ? 3.1486 1.6137 3.2169 0.7825  -0.6912 -0.4819 1529 GLU B N   
26025 C CA  . GLU C 1529 ? 3.1673 1.6197 3.4031 0.7761  -0.7487 -0.4991 1529 GLU B CA  
26026 C C   . GLU C 1529 ? 3.1820 1.6636 3.6731 0.7562  -0.8080 -0.4924 1529 GLU B C   
26027 O O   . GLU C 1529 ? 3.1722 1.6149 3.8263 0.7416  -0.8839 -0.4874 1529 GLU B O   
26028 C CB  . GLU C 1529 ? 3.0698 1.6695 3.3896 0.8068  -0.6623 -0.5700 1529 GLU B CB  
26029 C CG  . GLU C 1529 ? 3.0570 1.6572 3.5563 0.8040  -0.7119 -0.5947 1529 GLU B CG  
26030 C CD  . GLU C 1529 ? 3.1435 1.5850 3.4790 0.7917  -0.7852 -0.5660 1529 GLU B CD  
26031 O OE1 . GLU C 1529 ? 3.1314 1.5831 3.3057 0.8113  -0.7298 -0.5875 1529 GLU B OE1 
26032 O OE2 . GLU C 1529 ? 3.2215 1.5250 3.5889 0.7564  -0.8997 -0.5213 1529 GLU B OE2 
26033 N N   . ALA C 1530 ? 3.2151 1.7677 3.7433 0.7548  -0.7726 -0.4930 1530 ALA B N   
26034 C CA  . ALA C 1530 ? 3.2636 1.8533 4.0267 0.7363  -0.8179 -0.4873 1530 ALA B CA  
26035 C C   . ALA C 1530 ? 3.4203 1.8434 4.0840 0.6988  -0.9245 -0.3999 1530 ALA B C   
26036 O O   . ALA C 1530 ? 3.4267 1.8680 4.0973 0.6871  -0.9254 -0.3802 1530 ALA B O   
26037 C CB  . ALA C 1530 ? 3.1893 1.9426 4.0400 0.7462  -0.7222 -0.5403 1530 ALA B CB  
26038 N N   . ASP C 1531 ? 3.5585 1.8131 4.1142 0.6731  -1.0130 -0.3477 1531 ASP B N   
26039 C CA  . ASP C 1531 ? 3.7213 1.7948 4.1996 0.6198  -1.1286 -0.2574 1531 ASP B CA  
26040 C C   . ASP C 1531 ? 3.8608 1.7555 4.2643 0.5798  -1.2289 -0.2147 1531 ASP B C   
26041 O O   . ASP C 1531 ? 3.9757 1.7013 4.3217 0.5201  -1.3366 -0.1353 1531 ASP B O   
26042 C CB  . ASP C 1531 ? 3.7788 1.7777 3.9903 0.6087  -1.1013 -0.2132 1531 ASP B CB  
26043 C CG  . ASP C 1531 ? 3.7349 1.8248 4.0494 0.6086  -1.0871 -0.2092 1531 ASP B CG  
26044 O OD1 . ASP C 1531 ? 3.7901 1.8037 4.1869 0.5675  -1.1800 -0.1488 1531 ASP B OD1 
26045 O OD2 . ASP C 1531 ? 3.6470 1.8816 3.9567 0.6441  -0.9860 -0.2652 1531 ASP B OD2 
26046 N N   . CYS C 1532 ? 3.8571 1.7874 4.2577 0.6057  -1.1949 -0.2674 1532 CYS B N   
26047 C CA  . CYS C 1532 ? 3.9689 1.7406 4.2879 0.5682  -1.2813 -0.2435 1532 CYS B CA  
26048 C C   . CYS C 1532 ? 3.9935 1.7134 4.5567 0.5273  -1.4092 -0.2112 1532 CYS B C   
26049 O O   . CYS C 1532 ? 4.1098 1.6356 4.5892 0.4594  -1.5271 -0.1439 1532 CYS B O   
26050 C CB  . CYS C 1532 ? 3.9169 1.7630 4.1791 0.6115  -1.2046 -0.3151 1532 CYS B CB  
26051 S SG  . CYS C 1532 ? 3.8273 1.7100 3.7929 0.6528  -1.0680 -0.3426 1532 CYS B SG  
26052 N N   . LEU D 40   ? 2.1666 2.6029 3.2557 -0.2032 0.1384  0.0506  40   LEU Y N   
26053 C CA  . LEU D 40   ? 2.1546 2.6044 3.2647 -0.1736 0.1773  0.0473  40   LEU Y CA  
26054 C C   . LEU D 40   ? 2.2168 2.6291 3.2659 -0.1720 0.2029  0.0125  40   LEU Y C   
26055 O O   . LEU D 40   ? 2.2121 2.6363 3.2708 -0.1583 0.2319  0.0065  40   LEU Y O   
26056 C CB  . LEU D 40   ? 2.1257 2.5741 3.2639 -0.1453 0.1870  0.0610  40   LEU Y CB  
26057 C CG  . LEU D 40   ? 2.0693 2.5592 3.2776 -0.1446 0.1650  0.0982  40   LEU Y CG  
26058 C CD1 . LEU D 40   ? 2.0696 2.5563 3.3026 -0.1168 0.1757  0.1104  40   LEU Y CD1 
26059 C CD2 . LEU D 40   ? 2.0249 2.5697 3.2939 -0.1430 0.1716  0.1204  40   LEU Y CD2 
26060 N N   . HIS D 41   ? 2.2669 2.6314 3.2541 -0.1858 0.1918  -0.0092 41   HIS Y N   
26061 C CA  . HIS D 41   ? 2.3493 2.6768 3.2742 -0.1965 0.2046  -0.0408 41   HIS Y CA  
26062 C C   . HIS D 41   ? 2.6022 2.9104 3.5089 -0.1729 0.2435  -0.0588 41   HIS Y C   
26063 O O   . HIS D 41   ? 2.5859 2.9230 3.5299 -0.1567 0.2656  -0.0506 41   HIS Y O   
26064 C CB  . HIS D 41   ? 2.4876 2.8344 3.4071 -0.2258 0.1907  -0.0435 41   HIS Y CB  
26065 C CG  . HIS D 41   ? 2.5464 2.9151 3.4887 -0.2474 0.1536  -0.0208 41   HIS Y CG  
26066 N ND1 . HIS D 41   ? 2.5431 2.9626 3.5512 -0.2438 0.1437  0.0094  41   HIS Y ND1 
26067 C CD2 . HIS D 41   ? 2.5614 2.9045 3.4675 -0.2732 0.1237  -0.0226 41   HIS Y CD2 
26068 C CE1 . HIS D 41   ? 2.5347 2.9577 3.5452 -0.2668 0.1079  0.0254  41   HIS Y CE1 
26069 N NE2 . HIS D 41   ? 2.5472 2.9229 3.4948 -0.2848 0.0956  0.0062  41   HIS Y NE2 
26070 N N   . ASP D 42   ? 2.6195 2.8752 3.4670 -0.1715 0.2508  -0.0823 42   ASP Y N   
26071 C CA  . ASP D 42   ? 2.6309 2.8547 3.4471 -0.1533 0.2836  -0.1015 42   ASP Y CA  
26072 C C   . ASP D 42   ? 2.6072 2.7751 3.3673 -0.1490 0.2821  -0.1178 42   ASP Y C   
26073 O O   . ASP D 42   ? 2.6368 2.7986 3.3967 -0.1501 0.2618  -0.1099 42   ASP Y O   
26074 C CB  . ASP D 42   ? 2.6664 2.9121 3.5262 -0.1207 0.3107  -0.0859 42   ASP Y CB  
26075 C CG  . ASP D 42   ? 2.6902 2.9046 3.5198 -0.1051 0.3450  -0.1041 42   ASP Y CG  
26076 O OD1 . ASP D 42   ? 2.7138 2.8758 3.4862 -0.1038 0.3513  -0.1243 42   ASP Y OD1 
26077 O OD2 . ASP D 42   ? 2.6837 2.9238 3.5468 -0.0938 0.3654  -0.0972 42   ASP Y OD2 
26078 N N   . ILE D 43   ? 2.5576 2.6831 3.2700 -0.1447 0.3022  -0.1400 43   ILE Y N   
26079 C CA  . ILE D 43   ? 2.5399 2.6115 3.1986 -0.1401 0.3006  -0.1544 43   ILE Y CA  
26080 C C   . ILE D 43   ? 2.5317 2.5842 3.1878 -0.1060 0.3210  -0.1493 43   ILE Y C   
26081 O O   . ILE D 43   ? 2.5280 2.5557 3.1626 -0.0981 0.3117  -0.1496 43   ILE Y O   
26082 C CB  . ILE D 43   ? 2.5380 2.5656 3.1391 -0.1570 0.3059  -0.1805 43   ILE Y CB  
26083 C CG1 . ILE D 43   ? 2.5302 2.5059 3.0799 -0.1561 0.2974  -0.1920 43   ILE Y CG1 
26084 C CG2 . ILE D 43   ? 2.5799 2.5951 3.1735 -0.1438 0.3371  -0.1902 43   ILE Y CG2 
26085 C CD1 . ILE D 43   ? 2.5034 2.4341 2.9982 -0.1738 0.2994  -0.2147 43   ILE Y CD1 
26086 N N   . ARG D 44   ? 2.5400 2.6020 3.2157 -0.0855 0.3488  -0.1445 44   ARG Y N   
26087 C CA  . ARG D 44   ? 2.5811 2.6228 3.2520 -0.0517 0.3706  -0.1374 44   ARG Y CA  
26088 C C   . ARG D 44   ? 2.6511 2.7202 3.3599 -0.0374 0.3589  -0.1153 44   ARG Y C   
26089 O O   . ARG D 44   ? 2.6890 2.7291 3.3720 -0.0210 0.3597  -0.1158 44   ARG Y O   
26090 C CB  . ARG D 44   ? 2.5367 2.5841 3.2252 -0.0326 0.4032  -0.1336 44   ARG Y CB  
26091 C CG  . ARG D 44   ? 2.5056 2.4927 3.1348 -0.0256 0.4250  -0.1540 44   ARG Y CG  
26092 C CD  . ARG D 44   ? 2.4541 2.4461 3.0938 -0.0255 0.4480  -0.1595 44   ARG Y CD  
26093 N NE  . ARG D 44   ? 2.3871 2.4137 3.0458 -0.0567 0.4322  -0.1668 44   ARG Y NE  
26094 C CZ  . ARG D 44   ? 2.3436 2.3631 2.9910 -0.0691 0.4437  -0.1823 44   ARG Y CZ  
26095 N NH1 . ARG D 44   ? 2.3463 2.3214 2.9630 -0.0535 0.4710  -0.1927 44   ARG Y NH1 
26096 N NH2 . ARG D 44   ? 2.3017 2.3556 2.9658 -0.0975 0.4273  -0.1875 44   ARG Y NH2 
26097 N N   . ASP D 45   ? 2.6637 2.7877 3.4329 -0.0448 0.3466  -0.0958 45   ASP Y N   
26098 C CA  . ASP D 45   ? 2.7019 2.8569 3.5163 -0.0329 0.3347  -0.0720 45   ASP Y CA  
26099 C C   . ASP D 45   ? 2.7266 2.8626 3.5168 -0.0455 0.3050  -0.0767 45   ASP Y C   
26100 O O   . ASP D 45   ? 2.7408 2.8693 3.5324 -0.0276 0.3036  -0.0690 45   ASP Y O   
26101 C CB  . ASP D 45   ? 2.6894 2.9057 3.5737 -0.0421 0.3249  -0.0492 45   ASP Y CB  
26102 C CG  . ASP D 45   ? 2.7011 2.9412 3.6193 -0.0253 0.3550  -0.0402 45   ASP Y CG  
26103 O OD1 . ASP D 45   ? 2.7339 2.9426 3.6255 -0.0022 0.3848  -0.0478 45   ASP Y OD1 
26104 O OD2 . ASP D 45   ? 2.6817 2.9698 3.6518 -0.0351 0.3482  -0.0247 45   ASP Y OD2 
26105 N N   . LEU D 46   ? 2.7414 2.8688 3.5088 -0.0761 0.2816  -0.0892 46   LEU Y N   
26106 C CA  . LEU D 46   ? 2.7733 2.8810 3.5185 -0.0904 0.2523  -0.0933 46   LEU Y CA  
26107 C C   . LEU D 46   ? 2.8034 2.8594 3.4933 -0.0759 0.2589  -0.1095 46   LEU Y C   
26108 O O   . LEU D 46   ? 2.8146 2.8528 3.4877 -0.0804 0.2382  -0.1119 46   LEU Y O   
26109 C CB  . LEU D 46   ? 2.7691 2.8705 3.4932 -0.1252 0.2299  -0.1038 46   LEU Y CB  
26110 C CG  . LEU D 46   ? 2.7515 2.8975 3.5164 -0.1438 0.2224  -0.0919 46   LEU Y CG  
26111 C CD1 . LEU D 46   ? 2.7412 2.8736 3.4778 -0.1777 0.1956  -0.1001 46   LEU Y CD1 
26112 C CD2 . LEU D 46   ? 2.7454 2.9424 3.5802 -0.1352 0.2146  -0.0621 46   LEU Y CD2 
26113 N N   . HIS D 47   ? 2.8174 2.8473 3.4778 -0.0588 0.2869  -0.1201 47   HIS Y N   
26114 C CA  . HIS D 47   ? 2.8366 2.8162 3.4433 -0.0423 0.2954  -0.1332 47   HIS Y CA  
26115 C C   . HIS D 47   ? 2.8316 2.8182 3.4566 -0.0092 0.3100  -0.1179 47   HIS Y C   
26116 O O   . HIS D 47   ? 2.8554 2.8055 3.4402 0.0062  0.3129  -0.1248 47   HIS Y O   
26117 C CB  . HIS D 47   ? 2.8536 2.7936 3.4135 -0.0413 0.3167  -0.1515 47   HIS Y CB  
26118 C CG  . HIS D 47   ? 2.8778 2.7604 3.3750 -0.0320 0.3188  -0.1665 47   HIS Y CG  
26119 N ND1 . HIS D 47   ? 2.8832 2.7224 3.3289 -0.0471 0.3181  -0.1866 47   HIS Y ND1 
26120 C CD2 . HIS D 47   ? 2.9009 2.7625 3.3785 -0.0095 0.3204  -0.1635 47   HIS Y CD2 
26121 C CE1 . HIS D 47   ? 2.9041 2.6977 3.3020 -0.0342 0.3188  -0.1944 47   HIS Y CE1 
26122 N NE2 . HIS D 47   ? 2.9173 2.7236 3.3319 -0.0112 0.3201  -0.1813 47   HIS Y NE2 
26123 N N   . ARG D 48   ? 2.7937 2.8271 3.4789 0.0018  0.3196  -0.0961 48   ARG Y N   
26124 C CA  . ARG D 48   ? 2.7734 2.8174 3.4818 0.0340  0.3364  -0.0782 48   ARG Y CA  
26125 C C   . ARG D 48   ? 2.7126 2.7910 3.4665 0.0338  0.3143  -0.0600 48   ARG Y C   
26126 O O   . ARG D 48   ? 2.7328 2.8054 3.4857 0.0559  0.3188  -0.0521 48   ARG Y O   
26127 C CB  . ARG D 48   ? 2.7957 2.8646 3.5412 0.0511  0.3664  -0.0639 48   ARG Y CB  
26128 C CG  . ARG D 48   ? 2.8198 2.8534 3.5231 0.0508  0.3886  -0.0816 48   ARG Y CG  
26129 C CD  . ARG D 48   ? 2.8346 2.8934 3.5779 0.0667  0.4172  -0.0673 48   ARG Y CD  
26130 N NE  . ARG D 48   ? 2.8149 2.9363 3.6297 0.0550  0.4053  -0.0485 48   ARG Y NE  
26131 C CZ  . ARG D 48   ? 2.8108 2.9669 3.6762 0.0685  0.4257  -0.0304 48   ARG Y CZ  
26132 N NH1 . ARG D 48   ? 2.7832 2.9957 3.7128 0.0561  0.4112  -0.0123 48   ARG Y NH1 
26133 N NH2 . ARG D 48   ? 2.8348 2.9662 3.6853 0.0947  0.4603  -0.0292 48   ARG Y NH2 
26134 N N   . TYR D 49   ? 2.6185 2.7304 3.4103 0.0085  0.2898  -0.0527 49   TYR Y N   
26135 C CA  . TYR D 49   ? 2.5437 2.6865 3.3814 0.0050  0.2661  -0.0339 49   TYR Y CA  
26136 C C   . TYR D 49   ? 2.4952 2.6042 3.2929 -0.0051 0.2401  -0.0479 49   TYR Y C   
26137 O O   . TYR D 49   ? 2.4941 2.6101 3.3098 0.0049  0.2299  -0.0375 49   TYR Y O   
26138 C CB  . TYR D 49   ? 2.5137 2.7000 3.4036 -0.0191 0.2474  -0.0192 49   TYR Y CB  
26139 C CG  . TYR D 49   ? 2.4946 2.7231 3.4369 -0.0088 0.2697  -0.0009 49   TYR Y CG  
26140 C CD1 . TYR D 49   ? 2.4868 2.7620 3.4997 0.0032  0.2699  0.0296  49   TYR Y CD1 
26141 C CD2 . TYR D 49   ? 2.4793 2.7005 3.4018 -0.0118 0.2899  -0.0137 49   TYR Y CD2 
26142 C CE1 . TYR D 49   ? 2.4714 2.7851 3.5339 0.0132  0.2905  0.0473  49   TYR Y CE1 
26143 C CE2 . TYR D 49   ? 2.4677 2.7258 3.4372 -0.0022 0.3102  0.0019  49   TYR Y CE2 
26144 C CZ  . TYR D 49   ? 2.4641 2.7687 3.5037 0.0107  0.3107  0.0327  49   TYR Y CZ  
26145 O OH  . TYR D 49   ? 2.4541 2.7952 3.5421 0.0210  0.3315  0.0492  49   TYR Y OH  
26146 N N   . TYR D 50   ? 2.4415 2.5132 3.1855 -0.0250 0.2299  -0.0713 50   TYR Y N   
26147 C CA  . TYR D 50   ? 2.4175 2.4544 3.1219 -0.0368 0.2048  -0.0854 50   TYR Y CA  
26148 C C   . TYR D 50   ? 2.3975 2.3900 3.0461 -0.0166 0.2167  -0.1015 50   TYR Y C   
26149 O O   . TYR D 50   ? 2.3878 2.3499 3.0020 -0.0226 0.1980  -0.1137 50   TYR Y O   
26150 C CB  . TYR D 50   ? 2.4187 2.4368 3.0950 -0.0694 0.1854  -0.0997 50   TYR Y CB  
26151 C CG  . TYR D 50   ? 2.4249 2.4737 3.1444 -0.0928 0.1582  -0.0839 50   TYR Y CG  
26152 C CD1 . TYR D 50   ? 2.4369 2.5044 3.1945 -0.0896 0.1395  -0.0668 50   TYR Y CD1 
26153 C CD2 . TYR D 50   ? 2.4166 2.4731 3.1365 -0.1185 0.1499  -0.0854 50   TYR Y CD2 
26154 C CE1 . TYR D 50   ? 2.4291 2.5195 3.2241 -0.1113 0.1126  -0.0504 50   TYR Y CE1 
26155 C CE2 . TYR D 50   ? 2.4121 2.4927 3.1671 -0.1398 0.1233  -0.0690 50   TYR Y CE2 
26156 C CZ  . TYR D 50   ? 2.4215 2.5176 3.2139 -0.1362 0.1043  -0.0510 50   TYR Y CZ  
26157 O OH  . TYR D 50   ? 2.4208 2.5360 3.2464 -0.1578 0.0759  -0.0328 50   TYR Y OH  
26158 N N   . SER D 51   ? 2.3994 2.3858 3.0373 0.0074  0.2475  -0.1009 51   SER Y N   
26159 C CA  . SER D 51   ? 2.4168 2.3608 3.0011 0.0294  0.2604  -0.1125 51   SER Y CA  
26160 C C   . SER D 51   ? 2.4283 2.3903 3.0385 0.0570  0.2681  -0.0955 51   SER Y C   
26161 O O   . SER D 51   ? 2.4706 2.4022 3.0406 0.0779  0.2768  -0.1013 51   SER Y O   
26162 C CB  . SER D 51   ? 2.4043 2.3211 2.9531 0.0393  0.2888  -0.1214 51   SER Y CB  
26163 O OG  . SER D 51   ? 2.3844 2.3359 2.9783 0.0458  0.3092  -0.1064 51   SER Y OG  
26164 N N   . SER D 52   ? 2.4043 2.4161 3.0823 0.0563  0.2638  -0.0732 52   SER Y N   
26165 C CA  . SER D 52   ? 2.4139 2.4516 3.1300 0.0820  0.2740  -0.0520 52   SER Y CA  
26166 C C   . SER D 52   ? 2.4293 2.4513 3.1264 0.0889  0.2566  -0.0564 52   SER Y C   
26167 O O   . SER D 52   ? 2.4025 2.3937 3.0590 0.0725  0.2340  -0.0759 52   SER Y O   
26168 C CB  . SER D 52   ? 2.4021 2.4972 3.1990 0.0743  0.2678  -0.0263 52   SER Y CB  
26169 O OG  . SER D 52   ? 2.3907 2.4951 3.2028 0.0428  0.2334  -0.0290 52   SER Y OG  
26170 N N   . GLU D 53   ? 2.4865 2.5294 3.2136 0.1138  0.2681  -0.0378 53   GLU Y N   
26171 C CA  . GLU D 53   ? 2.5291 2.5650 3.2482 0.1211  0.2518  -0.0391 53   GLU Y CA  
26172 C C   . GLU D 53   ? 2.6168 2.6873 3.3941 0.1015  0.2217  -0.0262 53   GLU Y C   
26173 O O   . GLU D 53   ? 2.6027 2.7174 3.4467 0.1074  0.2262  0.0001  53   GLU Y O   
26174 C CB  . GLU D 53   ? 2.4801 2.5187 3.1992 0.1573  0.2782  -0.0251 53   GLU Y CB  
26175 C CG  . GLU D 53   ? 2.4348 2.4222 3.0759 0.1767  0.2976  -0.0420 53   GLU Y CG  
26176 C CD  . GLU D 53   ? 2.3859 2.3316 2.9654 0.1658  0.2735  -0.0684 53   GLU Y CD  
26177 O OE1 . GLU D 53   ? 2.3642 2.3090 2.9392 0.1740  0.2610  -0.0689 53   GLU Y OE1 
26178 O OE2 . GLU D 53   ? 2.3707 2.2839 2.9065 0.1494  0.2676  -0.0884 53   GLU Y OE2 
26179 N N   . SER D 54   ? 2.7179 2.7643 3.4681 0.0782  0.1908  -0.0440 54   SER Y N   
26180 C CA  . SER D 54   ? 2.8290 2.8945 3.6216 0.0583  0.1583  -0.0348 54   SER Y CA  
26181 C C   . SER D 54   ? 2.9819 3.0527 3.7876 0.0747  0.1516  -0.0279 54   SER Y C   
26182 O O   . SER D 54   ? 2.9933 3.0425 3.7579 0.0977  0.1665  -0.0375 54   SER Y O   
26183 C CB  . SER D 54   ? 2.8265 2.8560 3.5781 0.0286  0.1295  -0.0572 54   SER Y CB  
26184 O OG  . SER D 54   ? 2.8348 2.8653 3.6080 0.0138  0.0973  -0.0533 54   SER Y OG  
26185 N N   . PHE D 55   ? 3.1083 3.2062 3.9700 0.0620  0.1281  -0.0107 55   PHE Y N   
26186 C CA  . PHE D 55   ? 3.2494 3.3537 4.1293 0.0736  0.1179  -0.0036 55   PHE Y CA  
26187 C C   . PHE D 55   ? 3.3200 3.4289 4.2349 0.0456  0.0789  0.0027  55   PHE Y C   
26188 O O   . PHE D 55   ? 3.3174 3.4362 4.2569 0.0218  0.0646  0.0105  55   PHE Y O   
26189 C CB  . PHE D 55   ? 3.2828 3.4296 4.2169 0.1013  0.1448  0.0254  55   PHE Y CB  
26190 C CG  . PHE D 55   ? 3.3107 3.4627 4.2568 0.1181  0.1406  0.0319  55   PHE Y CG  
26191 C CD1 . PHE D 55   ? 3.3430 3.4662 4.2307 0.1414  0.1553  0.0152  55   PHE Y CD1 
26192 C CD2 . PHE D 55   ? 3.3035 3.4887 4.3190 0.1105  0.1216  0.0558  55   PHE Y CD2 
26193 C CE1 . PHE D 55   ? 3.3532 3.4821 4.2499 0.1568  0.1517  0.0206  55   PHE Y CE1 
26194 C CE2 . PHE D 55   ? 3.3111 3.5015 4.3389 0.1253  0.1179  0.0616  55   PHE Y CE2 
26195 C CZ  . PHE D 55   ? 3.3378 3.5008 4.3054 0.1487  0.1334  0.0433  55   PHE Y CZ  
26196 N N   . GLU D 56   ? 3.3985 3.4975 4.3130 0.0482  0.0610  -0.0005 56   GLU Y N   
26197 C CA  . GLU D 56   ? 3.4593 3.5546 4.4027 0.0222  0.0223  0.0049  56   GLU Y CA  
26198 C C   . GLU D 56   ? 3.4186 3.5316 4.4002 0.0352  0.0153  0.0188  56   GLU Y C   
26199 O O   . GLU D 56   ? 3.4390 3.5461 4.3939 0.0601  0.0323  0.0099  56   GLU Y O   
26200 C CB  . GLU D 56   ? 3.5683 3.6082 4.4457 0.0013  -0.0023 -0.0265 56   GLU Y CB  
26201 C CG  . GLU D 56   ? 3.6538 3.6790 4.5517 -0.0288 -0.0431 -0.0221 56   GLU Y CG  
26202 C CD  . GLU D 56   ? 3.7244 3.7413 4.6330 -0.0248 -0.0623 -0.0230 56   GLU Y CD  
26203 O OE1 . GLU D 56   ? 3.7518 3.7571 4.6250 -0.0030 -0.0492 -0.0394 56   GLU Y OE1 
26204 O OE2 . GLU D 56   ? 3.7461 3.7663 4.6969 -0.0441 -0.0916 -0.0073 56   GLU Y OE2 
26205 N N   . TYR D 57   ? 3.3500 3.4832 4.3929 0.0179  -0.0105 0.0413  57   TYR Y N   
26206 C CA  . TYR D 57   ? 3.2774 3.4317 4.3663 0.0289  -0.0170 0.0585  57   TYR Y CA  
26207 C C   . TYR D 57   ? 3.2252 3.3630 4.3379 0.0004  -0.0612 0.0627  57   TYR Y C   
26208 O O   . TYR D 57   ? 3.2378 3.3565 4.3452 -0.0278 -0.0850 0.0610  57   TYR Y O   
26209 C CB  . TYR D 57   ? 3.2362 3.4482 4.4000 0.0472  0.0077  0.0957  57   TYR Y CB  
26210 C CG  . TYR D 57   ? 3.2102 3.4429 4.3980 0.0752  0.0237  0.1079  57   TYR Y CG  
26211 C CD1 . TYR D 57   ? 3.1882 3.4631 4.4195 0.1023  0.0589  0.1345  57   TYR Y CD1 
26212 C CD2 . TYR D 57   ? 3.2090 3.4171 4.3735 0.0751  0.0044  0.0923  57   TYR Y CD2 
26213 C CE1 . TYR D 57   ? 3.1867 3.4790 4.4382 0.1285  0.0748  0.1472  57   TYR Y CE1 
26214 C CE2 . TYR D 57   ? 3.2036 3.4307 4.3879 0.1004  0.0190  0.1032  57   TYR Y CE2 
26215 C CZ  . TYR D 57   ? 3.1910 3.4601 4.4184 0.1272  0.0546  0.1314  57   TYR Y CZ  
26216 O OH  . TYR D 57   ? 3.1902 3.4767 4.4353 0.1530  0.0704  0.1437  57   TYR Y OH  
26217 N N   . SER D 58   ? 3.1459 3.2882 4.2822 0.0078  -0.0718 0.0684  58   SER Y N   
26218 C CA  . SER D 58   ? 3.0613 3.1839 4.2203 -0.0175 -0.1139 0.0726  58   SER Y CA  
26219 C C   . SER D 58   ? 2.9553 3.1081 4.1742 -0.0050 -0.1167 0.0952  58   SER Y C   
26220 O O   . SER D 58   ? 2.9239 3.1106 4.1609 0.0247  -0.0848 0.1060  58   SER Y O   
26221 C CB  . SER D 58   ? 3.0933 3.1536 4.1752 -0.0302 -0.1358 0.0336  58   SER Y CB  
26222 O OG  . SER D 58   ? 3.1118 3.1622 4.1499 -0.0050 -0.1180 0.0113  58   SER Y OG  
26223 N N   . ASN D 59   ? 2.8873 3.0243 4.1350 -0.0279 -0.1551 0.1031  59   ASN Y N   
26224 C CA  . ASN D 59   ? 2.8141 2.9783 4.1247 -0.0204 -0.1622 0.1270  59   ASN Y CA  
26225 C C   . ASN D 59   ? 2.7924 3.0183 4.1897 -0.0107 -0.1446 0.1718  59   ASN Y C   
26226 O O   . ASN D 59   ? 2.7915 3.0500 4.2465 0.0026  -0.1398 0.1961  59   ASN Y O   
26227 C CB  . ASN D 59   ? 2.7478 2.9099 4.0242 0.0080  -0.1419 0.1075  59   ASN Y CB  
26228 C CG  . ASN D 59   ? 2.6935 2.7961 3.8871 -0.0004 -0.1602 0.0637  59   ASN Y CG  
26229 O OD1 . ASN D 59   ? 2.6753 2.7589 3.8644 -0.0030 -0.1800 0.0533  59   ASN Y OD1 
26230 N ND2 . ASN D 59   ? 2.6726 2.7446 3.8006 -0.0049 -0.1537 0.0379  59   ASN Y ND2 
26231 N N   . VAL D 60   ? 2.7817 3.0233 4.1878 -0.0169 -0.1344 0.1826  60   VAL Y N   
26232 C CA  . VAL D 60   ? 2.7919 3.0913 4.2782 -0.0081 -0.1170 0.2243  60   VAL Y CA  
26233 C C   . VAL D 60   ? 2.8349 3.1438 4.3873 -0.0381 -0.1543 0.2568  60   VAL Y C   
26234 O O   . VAL D 60   ? 2.8373 3.1246 4.3707 -0.0636 -0.1749 0.2528  60   VAL Y O   
26235 C CB  . VAL D 60   ? 2.4272 2.7440 3.8917 0.0049  -0.0814 0.2206  60   VAL Y CB  
26236 C CG1 . VAL D 60   ? 2.4307 2.7489 3.8500 0.0401  -0.0396 0.2020  60   VAL Y CG1 
26237 C CG2 . VAL D 60   ? 2.4253 2.7027 3.8323 -0.0210 -0.0990 0.1962  60   VAL Y CG2 
26238 N N   . SER D 61   ? 2.8918 3.2313 4.5204 -0.0349 -0.1631 0.2902  61   SER Y N   
26239 C CA  . SER D 61   ? 2.9467 3.3007 4.6478 -0.0605 -0.1967 0.3280  61   SER Y CA  
26240 C C   . SER D 61   ? 2.9986 3.4193 4.7884 -0.0448 -0.1734 0.3737  61   SER Y C   
26241 O O   . SER D 61   ? 2.9841 3.4404 4.8087 -0.0154 -0.1429 0.3875  61   SER Y O   
26242 C CB  . SER D 61   ? 2.9567 3.2864 4.6814 -0.0763 -0.2347 0.3340  61   SER Y CB  
26243 O OG  . SER D 61   ? 2.9514 3.2986 4.7537 -0.0981 -0.2652 0.3762  61   SER Y OG  
26244 N N   . GLY D 62   ? 3.0691 3.5053 4.8949 -0.0642 -0.1883 0.3981  62   GLY Y N   
26245 C CA  . GLY D 62   ? 3.1378 3.6361 5.0469 -0.0510 -0.1677 0.4412  62   GLY Y CA  
26246 C C   . GLY D 62   ? 3.2148 3.7260 5.1909 -0.0798 -0.2060 0.4807  62   GLY Y C   
26247 O O   . GLY D 62   ? 3.2224 3.6898 5.1759 -0.1117 -0.2499 0.4746  62   GLY Y O   
26248 N N   . LYS D 63   ? 3.2831 3.8519 5.3398 -0.0683 -0.1894 0.5223  63   LYS Y N   
26249 C CA  . LYS D 63   ? 3.3443 3.9317 5.4735 -0.0931 -0.2246 0.5658  63   LYS Y CA  
26250 C C   . LYS D 63   ? 3.3675 3.9997 5.5311 -0.0889 -0.2056 0.5883  63   LYS Y C   
26251 O O   . LYS D 63   ? 3.3790 4.0607 5.5875 -0.0594 -0.1650 0.6064  63   LYS Y O   
26252 C CB  . LYS D 63   ? 3.3612 3.9757 5.5791 -0.0880 -0.2358 0.6061  63   LYS Y CB  
26253 C CG  . LYS D 63   ? 3.3645 4.0282 5.6253 -0.0472 -0.1860 0.6199  63   LYS Y CG  
26254 C CD  . LYS D 63   ? 3.3850 4.0737 5.7342 -0.0440 -0.1988 0.6608  63   LYS Y CD  
26255 C CE  . LYS D 63   ? 3.3962 4.1388 5.7977 -0.0032 -0.1474 0.6833  63   LYS Y CE  
26256 N NZ  . LYS D 63   ? 3.3953 4.1790 5.8211 0.0102  -0.1165 0.7001  63   LYS Y NZ  
26257 N N   . VAL D 64   ? 3.3678 3.9798 5.5099 -0.1193 -0.2366 0.5883  64   VAL Y N   
26258 C CA  . VAL D 64   ? 3.3442 3.9870 5.4964 -0.1212 -0.2240 0.5991  64   VAL Y CA  
26259 C C   . VAL D 64   ? 3.2676 3.9807 5.5110 -0.0989 -0.1955 0.6417  64   VAL Y C   
26260 O O   . VAL D 64   ? 3.2617 4.0048 5.5876 -0.0934 -0.2027 0.6816  64   VAL Y O   
26261 C CB  . VAL D 64   ? 3.3966 4.0119 5.5399 -0.1616 -0.2744 0.6108  64   VAL Y CB  
26262 C CG1 . VAL D 64   ? 3.4217 4.0413 5.6411 -0.1791 -0.3159 0.6555  64   VAL Y CG1 
26263 C CG2 . VAL D 64   ? 3.3956 4.0438 5.5482 -0.1649 -0.2634 0.6219  64   VAL Y CG2 
26264 N N   . GLU D 65   ? 3.1959 3.9324 5.4217 -0.0861 -0.1624 0.6319  65   GLU Y N   
26265 C CA  . GLU D 65   ? 3.1198 3.9158 5.4210 -0.0751 -0.1445 0.6702  65   GLU Y CA  
26266 C C   . GLU D 65   ? 3.0431 3.8403 5.2983 -0.0825 -0.1338 0.6504  65   GLU Y C   
26267 O O   . GLU D 65   ? 3.0401 3.8125 5.2182 -0.0730 -0.1082 0.6078  65   GLU Y O   
26268 C CB  . GLU D 65   ? 3.0733 3.9160 5.4339 -0.0343 -0.0963 0.6908  65   GLU Y CB  
26269 C CG  . GLU D 65   ? 3.0563 3.8850 5.3768 -0.0013 -0.0559 0.6628  65   GLU Y CG  
26270 C CD  . GLU D 65   ? 3.0619 3.8302 5.2839 -0.0097 -0.0658 0.6123  65   GLU Y CD  
26271 O OE1 . GLU D 65   ? 3.0591 3.7900 5.2178 -0.0359 -0.0907 0.5848  65   GLU Y OE1 
26272 O OE2 . GLU D 65   ? 3.0697 3.8282 5.2761 0.0126  -0.0455 0.6001  65   GLU Y OE2 
26273 N N   . ASN D 66   ? 2.9744 3.7987 5.2748 -0.1004 -0.1550 0.6814  66   ASN Y N   
26274 C CA  . ASN D 66   ? 2.8905 3.7203 5.1516 -0.1074 -0.1446 0.6645  66   ASN Y CA  
26275 C C   . ASN D 66   ? 2.8339 3.7159 5.1341 -0.0760 -0.0945 0.6745  66   ASN Y C   
26276 O O   . ASN D 66   ? 2.8072 3.7389 5.1953 -0.0678 -0.0914 0.7186  66   ASN Y O   
26277 C CB  . ASN D 66   ? 2.8427 3.6651 5.1094 -0.1456 -0.1941 0.6839  66   ASN Y CB  
26278 C CG  . ASN D 66   ? 2.8013 3.6390 5.1511 -0.1597 -0.2334 0.7346  66   ASN Y CG  
26279 O OD1 . ASN D 66   ? 2.7982 3.6202 5.1676 -0.1566 -0.2442 0.7417  66   ASN Y OD1 
26280 N ND2 . ASN D 66   ? 2.7700 3.6366 5.1675 -0.1765 -0.2567 0.7704  66   ASN Y ND2 
26281 N N   . TYR D 67   ? 2.8104 3.6774 5.0441 -0.0582 -0.0557 0.6339  67   TYR Y N   
26282 C CA  . TYR D 67   ? 2.7672 3.6712 5.0186 -0.0307 -0.0077 0.6351  67   TYR Y CA  
26283 C C   . TYR D 67   ? 2.7093 3.6450 4.9902 -0.0482 -0.0211 0.6541  67   TYR Y C   
26284 O O   . TYR D 67   ? 2.7237 3.7087 5.0909 -0.0397 -0.0177 0.6970  67   TYR Y O   
26285 C CB  . TYR D 67   ? 2.7741 3.6433 4.9355 -0.0144 0.0289  0.5844  67   TYR Y CB  
26286 C CG  . TYR D 67   ? 2.7462 3.6217 4.8725 -0.0152 0.0500  0.5643  67   TYR Y CG  
26287 C CD1 . TYR D 67   ? 2.7240 3.6440 4.9016 0.0076  0.0852  0.5844  67   TYR Y CD1 
26288 C CD2 . TYR D 67   ? 2.7353 3.5705 4.7768 -0.0386 0.0351  0.5251  67   TYR Y CD2 
26289 C CE1 . TYR D 67   ? 2.6890 3.6132 4.8339 0.0060  0.1036  0.5646  67   TYR Y CE1 
26290 C CE2 . TYR D 67   ? 2.7014 3.5419 4.7109 -0.0405 0.0536  0.5062  67   TYR Y CE2 
26291 C CZ  . TYR D 67   ? 2.6748 3.5598 4.7360 -0.0185 0.0874  0.5253  67   TYR Y CZ  
26292 O OH  . TYR D 67   ? 2.6439 3.5329 4.6732 -0.0208 0.1055  0.5053  67   TYR Y OH  
26293 N N   . ASN D 68   ? 2.6633 3.5714 4.8740 -0.0722 -0.0364 0.6235  68   ASN Y N   
26294 C CA  . ASN D 68   ? 2.6483 3.5794 4.8793 -0.0965 -0.0617 0.6418  68   ASN Y CA  
26295 C C   . ASN D 68   ? 2.8482 3.7446 5.0484 -0.1380 -0.1197 0.6438  68   ASN Y C   
26296 O O   . ASN D 68   ? 2.8758 3.7799 5.1312 -0.1520 -0.1559 0.6814  68   ASN Y O   
26297 C CB  . ASN D 68   ? 2.6712 3.6127 4.8637 -0.0897 -0.0297 0.6158  68   ASN Y CB  
26298 C CG  . ASN D 68   ? 2.7490 3.6369 4.8333 -0.1008 -0.0261 0.5618  68   ASN Y CG  
26299 O OD1 . ASN D 68   ? 2.7970 3.6389 4.8314 -0.1168 -0.0511 0.5436  68   ASN Y OD1 
26300 N ND2 . ASN D 68   ? 2.7614 3.6543 4.8104 -0.0919 0.0059  0.5365  68   ASN Y ND2 
26301 N N   . GLY D 69   ? 2.8315 3.6860 4.9424 -0.1571 -0.1281 0.6044  69   GLY Y N   
26302 C CA  . GLY D 69   ? 2.8182 3.6387 4.8919 -0.1960 -0.1787 0.6057  69   GLY Y CA  
26303 C C   . GLY D 69   ? 2.8082 3.5929 4.8887 -0.2143 -0.2221 0.6217  69   GLY Y C   
26304 O O   . GLY D 69   ? 2.8102 3.5988 4.9274 -0.2379 -0.2641 0.6572  69   GLY Y O   
26305 N N   . SER D 70   ? 2.7752 3.5232 4.8194 -0.2040 -0.2130 0.5960  70   SER Y N   
26306 C CA  . SER D 70   ? 2.7326 3.4346 4.7643 -0.2238 -0.2542 0.6009  70   SER Y CA  
26307 C C   . SER D 70   ? 2.6543 3.3410 4.6867 -0.2021 -0.2373 0.5876  70   SER Y C   
26308 O O   . SER D 70   ? 2.6518 3.3085 4.6916 -0.2149 -0.2696 0.5975  70   SER Y O   
26309 C CB  . SER D 70   ? 2.7526 3.3924 4.6906 -0.2538 -0.2820 0.5701  70   SER Y CB  
26310 O OG  . SER D 70   ? 2.7502 3.3942 4.6880 -0.2802 -0.3112 0.5894  70   SER Y OG  
26311 N N   . ASN D 71   ? 2.5826 3.2859 4.6031 -0.1701 -0.1881 0.5646  71   ASN Y N   
26312 C CA  . ASN D 71   ? 2.5339 3.2132 4.5334 -0.1515 -0.1729 0.5441  71   ASN Y CA  
26313 C C   . ASN D 71   ? 2.4956 3.1957 4.4862 -0.1136 -0.1166 0.5246  71   ASN Y C   
26314 O O   . ASN D 71   ? 2.4955 3.2208 4.4828 -0.1027 -0.0873 0.5193  71   ASN Y O   
26315 C CB  . ASN D 71   ? 2.5175 3.1276 4.4248 -0.1727 -0.1965 0.5050  71   ASN Y CB  
26316 C CG  . ASN D 71   ? 2.4983 3.0747 4.4126 -0.1818 -0.2279 0.5109  71   ASN Y CG  
26317 O OD1 . ASN D 71   ? 2.4780 3.0826 4.4619 -0.1686 -0.2269 0.5397  71   ASN Y OD1 
26318 N ND2 . ASN D 71   ? 2.5036 3.0176 4.3451 -0.2047 -0.2558 0.4835  71   ASN Y ND2 
26319 N N   . VAL D 72   ? 2.4684 3.1543 4.4525 -0.0943 -0.1032 0.5143  72   VAL Y N   
26320 C CA  . VAL D 72   ? 2.4534 3.1448 4.4147 -0.0584 -0.0530 0.4931  72   VAL Y CA  
26321 C C   . VAL D 72   ? 2.4725 3.1520 4.4456 -0.0439 -0.0532 0.4951  72   VAL Y C   
26322 O O   . VAL D 72   ? 2.4425 3.1355 4.4776 -0.0521 -0.0795 0.5274  72   VAL Y O   
26323 C CB  . VAL D 72   ? 2.4494 3.1958 4.4683 -0.0314 -0.0122 0.5168  72   VAL Y CB  
26324 C CG1 . VAL D 72   ? 2.4612 3.2231 4.5066 0.0061  0.0255  0.5244  72   VAL Y CG1 
26325 C CG2 . VAL D 72   ? 2.4457 3.1863 4.4090 -0.0290 0.0134  0.4876  72   VAL Y CG2 
26326 N N   . VAL D 73   ? 2.5162 3.1708 4.4306 -0.0223 -0.0242 0.4617  73   VAL Y N   
26327 C CA  . VAL D 73   ? 2.5488 3.1800 4.4509 -0.0134 -0.0296 0.4530  73   VAL Y CA  
26328 C C   . VAL D 73   ? 2.5373 3.1782 4.4264 0.0268  0.0205  0.4436  73   VAL Y C   
26329 O O   . VAL D 73   ? 2.5174 3.1813 4.4107 0.0464  0.0574  0.4461  73   VAL Y O   
26330 C CB  . VAL D 73   ? 1.9365 2.5052 3.7499 -0.0365 -0.0569 0.4113  73   VAL Y CB  
26331 C CG1 . VAL D 73   ? 1.9509 2.4873 3.7240 -0.0235 -0.0537 0.3877  73   VAL Y CG1 
26332 C CG2 . VAL D 73   ? 1.9360 2.4854 3.7534 -0.0764 -0.1071 0.4206  73   VAL Y CG2 
26333 N N   . ARG D 74   ? 2.5420 3.1635 4.4138 0.0391  0.0216  0.4334  74   ARG Y N   
26334 C CA  . ARG D 74   ? 2.5618 3.1816 4.4045 0.0760  0.0660  0.4204  74   ARG Y CA  
26335 C C   . ARG D 74   ? 2.6085 3.1932 4.4088 0.0806  0.0561  0.3984  74   ARG Y C   
26336 O O   . ARG D 74   ? 2.6245 3.1970 4.4422 0.0593  0.0174  0.4033  74   ARG Y O   
26337 C CB  . ARG D 74   ? 2.5401 3.2123 4.4632 0.1051  0.0994  0.4616  74   ARG Y CB  
26338 C CG  . ARG D 74   ? 2.5439 3.2409 4.5439 0.1064  0.0826  0.4973  74   ARG Y CG  
26339 C CD  . ARG D 74   ? 2.5376 3.2878 4.6216 0.1342  0.1164  0.5414  74   ARG Y CD  
26340 N NE  . ARG D 74   ? 2.5150 3.2986 4.6483 0.1233  0.1143  0.5652  74   ARG Y NE  
26341 C CZ  . ARG D 74   ? 2.4957 3.3102 4.7088 0.1033  0.0835  0.6029  74   ARG Y CZ  
26342 N NH1 . ARG D 74   ? 2.4986 3.3130 4.7528 0.0914  0.0519  0.6216  74   ARG Y NH1 
26343 N NH2 . ARG D 74   ? 2.4746 3.3187 4.7258 0.0948  0.0833  0.6223  74   ARG Y NH2 
26344 N N   . PHE D 75   ? 2.6516 3.2179 4.3942 0.1082  0.0904  0.3743  75   PHE Y N   
26345 C CA  . PHE D 75   ? 2.6971 3.2309 4.3928 0.1162  0.0852  0.3514  75   PHE Y CA  
26346 C C   . PHE D 75   ? 2.6497 3.1776 4.3046 0.1548  0.1304  0.3406  75   PHE Y C   
26347 O O   . PHE D 75   ? 2.6466 3.1676 4.2623 0.1691  0.1613  0.3283  75   PHE Y O   
26348 C CB  . PHE D 75   ? 2.7926 3.2735 4.4118 0.0889  0.0525  0.3108  75   PHE Y CB  
26349 C CG  . PHE D 75   ? 2.8813 3.3481 4.5227 0.0631  0.0066  0.3151  75   PHE Y CG  
26350 C CD1 . PHE D 75   ? 2.9259 3.3799 4.5600 0.0728  0.0008  0.3087  75   PHE Y CD1 
26351 C CD2 . PHE D 75   ? 2.9078 3.3725 4.5770 0.0292  -0.0310 0.3268  75   PHE Y CD2 
26352 C CE1 . PHE D 75   ? 2.9488 3.3867 4.6038 0.0487  -0.0416 0.3124  75   PHE Y CE1 
26353 C CE2 . PHE D 75   ? 2.9323 3.3780 4.6201 0.0052  -0.0738 0.3321  75   PHE Y CE2 
26354 C CZ  . PHE D 75   ? 2.9487 3.3807 4.6305 0.0148  -0.0791 0.3244  75   PHE Y CZ  
26355 N N   . ASN D 76   ? 2.6067 3.1345 4.2690 0.1707  0.1328  0.3455  76   ASN Y N   
26356 C CA  . ASN D 76   ? 2.5699 3.0892 4.1919 0.2078  0.1727  0.3381  76   ASN Y CA  
26357 C C   . ASN D 76   ? 2.5370 3.0030 4.0593 0.2061  0.1642  0.2920  76   ASN Y C   
26358 O O   . ASN D 76   ? 2.5385 2.9895 4.0489 0.2017  0.1430  0.2818  76   ASN Y O   
26359 C CB  . ASN D 76   ? 2.5540 3.1056 4.2416 0.2275  0.1819  0.3720  76   ASN Y CB  
26360 C CG  . ASN D 76   ? 2.5548 3.1094 4.2210 0.2702  0.2319  0.3791  76   ASN Y CG  
26361 O OD1 . ASN D 76   ? 2.5638 3.0811 4.1475 0.2846  0.2447  0.3488  76   ASN Y OD1 
26362 N ND2 . ASN D 76   ? 2.5432 3.1399 4.2829 0.2909  0.2601  0.4209  76   ASN Y ND2 
26363 N N   . PRO D 77   ? 2.5218 2.9586 3.9731 0.2092  0.1803  0.2643  77   PRO Y N   
26364 C CA  . PRO D 77   ? 2.5254 2.9096 3.8795 0.2047  0.1719  0.2200  77   PRO Y CA  
26365 C C   . PRO D 77   ? 2.5731 2.9352 3.8715 0.2346  0.1933  0.2063  77   PRO Y C   
26366 O O   . PRO D 77   ? 2.5795 2.8991 3.8022 0.2289  0.1806  0.1710  77   PRO Y O   
26367 C CB  . PRO D 77   ? 2.5105 2.8806 3.8244 0.2030  0.1901  0.2059  77   PRO Y CB  
26368 C CG  . PRO D 77   ? 2.4956 2.9067 3.8695 0.2236  0.2243  0.2410  77   PRO Y CG  
26369 C CD  . PRO D 77   ? 2.4874 2.9410 3.9544 0.2117  0.2031  0.2751  77   PRO Y CD  
26370 N N   . LYS D 78   ? 2.6124 3.0015 3.9463 0.2655  0.2246  0.2345  78   LYS Y N   
26371 C CA  . LYS D 78   ? 2.6711 3.0423 3.9553 0.2978  0.2493  0.2279  78   LYS Y CA  
26372 C C   . LYS D 78   ? 2.7991 3.1660 4.0563 0.3324  0.2990  0.2383  78   LYS Y C   
26373 O O   . LYS D 78   ? 2.8392 3.1889 4.0520 0.3616  0.3228  0.2364  78   LYS Y O   
26374 C CB  . LYS D 78   ? 2.6109 2.9342 3.8083 0.2898  0.2271  0.1856  78   LYS Y CB  
26375 C CG  . LYS D 78   ? 2.5586 2.8378 3.6701 0.2856  0.2315  0.1516  78   LYS Y CG  
26376 C CD  . LYS D 78   ? 2.5452 2.8070 3.6047 0.3204  0.2749  0.1527  78   LYS Y CD  
26377 C CE  . LYS D 78   ? 2.5210 2.7558 3.5332 0.3130  0.2838  0.1345  78   LYS Y CE  
26378 N NZ  . LYS D 78   ? 2.5314 2.7528 3.5094 0.3461  0.3283  0.1439  78   LYS Y NZ  
26379 N N   . ASP D 79   ? 2.8713 3.2523 4.1551 0.3292  0.3140  0.2503  79   ASP Y N   
26380 C CA  . ASP D 79   ? 2.9627 3.3326 4.2172 0.3584  0.3593  0.2574  79   ASP Y CA  
26381 C C   . ASP D 79   ? 3.0110 3.4214 4.3430 0.3602  0.3781  0.2905  79   ASP Y C   
26382 O O   . ASP D 79   ? 3.0207 3.4322 4.3534 0.3894  0.4192  0.3085  79   ASP Y O   
26383 C CB  . ASP D 79   ? 2.9787 3.2974 4.1384 0.3523  0.3595  0.2188  79   ASP Y CB  
26384 C CG  . ASP D 79   ? 3.0122 3.3032 4.1193 0.3856  0.4043  0.2209  79   ASP Y CG  
26385 O OD1 . ASP D 79   ? 3.0105 3.3204 4.1565 0.3973  0.4323  0.2443  79   ASP Y OD1 
26386 O OD2 . ASP D 79   ? 3.0397 3.2868 4.0638 0.3995  0.4106  0.1991  79   ASP Y OD2 
26387 N N   . GLN D 80   ? 3.0463 3.4874 4.4413 0.3294  0.3475  0.2990  80   GLN Y N   
26388 C CA  . GLN D 80   ? 3.0901 3.5735 4.5637 0.3278  0.3596  0.3310  80   GLN Y CA  
26389 C C   . GLN D 80   ? 3.0942 3.6152 4.6477 0.2967  0.3197  0.3489  80   GLN Y C   
26390 O O   . GLN D 80   ? 3.0902 3.6159 4.6631 0.2878  0.2936  0.3517  80   GLN Y O   
26391 C CB  . GLN D 80   ? 3.1048 3.5706 4.5412 0.3216  0.3727  0.3140  80   GLN Y CB  
26392 C CG  . GLN D 80   ? 3.1072 3.5492 4.5016 0.2849  0.3355  0.2798  80   GLN Y CG  
26393 C CD  . GLN D 80   ? 3.1420 3.5277 4.4331 0.2883  0.3360  0.2399  80   GLN Y CD  
26394 O OE1 . GLN D 80   ? 3.1437 3.5033 4.3899 0.2631  0.3131  0.2106  80   GLN Y OE1 
26395 N NE2 . GLN D 80   ? 3.1703 3.5359 4.4221 0.3200  0.3626  0.2401  80   GLN Y NE2 
26396 N N   . ASN D 81   ? 3.1103 3.6561 4.7084 0.2800  0.3145  0.3612  81   ASN Y N   
26397 C CA  . ASN D 81   ? 3.1170 3.6946 4.7863 0.2486  0.2751  0.3794  81   ASN Y CA  
26398 C C   . ASN D 81   ? 3.1551 3.7339 4.8210 0.2221  0.2609  0.3694  81   ASN Y C   
26399 O O   . ASN D 81   ? 3.1501 3.7545 4.8513 0.2302  0.2837  0.3878  81   ASN Y O   
26400 C CB  . ASN D 81   ? 3.0758 3.7055 4.8471 0.2628  0.2863  0.4290  81   ASN Y CB  
26401 C CG  . ASN D 81   ? 3.0525 3.6866 4.8452 0.2733  0.2791  0.4413  81   ASN Y CG  
26402 O OD1 . ASN D 81   ? 3.0324 3.6675 4.8474 0.2481  0.2381  0.4412  81   ASN Y OD1 
26403 N ND2 . ASN D 81   ? 3.0593 3.6935 4.8437 0.3105  0.3190  0.4526  81   ASN Y ND2 
26404 N N   . HIS D 82   ? 3.2037 3.7539 4.8267 0.1904  0.2233  0.3408  82   HIS Y N   
26405 C CA  . HIS D 82   ? 3.2411 3.7818 4.8399 0.1651  0.2103  0.3239  82   HIS Y CA  
26406 C C   . HIS D 82   ? 3.1710 3.7482 4.8432 0.1385  0.1821  0.3510  82   HIS Y C   
26407 O O   . HIS D 82   ? 3.1415 3.7588 4.8953 0.1432  0.1789  0.3890  82   HIS Y O   
26408 C CB  . HIS D 82   ? 3.3424 3.8317 4.8573 0.1437  0.1843  0.2814  82   HIS Y CB  
26409 C CG  . HIS D 82   ? 3.4412 3.8899 4.8720 0.1654  0.2113  0.2505  82   HIS Y CG  
26410 N ND1 . HIS D 82   ? 3.4749 3.9095 4.8635 0.1762  0.2410  0.2365  82   HIS Y ND1 
26411 C CD2 . HIS D 82   ? 3.4893 3.9065 4.8687 0.1776  0.2113  0.2311  82   HIS Y CD2 
26412 C CE1 . HIS D 82   ? 3.5074 3.9020 4.8224 0.1941  0.2577  0.2115  82   HIS Y CE1 
26413 N NE2 . HIS D 82   ? 3.5169 3.9015 4.8244 0.1956  0.2403  0.2077  82   HIS Y NE2 
26414 N N   . GLN D 83   ? 3.1419 3.7030 4.7821 0.1104  0.1612  0.3318  83   GLN Y N   
26415 C CA  . GLN D 83   ? 3.0996 3.6866 4.7933 0.0813  0.1299  0.3530  83   GLN Y CA  
26416 C C   . GLN D 83   ? 3.1097 3.6571 4.7423 0.0471  0.0957  0.3223  83   GLN Y C   
26417 O O   . GLN D 83   ? 3.1266 3.6343 4.6804 0.0484  0.1053  0.2858  83   GLN Y O   
26418 C CB  . GLN D 83   ? 3.0461 3.6716 4.7821 0.0903  0.1559  0.3733  83   GLN Y CB  
26419 C CG  . GLN D 83   ? 2.9928 3.6501 4.7895 0.0626  0.1247  0.3999  83   GLN Y CG  
26420 C CD  . GLN D 83   ? 2.9541 3.6549 4.8023 0.0754  0.1521  0.4239  83   GLN Y CD  
26421 O OE1 . GLN D 83   ? 2.9587 3.6584 4.7855 0.1019  0.1943  0.4146  83   GLN Y OE1 
26422 N NE2 . GLN D 83   ? 2.9210 3.6579 4.8361 0.0566  0.1277  0.4554  83   GLN Y NE2 
26423 N N   . LEU D 84   ? 3.0954 3.6509 4.7634 0.0167  0.0558  0.3388  84   LEU Y N   
26424 C CA  . LEU D 84   ? 3.0780 3.5933 4.6901 -0.0166 0.0217  0.3138  84   LEU Y CA  
26425 C C   . LEU D 84   ? 3.0093 3.5463 4.6662 -0.0451 -0.0084 0.3390  84   LEU Y C   
26426 O O   . LEU D 84   ? 3.0200 3.5842 4.7475 -0.0517 -0.0293 0.3744  84   LEU Y O   
26427 C CB  . LEU D 84   ? 3.1355 3.6092 4.7142 -0.0271 -0.0072 0.2978  84   LEU Y CB  
26428 C CG  . LEU D 84   ? 3.1751 3.6039 4.7064 -0.0632 -0.0485 0.2793  84   LEU Y CG  
26429 C CD1 . LEU D 84   ? 3.1817 3.5820 4.6386 -0.0700 -0.0364 0.2458  84   LEU Y CD1 
26430 C CD2 . LEU D 84   ? 3.2053 3.5930 4.7068 -0.0685 -0.0723 0.2637  84   LEU Y CD2 
26431 N N   . PHE D 85   ? 2.9158 3.4397 4.5306 -0.0622 -0.0108 0.3214  85   PHE Y N   
26432 C CA  . PHE D 85   ? 2.8330 3.3754 4.4804 -0.0892 -0.0380 0.3431  85   PHE Y CA  
26433 C C   . PHE D 85   ? 2.7797 3.2744 4.3789 -0.1245 -0.0820 0.3292  85   PHE Y C   
26434 O O   . PHE D 85   ? 2.8014 3.2583 4.3268 -0.1352 -0.0811 0.2962  85   PHE Y O   
26435 C CB  . PHE D 85   ? 2.8031 3.3682 4.4428 -0.0849 -0.0111 0.3374  85   PHE Y CB  
26436 C CG  . PHE D 85   ? 2.7970 3.4111 4.4950 -0.0531 0.0286  0.3588  85   PHE Y CG  
26437 C CD1 . PHE D 85   ? 2.8118 3.4224 4.5007 -0.0203 0.0638  0.3499  85   PHE Y CD1 
26438 C CD2 . PHE D 85   ? 2.7866 3.4479 4.5459 -0.0557 0.0310  0.3884  85   PHE Y CD2 
26439 C CE1 . PHE D 85   ? 2.8130 3.4630 4.5518 0.0097  0.1017  0.3707  85   PHE Y CE1 
26440 C CE2 . PHE D 85   ? 2.7850 3.4883 4.5975 -0.0256 0.0689  0.4085  85   PHE Y CE2 
26441 C CZ  . PHE D 85   ? 2.8011 3.4973 4.6029 0.0073  0.1049  0.4000  85   PHE Y CZ  
26442 N N   . LEU D 86   ? 2.7109 3.2046 4.3519 -0.1422 -0.1202 0.3560  86   LEU Y N   
26443 C CA  . LEU D 86   ? 2.6420 3.0882 4.2435 -0.1768 -0.1648 0.3498  86   LEU Y CA  
26444 C C   . LEU D 86   ? 2.5721 3.0360 4.1903 -0.2001 -0.1831 0.3699  86   LEU Y C   
26445 O O   . LEU D 86   ? 2.5425 3.0544 4.2356 -0.1983 -0.1865 0.4074  86   LEU Y O   
26446 C CB  . LEU D 86   ? 2.6367 3.0690 4.2746 -0.1850 -0.1984 0.3704  86   LEU Y CB  
26447 C CG  . LEU D 86   ? 2.6429 3.0081 4.2248 -0.2116 -0.2382 0.3533  86   LEU Y CG  
26448 C CD1 . LEU D 86   ? 2.6495 2.9689 4.1417 -0.2059 -0.2210 0.3054  86   LEU Y CD1 
26449 C CD2 . LEU D 86   ? 2.6484 3.0056 4.2727 -0.2122 -0.2623 0.3719  86   LEU Y CD2 
26450 N N   . LEU D 87   ? 2.5434 2.9696 4.0922 -0.2213 -0.1940 0.3459  87   LEU Y N   
26451 C CA  . LEU D 87   ? 2.4882 2.9268 4.0436 -0.2450 -0.2130 0.3631  87   LEU Y CA  
26452 C C   . LEU D 87   ? 2.5635 2.9438 4.0342 -0.2727 -0.2346 0.3377  87   LEU Y C   
26453 O O   . LEU D 87   ? 2.5547 2.9411 4.0053 -0.2871 -0.2363 0.3370  87   LEU Y O   
26454 C CB  . LEU D 87   ? 2.3636 2.8592 3.9520 -0.2281 -0.1774 0.3694  87   LEU Y CB  
26455 C CG  . LEU D 87   ? 2.2555 2.7543 3.8035 -0.2042 -0.1301 0.3347  87   LEU Y CG  
26456 C CD1 . LEU D 87   ? 2.2261 2.6910 3.6966 -0.2232 -0.1316 0.3043  87   LEU Y CD1 
26457 C CD2 . LEU D 87   ? 2.1913 2.7518 3.8011 -0.1800 -0.0957 0.3532  87   LEU Y CD2 
26458 N N   . GLY D 88   ? 2.6336 2.9567 4.0547 -0.2795 -0.2504 0.3171  88   GLY Y N   
26459 C CA  . GLY D 88   ? 2.7279 2.9886 4.0695 -0.3053 -0.2726 0.2956  88   GLY Y CA  
26460 C C   . GLY D 88   ? 2.8451 3.0756 4.1959 -0.3350 -0.3226 0.3236  88   GLY Y C   
26461 O O   . GLY D 88   ? 2.8522 3.1069 4.2704 -0.3345 -0.3404 0.3569  88   GLY Y O   
26462 N N   . LYS D 89   ? 2.9576 3.1326 4.2405 -0.3609 -0.3455 0.3120  89   LYS Y N   
26463 C CA  . LYS D 89   ? 3.0870 3.2217 4.3677 -0.3904 -0.3946 0.3383  89   LYS Y CA  
26464 C C   . LYS D 89   ? 3.2051 3.3076 4.5024 -0.3891 -0.4160 0.3432  89   LYS Y C   
26465 O O   . LYS D 89   ? 3.2380 3.3167 4.5565 -0.4091 -0.4567 0.3723  89   LYS Y O   
26466 C CB  . LYS D 89   ? 3.0990 3.1702 4.2928 -0.4159 -0.4114 0.3213  89   LYS Y CB  
26467 C CG  . LYS D 89   ? 3.1324 3.1548 4.3156 -0.4471 -0.4623 0.3498  89   LYS Y CG  
26468 C CD  . LYS D 89   ? 3.1293 3.2028 4.3808 -0.4555 -0.4802 0.3941  89   LYS Y CD  
26469 C CE  . LYS D 89   ? 3.1767 3.1970 4.4167 -0.4867 -0.5334 0.4252  89   LYS Y CE  
26470 N NZ  . LYS D 89   ? 3.1749 3.2442 4.4775 -0.4961 -0.5522 0.4695  89   LYS Y NZ  
26471 N N   . ASP D 90   ? 3.2794 3.3797 4.5651 -0.3657 -0.3892 0.3145  90   ASP Y N   
26472 C CA  . ASP D 90   ? 3.3446 3.4213 4.6473 -0.3600 -0.4034 0.3147  90   ASP Y CA  
26473 C C   . ASP D 90   ? 3.3110 3.4510 4.7088 -0.3419 -0.3967 0.3456  90   ASP Y C   
26474 O O   . ASP D 90   ? 3.3294 3.4561 4.7551 -0.3402 -0.4137 0.3545  90   ASP Y O   
26475 C CB  . ASP D 90   ? 3.3961 3.4430 4.6426 -0.3423 -0.3781 0.2707  90   ASP Y CB  
26476 C CG  . ASP D 90   ? 3.4487 3.4190 4.6043 -0.3618 -0.3928 0.2429  90   ASP Y CG  
26477 O OD1 . ASP D 90   ? 3.4754 3.4091 4.6098 -0.3897 -0.4254 0.2586  90   ASP Y OD1 
26478 O OD2 . ASP D 90   ? 3.4635 3.4085 4.5677 -0.3490 -0.3718 0.2067  90   ASP Y OD2 
26479 N N   . LYS D 91   ? 3.2562 3.4635 4.7031 -0.3280 -0.3709 0.3617  91   LYS Y N   
26480 C CA  . LYS D 91   ? 3.2044 3.4749 4.7452 -0.3100 -0.3618 0.3950  91   LYS Y CA  
26481 C C   . LYS D 91   ? 3.1521 3.4303 4.7523 -0.3321 -0.4039 0.4421  91   LYS Y C   
26482 O O   . LYS D 91   ? 3.1525 3.4570 4.8233 -0.3241 -0.4116 0.4699  91   LYS Y O   
26483 C CB  . LYS D 91   ? 3.2068 3.5436 4.7794 -0.2865 -0.3184 0.3966  91   LYS Y CB  
26484 C CG  . LYS D 91   ? 3.2235 3.6246 4.8935 -0.2656 -0.3055 0.4321  91   LYS Y CG  
26485 C CD  . LYS D 91   ? 3.2262 3.6891 4.9434 -0.2580 -0.2850 0.4537  91   LYS Y CD  
26486 C CE  . LYS D 91   ? 3.2478 3.7340 5.0308 -0.2780 -0.3213 0.5020  91   LYS Y CE  
26487 N NZ  . LYS D 91   ? 3.2712 3.7137 5.0038 -0.3134 -0.3603 0.5026  91   LYS Y NZ  
26488 N N   . GLU D 92   ? 3.0777 3.3332 4.6495 -0.3596 -0.4309 0.4526  92   GLU Y N   
26489 C CA  . GLU D 92   ? 3.0023 3.2574 4.6216 -0.3833 -0.4749 0.4983  92   GLU Y CA  
26490 C C   . GLU D 92   ? 3.0272 3.2241 4.6417 -0.3979 -0.5131 0.5046  92   GLU Y C   
26491 O O   . GLU D 92   ? 3.0291 3.2200 4.6893 -0.4159 -0.5517 0.5440  92   GLU Y O   
26492 C CB  . GLU D 92   ? 2.9172 3.1518 4.4929 -0.4102 -0.4961 0.5051  92   GLU Y CB  
26493 C CG  . GLU D 92   ? 2.8437 3.0886 4.4730 -0.4324 -0.5382 0.5564  92   GLU Y CG  
26494 C CD  . GLU D 92   ? 2.7566 3.0784 4.4937 -0.4134 -0.5267 0.5930  92   GLU Y CD  
26495 O OE1 . GLU D 92   ? 2.7013 3.0843 4.4677 -0.3872 -0.4829 0.5845  92   GLU Y OE1 
26496 O OE2 . GLU D 92   ? 2.7508 3.0692 4.5434 -0.4246 -0.5614 0.6314  92   GLU Y OE2 
26497 N N   . GLN D 93   ? 3.0431 3.1956 4.6011 -0.3903 -0.5023 0.4654  93   GLN Y N   
26498 C CA  . GLN D 93   ? 3.0736 3.1721 4.6246 -0.3992 -0.5317 0.4637  93   GLN Y CA  
26499 C C   . GLN D 93   ? 3.0792 3.2158 4.6815 -0.3699 -0.5062 0.4591  93   GLN Y C   
26500 O O   . GLN D 93   ? 3.1081 3.2074 4.7089 -0.3729 -0.5249 0.4542  93   GLN Y O   
26501 C CB  . GLN D 93   ? 3.0719 3.0886 4.5208 -0.4119 -0.5399 0.4229  93   GLN Y CB  
26502 C CG  . GLN D 93   ? 3.0581 3.0373 4.4447 -0.4365 -0.5555 0.4212  93   GLN Y CG  
26503 C CD  . GLN D 93   ? 3.0537 2.9596 4.3402 -0.4432 -0.5531 0.3783  93   GLN Y CD  
26504 O OE1 . GLN D 93   ? 3.0454 2.9311 4.3081 -0.4284 -0.5383 0.3476  93   GLN Y OE1 
26505 N NE2 . GLN D 93   ? 3.0591 2.9245 4.2858 -0.4652 -0.5673 0.3768  93   GLN Y NE2 
26506 N N   . TYR D 94   ? 3.0658 3.2742 4.7113 -0.3416 -0.4634 0.4609  94   TYR Y N   
26507 C CA  . TYR D 94   ? 3.0734 3.3190 4.7599 -0.3104 -0.4326 0.4551  94   TYR Y CA  
26508 C C   . TYR D 94   ? 2.9767 3.3063 4.7470 -0.2860 -0.4011 0.4842  94   TYR Y C   
26509 O O   . TYR D 94   ? 2.9509 3.3141 4.7238 -0.2554 -0.3572 0.4668  94   TYR Y O   
26510 C CB  . TYR D 94   ? 3.1658 3.3890 4.7789 -0.2915 -0.3989 0.4042  94   TYR Y CB  
26511 C CG  . TYR D 94   ? 3.2800 3.4473 4.8556 -0.2940 -0.4152 0.3805  94   TYR Y CG  
26512 C CD1 . TYR D 94   ? 3.3136 3.4971 4.9445 -0.2824 -0.4192 0.3953  94   TYR Y CD1 
26513 C CD2 . TYR D 94   ? 3.3411 3.4396 4.8263 -0.3075 -0.4256 0.3434  94   TYR Y CD2 
26514 C CE1 . TYR D 94   ? 3.3567 3.4895 4.9525 -0.2849 -0.4344 0.3721  94   TYR Y CE1 
26515 C CE2 . TYR D 94   ? 3.3841 3.4308 4.8345 -0.3093 -0.4403 0.3207  94   TYR Y CE2 
26516 C CZ  . TYR D 94   ? 3.3884 3.4526 4.8936 -0.2983 -0.4451 0.3343  94   TYR Y CZ  
26517 O OH  . TYR D 94   ? 3.4144 3.4270 4.8839 -0.3005 -0.4603 0.3102  94   TYR Y OH  
26518 N N   . LYS D 95   ? 2.9141 3.2748 4.7507 -0.2991 -0.4233 0.5293  95   LYS Y N   
26519 C CA  . LYS D 95   ? 2.8280 3.2664 4.7546 -0.2765 -0.3974 0.5627  95   LYS Y CA  
26520 C C   . LYS D 95   ? 2.8046 3.2598 4.7964 -0.2621 -0.3984 0.5827  95   LYS Y C   
26521 O O   . LYS D 95   ? 2.7974 3.3138 4.8690 -0.2414 -0.3769 0.6130  95   LYS Y O   
26522 C CB  . LYS D 95   ? 2.7853 3.2516 4.7626 -0.2959 -0.4228 0.6061  95   LYS Y CB  
26523 C CG  . LYS D 95   ? 2.7404 3.2162 4.6750 -0.3018 -0.4096 0.5929  95   LYS Y CG  
26524 C CD  . LYS D 95   ? 2.7046 3.2237 4.7048 -0.3139 -0.4280 0.6398  95   LYS Y CD  
26525 C CE  . LYS D 95   ? 2.6715 3.2055 4.6320 -0.3182 -0.4125 0.6261  95   LYS Y CE  
26526 N NZ  . LYS D 95   ? 2.6448 3.2304 4.6741 -0.3250 -0.4243 0.6709  95   LYS Y NZ  
26527 N N   . GLU D 96   ? 2.7862 3.1853 4.7433 -0.2732 -0.4234 0.5659  96   GLU Y N   
26528 C CA  . GLU D 96   ? 2.7499 3.1559 4.7622 -0.2639 -0.4304 0.5825  96   GLU Y CA  
26529 C C   . GLU D 96   ? 2.7128 3.1438 4.7186 -0.2270 -0.3825 0.5566  96   GLU Y C   
26530 O O   . GLU D 96   ? 2.6962 3.1767 4.7751 -0.2047 -0.3628 0.5823  96   GLU Y O   
26531 C CB  . GLU D 96   ? 2.7670 3.0979 4.7404 -0.2921 -0.4782 0.5730  96   GLU Y CB  
26532 C CG  . GLU D 96   ? 2.7777 3.0457 4.6435 -0.2955 -0.4738 0.5180  96   GLU Y CG  
26533 C CD  . GLU D 96   ? 2.8130 2.9994 4.6303 -0.3301 -0.5249 0.5118  96   GLU Y CD  
26534 O OE1 . GLU D 96   ? 2.8247 2.9968 4.6644 -0.3569 -0.5627 0.5451  96   GLU Y OE1 
26535 O OE2 . GLU D 96   ? 2.8302 2.9641 4.5846 -0.3302 -0.5274 0.4741  96   GLU Y OE2 
26536 N N   . GLY D 97   ? 2.7009 3.0953 4.6180 -0.2205 -0.3644 0.5074  97   GLY Y N   
26537 C CA  . GLY D 97   ? 2.6764 3.0853 4.5729 -0.1870 -0.3213 0.4798  97   GLY Y CA  
26538 C C   . GLY D 97   ? 2.6746 3.0216 4.4727 -0.1900 -0.3223 0.4282  97   GLY Y C   
26539 O O   . GLY D 97   ? 2.6903 2.9801 4.4381 -0.2185 -0.3574 0.4144  97   GLY Y O   
26540 N N   . LEU D 98   ? 2.6555 3.0118 4.4247 -0.1600 -0.2835 0.4011  98   LEU Y N   
26541 C CA  . LEU D 98   ? 2.6562 2.9581 4.3347 -0.1587 -0.2810 0.3526  98   LEU Y CA  
26542 C C   . LEU D 98   ? 2.6679 2.9456 4.3478 -0.1553 -0.2957 0.3444  98   LEU Y C   
26543 O O   . LEU D 98   ? 2.6561 2.9727 4.3884 -0.1328 -0.2776 0.3613  98   LEU Y O   
26544 C CB  . LEU D 98   ? 2.6430 2.9626 4.2783 -0.1287 -0.2313 0.3251  98   LEU Y CB  
26545 C CG  . LEU D 98   ? 2.6305 2.9582 4.2330 -0.1302 -0.2116 0.3152  98   LEU Y CG  
26546 C CD1 . LEU D 98   ? 2.6256 2.9496 4.1689 -0.1026 -0.1693 0.2803  98   LEU Y CD1 
26547 C CD2 . LEU D 98   ? 2.6388 2.9165 4.1906 -0.1649 -0.2463 0.3025  98   LEU Y CD2 
26548 N N   . GLN D 99   ? 2.6921 2.9042 4.3133 -0.1774 -0.3282 0.3185  99   GLN Y N   
26549 C CA  . GLN D 99   ? 2.7200 2.9009 4.3191 -0.1719 -0.3371 0.2972  99   GLN Y CA  
26550 C C   . GLN D 99   ? 2.7551 2.9075 4.2647 -0.1560 -0.3112 0.2484  99   GLN Y C   
26551 O O   . GLN D 99   ? 2.7544 2.8615 4.1967 -0.1718 -0.3207 0.2227  99   GLN Y O   
26552 C CB  . GLN D 99   ? 2.7296 2.8509 4.3199 -0.2057 -0.3900 0.2989  99   GLN Y CB  
26553 C CG  . GLN D 99   ? 2.7198 2.8566 4.3877 -0.2280 -0.4229 0.3475  99   GLN Y CG  
26554 C CD  . GLN D 99   ? 2.7187 2.8314 4.3630 -0.2548 -0.4439 0.3556  99   GLN Y CD  
26555 O OE1 . GLN D 99   ? 2.7257 2.8101 4.2966 -0.2572 -0.4331 0.3244  99   GLN Y OE1 
26556 N NE2 . GLN D 99   ? 2.7146 2.8375 4.4204 -0.2755 -0.4746 0.3986  99   GLN Y NE2 
26557 N N   . GLY D 100  ? 2.7787 2.9561 4.2873 -0.1249 -0.2791 0.2373  100  GLY Y N   
26558 C CA  . GLY D 100  ? 2.8021 2.9617 4.2328 -0.1050 -0.2496 0.1964  100  GLY Y CA  
26559 C C   . GLY D 100  ? 2.8144 2.9219 4.1630 -0.1219 -0.2579 0.1634  100  GLY Y C   
26560 O O   . GLY D 100  ? 2.8290 2.8814 4.1187 -0.1320 -0.2769 0.1327  100  GLY Y O   
26561 N N   . GLN D 101  ? 2.8248 2.9498 4.1701 -0.1246 -0.2428 0.1698  101  GLN Y N   
26562 C CA  . GLN D 101  ? 2.8592 2.9407 4.1287 -0.1380 -0.2446 0.1402  101  GLN Y CA  
26563 C C   . GLN D 101  ? 2.8934 2.9812 4.1110 -0.1115 -0.2033 0.1127  101  GLN Y C   
26564 O O   . GLN D 101  ? 2.8685 2.9921 4.1060 -0.0825 -0.1734 0.1169  101  GLN Y O   
26565 C CB  . GLN D 101  ? 2.8565 2.9481 4.1462 -0.1595 -0.2549 0.1617  101  GLN Y CB  
26566 C CG  . GLN D 101  ? 2.8843 2.9520 4.2038 -0.1915 -0.3010 0.1850  101  GLN Y CG  
26567 C CD  . GLN D 101  ? 2.8900 3.0124 4.3051 -0.1900 -0.3062 0.2309  101  GLN Y CD  
26568 O OE1 . GLN D 101  ? 2.8781 3.0551 4.3389 -0.1632 -0.2748 0.2444  101  GLN Y OE1 
26569 N NE2 . GLN D 101  ? 2.9105 3.0163 4.3557 -0.2187 -0.3459 0.2569  101  GLN Y NE2 
26570 N N   . ASN D 102  ? 2.9595 3.0091 4.1092 -0.1219 -0.2023 0.0860  102  ASN Y N   
26571 C CA  . ASN D 102  ? 3.0051 3.0584 4.1062 -0.1011 -0.1653 0.0632  102  ASN Y CA  
26572 C C   . ASN D 102  ? 3.0861 3.1768 4.2116 -0.1007 -0.1445 0.0803  102  ASN Y C   
26573 O O   . ASN D 102  ? 3.0898 3.1711 4.2173 -0.1255 -0.1628 0.0884  102  ASN Y O   
26574 C CB  . ASN D 102  ? 2.9589 2.9500 3.9735 -0.1119 -0.1741 0.0250  102  ASN Y CB  
26575 C CG  . ASN D 102  ? 2.9108 2.8670 3.8903 -0.1047 -0.1849 0.0015  102  ASN Y CG  
26576 O OD1 . ASN D 102  ? 2.9043 2.8133 3.8601 -0.1255 -0.2173 -0.0096 102  ASN Y OD1 
26577 N ND2 . ASN D 102  ? 2.8864 2.8632 3.8599 -0.0748 -0.1578 -0.0062 102  ASN Y ND2 
26578 N N   . VAL D 103  ? 3.1750 3.3050 4.3157 -0.0723 -0.1061 0.0855  103  VAL Y N   
26579 C CA  . VAL D 103  ? 3.2758 3.4413 4.4397 -0.0694 -0.0837 0.1002  103  VAL Y CA  
26580 C C   . VAL D 103  ? 3.3885 3.5445 4.4954 -0.0501 -0.0482 0.0750  103  VAL Y C   
26581 O O   . VAL D 103  ? 3.3872 3.5580 4.4920 -0.0208 -0.0191 0.0731  103  VAL Y O   
26582 C CB  . VAL D 103  ? 3.3132 3.5401 4.5634 -0.0539 -0.0692 0.1388  103  VAL Y CB  
26583 C CG1 . VAL D 103  ? 3.3047 3.5658 4.5713 -0.0467 -0.0407 0.1494  103  VAL Y CG1 
26584 C CG2 . VAL D 103  ? 3.3260 3.5638 4.6378 -0.0763 -0.1062 0.1683  103  VAL Y CG2 
26585 N N   . PHE D 104  ? 3.5042 3.6320 4.5630 -0.0673 -0.0517 0.0566  104  PHE Y N   
26586 C CA  . PHE D 104  ? 3.6132 3.7307 4.6208 -0.0537 -0.0206 0.0352  104  PHE Y CA  
26587 C C   . PHE D 104  ? 3.5854 3.7532 4.6394 -0.0356 0.0114  0.0569  104  PHE Y C   
26588 O O   . PHE D 104  ? 3.5730 3.7559 4.6389 -0.0477 0.0152  0.0640  104  PHE Y O   
26589 C CB  . PHE D 104  ? 3.7160 3.7976 4.6745 -0.0799 -0.0341 0.0169  104  PHE Y CB  
26590 C CG  . PHE D 104  ? 3.7912 3.8498 4.6876 -0.0697 -0.0080 -0.0093 104  PHE Y CG  
26591 C CD1 . PHE D 104  ? 3.8335 3.8566 4.6740 -0.0552 -0.0009 -0.0347 104  PHE Y CD1 
26592 C CD2 . PHE D 104  ? 3.8034 3.8743 4.6963 -0.0754 0.0081  -0.0085 104  PHE Y CD2 
26593 C CE1 . PHE D 104  ? 3.8467 3.8461 4.6306 -0.0466 0.0212  -0.0567 104  PHE Y CE1 
26594 C CE2 . PHE D 104  ? 3.8156 3.8622 4.6521 -0.0674 0.0307  -0.0319 104  PHE Y CE2 
26595 C CZ  . PHE D 104  ? 3.8356 3.8459 4.6181 -0.0530 0.0369  -0.0551 104  PHE Y CZ  
26596 N N   . VAL D 105  ? 3.5612 3.7534 4.6401 -0.0062 0.0349  0.0677  105  VAL Y N   
26597 C CA  . VAL D 105  ? 3.5134 3.7514 4.6399 0.0137  0.0667  0.0910  105  VAL Y CA  
26598 C C   . VAL D 105  ? 3.4576 3.6817 4.5337 0.0306  0.1018  0.0724  105  VAL Y C   
26599 O O   . VAL D 105  ? 3.4799 3.6938 4.5283 0.0577  0.1266  0.0646  105  VAL Y O   
26600 C CB  . VAL D 105  ? 3.5274 3.7978 4.7073 0.0386  0.0783  0.1154  105  VAL Y CB  
26601 C CG1 . VAL D 105  ? 3.5545 3.7934 4.6860 0.0551  0.0808  0.0948  105  VAL Y CG1 
26602 C CG2 . VAL D 105  ? 3.5203 3.8294 4.7375 0.0643  0.1175  0.1363  105  VAL Y CG2 
26603 N N   . VAL D 106  ? 3.3699 3.5906 4.4317 0.0136  0.1025  0.0655  106  VAL Y N   
26604 C CA  . VAL D 106  ? 3.2899 3.5019 4.3150 0.0272  0.1355  0.0523  106  VAL Y CA  
26605 C C   . VAL D 106  ? 3.1774 3.4368 4.2629 0.0339  0.1554  0.0784  106  VAL Y C   
26606 O O   . VAL D 106  ? 3.1568 3.4459 4.2934 0.0150  0.1364  0.0978  106  VAL Y O   
26607 C CB  . VAL D 106  ? 3.2953 3.4683 4.2588 0.0041  0.1252  0.0244  106  VAL Y CB  
26608 C CG1 . VAL D 106  ? 3.3175 3.4456 4.2303 -0.0067 0.1002  0.0021  106  VAL Y CG1 
26609 C CG2 . VAL D 106  ? 3.2782 3.4718 4.2734 -0.0241 0.1073  0.0356  106  VAL Y CG2 
26610 N N   . GLN D 107  ? 3.0960 3.3599 4.1744 0.0612  0.1932  0.0798  107  GLN Y N   
26611 C CA  . GLN D 107  ? 2.9968 3.3042 4.1332 0.0716  0.2156  0.1050  107  GLN Y CA  
26612 C C   . GLN D 107  ? 2.9253 3.2365 4.0549 0.0508  0.2153  0.0972  107  GLN Y C   
26613 O O   . GLN D 107  ? 2.9298 3.2039 3.9961 0.0438  0.2202  0.0696  107  GLN Y O   
26614 C CB  . GLN D 107  ? 2.9802 3.2863 4.1101 0.1093  0.2573  0.1108  107  GLN Y CB  
26615 C CG  . GLN D 107  ? 2.9658 3.2196 4.0104 0.1202  0.2754  0.0802  107  GLN Y CG  
26616 C CD  . GLN D 107  ? 2.9638 3.2082 3.9953 0.1583  0.3115  0.0878  107  GLN Y CD  
26617 O OE1 . GLN D 107  ? 2.9661 3.2278 4.0292 0.1758  0.3142  0.1065  107  GLN Y OE1 
26618 N NE2 . GLN D 107  ? 2.9617 3.1754 3.9443 0.1711  0.3392  0.0742  107  GLN Y NE2 
26619 N N   . GLU D 108  ? 2.8518 3.2077 4.0470 0.0405  0.2084  0.1223  108  GLU Y N   
26620 C CA  . GLU D 108  ? 2.7758 3.1428 3.9719 0.0228  0.2100  0.1183  108  GLU Y CA  
26621 C C   . GLU D 108  ? 2.7421 3.1381 3.9730 0.0470  0.2480  0.1335  108  GLU Y C   
26622 O O   . GLU D 108  ? 2.7308 3.1216 3.9404 0.0435  0.2641  0.1210  108  GLU Y O   
26623 C CB  . GLU D 108  ? 2.7293 3.1243 3.9706 -0.0071 0.1740  0.1361  108  GLU Y CB  
26624 C CG  . GLU D 108  ? 2.7099 3.0785 3.9309 -0.0285 0.1350  0.1295  108  GLU Y CG  
26625 C CD  . GLU D 108  ? 2.6839 3.0061 3.8308 -0.0514 0.1210  0.0972  108  GLU Y CD  
26626 O OE1 . GLU D 108  ? 2.6611 2.9861 3.7947 -0.0661 0.1240  0.0899  108  GLU Y OE1 
26627 O OE2 . GLU D 108  ? 2.6931 2.9759 3.7957 -0.0547 0.1070  0.0795  108  GLU Y OE2 
26628 N N   . LEU D 109  ? 2.7259 3.1503 4.0103 0.0715  0.2623  0.1608  109  LEU Y N   
26629 C CA  . LEU D 109  ? 2.7334 3.1809 4.0516 0.0999  0.3013  0.1782  109  LEU Y CA  
26630 C C   . LEU D 109  ? 2.8340 3.2921 4.1842 0.1280  0.3134  0.2002  109  LEU Y C   
26631 O O   . LEU D 109  ? 2.8498 3.3066 4.2077 0.1203  0.2873  0.2041  109  LEU Y O   
26632 C CB  . LEU D 109  ? 2.6494 3.1456 4.0333 0.0887  0.2983  0.2012  109  LEU Y CB  
26633 C CG  . LEU D 109  ? 2.6096 3.1013 3.9673 0.0708  0.3015  0.1828  109  LEU Y CG  
26634 C CD1 . LEU D 109  ? 2.5837 3.1287 4.0124 0.0589  0.2932  0.2090  109  LEU Y CD1 
26635 C CD2 . LEU D 109  ? 2.5961 3.0586 3.9093 0.0943  0.3429  0.1651  109  LEU Y CD2 
26636 N N   . ILE D 110  ? 2.9345 3.4014 4.3034 0.1602  0.3526  0.2154  110  ILE Y N   
26637 C CA  . ILE D 110  ? 3.0634 3.5334 4.4512 0.1898  0.3685  0.2342  110  ILE Y CA  
26638 C C   . ILE D 110  ? 3.1579 3.6667 4.6154 0.2175  0.4008  0.2706  110  ILE Y C   
26639 O O   . ILE D 110  ? 3.1500 3.6744 4.6281 0.2198  0.4194  0.2767  110  ILE Y O   
26640 C CB  . ILE D 110  ? 3.0999 3.5142 4.4037 0.2101  0.3888  0.2085  110  ILE Y CB  
26641 C CG1 . ILE D 110  ? 3.0946 3.4693 4.3299 0.1844  0.3589  0.1732  110  ILE Y CG1 
26642 C CG2 . ILE D 110  ? 3.1390 3.5546 4.4558 0.2387  0.4016  0.2265  110  ILE Y CG2 
26643 C CD1 . ILE D 110  ? 3.1182 3.4428 4.2790 0.2029  0.3707  0.1524  110  ILE Y CD1 
26644 N N   . ASP D 111  ? 3.2661 3.7901 4.7605 0.2380  0.4067  0.2951  111  ASP Y N   
26645 C CA  . ASP D 111  ? 3.3605 3.9130 4.9127 0.2703  0.4424  0.3301  111  ASP Y CA  
26646 C C   . ASP D 111  ? 3.4373 3.9478 4.9326 0.3057  0.4783  0.3231  111  ASP Y C   
26647 O O   . ASP D 111  ? 3.4632 3.9364 4.8959 0.3042  0.4670  0.2997  111  ASP Y O   
26648 C CB  . ASP D 111  ? 3.3779 3.9796 5.0184 0.2675  0.4228  0.3672  111  ASP Y CB  
26649 C CG  . ASP D 111  ? 3.4001 4.0382 5.1132 0.2977  0.4576  0.4080  111  ASP Y CG  
26650 O OD1 . ASP D 111  ? 3.4419 4.0653 5.1437 0.3308  0.4888  0.4181  111  ASP Y OD1 
26651 O OD2 . ASP D 111  ? 3.3732 4.0541 5.1544 0.2887  0.4537  0.4312  111  ASP Y OD2 
26652 N N   . PRO D 112  ? 3.4721 3.9855 4.9858 0.3379  0.5218  0.3435  112  PRO Y N   
26653 C CA  . PRO D 112  ? 3.5081 3.9765 4.9632 0.3731  0.5583  0.3395  112  PRO Y CA  
26654 C C   . PRO D 112  ? 3.5133 3.9740 4.9568 0.3849  0.5499  0.3447  112  PRO Y C   
26655 O O   . PRO D 112  ? 3.5526 3.9646 4.9208 0.4031  0.5654  0.3278  112  PRO Y O   
26656 C CB  . PRO D 112  ? 3.5230 4.0110 5.0296 0.4040  0.6016  0.3732  112  PRO Y CB  
26657 C CG  . PRO D 112  ? 3.4884 4.0412 5.0930 0.3847  0.5825  0.3991  112  PRO Y CG  
26658 C CD  . PRO D 112  ? 3.4611 4.0128 5.0415 0.3432  0.5408  0.3689  112  PRO Y CD  
26659 N N   . ASN D 113  ? 3.4685 3.9745 4.9833 0.3743  0.5248  0.3676  113  ASN Y N   
26660 C CA  . ASN D 113  ? 3.4514 3.9539 4.9618 0.3844  0.5156  0.3734  113  ASN Y CA  
26661 C C   . ASN D 113  ? 3.4106 3.8778 4.8507 0.3617  0.4808  0.3353  113  ASN Y C   
26662 O O   . ASN D 113  ? 3.4153 3.8764 4.8445 0.3666  0.4688  0.3345  113  ASN Y O   
26663 C CB  . ASN D 113  ? 3.4461 4.0065 5.0584 0.3797  0.4995  0.4116  113  ASN Y CB  
26664 C CG  . ASN D 113  ? 3.4301 4.0134 5.0735 0.3376  0.4478  0.4040  113  ASN Y CG  
26665 O OD1 . ASN D 113  ? 3.4256 4.0303 5.1112 0.3275  0.4208  0.4178  113  ASN Y OD1 
26666 N ND2 . ASN D 113  ? 3.4224 3.9981 5.0430 0.3127  0.4337  0.3823  113  ASN Y ND2 
26667 N N   . GLY D 114  ? 3.3640 3.8077 4.7568 0.3373  0.4651  0.3040  114  GLY Y N   
26668 C CA  . GLY D 114  ? 3.3231 3.7313 4.6490 0.3153  0.4333  0.2678  114  GLY Y CA  
26669 C C   . GLY D 114  ? 3.2512 3.6840 4.6144 0.2768  0.3862  0.2644  114  GLY Y C   
26670 O O   . GLY D 114  ? 3.2527 3.6561 4.5631 0.2529  0.3591  0.2332  114  GLY Y O   
26671 N N   . ARG D 115  ? 3.1847 3.6686 4.6382 0.2710  0.3762  0.2978  115  ARG Y N   
26672 C CA  . ARG D 115  ? 3.1197 3.6248 4.6113 0.2343  0.3307  0.2991  115  ARG Y CA  
26673 C C   . ARG D 115  ? 3.0988 3.5966 4.5680 0.2089  0.3205  0.2802  115  ARG Y C   
26674 O O   . ARG D 115  ? 3.0787 3.5824 4.5502 0.2191  0.3484  0.2835  115  ARG Y O   
26675 C CB  . ARG D 115  ? 3.0818 3.6425 4.6770 0.2341  0.3234  0.3427  115  ARG Y CB  
26676 C CG  . ARG D 115  ? 3.0495 3.6474 4.7017 0.2287  0.3323  0.3642  115  ARG Y CG  
26677 C CD  . ARG D 115  ? 3.0282 3.6797 4.7837 0.2264  0.3200  0.4087  115  ARG Y CD  
26678 N NE  . ARG D 115  ? 3.0077 3.6967 4.8211 0.2354  0.3430  0.4353  115  ARG Y NE  
26679 C CZ  . ARG D 115  ? 3.0083 3.7176 4.8621 0.2696  0.3834  0.4633  115  ARG Y CZ  
26680 N NH1 . ARG D 115  ? 3.0299 3.7259 4.8712 0.2978  0.4051  0.4693  115  ARG Y NH1 
26681 N NH2 . ARG D 115  ? 2.9894 3.7312 4.8947 0.2759  0.4024  0.4857  115  ARG Y NH2 
26682 N N   . LEU D 116  ? 3.1108 3.5940 4.5572 0.1757  0.2806  0.2606  116  LEU Y N   
26683 C CA  . LEU D 116  ? 3.1203 3.5886 4.5316 0.1508  0.2699  0.2382  116  LEU Y CA  
26684 C C   . LEU D 116  ? 3.1451 3.6326 4.5942 0.1146  0.2265  0.2463  116  LEU Y C   
26685 O O   . LEU D 116  ? 3.1540 3.6358 4.6111 0.1009  0.1951  0.2480  116  LEU Y O   
26686 C CB  . LEU D 116  ? 3.0961 3.5073 4.4102 0.1483  0.2699  0.1970  116  LEU Y CB  
26687 C CG  . LEU D 116  ? 3.0646 3.4475 4.3441 0.1416  0.2436  0.1813  116  LEU Y CG  
26688 C CD1 . LEU D 116  ? 3.0379 3.4071 4.3030 0.1033  0.2011  0.1659  116  LEU Y CD1 
26689 C CD2 . LEU D 116  ? 3.0696 3.4049 4.2666 0.1611  0.2635  0.1535  116  LEU Y CD2 
26690 N N   . SER D 117  ? 3.1636 3.6716 4.6344 0.0993  0.2248  0.2519  117  SER Y N   
26691 C CA  . SER D 117  ? 3.1761 3.6967 4.6723 0.0636  0.1841  0.2586  117  SER Y CA  
26692 C C   . SER D 117  ? 3.1823 3.6543 4.6008 0.0378  0.1592  0.2219  117  SER Y C   
26693 O O   . SER D 117  ? 3.2076 3.6442 4.5579 0.0448  0.1777  0.1917  117  SER Y O   
26694 C CB  . SER D 117  ? 3.1773 3.7360 4.7184 0.0568  0.1916  0.2763  117  SER Y CB  
26695 O OG  . SER D 117  ? 3.1917 3.7341 4.6858 0.0667  0.2229  0.2538  117  SER Y OG  
26696 N N   . THR D 118  ? 3.1623 3.6300 4.5913 0.0081  0.1172  0.2262  118  THR Y N   
26697 C CA  . THR D 118  ? 3.1442 3.5639 4.5040 -0.0175 0.0909  0.1952  118  THR Y CA  
26698 C C   . THR D 118  ? 3.1239 3.5485 4.5091 -0.0521 0.0479  0.2097  118  THR Y C   
26699 O O   . THR D 118  ? 3.1125 3.5738 4.5691 -0.0554 0.0340  0.2438  118  THR Y O   
26700 C CB  . THR D 118  ? 3.3865 3.7668 4.7012 -0.0087 0.0853  0.1753  118  THR Y CB  
26701 O OG1 . THR D 118  ? 3.3924 3.7258 4.6444 -0.0344 0.0583  0.1477  118  THR Y OG1 
26702 C CG2 . THR D 118  ? 3.3915 3.7916 4.7637 -0.0044 0.0680  0.2014  118  THR Y CG2 
26703 N N   . VAL D 119  ? 3.0965 3.4817 4.4228 -0.0778 0.0267  0.1856  119  VAL Y N   
26704 C CA  . VAL D 119  ? 3.0627 3.4449 4.4030 -0.1111 -0.0135 0.1989  119  VAL Y CA  
26705 C C   . VAL D 119  ? 3.0586 3.3828 4.3368 -0.1327 -0.0438 0.1756  119  VAL Y C   
26706 O O   . VAL D 119  ? 3.0631 3.3493 4.2718 -0.1362 -0.0358 0.1437  119  VAL Y O   
26707 C CB  . VAL D 119  ? 3.0250 3.4261 4.3660 -0.1260 -0.0099 0.2016  119  VAL Y CB  
26708 C CG1 . VAL D 119  ? 3.0096 3.3851 4.2826 -0.1202 0.0175  0.1664  119  VAL Y CG1 
26709 C CG2 . VAL D 119  ? 3.0207 3.4062 4.3567 -0.1618 -0.0527 0.2109  119  VAL Y CG2 
26710 N N   . GLY D 120  ? 3.0428 3.3583 4.3472 -0.1473 -0.0788 0.1927  120  GLY Y N   
26711 C CA  . GLY D 120  ? 3.0336 3.2912 4.2836 -0.1677 -0.1094 0.1736  120  GLY Y CA  
26712 C C   . GLY D 120  ? 3.0185 3.2450 4.2260 -0.1489 -0.0966 0.1466  120  GLY Y C   
26713 O O   . GLY D 120  ? 3.0345 3.2865 4.2710 -0.1218 -0.0741 0.1523  120  GLY Y O   
26714 N N   . GLY D 121  ? 3.0014 3.1715 4.1388 -0.1631 -0.1110 0.1180  121  GLY Y N   
26715 C CA  . GLY D 121  ? 2.9899 3.1257 4.0778 -0.1472 -0.1006 0.0893  121  GLY Y CA  
26716 C C   . GLY D 121  ? 2.9987 3.1136 4.0971 -0.1492 -0.1265 0.0923  121  GLY Y C   
26717 O O   . GLY D 121  ? 3.0068 3.0937 4.0657 -0.1362 -0.1207 0.0690  121  GLY Y O   
26718 N N   . VAL D 122  ? 2.9808 3.1077 4.1313 -0.1660 -0.1562 0.1210  122  VAL Y N   
26719 C CA  . VAL D 122  ? 2.9499 3.0586 4.1181 -0.1693 -0.1824 0.1270  122  VAL Y CA  
26720 C C   . VAL D 122  ? 2.9049 2.9447 4.0138 -0.1940 -0.2158 0.1066  122  VAL Y C   
26721 O O   . VAL D 122  ? 2.9238 2.9358 4.0018 -0.2178 -0.2316 0.1042  122  VAL Y O   
26722 C CB  . VAL D 122  ? 2.9519 3.1005 4.2052 -0.1761 -0.2011 0.1692  122  VAL Y CB  
26723 C CG1 . VAL D 122  ? 2.9643 3.0985 4.2404 -0.1751 -0.2232 0.1751  122  VAL Y CG1 
26724 C CG2 . VAL D 122  ? 2.9238 3.1393 4.2360 -0.1522 -0.1667 0.1911  122  VAL Y CG2 
26725 N N   . THR D 123  ? 2.8325 2.8438 3.9250 -0.1878 -0.2258 0.0922  123  THR Y N   
26726 C CA  . THR D 123  ? 2.7798 2.7217 3.8143 -0.2075 -0.2552 0.0703  123  THR Y CA  
26727 C C   . THR D 123  ? 2.7449 2.6731 3.8084 -0.2100 -0.2818 0.0785  123  THR Y C   
26728 O O   . THR D 123  ? 2.7236 2.6987 3.8509 -0.1953 -0.2749 0.1007  123  THR Y O   
26729 C CB  . THR D 123  ? 3.0430 2.9488 3.9987 -0.1961 -0.2349 0.0297  123  THR Y CB  
26730 O OG1 . THR D 123  ? 3.0651 2.9215 3.9845 -0.1979 -0.2537 0.0084  123  THR Y OG1 
26731 C CG2 . THR D 123  ? 3.0221 2.9721 3.9847 -0.1636 -0.1924 0.0233  123  THR Y CG2 
26732 N N   . LYS D 124  ? 2.7036 2.5664 3.7206 -0.2285 -0.3116 0.0612  124  LYS Y N   
26733 C CA  . LYS D 124  ? 2.6552 2.4953 3.6988 -0.2387 -0.3448 0.0712  124  LYS Y CA  
26734 C C   . LYS D 124  ? 2.6269 2.4951 3.7017 -0.2140 -0.3331 0.0684  124  LYS Y C   
26735 O O   . LYS D 124  ? 2.6260 2.5415 3.7743 -0.2077 -0.3338 0.0991  124  LYS Y O   
26736 C CB  . LYS D 124  ? 2.6221 2.3784 3.6015 -0.2630 -0.3774 0.0502  124  LYS Y CB  
26737 C CG  . LYS D 124  ? 2.5659 2.2802 3.4652 -0.2533 -0.3621 0.0076  124  LYS Y CG  
26738 C CD  . LYS D 124  ? 2.5490 2.1813 3.3858 -0.2799 -0.3915 -0.0074 124  LYS Y CD  
26739 C CE  . LYS D 124  ? 2.5485 2.1350 3.3932 -0.2951 -0.4298 -0.0039 124  LYS Y CE  
26740 N NZ  . LYS D 124  ? 2.5487 2.1181 3.3679 -0.2779 -0.4247 -0.0339 124  LYS Y NZ  
26741 N N   . LYS D 125  ? 2.6022 2.4414 3.6217 -0.2001 -0.3228 0.0332  125  LYS Y N   
26742 C CA  . LYS D 125  ? 2.5763 2.4325 3.6145 -0.1789 -0.3158 0.0274  125  LYS Y CA  
26743 C C   . LYS D 125  ? 2.6011 2.4352 3.6758 -0.1969 -0.3549 0.0424  125  LYS Y C   
26744 O O   . LYS D 125  ? 2.5793 2.4421 3.7214 -0.2077 -0.3693 0.0790  125  LYS Y O   
26745 C CB  . LYS D 125  ? 2.5282 2.4591 3.6217 -0.1504 -0.2799 0.0480  125  LYS Y CB  
26746 C CG  . LYS D 125  ? 2.5080 2.4598 3.6203 -0.1260 -0.2689 0.0444  125  LYS Y CG  
26747 C CD  . LYS D 125  ? 2.4926 2.4214 3.5316 -0.1054 -0.2474 0.0053  125  LYS Y CD  
26748 C CE  . LYS D 125  ? 2.4746 2.4272 3.5299 -0.0798 -0.2344 0.0035  125  LYS Y CE  
26749 N NZ  . LYS D 125  ? 2.4746 2.3993 3.5441 -0.0943 -0.2698 0.0018  125  LYS Y NZ  
26750 N N   . ASN D 126  ? 2.6424 2.4251 3.6739 -0.2004 -0.3728 0.0149  126  ASN Y N   
26751 C CA  . ASN D 126  ? 2.6817 2.4335 3.6369 -0.1859 -0.3560 -0.0270 126  ASN Y CA  
26752 C C   . ASN D 126  ? 2.7889 2.5019 3.6790 -0.1968 -0.3513 -0.0460 126  ASN Y C   
26753 O O   . ASN D 126  ? 2.8342 2.4889 3.6924 -0.2226 -0.3797 -0.0514 126  ASN Y O   
26754 C CB  . ASN D 126  ? 2.6146 2.3167 3.5415 -0.1905 -0.3811 -0.0503 126  ASN Y CB  
26755 C CG  . ASN D 126  ? 2.5407 2.2820 3.5259 -0.1767 -0.3817 -0.0357 126  ASN Y CG  
26756 O OD1 . ASN D 126  ? 2.4442 2.2491 3.4721 -0.1535 -0.3524 -0.0186 126  ASN Y OD1 
26757 N ND2 . ASN D 126  ? 2.5593 2.2602 3.5457 -0.1908 -0.4147 -0.0420 126  ASN Y ND2 
26758 N N   . ASN D 127  ? 2.8571 2.6009 3.7275 -0.1766 -0.3148 -0.0549 127  ASN Y N   
26759 C CA  . ASN D 127  ? 2.9646 2.6803 3.7779 -0.1837 -0.3048 -0.0716 127  ASN Y CA  
26760 C C   . ASN D 127  ? 3.0423 2.7101 3.7789 -0.1751 -0.2996 -0.1117 127  ASN Y C   
26761 O O   . ASN D 127  ? 3.0380 2.7275 3.7593 -0.1488 -0.2741 -0.1264 127  ASN Y O   
26762 C CB  . ASN D 127  ? 2.9762 2.7485 3.8100 -0.1675 -0.2686 -0.0590 127  ASN Y CB  
26763 C CG  . ASN D 127  ? 3.0367 2.7868 3.8292 -0.1815 -0.2630 -0.0661 127  ASN Y CG  
26764 O OD1 . ASN D 127  ? 3.0780 2.7705 3.8273 -0.2035 -0.2858 -0.0780 127  ASN Y OD1 
26765 N ND2 . ASN D 127  ? 3.0366 2.8303 3.8414 -0.1687 -0.2321 -0.0585 127  ASN Y ND2 
26766 N N   . LYS D 128  ? 3.1439 2.7446 3.8312 -0.1969 -0.3239 -0.1280 128  LYS Y N   
26767 C CA  . LYS D 128  ? 3.2037 2.7527 3.8175 -0.1913 -0.3223 -0.1653 128  LYS Y CA  
26768 C C   . LYS D 128  ? 3.2421 2.8138 3.8227 -0.1690 -0.2851 -0.1803 128  LYS Y C   
26769 O O   . LYS D 128  ? 3.2408 2.8348 3.8276 -0.1713 -0.2682 -0.1686 128  LYS Y O   
26770 C CB  . LYS D 128  ? 3.1965 2.6714 3.7628 -0.2189 -0.3482 -0.1751 128  LYS Y CB  
26771 C CG  . LYS D 128  ? 3.1641 2.6093 3.7598 -0.2446 -0.3864 -0.1557 128  LYS Y CG  
26772 C CD  . LYS D 128  ? 3.1440 2.5096 3.6843 -0.2702 -0.4091 -0.1652 128  LYS Y CD  
26773 C CE  . LYS D 128  ? 3.1261 2.4405 3.5931 -0.2619 -0.4022 -0.2036 128  LYS Y CE  
26774 N NZ  . LYS D 128  ? 3.1197 2.4282 3.5843 -0.2479 -0.4089 -0.2235 128  LYS Y NZ  
26775 N N   . THR D 129  ? 3.1136 2.0880 2.8153 -0.4337 -1.0089 -0.3727 129  THR Y N   
26776 C CA  . THR D 129  ? 3.0860 2.1351 2.7984 -0.4497 -0.9662 -0.3597 129  THR Y CA  
26777 C C   . THR D 129  ? 3.1171 2.1841 2.7420 -0.4533 -0.9338 -0.3121 129  THR Y C   
26778 O O   . THR D 129  ? 3.0988 2.1941 2.7062 -0.4710 -0.9239 -0.2904 129  THR Y O   
26779 C CB  . THR D 129  ? 3.0844 2.1351 2.8389 -0.4667 -0.9905 -0.3748 129  THR Y CB  
26780 O OG1 . THR D 129  ? 3.0906 2.1158 2.9252 -0.4591 -1.0251 -0.4181 129  THR Y OG1 
26781 C CG2 . THR D 129  ? 3.0267 2.1540 2.8072 -0.4834 -0.9471 -0.3709 129  THR Y CG2 
26782 N N   . SER D 130  ? 3.1671 2.2159 2.7384 -0.4361 -0.9179 -0.2956 130  SER Y N   
26783 C CA  . SER D 130  ? 3.2016 2.2747 2.6984 -0.4340 -0.8787 -0.2521 130  SER Y CA  
26784 C C   . SER D 130  ? 3.1798 2.3450 2.7076 -0.4429 -0.8279 -0.2407 130  SER Y C   
26785 O O   . SER D 130  ? 3.1410 2.3437 2.7344 -0.4444 -0.8151 -0.2677 130  SER Y O   
26786 C CB  . SER D 130  ? 3.2174 2.2466 2.6543 -0.4101 -0.8712 -0.2431 130  SER Y CB  
26787 O OG  . SER D 130  ? 3.1884 2.2667 2.5853 -0.4028 -0.8189 -0.2110 130  SER Y OG  
26788 N N   . GLU D 131  ? 3.2039 2.4041 2.6840 -0.4498 -0.7995 -0.1995 131  GLU Y N   
26789 C CA  . GLU D 131  ? 3.1430 2.4283 2.6474 -0.4616 -0.7570 -0.1821 131  GLU Y CA  
26790 C C   . GLU D 131  ? 3.1476 2.4610 2.5937 -0.4492 -0.7166 -0.1393 131  GLU Y C   
26791 O O   . GLU D 131  ? 3.1748 2.4943 2.5772 -0.4569 -0.7116 -0.1035 131  GLU Y O   
26792 C CB  . GLU D 131  ? 3.1209 2.4314 2.6429 -0.4906 -0.7691 -0.1728 131  GLU Y CB  
26793 C CG  . GLU D 131  ? 3.0717 2.4587 2.5862 -0.5052 -0.7303 -0.1344 131  GLU Y CG  
26794 C CD  . GLU D 131  ? 3.0592 2.4586 2.5724 -0.5354 -0.7476 -0.1166 131  GLU Y CD  
26795 O OE1 . GLU D 131  ? 3.0474 2.4311 2.6001 -0.5506 -0.7749 -0.1459 131  GLU Y OE1 
26796 O OE2 . GLU D 131  ? 3.0585 2.4839 2.5320 -0.5442 -0.7331 -0.0726 131  GLU Y OE2 
26797 N N   . THR D 132  ? 3.1188 2.4493 2.5649 -0.4296 -0.6872 -0.1423 132  THR Y N   
26798 C CA  . THR D 132  ? 3.1164 2.4718 2.5096 -0.4132 -0.6474 -0.1033 132  THR Y CA  
26799 C C   . THR D 132  ? 3.0318 2.4771 2.4551 -0.4234 -0.6080 -0.0803 132  THR Y C   
26800 O O   . THR D 132  ? 2.9827 2.4644 2.4607 -0.4338 -0.6018 -0.1016 132  THR Y O   
26801 C CB  . THR D 132  ? 3.1562 2.4662 2.5120 -0.3823 -0.6386 -0.1124 132  THR Y CB  
26802 O OG1 . THR D 132  ? 3.1743 2.5120 2.4815 -0.3642 -0.5961 -0.0747 132  THR Y OG1 
26803 C CG2 . THR D 132  ? 3.1178 2.4416 2.5304 -0.3802 -0.6365 -0.1478 132  THR Y CG2 
26804 N N   . ASN D 133  ? 2.9975 2.4767 2.3842 -0.4215 -0.5822 -0.0357 133  ASN Y N   
26805 C CA  . ASN D 133  ? 2.8921 2.4553 2.3023 -0.4282 -0.5457 -0.0068 133  ASN Y CA  
26806 C C   . ASN D 133  ? 2.8514 2.4245 2.2310 -0.3958 -0.5081 0.0092  133  ASN Y C   
26807 O O   . ASN D 133  ? 2.9032 2.4745 2.2339 -0.3788 -0.4876 0.0425  133  ASN Y O   
26808 C CB  . ASN D 133  ? 2.8783 2.4788 2.2762 -0.4477 -0.5420 0.0353  133  ASN Y CB  
26809 C CG  . ASN D 133  ? 2.7953 2.4823 2.2349 -0.4669 -0.5197 0.0601  133  ASN Y CG  
26810 O OD1 . ASN D 133  ? 2.7486 2.4567 2.2343 -0.4848 -0.5274 0.0373  133  ASN Y OD1 
26811 N ND2 . ASN D 133  ? 2.7844 2.5211 2.2078 -0.4638 -0.4918 0.1079  133  ASN Y ND2 
26812 N N   . THR D 134  ? 2.7405 2.3217 2.1467 -0.3870 -0.4980 -0.0146 134  THR Y N   
26813 C CA  . THR D 134  ? 2.6802 2.2545 2.0533 -0.3541 -0.4683 -0.0065 134  THR Y CA  
26814 C C   . THR D 134  ? 2.5801 2.2306 1.9672 -0.3492 -0.4289 0.0263  134  THR Y C   
26815 O O   . THR D 134  ? 2.5189 2.2221 1.9560 -0.3710 -0.4259 0.0232  134  THR Y O   
26816 C CB  . THR D 134  ? 2.9731 2.5034 2.3584 -0.3443 -0.4803 -0.0495 134  THR Y CB  
26817 O OG1 . THR D 134  ? 2.9853 2.5172 2.3409 -0.3161 -0.4498 -0.0386 134  THR Y OG1 
26818 C CG2 . THR D 134  ? 2.9129 2.4794 2.3676 -0.3713 -0.4889 -0.0771 134  THR Y CG2 
26819 N N   . PRO D 135  ? 2.5790 2.2314 1.9198 -0.3193 -0.3987 0.0574  135  PRO Y N   
26820 C CA  . PRO D 135  ? 2.5395 2.2562 1.8938 -0.3067 -0.3619 0.0857  135  PRO Y CA  
26821 C C   . PRO D 135  ? 2.5031 2.2234 1.8876 -0.3085 -0.3620 0.0567  135  PRO Y C   
26822 O O   . PRO D 135  ? 2.5164 2.1850 1.9052 -0.3136 -0.3862 0.0160  135  PRO Y O   
26823 C CB  . PRO D 135  ? 2.5934 2.2786 1.8823 -0.2657 -0.3343 0.1077  135  PRO Y CB  
26824 C CG  . PRO D 135  ? 2.6434 2.2351 1.8804 -0.2586 -0.3610 0.0823  135  PRO Y CG  
26825 C CD  . PRO D 135  ? 2.6255 2.2205 1.8975 -0.2956 -0.3959 0.0700  135  PRO Y CD  
26826 N N   . LEU D 136  ? 2.4498 2.2301 1.8563 -0.3055 -0.3364 0.0783  136  LEU Y N   
26827 C CA  . LEU D 136  ? 2.3942 2.1875 1.8337 -0.3172 -0.3374 0.0546  136  LEU Y CA  
26828 C C   . LEU D 136  ? 2.3701 2.2385 1.8358 -0.3210 -0.3136 0.0885  136  LEU Y C   
26829 O O   . LEU D 136  ? 2.3409 2.2644 1.8422 -0.3491 -0.3179 0.1082  136  LEU Y O   
26830 C CB  . LEU D 136  ? 2.3329 2.1220 1.8150 -0.3551 -0.3670 0.0212  136  LEU Y CB  
26831 C CG  . LEU D 136  ? 2.2658 2.1011 1.7914 -0.3816 -0.3628 0.0144  136  LEU Y CG  
26832 C CD1 . LEU D 136  ? 2.2573 2.0686 1.7759 -0.3679 -0.3526 -0.0087 136  LEU Y CD1 
26833 C CD2 . LEU D 136  ? 2.2311 2.0659 1.7947 -0.4190 -0.3882 -0.0125 136  LEU Y CD2 
26834 N N   . PHE D 137  ? 2.3933 2.2611 1.8406 -0.2936 -0.2914 0.0959  137  PHE Y N   
26835 C CA  . PHE D 137  ? 2.3972 2.3342 1.8680 -0.2926 -0.2701 0.1318  137  PHE Y CA  
26836 C C   . PHE D 137  ? 2.3678 2.3162 1.8645 -0.3135 -0.2749 0.1125  137  PHE Y C   
26837 O O   . PHE D 137  ? 2.3706 2.2726 1.8645 -0.3232 -0.2889 0.0710  137  PHE Y O   
26838 C CB  . PHE D 137  ? 2.4479 2.3854 1.8831 -0.2466 -0.2392 0.1611  137  PHE Y CB  
26839 C CG  . PHE D 137  ? 2.4981 2.4052 1.8918 -0.2219 -0.2307 0.1736  137  PHE Y CG  
26840 C CD1 . PHE D 137  ? 2.5089 2.3931 1.9002 -0.2428 -0.2529 0.1619  137  PHE Y CD1 
26841 C CD2 . PHE D 137  ? 2.5524 2.4511 1.9064 -0.1778 -0.1999 0.1977  137  PHE Y CD2 
26842 C CE1 . PHE D 137  ? 2.5442 2.3951 1.8908 -0.2229 -0.2458 0.1739  137  PHE Y CE1 
26843 C CE2 . PHE D 137  ? 2.5917 2.4579 1.9004 -0.1565 -0.1893 0.2091  137  PHE Y CE2 
26844 C CZ  . PHE D 137  ? 2.5938 2.4354 1.8972 -0.1804 -0.2128 0.1976  137  PHE Y CZ  
26845 N N   . VAL D 138  ? 2.3496 2.3600 1.8722 -0.3214 -0.2637 0.1437  138  VAL Y N   
26846 C CA  . VAL D 138  ? 2.3261 2.3460 1.8663 -0.3432 -0.2675 0.1295  138  VAL Y CA  
26847 C C   . VAL D 138  ? 2.3343 2.4076 1.8848 -0.3315 -0.2500 0.1704  138  VAL Y C   
26848 O O   . VAL D 138  ? 2.3343 2.4698 1.9152 -0.3441 -0.2493 0.2082  138  VAL Y O   
26849 C CB  . VAL D 138  ? 2.2541 2.2876 1.8277 -0.3922 -0.2895 0.1109  138  VAL Y CB  
26850 C CG1 . VAL D 138  ? 2.2378 2.3172 1.8340 -0.4183 -0.2887 0.1283  138  VAL Y CG1 
26851 C CG2 . VAL D 138  ? 2.2395 2.2128 1.8079 -0.4034 -0.3035 0.0569  138  VAL Y CG2 
26852 N N   . ASN D 139  ? 2.3496 2.3962 1.8750 -0.3065 -0.2379 0.1637  139  ASN Y N   
26853 C CA  . ASN D 139  ? 2.3326 2.4201 1.8654 -0.2918 -0.2235 0.1984  139  ASN Y CA  
26854 C C   . ASN D 139  ? 2.3383 2.4179 1.8751 -0.3197 -0.2332 0.1802  139  ASN Y C   
26855 O O   . ASN D 139  ? 2.3436 2.3669 1.8543 -0.3199 -0.2360 0.1427  139  ASN Y O   
26856 C CB  . ASN D 139  ? 2.3629 2.4208 1.8562 -0.2378 -0.2009 0.2082  139  ASN Y CB  
26857 C CG  . ASN D 139  ? 2.3894 2.4131 1.8538 -0.2123 -0.1940 0.2033  139  ASN Y CG  
26858 O OD1 . ASN D 139  ? 2.4258 2.3787 1.8505 -0.2007 -0.1992 0.1689  139  ASN Y OD1 
26859 N ND2 . ASN D 139  ? 2.3875 2.4596 1.8706 -0.2058 -0.1837 0.2386  139  ASN Y ND2 
26860 N N   . LYS D 140  ? 2.3229 2.4564 1.8905 -0.3459 -0.2393 0.2069  140  LYS Y N   
26861 C CA  . LYS D 140  ? 2.3298 2.4521 1.8923 -0.3712 -0.2467 0.1938  140  LYS Y CA  
26862 C C   . LYS D 140  ? 2.3414 2.4714 1.8907 -0.3391 -0.2341 0.2206  140  LYS Y C   
26863 O O   . LYS D 140  ? 2.3199 2.5033 1.8923 -0.3211 -0.2272 0.2653  140  LYS Y O   
26864 C CB  . LYS D 140  ? 2.3136 2.4751 1.9059 -0.4213 -0.2643 0.2037  140  LYS Y CB  
26865 C CG  . LYS D 140  ? 2.2913 2.4425 1.8956 -0.4519 -0.2776 0.1773  140  LYS Y CG  
26866 C CD  . LYS D 140  ? 2.2663 2.4272 1.8818 -0.5046 -0.2946 0.1699  140  LYS Y CD  
26867 C CE  . LYS D 140  ? 2.2680 2.3750 1.8608 -0.5247 -0.2942 0.1218  140  LYS Y CE  
26868 N NZ  . LYS D 140  ? 2.2655 2.3737 1.8632 -0.5754 -0.3078 0.1096  140  LYS Y NZ  
26869 N N   . VAL D 141  ? 2.3816 2.4571 1.8951 -0.3307 -0.2312 0.1935  141  VAL Y N   
26870 C CA  . VAL D 141  ? 2.4473 2.5204 1.9430 -0.3038 -0.2229 0.2149  141  VAL Y CA  
26871 C C   . VAL D 141  ? 2.4648 2.5600 1.9721 -0.3422 -0.2370 0.2260  141  VAL Y C   
26872 O O   . VAL D 141  ? 2.4436 2.5246 1.9507 -0.3876 -0.2493 0.1995  141  VAL Y O   
26873 C CB  . VAL D 141  ? 2.4930 2.4909 1.9381 -0.2797 -0.2163 0.1824  141  VAL Y CB  
26874 C CG1 . VAL D 141  ? 2.5354 2.5290 1.9586 -0.2356 -0.2041 0.2105  141  VAL Y CG1 
26875 C CG2 . VAL D 141  ? 2.5007 2.4569 1.9278 -0.2611 -0.2119 0.1551  141  VAL Y CG2 
26876 N N   . ASN D 142  ? 2.5145 2.6420 2.0303 -0.3232 -0.2351 0.2657  142  ASN Y N   
26877 C CA  . ASN D 142  ? 2.5252 2.6626 2.0418 -0.3545 -0.2505 0.2786  142  ASN Y CA  
26878 C C   . ASN D 142  ? 2.5730 2.7069 2.0759 -0.3130 -0.2436 0.3052  142  ASN Y C   
26879 O O   . ASN D 142  ? 2.5823 2.7668 2.1155 -0.3071 -0.2498 0.3485  142  ASN Y O   
26880 C CB  . ASN D 142  ? 2.4821 2.6855 2.0444 -0.3884 -0.2663 0.3116  142  ASN Y CB  
26881 C CG  . ASN D 142  ? 2.4662 2.6659 2.0191 -0.4313 -0.2867 0.3176  142  ASN Y CG  
26882 O OD1 . ASN D 142  ? 2.4716 2.6915 2.0305 -0.4202 -0.2937 0.3520  142  ASN Y OD1 
26883 N ND2 . ASN D 142  ? 2.4488 2.6199 1.9853 -0.4802 -0.2966 0.2843  142  ASN Y ND2 
26884 N N   . GLY D 143  ? 2.6128 2.6844 2.0705 -0.2834 -0.2320 0.2789  143  GLY Y N   
26885 C CA  . GLY D 143  ? 2.6692 2.7246 2.1052 -0.2361 -0.2229 0.2991  143  GLY Y CA  
26886 C C   . GLY D 143  ? 2.6982 2.7999 2.1631 -0.1857 -0.2040 0.3344  143  GLY Y C   
26887 O O   . GLY D 143  ? 2.7160 2.7924 2.1620 -0.1543 -0.1867 0.3201  143  GLY Y O   
26888 N N   . GLU D 144  ? 2.6979 2.8669 2.2089 -0.1788 -0.2073 0.3814  144  GLU Y N   
26889 C CA  . GLU D 144  ? 2.7022 2.9258 2.2499 -0.1321 -0.1862 0.4194  144  GLU Y CA  
26890 C C   . GLU D 144  ? 2.6190 2.9018 2.2137 -0.1560 -0.1860 0.4308  144  GLU Y C   
26891 O O   . GLU D 144  ? 2.6041 2.9285 2.2258 -0.1230 -0.1652 0.4559  144  GLU Y O   
26892 C CB  . GLU D 144  ? 2.7514 3.0241 2.3351 -0.1100 -0.1896 0.4671  144  GLU Y CB  
26893 C CG  . GLU D 144  ? 2.8351 3.0495 2.3714 -0.0680 -0.1831 0.4619  144  GLU Y CG  
26894 C CD  . GLU D 144  ? 2.8938 3.0552 2.3834 -0.0158 -0.1539 0.4412  144  GLU Y CD  
26895 O OE1 . GLU D 144  ? 2.8874 3.0796 2.3970 0.0023  -0.1333 0.4486  144  GLU Y OE1 
26896 O OE2 . GLU D 144  ? 2.9476 3.0323 2.3760 0.0054  -0.1527 0.4181  144  GLU Y OE2 
26897 N N   . ASP D 145  ? 2.5642 2.8470 2.1652 -0.2140 -0.2085 0.4120  145  ASP Y N   
26898 C CA  . ASP D 145  ? 2.4960 2.8298 2.1384 -0.2446 -0.2147 0.4223  145  ASP Y CA  
26899 C C   . ASP D 145  ? 2.4365 2.7287 2.0526 -0.2467 -0.2062 0.3827  145  ASP Y C   
26900 O O   . ASP D 145  ? 2.4457 2.6665 2.0139 -0.2455 -0.2052 0.3393  145  ASP Y O   
26901 C CB  . ASP D 145  ? 2.4890 2.8438 2.1507 -0.3062 -0.2450 0.4261  145  ASP Y CB  
26902 C CG  . ASP D 145  ? 2.5035 2.9184 2.2074 -0.3087 -0.2587 0.4775  145  ASP Y CG  
26903 O OD1 . ASP D 145  ? 2.5253 2.9768 2.2552 -0.2614 -0.2431 0.5125  145  ASP Y OD1 
26904 O OD2 . ASP D 145  ? 2.4929 2.9166 2.2037 -0.3580 -0.2858 0.4831  145  ASP Y OD2 
26905 N N   . LEU D 146  ? 2.3715 2.7087 2.0206 -0.2505 -0.2020 0.3996  146  LEU Y N   
26906 C CA  . LEU D 146  ? 2.3189 2.6213 1.9481 -0.2564 -0.1989 0.3669  146  LEU Y CA  
26907 C C   . LEU D 146  ? 2.2606 2.6178 1.9323 -0.2883 -0.2092 0.3864  146  LEU Y C   
26908 O O   . LEU D 146  ? 2.2163 2.6318 1.9222 -0.2699 -0.1968 0.4271  146  LEU Y O   
26909 C CB  . LEU D 146  ? 2.3433 2.6155 1.9415 -0.2014 -0.1716 0.3640  146  LEU Y CB  
26910 C CG  . LEU D 146  ? 2.3436 2.5575 1.9064 -0.2031 -0.1718 0.3237  146  LEU Y CG  
26911 C CD1 . LEU D 146  ? 2.3558 2.5826 1.9139 -0.1656 -0.1484 0.3448  146  LEU Y CD1 
26912 C CD2 . LEU D 146  ? 2.3065 2.5233 1.8881 -0.2573 -0.1964 0.3015  146  LEU Y CD2 
26913 N N   . ASP D 147  ? 2.2521 2.5881 1.9205 -0.3359 -0.2310 0.3566  147  ASP Y N   
26914 C CA  . ASP D 147  ? 2.2247 2.5936 1.9211 -0.3679 -0.2437 0.3656  147  ASP Y CA  
26915 C C   . ASP D 147  ? 2.2840 2.6012 1.9523 -0.3620 -0.2406 0.3277  147  ASP Y C   
26916 O O   . ASP D 147  ? 2.3057 2.5708 1.9527 -0.3849 -0.2531 0.2828  147  ASP Y O   
26917 C CB  . ASP D 147  ? 2.1177 2.4958 1.8276 -0.4249 -0.2716 0.3604  147  ASP Y CB  
26918 C CG  . ASP D 147  ? 2.0280 2.4612 1.7689 -0.4356 -0.2808 0.4051  147  ASP Y CG  
26919 O OD1 . ASP D 147  ? 1.9923 2.4818 1.7662 -0.4062 -0.2687 0.4502  147  ASP Y OD1 
26920 O OD2 . ASP D 147  ? 2.0067 2.4259 1.7388 -0.4737 -0.3003 0.3954  147  ASP Y OD2 
26921 N N   . ALA D 148  ? 2.3319 2.6633 2.0007 -0.3301 -0.2233 0.3469  148  ALA Y N   
26922 C CA  . ALA D 148  ? 2.3677 2.6468 2.0049 -0.3190 -0.2207 0.3163  148  ALA Y CA  
26923 C C   . ALA D 148  ? 2.3872 2.6922 2.0458 -0.3468 -0.2334 0.3271  148  ALA Y C   
26924 O O   . ALA D 148  ? 2.4027 2.7747 2.1014 -0.3648 -0.2372 0.3679  148  ALA Y O   
26925 C CB  . ALA D 148  ? 2.4072 2.6641 2.0122 -0.2628 -0.1919 0.3246  148  ALA Y CB  
26926 N N   . SER D 149  ? 2.3788 2.6282 2.0102 -0.3500 -0.2419 0.2915  149  SER Y N   
26927 C CA  . SER D 149  ? 2.3394 2.5978 1.9826 -0.3772 -0.2579 0.2948  149  SER Y CA  
26928 C C   . SER D 149  ? 2.2968 2.4887 1.8992 -0.3571 -0.2575 0.2647  149  SER Y C   
26929 O O   . SER D 149  ? 2.2789 2.4083 1.8540 -0.3480 -0.2622 0.2227  149  SER Y O   
26930 C CB  . SER D 149  ? 2.3672 2.6211 2.0288 -0.4278 -0.2870 0.2714  149  SER Y CB  
26931 O OG  . SER D 149  ? 2.3725 2.6622 2.0556 -0.4455 -0.2897 0.2859  149  SER Y OG  
26932 N N   . ILE D 150  ? 2.2252 2.4283 1.8221 -0.3512 -0.2529 0.2874  150  ILE Y N   
26933 C CA  . ILE D 150  ? 2.1263 2.2620 1.6823 -0.3403 -0.2599 0.2599  150  ILE Y CA  
26934 C C   . ILE D 150  ? 2.0972 2.2159 1.6687 -0.3839 -0.2942 0.2347  150  ILE Y C   
26935 O O   . ILE D 150  ? 2.0759 2.2443 1.6827 -0.4181 -0.3062 0.2553  150  ILE Y O   
26936 C CB  . ILE D 150  ? 2.0095 2.1578 1.5452 -0.3173 -0.2397 0.2948  150  ILE Y CB  
26937 C CG1 . ILE D 150  ? 1.8467 2.0116 1.3973 -0.3531 -0.2606 0.3067  150  ILE Y CG1 
26938 C CG2 . ILE D 150  ? 1.9967 2.2144 1.5536 -0.2925 -0.2065 0.3433  150  ILE Y CG2 
26939 C CD1 . ILE D 150  ? 1.8066 1.8935 1.3233 -0.3625 -0.2870 0.2662  150  ILE Y CD1 
26940 N N   . ASP D 151  ? 2.0826 2.1302 1.6288 -0.3832 -0.3119 0.1912  151  ASP Y N   
26941 C CA  . ASP D 151  ? 2.0781 2.1076 1.6430 -0.4218 -0.3441 0.1640  151  ASP Y CA  
26942 C C   . ASP D 151  ? 2.1836 2.1412 1.7190 -0.4153 -0.3635 0.1325  151  ASP Y C   
26943 O O   . ASP D 151  ? 2.2001 2.1346 1.6993 -0.3916 -0.3553 0.1471  151  ASP Y O   
26944 C CB  . ASP D 151  ? 1.9828 2.0101 1.5723 -0.4428 -0.3527 0.1323  151  ASP Y CB  
26945 C CG  . ASP D 151  ? 1.9042 1.9475 1.5231 -0.4881 -0.3770 0.1250  151  ASP Y CG  
26946 O OD1 . ASP D 151  ? 1.8984 1.9489 1.5184 -0.5035 -0.3914 0.1414  151  ASP Y OD1 
26947 O OD2 . ASP D 151  ? 1.8471 1.8919 1.4834 -0.5089 -0.3813 0.1028  151  ASP Y OD2 
26948 N N   . SER D 152  ? 2.2823 2.2033 1.8333 -0.4365 -0.3894 0.0897  152  SER Y N   
26949 C CA  . SER D 152  ? 2.4374 2.2918 1.9706 -0.4349 -0.4149 0.0588  152  SER Y CA  
26950 C C   . SER D 152  ? 2.5551 2.3726 2.1144 -0.4492 -0.4358 0.0069  152  SER Y C   
26951 O O   . SER D 152  ? 2.5318 2.3783 2.1243 -0.4724 -0.4349 -0.0040 152  SER Y O   
26952 C CB  . SER D 152  ? 2.4339 2.2954 1.9656 -0.4570 -0.4337 0.0789  152  SER Y CB  
26953 O OG  . SER D 152  ? 2.4504 2.3375 1.9552 -0.4417 -0.4138 0.1244  152  SER Y OG  
26954 N N   . PHE D 153  ? 2.7306 2.4825 2.2738 -0.4353 -0.4543 -0.0241 153  PHE Y N   
26955 C CA  . PHE D 153  ? 2.8695 2.5844 2.4443 -0.4479 -0.4776 -0.0734 153  PHE Y CA  
26956 C C   . PHE D 153  ? 2.9487 2.6087 2.5162 -0.4502 -0.5124 -0.0906 153  PHE Y C   
26957 O O   . PHE D 153  ? 2.9909 2.6156 2.5148 -0.4315 -0.5179 -0.0757 153  PHE Y O   
26958 C CB  . PHE D 153  ? 2.9622 2.6489 2.5363 -0.4279 -0.4684 -0.1009 153  PHE Y CB  
26959 C CG  . PHE D 153  ? 3.0445 2.7009 2.6603 -0.4407 -0.4889 -0.1504 153  PHE Y CG  
26960 C CD1 . PHE D 153  ? 3.0487 2.7324 2.7017 -0.4576 -0.4761 -0.1709 153  PHE Y CD1 
26961 C CD2 . PHE D 153  ? 3.1149 2.7153 2.7338 -0.4362 -0.5208 -0.1757 153  PHE Y CD2 
26962 C CE1 . PHE D 153  ? 3.0632 2.7235 2.7591 -0.4686 -0.4903 -0.2160 153  PHE Y CE1 
26963 C CE2 . PHE D 153  ? 3.1244 2.7026 2.7913 -0.4463 -0.5389 -0.2202 153  PHE Y CE2 
26964 C CZ  . PHE D 153  ? 3.0966 2.7070 2.8038 -0.4620 -0.5215 -0.2405 153  PHE Y CZ  
26965 N N   . LEU D 154  ? 2.9826 2.6321 2.5902 -0.4730 -0.5359 -0.1223 154  LEU Y N   
26966 C CA  . LEU D 154  ? 3.0280 2.6255 2.6349 -0.4768 -0.5729 -0.1401 154  LEU Y CA  
26967 C C   . LEU D 154  ? 3.0634 2.6092 2.6970 -0.4665 -0.5937 -0.1873 154  LEU Y C   
26968 O O   . LEU D 154  ? 3.0299 2.5836 2.7145 -0.4801 -0.5974 -0.2208 154  LEU Y O   
26969 C CB  . LEU D 154  ? 2.9922 2.6099 2.6230 -0.5086 -0.5888 -0.1385 154  LEU Y CB  
26970 C CG  . LEU D 154  ? 2.9590 2.6301 2.5676 -0.5219 -0.5717 -0.0885 154  LEU Y CG  
26971 C CD1 . LEU D 154  ? 2.9252 2.6254 2.5611 -0.5572 -0.5810 -0.0884 154  LEU Y CD1 
26972 C CD2 . LEU D 154  ? 2.9855 2.6343 2.5469 -0.5124 -0.5807 -0.0570 154  LEU Y CD2 
26973 N N   . ILE D 155  ? 3.1359 2.6279 2.7339 -0.4428 -0.6067 -0.1886 155  ILE Y N   
26974 C CA  . ILE D 155  ? 3.1669 2.6042 2.7886 -0.4333 -0.6341 -0.2288 155  ILE Y CA  
26975 C C   . ILE D 155  ? 3.2476 2.6422 2.8821 -0.4432 -0.6770 -0.2443 155  ILE Y C   
26976 O O   . ILE D 155  ? 3.2746 2.6349 2.8601 -0.4392 -0.6941 -0.2225 155  ILE Y O   
26977 C CB  . ILE D 155  ? 3.1943 2.5829 2.7642 -0.4049 -0.6341 -0.2223 155  ILE Y CB  
26978 C CG1 . ILE D 155  ? 3.1543 2.5818 2.6905 -0.3917 -0.5909 -0.1933 155  ILE Y CG1 
26979 C CG2 . ILE D 155  ? 3.1964 2.5421 2.8016 -0.3976 -0.6568 -0.2633 155  ILE Y CG2 
26980 C CD1 . ILE D 155  ? 3.1957 2.5713 2.6739 -0.3623 -0.5878 -0.1870 155  ILE Y CD1 
26981 N N   . GLN D 156  ? 3.2877 2.6826 2.9874 -0.4557 -0.6937 -0.2821 156  GLN Y N   
26982 C CA  . GLN D 156  ? 3.3736 2.7336 3.0941 -0.4662 -0.7339 -0.2984 156  GLN Y CA  
26983 C C   . GLN D 156  ? 3.4591 2.7517 3.1947 -0.4513 -0.7746 -0.3269 156  GLN Y C   
26984 O O   . GLN D 156  ? 3.4628 2.7286 3.2385 -0.4580 -0.8091 -0.3518 156  GLN Y O   
26985 C CB  . GLN D 156  ? 3.3627 2.7595 3.1442 -0.4882 -0.7292 -0.3221 156  GLN Y CB  
26986 C CG  . GLN D 156  ? 3.3982 2.7618 3.1967 -0.4999 -0.7684 -0.3354 156  GLN Y CG  
26987 C CD  . GLN D 156  ? 3.4377 2.7689 3.1707 -0.5009 -0.7901 -0.3002 156  GLN Y CD  
26988 O OE1 . GLN D 156  ? 3.4351 2.7993 3.1234 -0.5093 -0.7677 -0.2609 156  GLN Y OE1 
26989 N NE2 . GLN D 156  ? 3.4797 2.7458 3.2078 -0.4933 -0.8343 -0.3133 156  GLN Y NE2 
26990 N N   . LYS D 157  ? 3.5296 2.7914 3.2321 -0.4310 -0.7730 -0.3226 157  LYS Y N   
26991 C CA  . LYS D 157  ? 3.6141 2.8094 3.3301 -0.4183 -0.8146 -0.3482 157  LYS Y CA  
26992 C C   . LYS D 157  ? 3.6971 2.8342 3.3336 -0.3981 -0.8227 -0.3276 157  LYS Y C   
26993 O O   . LYS D 157  ? 3.7111 2.8615 3.2821 -0.3910 -0.7916 -0.2937 157  LYS Y O   
26994 C CB  . LYS D 157  ? 3.5889 2.8031 3.3869 -0.4179 -0.8116 -0.3876 157  LYS Y CB  
26995 C CG  . LYS D 157  ? 3.5538 2.8081 3.4330 -0.4355 -0.8101 -0.4161 157  LYS Y CG  
26996 C CD  . LYS D 157  ? 3.5840 2.7937 3.4880 -0.4386 -0.8592 -0.4319 157  LYS Y CD  
26997 C CE  . LYS D 157  ? 3.5492 2.7949 3.5236 -0.4542 -0.8543 -0.4583 157  LYS Y CE  
26998 N NZ  . LYS D 157  ? 3.5816 2.7807 3.5775 -0.4555 -0.9033 -0.4728 157  LYS Y NZ  
26999 N N   . GLU D 158  ? 3.7625 2.8326 3.4053 -0.3888 -0.8658 -0.3483 158  GLU Y N   
27000 C CA  . GLU D 158  ? 3.8576 2.8565 3.4209 -0.3708 -0.8807 -0.3335 158  GLU Y CA  
27001 C C   . GLU D 158  ? 3.8329 2.8351 3.4024 -0.3580 -0.8618 -0.3435 158  GLU Y C   
27002 O O   . GLU D 158  ? 3.8754 2.8567 3.3692 -0.3429 -0.8403 -0.3205 158  GLU Y O   
27003 C CB  . GLU D 158  ? 3.9518 2.8683 3.5135 -0.3697 -0.9433 -0.3492 158  GLU Y CB  
27004 C CG  . GLU D 158  ? 4.0654 2.8961 3.5538 -0.3528 -0.9675 -0.3428 158  GLU Y CG  
27005 C CD  . GLU D 158  ? 4.1510 2.9500 3.5214 -0.3433 -0.9457 -0.3029 158  GLU Y CD  
27006 O OE1 . GLU D 158  ? 4.1440 2.9881 3.4950 -0.3514 -0.9171 -0.2787 158  GLU Y OE1 
27007 O OE2 . GLU D 158  ? 4.2296 2.9571 3.5261 -0.3281 -0.9569 -0.2955 158  GLU Y OE2 
27008 N N   . GLU D 159  ? 3.7685 2.7956 3.4281 -0.3644 -0.8690 -0.3778 159  GLU Y N   
27009 C CA  . GLU D 159  ? 3.7203 2.7610 3.3978 -0.3577 -0.8487 -0.3889 159  GLU Y CA  
27010 C C   . GLU D 159  ? 3.5953 2.7220 3.3482 -0.3723 -0.8105 -0.4034 159  GLU Y C   
27011 O O   . GLU D 159  ? 3.5600 2.7168 3.3832 -0.3864 -0.8189 -0.4238 159  GLU Y O   
27012 C CB  . GLU D 159  ? 3.7574 2.7424 3.4739 -0.3538 -0.8949 -0.4170 159  GLU Y CB  
27013 C CG  . GLU D 159  ? 3.7364 2.7396 3.4856 -0.3520 -0.8768 -0.4317 159  GLU Y CG  
27014 C CD  . GLU D 159  ? 3.7574 2.7148 3.5621 -0.3523 -0.9249 -0.4597 159  GLU Y CD  
27015 O OE1 . GLU D 159  ? 3.7231 2.7174 3.6019 -0.3597 -0.9141 -0.4821 159  GLU Y OE1 
27016 O OE2 . GLU D 159  ? 3.8064 2.6908 3.5816 -0.3465 -0.9745 -0.4583 159  GLU Y OE2 
27017 N N   . ILE D 160  ? 3.5344 2.6959 3.2689 -0.3689 -0.7691 -0.3934 160  ILE Y N   
27018 C CA  . ILE D 160  ? 3.4309 2.6701 3.2198 -0.3845 -0.7298 -0.4019 160  ILE Y CA  
27019 C C   . ILE D 160  ? 3.3986 2.6551 3.2088 -0.3840 -0.7069 -0.4145 160  ILE Y C   
27020 O O   . ILE D 160  ? 3.4184 2.6476 3.1679 -0.3692 -0.6977 -0.3980 160  ILE Y O   
27021 C CB  . ILE D 160  ? 3.2589 2.5433 3.0020 -0.3888 -0.6952 -0.3681 160  ILE Y CB  
27022 C CG1 . ILE D 160  ? 3.1736 2.5310 2.9679 -0.4078 -0.6591 -0.3769 160  ILE Y CG1 
27023 C CG2 . ILE D 160  ? 3.2950 2.5610 2.9488 -0.3692 -0.6748 -0.3331 160  ILE Y CG2 
27024 C CD1 . ILE D 160  ? 3.1426 2.5448 2.9037 -0.4163 -0.6330 -0.3449 160  ILE Y CD1 
27025 N N   . SER D 161  ? 3.3524 2.6508 3.2476 -0.4005 -0.6976 -0.4447 161  SER Y N   
27026 C CA  . SER D 161  ? 3.3275 2.6453 3.2549 -0.4055 -0.6768 -0.4607 161  SER Y CA  
27027 C C   . SER D 161  ? 3.3203 2.6790 3.2024 -0.4078 -0.6296 -0.4376 161  SER Y C   
27028 O O   . SER D 161  ? 3.2924 2.6952 3.1686 -0.4176 -0.6057 -0.4245 161  SER Y O   
27029 C CB  . SER D 161  ? 3.2863 2.6411 3.3184 -0.4238 -0.6754 -0.4990 161  SER Y CB  
27030 O OG  . SER D 161  ? 3.2435 2.6435 3.2965 -0.4377 -0.6559 -0.5004 161  SER Y OG  
27031 N N   . LEU D 162  ? 3.3364 2.6774 3.1863 -0.3995 -0.6192 -0.4322 162  LEU Y N   
27032 C CA  . LEU D 162  ? 3.3318 2.7051 3.1373 -0.3992 -0.5778 -0.4101 162  LEU Y CA  
27033 C C   . LEU D 162  ? 3.2675 2.7052 3.1279 -0.4244 -0.5454 -0.4248 162  LEU Y C   
27034 O O   . LEU D 162  ? 3.2393 2.7128 3.0683 -0.4290 -0.5133 -0.4040 162  LEU Y O   
27035 C CB  . LEU D 162  ? 3.3777 2.7106 3.1404 -0.3858 -0.5776 -0.4058 162  LEU Y CB  
27036 C CG  . LEU D 162  ? 3.3846 2.7353 3.0872 -0.3785 -0.5406 -0.3791 162  LEU Y CG  
27037 C CD1 . LEU D 162  ? 3.3906 2.7510 3.0321 -0.3629 -0.5278 -0.3426 162  LEU Y CD1 
27038 C CD2 . LEU D 162  ? 3.4374 2.7338 3.0940 -0.3637 -0.5476 -0.3776 162  LEU Y CD2 
27039 N N   . LYS D 163  ? 3.2509 2.7012 3.1926 -0.4406 -0.5539 -0.4602 163  LYS Y N   
27040 C CA  . LYS D 163  ? 3.2024 2.7073 3.1929 -0.4652 -0.5229 -0.4768 163  LYS Y CA  
27041 C C   . LYS D 163  ? 3.2012 2.7332 3.1767 -0.4714 -0.5160 -0.4612 163  LYS Y C   
27042 O O   . LYS D 163  ? 3.2075 2.7752 3.1559 -0.4825 -0.4860 -0.4440 163  LYS Y O   
27043 C CB  . LYS D 163  ? 3.1686 2.6797 3.2527 -0.4778 -0.5336 -0.5185 163  LYS Y CB  
27044 C CG  . LYS D 163  ? 3.1071 2.6668 3.2391 -0.5013 -0.5045 -0.5379 163  LYS Y CG  
27045 C CD  . LYS D 163  ? 3.0715 2.6318 3.2923 -0.5053 -0.5234 -0.5747 163  LYS Y CD  
27046 C CE  . LYS D 163  ? 3.0230 2.6260 3.2891 -0.5280 -0.4894 -0.5980 163  LYS Y CE  
27047 N NZ  . LYS D 163  ? 3.0046 2.6322 3.2800 -0.5449 -0.4516 -0.6076 163  LYS Y NZ  
27048 N N   . GLU D 164  ? 3.1994 2.7110 3.1914 -0.4656 -0.5473 -0.4662 164  GLU Y N   
27049 C CA  . GLU D 164  ? 3.1919 2.7221 3.1692 -0.4727 -0.5473 -0.4513 164  GLU Y CA  
27050 C C   . GLU D 164  ? 3.1175 2.6539 3.0151 -0.4632 -0.5350 -0.4064 164  GLU Y C   
27051 O O   . GLU D 164  ? 3.0660 2.6368 2.9478 -0.4757 -0.5193 -0.3878 164  GLU Y O   
27052 C CB  . GLU D 164  ? 3.2993 2.7954 3.3017 -0.4661 -0.5885 -0.4634 164  GLU Y CB  
27053 C CG  . GLU D 164  ? 3.3784 2.8866 3.3598 -0.4743 -0.5931 -0.4459 164  GLU Y CG  
27054 C CD  . GLU D 164  ? 3.4712 2.9348 3.4562 -0.4648 -0.6373 -0.4496 164  GLU Y CD  
27055 O OE1 . GLU D 164  ? 3.5186 2.9414 3.5253 -0.4517 -0.6660 -0.4666 164  GLU Y OE1 
27056 O OE2 . GLU D 164  ? 3.4961 2.9627 3.4603 -0.4720 -0.6457 -0.4342 164  GLU Y OE2 
27057 N N   . LEU D 165  ? 3.0987 2.6006 2.9471 -0.4411 -0.5427 -0.3887 165  LEU Y N   
27058 C CA  . LEU D 165  ? 3.0654 2.5731 2.8410 -0.4276 -0.5271 -0.3467 165  LEU Y CA  
27059 C C   . LEU D 165  ? 3.0346 2.5905 2.8023 -0.4386 -0.4887 -0.3341 165  LEU Y C   
27060 O O   . LEU D 165  ? 3.0266 2.6158 2.7645 -0.4413 -0.4718 -0.3029 165  LEU Y O   
27061 C CB  . LEU D 165  ? 3.0435 2.4968 2.7664 -0.4003 -0.5396 -0.3360 165  LEU Y CB  
27062 C CG  . LEU D 165  ? 2.9969 2.4354 2.6425 -0.3789 -0.5345 -0.2954 165  LEU Y CG  
27063 C CD1 . LEU D 165  ? 2.9918 2.4023 2.6273 -0.3769 -0.5641 -0.2903 165  LEU Y CD1 
27064 C CD2 . LEU D 165  ? 3.0124 2.4016 2.6006 -0.3530 -0.5336 -0.2870 165  LEU Y CD2 
27065 N N   . ASP D 166  ? 3.0404 2.5991 2.8364 -0.4467 -0.4765 -0.3578 166  ASP Y N   
27066 C CA  . ASP D 166  ? 3.0402 2.6342 2.8233 -0.4576 -0.4428 -0.3478 166  ASP Y CA  
27067 C C   . ASP D 166  ? 3.0212 2.6607 2.8374 -0.4871 -0.4264 -0.3554 166  ASP Y C   
27068 O O   . ASP D 166  ? 3.0084 2.6805 2.7999 -0.4971 -0.4032 -0.3338 166  ASP Y O   
27069 C CB  . ASP D 166  ? 3.0673 2.6424 2.8643 -0.4584 -0.4368 -0.3704 166  ASP Y CB  
27070 C CG  . ASP D 166  ? 3.1066 2.6963 2.8608 -0.4575 -0.4087 -0.3495 166  ASP Y CG  
27071 O OD1 . ASP D 166  ? 3.1167 2.7311 2.8322 -0.4525 -0.3954 -0.3159 166  ASP Y OD1 
27072 O OD2 . ASP D 166  ? 3.1284 2.7047 2.8892 -0.4621 -0.4014 -0.3655 166  ASP Y OD2 
27073 N N   . PHE D 167  ? 3.0443 2.6819 2.9145 -0.5006 -0.4399 -0.3862 167  PHE Y N   
27074 C CA  . PHE D 167  ? 3.0548 2.7252 2.9533 -0.5284 -0.4258 -0.3983 167  PHE Y CA  
27075 C C   . PHE D 167  ? 3.0135 2.7055 2.8788 -0.5342 -0.4281 -0.3650 167  PHE Y C   
27076 O O   . PHE D 167  ? 3.0166 2.7395 2.8715 -0.5554 -0.4089 -0.3546 167  PHE Y O   
27077 C CB  . PHE D 167  ? 3.1180 2.7761 3.0841 -0.5366 -0.4405 -0.4409 167  PHE Y CB  
27078 C CG  . PHE D 167  ? 3.1483 2.8318 3.1421 -0.5644 -0.4221 -0.4598 167  PHE Y CG  
27079 C CD1 . PHE D 167  ? 3.1654 2.8515 3.1594 -0.5729 -0.4352 -0.4559 167  PHE Y CD1 
27080 C CD2 . PHE D 167  ? 3.1628 2.8620 3.1772 -0.5829 -0.3919 -0.4819 167  PHE Y CD2 
27081 C CE1 . PHE D 167  ? 3.1691 2.8699 3.1803 -0.5981 -0.4190 -0.4742 167  PHE Y CE1 
27082 C CE2 . PHE D 167  ? 3.1682 2.8833 3.1993 -0.6084 -0.3729 -0.5004 167  PHE Y CE2 
27083 C CZ  . PHE D 167  ? 3.1713 2.8855 3.1996 -0.6153 -0.3868 -0.4969 167  PHE Y CZ  
27084 N N   . LYS D 168  ? 2.9501 2.6237 2.7970 -0.5173 -0.4527 -0.3473 168  LYS Y N   
27085 C CA  . LYS D 168  ? 2.8648 2.5589 2.6818 -0.5230 -0.4569 -0.3128 168  LYS Y CA  
27086 C C   . LYS D 168  ? 2.8072 2.5257 2.5730 -0.5119 -0.4385 -0.2679 168  LYS Y C   
27087 O O   . LYS D 168  ? 2.7783 2.5318 2.5281 -0.5253 -0.4310 -0.2384 168  LYS Y O   
27088 C CB  . LYS D 168  ? 2.8530 2.5163 2.6701 -0.5126 -0.4901 -0.3119 168  LYS Y CB  
27089 C CG  . LYS D 168  ? 2.8273 2.4716 2.6976 -0.5251 -0.5107 -0.3518 168  LYS Y CG  
27090 C CD  . LYS D 168  ? 2.8279 2.4338 2.6946 -0.5135 -0.5479 -0.3507 168  LYS Y CD  
27091 C CE  . LYS D 168  ? 2.8130 2.4023 2.7339 -0.5253 -0.5687 -0.3882 168  LYS Y CE  
27092 N NZ  . LYS D 168  ? 2.8324 2.3827 2.7449 -0.5176 -0.6077 -0.3842 168  LYS Y NZ  
27093 N N   . ILE D 169  ? 2.7780 2.4768 2.5200 -0.4875 -0.4326 -0.2629 169  ILE Y N   
27094 C CA  . ILE D 169  ? 2.7165 2.4344 2.4131 -0.4722 -0.4124 -0.2247 169  ILE Y CA  
27095 C C   . ILE D 169  ? 2.7083 2.4649 2.4071 -0.4920 -0.3876 -0.2178 169  ILE Y C   
27096 O O   . ILE D 169  ? 2.7188 2.5064 2.3904 -0.4880 -0.3735 -0.1808 169  ILE Y O   
27097 C CB  . ILE D 169  ? 2.6602 2.3378 2.3279 -0.4421 -0.4118 -0.2273 169  ILE Y CB  
27098 C CG1 . ILE D 169  ? 2.6274 2.2650 2.2682 -0.4183 -0.4333 -0.2187 169  ILE Y CG1 
27099 C CG2 . ILE D 169  ? 2.6354 2.3333 2.2648 -0.4290 -0.3864 -0.1966 169  ILE Y CG2 
27100 C CD1 . ILE D 169  ? 2.5994 2.2621 2.2184 -0.4168 -0.4332 -0.1819 169  ILE Y CD1 
27101 N N   . ARG D 170  ? 2.7013 2.4547 2.4331 -0.5135 -0.3823 -0.2534 170  ARG Y N   
27102 C CA  . ARG D 170  ? 2.7008 2.4820 2.4302 -0.5367 -0.3600 -0.2511 170  ARG Y CA  
27103 C C   . ARG D 170  ? 2.6600 2.4646 2.4071 -0.5696 -0.3607 -0.2553 170  ARG Y C   
27104 O O   . ARG D 170  ? 2.6442 2.4764 2.3737 -0.5883 -0.3482 -0.2348 170  ARG Y O   
27105 C CB  . ARG D 170  ? 2.7706 2.5318 2.5146 -0.5414 -0.3477 -0.2844 170  ARG Y CB  
27106 C CG  . ARG D 170  ? 2.8642 2.5957 2.5840 -0.5116 -0.3488 -0.2800 170  ARG Y CG  
27107 C CD  . ARG D 170  ? 2.9441 2.6687 2.6605 -0.5220 -0.3301 -0.2954 170  ARG Y CD  
27108 N NE  . ARG D 170  ? 3.0153 2.6995 2.7270 -0.5019 -0.3375 -0.3100 170  ARG Y NE  
27109 C CZ  . ARG D 170  ? 3.0530 2.7233 2.7593 -0.5085 -0.3253 -0.3230 170  ARG Y CZ  
27110 N NH1 . ARG D 170  ? 3.0589 2.7514 2.7614 -0.5343 -0.3035 -0.3236 170  ARG Y NH1 
27111 N NH2 . ARG D 170  ? 3.0778 2.7076 2.7782 -0.4912 -0.3365 -0.3346 170  ARG Y NH2 
27112 N N   . GLN D 171  ? 2.6435 2.4327 2.4225 -0.5766 -0.3775 -0.2813 171  GLN Y N   
27113 C CA  . GLN D 171  ? 2.6216 2.4237 2.4112 -0.6055 -0.3815 -0.2856 171  GLN Y CA  
27114 C C   . GLN D 171  ? 2.6107 2.4434 2.3687 -0.6103 -0.3866 -0.2374 171  GLN Y C   
27115 O O   . GLN D 171  ? 2.5837 2.4364 2.3320 -0.6380 -0.3820 -0.2260 171  GLN Y O   
27116 C CB  . GLN D 171  ? 2.6114 2.3877 2.4360 -0.6040 -0.4044 -0.3147 171  GLN Y CB  
27117 C CG  . GLN D 171  ? 2.5846 2.3659 2.4146 -0.6313 -0.4121 -0.3190 171  GLN Y CG  
27118 C CD  . GLN D 171  ? 2.5561 2.3141 2.4029 -0.6237 -0.4426 -0.3267 171  GLN Y CD  
27119 O OE1 . GLN D 171  ? 2.5490 2.3005 2.3810 -0.6032 -0.4595 -0.3040 171  GLN Y OE1 
27120 N NE2 . GLN D 171  ? 2.5467 2.2883 2.4209 -0.6401 -0.4495 -0.3589 171  GLN Y NE2 
27121 N N   . GLN D 172  ? 2.6089 2.4431 2.3503 -0.5840 -0.3962 -0.2089 172  GLN Y N   
27122 C CA  . GLN D 172  ? 2.5912 2.4586 2.3089 -0.5842 -0.3997 -0.1601 172  GLN Y CA  
27123 C C   . GLN D 172  ? 2.6114 2.5152 2.3080 -0.5866 -0.3798 -0.1267 172  GLN Y C   
27124 O O   . GLN D 172  ? 2.6042 2.5422 2.2942 -0.6068 -0.3813 -0.0959 172  GLN Y O   
27125 C CB  . GLN D 172  ? 2.5305 2.3853 2.2344 -0.5536 -0.4109 -0.1417 172  GLN Y CB  
27126 C CG  . GLN D 172  ? 2.4731 2.2983 2.1912 -0.5566 -0.4372 -0.1600 172  GLN Y CG  
27127 C CD  . GLN D 172  ? 2.4380 2.2710 2.1327 -0.5452 -0.4480 -0.1219 172  GLN Y CD  
27128 O OE1 . GLN D 172  ? 2.4336 2.2680 2.1025 -0.5181 -0.4381 -0.0980 172  GLN Y OE1 
27129 N NE2 . GLN D 172  ? 2.4202 2.2563 2.1209 -0.5664 -0.4673 -0.1156 172  GLN Y NE2 
27130 N N   . LEU D 173  ? 2.6333 2.5271 2.3191 -0.5665 -0.3641 -0.1321 173  LEU Y N   
27131 C CA  . LEU D 173  ? 2.6467 2.5678 2.3127 -0.5668 -0.3466 -0.1048 173  LEU Y CA  
27132 C C   . LEU D 173  ? 2.6527 2.5841 2.3212 -0.6056 -0.3411 -0.1147 173  LEU Y C   
27133 O O   . LEU D 173  ? 2.6583 2.6214 2.3132 -0.6187 -0.3376 -0.0813 173  LEU Y O   
27134 C CB  . LEU D 173  ? 2.6598 2.5562 2.3105 -0.5391 -0.3334 -0.1152 173  LEU Y CB  
27135 C CG  . LEU D 173  ? 2.6908 2.5666 2.3255 -0.4991 -0.3368 -0.1052 173  LEU Y CG  
27136 C CD1 . LEU D 173  ? 2.7172 2.5553 2.3356 -0.4778 -0.3282 -0.1250 173  LEU Y CD1 
27137 C CD2 . LEU D 173  ? 2.6940 2.6065 2.3101 -0.4810 -0.3308 -0.0540 173  LEU Y CD2 
27138 N N   . VAL D 174  ? 2.6432 2.5460 2.3292 -0.6236 -0.3405 -0.1602 174  VAL Y N   
27139 C CA  . VAL D 174  ? 2.6379 2.5392 2.3207 -0.6609 -0.3319 -0.1771 174  VAL Y CA  
27140 C C   . VAL D 174  ? 2.6144 2.5350 2.2908 -0.6893 -0.3453 -0.1557 174  VAL Y C   
27141 O O   . VAL D 174  ? 2.6345 2.5615 2.2913 -0.7188 -0.3402 -0.1480 174  VAL Y O   
27142 C CB  . VAL D 174  ? 2.7158 2.5832 2.4252 -0.6714 -0.3263 -0.2325 174  VAL Y CB  
27143 C CG1 . VAL D 174  ? 2.7335 2.5957 2.4332 -0.7106 -0.3150 -0.2496 174  VAL Y CG1 
27144 C CG2 . VAL D 174  ? 2.7165 2.5643 2.4335 -0.6513 -0.3137 -0.2547 174  VAL Y CG2 
27145 N N   . ASN D 175  ? 2.5994 2.5244 2.2882 -0.6823 -0.3643 -0.1456 175  ASN Y N   
27146 C CA  . ASN D 175  ? 2.5636 2.4996 2.2475 -0.7111 -0.3811 -0.1292 175  ASN Y CA  
27147 C C   . ASN D 175  ? 2.5186 2.4968 2.1936 -0.7074 -0.3923 -0.0725 175  ASN Y C   
27148 O O   . ASN D 175  ? 2.5208 2.5126 2.1899 -0.7344 -0.4081 -0.0513 175  ASN Y O   
27149 C CB  . ASN D 175  ? 2.5628 2.4694 2.2674 -0.7126 -0.3972 -0.1606 175  ASN Y CB  
27150 C CG  . ASN D 175  ? 2.5528 2.4237 2.2788 -0.7103 -0.3856 -0.2157 175  ASN Y CG  
27151 O OD1 . ASN D 175  ? 2.5515 2.3979 2.3036 -0.6981 -0.3970 -0.2438 175  ASN Y OD1 
27152 N ND2 . ASN D 175  ? 2.5494 2.4170 2.2661 -0.7226 -0.3633 -0.2308 175  ASN Y ND2 
27153 N N   . ASN D 176  ? 2.4662 2.4643 2.1406 -0.6741 -0.3838 -0.0476 176  ASN Y N   
27154 C CA  . ASN D 176  ? 2.4063 2.4482 2.0797 -0.6654 -0.3903 0.0059  176  ASN Y CA  
27155 C C   . ASN D 176  ? 2.3522 2.4258 2.0183 -0.6402 -0.3734 0.0401  176  ASN Y C   
27156 O O   . ASN D 176  ? 2.3201 2.4387 1.9911 -0.6355 -0.3755 0.0877  176  ASN Y O   
27157 C CB  . ASN D 176  ? 2.4150 2.4491 2.0965 -0.6466 -0.4024 0.0087  176  ASN Y CB  
27158 C CG  . ASN D 176  ? 2.4208 2.4248 2.1099 -0.6712 -0.4235 -0.0194 176  ASN Y CG  
27159 O OD1 . ASN D 176  ? 2.4172 2.4370 2.1061 -0.6911 -0.4412 0.0051  176  ASN Y OD1 
27160 N ND2 . ASN D 176  ? 2.4224 2.3828 2.1202 -0.6696 -0.4220 -0.0706 176  ASN Y ND2 
27161 N N   . TYR D 177  ? 2.3215 2.3726 1.9779 -0.6243 -0.3568 0.0171  177  TYR Y N   
27162 C CA  . TYR D 177  ? 2.3043 2.3782 1.9502 -0.5987 -0.3418 0.0472  177  TYR Y CA  
27163 C C   . TYR D 177  ? 2.3684 2.4337 1.9991 -0.6141 -0.3323 0.0380  177  TYR Y C   
27164 O O   . TYR D 177  ? 2.3888 2.4575 2.0070 -0.5907 -0.3197 0.0514  177  TYR Y O   
27165 C CB  . TYR D 177  ? 2.2346 2.2878 1.8730 -0.5536 -0.3312 0.0409  177  TYR Y CB  
27166 C CG  . TYR D 177  ? 2.1642 2.2339 1.8092 -0.5372 -0.3378 0.0651  177  TYR Y CG  
27167 C CD1 . TYR D 177  ? 2.1412 2.1805 1.7918 -0.5413 -0.3521 0.0388  177  TYR Y CD1 
27168 C CD2 . TYR D 177  ? 2.1298 2.2466 1.7770 -0.5196 -0.3302 0.1154  177  TYR Y CD2 
27169 C CE1 . TYR D 177  ? 2.1182 2.1681 1.7690 -0.5297 -0.3593 0.0618  177  TYR Y CE1 
27170 C CE2 . TYR D 177  ? 2.1130 2.2456 1.7644 -0.5073 -0.3335 0.1389  177  TYR Y CE2 
27171 C CZ  . TYR D 177  ? 2.1007 2.1973 1.7502 -0.5137 -0.3486 0.1118  177  TYR Y CZ  
27172 O OH  . TYR D 177  ? 2.0784 2.1852 1.7260 -0.5043 -0.3528 0.1350  177  TYR Y OH  
27173 N N   . GLY D 178  ? 2.4079 2.4581 2.0352 -0.6539 -0.3383 0.0156  178  GLY Y N   
27174 C CA  . GLY D 178  ? 2.4814 2.5182 2.0875 -0.6753 -0.3298 0.0061  178  GLY Y CA  
27175 C C   . GLY D 178  ? 2.5540 2.5534 2.1501 -0.6584 -0.3124 -0.0296 178  GLY Y C   
27176 O O   . GLY D 178  ? 2.5561 2.5523 2.1317 -0.6552 -0.3030 -0.0205 178  GLY Y O   
27177 N N   . LEU D 179  ? 2.6305 2.6002 2.2418 -0.6484 -0.3104 -0.0691 179  LEU Y N   
27178 C CA  . LEU D 179  ? 2.7187 2.6529 2.3260 -0.6350 -0.2966 -0.1038 179  LEU Y CA  
27179 C C   . LEU D 179  ? 2.8148 2.7231 2.4191 -0.6705 -0.2863 -0.1428 179  LEU Y C   
27180 O O   . LEU D 179  ? 2.8077 2.7129 2.4214 -0.6983 -0.2907 -0.1595 179  LEU Y O   
27181 C CB  . LEU D 179  ? 2.7116 2.6249 2.3390 -0.6061 -0.3015 -0.1257 179  LEU Y CB  
27182 C CG  . LEU D 179  ? 2.7103 2.5865 2.3356 -0.5897 -0.2916 -0.1573 179  LEU Y CG  
27183 C CD1 . LEU D 179  ? 2.7241 2.6004 2.3170 -0.5695 -0.2816 -0.1319 179  LEU Y CD1 
27184 C CD2 . LEU D 179  ? 2.6908 2.5432 2.3348 -0.5635 -0.3026 -0.1763 179  LEU Y CD2 
27185 N N   . TYR D 180  ? 2.9113 2.7983 2.4993 -0.6690 -0.2715 -0.1572 180  TYR Y N   
27186 C CA  . TYR D 180  ? 3.0116 2.8729 2.5937 -0.7015 -0.2561 -0.1941 180  TYR Y CA  
27187 C C   . TYR D 180  ? 3.0917 2.9586 2.6483 -0.7421 -0.2555 -0.1835 180  TYR Y C   
27188 O O   . TYR D 180  ? 3.1172 2.9650 2.6745 -0.7723 -0.2459 -0.2161 180  TYR Y O   
27189 C CB  . TYR D 180  ? 3.0237 2.8649 2.6445 -0.7034 -0.2527 -0.2418 180  TYR Y CB  
27190 C CG  . TYR D 180  ? 3.0394 2.8646 2.6803 -0.6698 -0.2542 -0.2568 180  TYR Y CG  
27191 C CD1 . TYR D 180  ? 3.0660 2.8785 2.6829 -0.6540 -0.2469 -0.2478 180  TYR Y CD1 
27192 C CD2 . TYR D 180  ? 3.0351 2.8523 2.7152 -0.6548 -0.2657 -0.2795 180  TYR Y CD2 
27193 C CE1 . TYR D 180  ? 3.0699 2.8607 2.6986 -0.6250 -0.2511 -0.2606 180  TYR Y CE1 
27194 C CE2 . TYR D 180  ? 3.0371 2.8339 2.7315 -0.6261 -0.2711 -0.2920 180  TYR Y CE2 
27195 C CZ  . TYR D 180  ? 3.0539 2.8367 2.7210 -0.6119 -0.2637 -0.2825 180  TYR Y CZ  
27196 O OH  . TYR D 180  ? 3.0549 2.8107 2.7300 -0.5852 -0.2717 -0.2943 180  TYR Y OH  
27197 N N   . LYS D 181  ? 3.1399 3.0314 2.6734 -0.7421 -0.2660 -0.1375 181  LYS Y N   
27198 C CA  . LYS D 181  ? 3.2009 3.0963 2.7059 -0.7807 -0.2721 -0.1200 181  LYS Y CA  
27199 C C   . LYS D 181  ? 3.2040 3.1151 2.6803 -0.7769 -0.2778 -0.0760 181  LYS Y C   
27200 O O   . LYS D 181  ? 3.1861 3.1345 2.6724 -0.7614 -0.2935 -0.0326 181  LYS Y O   
27201 C CB  . LYS D 181  ? 3.2357 3.1537 2.7575 -0.7897 -0.2914 -0.1038 181  LYS Y CB  
27202 C CG  . LYS D 181  ? 3.3101 3.2265 2.8003 -0.8324 -0.3024 -0.0860 181  LYS Y CG  
27203 C CD  . LYS D 181  ? 3.3298 3.2640 2.8366 -0.8418 -0.3233 -0.0719 181  LYS Y CD  
27204 C CE  . LYS D 181  ? 3.3770 3.2988 2.8465 -0.8883 -0.3364 -0.0587 181  LYS Y CE  
27205 N NZ  . LYS D 181  ? 3.3735 3.3076 2.8558 -0.9001 -0.3590 -0.0454 181  LYS Y NZ  
27206 N N   . GLY D 182  ? 3.2232 3.1059 2.6659 -0.7914 -0.2651 -0.0869 182  GLY Y N   
27207 C CA  . GLY D 182  ? 3.2248 3.1149 2.6398 -0.7846 -0.2712 -0.0489 182  GLY Y CA  
27208 C C   . GLY D 182  ? 3.1894 3.0744 2.6083 -0.7426 -0.2629 -0.0477 182  GLY Y C   
27209 O O   . GLY D 182  ? 3.1712 3.0272 2.5933 -0.7361 -0.2478 -0.0851 182  GLY Y O   
27210 N N   . THR D 183  ? 3.1740 3.0861 2.5929 -0.7139 -0.2732 -0.0040 183  THR Y N   
27211 C CA  . THR D 183  ? 3.1729 3.0751 2.5885 -0.6710 -0.2661 -0.0002 183  THR Y CA  
27212 C C   . THR D 183  ? 3.1931 3.0990 2.6405 -0.6358 -0.2618 -0.0165 183  THR Y C   
27213 O O   . THR D 183  ? 3.2250 3.1184 2.6666 -0.5979 -0.2570 -0.0136 183  THR Y O   
27214 C CB  . THR D 183  ? 3.1042 3.0340 2.5126 -0.6454 -0.2763 0.0515  183  THR Y CB  
27215 O OG1 . THR D 183  ? 3.0676 3.0466 2.5014 -0.6531 -0.2914 0.0875  183  THR Y OG1 
27216 C CG2 . THR D 183  ? 3.1322 3.0342 2.4971 -0.6662 -0.2785 0.0591  183  THR Y CG2 
27217 N N   . SER D 184  ? 3.2083 3.1258 2.6845 -0.6486 -0.2652 -0.0334 184  SER Y N   
27218 C CA  . SER D 184  ? 3.2110 3.1282 2.7155 -0.6187 -0.2652 -0.0485 184  SER Y CA  
27219 C C   . SER D 184  ? 3.2387 3.1149 2.7506 -0.6233 -0.2557 -0.1001 184  SER Y C   
27220 O O   . SER D 184  ? 3.2366 3.1035 2.7616 -0.6549 -0.2525 -0.1312 184  SER Y O   
27221 C CB  . SER D 184  ? 3.1838 3.1333 2.7169 -0.6270 -0.2774 -0.0372 184  SER Y CB  
27222 O OG  . SER D 184  ? 3.1780 3.1714 2.7149 -0.6146 -0.2863 0.0135  184  SER Y OG  
27223 N N   . LYS D 185  ? 3.2732 3.1243 2.7780 -0.5912 -0.2515 -0.1086 185  LYS Y N   
27224 C CA  . LYS D 185  ? 3.2889 3.1025 2.8046 -0.5951 -0.2451 -0.1540 185  LYS Y CA  
27225 C C   . LYS D 185  ? 3.2627 3.0459 2.7662 -0.5562 -0.2466 -0.1567 185  LYS Y C   
27226 O O   . LYS D 185  ? 3.2634 3.0192 2.7849 -0.5538 -0.2477 -0.1904 185  LYS Y O   
27227 C CB  . LYS D 185  ? 3.3593 3.1530 2.8590 -0.6330 -0.2317 -0.1768 185  LYS Y CB  
27228 C CG  . LYS D 185  ? 3.4233 3.1929 2.8818 -0.6246 -0.2263 -0.1647 185  LYS Y CG  
27229 C CD  . LYS D 185  ? 3.4678 3.2156 2.9064 -0.6665 -0.2122 -0.1868 185  LYS Y CD  
27230 C CE  . LYS D 185  ? 3.4897 3.2551 2.9043 -0.6970 -0.2133 -0.1636 185  LYS Y CE  
27231 N NZ  . LYS D 185  ? 3.5231 3.2621 2.9140 -0.7417 -0.1974 -0.1890 185  LYS Y NZ  
27232 N N   . TYR D 186  ? 3.2332 3.0186 2.7059 -0.5260 -0.2473 -0.1215 186  TYR Y N   
27233 C CA  . TYR D 186  ? 3.2125 2.9621 2.6631 -0.4865 -0.2489 -0.1215 186  TYR Y CA  
27234 C C   . TYR D 186  ? 3.1709 2.9333 2.6223 -0.4473 -0.2547 -0.0967 186  TYR Y C   
27235 O O   . TYR D 186  ? 3.1348 2.9391 2.5906 -0.4409 -0.2539 -0.0617 186  TYR Y O   
27236 C CB  . TYR D 186  ? 3.2445 2.9736 2.6510 -0.4759 -0.2431 -0.1037 186  TYR Y CB  
27237 C CG  . TYR D 186  ? 3.2537 2.9695 2.6500 -0.5161 -0.2364 -0.1218 186  TYR Y CG  
27238 C CD1 . TYR D 186  ? 3.2621 2.9926 2.6347 -0.5308 -0.2340 -0.0959 186  TYR Y CD1 
27239 C CD2 . TYR D 186  ? 3.2544 2.9427 2.6653 -0.5405 -0.2325 -0.1640 186  TYR Y CD2 
27240 C CE1 . TYR D 186  ? 3.2848 2.9969 2.6396 -0.5698 -0.2275 -0.1119 186  TYR Y CE1 
27241 C CE2 . TYR D 186  ? 3.2734 2.9490 2.6724 -0.5788 -0.2224 -0.1805 186  TYR Y CE2 
27242 C CZ  . TYR D 186  ? 3.2867 2.9714 2.6530 -0.5940 -0.2196 -0.1546 186  TYR Y CZ  
27243 O OH  . TYR D 186  ? 3.3062 2.9724 2.6522 -0.6345 -0.2092 -0.1703 186  TYR Y OH  
27244 N N   . GLY D 187  ? 3.1512 2.8757 2.5967 -0.4222 -0.2607 -0.1134 187  GLY Y N   
27245 C CA  . GLY D 187  ? 3.1258 2.8519 2.5619 -0.3850 -0.2643 -0.0920 187  GLY Y CA  
27246 C C   . GLY D 187  ? 3.0912 2.7670 2.5207 -0.3668 -0.2758 -0.1176 187  GLY Y C   
27247 O O   . GLY D 187  ? 3.0954 2.7380 2.5349 -0.3827 -0.2826 -0.1524 187  GLY Y O   
27248 N N   . LYS D 188  ? 3.0951 2.7654 2.5086 -0.3351 -0.2785 -0.0993 188  LYS Y N   
27249 C CA  . LYS D 188  ? 3.1148 2.7286 2.5094 -0.3142 -0.2920 -0.1184 188  LYS Y CA  
27250 C C   . LYS D 188  ? 3.1076 2.7306 2.5083 -0.3019 -0.2995 -0.1073 188  LYS Y C   
27251 O O   . LYS D 188  ? 3.1213 2.7683 2.5028 -0.2790 -0.2876 -0.0721 188  LYS Y O   
27252 C CB  . LYS D 188  ? 3.1868 2.7497 2.5200 -0.2766 -0.2861 -0.1071 188  LYS Y CB  
27253 C CG  . LYS D 188  ? 3.2137 2.7473 2.5318 -0.2877 -0.2848 -0.1233 188  LYS Y CG  
27254 C CD  . LYS D 188  ? 3.2319 2.7111 2.5555 -0.2992 -0.3038 -0.1623 188  LYS Y CD  
27255 C CE  . LYS D 188  ? 3.2538 2.6950 2.5512 -0.3054 -0.3026 -0.1740 188  LYS Y CE  
27256 N NZ  . LYS D 188  ? 3.2163 2.7007 2.5407 -0.3399 -0.2897 -0.1753 188  LYS Y NZ  
27257 N N   . ILE D 189  ? 3.0693 2.6729 2.4978 -0.3171 -0.3192 -0.1366 189  ILE Y N   
27258 C CA  . ILE D 189  ? 3.0405 2.6437 2.4716 -0.3089 -0.3307 -0.1292 189  ILE Y CA  
27259 C C   . ILE D 189  ? 3.0994 2.6353 2.4786 -0.2750 -0.3407 -0.1301 189  ILE Y C   
27260 O O   . ILE D 189  ? 3.1116 2.5950 2.4897 -0.2772 -0.3603 -0.1604 189  ILE Y O   
27261 C CB  . ILE D 189  ? 2.9942 2.6025 2.4791 -0.3402 -0.3511 -0.1609 189  ILE Y CB  
27262 C CG1 . ILE D 189  ? 2.9475 2.5981 2.4778 -0.3769 -0.3429 -0.1755 189  ILE Y CG1 
27263 C CG2 . ILE D 189  ? 2.9820 2.6073 2.4732 -0.3393 -0.3602 -0.1452 189  ILE Y CG2 
27264 C CD1 . ILE D 189  ? 2.9180 2.5666 2.5018 -0.4047 -0.3596 -0.2125 189  ILE Y CD1 
27265 N N   . ILE D 190  ? 3.1268 2.6627 2.4629 -0.2444 -0.3274 -0.0968 190  ILE Y N   
27266 C CA  . ILE D 190  ? 3.2076 2.6721 2.4823 -0.2116 -0.3348 -0.0963 190  ILE Y CA  
27267 C C   . ILE D 190  ? 3.2275 2.6767 2.5009 -0.2130 -0.3523 -0.0966 190  ILE Y C   
27268 O O   . ILE D 190  ? 3.2291 2.7021 2.4846 -0.1997 -0.3384 -0.0660 190  ILE Y O   
27269 C CB  . ILE D 190  ? 2.2954 1.7489 1.5085 -0.1708 -0.3071 -0.0637 190  ILE Y CB  
27270 C CG1 . ILE D 190  ? 2.3332 1.7468 1.4889 -0.1390 -0.3032 -0.0457 190  ILE Y CG1 
27271 C CG2 . ILE D 190  ? 2.2548 1.7891 1.4982 -0.1753 -0.2814 -0.0336 190  ILE Y CG2 
27272 C CD1 . ILE D 190  ? 2.3608 1.7740 1.4629 -0.0972 -0.2701 -0.0111 190  ILE Y CD1 
27273 N N   . ILE D 191  ? 3.2593 2.6696 2.5545 -0.2302 -0.3835 -0.1306 191  ILE Y N   
27274 C CA  . ILE D 191  ? 3.3193 2.7019 2.6082 -0.2315 -0.4061 -0.1337 191  ILE Y CA  
27275 C C   . ILE D 191  ? 3.4362 2.7469 2.6411 -0.1960 -0.4062 -0.1206 191  ILE Y C   
27276 O O   . ILE D 191  ? 3.5096 2.7584 2.6748 -0.1806 -0.4135 -0.1339 191  ILE Y O   
27277 C CB  . ILE D 191  ? 2.6372 1.9874 1.9704 -0.2548 -0.4435 -0.1745 191  ILE Y CB  
27278 C CG1 . ILE D 191  ? 2.5325 1.9304 1.9376 -0.2851 -0.4407 -0.1981 191  ILE Y CG1 
27279 C CG2 . ILE D 191  ? 2.6647 2.0098 2.0103 -0.2646 -0.4661 -0.1748 191  ILE Y CG2 
27280 C CD1 . ILE D 191  ? 2.4748 1.8526 1.9359 -0.3071 -0.4731 -0.2370 191  ILE Y CD1 
27281 N N   . ASN D 192  ? 3.4896 2.8043 2.6630 -0.1840 -0.3977 -0.0942 192  ASN Y N   
27282 C CA  . ASN D 192  ? 3.6061 2.8419 2.6938 -0.1533 -0.3999 -0.0851 192  ASN Y CA  
27283 C C   . ASN D 192  ? 3.6807 2.8512 2.7608 -0.1655 -0.4430 -0.1092 192  ASN Y C   
27284 O O   . ASN D 192  ? 3.6335 2.8347 2.7718 -0.1935 -0.4635 -0.1206 192  ASN Y O   
27285 C CB  . ASN D 192  ? 3.6226 2.8899 2.6729 -0.1317 -0.3650 -0.0433 192  ASN Y CB  
27286 C CG  . ASN D 192  ? 3.6088 2.9278 2.6599 -0.1125 -0.3252 -0.0188 192  ASN Y CG  
27287 O OD1 . ASN D 192  ? 3.6402 2.9213 2.6584 -0.0930 -0.3189 -0.0267 192  ASN Y OD1 
27288 N ND2 . ASN D 192  ? 3.5670 2.9709 2.6560 -0.1185 -0.3008 0.0119  192  ASN Y ND2 
27289 N N   . LEU D 193  ? 3.8094 2.8854 2.8160 -0.1445 -0.4589 -0.1170 193  LEU Y N   
27290 C CA  . LEU D 193  ? 3.8803 2.8842 2.8753 -0.1550 -0.5052 -0.1399 193  LEU Y CA  
27291 C C   . LEU D 193  ? 4.0219 2.9338 2.9076 -0.1271 -0.5073 -0.1254 193  LEU Y C   
27292 O O   . LEU D 193  ? 4.0684 2.9266 2.9278 -0.1337 -0.5382 -0.1303 193  LEU Y O   
27293 C CB  . LEU D 193  ? 3.8583 2.8294 2.8909 -0.1684 -0.5374 -0.1763 193  LEU Y CB  
27294 C CG  . LEU D 193  ? 3.7431 2.7947 2.8838 -0.1995 -0.5388 -0.1963 193  LEU Y CG  
27295 C CD1 . LEU D 193  ? 3.7305 2.7516 2.9029 -0.2095 -0.5622 -0.2285 193  LEU Y CD1 
27296 C CD2 . LEU D 193  ? 3.6952 2.7765 2.8928 -0.2239 -0.5609 -0.2042 193  LEU Y CD2 
27297 N N   . LYS D 194  ? 4.0924 2.9824 2.9110 -0.0954 -0.4740 -0.1078 194  LYS Y N   
27298 C CA  . LYS D 194  ? 4.2273 3.0345 2.9332 -0.0647 -0.4638 -0.0901 194  LYS Y CA  
27299 C C   . LYS D 194  ? 4.2517 3.0692 2.9081 -0.0292 -0.4145 -0.0668 194  LYS Y C   
27300 O O   . LYS D 194  ? 4.1707 3.0501 2.8783 -0.0300 -0.3958 -0.0668 194  LYS Y O   
27301 C CB  . LYS D 194  ? 4.3558 3.0419 2.9998 -0.0632 -0.5105 -0.1146 194  LYS Y CB  
27302 C CG  . LYS D 194  ? 4.4057 3.0658 3.0719 -0.0677 -0.5314 -0.1410 194  LYS Y CG  
27303 C CD  . LYS D 194  ? 4.5396 3.0850 3.1569 -0.0722 -0.5852 -0.1638 194  LYS Y CD  
27304 C CE  . LYS D 194  ? 4.5818 3.1030 3.2248 -0.0795 -0.6074 -0.1884 194  LYS Y CE  
27305 N NZ  . LYS D 194  ? 4.6443 3.1454 3.2229 -0.0501 -0.5717 -0.1758 194  LYS Y NZ  
27306 N N   . ASP D 195  ? 4.3574 3.1110 2.9121 0.0023  -0.3935 -0.0472 195  ASP Y N   
27307 C CA  . ASP D 195  ? 4.3895 3.1555 2.8952 0.0411  -0.3411 -0.0210 195  ASP Y CA  
27308 C C   . ASP D 195  ? 4.4584 3.2270 2.9772 0.0517  -0.3357 -0.0323 195  ASP Y C   
27309 O O   . ASP D 195  ? 4.4771 3.2926 2.9963 0.0762  -0.2935 -0.0111 195  ASP Y O   
27310 C CB  . ASP D 195  ? 4.3928 3.0527 2.7684 0.0749  -0.3282 -0.0096 195  ASP Y CB  
27311 C CG  . ASP D 195  ? 4.2848 2.9731 2.6413 0.0778  -0.3015 0.0191  195  ASP Y CG  
27312 O OD1 . ASP D 195  ? 4.1841 2.9732 2.5903 0.0843  -0.2587 0.0471  195  ASP Y OD1 
27313 O OD2 . ASP D 195  ? 4.3115 2.9198 2.6023 0.0725  -0.3246 0.0148  195  ASP Y OD2 
27314 N N   . GLU D 196  ? 4.5147 3.2354 3.0483 0.0320  -0.3792 -0.0648 196  GLU Y N   
27315 C CA  . GLU D 196  ? 4.6011 3.2978 3.1240 0.0426  -0.3784 -0.0764 196  GLU Y CA  
27316 C C   . GLU D 196  ? 4.4664 3.1978 3.0804 0.0048  -0.4118 -0.1055 196  GLU Y C   
27317 O O   . GLU D 196  ? 4.4899 3.1850 3.0911 0.0069  -0.4216 -0.1199 196  GLU Y O   
27318 C CB  . GLU D 196  ? 4.8697 3.4298 3.2708 0.0699  -0.3925 -0.0841 196  GLU Y CB  
27319 C CG  . GLU D 196  ? 5.0511 3.5234 3.4351 0.0461  -0.4521 -0.1130 196  GLU Y CG  
27320 C CD  . GLU D 196  ? 5.2016 3.6434 3.5579 0.0391  -0.4680 -0.1082 196  GLU Y CD  
27321 O OE1 . GLU D 196  ? 5.2297 3.7231 3.5833 0.0498  -0.4314 -0.0825 196  GLU Y OE1 
27322 O OE2 . GLU D 196  ? 5.2829 3.6478 3.6206 0.0216  -0.5190 -0.1291 196  GLU Y OE2 
27323 N N   . ASN D 197  ? 4.3223 3.1224 3.0266 -0.0297 -0.4277 -0.1140 197  ASN Y N   
27324 C CA  . ASN D 197  ? 4.1741 3.0051 2.9653 -0.0650 -0.4565 -0.1433 197  ASN Y CA  
27325 C C   . ASN D 197  ? 3.9641 2.9140 2.8558 -0.0897 -0.4376 -0.1385 197  ASN Y C   
27326 O O   . ASN D 197  ? 3.9218 2.9283 2.8298 -0.0894 -0.4173 -0.1164 197  ASN Y O   
27327 C CB  . ASN D 197  ? 4.1986 2.9720 3.0023 -0.0869 -0.5086 -0.1699 197  ASN Y CB  
27328 C CG  . ASN D 197  ? 4.1383 2.9261 3.0215 -0.1177 -0.5382 -0.2021 197  ASN Y CG  
27329 O OD1 . ASN D 197  ? 4.0473 2.9230 3.0212 -0.1418 -0.5281 -0.2090 197  ASN Y OD1 
27330 N ND2 . ASN D 197  ? 4.1874 2.8870 3.0358 -0.1181 -0.5750 -0.2213 197  ASN Y ND2 
27331 N N   . LYS D 198  ? 3.8165 2.8006 2.7717 -0.1127 -0.4445 -0.1585 198  LYS Y N   
27332 C CA  . LYS D 198  ? 3.6311 2.7177 2.6769 -0.1399 -0.4297 -0.1580 198  LYS Y CA  
27333 C C   . LYS D 198  ? 3.5629 2.6651 2.6774 -0.1716 -0.4482 -0.1901 198  LYS Y C   
27334 O O   . LYS D 198  ? 3.5993 2.6580 2.6903 -0.1675 -0.4543 -0.2019 198  LYS Y O   
27335 C CB  . LYS D 198  ? 3.5504 2.6960 2.5860 -0.1224 -0.3859 -0.1263 198  LYS Y CB  
27336 C CG  . LYS D 198  ? 3.5111 2.6404 2.5220 -0.1104 -0.3724 -0.1271 198  LYS Y CG  
27337 C CD  . LYS D 198  ? 3.4212 2.6334 2.4582 -0.1066 -0.3358 -0.0998 198  LYS Y CD  
27338 C CE  . LYS D 198  ? 3.4155 2.6027 2.4086 -0.0844 -0.3191 -0.0922 198  LYS Y CE  
27339 N NZ  . LYS D 198  ? 3.3514 2.6174 2.3704 -0.0790 -0.2870 -0.0628 198  LYS Y NZ  
27340 N N   . VAL D 199  ? 3.4663 2.6288 2.6639 -0.2033 -0.4563 -0.2040 199  VAL Y N   
27341 C CA  . VAL D 199  ? 3.3949 2.5850 2.6668 -0.2352 -0.4666 -0.2341 199  VAL Y CA  
27342 C C   . VAL D 199  ? 3.2988 2.5751 2.6190 -0.2538 -0.4360 -0.2260 199  VAL Y C   
27343 O O   . VAL D 199  ? 3.2615 2.5947 2.6221 -0.2682 -0.4292 -0.2190 199  VAL Y O   
27344 C CB  . VAL D 199  ? 3.3776 2.5653 2.7119 -0.2586 -0.5003 -0.2616 199  VAL Y CB  
27345 C CG1 . VAL D 199  ? 3.3403 2.5542 2.7516 -0.2888 -0.5068 -0.2937 199  VAL Y CG1 
27346 C CG2 . VAL D 199  ? 3.4479 2.5475 2.7335 -0.2426 -0.5358 -0.2678 199  VAL Y CG2 
27347 N N   . GLU D 200  ? 3.2591 2.5390 2.5709 -0.2553 -0.4203 -0.2268 200  GLU Y N   
27348 C CA  . GLU D 200  ? 3.1712 2.5221 2.5141 -0.2715 -0.3920 -0.2160 200  GLU Y CA  
27349 C C   . GLU D 200  ? 3.0958 2.4842 2.5149 -0.3116 -0.3958 -0.2462 200  GLU Y C   
27350 O O   . GLU D 200  ? 3.0867 2.4441 2.5353 -0.3246 -0.4172 -0.2766 200  GLU Y O   
27351 C CB  . GLU D 200  ? 3.1822 2.5164 2.4715 -0.2522 -0.3722 -0.1986 200  GLU Y CB  
27352 C CG  . GLU D 200  ? 3.2253 2.5299 2.4399 -0.2095 -0.3599 -0.1666 200  GLU Y CG  
27353 C CD  . GLU D 200  ? 3.2512 2.5562 2.4248 -0.1906 -0.3364 -0.1461 200  GLU Y CD  
27354 O OE1 . GLU D 200  ? 3.2301 2.5581 2.4305 -0.2135 -0.3313 -0.1555 200  GLU Y OE1 
27355 O OE2 . GLU D 200  ? 3.2986 2.5792 2.4118 -0.1526 -0.3223 -0.1205 200  GLU Y OE2 
27356 N N   . ILE D 201  ? 3.0505 2.5041 2.5007 -0.3312 -0.3744 -0.2370 201  ILE Y N   
27357 C CA  . ILE D 201  ? 2.9974 2.4858 2.5104 -0.3691 -0.3708 -0.2639 201  ILE Y CA  
27358 C C   . ILE D 201  ? 3.0257 2.5574 2.5334 -0.3832 -0.3440 -0.2482 201  ILE Y C   
27359 O O   . ILE D 201  ? 3.0068 2.5854 2.5191 -0.3876 -0.3323 -0.2258 201  ILE Y O   
27360 C CB  . ILE D 201  ? 2.9000 2.4236 2.4692 -0.3890 -0.3795 -0.2764 201  ILE Y CB  
27361 C CG1 . ILE D 201  ? 2.8752 2.3591 2.4428 -0.3726 -0.4081 -0.2833 201  ILE Y CG1 
27362 C CG2 . ILE D 201  ? 2.8512 2.3967 2.4833 -0.4244 -0.3760 -0.3108 201  ILE Y CG2 
27363 C CD1 . ILE D 201  ? 2.8167 2.3302 2.4310 -0.3885 -0.4188 -0.2912 201  ILE Y CD1 
27364 N N   . ASP D 202  ? 3.0906 2.6047 2.5881 -0.3925 -0.3367 -0.2590 202  ASP Y N   
27365 C CA  . ASP D 202  ? 3.1357 2.6842 2.6263 -0.4100 -0.3143 -0.2464 202  ASP Y CA  
27366 C C   . ASP D 202  ? 3.1437 2.7436 2.6874 -0.4444 -0.3074 -0.2579 202  ASP Y C   
27367 O O   . ASP D 202  ? 3.1082 2.7087 2.7007 -0.4607 -0.3172 -0.2879 202  ASP Y O   
27368 C CB  . ASP D 202  ? 3.1795 2.6971 2.6567 -0.4226 -0.3099 -0.2627 202  ASP Y CB  
27369 C CG  . ASP D 202  ? 3.2070 2.7500 2.6635 -0.4385 -0.2890 -0.2460 202  ASP Y CG  
27370 O OD1 . ASP D 202  ? 3.2252 2.7499 2.6765 -0.4586 -0.2832 -0.2613 202  ASP Y OD1 
27371 O OD2 . ASP D 202  ? 3.2067 2.7869 2.6523 -0.4325 -0.2799 -0.2166 202  ASP Y OD2 
27372 N N   . LEU D 203  ? 3.1957 2.8360 2.7289 -0.4542 -0.2922 -0.2333 203  LEU Y N   
27373 C CA  . LEU D 203  ? 3.2285 2.9112 2.7996 -0.4878 -0.2858 -0.2411 203  LEU Y CA  
27374 C C   . LEU D 203  ? 3.3342 3.0205 2.9083 -0.5216 -0.2696 -0.2574 203  LEU Y C   
27375 O O   . LEU D 203  ? 3.3187 3.0293 2.9203 -0.5537 -0.2617 -0.2717 203  LEU Y O   
27376 C CB  . LEU D 203  ? 3.1705 2.8938 2.7283 -0.4815 -0.2829 -0.2022 203  LEU Y CB  
27377 C CG  . LEU D 203  ? 3.1293 2.8462 2.6773 -0.4474 -0.2952 -0.1840 203  LEU Y CG  
27378 C CD1 . LEU D 203  ? 3.1106 2.8711 2.6467 -0.4389 -0.2900 -0.1409 203  LEU Y CD1 
27379 C CD2 . LEU D 203  ? 3.1003 2.8080 2.6880 -0.4557 -0.3116 -0.2122 203  LEU Y CD2 
27380 N N   . GLY D 204  ? 3.4630 3.1198 3.0034 -0.5149 -0.2645 -0.2555 204  GLY Y N   
27381 C CA  . GLY D 204  ? 3.5708 3.2243 3.1041 -0.5469 -0.2488 -0.2683 204  GLY Y CA  
27382 C C   . GLY D 204  ? 3.6611 3.3063 3.2404 -0.5759 -0.2436 -0.3123 204  GLY Y C   
27383 O O   . GLY D 204  ? 3.6789 3.3256 3.2572 -0.6083 -0.2265 -0.3262 204  GLY Y O   
27384 N N   . ASP D 205  ? 3.7302 3.3662 3.3505 -0.5645 -0.2581 -0.3338 205  ASP Y N   
27385 C CA  . ASP D 205  ? 3.7996 3.4307 3.4753 -0.5871 -0.2551 -0.3754 205  ASP Y CA  
27386 C C   . ASP D 205  ? 3.7913 3.4183 3.5140 -0.5703 -0.2771 -0.3916 205  ASP Y C   
27387 O O   . ASP D 205  ? 3.8055 3.4141 3.5056 -0.5384 -0.2970 -0.3734 205  ASP Y O   
27388 C CB  . ASP D 205  ? 3.8993 3.4958 3.5618 -0.5916 -0.2528 -0.3867 205  ASP Y CB  
27389 C CG  . ASP D 205  ? 3.9515 3.5498 3.6782 -0.6180 -0.2462 -0.4280 205  ASP Y CG  
27390 O OD1 . ASP D 205  ? 3.9439 3.5726 3.7187 -0.6381 -0.2347 -0.4488 205  ASP Y OD1 
27391 O OD2 . ASP D 205  ? 3.9933 3.5622 3.7231 -0.6187 -0.2524 -0.4392 205  ASP Y OD2 
27392 N N   . LYS D 206  ? 3.7571 3.3986 3.5433 -0.5916 -0.2731 -0.4259 206  LYS Y N   
27393 C CA  . LYS D 206  ? 3.7213 3.3564 3.5587 -0.5780 -0.2966 -0.4444 206  LYS Y CA  
27394 C C   . LYS D 206  ? 3.6982 3.3097 3.5793 -0.5804 -0.3063 -0.4730 206  LYS Y C   
27395 O O   . LYS D 206  ? 3.6932 3.3148 3.6444 -0.5900 -0.3108 -0.5037 206  LYS Y O   
27396 C CB  . LYS D 206  ? 3.6975 3.3644 3.5814 -0.5961 -0.2893 -0.4625 206  LYS Y CB  
27397 C CG  . LYS D 206  ? 3.6886 3.3804 3.5307 -0.6040 -0.2772 -0.4356 206  LYS Y CG  
27398 C CD  . LYS D 206  ? 3.6688 3.3843 3.5486 -0.6263 -0.2684 -0.4555 206  LYS Y CD  
27399 C CE  . LYS D 206  ? 3.6651 3.4015 3.4980 -0.6397 -0.2576 -0.4270 206  LYS Y CE  
27400 N NZ  . LYS D 206  ? 3.6550 3.4067 3.5122 -0.6587 -0.2548 -0.4413 206  LYS Y NZ  
27401 N N   . LEU D 207  ? 3.6740 3.2533 3.5148 -0.5717 -0.3106 -0.4621 207  LEU Y N   
27402 C CA  . LEU D 207  ? 3.6358 3.1909 3.5124 -0.5785 -0.3203 -0.4855 207  LEU Y CA  
27403 C C   . LEU D 207  ? 3.5935 3.1124 3.4865 -0.5527 -0.3595 -0.4893 207  LEU Y C   
27404 O O   . LEU D 207  ? 3.6146 3.1039 3.5245 -0.5542 -0.3753 -0.5013 207  LEU Y O   
27405 C CB  . LEU D 207  ? 3.6620 3.1918 3.4825 -0.5843 -0.3097 -0.4723 207  LEU Y CB  
27406 C CG  . LEU D 207  ? 3.6801 3.1897 3.5321 -0.6021 -0.3126 -0.4941 207  LEU Y CG  
27407 C CD1 . LEU D 207  ? 3.6570 3.2081 3.5848 -0.6384 -0.2862 -0.5266 207  LEU Y CD1 
27408 C CD2 . LEU D 207  ? 3.7156 3.1921 3.4940 -0.6036 -0.3060 -0.4744 207  LEU Y CD2 
27409 N N   . GLN D 208  ? 3.5286 3.0469 3.4143 -0.5313 -0.3768 -0.4781 208  GLN Y N   
27410 C CA  . GLN D 208  ? 3.4914 2.9674 3.3768 -0.5060 -0.4157 -0.4774 208  GLN Y CA  
27411 C C   . GLN D 208  ? 3.4361 2.9216 3.4105 -0.5133 -0.4361 -0.5087 208  GLN Y C   
27412 O O   . GLN D 208  ? 3.4189 2.8948 3.3992 -0.4974 -0.4595 -0.5059 208  GLN Y O   
27413 C CB  . GLN D 208  ? 3.4747 2.9365 3.2941 -0.4771 -0.4247 -0.4452 208  GLN Y CB  
27414 C CG  . GLN D 208  ? 3.4872 2.8912 3.2796 -0.4496 -0.4627 -0.4393 208  GLN Y CG  
27415 C CD  . GLN D 208  ? 3.5175 2.8662 3.2518 -0.4364 -0.4721 -0.4297 208  GLN Y CD  
27416 O OE1 . GLN D 208  ? 3.5294 2.8415 3.2879 -0.4398 -0.4975 -0.4474 208  GLN Y OE1 
27417 N NE2 . GLN D 208  ? 3.5347 2.8751 3.1925 -0.4212 -0.4532 -0.4010 208  GLN Y NE2 
27418 N N   . PHE D 209  ? 3.4126 2.9167 3.4573 -0.5372 -0.4270 -0.5378 209  PHE Y N   
27419 C CA  . PHE D 209  ? 3.3782 2.8960 3.5187 -0.5436 -0.4441 -0.5691 209  PHE Y CA  
27420 C C   . PHE D 209  ? 3.4618 2.9300 3.6110 -0.5225 -0.4941 -0.5695 209  PHE Y C   
27421 O O   . PHE D 209  ? 3.4581 2.9268 3.6553 -0.5150 -0.5184 -0.5817 209  PHE Y O   
27422 C CB  . PHE D 209  ? 3.3062 2.8554 3.5205 -0.5733 -0.4201 -0.5983 209  PHE Y CB  
27423 C CG  . PHE D 209  ? 3.2755 2.8001 3.4585 -0.5821 -0.4171 -0.5915 209  PHE Y CG  
27424 C CD1 . PHE D 209  ? 3.2747 2.7668 3.4912 -0.5797 -0.4503 -0.6003 209  PHE Y CD1 
27425 C CD2 . PHE D 209  ? 3.2510 2.7811 3.3692 -0.5940 -0.3842 -0.5754 209  PHE Y CD2 
27426 C CE1 . PHE D 209  ? 3.2878 2.7527 3.4717 -0.5896 -0.4499 -0.5933 209  PHE Y CE1 
27427 C CE2 . PHE D 209  ? 3.2636 2.7660 3.3489 -0.6026 -0.3834 -0.5689 209  PHE Y CE2 
27428 C CZ  . PHE D 209  ? 3.2861 2.7555 3.4032 -0.6007 -0.4158 -0.5780 209  PHE Y CZ  
27429 N N   . GLU D 210  ? 3.5454 2.9652 3.6425 -0.5135 -0.5114 -0.5557 210  GLU Y N   
27430 C CA  . GLU D 210  ? 3.6330 2.9977 3.7385 -0.4994 -0.5608 -0.5588 210  GLU Y CA  
27431 C C   . GLU D 210  ? 3.6431 2.9587 3.6805 -0.4693 -0.5920 -0.5370 210  GLU Y C   
27432 O O   . GLU D 210  ? 3.6784 2.9559 3.7390 -0.4601 -0.6352 -0.5444 210  GLU Y O   
27433 C CB  . GLU D 210  ? 3.7370 3.0627 3.8164 -0.5057 -0.5698 -0.5556 210  GLU Y CB  
27434 C CG  . GLU D 210  ? 3.8593 3.1079 3.8318 -0.4793 -0.5969 -0.5286 210  GLU Y CG  
27435 C CD  . GLU D 210  ? 3.9204 3.1662 3.7943 -0.4667 -0.5645 -0.5002 210  GLU Y CD  
27436 O OE1 . GLU D 210  ? 3.9076 3.2017 3.7907 -0.4843 -0.5246 -0.5011 210  GLU Y OE1 
27437 O OE2 . GLU D 210  ? 3.9831 3.1766 3.7697 -0.4388 -0.5789 -0.4766 210  GLU Y OE2 
27438 N N   . ARG D 211  ? 3.5983 2.9135 3.5523 -0.4548 -0.5710 -0.5095 211  ARG Y N   
27439 C CA  . ARG D 211  ? 3.5606 2.8355 3.4505 -0.4280 -0.5936 -0.4879 211  ARG Y CA  
27440 C C   . ARG D 211  ? 3.5067 2.8202 3.4388 -0.4303 -0.5928 -0.4934 211  ARG Y C   
27441 O O   . ARG D 211  ? 3.5103 2.7939 3.4066 -0.4128 -0.6155 -0.4803 211  ARG Y O   
27442 C CB  . ARG D 211  ? 3.5126 2.7682 3.2959 -0.4086 -0.5722 -0.4537 211  ARG Y CB  
27443 C CG  . ARG D 211  ? 3.4786 2.6857 3.1881 -0.3797 -0.5927 -0.4303 211  ARG Y CG  
27444 C CD  . ARG D 211  ? 3.4564 2.6299 3.0625 -0.3566 -0.5753 -0.3998 211  ARG Y CD  
27445 N NE  . ARG D 211  ? 3.3726 2.6034 2.9701 -0.3631 -0.5314 -0.3859 211  ARG Y NE  
27446 C CZ  . ARG D 211  ? 3.3673 2.5830 2.8911 -0.3465 -0.5104 -0.3618 211  ARG Y CZ  
27447 N NH1 . ARG D 211  ? 3.4228 2.5656 2.8708 -0.3214 -0.5264 -0.3500 211  ARG Y NH1 
27448 N NH2 . ARG D 211  ? 3.3224 2.5917 2.8458 -0.3547 -0.4747 -0.3495 211  ARG Y NH2 
27449 N N   . MET D 212  ? 3.4692 2.8444 3.4728 -0.4529 -0.5664 -0.5131 212  MET Y N   
27450 C CA  . MET D 212  ? 3.4143 2.8244 3.4634 -0.4581 -0.5656 -0.5226 212  MET Y CA  
27451 C C   . MET D 212  ? 3.4072 2.7854 3.5060 -0.4504 -0.6121 -0.5397 212  MET Y C   
27452 O O   . MET D 212  ? 3.4075 2.8028 3.5460 -0.4522 -0.6207 -0.5496 212  MET Y O   
27453 C CB  . MET D 212  ? 3.3763 2.8483 3.4925 -0.4846 -0.5291 -0.5454 212  MET Y CB  
27454 C CG  . MET D 212  ? 3.3575 2.8630 3.4191 -0.4930 -0.4872 -0.5246 212  MET Y CG  
27455 S SD  . MET D 212  ? 3.0398 2.6066 3.1598 -0.5264 -0.4426 -0.5493 212  MET Y SD  
27456 C CE  . MET D 212  ? 1.7941 1.3825 1.8274 -0.5290 -0.4113 -0.5128 212  MET Y CE  
27457 N N   . GLY D 213  ? 3.3937 2.7212 3.4876 -0.4425 -0.6446 -0.5425 213  GLY Y N   
27458 C CA  . GLY D 213  ? 3.3872 2.6711 3.5147 -0.4336 -0.6963 -0.5538 213  GLY Y CA  
27459 C C   . GLY D 213  ? 3.4274 2.6470 3.4582 -0.4102 -0.7241 -0.5262 213  GLY Y C   
27460 O O   . GLY D 213  ? 3.4201 2.6126 3.4615 -0.4029 -0.7594 -0.5290 213  GLY Y O   
27461 N N   . ASP D 214  ? 3.4489 2.6418 3.3842 -0.3983 -0.7074 -0.4998 214  ASP Y N   
27462 C CA  . ASP D 214  ? 3.4812 2.6149 3.3139 -0.3746 -0.7230 -0.4712 214  ASP Y CA  
27463 C C   . ASP D 214  ? 3.4730 2.6212 3.3080 -0.3715 -0.7292 -0.4647 214  ASP Y C   
27464 O O   . ASP D 214  ? 3.4663 2.6781 3.3570 -0.3856 -0.7063 -0.4738 214  ASP Y O   
27465 C CB  . ASP D 214  ? 3.4150 2.5498 3.1591 -0.3630 -0.6844 -0.4433 214  ASP Y CB  
27466 C CG  . ASP D 214  ? 3.3939 2.4495 3.0281 -0.3364 -0.7013 -0.4181 214  ASP Y CG  
27467 O OD1 . ASP D 214  ? 3.3846 2.4041 2.9872 -0.3254 -0.7255 -0.4094 214  ASP Y OD1 
27468 O OD2 . ASP D 214  ? 3.3989 2.4248 2.9728 -0.3263 -0.6888 -0.4066 214  ASP Y OD2 
27469 N N   . VAL D 215  ? 3.4799 2.5646 3.2511 -0.3548 -0.7609 -0.4493 215  VAL Y N   
27470 C CA  . VAL D 215  ? 3.4174 2.5071 3.1787 -0.3525 -0.7694 -0.4395 215  VAL Y CA  
27471 C C   . VAL D 215  ? 3.4284 2.4757 3.0738 -0.3320 -0.7623 -0.4035 215  VAL Y C   
27472 O O   . VAL D 215  ? 3.4603 2.4526 3.0320 -0.3161 -0.7649 -0.3907 215  VAL Y O   
27473 C CB  . VAL D 215  ? 3.9034 2.9588 3.7222 -0.3570 -0.8228 -0.4618 215  VAL Y CB  
27474 C CG1 . VAL D 215  ? 3.8441 2.9572 3.7874 -0.3760 -0.8211 -0.4964 215  VAL Y CG1 
27475 C CG2 . VAL D 215  ? 3.9754 2.9423 3.7545 -0.3461 -0.8694 -0.4625 215  VAL Y CG2 
27476 N N   . LEU D 216  ? 3.3840 2.4557 3.0126 -0.3327 -0.7524 -0.3869 216  LEU Y N   
27477 C CA  . LEU D 216  ? 3.3693 2.4188 2.8972 -0.3150 -0.7347 -0.3504 216  LEU Y CA  
27478 C C   . LEU D 216  ? 3.3532 2.3689 2.8491 -0.3135 -0.7611 -0.3386 216  LEU Y C   
27479 O O   . LEU D 216  ? 3.3098 2.3532 2.8651 -0.3292 -0.7760 -0.3508 216  LEU Y O   
27480 C CB  . LEU D 216  ? 3.2951 2.4206 2.8170 -0.3170 -0.6810 -0.3292 216  LEU Y CB  
27481 C CG  . LEU D 216  ? 3.2305 2.3810 2.7519 -0.3143 -0.6489 -0.3299 216  LEU Y CG  
27482 C CD1 . LEU D 216  ? 3.2822 2.3544 2.7391 -0.2946 -0.6644 -0.3286 216  LEU Y CD1 
27483 C CD2 . LEU D 216  ? 3.1509 2.3516 2.7694 -0.3381 -0.6450 -0.3614 216  LEU Y CD2 
27484 N N   . ASN D 217  ? 3.3812 2.3330 2.7780 -0.2944 -0.7656 -0.3145 217  ASN Y N   
27485 C CA  . ASN D 217  ? 3.3993 2.3138 2.7461 -0.2926 -0.7847 -0.2974 217  ASN Y CA  
27486 C C   . ASN D 217  ? 3.3667 2.3475 2.6983 -0.2955 -0.7432 -0.2678 217  ASN Y C   
27487 O O   . ASN D 217  ? 3.3476 2.3480 2.6276 -0.2809 -0.7024 -0.2421 217  ASN Y O   
27488 C CB  . ASN D 217  ? 3.4998 2.3165 2.7373 -0.2714 -0.8005 -0.2821 217  ASN Y CB  
27489 C CG  . ASN D 217  ? 3.5562 2.3073 2.7957 -0.2670 -0.8355 -0.3056 217  ASN Y CG  
27490 O OD1 . ASN D 217  ? 3.5359 2.3099 2.8675 -0.2816 -0.8575 -0.3350 217  ASN Y OD1 
27491 N ND2 . ASN D 217  ? 3.6323 2.3002 2.7696 -0.2473 -0.8405 -0.2923 217  ASN Y ND2 
27492 N N   . SER D 218  ? 3.3664 2.3797 2.7431 -0.3140 -0.7551 -0.2703 218  SER Y N   
27493 C CA  . SER D 218  ? 3.3624 2.4432 2.7355 -0.3221 -0.7201 -0.2427 218  SER Y CA  
27494 C C   . SER D 218  ? 3.4627 2.5244 2.7395 -0.3046 -0.6948 -0.2026 218  SER Y C   
27495 O O   . SER D 218  ? 3.4206 2.5364 2.6834 -0.2973 -0.6500 -0.1784 218  SER Y O   
27496 C CB  . SER D 218  ? 3.3242 2.4198 2.7442 -0.3444 -0.7466 -0.2511 218  SER Y CB  
27497 O OG  . SER D 218  ? 3.2511 2.3807 2.7654 -0.3596 -0.7574 -0.2860 218  SER Y OG  
27498 N N   . LYS D 219  ? 3.5904 2.5740 2.8009 -0.2975 -0.7230 -0.1953 219  LYS Y N   
27499 C CA  . LYS D 219  ? 3.6960 2.6577 2.8126 -0.2823 -0.6978 -0.1574 219  LYS Y CA  
27500 C C   . LYS D 219  ? 3.6726 2.6195 2.7287 -0.2537 -0.6614 -0.1437 219  LYS Y C   
27501 O O   . LYS D 219  ? 3.7293 2.6794 2.7194 -0.2380 -0.6266 -0.1105 219  LYS Y O   
27502 C CB  . LYS D 219  ? 3.9325 2.8008 2.9835 -0.2826 -0.7389 -0.1556 219  LYS Y CB  
27503 C CG  . LYS D 219  ? 4.0822 2.9578 3.1782 -0.3087 -0.7745 -0.1633 219  LYS Y CG  
27504 C CD  . LYS D 219  ? 4.2372 3.0135 3.2567 -0.3087 -0.8150 -0.1583 219  LYS Y CD  
27505 C CE  . LYS D 219  ? 4.3516 3.0383 3.3571 -0.2991 -0.8602 -0.1870 219  LYS Y CE  
27506 N NZ  . LYS D 219  ? 4.3676 3.0752 3.4816 -0.3139 -0.8977 -0.2249 219  LYS Y NZ  
27507 N N   . ASP D 220  ? 3.5879 2.5172 2.6665 -0.2468 -0.6693 -0.1688 220  ASP Y N   
27508 C CA  . ASP D 220  ? 3.5479 2.4514 2.5655 -0.2194 -0.6404 -0.1590 220  ASP Y CA  
27509 C C   . ASP D 220  ? 3.4484 2.4419 2.4861 -0.2123 -0.5852 -0.1365 220  ASP Y C   
27510 O O   . ASP D 220  ? 3.4957 2.4794 2.4655 -0.1868 -0.5502 -0.1107 220  ASP Y O   
27511 C CB  . ASP D 220  ? 3.5448 2.4003 2.5807 -0.2174 -0.6689 -0.1918 220  ASP Y CB  
27512 C CG  . ASP D 220  ? 3.6321 2.3736 2.6081 -0.2124 -0.7182 -0.2042 220  ASP Y CG  
27513 O OD1 . ASP D 220  ? 3.6998 2.3878 2.5962 -0.2045 -0.7225 -0.1848 220  ASP Y OD1 
27514 O OD2 . ASP D 220  ? 3.6382 2.3422 2.6458 -0.2178 -0.7532 -0.2325 220  ASP Y OD2 
27515 N N   . ILE D 221  ? 3.3062 2.3836 2.4353 -0.2344 -0.5783 -0.1461 221  ILE Y N   
27516 C CA  . ILE D 221  ? 3.1754 2.3371 2.3326 -0.2320 -0.5328 -0.1281 221  ILE Y CA  
27517 C C   . ILE D 221  ? 3.1179 2.3190 2.2354 -0.2205 -0.4955 -0.0848 221  ILE Y C   
27518 O O   . ILE D 221  ? 3.1122 2.3492 2.2497 -0.2382 -0.4983 -0.0702 221  ILE Y O   
27519 C CB  . ILE D 221  ? 2.5894 1.8293 1.8455 -0.2627 -0.5347 -0.1447 221  ILE Y CB  
27520 C CG1 . ILE D 221  ? 2.5439 1.7532 1.8544 -0.2784 -0.5732 -0.1880 221  ILE Y CG1 
27521 C CG2 . ILE D 221  ? 2.5701 1.8772 1.8481 -0.2596 -0.4949 -0.1324 221  ILE Y CG2 
27522 C CD1 . ILE D 221  ? 2.4391 1.7194 1.8409 -0.3064 -0.5695 -0.2071 221  ILE Y CD1 
27523 N N   . ARG D 222  ? 3.0634 2.2591 2.1275 -0.1909 -0.4603 -0.0641 222  ARG Y N   
27524 C CA  . ARG D 222  ? 3.0460 2.2786 2.0732 -0.1747 -0.4206 -0.0217 222  ARG Y CA  
27525 C C   . ARG D 222  ? 2.9278 2.2710 2.0235 -0.1893 -0.3926 0.0002  222  ARG Y C   
27526 O O   . ARG D 222  ? 2.8849 2.2758 1.9871 -0.1971 -0.3780 0.0303  222  ARG Y O   
27527 C CB  . ARG D 222  ? 3.1276 2.3108 2.0731 -0.1343 -0.3921 -0.0085 222  ARG Y CB  
27528 C CG  . ARG D 222  ? 3.1904 2.4183 2.1052 -0.1125 -0.3442 0.0352  222  ARG Y CG  
27529 C CD  . ARG D 222  ? 3.3058 2.4777 2.1406 -0.0700 -0.3168 0.0425  222  ARG Y CD  
27530 N NE  . ARG D 222  ? 3.4225 2.4754 2.1785 -0.0604 -0.3469 0.0197  222  ARG Y NE  
27531 C CZ  . ARG D 222  ? 3.5158 2.4895 2.1841 -0.0257 -0.3341 0.0192  222  ARG Y CZ  
27532 N NH1 . ARG D 222  ? 3.5226 2.5251 2.1733 0.0055  -0.2897 0.0396  222  ARG Y NH1 
27533 N NH2 . ARG D 222  ? 3.5971 2.4588 2.1935 -0.0221 -0.3679 -0.0014 222  ARG Y NH2 
27534 N N   . GLY D 223  ? 2.8963 2.2775 2.0402 -0.1949 -0.3864 -0.0136 223  GLY Y N   
27535 C CA  . GLY D 223  ? 2.7801 2.2580 1.9871 -0.2123 -0.3659 0.0043  223  GLY Y CA  
27536 C C   . GLY D 223  ? 2.6745 2.1773 1.9165 -0.2150 -0.3580 -0.0115 223  GLY Y C   
27537 O O   . GLY D 223  ? 2.6792 2.1526 1.8827 -0.1879 -0.3423 -0.0108 223  GLY Y O   
27538 N N   . ILE D 224  ? 2.5701 2.1229 1.8804 -0.2486 -0.3687 -0.0254 224  ILE Y N   
27539 C CA  . ILE D 224  ? 2.5551 2.1403 1.9009 -0.2576 -0.3586 -0.0371 224  ILE Y CA  
27540 C C   . ILE D 224  ? 2.5921 2.2402 1.9387 -0.2460 -0.3239 0.0006  224  ILE Y C   
27541 O O   . ILE D 224  ? 2.5907 2.2838 1.9377 -0.2429 -0.3089 0.0366  224  ILE Y O   
27542 C CB  . ILE D 224  ? 2.2955 1.9153 1.7100 -0.2985 -0.3766 -0.0624 224  ILE Y CB  
27543 C CG1 . ILE D 224  ? 2.2869 1.8576 1.7161 -0.3118 -0.4120 -0.0969 224  ILE Y CG1 
27544 C CG2 . ILE D 224  ? 2.2723 1.9048 1.7116 -0.3076 -0.3682 -0.0814 224  ILE Y CG2 
27545 C CD1 . ILE D 224  ? 2.2259 1.8221 1.7205 -0.3460 -0.4249 -0.1277 224  ILE Y CD1 
27546 N N   . SER D 225  ? 2.6529 2.3049 2.0035 -0.2417 -0.3131 -0.0074 225  SER Y N   
27547 C CA  . SER D 225  ? 2.7025 2.4098 2.0578 -0.2312 -0.2849 0.0253  225  SER Y CA  
27548 C C   . SER D 225  ? 2.7290 2.4449 2.1081 -0.2477 -0.2852 0.0057  225  SER Y C   
27549 O O   . SER D 225  ? 2.7813 2.4442 2.1339 -0.2357 -0.2885 -0.0173 225  SER Y O   
27550 C CB  . SER D 225  ? 2.7390 2.4180 2.0342 -0.1845 -0.2611 0.0494  225  SER Y CB  
27551 O OG  . SER D 225  ? 2.7154 2.4600 2.0212 -0.1726 -0.2350 0.0942  225  SER Y OG  
27552 N N   . VAL D 226  ? 2.7093 2.4877 2.1347 -0.2778 -0.2832 0.0151  226  VAL Y N   
27553 C CA  . VAL D 226  ? 2.7081 2.4972 2.1529 -0.2981 -0.2818 -0.0006 226  VAL Y CA  
27554 C C   . VAL D 226  ? 2.7454 2.5762 2.1842 -0.2849 -0.2605 0.0352  226  VAL Y C   
27555 O O   . VAL D 226  ? 2.7138 2.5903 2.1574 -0.2722 -0.2483 0.0743  226  VAL Y O   
27556 C CB  . VAL D 226  ? 3.1198 2.9394 2.6144 -0.3447 -0.2961 -0.0195 226  VAL Y CB  
27557 C CG1 . VAL D 226  ? 3.1028 2.9271 2.6096 -0.3672 -0.2917 -0.0366 226  VAL Y CG1 
27558 C CG2 . VAL D 226  ? 3.1194 2.8999 2.6271 -0.3562 -0.3183 -0.0551 226  VAL Y CG2 
27559 N N   . THR D 227  ? 2.8014 2.6168 2.2319 -0.2887 -0.2569 0.0223  227  THR Y N   
27560 C CA  . THR D 227  ? 2.8353 2.6866 2.2633 -0.2809 -0.2418 0.0528  227  THR Y CA  
27561 C C   . THR D 227  ? 2.8854 2.7400 2.3297 -0.3179 -0.2480 0.0325  227  THR Y C   
27562 O O   . THR D 227  ? 2.9163 2.7224 2.3448 -0.3231 -0.2523 -0.0006 227  THR Y O   
27563 C CB  . THR D 227  ? 2.8377 2.6506 2.2161 -0.2340 -0.2269 0.0645  227  THR Y CB  
27564 O OG1 . THR D 227  ? 2.8400 2.6377 2.1940 -0.2002 -0.2192 0.0781  227  THR Y OG1 
27565 C CG2 . THR D 227  ? 2.8174 2.6726 2.1989 -0.2221 -0.2124 0.1007  227  THR Y CG2 
27566 N N   . ILE D 228  ? 2.8977 2.8078 2.3720 -0.3456 -0.2488 0.0531  228  ILE Y N   
27567 C CA  . ILE D 228  ? 2.9301 2.8435 2.4141 -0.3843 -0.2534 0.0371  228  ILE Y CA  
27568 C C   . ILE D 228  ? 2.9713 2.8968 2.4379 -0.3769 -0.2454 0.0631  228  ILE Y C   
27569 O O   . ILE D 228  ? 2.9718 2.9460 2.4511 -0.3686 -0.2424 0.1045  228  ILE Y O   
27570 C CB  . ILE D 228  ? 2.9173 2.8717 2.4376 -0.4268 -0.2638 0.0387  228  ILE Y CB  
27571 C CG1 . ILE D 228  ? 2.9154 2.8394 2.4511 -0.4498 -0.2736 -0.0066 228  ILE Y CG1 
27572 C CG2 . ILE D 228  ? 2.9307 2.9051 2.4517 -0.4589 -0.2646 0.0480  228  ILE Y CG2 
27573 C CD1 . ILE D 228  ? 2.8981 2.8466 2.4597 -0.4954 -0.2823 -0.0148 228  ILE Y CD1 
27574 N N   . ASN D 229  ? 3.0062 2.8871 2.4459 -0.3806 -0.2436 0.0395  229  ASN Y N   
27575 C CA  . ASN D 229  ? 3.0242 2.9067 2.4432 -0.3807 -0.2400 0.0585  229  ASN Y CA  
27576 C C   . ASN D 229  ? 2.9302 2.8149 2.3540 -0.4318 -0.2460 0.0431  229  ASN Y C   
27577 O O   . ASN D 229  ? 2.9118 2.7586 2.3280 -0.4551 -0.2458 0.0039  229  ASN Y O   
27578 C CB  . ASN D 229  ? 3.1379 2.9652 2.5119 -0.3452 -0.2335 0.0516  229  ASN Y CB  
27579 C CG  . ASN D 229  ? 3.1971 2.9651 2.5566 -0.3504 -0.2369 0.0056  229  ASN Y CG  
27580 O OD1 . ASN D 229  ? 3.1888 2.9565 2.5728 -0.3624 -0.2425 -0.0171 229  ASN Y OD1 
27581 N ND2 . ASN D 229  ? 3.2492 2.9656 2.5695 -0.3408 -0.2358 -0.0068 229  ASN Y ND2 
27582 N N   . GLN D 230  ? 2.8564 2.7852 2.2926 -0.4497 -0.2510 0.0752  230  GLN Y N   
27583 C CA  . GLN D 230  ? 2.7850 2.7140 2.2185 -0.5000 -0.2574 0.0649  230  GLN Y CA  
27584 C C   . GLN D 230  ? 2.7986 2.7016 2.1949 -0.5043 -0.2571 0.0726  230  GLN Y C   
27585 O O   . GLN D 230  ? 2.7903 2.7045 2.1791 -0.5372 -0.2650 0.0864  230  GLN Y O   
27586 C CB  . GLN D 230  ? 2.7100 2.6937 2.1725 -0.5238 -0.2685 0.0948  230  GLN Y CB  
27587 C CG  . GLN D 230  ? 2.6260 2.6389 2.1231 -0.5149 -0.2707 0.0970  230  GLN Y CG  
27588 C CD  . GLN D 230  ? 2.5595 2.6210 2.0828 -0.5453 -0.2844 0.1242  230  GLN Y CD  
27589 O OE1 . GLN D 230  ? 2.5298 2.6389 2.0772 -0.5271 -0.2878 0.1644  230  GLN Y OE1 
27590 N NE2 . GLN D 230  ? 2.5461 2.5941 2.0636 -0.5923 -0.2918 0.1025  230  GLN Y NE2 
27592 C C1  . NAG F .    ? 5.5455 4.8012 1.2770 1.7517  0.7290  -1.0497 2001 NAG A C1  
27593 C C2  . NAG F .    ? 5.5512 4.8323 1.2881 1.7349  0.7261  -1.0684 2001 NAG A C2  
27594 C C3  . NAG F .    ? 5.5710 4.8202 1.2436 1.7284  0.7533  -1.0799 2001 NAG A C3  
27595 C C4  . NAG F .    ? 5.5854 4.8080 1.2213 1.7249  0.7673  -1.0712 2001 NAG A C4  
27596 C C5  . NAG F .    ? 5.5943 4.7986 1.2475 1.7236  0.7723  -1.0533 2001 NAG A C5  
27597 C C6  . NAG F .    ? 5.6146 4.7926 1.2364 1.7135  0.7898  -1.0478 2001 NAG A C6  
27598 C C7  . NAG F .    ? 5.5498 4.8939 1.3708 1.7084  0.7081  -1.0924 2001 NAG A C7  
27599 C C8  . NAG F .    ? 5.5456 4.8959 1.3662 1.7097  0.7135  -1.1066 2001 NAG A C8  
27600 N N2  . NAG F .    ? 5.5519 4.8582 1.3350 1.7233  0.7217  -1.0741 2001 NAG A N2  
27601 O O3  . NAG F .    ? 5.5610 4.8269 1.2260 1.7309  0.7450  -1.1023 2001 NAG A O3  
27602 O O4  . NAG F .    ? 5.5964 4.7909 1.1722 1.7254  0.7968  -1.0804 2001 NAG A O4  
27603 O O5  . NAG F .    ? 5.5744 4.8017 1.2755 1.7343  0.7459  -1.0460 2001 NAG A O5  
27604 O O6  . NAG F .    ? 5.6117 4.8021 1.2244 1.7114  0.7746  -1.0501 2001 NAG A O6  
27605 O O7  . NAG F .    ? 5.5490 4.9173 1.3974 1.6977  0.6900  -1.0996 2001 NAG A O7  
27606 C C1  . NAG G .    ? 5.5924 4.7929 1.1444 1.7269  0.7964  -1.0986 2002 NAG A C1  
27607 C C2  . NAG G .    ? 5.6170 4.7939 1.1291 1.7114  0.8308  -1.0988 2002 NAG A C2  
27608 C C3  . NAG G .    ? 5.6249 4.8097 1.1274 1.7001  0.8318  -1.1177 2002 NAG A C3  
27609 C C4  . NAG G .    ? 5.6141 4.8071 1.1199 1.7074  0.8244  -1.1451 2002 NAG A C4  
27610 C C5  . NAG G .    ? 5.5884 4.8054 1.1342 1.7232  0.7889  -1.1442 2002 NAG A C5  
27611 C C6  . NAG G .    ? 5.5793 4.8043 1.1304 1.7282  0.7838  -1.1757 2002 NAG A C6  
27612 C C7  . NAG G .    ? 5.6458 4.7898 1.1469 1.6947  0.8650  -1.0709 2002 NAG A C7  
27613 C C8  . NAG G .    ? 5.6545 4.7830 1.1153 1.6913  0.8909  -1.0684 2002 NAG A C8  
27614 N N2  . NAG G .    ? 5.6320 4.7986 1.1494 1.7002  0.8372  -1.0793 2002 NAG A N2  
27615 O O3  . NAG G .    ? 5.6519 4.8261 1.1349 1.6767  0.8676  -1.1196 2002 NAG A O3  
27616 O O4  . NAG G .    ? 5.6210 4.8163 1.1235 1.6990  0.8214  -1.1651 2002 NAG A O4  
27617 O O5  . NAG G .    ? 5.5838 4.7983 1.1412 1.7294  0.7896  -1.1223 2002 NAG A O5  
27618 O O6  . NAG G .    ? 5.5926 4.7910 1.1017 1.7263  0.8157  -1.1852 2002 NAG A O6  
27619 O O7  . NAG G .    ? 5.6486 4.7820 1.1631 1.6958  0.8688  -1.0656 2002 NAG A O7  
27624 C C1  . NAG L .    ? 3.5970 4.1668 4.1566 -0.3902 -0.1653 -0.7227 1682 NAG A C1  
27625 C C2  . NAG L .    ? 3.3295 4.2158 3.9941 -0.2358 -0.1194 -0.9723 1682 NAG A C2  
27626 C C3  . NAG L .    ? 2.9429 4.2078 4.2986 -0.1136 -0.0810 -1.1886 1682 NAG A C3  
27627 C C4  . NAG L .    ? 2.8931 4.0801 4.5397 -0.1050 -0.0534 -1.1591 1682 NAG A C4  
27628 C C5  . NAG L .    ? 3.0328 3.9688 4.6355 -0.2842 -0.1241 -0.9082 1682 NAG A C5  
27629 C C6  . NAG L .    ? 2.8741 3.7553 4.8212 -0.2886 -0.1047 -0.8784 1682 NAG A C6  
27630 C C7  . NAG L .    ? 3.2295 4.3292 3.5219 -0.2186 -0.1505 -1.0868 1682 NAG A C7  
27631 C C8  . NAG L .    ? 3.0282 4.4622 3.6084 -0.2282 -0.1878 -1.1922 1682 NAG A C8  
27632 N N2  . NAG L .    ? 3.2738 4.2853 3.8519 -0.2941 -0.1731 -0.9682 1682 NAG A N2  
27633 O O3  . NAG L .    ? 2.8361 4.2647 4.1171 0.0488  -0.0134 -1.4009 1682 NAG A O3  
27634 O O4  . NAG L .    ? 2.5654 4.1176 4.8960 -0.0187 -0.0352 -1.3385 1682 NAG A O4  
27635 O O5  . NAG L .    ? 3.4498 4.0118 4.3610 -0.3618 -0.1339 -0.7351 1682 NAG A O5  
27636 O O6  . NAG L .    ? 2.9492 3.6003 4.5248 -0.2235 -0.0337 -0.8823 1682 NAG A O6  
27637 O O7  . NAG L .    ? 3.3719 4.2933 3.1866 -0.1459 -0.1037 -1.1129 1682 NAG A O7  
27638 C C1  . NAG M .    ? 6.8943 3.5946 1.7836 0.4903  -0.2157 1.2519  2001 NAG B C1  
27639 C C2  . NAG M .    ? 6.8952 3.5497 1.7264 0.4888  -0.2386 1.2631  2001 NAG B C2  
27640 C C3  . NAG M .    ? 6.8938 3.5368 1.6875 0.4951  -0.2354 1.2865  2001 NAG B C3  
27641 C C4  . NAG M .    ? 6.8912 3.5225 1.6629 0.5063  -0.2169 1.2932  2001 NAG B C4  
27642 C C5  . NAG M .    ? 6.8903 3.5434 1.6947 0.5083  -0.1951 1.2855  2001 NAG B C5  
27643 C C6  . NAG M .    ? 6.8866 3.5168 1.6574 0.5223  -0.1717 1.2958  2001 NAG B C6  
27644 C C7  . NAG M .    ? 6.8977 3.5244 1.7085 0.4771  -0.2719 1.2603  2001 NAG B C7  
27645 C C8  . NAG M .    ? 6.8981 3.5148 1.6954 0.4748  -0.2808 1.2637  2001 NAG B C8  
27646 N N2  . NAG M .    ? 6.8966 3.5445 1.7258 0.4827  -0.2500 1.2587  2001 NAG B N2  
27647 O O3  . NAG M .    ? 6.8942 3.5246 1.6718 0.4928  -0.2553 1.2919  2001 NAG B O3  
27648 O O4  . NAG M .    ? 6.8896 3.4889 1.6050 0.5147  -0.2117 1.3132  2001 NAG B O4  
27649 O O5  . NAG M .    ? 6.8912 3.5663 1.7436 0.5035  -0.1990 1.2632  2001 NAG B O5  
27650 O O6  . NAG M .    ? 6.8843 3.4868 1.6327 0.5321  -0.1731 1.2885  2001 NAG B O6  
27651 O O7  . NAG M .    ? 6.8981 3.5153 1.7046 0.4743  -0.2843 1.2592  2001 NAG B O7  
27652 C C1  . NAG N .    ? 6.8887 3.4539 1.5604 0.5198  -0.2269 1.3193  2002 NAG B C1  
27653 C C2  . NAG N .    ? 6.8861 3.4535 1.5375 0.5292  -0.2123 1.3327  2002 NAG B C2  
27654 C C3  . NAG N .    ? 6.8844 3.4517 1.5293 0.5345  -0.2255 1.3316  2002 NAG B C3  
27655 C C4  . NAG N .    ? 6.8853 3.4370 1.5201 0.5318  -0.2456 1.3341  2002 NAG B C4  
27656 C C5  . NAG N .    ? 6.8881 3.4265 1.5311 0.5217  -0.2596 1.3245  2002 NAG B C5  
27657 C C6  . NAG N .    ? 6.8881 3.4071 1.5157 0.5214  -0.2773 1.3308  2002 NAG B C6  
27658 C C7  . NAG N .    ? 6.8835 3.4902 1.5637 0.5339  -0.1690 1.3418  2002 NAG B C7  
27659 C C8  . NAG N .    ? 6.8804 3.4934 1.5422 0.5425  -0.1541 1.3551  2002 NAG B C8  
27660 N N2  . NAG N .    ? 6.8845 3.4762 1.5599 0.5326  -0.1916 1.3304  2002 NAG B N2  
27661 O O3  . NAG N .    ? 6.8817 3.4749 1.5293 0.5420  -0.2102 1.3423  2002 NAG B O3  
27662 O O4  . NAG N .    ? 6.8834 3.4410 1.5237 0.5371  -0.2566 1.3292  2002 NAG B O4  
27663 O O5  . NAG N .    ? 6.8895 3.4398 1.5466 0.5169  -0.2461 1.3237  2002 NAG B O5  
27664 O O6  . NAG N .    ? 6.8872 3.3959 1.4895 0.5263  -0.2708 1.3464  2002 NAG B O6  
27665 O O7  . NAG N .    ? 6.8846 3.4932 1.5764 0.5297  -0.1594 1.3407  2002 NAG B O7  
27670 C C1  . NAG S .    ? 3.6913 5.3465 3.6437 -0.3960 -0.8403 0.6584  1681 NAG B C1  
27671 C C2  . NAG S .    ? 3.5234 4.7774 3.4848 -0.2678 -0.9408 0.7726  1681 NAG B C2  
27672 C C3  . NAG S .    ? 3.4394 3.9344 3.5820 -0.2273 -0.9753 0.7561  1681 NAG B C3  
27673 C C4  . NAG S .    ? 3.4112 3.6832 3.6835 -0.1713 -0.9165 0.7096  1681 NAG B C4  
27674 C C5  . NAG S .    ? 3.5417 4.1928 3.8020 -0.3895 -0.8232 0.5386  1681 NAG B C5  
27675 C C6  . NAG S .    ? 3.4522 3.8653 3.8558 -0.3661 -0.7642 0.4663  1681 NAG B C6  
27676 C C7  . NAG S .    ? 3.3901 4.7773 3.1816 -0.3731 -1.0632 0.8304  1681 NAG B C7  
27677 C C8  . NAG S .    ? 3.4255 4.6760 3.1944 -0.6084 -1.1204 0.7330  1681 NAG B C8  
27678 N N2  . NAG S .    ? 3.5219 4.9303 3.3839 -0.4590 -0.9806 0.7180  1681 NAG B N2  
27679 O O3  . NAG S .    ? 3.3031 3.5500 3.4347 0.0008  -1.0492 0.9328  1681 NAG B O3  
27680 O O4  . NAG S .    ? 3.3889 2.9887 3.8292 -0.2005 -0.9406 0.6645  1681 NAG B O4  
27681 O O5  . NAG S .    ? 3.6196 4.9477 3.7217 -0.3401 -0.7993 0.6129  1681 NAG B O5  
27682 O O6  . NAG S .    ? 3.2692 3.8659 3.6376 -0.1144 -0.7707 0.6162  1681 NAG B O6  
27683 O O7  . NAG S .    ? 3.2732 4.7464 3.0177 -0.1219 -1.0930 1.0029  1681 NAG B O7  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1    MET 1    1    ?    ?   ?   A . n 
A 1 2    GLY 2    2    ?    ?   ?   A . n 
A 1 3    LEU 3    3    ?    ?   ?   A . n 
A 1 4    LEU 4    4    ?    ?   ?   A . n 
A 1 5    GLY 5    5    ?    ?   ?   A . n 
A 1 6    ILE 6    6    ?    ?   ?   A . n 
A 1 7    LEU 7    7    ?    ?   ?   A . n 
A 1 8    CYS 8    8    ?    ?   ?   A . n 
A 1 9    PHE 9    9    ?    ?   ?   A . n 
A 1 10   LEU 10   10   ?    ?   ?   A . n 
A 1 11   ILE 11   11   ?    ?   ?   A . n 
A 1 12   PHE 12   12   ?    ?   ?   A . n 
A 1 13   LEU 13   13   ?    ?   ?   A . n 
A 1 14   GLY 14   14   ?    ?   ?   A . n 
A 1 15   LYS 15   15   ?    ?   ?   A . n 
A 1 16   THR 16   16   ?    ?   ?   A . n 
A 1 17   TRP 17   17   ?    ?   ?   A . n 
A 1 18   GLY 18   18   ?    ?   ?   A . n 
A 1 19   GLN 19   19   ?    ?   ?   A . n 
A 1 20   GLU 20   20   ?    ?   ?   A . n 
A 1 21   GLN 21   21   ?    ?   ?   A . n 
A 1 22   THR 22   22   22   THR THR A . n 
A 1 23   TYR 23   23   23   TYR TYR A . n 
A 1 24   VAL 24   24   24   VAL VAL A . n 
A 1 25   ILE 25   25   25   ILE ILE A . n 
A 1 26   SER 26   26   26   SER SER A . n 
A 1 27   ALA 27   27   27   ALA ALA A . n 
A 1 28   PRO 28   28   28   PRO PRO A . n 
A 1 29   LYS 29   29   29   LYS LYS A . n 
A 1 30   ILE 30   30   30   ILE ILE A . n 
A 1 31   PHE 31   31   31   PHE PHE A . n 
A 1 32   ARG 32   32   32   ARG ARG A . n 
A 1 33   VAL 33   33   33   VAL VAL A . n 
A 1 34   GLY 34   34   34   GLY GLY A . n 
A 1 35   ALA 35   35   35   ALA ALA A . n 
A 1 36   SER 36   36   36   SER SER A . n 
A 1 37   GLU 37   37   37   GLU GLU A . n 
A 1 38   ASN 38   38   38   ASN ASN A . n 
A 1 39   ILE 39   39   39   ILE ILE A . n 
A 1 40   VAL 40   40   40   VAL VAL A . n 
A 1 41   ILE 41   41   41   ILE ILE A . n 
A 1 42   GLN 42   42   42   GLN GLN A . n 
A 1 43   VAL 43   43   43   VAL VAL A . n 
A 1 44   TYR 44   44   44   TYR TYR A . n 
A 1 45   GLY 45   45   45   GLY GLY A . n 
A 1 46   TYR 46   46   46   TYR TYR A . n 
A 1 47   THR 47   47   47   THR THR A . n 
A 1 48   GLU 48   48   48   GLU GLU A . n 
A 1 49   ALA 49   49   49   ALA ALA A . n 
A 1 50   PHE 50   50   50   PHE PHE A . n 
A 1 51   ASP 51   51   51   ASP ASP A . n 
A 1 52   ALA 52   52   52   ALA ALA A . n 
A 1 53   THR 53   53   53   THR THR A . n 
A 1 54   ILE 54   54   54   ILE ILE A . n 
A 1 55   SER 55   55   55   SER SER A . n 
A 1 56   ILE 56   56   56   ILE ILE A . n 
A 1 57   LYS 57   57   57   LYS LYS A . n 
A 1 58   SER 58   58   58   SER SER A . n 
A 1 59   TYR 59   59   59   TYR TYR A . n 
A 1 60   PRO 60   60   60   PRO PRO A . n 
A 1 61   ASP 61   61   61   ASP ASP A . n 
A 1 62   LYS 62   62   62   LYS LYS A . n 
A 1 63   LYS 63   63   63   LYS LYS A . n 
A 1 64   PHE 64   64   64   PHE PHE A . n 
A 1 65   SER 65   65   65   SER SER A . n 
A 1 66   TYR 66   66   66   TYR TYR A . n 
A 1 67   SER 67   67   67   SER SER A . n 
A 1 68   SER 68   68   68   SER SER A . n 
A 1 69   GLY 69   69   69   GLY GLY A . n 
A 1 70   HIS 70   70   70   HIS HIS A . n 
A 1 71   VAL 71   71   71   VAL VAL A . n 
A 1 72   HIS 72   72   72   HIS HIS A . n 
A 1 73   LEU 73   73   73   LEU LEU A . n 
A 1 74   SER 74   74   74   SER SER A . n 
A 1 75   SER 75   75   75   SER SER A . n 
A 1 76   GLU 76   76   76   GLU GLU A . n 
A 1 77   ASN 77   77   77   ASN ASN A . n 
A 1 78   LYS 78   78   78   LYS LYS A . n 
A 1 79   PHE 79   79   79   PHE PHE A . n 
A 1 80   GLN 80   80   80   GLN GLN A . n 
A 1 81   ASN 81   81   81   ASN ASN A . n 
A 1 82   SER 82   82   82   SER SER A . n 
A 1 83   ALA 83   83   83   ALA ALA A . n 
A 1 84   ILE 84   84   84   ILE ILE A . n 
A 1 85   LEU 85   85   85   LEU LEU A . n 
A 1 86   THR 86   86   86   THR THR A . n 
A 1 87   ILE 87   87   87   ILE ILE A . n 
A 1 88   GLN 88   88   88   GLN GLN A . n 
A 1 89   PRO 89   89   89   PRO PRO A . n 
A 1 90   LYS 90   90   90   LYS LYS A . n 
A 1 91   GLN 91   91   91   GLN GLN A . n 
A 1 92   LEU 92   92   92   LEU LEU A . n 
A 1 93   PRO 93   93   93   PRO PRO A . n 
A 1 94   GLY 94   94   94   GLY GLY A . n 
A 1 95   GLY 95   95   95   GLY GLY A . n 
A 1 96   GLN 96   96   96   GLN GLN A . n 
A 1 97   ASN 97   97   97   ASN ASN A . n 
A 1 98   PRO 98   98   98   PRO PRO A . n 
A 1 99   VAL 99   99   99   VAL VAL A . n 
A 1 100  SER 100  100  100  SER SER A . n 
A 1 101  TYR 101  101  101  TYR TYR A . n 
A 1 102  VAL 102  102  102  VAL VAL A . n 
A 1 103  TYR 103  103  103  TYR TYR A . n 
A 1 104  LEU 104  104  104  LEU LEU A . n 
A 1 105  GLU 105  105  105  GLU GLU A . n 
A 1 106  VAL 106  106  106  VAL VAL A . n 
A 1 107  VAL 107  107  107  VAL VAL A . n 
A 1 108  SER 108  108  108  SER SER A . n 
A 1 109  LYS 109  109  109  LYS LYS A . n 
A 1 110  HIS 110  110  110  HIS HIS A . n 
A 1 111  PHE 111  111  111  PHE PHE A . n 
A 1 112  SER 112  112  112  SER SER A . n 
A 1 113  LYS 113  113  113  LYS LYS A . n 
A 1 114  SER 114  114  114  SER SER A . n 
A 1 115  LYS 115  115  115  LYS LYS A . n 
A 1 116  ARG 116  116  116  ARG ARG A . n 
A 1 117  MET 117  117  117  MET MET A . n 
A 1 118  PRO 118  118  118  PRO PRO A . n 
A 1 119  ILE 119  119  119  ILE ILE A . n 
A 1 120  THR 120  120  120  THR THR A . n 
A 1 121  TYR 121  121  121  TYR TYR A . n 
A 1 122  ASP 122  122  122  ASP ASP A . n 
A 1 123  ASN 123  123  123  ASN ASN A . n 
A 1 124  GLY 124  124  124  GLY GLY A . n 
A 1 125  PHE 125  125  125  PHE PHE A . n 
A 1 126  LEU 126  126  126  LEU LEU A . n 
A 1 127  PHE 127  127  127  PHE PHE A . n 
A 1 128  ILE 128  128  128  ILE ILE A . n 
A 1 129  HIS 129  129  129  HIS HIS A . n 
A 1 130  THR 130  130  130  THR THR A . n 
A 1 131  ASP 131  131  131  ASP ASP A . n 
A 1 132  LYS 132  132  132  LYS LYS A . n 
A 1 133  PRO 133  133  133  PRO PRO A . n 
A 1 134  VAL 134  134  134  VAL VAL A . n 
A 1 135  TYR 135  135  135  TYR TYR A . n 
A 1 136  THR 136  136  136  THR THR A . n 
A 1 137  PRO 137  137  137  PRO PRO A . n 
A 1 138  ASP 138  138  138  ASP ASP A . n 
A 1 139  GLN 139  139  139  GLN GLN A . n 
A 1 140  SER 140  140  140  SER SER A . n 
A 1 141  VAL 141  141  141  VAL VAL A . n 
A 1 142  LYS 142  142  142  LYS LYS A . n 
A 1 143  VAL 143  143  143  VAL VAL A . n 
A 1 144  ARG 144  144  144  ARG ARG A . n 
A 1 145  VAL 145  145  145  VAL VAL A . n 
A 1 146  TYR 146  146  146  TYR TYR A . n 
A 1 147  SER 147  147  147  SER SER A . n 
A 1 148  LEU 148  148  148  LEU LEU A . n 
A 1 149  ASN 149  149  149  ASN ASN A . n 
A 1 150  ASP 150  150  150  ASP ASP A . n 
A 1 151  ASP 151  151  151  ASP ASP A . n 
A 1 152  LEU 152  152  152  LEU LEU A . n 
A 1 153  LYS 153  153  153  LYS LYS A . n 
A 1 154  PRO 154  154  154  PRO PRO A . n 
A 1 155  ALA 155  155  155  ALA ALA A . n 
A 1 156  LYS 156  156  156  LYS LYS A . n 
A 1 157  ARG 157  157  157  ARG ARG A . n 
A 1 158  GLU 158  158  158  GLU GLU A . n 
A 1 159  THR 159  159  159  THR THR A . n 
A 1 160  VAL 160  160  160  VAL VAL A . n 
A 1 161  LEU 161  161  161  LEU LEU A . n 
A 1 162  THR 162  162  162  THR THR A . n 
A 1 163  PHE 163  163  163  PHE PHE A . n 
A 1 164  ILE 164  164  164  ILE ILE A . n 
A 1 165  ASP 165  165  165  ASP ASP A . n 
A 1 166  PRO 166  166  166  PRO PRO A . n 
A 1 167  GLU 167  167  167  GLU GLU A . n 
A 1 168  GLY 168  168  168  GLY GLY A . n 
A 1 169  SER 169  169  169  SER SER A . n 
A 1 170  GLU 170  170  170  GLU GLU A . n 
A 1 171  VAL 171  171  171  VAL VAL A . n 
A 1 172  ASP 172  172  172  ASP ASP A . n 
A 1 173  MET 173  173  173  MET MET A . n 
A 1 174  VAL 174  174  174  VAL VAL A . n 
A 1 175  GLU 175  175  175  GLU GLU A . n 
A 1 176  GLU 176  176  176  GLU GLU A . n 
A 1 177  ILE 177  177  177  ILE ILE A . n 
A 1 178  ASP 178  178  178  ASP ASP A . n 
A 1 179  HIS 179  179  179  HIS HIS A . n 
A 1 180  ILE 180  180  180  ILE ILE A . n 
A 1 181  GLY 181  181  181  GLY GLY A . n 
A 1 182  ILE 182  182  182  ILE ILE A . n 
A 1 183  ILE 183  183  183  ILE ILE A . n 
A 1 184  SER 184  184  184  SER SER A . n 
A 1 185  PHE 185  185  185  PHE PHE A . n 
A 1 186  PRO 186  186  186  PRO PRO A . n 
A 1 187  ASP 187  187  187  ASP ASP A . n 
A 1 188  PHE 188  188  188  PHE PHE A . n 
A 1 189  LYS 189  189  189  LYS LYS A . n 
A 1 190  ILE 190  190  190  ILE ILE A . n 
A 1 191  PRO 191  191  191  PRO PRO A . n 
A 1 192  SER 192  192  192  SER SER A . n 
A 1 193  ASN 193  193  193  ASN ASN A . n 
A 1 194  PRO 194  194  194  PRO PRO A . n 
A 1 195  ARG 195  195  195  ARG ARG A . n 
A 1 196  TYR 196  196  196  TYR TYR A . n 
A 1 197  GLY 197  197  197  GLY GLY A . n 
A 1 198  MET 198  198  198  MET MET A . n 
A 1 199  TRP 199  199  199  TRP TRP A . n 
A 1 200  THR 200  200  200  THR THR A . n 
A 1 201  ILE 201  201  201  ILE ILE A . n 
A 1 202  LYS 202  202  202  LYS LYS A . n 
A 1 203  ALA 203  203  203  ALA ALA A . n 
A 1 204  LYS 204  204  204  LYS LYS A . n 
A 1 205  TYR 205  205  205  TYR TYR A . n 
A 1 206  LYS 206  206  206  LYS LYS A . n 
A 1 207  GLU 207  207  207  GLU GLU A . n 
A 1 208  ASP 208  208  208  ASP ASP A . n 
A 1 209  PHE 209  209  209  PHE PHE A . n 
A 1 210  SER 210  210  210  SER SER A . n 
A 1 211  THR 211  211  211  THR THR A . n 
A 1 212  THR 212  212  212  THR THR A . n 
A 1 213  GLY 213  213  213  GLY GLY A . n 
A 1 214  THR 214  214  214  THR THR A . n 
A 1 215  ALA 215  215  215  ALA ALA A . n 
A 1 216  TYR 216  216  216  TYR TYR A . n 
A 1 217  PHE 217  217  217  PHE PHE A . n 
A 1 218  GLU 218  218  218  GLU GLU A . n 
A 1 219  VAL 219  219  219  VAL VAL A . n 
A 1 220  LYS 220  220  220  LYS LYS A . n 
A 1 221  GLU 221  221  221  GLU GLU A . n 
A 1 222  TYR 222  222  222  TYR TYR A . n 
A 1 223  VAL 223  223  223  VAL VAL A . n 
A 1 224  LEU 224  224  224  LEU LEU A . n 
A 1 225  PRO 225  225  225  PRO PRO A . n 
A 1 226  HIS 226  226  226  HIS HIS A . n 
A 1 227  PHE 227  227  227  PHE PHE A . n 
A 1 228  SER 228  228  228  SER SER A . n 
A 1 229  VAL 229  229  229  VAL VAL A . n 
A 1 230  SER 230  230  230  SER SER A . n 
A 1 231  ILE 231  231  231  ILE ILE A . n 
A 1 232  GLU 232  232  232  GLU GLU A . n 
A 1 233  PRO 233  233  233  PRO PRO A . n 
A 1 234  GLU 234  234  234  GLU GLU A . n 
A 1 235  TYR 235  235  235  TYR TYR A . n 
A 1 236  ASN 236  236  236  ASN ASN A . n 
A 1 237  PHE 237  237  237  PHE PHE A . n 
A 1 238  ILE 238  238  238  ILE ILE A . n 
A 1 239  GLY 239  239  239  GLY GLY A . n 
A 1 240  TYR 240  240  240  TYR TYR A . n 
A 1 241  LYS 241  241  241  LYS LYS A . n 
A 1 242  ASN 242  242  242  ASN ASN A . n 
A 1 243  PHE 243  243  243  PHE PHE A . n 
A 1 244  LYS 244  244  244  LYS LYS A . n 
A 1 245  ASN 245  245  245  ASN ASN A . n 
A 1 246  PHE 246  246  246  PHE PHE A . n 
A 1 247  GLU 247  247  247  GLU GLU A . n 
A 1 248  ILE 248  248  248  ILE ILE A . n 
A 1 249  THR 249  249  249  THR THR A . n 
A 1 250  ILE 250  250  250  ILE ILE A . n 
A 1 251  LYS 251  251  251  LYS LYS A . n 
A 1 252  ALA 252  252  252  ALA ALA A . n 
A 1 253  ARG 253  253  253  ARG ARG A . n 
A 1 254  TYR 254  254  254  TYR TYR A . n 
A 1 255  PHE 255  255  255  PHE PHE A . n 
A 1 256  TYR 256  256  256  TYR TYR A . n 
A 1 257  ASN 257  257  257  ASN ASN A . n 
A 1 258  LYS 258  258  258  LYS LYS A . n 
A 1 259  VAL 259  259  259  VAL VAL A . n 
A 1 260  VAL 260  260  260  VAL VAL A . n 
A 1 261  THR 261  261  261  THR THR A . n 
A 1 262  GLU 262  262  262  GLU GLU A . n 
A 1 263  ALA 263  263  263  ALA ALA A . n 
A 1 264  ASP 264  264  264  ASP ASP A . n 
A 1 265  VAL 265  265  265  VAL VAL A . n 
A 1 266  TYR 266  266  266  TYR TYR A . n 
A 1 267  ILE 267  267  267  ILE ILE A . n 
A 1 268  THR 268  268  268  THR THR A . n 
A 1 269  PHE 269  269  269  PHE PHE A . n 
A 1 270  GLY 270  270  270  GLY GLY A . n 
A 1 271  ILE 271  271  271  ILE ILE A . n 
A 1 272  ARG 272  272  272  ARG ARG A . n 
A 1 273  GLU 273  273  273  GLU GLU A . n 
A 1 274  ASP 274  274  274  ASP ASP A . n 
A 1 275  LEU 275  275  275  LEU LEU A . n 
A 1 276  LYS 276  276  276  LYS LYS A . n 
A 1 277  ASP 277  277  277  ASP ASP A . n 
A 1 278  ASP 278  278  278  ASP ASP A . n 
A 1 279  GLN 279  279  279  GLN GLN A . n 
A 1 280  LYS 280  280  280  LYS LYS A . n 
A 1 281  GLU 281  281  281  GLU GLU A . n 
A 1 282  MET 282  282  282  MET MET A . n 
A 1 283  MET 283  283  283  MET MET A . n 
A 1 284  GLN 284  284  284  GLN GLN A . n 
A 1 285  THR 285  285  285  THR THR A . n 
A 1 286  ALA 286  286  286  ALA ALA A . n 
A 1 287  MET 287  287  287  MET MET A . n 
A 1 288  GLN 288  288  288  GLN GLN A . n 
A 1 289  ASN 289  289  289  ASN ASN A . n 
A 1 290  THR 290  290  290  THR THR A . n 
A 1 291  MET 291  291  291  MET MET A . n 
A 1 292  LEU 292  292  292  LEU LEU A . n 
A 1 293  ILE 293  293  293  ILE ILE A . n 
A 1 294  ASN 294  294  294  ASN ASN A . n 
A 1 295  GLY 295  295  295  GLY GLY A . n 
A 1 296  ILE 296  296  296  ILE ILE A . n 
A 1 297  ALA 297  297  297  ALA ALA A . n 
A 1 298  GLN 298  298  298  GLN GLN A . n 
A 1 299  VAL 299  299  299  VAL VAL A . n 
A 1 300  THR 300  300  300  THR THR A . n 
A 1 301  PHE 301  301  301  PHE PHE A . n 
A 1 302  ASP 302  302  302  ASP ASP A . n 
A 1 303  SER 303  303  303  SER SER A . n 
A 1 304  GLU 304  304  304  GLU GLU A . n 
A 1 305  THR 305  305  305  THR THR A . n 
A 1 306  ALA 306  306  306  ALA ALA A . n 
A 1 307  VAL 307  307  307  VAL VAL A . n 
A 1 308  LYS 308  308  308  LYS LYS A . n 
A 1 309  GLU 309  309  309  GLU GLU A . n 
A 1 310  LEU 310  310  310  LEU LEU A . n 
A 1 311  SER 311  311  311  SER SER A . n 
A 1 312  TYR 312  312  312  TYR TYR A . n 
A 1 313  TYR 313  313  313  TYR TYR A . n 
A 1 314  SER 314  314  314  SER SER A . n 
A 1 315  LEU 315  315  315  LEU LEU A . n 
A 1 316  GLU 316  316  316  GLU GLU A . n 
A 1 317  ASP 317  317  317  ASP ASP A . n 
A 1 318  LEU 318  318  318  LEU LEU A . n 
A 1 319  ASN 319  319  319  ASN ASN A . n 
A 1 320  ASN 320  320  320  ASN ASN A . n 
A 1 321  LYS 321  321  321  LYS LYS A . n 
A 1 322  TYR 322  322  322  TYR TYR A . n 
A 1 323  LEU 323  323  323  LEU LEU A . n 
A 1 324  TYR 324  324  324  TYR TYR A . n 
A 1 325  ILE 325  325  325  ILE ILE A . n 
A 1 326  ALA 326  326  326  ALA ALA A . n 
A 1 327  VAL 327  327  327  VAL VAL A . n 
A 1 328  THR 328  328  328  THR THR A . n 
A 1 329  VAL 329  329  329  VAL VAL A . n 
A 1 330  ILE 330  330  330  ILE ILE A . n 
A 1 331  GLU 331  331  331  GLU GLU A . n 
A 1 332  SER 332  332  332  SER SER A . n 
A 1 333  THR 333  333  333  THR THR A . n 
A 1 334  GLY 334  334  334  GLY GLY A . n 
A 1 335  GLY 335  335  335  GLY GLY A . n 
A 1 336  PHE 336  336  336  PHE PHE A . n 
A 1 337  SER 337  337  337  SER SER A . n 
A 1 338  GLU 338  338  338  GLU GLU A . n 
A 1 339  GLU 339  339  339  GLU GLU A . n 
A 1 340  ALA 340  340  340  ALA ALA A . n 
A 1 341  GLU 341  341  341  GLU GLU A . n 
A 1 342  ILE 342  342  342  ILE ILE A . n 
A 1 343  PRO 343  343  343  PRO PRO A . n 
A 1 344  GLY 344  344  344  GLY GLY A . n 
A 1 345  ILE 345  345  345  ILE ILE A . n 
A 1 346  LYS 346  346  346  LYS LYS A . n 
A 1 347  TYR 347  347  347  TYR TYR A . n 
A 1 348  VAL 348  348  348  VAL VAL A . n 
A 1 349  LEU 349  349  349  LEU LEU A . n 
A 1 350  SER 350  350  350  SER SER A . n 
A 1 351  PRO 351  351  351  PRO PRO A . n 
A 1 352  TYR 352  352  352  TYR TYR A . n 
A 1 353  LYS 353  353  353  LYS LYS A . n 
A 1 354  LEU 354  354  354  LEU LEU A . n 
A 1 355  ASN 355  355  355  ASN ASN A . n 
A 1 356  LEU 356  356  356  LEU LEU A . n 
A 1 357  VAL 357  357  357  VAL VAL A . n 
A 1 358  ALA 358  358  358  ALA ALA A . n 
A 1 359  THR 359  359  359  THR THR A . n 
A 1 360  PRO 360  360  360  PRO PRO A . n 
A 1 361  LEU 361  361  361  LEU LEU A . n 
A 1 362  PHE 362  362  362  PHE PHE A . n 
A 1 363  LEU 363  363  363  LEU LEU A . n 
A 1 364  LYS 364  364  364  LYS LYS A . n 
A 1 365  PRO 365  365  365  PRO PRO A . n 
A 1 366  GLY 366  366  366  GLY GLY A . n 
A 1 367  ILE 367  367  367  ILE ILE A . n 
A 1 368  PRO 368  368  368  PRO PRO A . n 
A 1 369  TYR 369  369  369  TYR TYR A . n 
A 1 370  PRO 370  370  370  PRO PRO A . n 
A 1 371  ILE 371  371  371  ILE ILE A . n 
A 1 372  LYS 372  372  372  LYS LYS A . n 
A 1 373  VAL 373  373  373  VAL VAL A . n 
A 1 374  GLN 374  374  374  GLN GLN A . n 
A 1 375  VAL 375  375  375  VAL VAL A . n 
A 1 376  LYS 376  376  376  LYS LYS A . n 
A 1 377  ASP 377  377  377  ASP ASP A . n 
A 1 378  SER 378  378  378  SER SER A . n 
A 1 379  LEU 379  379  379  LEU LEU A . n 
A 1 380  ASP 380  380  380  ASP ASP A . n 
A 1 381  GLN 381  381  381  GLN GLN A . n 
A 1 382  LEU 382  382  382  LEU LEU A . n 
A 1 383  VAL 383  383  383  VAL VAL A . n 
A 1 384  GLY 384  384  384  GLY GLY A . n 
A 1 385  GLY 385  385  385  GLY GLY A . n 
A 1 386  VAL 386  386  386  VAL VAL A . n 
A 1 387  PRO 387  387  387  PRO PRO A . n 
A 1 388  VAL 388  388  388  VAL VAL A . n 
A 1 389  THR 389  389  389  THR THR A . n 
A 1 390  LEU 390  390  390  LEU LEU A . n 
A 1 391  ASN 391  391  391  ASN ASN A . n 
A 1 392  ALA 392  392  392  ALA ALA A . n 
A 1 393  GLN 393  393  393  GLN GLN A . n 
A 1 394  THR 394  394  394  THR THR A . n 
A 1 395  ILE 395  395  395  ILE ILE A . n 
A 1 396  ASP 396  396  396  ASP ASP A . n 
A 1 397  VAL 397  397  397  VAL VAL A . n 
A 1 398  ASN 398  398  398  ASN ASN A . n 
A 1 399  GLN 399  399  399  GLN GLN A . n 
A 1 400  GLU 400  400  400  GLU GLU A . n 
A 1 401  THR 401  401  401  THR THR A . n 
A 1 402  SER 402  402  402  SER SER A . n 
A 1 403  ASP 403  403  403  ASP ASP A . n 
A 1 404  LEU 404  404  404  LEU LEU A . n 
A 1 405  ASP 405  405  405  ASP ASP A . n 
A 1 406  PRO 406  406  406  PRO PRO A . n 
A 1 407  SER 407  407  407  SER SER A . n 
A 1 408  LYS 408  408  408  LYS LYS A . n 
A 1 409  SER 409  409  409  SER SER A . n 
A 1 410  VAL 410  410  410  VAL VAL A . n 
A 1 411  THR 411  411  411  THR THR A . n 
A 1 412  ARG 412  412  412  ARG ARG A . n 
A 1 413  VAL 413  413  413  VAL VAL A . n 
A 1 414  ASP 414  414  414  ASP ASP A . n 
A 1 415  ASP 415  415  415  ASP ASP A . n 
A 1 416  GLY 416  416  416  GLY GLY A . n 
A 1 417  VAL 417  417  417  VAL VAL A . n 
A 1 418  ALA 418  418  418  ALA ALA A . n 
A 1 419  SER 419  419  419  SER SER A . n 
A 1 420  PHE 420  420  420  PHE PHE A . n 
A 1 421  VAL 421  421  421  VAL VAL A . n 
A 1 422  LEU 422  422  422  LEU LEU A . n 
A 1 423  ASN 423  423  423  ASN ASN A . n 
A 1 424  LEU 424  424  424  LEU LEU A . n 
A 1 425  PRO 425  425  425  PRO PRO A . n 
A 1 426  SER 426  426  426  SER SER A . n 
A 1 427  GLY 427  427  427  GLY GLY A . n 
A 1 428  VAL 428  428  428  VAL VAL A . n 
A 1 429  THR 429  429  429  THR THR A . n 
A 1 430  VAL 430  430  430  VAL VAL A . n 
A 1 431  LEU 431  431  431  LEU LEU A . n 
A 1 432  GLU 432  432  432  GLU GLU A . n 
A 1 433  PHE 433  433  433  PHE PHE A . n 
A 1 434  ASN 434  434  434  ASN ASN A . n 
A 1 435  VAL 435  435  435  VAL VAL A . n 
A 1 436  LYS 436  436  436  LYS LYS A . n 
A 1 437  THR 437  437  437  THR THR A . n 
A 1 438  ASP 438  438  438  ASP ASP A . n 
A 1 439  ALA 439  439  439  ALA ALA A . n 
A 1 440  PRO 440  440  440  PRO PRO A . n 
A 1 441  ASP 441  441  441  ASP ASP A . n 
A 1 442  LEU 442  442  442  LEU LEU A . n 
A 1 443  PRO 443  443  443  PRO PRO A . n 
A 1 444  GLU 444  444  444  GLU GLU A . n 
A 1 445  GLU 445  445  445  GLU GLU A . n 
A 1 446  ASN 446  446  446  ASN ASN A . n 
A 1 447  GLN 447  447  447  GLN GLN A . n 
A 1 448  ALA 448  448  448  ALA ALA A . n 
A 1 449  ARG 449  449  449  ARG ARG A . n 
A 1 450  GLU 450  450  450  GLU GLU A . n 
A 1 451  GLY 451  451  451  GLY GLY A . n 
A 1 452  TYR 452  452  452  TYR TYR A . n 
A 1 453  ARG 453  453  453  ARG ARG A . n 
A 1 454  ALA 454  454  454  ALA ALA A . n 
A 1 455  ILE 455  455  455  ILE ILE A . n 
A 1 456  ALA 456  456  456  ALA ALA A . n 
A 1 457  TYR 457  457  457  TYR TYR A . n 
A 1 458  SER 458  458  458  SER SER A . n 
A 1 459  SER 459  459  459  SER SER A . n 
A 1 460  LEU 460  460  460  LEU LEU A . n 
A 1 461  SER 461  461  461  SER SER A . n 
A 1 462  GLN 462  462  462  GLN GLN A . n 
A 1 463  SER 463  463  463  SER SER A . n 
A 1 464  TYR 464  464  464  TYR TYR A . n 
A 1 465  LEU 465  465  465  LEU LEU A . n 
A 1 466  TYR 466  466  466  TYR TYR A . n 
A 1 467  ILE 467  467  467  ILE ILE A . n 
A 1 468  ASP 468  468  468  ASP ASP A . n 
A 1 469  TRP 469  469  469  TRP TRP A . n 
A 1 470  THR 470  470  470  THR THR A . n 
A 1 471  ASP 471  471  471  ASP ASP A . n 
A 1 472  ASN 472  472  472  ASN ASN A . n 
A 1 473  HIS 473  473  473  HIS HIS A . n 
A 1 474  LYS 474  474  474  LYS LYS A . n 
A 1 475  ALA 475  475  475  ALA ALA A . n 
A 1 476  LEU 476  476  476  LEU LEU A . n 
A 1 477  LEU 477  477  477  LEU LEU A . n 
A 1 478  VAL 478  478  478  VAL VAL A . n 
A 1 479  GLY 479  479  479  GLY GLY A . n 
A 1 480  GLU 480  480  480  GLU GLU A . n 
A 1 481  HIS 481  481  481  HIS HIS A . n 
A 1 482  LEU 482  482  482  LEU LEU A . n 
A 1 483  ASN 483  483  483  ASN ASN A . n 
A 1 484  ILE 484  484  484  ILE ILE A . n 
A 1 485  ILE 485  485  485  ILE ILE A . n 
A 1 486  VAL 486  486  486  VAL VAL A . n 
A 1 487  THR 487  487  487  THR THR A . n 
A 1 488  PRO 488  488  488  PRO PRO A . n 
A 1 489  LYS 489  489  489  LYS LYS A . n 
A 1 490  SER 490  490  490  SER SER A . n 
A 1 491  PRO 491  491  491  PRO PRO A . n 
A 1 492  TYR 492  492  492  TYR TYR A . n 
A 1 493  ILE 493  493  493  ILE ILE A . n 
A 1 494  ASP 494  494  494  ASP ASP A . n 
A 1 495  LYS 495  495  495  LYS LYS A . n 
A 1 496  ILE 496  496  496  ILE ILE A . n 
A 1 497  THR 497  497  497  THR THR A . n 
A 1 498  HIS 498  498  498  HIS HIS A . n 
A 1 499  TYR 499  499  499  TYR TYR A . n 
A 1 500  ASN 500  500  500  ASN ASN A . n 
A 1 501  TYR 501  501  501  TYR TYR A . n 
A 1 502  LEU 502  502  502  LEU LEU A . n 
A 1 503  ILE 503  503  503  ILE ILE A . n 
A 1 504  LEU 504  504  504  LEU LEU A . n 
A 1 505  SER 505  505  505  SER SER A . n 
A 1 506  LYS 506  506  506  LYS LYS A . n 
A 1 507  GLY 507  507  507  GLY GLY A . n 
A 1 508  LYS 508  508  508  LYS LYS A . n 
A 1 509  ILE 509  509  509  ILE ILE A . n 
A 1 510  ILE 510  510  510  ILE ILE A . n 
A 1 511  HIS 511  511  511  HIS HIS A . n 
A 1 512  PHE 512  512  512  PHE PHE A . n 
A 1 513  GLY 513  513  513  GLY GLY A . n 
A 1 514  THR 514  514  514  THR THR A . n 
A 1 515  ARG 515  515  515  ARG ARG A . n 
A 1 516  GLU 516  516  516  GLU GLU A . n 
A 1 517  LYS 517  517  517  LYS LYS A . n 
A 1 518  PHE 518  518  518  PHE PHE A . n 
A 1 519  SER 519  519  519  SER SER A . n 
A 1 520  ASP 520  520  520  ASP ASP A . n 
A 1 521  ALA 521  521  521  ALA ALA A . n 
A 1 522  SER 522  522  522  SER SER A . n 
A 1 523  TYR 523  523  523  TYR TYR A . n 
A 1 524  GLN 524  524  524  GLN GLN A . n 
A 1 525  SER 525  525  525  SER SER A . n 
A 1 526  ILE 526  526  526  ILE ILE A . n 
A 1 527  ASN 527  527  527  ASN ASN A . n 
A 1 528  ILE 528  528  528  ILE ILE A . n 
A 1 529  PRO 529  529  529  PRO PRO A . n 
A 1 530  VAL 530  530  530  VAL VAL A . n 
A 1 531  THR 531  531  531  THR THR A . n 
A 1 532  GLN 532  532  532  GLN GLN A . n 
A 1 533  ASN 533  533  533  ASN ASN A . n 
A 1 534  MET 534  534  534  MET MET A . n 
A 1 535  VAL 535  535  535  VAL VAL A . n 
A 1 536  PRO 536  536  536  PRO PRO A . n 
A 1 537  SER 537  537  537  SER SER A . n 
A 1 538  SER 538  538  538  SER SER A . n 
A 1 539  ARG 539  539  539  ARG ARG A . n 
A 1 540  LEU 540  540  540  LEU LEU A . n 
A 1 541  LEU 541  541  541  LEU LEU A . n 
A 1 542  VAL 542  542  542  VAL VAL A . n 
A 1 543  TYR 543  543  543  TYR TYR A . n 
A 1 544  TYR 544  544  544  TYR TYR A . n 
A 1 545  ILE 545  545  545  ILE ILE A . n 
A 1 546  VAL 546  546  546  VAL VAL A . n 
A 1 547  THR 547  547  547  THR THR A . n 
A 1 548  GLY 548  548  548  GLY GLY A . n 
A 1 549  GLU 549  549  549  GLU GLU A . n 
A 1 550  GLN 550  550  550  GLN GLN A . n 
A 1 551  THR 551  551  551  THR THR A . n 
A 1 552  ALA 552  552  552  ALA ALA A . n 
A 1 553  GLU 553  553  553  GLU GLU A . n 
A 1 554  LEU 554  554  554  LEU LEU A . n 
A 1 555  VAL 555  555  555  VAL VAL A . n 
A 1 556  SER 556  556  556  SER SER A . n 
A 1 557  ASP 557  557  557  ASP ASP A . n 
A 1 558  SER 558  558  558  SER SER A . n 
A 1 559  VAL 559  559  559  VAL VAL A . n 
A 1 560  TRP 560  560  560  TRP TRP A . n 
A 1 561  LEU 561  561  561  LEU LEU A . n 
A 1 562  ASN 562  562  562  ASN ASN A . n 
A 1 563  ILE 563  563  563  ILE ILE A . n 
A 1 564  GLU 564  564  564  GLU GLU A . n 
A 1 565  GLU 565  565  565  GLU GLU A . n 
A 1 566  LYS 566  566  566  LYS LYS A . n 
A 1 567  CYS 567  567  567  CYS CYS A . n 
A 1 568  GLY 568  568  568  GLY GLY A . n 
A 1 569  ASN 569  569  569  ASN ASN A . n 
A 1 570  GLN 570  570  570  GLN GLN A . n 
A 1 571  LEU 571  571  571  LEU LEU A . n 
A 1 572  GLN 572  572  572  GLN GLN A . n 
A 1 573  VAL 573  573  573  VAL VAL A . n 
A 1 574  HIS 574  574  574  HIS HIS A . n 
A 1 575  LEU 575  575  575  LEU LEU A . n 
A 1 576  SER 576  576  576  SER SER A . n 
A 1 577  PRO 577  577  577  PRO PRO A . n 
A 1 578  ASP 578  578  578  ASP ASP A . n 
A 1 579  ALA 579  579  579  ALA ALA A . n 
A 1 580  ASP 580  580  580  ASP ASP A . n 
A 1 581  ALA 581  581  581  ALA ALA A . n 
A 1 582  TYR 582  582  582  TYR TYR A . n 
A 1 583  SER 583  583  583  SER SER A . n 
A 1 584  PRO 584  584  584  PRO PRO A . n 
A 1 585  GLY 585  585  585  GLY GLY A . n 
A 1 586  GLN 586  586  586  GLN GLN A . n 
A 1 587  THR 587  587  587  THR THR A . n 
A 1 588  VAL 588  588  588  VAL VAL A . n 
A 1 589  SER 589  589  589  SER SER A . n 
A 1 590  LEU 590  590  590  LEU LEU A . n 
A 1 591  ASN 591  591  591  ASN ASN A . n 
A 1 592  MET 592  592  592  MET MET A . n 
A 1 593  ALA 593  593  593  ALA ALA A . n 
A 1 594  THR 594  594  594  THR THR A . n 
A 1 595  GLY 595  595  595  GLY GLY A . n 
A 1 596  MET 596  596  596  MET MET A . n 
A 1 597  ASP 597  597  597  ASP ASP A . n 
A 1 598  SER 598  598  598  SER SER A . n 
A 1 599  TRP 599  599  599  TRP TRP A . n 
A 1 600  VAL 600  600  600  VAL VAL A . n 
A 1 601  ALA 601  601  601  ALA ALA A . n 
A 1 602  LEU 602  602  602  LEU LEU A . n 
A 1 603  ALA 603  603  603  ALA ALA A . n 
A 1 604  ALA 604  604  604  ALA ALA A . n 
A 1 605  VAL 605  605  605  VAL VAL A . n 
A 1 606  ASP 606  606  606  ASP ASP A . n 
A 1 607  SER 607  607  607  SER SER A . n 
A 1 608  ALA 608  608  608  ALA ALA A . n 
A 1 609  VAL 609  609  609  VAL VAL A . n 
A 1 610  TYR 610  610  610  TYR TYR A . n 
A 1 611  GLY 611  611  611  GLY GLY A . n 
A 1 612  VAL 612  612  612  VAL VAL A . n 
A 1 613  GLN 613  613  613  GLN GLN A . n 
A 1 614  ARG 614  614  614  ARG ARG A . n 
A 1 615  GLY 615  615  615  GLY GLY A . n 
A 1 616  ALA 616  616  616  ALA ALA A . n 
A 1 617  LYS 617  617  617  LYS LYS A . n 
A 1 618  LYS 618  618  618  LYS LYS A . n 
A 1 619  PRO 619  619  619  PRO PRO A . n 
A 1 620  LEU 620  620  620  LEU LEU A . n 
A 1 621  GLU 621  621  621  GLU GLU A . n 
A 1 622  ARG 622  622  622  ARG ARG A . n 
A 1 623  VAL 623  623  623  VAL VAL A . n 
A 1 624  PHE 624  624  624  PHE PHE A . n 
A 1 625  GLN 625  625  625  GLN GLN A . n 
A 1 626  PHE 626  626  626  PHE PHE A . n 
A 1 627  LEU 627  627  627  LEU LEU A . n 
A 1 628  GLU 628  628  628  GLU GLU A . n 
A 1 629  LYS 629  629  629  LYS LYS A . n 
A 1 630  SER 630  630  630  SER SER A . n 
A 1 631  ASP 631  631  631  ASP ASP A . n 
A 1 632  LEU 632  632  632  LEU LEU A . n 
A 1 633  GLY 633  633  633  GLY GLY A . n 
A 1 634  CYS 634  634  634  CYS CYS A . n 
A 1 635  GLY 635  635  635  GLY GLY A . n 
A 1 636  ALA 636  636  636  ALA ALA A . n 
A 1 637  GLY 637  637  637  GLY GLY A . n 
A 1 638  GLY 638  638  638  GLY GLY A . n 
A 1 639  GLY 639  639  639  GLY GLY A . n 
A 1 640  LEU 640  640  640  LEU LEU A . n 
A 1 641  ASN 641  641  641  ASN ASN A . n 
A 1 642  ASN 642  642  642  ASN ASN A . n 
A 1 643  ALA 643  643  643  ALA ALA A . n 
A 1 644  ASN 644  644  644  ASN ASN A . n 
A 1 645  VAL 645  645  645  VAL VAL A . n 
A 1 646  PHE 646  646  646  PHE PHE A . n 
A 1 647  HIS 647  647  647  HIS HIS A . n 
A 1 648  LEU 648  648  648  LEU LEU A . n 
A 1 649  ALA 649  649  649  ALA ALA A . n 
A 1 650  GLY 650  650  650  GLY GLY A . n 
A 1 651  LEU 651  651  651  LEU LEU A . n 
A 1 652  THR 652  652  652  THR THR A . n 
A 1 653  PHE 653  653  653  PHE PHE A . n 
A 1 654  LEU 654  654  654  LEU LEU A . n 
A 1 655  THR 655  655  655  THR THR A . n 
A 1 656  ASN 656  656  656  ASN ASN A . n 
A 1 657  ALA 657  657  657  ALA ALA A . n 
A 1 658  ASN 658  658  658  ASN ASN A . n 
A 1 659  ALA 659  659  659  ALA ALA A . n 
A 1 660  ASP 660  660  660  ASP ASP A . n 
A 1 661  ASP 661  661  661  ASP ASP A . n 
A 1 662  SER 662  662  662  SER SER A . n 
A 1 663  GLN 663  663  663  GLN GLN A . n 
A 1 664  GLU 664  664  664  GLU GLU A . n 
A 1 665  ASN 665  665  665  ASN ASN A . n 
A 1 666  ASP 666  666  666  ASP ASP A . n 
A 1 667  GLU 667  667  667  GLU GLU A . n 
A 1 668  PRO 668  668  668  PRO PRO A . n 
A 1 669  CYS 669  669  669  CYS CYS A . n 
A 1 670  LYS 670  670  670  LYS LYS A . n 
A 1 671  GLU 671  671  671  GLU GLU A . n 
A 1 672  ILE 672  672  672  ILE ILE A . n 
A 1 673  LEU 673  673  673  LEU LEU A . n 
A 1 674  ARG 674  674  ?    ?   ?   A . n 
A 1 675  PRO 675  675  ?    ?   ?   A . n 
A 1 676  ARG 676  676  ?    ?   ?   A . n 
A 1 677  ARG 677  677  ?    ?   ?   A . n 
A 1 678  THR 678  678  ?    ?   ?   A . n 
A 1 679  LEU 679  679  679  LEU LEU A . n 
A 1 680  GLN 680  680  680  GLN GLN A . n 
A 1 681  LYS 681  681  681  LYS LYS A . n 
A 1 682  LYS 682  682  682  LYS LYS A . n 
A 1 683  ILE 683  683  683  ILE ILE A . n 
A 1 684  GLU 684  684  684  GLU GLU A . n 
A 1 685  GLU 685  685  685  GLU GLU A . n 
A 1 686  ILE 686  686  686  ILE ILE A . n 
A 1 687  ALA 687  687  687  ALA ALA A . n 
A 1 688  ALA 688  688  688  ALA ALA A . n 
A 1 689  LYS 689  689  689  LYS LYS A . n 
A 1 690  TYR 690  690  690  TYR TYR A . n 
A 1 691  LYS 691  691  691  LYS LYS A . n 
A 1 692  HIS 692  692  692  HIS HIS A . n 
A 1 693  SER 693  693  693  SER SER A . n 
A 1 694  VAL 694  694  694  VAL VAL A . n 
A 1 695  VAL 695  695  695  VAL VAL A . n 
A 1 696  LYS 696  696  696  LYS LYS A . n 
A 1 697  LYS 697  697  697  LYS LYS A . n 
A 1 698  CYS 698  698  698  CYS CYS A . n 
A 1 699  CYS 699  699  699  CYS CYS A . n 
A 1 700  TYR 700  700  700  TYR TYR A . n 
A 1 701  ASP 701  701  701  ASP ASP A . n 
A 1 702  GLY 702  702  702  GLY GLY A . n 
A 1 703  ALA 703  703  703  ALA ALA A . n 
A 1 704  CYS 704  704  704  CYS CYS A . n 
A 1 705  VAL 705  705  705  VAL VAL A . n 
A 1 706  ASN 706  706  706  ASN ASN A . n 
A 1 707  ASN 707  707  707  ASN ASN A . n 
A 1 708  ASP 708  708  708  ASP ASP A . n 
A 1 709  GLU 709  709  709  GLU GLU A . n 
A 1 710  THR 710  710  710  THR THR A . n 
A 1 711  CYS 711  711  711  CYS CYS A . n 
A 1 712  GLU 712  712  712  GLU GLU A . n 
A 1 713  GLN 713  713  713  GLN GLN A . n 
A 1 714  ARG 714  714  714  ARG ARG A . n 
A 1 715  ALA 715  715  715  ALA ALA A . n 
A 1 716  ALA 716  716  716  ALA ALA A . n 
A 1 717  ARG 717  717  717  ARG ARG A . n 
A 1 718  ILE 718  718  718  ILE ILE A . n 
A 1 719  SER 719  719  719  SER SER A . n 
A 1 720  LEU 720  720  720  LEU LEU A . n 
A 1 721  GLY 721  721  721  GLY GLY A . n 
A 1 722  PRO 722  722  722  PRO PRO A . n 
A 1 723  ARG 723  723  723  ARG ARG A . n 
A 1 724  CYS 724  724  724  CYS CYS A . n 
A 1 725  ILE 725  725  725  ILE ILE A . n 
A 1 726  LYS 726  726  726  LYS LYS A . n 
A 1 727  ALA 727  727  727  ALA ALA A . n 
A 1 728  PHE 728  728  728  PHE PHE A . n 
A 1 729  THR 729  729  729  THR THR A . n 
A 1 730  GLU 730  730  730  GLU GLU A . n 
A 1 731  CYS 731  731  731  CYS CYS A . n 
A 1 732  CYS 732  732  732  CYS CYS A . n 
A 1 733  VAL 733  733  733  VAL VAL A . n 
A 1 734  VAL 734  734  734  VAL VAL A . n 
A 1 735  ALA 735  735  735  ALA ALA A . n 
A 1 736  SER 736  736  736  SER SER A . n 
A 1 737  GLN 737  737  737  GLN GLN A . n 
A 1 738  LEU 738  738  738  LEU LEU A . n 
A 1 739  ARG 739  739  739  ARG ARG A . n 
A 1 740  ALA 740  740  740  ALA ALA A . n 
A 1 741  ASN 741  741  741  ASN ASN A . n 
A 1 742  ILE 742  742  742  ILE ILE A . n 
A 1 743  SER 743  743  743  SER SER A . n 
A 1 744  HIS 744  744  ?    ?   ?   A . n 
A 1 745  LYS 745  745  ?    ?   ?   A . n 
A 1 746  ASP 746  746  ?    ?   ?   A . n 
A 1 747  MET 747  747  ?    ?   ?   A . n 
A 1 748  GLN 748  748  ?    ?   ?   A . n 
A 1 749  LEU 749  749  749  LEU LEU A . n 
A 1 750  GLY 750  750  750  GLY GLY A . n 
A 1 751  ARG 751  751  751  ARG ARG A . n 
A 1 752  LEU 752  752  752  LEU LEU A . n 
A 1 753  HIS 753  753  753  HIS HIS A . n 
A 1 754  MET 754  754  754  MET MET A . n 
A 1 755  LYS 755  755  755  LYS LYS A . n 
A 1 756  THR 756  756  756  THR THR A . n 
A 1 757  LEU 757  757  757  LEU LEU A . n 
A 1 758  LEU 758  758  758  LEU LEU A . n 
A 1 759  PRO 759  759  759  PRO PRO A . n 
A 1 760  VAL 760  760  760  VAL VAL A . n 
A 1 761  SER 761  761  761  SER SER A . n 
A 1 762  LYS 762  762  762  LYS LYS A . n 
A 1 763  PRO 763  763  763  PRO PRO A . n 
A 1 764  GLU 764  764  764  GLU GLU A . n 
A 1 765  ILE 765  765  765  ILE ILE A . n 
A 1 766  ARG 766  766  766  ARG ARG A . n 
A 1 767  SER 767  767  767  SER SER A . n 
A 1 768  TYR 768  768  768  TYR TYR A . n 
A 1 769  PHE 769  769  769  PHE PHE A . n 
A 1 770  PRO 770  770  770  PRO PRO A . n 
A 1 771  GLU 771  771  771  GLU GLU A . n 
A 1 772  SER 772  772  772  SER SER A . n 
A 1 773  TRP 773  773  773  TRP TRP A . n 
A 1 774  LEU 774  774  774  LEU LEU A . n 
A 1 775  TRP 775  775  775  TRP TRP A . n 
A 1 776  GLU 776  776  776  GLU GLU A . n 
A 1 777  VAL 777  777  777  VAL VAL A . n 
A 1 778  HIS 778  778  778  HIS HIS A . n 
A 1 779  LEU 779  779  779  LEU LEU A . n 
A 1 780  VAL 780  780  780  VAL VAL A . n 
A 1 781  PRO 781  781  781  PRO PRO A . n 
A 1 782  ARG 782  782  782  ARG ARG A . n 
A 1 783  ARG 783  783  783  ARG ARG A . n 
A 1 784  LYS 784  784  784  LYS LYS A . n 
A 1 785  GLN 785  785  785  GLN GLN A . n 
A 1 786  LEU 786  786  786  LEU LEU A . n 
A 1 787  GLN 787  787  787  GLN GLN A . n 
A 1 788  PHE 788  788  788  PHE PHE A . n 
A 1 789  ALA 789  789  789  ALA ALA A . n 
A 1 790  LEU 790  790  790  LEU LEU A . n 
A 1 791  PRO 791  791  791  PRO PRO A . n 
A 1 792  ASP 792  792  792  ASP ASP A . n 
A 1 793  SER 793  793  793  SER SER A . n 
A 1 794  LEU 794  794  794  LEU LEU A . n 
A 1 795  THR 795  795  795  THR THR A . n 
A 1 796  THR 796  796  796  THR THR A . n 
A 1 797  TRP 797  797  797  TRP TRP A . n 
A 1 798  GLU 798  798  798  GLU GLU A . n 
A 1 799  ILE 799  799  799  ILE ILE A . n 
A 1 800  GLN 800  800  800  GLN GLN A . n 
A 1 801  GLY 801  801  801  GLY GLY A . n 
A 1 802  ILE 802  802  802  ILE ILE A . n 
A 1 803  GLY 803  803  803  GLY GLY A . n 
A 1 804  ILE 804  804  804  ILE ILE A . n 
A 1 805  SER 805  805  805  SER SER A . n 
A 1 806  ASN 806  806  806  ASN ASN A . n 
A 1 807  THR 807  807  807  THR THR A . n 
A 1 808  GLY 808  808  808  GLY GLY A . n 
A 1 809  ILE 809  809  809  ILE ILE A . n 
A 1 810  CYS 810  810  810  CYS CYS A . n 
A 1 811  VAL 811  811  811  VAL VAL A . n 
A 1 812  ALA 812  812  812  ALA ALA A . n 
A 1 813  ASP 813  813  813  ASP ASP A . n 
A 1 814  THR 814  814  814  THR THR A . n 
A 1 815  VAL 815  815  815  VAL VAL A . n 
A 1 816  LYS 816  816  816  LYS LYS A . n 
A 1 817  ALA 817  817  817  ALA ALA A . n 
A 1 818  LYS 818  818  818  LYS LYS A . n 
A 1 819  VAL 819  819  819  VAL VAL A . n 
A 1 820  PHE 820  820  820  PHE PHE A . n 
A 1 821  LYS 821  821  821  LYS LYS A . n 
A 1 822  ASP 822  822  822  ASP ASP A . n 
A 1 823  VAL 823  823  823  VAL VAL A . n 
A 1 824  PHE 824  824  824  PHE PHE A . n 
A 1 825  LEU 825  825  825  LEU LEU A . n 
A 1 826  GLU 826  826  826  GLU GLU A . n 
A 1 827  MET 827  827  827  MET MET A . n 
A 1 828  ASN 828  828  828  ASN ASN A . n 
A 1 829  ILE 829  829  829  ILE ILE A . n 
A 1 830  PRO 830  830  830  PRO PRO A . n 
A 1 831  TYR 831  831  831  TYR TYR A . n 
A 1 832  SER 832  832  832  SER SER A . n 
A 1 833  VAL 833  833  833  VAL VAL A . n 
A 1 834  VAL 834  834  834  VAL VAL A . n 
A 1 835  ARG 835  835  835  ARG ARG A . n 
A 1 836  GLY 836  836  836  GLY GLY A . n 
A 1 837  GLU 837  837  837  GLU GLU A . n 
A 1 838  GLN 838  838  838  GLN GLN A . n 
A 1 839  ILE 839  839  839  ILE ILE A . n 
A 1 840  GLN 840  840  840  GLN GLN A . n 
A 1 841  LEU 841  841  841  LEU LEU A . n 
A 1 842  LYS 842  842  842  LYS LYS A . n 
A 1 843  GLY 843  843  843  GLY GLY A . n 
A 1 844  THR 844  844  844  THR THR A . n 
A 1 845  VAL 845  845  845  VAL VAL A . n 
A 1 846  TYR 846  846  846  TYR TYR A . n 
A 1 847  ASN 847  847  847  ASN ASN A . n 
A 1 848  TYR 848  848  848  TYR TYR A . n 
A 1 849  ARG 849  849  849  ARG ARG A . n 
A 1 850  THR 850  850  850  THR THR A . n 
A 1 851  SER 851  851  851  SER SER A . n 
A 1 852  GLY 852  852  852  GLY GLY A . n 
A 1 853  MET 853  853  853  MET MET A . n 
A 1 854  GLN 854  854  854  GLN GLN A . n 
A 1 855  PHE 855  855  855  PHE PHE A . n 
A 1 856  CYS 856  856  856  CYS CYS A . n 
A 1 857  VAL 857  857  857  VAL VAL A . n 
A 1 858  LYS 858  858  858  LYS LYS A . n 
A 1 859  MET 859  859  859  MET MET A . n 
A 1 860  SER 860  860  860  SER SER A . n 
A 1 861  ALA 861  861  861  ALA ALA A . n 
A 1 862  VAL 862  862  862  VAL VAL A . n 
A 1 863  GLU 863  863  863  GLU GLU A . n 
A 1 864  GLY 864  864  864  GLY GLY A . n 
A 1 865  ILE 865  865  865  ILE ILE A . n 
A 1 866  CYS 866  866  866  CYS CYS A . n 
A 1 867  THR 867  867  867  THR THR A . n 
A 1 868  SER 868  868  868  SER SER A . n 
A 1 869  GLU 869  869  869  GLU GLU A . n 
A 1 870  SER 870  870  870  SER SER A . n 
A 1 871  PRO 871  871  ?    ?   ?   A . n 
A 1 872  VAL 872  872  ?    ?   ?   A . n 
A 1 873  ILE 873  873  ?    ?   ?   A . n 
A 1 874  ASP 874  874  ?    ?   ?   A . n 
A 1 875  HIS 875  875  ?    ?   ?   A . n 
A 1 876  GLN 876  876  ?    ?   ?   A . n 
A 1 877  GLY 877  877  ?    ?   ?   A . n 
A 1 878  THR 878  878  ?    ?   ?   A . n 
A 1 879  LYS 879  879  ?    ?   ?   A . n 
A 1 880  SER 880  880  ?    ?   ?   A . n 
A 1 881  SER 881  881  ?    ?   ?   A . n 
A 1 882  LYS 882  882  882  LYS LYS A . n 
A 1 883  CYS 883  883  883  CYS CYS A . n 
A 1 884  VAL 884  884  884  VAL VAL A . n 
A 1 885  ARG 885  885  885  ARG ARG A . n 
A 1 886  GLN 886  886  886  GLN GLN A . n 
A 1 887  LYS 887  887  887  LYS LYS A . n 
A 1 888  VAL 888  888  888  VAL VAL A . n 
A 1 889  GLU 889  889  889  GLU GLU A . n 
A 1 890  GLY 890  890  890  GLY GLY A . n 
A 1 891  SER 891  891  891  SER SER A . n 
A 1 892  SER 892  892  892  SER SER A . n 
A 1 893  SER 893  893  893  SER SER A . n 
A 1 894  HIS 894  894  894  HIS HIS A . n 
A 1 895  LEU 895  895  895  LEU LEU A . n 
A 1 896  VAL 896  896  896  VAL VAL A . n 
A 1 897  THR 897  897  897  THR THR A . n 
A 1 898  PHE 898  898  898  PHE PHE A . n 
A 1 899  THR 899  899  899  THR THR A . n 
A 1 900  VAL 900  900  900  VAL VAL A . n 
A 1 901  LEU 901  901  901  LEU LEU A . n 
A 1 902  PRO 902  902  902  PRO PRO A . n 
A 1 903  LEU 903  903  903  LEU LEU A . n 
A 1 904  GLU 904  904  904  GLU GLU A . n 
A 1 905  ILE 905  905  905  ILE ILE A . n 
A 1 906  GLY 906  906  906  GLY GLY A . n 
A 1 907  LEU 907  907  907  LEU LEU A . n 
A 1 908  HIS 908  908  908  HIS HIS A . n 
A 1 909  ASN 909  909  909  ASN ASN A . n 
A 1 910  ILE 910  910  910  ILE ILE A . n 
A 1 911  ASN 911  911  911  ASN ASN A . n 
A 1 912  PHE 912  912  912  PHE PHE A . n 
A 1 913  SER 913  913  913  SER SER A . n 
A 1 914  LEU 914  914  914  LEU LEU A . n 
A 1 915  GLU 915  915  915  GLU GLU A . n 
A 1 916  THR 916  916  916  THR THR A . n 
A 1 917  TRP 917  917  917  TRP TRP A . n 
A 1 918  PHE 918  918  918  PHE PHE A . n 
A 1 919  GLY 919  919  919  GLY GLY A . n 
A 1 920  LYS 920  920  920  LYS LYS A . n 
A 1 921  GLU 921  921  921  GLU GLU A . n 
A 1 922  ILE 922  922  922  ILE ILE A . n 
A 1 923  LEU 923  923  923  LEU LEU A . n 
A 1 924  VAL 924  924  924  VAL VAL A . n 
A 1 925  LYS 925  925  925  LYS LYS A . n 
A 1 926  THR 926  926  926  THR THR A . n 
A 1 927  LEU 927  927  927  LEU LEU A . n 
A 1 928  ARG 928  928  928  ARG ARG A . n 
A 1 929  VAL 929  929  929  VAL VAL A . n 
A 1 930  VAL 930  930  930  VAL VAL A . n 
A 1 931  PRO 931  931  931  PRO PRO A . n 
A 1 932  GLU 932  932  932  GLU GLU A . n 
A 1 933  GLY 933  933  933  GLY GLY A . n 
A 1 934  VAL 934  934  934  VAL VAL A . n 
A 1 935  LYS 935  935  935  LYS LYS A . n 
A 1 936  ARG 936  936  936  ARG ARG A . n 
A 1 937  GLU 937  937  937  GLU GLU A . n 
A 1 938  SER 938  938  938  SER SER A . n 
A 1 939  TYR 939  939  939  TYR TYR A . n 
A 1 940  SER 940  940  940  SER SER A . n 
A 1 941  GLY 941  941  941  GLY GLY A . n 
A 1 942  VAL 942  942  942  VAL VAL A . n 
A 1 943  THR 943  943  943  THR THR A . n 
A 1 944  LEU 944  944  944  LEU LEU A . n 
A 1 945  ASP 945  945  945  ASP ASP A . n 
A 1 946  PRO 946  946  946  PRO PRO A . n 
A 1 947  ARG 947  947  947  ARG ARG A . n 
A 1 948  GLY 948  948  948  GLY GLY A . n 
A 1 949  ILE 949  949  949  ILE ILE A . n 
A 1 950  TYR 950  950  950  TYR TYR A . n 
A 1 951  GLY 951  951  951  GLY GLY A . n 
A 1 952  THR 952  952  952  THR THR A . n 
A 1 953  ILE 953  953  953  ILE ILE A . n 
A 1 954  SER 954  954  954  SER SER A . n 
A 1 955  ARG 955  955  955  ARG ARG A . n 
A 1 956  ARG 956  956  956  ARG ARG A . n 
A 1 957  LYS 957  957  957  LYS LYS A . n 
A 1 958  GLU 958  958  958  GLU GLU A . n 
A 1 959  PHE 959  959  959  PHE PHE A . n 
A 1 960  PRO 960  960  960  PRO PRO A . n 
A 1 961  TYR 961  961  961  TYR TYR A . n 
A 1 962  ARG 962  962  962  ARG ARG A . n 
A 1 963  ILE 963  963  963  ILE ILE A . n 
A 1 964  PRO 964  964  964  PRO PRO A . n 
A 1 965  LEU 965  965  965  LEU LEU A . n 
A 1 966  ASP 966  966  966  ASP ASP A . n 
A 1 967  LEU 967  967  967  LEU LEU A . n 
A 1 968  VAL 968  968  968  VAL VAL A . n 
A 1 969  PRO 969  969  969  PRO PRO A . n 
A 1 970  LYS 970  970  970  LYS LYS A . n 
A 1 971  THR 971  971  971  THR THR A . n 
A 1 972  GLU 972  972  972  GLU GLU A . n 
A 1 973  ILE 973  973  973  ILE ILE A . n 
A 1 974  LYS 974  974  974  LYS LYS A . n 
A 1 975  ARG 975  975  975  ARG ARG A . n 
A 1 976  ILE 976  976  976  ILE ILE A . n 
A 1 977  LEU 977  977  977  LEU LEU A . n 
A 1 978  SER 978  978  978  SER SER A . n 
A 1 979  VAL 979  979  979  VAL VAL A . n 
A 1 980  LYS 980  980  980  LYS LYS A . n 
A 1 981  GLY 981  981  981  GLY GLY A . n 
A 1 982  LEU 982  982  982  LEU LEU A . n 
A 1 983  LEU 983  983  983  LEU LEU A . n 
A 1 984  VAL 984  984  984  VAL VAL A . n 
A 1 985  GLY 985  985  985  GLY GLY A . n 
A 1 986  GLU 986  986  986  GLU GLU A . n 
A 1 987  ILE 987  987  987  ILE ILE A . n 
A 1 988  LEU 988  988  988  LEU LEU A . n 
A 1 989  SER 989  989  989  SER SER A . n 
A 1 990  ALA 990  990  990  ALA ALA A . n 
A 1 991  VAL 991  991  991  VAL VAL A . n 
A 1 992  LEU 992  992  992  LEU LEU A . n 
A 1 993  SER 993  993  993  SER SER A . n 
A 1 994  GLN 994  994  994  GLN GLN A . n 
A 1 995  GLU 995  995  995  GLU GLU A . n 
A 1 996  GLY 996  996  996  GLY GLY A . n 
A 1 997  ILE 997  997  997  ILE ILE A . n 
A 1 998  ASN 998  998  998  ASN ASN A . n 
A 1 999  ILE 999  999  999  ILE ILE A . n 
A 1 1000 LEU 1000 1000 1000 LEU LEU A . n 
A 1 1001 THR 1001 1001 1001 THR THR A . n 
A 1 1002 HIS 1002 1002 1002 HIS HIS A . n 
A 1 1003 LEU 1003 1003 1003 LEU LEU A . n 
A 1 1004 PRO 1004 1004 1004 PRO PRO A . n 
A 1 1005 LYS 1005 1005 1005 LYS LYS A . n 
A 1 1006 GLY 1006 1006 1006 GLY GLY A . n 
A 1 1007 SER 1007 1007 1007 SER SER A . n 
A 1 1008 ALA 1008 1008 1008 ALA ALA A . n 
A 1 1009 GLU 1009 1009 1009 GLU GLU A . n 
A 1 1010 ALA 1010 1010 1010 ALA ALA A . n 
A 1 1011 GLU 1011 1011 1011 GLU GLU A . n 
A 1 1012 LEU 1012 1012 1012 LEU LEU A . n 
A 1 1013 MET 1013 1013 1013 MET MET A . n 
A 1 1014 SER 1014 1014 1014 SER SER A . n 
A 1 1015 VAL 1015 1015 1015 VAL VAL A . n 
A 1 1016 VAL 1016 1016 1016 VAL VAL A . n 
A 1 1017 PRO 1017 1017 1017 PRO PRO A . n 
A 1 1018 VAL 1018 1018 1018 VAL VAL A . n 
A 1 1019 PHE 1019 1019 1019 PHE PHE A . n 
A 1 1020 TYR 1020 1020 1020 TYR TYR A . n 
A 1 1021 VAL 1021 1021 1021 VAL VAL A . n 
A 1 1022 PHE 1022 1022 1022 PHE PHE A . n 
A 1 1023 HIS 1023 1023 1023 HIS HIS A . n 
A 1 1024 TYR 1024 1024 1024 TYR TYR A . n 
A 1 1025 LEU 1025 1025 1025 LEU LEU A . n 
A 1 1026 GLU 1026 1026 1026 GLU GLU A . n 
A 1 1027 THR 1027 1027 1027 THR THR A . n 
A 1 1028 GLY 1028 1028 1028 GLY GLY A . n 
A 1 1029 ASN 1029 1029 1029 ASN ASN A . n 
A 1 1030 HIS 1030 1030 1030 HIS HIS A . n 
A 1 1031 TRP 1031 1031 1031 TRP TRP A . n 
A 1 1032 ASN 1032 1032 1032 ASN ASN A . n 
A 1 1033 ILE 1033 1033 1033 ILE ILE A . n 
A 1 1034 PHE 1034 1034 1034 PHE PHE A . n 
A 1 1035 HIS 1035 1035 1035 HIS HIS A . n 
A 1 1036 SER 1036 1036 1036 SER SER A . n 
A 1 1037 ASP 1037 1037 1037 ASP ASP A . n 
A 1 1038 PRO 1038 1038 1038 PRO PRO A . n 
A 1 1039 LEU 1039 1039 1039 LEU LEU A . n 
A 1 1040 ILE 1040 1040 1040 ILE ILE A . n 
A 1 1041 GLU 1041 1041 1041 GLU GLU A . n 
A 1 1042 LYS 1042 1042 1042 LYS LYS A . n 
A 1 1043 GLN 1043 1043 1043 GLN GLN A . n 
A 1 1044 LYS 1044 1044 1044 LYS LYS A . n 
A 1 1045 LEU 1045 1045 1045 LEU LEU A . n 
A 1 1046 LYS 1046 1046 1046 LYS LYS A . n 
A 1 1047 LYS 1047 1047 1047 LYS LYS A . n 
A 1 1048 LYS 1048 1048 1048 LYS LYS A . n 
A 1 1049 LEU 1049 1049 1049 LEU LEU A . n 
A 1 1050 LYS 1050 1050 1050 LYS LYS A . n 
A 1 1051 GLU 1051 1051 1051 GLU GLU A . n 
A 1 1052 GLY 1052 1052 1052 GLY GLY A . n 
A 1 1053 MET 1053 1053 1053 MET MET A . n 
A 1 1054 LEU 1054 1054 1054 LEU LEU A . n 
A 1 1055 SER 1055 1055 1055 SER SER A . n 
A 1 1056 ILE 1056 1056 1056 ILE ILE A . n 
A 1 1057 MET 1057 1057 1057 MET MET A . n 
A 1 1058 SER 1058 1058 1058 SER SER A . n 
A 1 1059 TYR 1059 1059 1059 TYR TYR A . n 
A 1 1060 ARG 1060 1060 1060 ARG ARG A . n 
A 1 1061 ASN 1061 1061 1061 ASN ASN A . n 
A 1 1062 ALA 1062 1062 1062 ALA ALA A . n 
A 1 1063 ASP 1063 1063 1063 ASP ASP A . n 
A 1 1064 TYR 1064 1064 1064 TYR TYR A . n 
A 1 1065 SER 1065 1065 1065 SER SER A . n 
A 1 1066 TYR 1066 1066 1066 TYR TYR A . n 
A 1 1067 SER 1067 1067 1067 SER SER A . n 
A 1 1068 VAL 1068 1068 1068 VAL VAL A . n 
A 1 1069 TRP 1069 1069 1069 TRP TRP A . n 
A 1 1070 LYS 1070 1070 1070 LYS LYS A . n 
A 1 1071 GLY 1071 1071 1071 GLY GLY A . n 
A 1 1072 GLY 1072 1072 1072 GLY GLY A . n 
A 1 1073 SER 1073 1073 1073 SER SER A . n 
A 1 1074 ALA 1074 1074 1074 ALA ALA A . n 
A 1 1075 SER 1075 1075 1075 SER SER A . n 
A 1 1076 THR 1076 1076 1076 THR THR A . n 
A 1 1077 TRP 1077 1077 1077 TRP TRP A . n 
A 1 1078 LEU 1078 1078 1078 LEU LEU A . n 
A 1 1079 THR 1079 1079 1079 THR THR A . n 
A 1 1080 ALA 1080 1080 1080 ALA ALA A . n 
A 1 1081 PHE 1081 1081 1081 PHE PHE A . n 
A 1 1082 ALA 1082 1082 1082 ALA ALA A . n 
A 1 1083 LEU 1083 1083 1083 LEU LEU A . n 
A 1 1084 ARG 1084 1084 1084 ARG ARG A . n 
A 1 1085 VAL 1085 1085 1085 VAL VAL A . n 
A 1 1086 LEU 1086 1086 1086 LEU LEU A . n 
A 1 1087 GLY 1087 1087 1087 GLY GLY A . n 
A 1 1088 GLN 1088 1088 1088 GLN GLN A . n 
A 1 1089 VAL 1089 1089 1089 VAL VAL A . n 
A 1 1090 ASN 1090 1090 1090 ASN ASN A . n 
A 1 1091 LYS 1091 1091 1091 LYS LYS A . n 
A 1 1092 TYR 1092 1092 1092 TYR TYR A . n 
A 1 1093 VAL 1093 1093 1093 VAL VAL A . n 
A 1 1094 GLU 1094 1094 1094 GLU GLU A . n 
A 1 1095 GLN 1095 1095 1095 GLN GLN A . n 
A 1 1096 ASN 1096 1096 1096 ASN ASN A . n 
A 1 1097 GLN 1097 1097 1097 GLN GLN A . n 
A 1 1098 ASN 1098 1098 1098 ASN ASN A . n 
A 1 1099 SER 1099 1099 1099 SER SER A . n 
A 1 1100 ILE 1100 1100 1100 ILE ILE A . n 
A 1 1101 CYS 1101 1101 1101 CYS CYS A . n 
A 1 1102 ASN 1102 1102 1102 ASN ASN A . n 
A 1 1103 SER 1103 1103 1103 SER SER A . n 
A 1 1104 LEU 1104 1104 1104 LEU LEU A . n 
A 1 1105 LEU 1105 1105 1105 LEU LEU A . n 
A 1 1106 TRP 1106 1106 1106 TRP TRP A . n 
A 1 1107 LEU 1107 1107 1107 LEU LEU A . n 
A 1 1108 VAL 1108 1108 1108 VAL VAL A . n 
A 1 1109 GLU 1109 1109 1109 GLU GLU A . n 
A 1 1110 ASN 1110 1110 1110 ASN ASN A . n 
A 1 1111 TYR 1111 1111 1111 TYR TYR A . n 
A 1 1112 GLN 1112 1112 1112 GLN GLN A . n 
A 1 1113 LEU 1113 1113 1113 LEU LEU A . n 
A 1 1114 ASP 1114 1114 1114 ASP ASP A . n 
A 1 1115 ASN 1115 1115 1115 ASN ASN A . n 
A 1 1116 GLY 1116 1116 1116 GLY GLY A . n 
A 1 1117 SER 1117 1117 1117 SER SER A . n 
A 1 1118 PHE 1118 1118 1118 PHE PHE A . n 
A 1 1119 LYS 1119 1119 1119 LYS LYS A . n 
A 1 1120 GLU 1120 1120 1120 GLU GLU A . n 
A 1 1121 ASN 1121 1121 1121 ASN ASN A . n 
A 1 1122 SER 1122 1122 1122 SER SER A . n 
A 1 1123 GLN 1123 1123 1123 GLN GLN A . n 
A 1 1124 TYR 1124 1124 1124 TYR TYR A . n 
A 1 1125 GLN 1125 1125 1125 GLN GLN A . n 
A 1 1126 PRO 1126 1126 1126 PRO PRO A . n 
A 1 1127 ILE 1127 1127 1127 ILE ILE A . n 
A 1 1128 LYS 1128 1128 1128 LYS LYS A . n 
A 1 1129 LEU 1129 1129 1129 LEU LEU A . n 
A 1 1130 GLN 1130 1130 1130 GLN GLN A . n 
A 1 1131 GLY 1131 1131 1131 GLY GLY A . n 
A 1 1132 THR 1132 1132 1132 THR THR A . n 
A 1 1133 LEU 1133 1133 1133 LEU LEU A . n 
A 1 1134 PRO 1134 1134 1134 PRO PRO A . n 
A 1 1135 VAL 1135 1135 1135 VAL VAL A . n 
A 1 1136 GLU 1136 1136 1136 GLU GLU A . n 
A 1 1137 ALA 1137 1137 1137 ALA ALA A . n 
A 1 1138 ARG 1138 1138 1138 ARG ARG A . n 
A 1 1139 GLU 1139 1139 1139 GLU GLU A . n 
A 1 1140 ASN 1140 1140 1140 ASN ASN A . n 
A 1 1141 SER 1141 1141 1141 SER SER A . n 
A 1 1142 LEU 1142 1142 1142 LEU LEU A . n 
A 1 1143 TYR 1143 1143 1143 TYR TYR A . n 
A 1 1144 LEU 1144 1144 1144 LEU LEU A . n 
A 1 1145 THR 1145 1145 1145 THR THR A . n 
A 1 1146 ALA 1146 1146 1146 ALA ALA A . n 
A 1 1147 PHE 1147 1147 1147 PHE PHE A . n 
A 1 1148 THR 1148 1148 1148 THR THR A . n 
A 1 1149 VAL 1149 1149 1149 VAL VAL A . n 
A 1 1150 ILE 1150 1150 1150 ILE ILE A . n 
A 1 1151 GLY 1151 1151 1151 GLY GLY A . n 
A 1 1152 ILE 1152 1152 1152 ILE ILE A . n 
A 1 1153 ARG 1153 1153 1153 ARG ARG A . n 
A 1 1154 LYS 1154 1154 1154 LYS LYS A . n 
A 1 1155 ALA 1155 1155 1155 ALA ALA A . n 
A 1 1156 PHE 1156 1156 1156 PHE PHE A . n 
A 1 1157 ASP 1157 1157 1157 ASP ASP A . n 
A 1 1158 ILE 1158 1158 1158 ILE ILE A . n 
A 1 1159 CYS 1159 1159 1159 CYS CYS A . n 
A 1 1160 PRO 1160 1160 1160 PRO PRO A . n 
A 1 1161 LEU 1161 1161 1161 LEU LEU A . n 
A 1 1162 VAL 1162 1162 1162 VAL VAL A . n 
A 1 1163 LYS 1163 1163 1163 LYS LYS A . n 
A 1 1164 ILE 1164 1164 1164 ILE ILE A . n 
A 1 1165 ASP 1165 1165 1165 ASP ASP A . n 
A 1 1166 THR 1166 1166 1166 THR THR A . n 
A 1 1167 ALA 1167 1167 1167 ALA ALA A . n 
A 1 1168 LEU 1168 1168 1168 LEU LEU A . n 
A 1 1169 ILE 1169 1169 1169 ILE ILE A . n 
A 1 1170 LYS 1170 1170 1170 LYS LYS A . n 
A 1 1171 ALA 1171 1171 1171 ALA ALA A . n 
A 1 1172 ASP 1172 1172 1172 ASP ASP A . n 
A 1 1173 ASN 1173 1173 1173 ASN ASN A . n 
A 1 1174 PHE 1174 1174 1174 PHE PHE A . n 
A 1 1175 LEU 1175 1175 1175 LEU LEU A . n 
A 1 1176 LEU 1176 1176 1176 LEU LEU A . n 
A 1 1177 GLU 1177 1177 1177 GLU GLU A . n 
A 1 1178 ASN 1178 1178 1178 ASN ASN A . n 
A 1 1179 THR 1179 1179 1179 THR THR A . n 
A 1 1180 LEU 1180 1180 1180 LEU LEU A . n 
A 1 1181 PRO 1181 1181 1181 PRO PRO A . n 
A 1 1182 ALA 1182 1182 1182 ALA ALA A . n 
A 1 1183 GLN 1183 1183 1183 GLN GLN A . n 
A 1 1184 SER 1184 1184 1184 SER SER A . n 
A 1 1185 THR 1185 1185 1185 THR THR A . n 
A 1 1186 PHE 1186 1186 1186 PHE PHE A . n 
A 1 1187 THR 1187 1187 1187 THR THR A . n 
A 1 1188 LEU 1188 1188 1188 LEU LEU A . n 
A 1 1189 ALA 1189 1189 1189 ALA ALA A . n 
A 1 1190 ILE 1190 1190 1190 ILE ILE A . n 
A 1 1191 SER 1191 1191 1191 SER SER A . n 
A 1 1192 ALA 1192 1192 1192 ALA ALA A . n 
A 1 1193 TYR 1193 1193 1193 TYR TYR A . n 
A 1 1194 ALA 1194 1194 1194 ALA ALA A . n 
A 1 1195 LEU 1195 1195 1195 LEU LEU A . n 
A 1 1196 SER 1196 1196 1196 SER SER A . n 
A 1 1197 LEU 1197 1197 1197 LEU LEU A . n 
A 1 1198 GLY 1198 1198 1198 GLY GLY A . n 
A 1 1199 ASP 1199 1199 1199 ASP ASP A . n 
A 1 1200 LYS 1200 1200 1200 LYS LYS A . n 
A 1 1201 THR 1201 1201 1201 THR THR A . n 
A 1 1202 HIS 1202 1202 1202 HIS HIS A . n 
A 1 1203 PRO 1203 1203 1203 PRO PRO A . n 
A 1 1204 GLN 1204 1204 1204 GLN GLN A . n 
A 1 1205 PHE 1205 1205 1205 PHE PHE A . n 
A 1 1206 ARG 1206 1206 1206 ARG ARG A . n 
A 1 1207 SER 1207 1207 1207 SER SER A . n 
A 1 1208 ILE 1208 1208 1208 ILE ILE A . n 
A 1 1209 VAL 1209 1209 1209 VAL VAL A . n 
A 1 1210 SER 1210 1210 1210 SER SER A . n 
A 1 1211 ALA 1211 1211 1211 ALA ALA A . n 
A 1 1212 LEU 1212 1212 1212 LEU LEU A . n 
A 1 1213 LYS 1213 1213 1213 LYS LYS A . n 
A 1 1214 ARG 1214 1214 1214 ARG ARG A . n 
A 1 1215 GLU 1215 1215 1215 GLU GLU A . n 
A 1 1216 ALA 1216 1216 1216 ALA ALA A . n 
A 1 1217 LEU 1217 1217 1217 LEU LEU A . n 
A 1 1218 VAL 1218 1218 1218 VAL VAL A . n 
A 1 1219 LYS 1219 1219 1219 LYS LYS A . n 
A 1 1220 GLY 1220 1220 1220 GLY GLY A . n 
A 1 1221 ASN 1221 1221 1221 ASN ASN A . n 
A 1 1222 PRO 1222 1222 1222 PRO PRO A . n 
A 1 1223 PRO 1223 1223 1223 PRO PRO A . n 
A 1 1224 ILE 1224 1224 1224 ILE ILE A . n 
A 1 1225 TYR 1225 1225 1225 TYR TYR A . n 
A 1 1226 ARG 1226 1226 1226 ARG ARG A . n 
A 1 1227 PHE 1227 1227 1227 PHE PHE A . n 
A 1 1228 TRP 1228 1228 1228 TRP TRP A . n 
A 1 1229 LYS 1229 1229 1229 LYS LYS A . n 
A 1 1230 ASP 1230 1230 1230 ASP ASP A . n 
A 1 1231 ASN 1231 1231 1231 ASN ASN A . n 
A 1 1232 LEU 1232 1232 1232 LEU LEU A . n 
A 1 1233 GLN 1233 1233 1233 GLN GLN A . n 
A 1 1234 HIS 1234 1234 1234 HIS HIS A . n 
A 1 1235 LYS 1235 1235 1235 LYS LYS A . n 
A 1 1236 ASP 1236 1236 1236 ASP ASP A . n 
A 1 1237 SER 1237 1237 1237 SER SER A . n 
A 1 1238 SER 1238 1238 1238 SER SER A . n 
A 1 1239 VAL 1239 1239 1239 VAL VAL A . n 
A 1 1240 PRO 1240 1240 1240 PRO PRO A . n 
A 1 1241 ASN 1241 1241 1241 ASN ASN A . n 
A 1 1242 THR 1242 1242 1242 THR THR A . n 
A 1 1243 GLY 1243 1243 1243 GLY GLY A . n 
A 1 1244 THR 1244 1244 1244 THR THR A . n 
A 1 1245 ALA 1245 1245 1245 ALA ALA A . n 
A 1 1246 ARG 1246 1246 1246 ARG ARG A . n 
A 1 1247 MET 1247 1247 1247 MET MET A . n 
A 1 1248 VAL 1248 1248 1248 VAL VAL A . n 
A 1 1249 GLU 1249 1249 1249 GLU GLU A . n 
A 1 1250 THR 1250 1250 1250 THR THR A . n 
A 1 1251 THR 1251 1251 1251 THR THR A . n 
A 1 1252 ALA 1252 1252 1252 ALA ALA A . n 
A 1 1253 TYR 1253 1253 1253 TYR TYR A . n 
A 1 1254 ALA 1254 1254 1254 ALA ALA A . n 
A 1 1255 LEU 1255 1255 1255 LEU LEU A . n 
A 1 1256 LEU 1256 1256 1256 LEU LEU A . n 
A 1 1257 THR 1257 1257 1257 THR THR A . n 
A 1 1258 SER 1258 1258 1258 SER SER A . n 
A 1 1259 LEU 1259 1259 1259 LEU LEU A . n 
A 1 1260 ASN 1260 1260 1260 ASN ASN A . n 
A 1 1261 LEU 1261 1261 1261 LEU LEU A . n 
A 1 1262 LYS 1262 1262 1262 LYS LYS A . n 
A 1 1263 ASP 1263 1263 1263 ASP ASP A . n 
A 1 1264 ILE 1264 1264 1264 ILE ILE A . n 
A 1 1265 ASN 1265 1265 1265 ASN ASN A . n 
A 1 1266 TYR 1266 1266 1266 TYR TYR A . n 
A 1 1267 VAL 1267 1267 1267 VAL VAL A . n 
A 1 1268 ASN 1268 1268 1268 ASN ASN A . n 
A 1 1269 PRO 1269 1269 1269 PRO PRO A . n 
A 1 1270 VAL 1270 1270 1270 VAL VAL A . n 
A 1 1271 ILE 1271 1271 1271 ILE ILE A . n 
A 1 1272 LYS 1272 1272 1272 LYS LYS A . n 
A 1 1273 TRP 1273 1273 1273 TRP TRP A . n 
A 1 1274 LEU 1274 1274 1274 LEU LEU A . n 
A 1 1275 SER 1275 1275 1275 SER SER A . n 
A 1 1276 GLU 1276 1276 1276 GLU GLU A . n 
A 1 1277 GLU 1277 1277 1277 GLU GLU A . n 
A 1 1278 GLN 1278 1278 1278 GLN GLN A . n 
A 1 1279 ARG 1279 1279 1279 ARG ARG A . n 
A 1 1280 TYR 1280 1280 1280 TYR TYR A . n 
A 1 1281 GLY 1281 1281 1281 GLY GLY A . n 
A 1 1282 GLY 1282 1282 1282 GLY GLY A . n 
A 1 1283 GLY 1283 1283 1283 GLY GLY A . n 
A 1 1284 PHE 1284 1284 1284 PHE PHE A . n 
A 1 1285 TYR 1285 1285 1285 TYR TYR A . n 
A 1 1286 SER 1286 1286 1286 SER SER A . n 
A 1 1287 THR 1287 1287 1287 THR THR A . n 
A 1 1288 GLN 1288 1288 1288 GLN GLN A . n 
A 1 1289 ASP 1289 1289 1289 ASP ASP A . n 
A 1 1290 THR 1290 1290 1290 THR THR A . n 
A 1 1291 ILE 1291 1291 1291 ILE ILE A . n 
A 1 1292 ASN 1292 1292 1292 ASN ASN A . n 
A 1 1293 ALA 1293 1293 1293 ALA ALA A . n 
A 1 1294 ILE 1294 1294 1294 ILE ILE A . n 
A 1 1295 GLU 1295 1295 1295 GLU GLU A . n 
A 1 1296 GLY 1296 1296 1296 GLY GLY A . n 
A 1 1297 LEU 1297 1297 1297 LEU LEU A . n 
A 1 1298 THR 1298 1298 1298 THR THR A . n 
A 1 1299 GLU 1299 1299 1299 GLU GLU A . n 
A 1 1300 TYR 1300 1300 1300 TYR TYR A . n 
A 1 1301 SER 1301 1301 1301 SER SER A . n 
A 1 1302 LEU 1302 1302 1302 LEU LEU A . n 
A 1 1303 LEU 1303 1303 1303 LEU LEU A . n 
A 1 1304 VAL 1304 1304 1304 VAL VAL A . n 
A 1 1305 LYS 1305 1305 1305 LYS LYS A . n 
A 1 1306 GLN 1306 1306 1306 GLN GLN A . n 
A 1 1307 LEU 1307 1307 1307 LEU LEU A . n 
A 1 1308 ARG 1308 1308 1308 ARG ARG A . n 
A 1 1309 LEU 1309 1309 1309 LEU LEU A . n 
A 1 1310 SER 1310 1310 1310 SER SER A . n 
A 1 1311 MET 1311 1311 1311 MET MET A . n 
A 1 1312 ASP 1312 1312 1312 ASP ASP A . n 
A 1 1313 ILE 1313 1313 1313 ILE ILE A . n 
A 1 1314 ASP 1314 1314 1314 ASP ASP A . n 
A 1 1315 VAL 1315 1315 1315 VAL VAL A . n 
A 1 1316 SER 1316 1316 1316 SER SER A . n 
A 1 1317 TYR 1317 1317 1317 TYR TYR A . n 
A 1 1318 LYS 1318 1318 1318 LYS LYS A . n 
A 1 1319 HIS 1319 1319 1319 HIS HIS A . n 
A 1 1320 LYS 1320 1320 1320 LYS LYS A . n 
A 1 1321 GLY 1321 1321 1321 GLY GLY A . n 
A 1 1322 ALA 1322 1322 1322 ALA ALA A . n 
A 1 1323 LEU 1323 1323 1323 LEU LEU A . n 
A 1 1324 HIS 1324 1324 1324 HIS HIS A . n 
A 1 1325 ASN 1325 1325 1325 ASN ASN A . n 
A 1 1326 TYR 1326 1326 1326 TYR TYR A . n 
A 1 1327 LYS 1327 1327 1327 LYS LYS A . n 
A 1 1328 MET 1328 1328 1328 MET MET A . n 
A 1 1329 THR 1329 1329 1329 THR THR A . n 
A 1 1330 ASP 1330 1330 1330 ASP ASP A . n 
A 1 1331 LYS 1331 1331 1331 LYS LYS A . n 
A 1 1332 ASN 1332 1332 1332 ASN ASN A . n 
A 1 1333 PHE 1333 1333 1333 PHE PHE A . n 
A 1 1334 LEU 1334 1334 1334 LEU LEU A . n 
A 1 1335 GLY 1335 1335 1335 GLY GLY A . n 
A 1 1336 ARG 1336 1336 1336 ARG ARG A . n 
A 1 1337 PRO 1337 1337 1337 PRO PRO A . n 
A 1 1338 VAL 1338 1338 1338 VAL VAL A . n 
A 1 1339 GLU 1339 1339 1339 GLU GLU A . n 
A 1 1340 VAL 1340 1340 1340 VAL VAL A . n 
A 1 1341 LEU 1341 1341 1341 LEU LEU A . n 
A 1 1342 LEU 1342 1342 1342 LEU LEU A . n 
A 1 1343 ASN 1343 1343 1343 ASN ASN A . n 
A 1 1344 ASP 1344 1344 1344 ASP ASP A . n 
A 1 1345 ASP 1345 1345 1345 ASP ASP A . n 
A 1 1346 LEU 1346 1346 1346 LEU LEU A . n 
A 1 1347 ILE 1347 1347 1347 ILE ILE A . n 
A 1 1348 VAL 1348 1348 1348 VAL VAL A . n 
A 1 1349 SER 1349 1349 1349 SER SER A . n 
A 1 1350 THR 1350 1350 1350 THR THR A . n 
A 1 1351 GLY 1351 1351 1351 GLY GLY A . n 
A 1 1352 PHE 1352 1352 1352 PHE PHE A . n 
A 1 1353 GLY 1353 1353 1353 GLY GLY A . n 
A 1 1354 SER 1354 1354 1354 SER SER A . n 
A 1 1355 GLY 1355 1355 1355 GLY GLY A . n 
A 1 1356 LEU 1356 1356 1356 LEU LEU A . n 
A 1 1357 ALA 1357 1357 1357 ALA ALA A . n 
A 1 1358 THR 1358 1358 1358 THR THR A . n 
A 1 1359 VAL 1359 1359 1359 VAL VAL A . n 
A 1 1360 HIS 1360 1360 1360 HIS HIS A . n 
A 1 1361 VAL 1361 1361 1361 VAL VAL A . n 
A 1 1362 THR 1362 1362 1362 THR THR A . n 
A 1 1363 THR 1363 1363 1363 THR THR A . n 
A 1 1364 VAL 1364 1364 1364 VAL VAL A . n 
A 1 1365 VAL 1365 1365 1365 VAL VAL A . n 
A 1 1366 HIS 1366 1366 1366 HIS HIS A . n 
A 1 1367 LYS 1367 1367 1367 LYS LYS A . n 
A 1 1368 THR 1368 1368 1368 THR THR A . n 
A 1 1369 SER 1369 1369 1369 SER SER A . n 
A 1 1370 THR 1370 1370 1370 THR THR A . n 
A 1 1371 SER 1371 1371 1371 SER SER A . n 
A 1 1372 GLU 1372 1372 1372 GLU GLU A . n 
A 1 1373 GLU 1373 1373 1373 GLU GLU A . n 
A 1 1374 VAL 1374 1374 1374 VAL VAL A . n 
A 1 1375 CYS 1375 1375 1375 CYS CYS A . n 
A 1 1376 SER 1376 1376 1376 SER SER A . n 
A 1 1377 PHE 1377 1377 1377 PHE PHE A . n 
A 1 1378 TYR 1378 1378 1378 TYR TYR A . n 
A 1 1379 LEU 1379 1379 1379 LEU LEU A . n 
A 1 1380 LYS 1380 1380 1380 LYS LYS A . n 
A 1 1381 ILE 1381 1381 1381 ILE ILE A . n 
A 1 1382 ASP 1382 1382 1382 ASP ASP A . n 
A 1 1383 THR 1383 1383 1383 THR THR A . n 
A 1 1384 GLN 1384 1384 1384 GLN GLN A . n 
A 1 1385 ASP 1385 1385 1385 ASP ASP A . n 
A 1 1386 ILE 1386 1386 1386 ILE ILE A . n 
A 1 1387 GLU 1387 1387 ?    ?   ?   A . n 
A 1 1388 ALA 1388 1388 ?    ?   ?   A . n 
A 1 1389 SER 1389 1389 ?    ?   ?   A . n 
A 1 1390 HIS 1390 1390 ?    ?   ?   A . n 
A 1 1391 TYR 1391 1391 ?    ?   ?   A . n 
A 1 1392 ARG 1392 1392 ?    ?   ?   A . n 
A 1 1393 GLY 1393 1393 ?    ?   ?   A . n 
A 1 1394 TYR 1394 1394 ?    ?   ?   A . n 
A 1 1395 GLY 1395 1395 ?    ?   ?   A . n 
A 1 1396 ASN 1396 1396 ?    ?   ?   A . n 
A 1 1397 SER 1397 1397 ?    ?   ?   A . n 
A 1 1398 ASP 1398 1398 ?    ?   ?   A . n 
A 1 1399 TYR 1399 1399 1399 TYR TYR A . n 
A 1 1400 LYS 1400 1400 1400 LYS LYS A . n 
A 1 1401 ARG 1401 1401 1401 ARG ARG A . n 
A 1 1402 ILE 1402 1402 1402 ILE ILE A . n 
A 1 1403 VAL 1403 1403 1403 VAL VAL A . n 
A 1 1404 ALA 1404 1404 1404 ALA ALA A . n 
A 1 1405 CYS 1405 1405 1405 CYS CYS A . n 
A 1 1406 ALA 1406 1406 1406 ALA ALA A . n 
A 1 1407 SER 1407 1407 1407 SER SER A . n 
A 1 1408 TYR 1408 1408 1408 TYR TYR A . n 
A 1 1409 LYS 1409 1409 1409 LYS LYS A . n 
A 1 1410 PRO 1410 1410 1410 PRO PRO A . n 
A 1 1411 SER 1411 1411 1411 SER SER A . n 
A 1 1412 ARG 1412 1412 1412 ARG ARG A . n 
A 1 1413 GLU 1413 1413 1413 GLU GLU A . n 
A 1 1414 GLU 1414 1414 1414 GLU GLU A . n 
A 1 1415 SER 1415 1415 1415 SER SER A . n 
A 1 1416 SER 1416 1416 1416 SER SER A . n 
A 1 1417 SER 1417 1417 1417 SER SER A . n 
A 1 1418 GLY 1418 1418 1418 GLY GLY A . n 
A 1 1419 SER 1419 1419 1419 SER SER A . n 
A 1 1420 SER 1420 1420 1420 SER SER A . n 
A 1 1421 HIS 1421 1421 1421 HIS HIS A . n 
A 1 1422 ALA 1422 1422 1422 ALA ALA A . n 
A 1 1423 VAL 1423 1423 1423 VAL VAL A . n 
A 1 1424 MET 1424 1424 1424 MET MET A . n 
A 1 1425 ASP 1425 1425 1425 ASP ASP A . n 
A 1 1426 ILE 1426 1426 1426 ILE ILE A . n 
A 1 1427 SER 1427 1427 1427 SER SER A . n 
A 1 1428 LEU 1428 1428 1428 LEU LEU A . n 
A 1 1429 PRO 1429 1429 1429 PRO PRO A . n 
A 1 1430 THR 1430 1430 1430 THR THR A . n 
A 1 1431 GLY 1431 1431 1431 GLY GLY A . n 
A 1 1432 ILE 1432 1432 1432 ILE ILE A . n 
A 1 1433 SER 1433 1433 1433 SER SER A . n 
A 1 1434 ALA 1434 1434 1434 ALA ALA A . n 
A 1 1435 ASN 1435 1435 1435 ASN ASN A . n 
A 1 1436 GLU 1436 1436 1436 GLU GLU A . n 
A 1 1437 GLU 1437 1437 1437 GLU GLU A . n 
A 1 1438 ASP 1438 1438 1438 ASP ASP A . n 
A 1 1439 LEU 1439 1439 1439 LEU LEU A . n 
A 1 1440 LYS 1440 1440 1440 LYS LYS A . n 
A 1 1441 ALA 1441 1441 1441 ALA ALA A . n 
A 1 1442 LEU 1442 1442 1442 LEU LEU A . n 
A 1 1443 VAL 1443 1443 1443 VAL VAL A . n 
A 1 1444 GLU 1444 1444 1444 GLU GLU A . n 
A 1 1445 GLY 1445 1445 1445 GLY GLY A . n 
A 1 1446 VAL 1446 1446 1446 VAL VAL A . n 
A 1 1447 ASP 1447 1447 1447 ASP ASP A . n 
A 1 1448 GLN 1448 1448 1448 GLN GLN A . n 
A 1 1449 LEU 1449 1449 1449 LEU LEU A . n 
A 1 1450 PHE 1450 1450 1450 PHE PHE A . n 
A 1 1451 THR 1451 1451 1451 THR THR A . n 
A 1 1452 ASP 1452 1452 1452 ASP ASP A . n 
A 1 1453 TYR 1453 1453 1453 TYR TYR A . n 
A 1 1454 GLN 1454 1454 1454 GLN GLN A . n 
A 1 1455 ILE 1455 1455 1455 ILE ILE A . n 
A 1 1456 LYS 1456 1456 1456 LYS LYS A . n 
A 1 1457 ASP 1457 1457 1457 ASP ASP A . n 
A 1 1458 GLY 1458 1458 1458 GLY GLY A . n 
A 1 1459 HIS 1459 1459 1459 HIS HIS A . n 
A 1 1460 VAL 1460 1460 1460 VAL VAL A . n 
A 1 1461 ILE 1461 1461 1461 ILE ILE A . n 
A 1 1462 LEU 1462 1462 1462 LEU LEU A . n 
A 1 1463 GLN 1463 1463 1463 GLN GLN A . n 
A 1 1464 LEU 1464 1464 1464 LEU LEU A . n 
A 1 1465 ASN 1465 1465 1465 ASN ASN A . n 
A 1 1466 SER 1466 1466 1466 SER SER A . n 
A 1 1467 ILE 1467 1467 1467 ILE ILE A . n 
A 1 1468 PRO 1468 1468 1468 PRO PRO A . n 
A 1 1469 SER 1469 1469 1469 SER SER A . n 
A 1 1470 SER 1470 1470 1470 SER SER A . n 
A 1 1471 ASP 1471 1471 1471 ASP ASP A . n 
A 1 1472 PHE 1472 1472 1472 PHE PHE A . n 
A 1 1473 LEU 1473 1473 1473 LEU LEU A . n 
A 1 1474 CYS 1474 1474 1474 CYS CYS A . n 
A 1 1475 VAL 1475 1475 1475 VAL VAL A . n 
A 1 1476 ARG 1476 1476 1476 ARG ARG A . n 
A 1 1477 PHE 1477 1477 1477 PHE PHE A . n 
A 1 1478 ARG 1478 1478 1478 ARG ARG A . n 
A 1 1479 ILE 1479 1479 1479 ILE ILE A . n 
A 1 1480 PHE 1480 1480 1480 PHE PHE A . n 
A 1 1481 GLU 1481 1481 1481 GLU GLU A . n 
A 1 1482 LEU 1482 1482 1482 LEU LEU A . n 
A 1 1483 PHE 1483 1483 1483 PHE PHE A . n 
A 1 1484 GLU 1484 1484 1484 GLU GLU A . n 
A 1 1485 VAL 1485 1485 1485 VAL VAL A . n 
A 1 1486 GLY 1486 1486 1486 GLY GLY A . n 
A 1 1487 PHE 1487 1487 1487 PHE PHE A . n 
A 1 1488 LEU 1488 1488 1488 LEU LEU A . n 
A 1 1489 SER 1489 1489 1489 SER SER A . n 
A 1 1490 PRO 1490 1490 1490 PRO PRO A . n 
A 1 1491 ALA 1491 1491 1491 ALA ALA A . n 
A 1 1492 THR 1492 1492 1492 THR THR A . n 
A 1 1493 PHE 1493 1493 1493 PHE PHE A . n 
A 1 1494 THR 1494 1494 1494 THR THR A . n 
A 1 1495 VAL 1495 1495 1495 VAL VAL A . n 
A 1 1496 TYR 1496 1496 1496 TYR TYR A . n 
A 1 1497 GLU 1497 1497 1497 GLU GLU A . n 
A 1 1498 TYR 1498 1498 1498 TYR TYR A . n 
A 1 1499 HIS 1499 1499 1499 HIS HIS A . n 
A 1 1500 ARG 1500 1500 1500 ARG ARG A . n 
A 1 1501 PRO 1501 1501 1501 PRO PRO A . n 
A 1 1502 ASP 1502 1502 1502 ASP ASP A . n 
A 1 1503 LYS 1503 1503 1503 LYS LYS A . n 
A 1 1504 GLN 1504 1504 1504 GLN GLN A . n 
A 1 1505 CYS 1505 1505 1505 CYS CYS A . n 
A 1 1506 THR 1506 1506 1506 THR THR A . n 
A 1 1507 MET 1507 1507 1507 MET MET A . n 
A 1 1508 PHE 1508 1508 1508 PHE PHE A . n 
A 1 1509 TYR 1509 1509 1509 TYR TYR A . n 
A 1 1510 SER 1510 1510 1510 SER SER A . n 
A 1 1511 THR 1511 1511 1511 THR THR A . n 
A 1 1512 SER 1512 1512 1512 SER SER A . n 
A 1 1513 ASN 1513 1513 1513 ASN ASN A . n 
A 1 1514 ILE 1514 1514 1514 ILE ILE A . n 
A 1 1515 LYS 1515 1515 1515 LYS LYS A . n 
A 1 1516 ILE 1516 1516 1516 ILE ILE A . n 
A 1 1517 GLN 1517 1517 1517 GLN GLN A . n 
A 1 1518 LYS 1518 1518 1518 LYS LYS A . n 
A 1 1519 VAL 1519 1519 1519 VAL VAL A . n 
A 1 1520 CYS 1520 1520 1520 CYS CYS A . n 
A 1 1521 GLU 1521 1521 1521 GLU GLU A . n 
A 1 1522 GLY 1522 1522 1522 GLY GLY A . n 
A 1 1523 ALA 1523 1523 1523 ALA ALA A . n 
A 1 1524 ALA 1524 1524 1524 ALA ALA A . n 
A 1 1525 CYS 1525 1525 1525 CYS CYS A . n 
A 1 1526 LYS 1526 1526 1526 LYS LYS A . n 
A 1 1527 CYS 1527 1527 1527 CYS CYS A . n 
A 1 1528 VAL 1528 1528 1528 VAL VAL A . n 
A 1 1529 GLU 1529 1529 1529 GLU GLU A . n 
A 1 1530 ALA 1530 1530 1530 ALA ALA A . n 
A 1 1531 ASP 1531 1531 1531 ASP ASP A . n 
A 1 1532 CYS 1532 1532 1532 CYS CYS A . n 
A 1 1533 GLY 1533 1533 1533 GLY GLY A . n 
A 1 1534 GLN 1534 1534 1534 GLN GLN A . n 
A 1 1535 MET 1535 1535 1535 MET MET A . n 
A 1 1536 GLN 1536 1536 1536 GLN GLN A . n 
A 1 1537 GLU 1537 1537 1537 GLU GLU A . n 
A 1 1538 GLU 1538 1538 1538 GLU GLU A . n 
A 1 1539 LEU 1539 1539 1539 LEU LEU A . n 
A 1 1540 ASP 1540 1540 1540 ASP ASP A . n 
A 1 1541 LEU 1541 1541 1541 LEU LEU A . n 
A 1 1542 THR 1542 1542 1542 THR THR A . n 
A 1 1543 ILE 1543 1543 1543 ILE ILE A . n 
A 1 1544 SER 1544 1544 1544 SER SER A . n 
A 1 1545 ALA 1545 1545 1545 ALA ALA A . n 
A 1 1546 GLU 1546 1546 1546 GLU GLU A . n 
A 1 1547 THR 1547 1547 1547 THR THR A . n 
A 1 1548 ARG 1548 1548 1548 ARG ARG A . n 
A 1 1549 LYS 1549 1549 1549 LYS LYS A . n 
A 1 1550 GLN 1550 1550 1550 GLN GLN A . n 
A 1 1551 THR 1551 1551 1551 THR THR A . n 
A 1 1552 ALA 1552 1552 1552 ALA ALA A . n 
A 1 1553 CYS 1553 1553 1553 CYS CYS A . n 
A 1 1554 LYS 1554 1554 1554 LYS LYS A . n 
A 1 1555 PRO 1555 1555 1555 PRO PRO A . n 
A 1 1556 GLU 1556 1556 1556 GLU GLU A . n 
A 1 1557 ILE 1557 1557 1557 ILE ILE A . n 
A 1 1558 ALA 1558 1558 1558 ALA ALA A . n 
A 1 1559 TYR 1559 1559 1559 TYR TYR A . n 
A 1 1560 ALA 1560 1560 1560 ALA ALA A . n 
A 1 1561 TYR 1561 1561 1561 TYR TYR A . n 
A 1 1562 LYS 1562 1562 1562 LYS LYS A . n 
A 1 1563 VAL 1563 1563 1563 VAL VAL A . n 
A 1 1564 SER 1564 1564 1564 SER SER A . n 
A 1 1565 ILE 1565 1565 1565 ILE ILE A . n 
A 1 1566 THR 1566 1566 1566 THR THR A . n 
A 1 1567 SER 1567 1567 1567 SER SER A . n 
A 1 1568 ILE 1568 1568 1568 ILE ILE A . n 
A 1 1569 THR 1569 1569 1569 THR THR A . n 
A 1 1570 VAL 1570 1570 1570 VAL VAL A . n 
A 1 1571 GLU 1571 1571 1571 GLU GLU A . n 
A 1 1572 ASN 1572 1572 1572 ASN ASN A . n 
A 1 1573 VAL 1573 1573 1573 VAL VAL A . n 
A 1 1574 PHE 1574 1574 1574 PHE PHE A . n 
A 1 1575 VAL 1575 1575 1575 VAL VAL A . n 
A 1 1576 LYS 1576 1576 1576 LYS LYS A . n 
A 1 1577 TYR 1577 1577 1577 TYR TYR A . n 
A 1 1578 LYS 1578 1578 1578 LYS LYS A . n 
A 1 1579 ALA 1579 1579 1579 ALA ALA A . n 
A 1 1580 THR 1580 1580 1580 THR THR A . n 
A 1 1581 LEU 1581 1581 1581 LEU LEU A . n 
A 1 1582 LEU 1582 1582 1582 LEU LEU A . n 
A 1 1583 ASP 1583 1583 1583 ASP ASP A . n 
A 1 1584 ILE 1584 1584 1584 ILE ILE A . n 
A 1 1585 TYR 1585 1585 1585 TYR TYR A . n 
A 1 1586 LYS 1586 1586 1586 LYS LYS A . n 
A 1 1587 THR 1587 1587 1587 THR THR A . n 
A 1 1588 GLY 1588 1588 1588 GLY GLY A . n 
A 1 1589 GLU 1589 1589 1589 GLU GLU A . n 
A 1 1590 ALA 1590 1590 1590 ALA ALA A . n 
A 1 1591 VAL 1591 1591 1591 VAL VAL A . n 
A 1 1592 ALA 1592 1592 1592 ALA ALA A . n 
A 1 1593 GLU 1593 1593 1593 GLU GLU A . n 
A 1 1594 LYS 1594 1594 1594 LYS LYS A . n 
A 1 1595 ASP 1595 1595 1595 ASP ASP A . n 
A 1 1596 SER 1596 1596 1596 SER SER A . n 
A 1 1597 GLU 1597 1597 1597 GLU GLU A . n 
A 1 1598 ILE 1598 1598 1598 ILE ILE A . n 
A 1 1599 THR 1599 1599 1599 THR THR A . n 
A 1 1600 PHE 1600 1600 1600 PHE PHE A . n 
A 1 1601 ILE 1601 1601 1601 ILE ILE A . n 
A 1 1602 LYS 1602 1602 1602 LYS LYS A . n 
A 1 1603 LYS 1603 1603 1603 LYS LYS A . n 
A 1 1604 VAL 1604 1604 1604 VAL VAL A . n 
A 1 1605 THR 1605 1605 1605 THR THR A . n 
A 1 1606 CYS 1606 1606 1606 CYS CYS A . n 
A 1 1607 THR 1607 1607 1607 THR THR A . n 
A 1 1608 ASN 1608 1608 1608 ASN ASN A . n 
A 1 1609 ALA 1609 1609 1609 ALA ALA A . n 
A 1 1610 GLU 1610 1610 1610 GLU GLU A . n 
A 1 1611 LEU 1611 1611 1611 LEU LEU A . n 
A 1 1612 VAL 1612 1612 1612 VAL VAL A . n 
A 1 1613 LYS 1613 1613 1613 LYS LYS A . n 
A 1 1614 GLY 1614 1614 1614 GLY GLY A . n 
A 1 1615 ARG 1615 1615 1615 ARG ARG A . n 
A 1 1616 GLN 1616 1616 1616 GLN GLN A . n 
A 1 1617 TYR 1617 1617 1617 TYR TYR A . n 
A 1 1618 LEU 1618 1618 1618 LEU LEU A . n 
A 1 1619 ILE 1619 1619 1619 ILE ILE A . n 
A 1 1620 MET 1620 1620 1620 MET MET A . n 
A 1 1621 GLY 1621 1621 1621 GLY GLY A . n 
A 1 1622 LYS 1622 1622 1622 LYS LYS A . n 
A 1 1623 GLU 1623 1623 1623 GLU GLU A . n 
A 1 1624 ALA 1624 1624 1624 ALA ALA A . n 
A 1 1625 LEU 1625 1625 1625 LEU LEU A . n 
A 1 1626 GLN 1626 1626 1626 GLN GLN A . n 
A 1 1627 ILE 1627 1627 1627 ILE ILE A . n 
A 1 1628 LYS 1628 1628 1628 LYS LYS A . n 
A 1 1629 TYR 1629 1629 1629 TYR TYR A . n 
A 1 1630 ASN 1630 1630 1630 ASN ASN A . n 
A 1 1631 PHE 1631 1631 1631 PHE PHE A . n 
A 1 1632 SER 1632 1632 1632 SER SER A . n 
A 1 1633 PHE 1633 1633 1633 PHE PHE A . n 
A 1 1634 ARG 1634 1634 1634 ARG ARG A . n 
A 1 1635 TYR 1635 1635 1635 TYR TYR A . n 
A 1 1636 ILE 1636 1636 1636 ILE ILE A . n 
A 1 1637 TYR 1637 1637 1637 TYR TYR A . n 
A 1 1638 PRO 1638 1638 1638 PRO PRO A . n 
A 1 1639 LEU 1639 1639 1639 LEU LEU A . n 
A 1 1640 ASP 1640 1640 1640 ASP ASP A . n 
A 1 1641 SER 1641 1641 1641 SER SER A . n 
A 1 1642 LEU 1642 1642 1642 LEU LEU A . n 
A 1 1643 THR 1643 1643 1643 THR THR A . n 
A 1 1644 TRP 1644 1644 1644 TRP TRP A . n 
A 1 1645 ILE 1645 1645 1645 ILE ILE A . n 
A 1 1646 GLU 1646 1646 1646 GLU GLU A . n 
A 1 1647 TYR 1647 1647 1647 TYR TYR A . n 
A 1 1648 TRP 1648 1648 1648 TRP TRP A . n 
A 1 1649 PRO 1649 1649 1649 PRO PRO A . n 
A 1 1650 ARG 1650 1650 1650 ARG ARG A . n 
A 1 1651 ASP 1651 1651 1651 ASP ASP A . n 
A 1 1652 THR 1652 1652 1652 THR THR A . n 
A 1 1653 THR 1653 1653 1653 THR THR A . n 
A 1 1654 CYS 1654 1654 1654 CYS CYS A . n 
A 1 1655 SER 1655 1655 1655 SER SER A . n 
A 1 1656 SER 1656 1656 1656 SER SER A . n 
A 1 1657 CYS 1657 1657 1657 CYS CYS A . n 
A 1 1658 GLN 1658 1658 1658 GLN GLN A . n 
A 1 1659 ALA 1659 1659 1659 ALA ALA A . n 
A 1 1660 PHE 1660 1660 1660 PHE PHE A . n 
A 1 1661 LEU 1661 1661 1661 LEU LEU A . n 
A 1 1662 ALA 1662 1662 1662 ALA ALA A . n 
A 1 1663 ASN 1663 1663 1663 ASN ASN A . n 
A 1 1664 LEU 1664 1664 1664 LEU LEU A . n 
A 1 1665 ASP 1665 1665 1665 ASP ASP A . n 
A 1 1666 GLU 1666 1666 1666 GLU GLU A . n 
A 1 1667 PHE 1667 1667 1667 PHE PHE A . n 
A 1 1668 ALA 1668 1668 1668 ALA ALA A . n 
A 1 1669 GLU 1669 1669 1669 GLU GLU A . n 
A 1 1670 ASP 1670 1670 1670 ASP ASP A . n 
A 1 1671 ILE 1671 1671 1671 ILE ILE A . n 
A 1 1672 PHE 1672 1672 1672 PHE PHE A . n 
A 1 1673 LEU 1673 1673 1673 LEU LEU A . n 
A 1 1674 ASN 1674 1674 1674 ASN ASN A . n 
A 1 1675 GLY 1675 1675 1675 GLY GLY A . n 
A 1 1676 CYS 1676 1676 1676 CYS CYS A . n 
B 2 1    MET 1    1    ?    ?   ?   X . n 
B 2 2    LYS 2    2    ?    ?   ?   X . n 
B 2 3    LEU 3    3    ?    ?   ?   X . n 
B 2 4    LYS 4    4    ?    ?   ?   X . n 
B 2 5    THR 5    5    ?    ?   ?   X . n 
B 2 6    LEU 6    6    ?    ?   ?   X . n 
B 2 7    ALA 7    7    ?    ?   ?   X . n 
B 2 8    LYS 8    8    ?    ?   ?   X . n 
B 2 9    ALA 9    9    ?    ?   ?   X . n 
B 2 10   THR 10   10   ?    ?   ?   X . n 
B 2 11   LEU 11   11   ?    ?   ?   X . n 
B 2 12   ALA 12   12   ?    ?   ?   X . n 
B 2 13   LEU 13   13   ?    ?   ?   X . n 
B 2 14   GLY 14   14   ?    ?   ?   X . n 
B 2 15   LEU 15   15   ?    ?   ?   X . n 
B 2 16   LEU 16   16   ?    ?   ?   X . n 
B 2 17   THR 17   17   ?    ?   ?   X . n 
B 2 18   THR 18   18   ?    ?   ?   X . n 
B 2 19   GLY 19   19   ?    ?   ?   X . n 
B 2 20   VAL 20   20   ?    ?   ?   X . n 
B 2 21   ILE 21   21   ?    ?   ?   X . n 
B 2 22   THR 22   22   ?    ?   ?   X . n 
B 2 23   SER 23   23   ?    ?   ?   X . n 
B 2 24   GLU 24   24   ?    ?   ?   X . n 
B 2 25   GLY 25   25   ?    ?   ?   X . n 
B 2 26   GLN 26   26   ?    ?   ?   X . n 
B 2 27   ALA 27   27   ?    ?   ?   X . n 
B 2 28   VAL 28   28   ?    ?   ?   X . n 
B 2 29   GLN 29   29   ?    ?   ?   X . n 
B 2 30   ALA 30   30   ?    ?   ?   X . n 
B 2 31   ALA 31   31   ?    ?   ?   X . n 
B 2 32   GLU 32   32   ?    ?   ?   X . n 
B 2 33   LYS 33   33   ?    ?   ?   X . n 
B 2 34   GLN 34   34   ?    ?   ?   X . n 
B 2 35   GLY 35   35   ?    ?   ?   X . n 
B 2 36   ARG 36   36   ?    ?   ?   X . n 
B 2 37   VAL 37   37   ?    ?   ?   X . n 
B 2 38   GLN 38   38   ?    ?   ?   X . n 
B 2 39   HIS 39   39   ?    ?   ?   X . n 
B 2 40   LEU 40   40   40   LEU LEU X . n 
B 2 41   HIS 41   41   41   HIS HIS X . n 
B 2 42   ASP 42   42   42   ASP ASP X . n 
B 2 43   ILE 43   43   43   ILE ILE X . n 
B 2 44   ARG 44   44   44   ARG ARG X . n 
B 2 45   ASP 45   45   45   ASP ASP X . n 
B 2 46   LEU 46   46   46   LEU LEU X . n 
B 2 47   HIS 47   47   47   HIS HIS X . n 
B 2 48   ARG 48   48   48   ARG ARG X . n 
B 2 49   TYR 49   49   49   TYR TYR X . n 
B 2 50   TYR 50   50   50   TYR TYR X . n 
B 2 51   SER 51   51   51   SER SER X . n 
B 2 52   SER 52   52   52   SER SER X . n 
B 2 53   GLU 53   53   53   GLU GLU X . n 
B 2 54   SER 54   54   54   SER SER X . n 
B 2 55   PHE 55   55   55   PHE PHE X . n 
B 2 56   GLU 56   56   56   GLU GLU X . n 
B 2 57   TYR 57   57   57   TYR TYR X . n 
B 2 58   SER 58   58   58   SER SER X . n 
B 2 59   ASN 59   59   59   ASN ASN X . n 
B 2 60   VAL 60   60   60   VAL VAL X . n 
B 2 61   SER 61   61   61   SER SER X . n 
B 2 62   GLY 62   62   62   GLY GLY X . n 
B 2 63   LYS 63   63   63   LYS LYS X . n 
B 2 64   VAL 64   64   64   VAL VAL X . n 
B 2 65   GLU 65   65   65   GLU GLU X . n 
B 2 66   ASN 66   66   66   ASN ASN X . n 
B 2 67   TYR 67   67   67   TYR TYR X . n 
B 2 68   ASN 68   68   68   ASN ASN X . n 
B 2 69   GLY 69   69   69   GLY GLY X . n 
B 2 70   SER 70   70   70   SER SER X . n 
B 2 71   ASN 71   71   71   ASN ASN X . n 
B 2 72   VAL 72   72   72   VAL VAL X . n 
B 2 73   VAL 73   73   73   VAL VAL X . n 
B 2 74   ARG 74   74   74   ARG ARG X . n 
B 2 75   PHE 75   75   75   PHE PHE X . n 
B 2 76   ASN 76   76   76   ASN ASN X . n 
B 2 77   PRO 77   77   77   PRO PRO X . n 
B 2 78   LYS 78   78   78   LYS LYS X . n 
B 2 79   ASP 79   79   79   ASP ASP X . n 
B 2 80   GLN 80   80   80   GLN GLN X . n 
B 2 81   ASN 81   81   81   ASN ASN X . n 
B 2 82   HIS 82   82   82   HIS HIS X . n 
B 2 83   GLN 83   83   83   GLN GLN X . n 
B 2 84   LEU 84   84   84   LEU LEU X . n 
B 2 85   PHE 85   85   85   PHE PHE X . n 
B 2 86   LEU 86   86   86   LEU LEU X . n 
B 2 87   LEU 87   87   87   LEU LEU X . n 
B 2 88   GLY 88   88   88   GLY GLY X . n 
B 2 89   LYS 89   89   89   LYS LYS X . n 
B 2 90   ASP 90   90   90   ASP ASP X . n 
B 2 91   LYS 91   91   91   LYS LYS X . n 
B 2 92   GLU 92   92   92   GLU GLU X . n 
B 2 93   GLN 93   93   93   GLN GLN X . n 
B 2 94   TYR 94   94   94   TYR TYR X . n 
B 2 95   LYS 95   95   95   LYS LYS X . n 
B 2 96   GLU 96   96   96   GLU GLU X . n 
B 2 97   GLY 97   97   97   GLY GLY X . n 
B 2 98   LEU 98   98   98   LEU LEU X . n 
B 2 99   GLN 99   99   99   GLN GLN X . n 
B 2 100  GLY 100  100  100  GLY GLY X . n 
B 2 101  GLN 101  101  101  GLN GLN X . n 
B 2 102  ASN 102  102  102  ASN ASN X . n 
B 2 103  VAL 103  103  103  VAL VAL X . n 
B 2 104  PHE 104  104  104  PHE PHE X . n 
B 2 105  VAL 105  105  105  VAL VAL X . n 
B 2 106  VAL 106  106  106  VAL VAL X . n 
B 2 107  GLN 107  107  107  GLN GLN X . n 
B 2 108  GLU 108  108  108  GLU GLU X . n 
B 2 109  LEU 109  109  109  LEU LEU X . n 
B 2 110  ILE 110  110  110  ILE ILE X . n 
B 2 111  ASP 111  111  111  ASP ASP X . n 
B 2 112  PRO 112  112  112  PRO PRO X . n 
B 2 113  ASN 113  113  113  ASN ASN X . n 
B 2 114  GLY 114  114  114  GLY GLY X . n 
B 2 115  ARG 115  115  115  ARG ARG X . n 
B 2 116  LEU 116  116  116  LEU LEU X . n 
B 2 117  SER 117  117  117  SER SER X . n 
B 2 118  THR 118  118  118  THR THR X . n 
B 2 119  VAL 119  119  119  VAL VAL X . n 
B 2 120  GLY 120  120  120  GLY GLY X . n 
B 2 121  GLY 121  121  121  GLY GLY X . n 
B 2 122  VAL 122  122  122  VAL VAL X . n 
B 2 123  THR 123  123  123  THR THR X . n 
B 2 124  LYS 124  124  124  LYS LYS X . n 
B 2 125  LYS 125  125  125  LYS LYS X . n 
B 2 126  ASN 126  126  126  ASN ASN X . n 
B 2 127  ASN 127  127  127  ASN ASN X . n 
B 2 128  LYS 128  128  128  LYS LYS X . n 
B 2 129  THR 129  129  129  THR THR X . n 
B 2 130  SER 130  130  130  SER SER X . n 
B 2 131  GLU 131  131  131  GLU GLU X . n 
B 2 132  THR 132  132  132  THR THR X . n 
B 2 133  ASN 133  133  133  ASN ASN X . n 
B 2 134  THR 134  134  134  THR THR X . n 
B 2 135  PRO 135  135  135  PRO PRO X . n 
B 2 136  LEU 136  136  136  LEU LEU X . n 
B 2 137  PHE 137  137  137  PHE PHE X . n 
B 2 138  VAL 138  138  138  VAL VAL X . n 
B 2 139  ASN 139  139  139  ASN ASN X . n 
B 2 140  LYS 140  140  140  LYS LYS X . n 
B 2 141  VAL 141  141  141  VAL VAL X . n 
B 2 142  ASN 142  142  142  ASN ASN X . n 
B 2 143  GLY 143  143  143  GLY GLY X . n 
B 2 144  GLU 144  144  144  GLU GLU X . n 
B 2 145  ASP 145  145  145  ASP ASP X . n 
B 2 146  LEU 146  146  146  LEU LEU X . n 
B 2 147  ASP 147  147  147  ASP ASP X . n 
B 2 148  ALA 148  148  148  ALA ALA X . n 
B 2 149  SER 149  149  149  SER SER X . n 
B 2 150  ILE 150  150  150  ILE ILE X . n 
B 2 151  ASP 151  151  151  ASP ASP X . n 
B 2 152  SER 152  152  152  SER SER X . n 
B 2 153  PHE 153  153  153  PHE PHE X . n 
B 2 154  LEU 154  154  154  LEU LEU X . n 
B 2 155  ILE 155  155  155  ILE ILE X . n 
B 2 156  GLN 156  156  156  GLN GLN X . n 
B 2 157  LYS 157  157  157  LYS LYS X . n 
B 2 158  GLU 158  158  158  GLU GLU X . n 
B 2 159  GLU 159  159  159  GLU GLU X . n 
B 2 160  ILE 160  160  160  ILE ILE X . n 
B 2 161  SER 161  161  161  SER SER X . n 
B 2 162  LEU 162  162  162  LEU LEU X . n 
B 2 163  LYS 163  163  163  LYS LYS X . n 
B 2 164  GLU 164  164  164  GLU GLU X . n 
B 2 165  LEU 165  165  165  LEU LEU X . n 
B 2 166  ASP 166  166  166  ASP ASP X . n 
B 2 167  PHE 167  167  167  PHE PHE X . n 
B 2 168  LYS 168  168  168  LYS LYS X . n 
B 2 169  ILE 169  169  169  ILE ILE X . n 
B 2 170  ARG 170  170  170  ARG ARG X . n 
B 2 171  GLN 171  171  171  GLN GLN X . n 
B 2 172  GLN 172  172  172  GLN GLN X . n 
B 2 173  LEU 173  173  173  LEU LEU X . n 
B 2 174  VAL 174  174  174  VAL VAL X . n 
B 2 175  ASN 175  175  175  ASN ASN X . n 
B 2 176  ASN 176  176  176  ASN ASN X . n 
B 2 177  TYR 177  177  177  TYR TYR X . n 
B 2 178  GLY 178  178  178  GLY GLY X . n 
B 2 179  LEU 179  179  179  LEU LEU X . n 
B 2 180  TYR 180  180  180  TYR TYR X . n 
B 2 181  LYS 181  181  181  LYS LYS X . n 
B 2 182  GLY 182  182  182  GLY GLY X . n 
B 2 183  THR 183  183  183  THR THR X . n 
B 2 184  SER 184  184  184  SER SER X . n 
B 2 185  LYS 185  185  185  LYS LYS X . n 
B 2 186  TYR 186  186  186  TYR TYR X . n 
B 2 187  GLY 187  187  187  GLY GLY X . n 
B 2 188  LYS 188  188  188  LYS LYS X . n 
B 2 189  ILE 189  189  189  ILE ILE X . n 
B 2 190  ILE 190  190  190  ILE ILE X . n 
B 2 191  ILE 191  191  191  ILE ILE X . n 
B 2 192  ASN 192  192  192  ASN ASN X . n 
B 2 193  LEU 193  193  193  LEU LEU X . n 
B 2 194  LYS 194  194  194  LYS LYS X . n 
B 2 195  ASP 195  195  195  ASP ASP X . n 
B 2 196  GLU 196  196  196  GLU GLU X . n 
B 2 197  ASN 197  197  197  ASN ASN X . n 
B 2 198  LYS 198  198  198  LYS LYS X . n 
B 2 199  VAL 199  199  199  VAL VAL X . n 
B 2 200  GLU 200  200  200  GLU GLU X . n 
B 2 201  ILE 201  201  201  ILE ILE X . n 
B 2 202  ASP 202  202  202  ASP ASP X . n 
B 2 203  LEU 203  203  203  LEU LEU X . n 
B 2 204  GLY 204  204  204  GLY GLY X . n 
B 2 205  ASP 205  205  205  ASP ASP X . n 
B 2 206  LYS 206  206  206  LYS LYS X . n 
B 2 207  LEU 207  207  207  LEU LEU X . n 
B 2 208  GLN 208  208  208  GLN GLN X . n 
B 2 209  PHE 209  209  209  PHE PHE X . n 
B 2 210  GLU 210  210  210  GLU GLU X . n 
B 2 211  ARG 211  211  211  ARG ARG X . n 
B 2 212  MET 212  212  212  MET MET X . n 
B 2 213  GLY 213  213  213  GLY GLY X . n 
B 2 214  ASP 214  214  214  ASP ASP X . n 
B 2 215  VAL 215  215  215  VAL VAL X . n 
B 2 216  LEU 216  216  216  LEU LEU X . n 
B 2 217  ASN 217  217  217  ASN ASN X . n 
B 2 218  SER 218  218  218  SER SER X . n 
B 2 219  LYS 219  219  219  LYS LYS X . n 
B 2 220  ASP 220  220  220  ASP ASP X . n 
B 2 221  ILE 221  221  221  ILE ILE X . n 
B 2 222  ARG 222  222  222  ARG ARG X . n 
B 2 223  GLY 223  223  223  GLY GLY X . n 
B 2 224  ILE 224  224  224  ILE ILE X . n 
B 2 225  SER 225  225  225  SER SER X . n 
B 2 226  VAL 226  226  226  VAL VAL X . n 
B 2 227  THR 227  227  227  THR THR X . n 
B 2 228  ILE 228  228  228  ILE ILE X . n 
B 2 229  ASN 229  229  229  ASN ASN X . n 
B 2 230  GLN 230  230  230  GLN GLN X . n 
B 2 231  ILE 231  231  ?    ?   ?   X . n 
C 1 1    MET 1    1    ?    ?   ?   B . n 
C 1 2    GLY 2    2    ?    ?   ?   B . n 
C 1 3    LEU 3    3    ?    ?   ?   B . n 
C 1 4    LEU 4    4    ?    ?   ?   B . n 
C 1 5    GLY 5    5    ?    ?   ?   B . n 
C 1 6    ILE 6    6    ?    ?   ?   B . n 
C 1 7    LEU 7    7    ?    ?   ?   B . n 
C 1 8    CYS 8    8    ?    ?   ?   B . n 
C 1 9    PHE 9    9    ?    ?   ?   B . n 
C 1 10   LEU 10   10   ?    ?   ?   B . n 
C 1 11   ILE 11   11   ?    ?   ?   B . n 
C 1 12   PHE 12   12   ?    ?   ?   B . n 
C 1 13   LEU 13   13   ?    ?   ?   B . n 
C 1 14   GLY 14   14   ?    ?   ?   B . n 
C 1 15   LYS 15   15   ?    ?   ?   B . n 
C 1 16   THR 16   16   ?    ?   ?   B . n 
C 1 17   TRP 17   17   ?    ?   ?   B . n 
C 1 18   GLY 18   18   ?    ?   ?   B . n 
C 1 19   GLN 19   19   ?    ?   ?   B . n 
C 1 20   GLU 20   20   ?    ?   ?   B . n 
C 1 21   GLN 21   21   ?    ?   ?   B . n 
C 1 22   THR 22   22   22   THR THR B . n 
C 1 23   TYR 23   23   23   TYR TYR B . n 
C 1 24   VAL 24   24   24   VAL VAL B . n 
C 1 25   ILE 25   25   25   ILE ILE B . n 
C 1 26   SER 26   26   26   SER SER B . n 
C 1 27   ALA 27   27   27   ALA ALA B . n 
C 1 28   PRO 28   28   28   PRO PRO B . n 
C 1 29   LYS 29   29   29   LYS LYS B . n 
C 1 30   ILE 30   30   30   ILE ILE B . n 
C 1 31   PHE 31   31   31   PHE PHE B . n 
C 1 32   ARG 32   32   32   ARG ARG B . n 
C 1 33   VAL 33   33   33   VAL VAL B . n 
C 1 34   GLY 34   34   34   GLY GLY B . n 
C 1 35   ALA 35   35   35   ALA ALA B . n 
C 1 36   SER 36   36   36   SER SER B . n 
C 1 37   GLU 37   37   37   GLU GLU B . n 
C 1 38   ASN 38   38   38   ASN ASN B . n 
C 1 39   ILE 39   39   39   ILE ILE B . n 
C 1 40   VAL 40   40   40   VAL VAL B . n 
C 1 41   ILE 41   41   41   ILE ILE B . n 
C 1 42   GLN 42   42   42   GLN GLN B . n 
C 1 43   VAL 43   43   43   VAL VAL B . n 
C 1 44   TYR 44   44   44   TYR TYR B . n 
C 1 45   GLY 45   45   45   GLY GLY B . n 
C 1 46   TYR 46   46   46   TYR TYR B . n 
C 1 47   THR 47   47   47   THR THR B . n 
C 1 48   GLU 48   48   48   GLU GLU B . n 
C 1 49   ALA 49   49   49   ALA ALA B . n 
C 1 50   PHE 50   50   50   PHE PHE B . n 
C 1 51   ASP 51   51   51   ASP ASP B . n 
C 1 52   ALA 52   52   52   ALA ALA B . n 
C 1 53   THR 53   53   53   THR THR B . n 
C 1 54   ILE 54   54   54   ILE ILE B . n 
C 1 55   SER 55   55   55   SER SER B . n 
C 1 56   ILE 56   56   56   ILE ILE B . n 
C 1 57   LYS 57   57   57   LYS LYS B . n 
C 1 58   SER 58   58   58   SER SER B . n 
C 1 59   TYR 59   59   59   TYR TYR B . n 
C 1 60   PRO 60   60   60   PRO PRO B . n 
C 1 61   ASP 61   61   61   ASP ASP B . n 
C 1 62   LYS 62   62   62   LYS LYS B . n 
C 1 63   LYS 63   63   63   LYS LYS B . n 
C 1 64   PHE 64   64   64   PHE PHE B . n 
C 1 65   SER 65   65   65   SER SER B . n 
C 1 66   TYR 66   66   66   TYR TYR B . n 
C 1 67   SER 67   67   67   SER SER B . n 
C 1 68   SER 68   68   68   SER SER B . n 
C 1 69   GLY 69   69   69   GLY GLY B . n 
C 1 70   HIS 70   70   70   HIS HIS B . n 
C 1 71   VAL 71   71   71   VAL VAL B . n 
C 1 72   HIS 72   72   72   HIS HIS B . n 
C 1 73   LEU 73   73   73   LEU LEU B . n 
C 1 74   SER 74   74   74   SER SER B . n 
C 1 75   SER 75   75   75   SER SER B . n 
C 1 76   GLU 76   76   76   GLU GLU B . n 
C 1 77   ASN 77   77   77   ASN ASN B . n 
C 1 78   LYS 78   78   78   LYS LYS B . n 
C 1 79   PHE 79   79   79   PHE PHE B . n 
C 1 80   GLN 80   80   80   GLN GLN B . n 
C 1 81   ASN 81   81   81   ASN ASN B . n 
C 1 82   SER 82   82   82   SER SER B . n 
C 1 83   ALA 83   83   83   ALA ALA B . n 
C 1 84   ILE 84   84   84   ILE ILE B . n 
C 1 85   LEU 85   85   85   LEU LEU B . n 
C 1 86   THR 86   86   86   THR THR B . n 
C 1 87   ILE 87   87   87   ILE ILE B . n 
C 1 88   GLN 88   88   88   GLN GLN B . n 
C 1 89   PRO 89   89   89   PRO PRO B . n 
C 1 90   LYS 90   90   90   LYS LYS B . n 
C 1 91   GLN 91   91   91   GLN GLN B . n 
C 1 92   LEU 92   92   92   LEU LEU B . n 
C 1 93   PRO 93   93   93   PRO PRO B . n 
C 1 94   GLY 94   94   94   GLY GLY B . n 
C 1 95   GLY 95   95   95   GLY GLY B . n 
C 1 96   GLN 96   96   96   GLN GLN B . n 
C 1 97   ASN 97   97   97   ASN ASN B . n 
C 1 98   PRO 98   98   98   PRO PRO B . n 
C 1 99   VAL 99   99   99   VAL VAL B . n 
C 1 100  SER 100  100  100  SER SER B . n 
C 1 101  TYR 101  101  101  TYR TYR B . n 
C 1 102  VAL 102  102  102  VAL VAL B . n 
C 1 103  TYR 103  103  103  TYR TYR B . n 
C 1 104  LEU 104  104  104  LEU LEU B . n 
C 1 105  GLU 105  105  105  GLU GLU B . n 
C 1 106  VAL 106  106  106  VAL VAL B . n 
C 1 107  VAL 107  107  107  VAL VAL B . n 
C 1 108  SER 108  108  108  SER SER B . n 
C 1 109  LYS 109  109  109  LYS LYS B . n 
C 1 110  HIS 110  110  110  HIS HIS B . n 
C 1 111  PHE 111  111  111  PHE PHE B . n 
C 1 112  SER 112  112  112  SER SER B . n 
C 1 113  LYS 113  113  113  LYS LYS B . n 
C 1 114  SER 114  114  114  SER SER B . n 
C 1 115  LYS 115  115  115  LYS LYS B . n 
C 1 116  ARG 116  116  116  ARG ARG B . n 
C 1 117  MET 117  117  117  MET MET B . n 
C 1 118  PRO 118  118  118  PRO PRO B . n 
C 1 119  ILE 119  119  119  ILE ILE B . n 
C 1 120  THR 120  120  120  THR THR B . n 
C 1 121  TYR 121  121  121  TYR TYR B . n 
C 1 122  ASP 122  122  122  ASP ASP B . n 
C 1 123  ASN 123  123  123  ASN ASN B . n 
C 1 124  GLY 124  124  124  GLY GLY B . n 
C 1 125  PHE 125  125  125  PHE PHE B . n 
C 1 126  LEU 126  126  126  LEU LEU B . n 
C 1 127  PHE 127  127  127  PHE PHE B . n 
C 1 128  ILE 128  128  128  ILE ILE B . n 
C 1 129  HIS 129  129  129  HIS HIS B . n 
C 1 130  THR 130  130  130  THR THR B . n 
C 1 131  ASP 131  131  131  ASP ASP B . n 
C 1 132  LYS 132  132  132  LYS LYS B . n 
C 1 133  PRO 133  133  133  PRO PRO B . n 
C 1 134  VAL 134  134  134  VAL VAL B . n 
C 1 135  TYR 135  135  135  TYR TYR B . n 
C 1 136  THR 136  136  136  THR THR B . n 
C 1 137  PRO 137  137  137  PRO PRO B . n 
C 1 138  ASP 138  138  138  ASP ASP B . n 
C 1 139  GLN 139  139  139  GLN GLN B . n 
C 1 140  SER 140  140  140  SER SER B . n 
C 1 141  VAL 141  141  141  VAL VAL B . n 
C 1 142  LYS 142  142  142  LYS LYS B . n 
C 1 143  VAL 143  143  143  VAL VAL B . n 
C 1 144  ARG 144  144  144  ARG ARG B . n 
C 1 145  VAL 145  145  145  VAL VAL B . n 
C 1 146  TYR 146  146  146  TYR TYR B . n 
C 1 147  SER 147  147  147  SER SER B . n 
C 1 148  LEU 148  148  148  LEU LEU B . n 
C 1 149  ASN 149  149  149  ASN ASN B . n 
C 1 150  ASP 150  150  150  ASP ASP B . n 
C 1 151  ASP 151  151  151  ASP ASP B . n 
C 1 152  LEU 152  152  152  LEU LEU B . n 
C 1 153  LYS 153  153  153  LYS LYS B . n 
C 1 154  PRO 154  154  154  PRO PRO B . n 
C 1 155  ALA 155  155  155  ALA ALA B . n 
C 1 156  LYS 156  156  156  LYS LYS B . n 
C 1 157  ARG 157  157  157  ARG ARG B . n 
C 1 158  GLU 158  158  158  GLU GLU B . n 
C 1 159  THR 159  159  159  THR THR B . n 
C 1 160  VAL 160  160  160  VAL VAL B . n 
C 1 161  LEU 161  161  161  LEU LEU B . n 
C 1 162  THR 162  162  162  THR THR B . n 
C 1 163  PHE 163  163  163  PHE PHE B . n 
C 1 164  ILE 164  164  164  ILE ILE B . n 
C 1 165  ASP 165  165  165  ASP ASP B . n 
C 1 166  PRO 166  166  166  PRO PRO B . n 
C 1 167  GLU 167  167  167  GLU GLU B . n 
C 1 168  GLY 168  168  168  GLY GLY B . n 
C 1 169  SER 169  169  169  SER SER B . n 
C 1 170  GLU 170  170  170  GLU GLU B . n 
C 1 171  VAL 171  171  171  VAL VAL B . n 
C 1 172  ASP 172  172  172  ASP ASP B . n 
C 1 173  MET 173  173  173  MET MET B . n 
C 1 174  VAL 174  174  174  VAL VAL B . n 
C 1 175  GLU 175  175  175  GLU GLU B . n 
C 1 176  GLU 176  176  176  GLU GLU B . n 
C 1 177  ILE 177  177  177  ILE ILE B . n 
C 1 178  ASP 178  178  178  ASP ASP B . n 
C 1 179  HIS 179  179  179  HIS HIS B . n 
C 1 180  ILE 180  180  180  ILE ILE B . n 
C 1 181  GLY 181  181  181  GLY GLY B . n 
C 1 182  ILE 182  182  182  ILE ILE B . n 
C 1 183  ILE 183  183  183  ILE ILE B . n 
C 1 184  SER 184  184  184  SER SER B . n 
C 1 185  PHE 185  185  185  PHE PHE B . n 
C 1 186  PRO 186  186  186  PRO PRO B . n 
C 1 187  ASP 187  187  187  ASP ASP B . n 
C 1 188  PHE 188  188  188  PHE PHE B . n 
C 1 189  LYS 189  189  189  LYS LYS B . n 
C 1 190  ILE 190  190  190  ILE ILE B . n 
C 1 191  PRO 191  191  191  PRO PRO B . n 
C 1 192  SER 192  192  192  SER SER B . n 
C 1 193  ASN 193  193  193  ASN ASN B . n 
C 1 194  PRO 194  194  194  PRO PRO B . n 
C 1 195  ARG 195  195  195  ARG ARG B . n 
C 1 196  TYR 196  196  196  TYR TYR B . n 
C 1 197  GLY 197  197  197  GLY GLY B . n 
C 1 198  MET 198  198  198  MET MET B . n 
C 1 199  TRP 199  199  199  TRP TRP B . n 
C 1 200  THR 200  200  200  THR THR B . n 
C 1 201  ILE 201  201  201  ILE ILE B . n 
C 1 202  LYS 202  202  202  LYS LYS B . n 
C 1 203  ALA 203  203  203  ALA ALA B . n 
C 1 204  LYS 204  204  204  LYS LYS B . n 
C 1 205  TYR 205  205  205  TYR TYR B . n 
C 1 206  LYS 206  206  206  LYS LYS B . n 
C 1 207  GLU 207  207  207  GLU GLU B . n 
C 1 208  ASP 208  208  208  ASP ASP B . n 
C 1 209  PHE 209  209  209  PHE PHE B . n 
C 1 210  SER 210  210  210  SER SER B . n 
C 1 211  THR 211  211  211  THR THR B . n 
C 1 212  THR 212  212  212  THR THR B . n 
C 1 213  GLY 213  213  213  GLY GLY B . n 
C 1 214  THR 214  214  214  THR THR B . n 
C 1 215  ALA 215  215  215  ALA ALA B . n 
C 1 216  TYR 216  216  216  TYR TYR B . n 
C 1 217  PHE 217  217  217  PHE PHE B . n 
C 1 218  GLU 218  218  218  GLU GLU B . n 
C 1 219  VAL 219  219  219  VAL VAL B . n 
C 1 220  LYS 220  220  220  LYS LYS B . n 
C 1 221  GLU 221  221  221  GLU GLU B . n 
C 1 222  TYR 222  222  222  TYR TYR B . n 
C 1 223  VAL 223  223  223  VAL VAL B . n 
C 1 224  LEU 224  224  224  LEU LEU B . n 
C 1 225  PRO 225  225  225  PRO PRO B . n 
C 1 226  HIS 226  226  226  HIS HIS B . n 
C 1 227  PHE 227  227  227  PHE PHE B . n 
C 1 228  SER 228  228  228  SER SER B . n 
C 1 229  VAL 229  229  229  VAL VAL B . n 
C 1 230  SER 230  230  230  SER SER B . n 
C 1 231  ILE 231  231  231  ILE ILE B . n 
C 1 232  GLU 232  232  232  GLU GLU B . n 
C 1 233  PRO 233  233  233  PRO PRO B . n 
C 1 234  GLU 234  234  234  GLU GLU B . n 
C 1 235  TYR 235  235  235  TYR TYR B . n 
C 1 236  ASN 236  236  236  ASN ASN B . n 
C 1 237  PHE 237  237  237  PHE PHE B . n 
C 1 238  ILE 238  238  238  ILE ILE B . n 
C 1 239  GLY 239  239  239  GLY GLY B . n 
C 1 240  TYR 240  240  240  TYR TYR B . n 
C 1 241  LYS 241  241  241  LYS LYS B . n 
C 1 242  ASN 242  242  242  ASN ASN B . n 
C 1 243  PHE 243  243  243  PHE PHE B . n 
C 1 244  LYS 244  244  244  LYS LYS B . n 
C 1 245  ASN 245  245  245  ASN ASN B . n 
C 1 246  PHE 246  246  246  PHE PHE B . n 
C 1 247  GLU 247  247  247  GLU GLU B . n 
C 1 248  ILE 248  248  248  ILE ILE B . n 
C 1 249  THR 249  249  249  THR THR B . n 
C 1 250  ILE 250  250  250  ILE ILE B . n 
C 1 251  LYS 251  251  251  LYS LYS B . n 
C 1 252  ALA 252  252  252  ALA ALA B . n 
C 1 253  ARG 253  253  253  ARG ARG B . n 
C 1 254  TYR 254  254  254  TYR TYR B . n 
C 1 255  PHE 255  255  255  PHE PHE B . n 
C 1 256  TYR 256  256  256  TYR TYR B . n 
C 1 257  ASN 257  257  257  ASN ASN B . n 
C 1 258  LYS 258  258  258  LYS LYS B . n 
C 1 259  VAL 259  259  259  VAL VAL B . n 
C 1 260  VAL 260  260  260  VAL VAL B . n 
C 1 261  THR 261  261  261  THR THR B . n 
C 1 262  GLU 262  262  262  GLU GLU B . n 
C 1 263  ALA 263  263  263  ALA ALA B . n 
C 1 264  ASP 264  264  264  ASP ASP B . n 
C 1 265  VAL 265  265  265  VAL VAL B . n 
C 1 266  TYR 266  266  266  TYR TYR B . n 
C 1 267  ILE 267  267  267  ILE ILE B . n 
C 1 268  THR 268  268  268  THR THR B . n 
C 1 269  PHE 269  269  269  PHE PHE B . n 
C 1 270  GLY 270  270  270  GLY GLY B . n 
C 1 271  ILE 271  271  271  ILE ILE B . n 
C 1 272  ARG 272  272  272  ARG ARG B . n 
C 1 273  GLU 273  273  273  GLU GLU B . n 
C 1 274  ASP 274  274  274  ASP ASP B . n 
C 1 275  LEU 275  275  275  LEU LEU B . n 
C 1 276  LYS 276  276  276  LYS LYS B . n 
C 1 277  ASP 277  277  277  ASP ASP B . n 
C 1 278  ASP 278  278  278  ASP ASP B . n 
C 1 279  GLN 279  279  279  GLN GLN B . n 
C 1 280  LYS 280  280  280  LYS LYS B . n 
C 1 281  GLU 281  281  281  GLU GLU B . n 
C 1 282  MET 282  282  282  MET MET B . n 
C 1 283  MET 283  283  283  MET MET B . n 
C 1 284  GLN 284  284  284  GLN GLN B . n 
C 1 285  THR 285  285  285  THR THR B . n 
C 1 286  ALA 286  286  286  ALA ALA B . n 
C 1 287  MET 287  287  287  MET MET B . n 
C 1 288  GLN 288  288  288  GLN GLN B . n 
C 1 289  ASN 289  289  289  ASN ASN B . n 
C 1 290  THR 290  290  290  THR THR B . n 
C 1 291  MET 291  291  291  MET MET B . n 
C 1 292  LEU 292  292  292  LEU LEU B . n 
C 1 293  ILE 293  293  293  ILE ILE B . n 
C 1 294  ASN 294  294  294  ASN ASN B . n 
C 1 295  GLY 295  295  295  GLY GLY B . n 
C 1 296  ILE 296  296  296  ILE ILE B . n 
C 1 297  ALA 297  297  297  ALA ALA B . n 
C 1 298  GLN 298  298  298  GLN GLN B . n 
C 1 299  VAL 299  299  299  VAL VAL B . n 
C 1 300  THR 300  300  300  THR THR B . n 
C 1 301  PHE 301  301  301  PHE PHE B . n 
C 1 302  ASP 302  302  302  ASP ASP B . n 
C 1 303  SER 303  303  303  SER SER B . n 
C 1 304  GLU 304  304  304  GLU GLU B . n 
C 1 305  THR 305  305  305  THR THR B . n 
C 1 306  ALA 306  306  306  ALA ALA B . n 
C 1 307  VAL 307  307  307  VAL VAL B . n 
C 1 308  LYS 308  308  308  LYS LYS B . n 
C 1 309  GLU 309  309  309  GLU GLU B . n 
C 1 310  LEU 310  310  310  LEU LEU B . n 
C 1 311  SER 311  311  311  SER SER B . n 
C 1 312  TYR 312  312  312  TYR TYR B . n 
C 1 313  TYR 313  313  313  TYR TYR B . n 
C 1 314  SER 314  314  314  SER SER B . n 
C 1 315  LEU 315  315  315  LEU LEU B . n 
C 1 316  GLU 316  316  316  GLU GLU B . n 
C 1 317  ASP 317  317  317  ASP ASP B . n 
C 1 318  LEU 318  318  318  LEU LEU B . n 
C 1 319  ASN 319  319  319  ASN ASN B . n 
C 1 320  ASN 320  320  320  ASN ASN B . n 
C 1 321  LYS 321  321  321  LYS LYS B . n 
C 1 322  TYR 322  322  322  TYR TYR B . n 
C 1 323  LEU 323  323  323  LEU LEU B . n 
C 1 324  TYR 324  324  324  TYR TYR B . n 
C 1 325  ILE 325  325  325  ILE ILE B . n 
C 1 326  ALA 326  326  326  ALA ALA B . n 
C 1 327  VAL 327  327  327  VAL VAL B . n 
C 1 328  THR 328  328  328  THR THR B . n 
C 1 329  VAL 329  329  329  VAL VAL B . n 
C 1 330  ILE 330  330  330  ILE ILE B . n 
C 1 331  GLU 331  331  331  GLU GLU B . n 
C 1 332  SER 332  332  332  SER SER B . n 
C 1 333  THR 333  333  333  THR THR B . n 
C 1 334  GLY 334  334  334  GLY GLY B . n 
C 1 335  GLY 335  335  335  GLY GLY B . n 
C 1 336  PHE 336  336  336  PHE PHE B . n 
C 1 337  SER 337  337  337  SER SER B . n 
C 1 338  GLU 338  338  338  GLU GLU B . n 
C 1 339  GLU 339  339  339  GLU GLU B . n 
C 1 340  ALA 340  340  340  ALA ALA B . n 
C 1 341  GLU 341  341  341  GLU GLU B . n 
C 1 342  ILE 342  342  342  ILE ILE B . n 
C 1 343  PRO 343  343  343  PRO PRO B . n 
C 1 344  GLY 344  344  344  GLY GLY B . n 
C 1 345  ILE 345  345  345  ILE ILE B . n 
C 1 346  LYS 346  346  346  LYS LYS B . n 
C 1 347  TYR 347  347  347  TYR TYR B . n 
C 1 348  VAL 348  348  348  VAL VAL B . n 
C 1 349  LEU 349  349  349  LEU LEU B . n 
C 1 350  SER 350  350  350  SER SER B . n 
C 1 351  PRO 351  351  351  PRO PRO B . n 
C 1 352  TYR 352  352  352  TYR TYR B . n 
C 1 353  LYS 353  353  353  LYS LYS B . n 
C 1 354  LEU 354  354  354  LEU LEU B . n 
C 1 355  ASN 355  355  355  ASN ASN B . n 
C 1 356  LEU 356  356  356  LEU LEU B . n 
C 1 357  VAL 357  357  357  VAL VAL B . n 
C 1 358  ALA 358  358  358  ALA ALA B . n 
C 1 359  THR 359  359  359  THR THR B . n 
C 1 360  PRO 360  360  360  PRO PRO B . n 
C 1 361  LEU 361  361  361  LEU LEU B . n 
C 1 362  PHE 362  362  362  PHE PHE B . n 
C 1 363  LEU 363  363  363  LEU LEU B . n 
C 1 364  LYS 364  364  364  LYS LYS B . n 
C 1 365  PRO 365  365  365  PRO PRO B . n 
C 1 366  GLY 366  366  366  GLY GLY B . n 
C 1 367  ILE 367  367  367  ILE ILE B . n 
C 1 368  PRO 368  368  368  PRO PRO B . n 
C 1 369  TYR 369  369  369  TYR TYR B . n 
C 1 370  PRO 370  370  370  PRO PRO B . n 
C 1 371  ILE 371  371  371  ILE ILE B . n 
C 1 372  LYS 372  372  372  LYS LYS B . n 
C 1 373  VAL 373  373  373  VAL VAL B . n 
C 1 374  GLN 374  374  374  GLN GLN B . n 
C 1 375  VAL 375  375  375  VAL VAL B . n 
C 1 376  LYS 376  376  376  LYS LYS B . n 
C 1 377  ASP 377  377  377  ASP ASP B . n 
C 1 378  SER 378  378  378  SER SER B . n 
C 1 379  LEU 379  379  379  LEU LEU B . n 
C 1 380  ASP 380  380  380  ASP ASP B . n 
C 1 381  GLN 381  381  381  GLN GLN B . n 
C 1 382  LEU 382  382  382  LEU LEU B . n 
C 1 383  VAL 383  383  383  VAL VAL B . n 
C 1 384  GLY 384  384  384  GLY GLY B . n 
C 1 385  GLY 385  385  385  GLY GLY B . n 
C 1 386  VAL 386  386  386  VAL VAL B . n 
C 1 387  PRO 387  387  387  PRO PRO B . n 
C 1 388  VAL 388  388  388  VAL VAL B . n 
C 1 389  THR 389  389  389  THR THR B . n 
C 1 390  LEU 390  390  390  LEU LEU B . n 
C 1 391  ASN 391  391  391  ASN ASN B . n 
C 1 392  ALA 392  392  392  ALA ALA B . n 
C 1 393  GLN 393  393  393  GLN GLN B . n 
C 1 394  THR 394  394  394  THR THR B . n 
C 1 395  ILE 395  395  395  ILE ILE B . n 
C 1 396  ASP 396  396  396  ASP ASP B . n 
C 1 397  VAL 397  397  397  VAL VAL B . n 
C 1 398  ASN 398  398  398  ASN ASN B . n 
C 1 399  GLN 399  399  399  GLN GLN B . n 
C 1 400  GLU 400  400  400  GLU GLU B . n 
C 1 401  THR 401  401  401  THR THR B . n 
C 1 402  SER 402  402  402  SER SER B . n 
C 1 403  ASP 403  403  403  ASP ASP B . n 
C 1 404  LEU 404  404  404  LEU LEU B . n 
C 1 405  ASP 405  405  405  ASP ASP B . n 
C 1 406  PRO 406  406  406  PRO PRO B . n 
C 1 407  SER 407  407  407  SER SER B . n 
C 1 408  LYS 408  408  408  LYS LYS B . n 
C 1 409  SER 409  409  409  SER SER B . n 
C 1 410  VAL 410  410  410  VAL VAL B . n 
C 1 411  THR 411  411  411  THR THR B . n 
C 1 412  ARG 412  412  412  ARG ARG B . n 
C 1 413  VAL 413  413  413  VAL VAL B . n 
C 1 414  ASP 414  414  414  ASP ASP B . n 
C 1 415  ASP 415  415  415  ASP ASP B . n 
C 1 416  GLY 416  416  416  GLY GLY B . n 
C 1 417  VAL 417  417  417  VAL VAL B . n 
C 1 418  ALA 418  418  418  ALA ALA B . n 
C 1 419  SER 419  419  419  SER SER B . n 
C 1 420  PHE 420  420  420  PHE PHE B . n 
C 1 421  VAL 421  421  421  VAL VAL B . n 
C 1 422  LEU 422  422  422  LEU LEU B . n 
C 1 423  ASN 423  423  423  ASN ASN B . n 
C 1 424  LEU 424  424  424  LEU LEU B . n 
C 1 425  PRO 425  425  425  PRO PRO B . n 
C 1 426  SER 426  426  426  SER SER B . n 
C 1 427  GLY 427  427  427  GLY GLY B . n 
C 1 428  VAL 428  428  428  VAL VAL B . n 
C 1 429  THR 429  429  429  THR THR B . n 
C 1 430  VAL 430  430  430  VAL VAL B . n 
C 1 431  LEU 431  431  431  LEU LEU B . n 
C 1 432  GLU 432  432  432  GLU GLU B . n 
C 1 433  PHE 433  433  433  PHE PHE B . n 
C 1 434  ASN 434  434  434  ASN ASN B . n 
C 1 435  VAL 435  435  435  VAL VAL B . n 
C 1 436  LYS 436  436  436  LYS LYS B . n 
C 1 437  THR 437  437  437  THR THR B . n 
C 1 438  ASP 438  438  438  ASP ASP B . n 
C 1 439  ALA 439  439  439  ALA ALA B . n 
C 1 440  PRO 440  440  440  PRO PRO B . n 
C 1 441  ASP 441  441  441  ASP ASP B . n 
C 1 442  LEU 442  442  442  LEU LEU B . n 
C 1 443  PRO 443  443  443  PRO PRO B . n 
C 1 444  GLU 444  444  444  GLU GLU B . n 
C 1 445  GLU 445  445  445  GLU GLU B . n 
C 1 446  ASN 446  446  446  ASN ASN B . n 
C 1 447  GLN 447  447  447  GLN GLN B . n 
C 1 448  ALA 448  448  448  ALA ALA B . n 
C 1 449  ARG 449  449  449  ARG ARG B . n 
C 1 450  GLU 450  450  450  GLU GLU B . n 
C 1 451  GLY 451  451  451  GLY GLY B . n 
C 1 452  TYR 452  452  452  TYR TYR B . n 
C 1 453  ARG 453  453  453  ARG ARG B . n 
C 1 454  ALA 454  454  454  ALA ALA B . n 
C 1 455  ILE 455  455  455  ILE ILE B . n 
C 1 456  ALA 456  456  456  ALA ALA B . n 
C 1 457  TYR 457  457  457  TYR TYR B . n 
C 1 458  SER 458  458  458  SER SER B . n 
C 1 459  SER 459  459  459  SER SER B . n 
C 1 460  LEU 460  460  460  LEU LEU B . n 
C 1 461  SER 461  461  461  SER SER B . n 
C 1 462  GLN 462  462  462  GLN GLN B . n 
C 1 463  SER 463  463  463  SER SER B . n 
C 1 464  TYR 464  464  464  TYR TYR B . n 
C 1 465  LEU 465  465  465  LEU LEU B . n 
C 1 466  TYR 466  466  466  TYR TYR B . n 
C 1 467  ILE 467  467  467  ILE ILE B . n 
C 1 468  ASP 468  468  468  ASP ASP B . n 
C 1 469  TRP 469  469  469  TRP TRP B . n 
C 1 470  THR 470  470  470  THR THR B . n 
C 1 471  ASP 471  471  471  ASP ASP B . n 
C 1 472  ASN 472  472  472  ASN ASN B . n 
C 1 473  HIS 473  473  473  HIS HIS B . n 
C 1 474  LYS 474  474  474  LYS LYS B . n 
C 1 475  ALA 475  475  475  ALA ALA B . n 
C 1 476  LEU 476  476  476  LEU LEU B . n 
C 1 477  LEU 477  477  477  LEU LEU B . n 
C 1 478  VAL 478  478  478  VAL VAL B . n 
C 1 479  GLY 479  479  479  GLY GLY B . n 
C 1 480  GLU 480  480  480  GLU GLU B . n 
C 1 481  HIS 481  481  481  HIS HIS B . n 
C 1 482  LEU 482  482  482  LEU LEU B . n 
C 1 483  ASN 483  483  483  ASN ASN B . n 
C 1 484  ILE 484  484  484  ILE ILE B . n 
C 1 485  ILE 485  485  485  ILE ILE B . n 
C 1 486  VAL 486  486  486  VAL VAL B . n 
C 1 487  THR 487  487  487  THR THR B . n 
C 1 488  PRO 488  488  488  PRO PRO B . n 
C 1 489  LYS 489  489  489  LYS LYS B . n 
C 1 490  SER 490  490  490  SER SER B . n 
C 1 491  PRO 491  491  491  PRO PRO B . n 
C 1 492  TYR 492  492  492  TYR TYR B . n 
C 1 493  ILE 493  493  493  ILE ILE B . n 
C 1 494  ASP 494  494  494  ASP ASP B . n 
C 1 495  LYS 495  495  495  LYS LYS B . n 
C 1 496  ILE 496  496  496  ILE ILE B . n 
C 1 497  THR 497  497  497  THR THR B . n 
C 1 498  HIS 498  498  498  HIS HIS B . n 
C 1 499  TYR 499  499  499  TYR TYR B . n 
C 1 500  ASN 500  500  500  ASN ASN B . n 
C 1 501  TYR 501  501  501  TYR TYR B . n 
C 1 502  LEU 502  502  502  LEU LEU B . n 
C 1 503  ILE 503  503  503  ILE ILE B . n 
C 1 504  LEU 504  504  504  LEU LEU B . n 
C 1 505  SER 505  505  505  SER SER B . n 
C 1 506  LYS 506  506  506  LYS LYS B . n 
C 1 507  GLY 507  507  507  GLY GLY B . n 
C 1 508  LYS 508  508  508  LYS LYS B . n 
C 1 509  ILE 509  509  509  ILE ILE B . n 
C 1 510  ILE 510  510  510  ILE ILE B . n 
C 1 511  HIS 511  511  511  HIS HIS B . n 
C 1 512  PHE 512  512  512  PHE PHE B . n 
C 1 513  GLY 513  513  513  GLY GLY B . n 
C 1 514  THR 514  514  514  THR THR B . n 
C 1 515  ARG 515  515  515  ARG ARG B . n 
C 1 516  GLU 516  516  516  GLU GLU B . n 
C 1 517  LYS 517  517  517  LYS LYS B . n 
C 1 518  PHE 518  518  518  PHE PHE B . n 
C 1 519  SER 519  519  519  SER SER B . n 
C 1 520  ASP 520  520  520  ASP ASP B . n 
C 1 521  ALA 521  521  521  ALA ALA B . n 
C 1 522  SER 522  522  522  SER SER B . n 
C 1 523  TYR 523  523  523  TYR TYR B . n 
C 1 524  GLN 524  524  524  GLN GLN B . n 
C 1 525  SER 525  525  525  SER SER B . n 
C 1 526  ILE 526  526  526  ILE ILE B . n 
C 1 527  ASN 527  527  527  ASN ASN B . n 
C 1 528  ILE 528  528  528  ILE ILE B . n 
C 1 529  PRO 529  529  529  PRO PRO B . n 
C 1 530  VAL 530  530  530  VAL VAL B . n 
C 1 531  THR 531  531  531  THR THR B . n 
C 1 532  GLN 532  532  532  GLN GLN B . n 
C 1 533  ASN 533  533  533  ASN ASN B . n 
C 1 534  MET 534  534  534  MET MET B . n 
C 1 535  VAL 535  535  535  VAL VAL B . n 
C 1 536  PRO 536  536  536  PRO PRO B . n 
C 1 537  SER 537  537  537  SER SER B . n 
C 1 538  SER 538  538  538  SER SER B . n 
C 1 539  ARG 539  539  539  ARG ARG B . n 
C 1 540  LEU 540  540  540  LEU LEU B . n 
C 1 541  LEU 541  541  541  LEU LEU B . n 
C 1 542  VAL 542  542  542  VAL VAL B . n 
C 1 543  TYR 543  543  543  TYR TYR B . n 
C 1 544  TYR 544  544  544  TYR TYR B . n 
C 1 545  ILE 545  545  545  ILE ILE B . n 
C 1 546  VAL 546  546  546  VAL VAL B . n 
C 1 547  THR 547  547  547  THR THR B . n 
C 1 548  GLY 548  548  548  GLY GLY B . n 
C 1 549  GLU 549  549  549  GLU GLU B . n 
C 1 550  GLN 550  550  550  GLN GLN B . n 
C 1 551  THR 551  551  551  THR THR B . n 
C 1 552  ALA 552  552  552  ALA ALA B . n 
C 1 553  GLU 553  553  553  GLU GLU B . n 
C 1 554  LEU 554  554  554  LEU LEU B . n 
C 1 555  VAL 555  555  555  VAL VAL B . n 
C 1 556  SER 556  556  556  SER SER B . n 
C 1 557  ASP 557  557  557  ASP ASP B . n 
C 1 558  SER 558  558  558  SER SER B . n 
C 1 559  VAL 559  559  559  VAL VAL B . n 
C 1 560  TRP 560  560  560  TRP TRP B . n 
C 1 561  LEU 561  561  561  LEU LEU B . n 
C 1 562  ASN 562  562  562  ASN ASN B . n 
C 1 563  ILE 563  563  563  ILE ILE B . n 
C 1 564  GLU 564  564  564  GLU GLU B . n 
C 1 565  GLU 565  565  565  GLU GLU B . n 
C 1 566  LYS 566  566  566  LYS LYS B . n 
C 1 567  CYS 567  567  567  CYS CYS B . n 
C 1 568  GLY 568  568  568  GLY GLY B . n 
C 1 569  ASN 569  569  569  ASN ASN B . n 
C 1 570  GLN 570  570  570  GLN GLN B . n 
C 1 571  LEU 571  571  571  LEU LEU B . n 
C 1 572  GLN 572  572  572  GLN GLN B . n 
C 1 573  VAL 573  573  573  VAL VAL B . n 
C 1 574  HIS 574  574  574  HIS HIS B . n 
C 1 575  LEU 575  575  575  LEU LEU B . n 
C 1 576  SER 576  576  576  SER SER B . n 
C 1 577  PRO 577  577  577  PRO PRO B . n 
C 1 578  ASP 578  578  578  ASP ASP B . n 
C 1 579  ALA 579  579  579  ALA ALA B . n 
C 1 580  ASP 580  580  580  ASP ASP B . n 
C 1 581  ALA 581  581  581  ALA ALA B . n 
C 1 582  TYR 582  582  582  TYR TYR B . n 
C 1 583  SER 583  583  583  SER SER B . n 
C 1 584  PRO 584  584  584  PRO PRO B . n 
C 1 585  GLY 585  585  585  GLY GLY B . n 
C 1 586  GLN 586  586  586  GLN GLN B . n 
C 1 587  THR 587  587  587  THR THR B . n 
C 1 588  VAL 588  588  588  VAL VAL B . n 
C 1 589  SER 589  589  589  SER SER B . n 
C 1 590  LEU 590  590  590  LEU LEU B . n 
C 1 591  ASN 591  591  591  ASN ASN B . n 
C 1 592  MET 592  592  592  MET MET B . n 
C 1 593  ALA 593  593  593  ALA ALA B . n 
C 1 594  THR 594  594  594  THR THR B . n 
C 1 595  GLY 595  595  595  GLY GLY B . n 
C 1 596  MET 596  596  596  MET MET B . n 
C 1 597  ASP 597  597  597  ASP ASP B . n 
C 1 598  SER 598  598  598  SER SER B . n 
C 1 599  TRP 599  599  599  TRP TRP B . n 
C 1 600  VAL 600  600  600  VAL VAL B . n 
C 1 601  ALA 601  601  601  ALA ALA B . n 
C 1 602  LEU 602  602  602  LEU LEU B . n 
C 1 603  ALA 603  603  603  ALA ALA B . n 
C 1 604  ALA 604  604  604  ALA ALA B . n 
C 1 605  VAL 605  605  605  VAL VAL B . n 
C 1 606  ASP 606  606  606  ASP ASP B . n 
C 1 607  SER 607  607  607  SER SER B . n 
C 1 608  ALA 608  608  608  ALA ALA B . n 
C 1 609  VAL 609  609  609  VAL VAL B . n 
C 1 610  TYR 610  610  610  TYR TYR B . n 
C 1 611  GLY 611  611  611  GLY GLY B . n 
C 1 612  VAL 612  612  612  VAL VAL B . n 
C 1 613  GLN 613  613  613  GLN GLN B . n 
C 1 614  ARG 614  614  614  ARG ARG B . n 
C 1 615  GLY 615  615  615  GLY GLY B . n 
C 1 616  ALA 616  616  616  ALA ALA B . n 
C 1 617  LYS 617  617  617  LYS LYS B . n 
C 1 618  LYS 618  618  618  LYS LYS B . n 
C 1 619  PRO 619  619  619  PRO PRO B . n 
C 1 620  LEU 620  620  620  LEU LEU B . n 
C 1 621  GLU 621  621  621  GLU GLU B . n 
C 1 622  ARG 622  622  622  ARG ARG B . n 
C 1 623  VAL 623  623  623  VAL VAL B . n 
C 1 624  PHE 624  624  624  PHE PHE B . n 
C 1 625  GLN 625  625  625  GLN GLN B . n 
C 1 626  PHE 626  626  626  PHE PHE B . n 
C 1 627  LEU 627  627  627  LEU LEU B . n 
C 1 628  GLU 628  628  628  GLU GLU B . n 
C 1 629  LYS 629  629  629  LYS LYS B . n 
C 1 630  SER 630  630  630  SER SER B . n 
C 1 631  ASP 631  631  631  ASP ASP B . n 
C 1 632  LEU 632  632  632  LEU LEU B . n 
C 1 633  GLY 633  633  633  GLY GLY B . n 
C 1 634  CYS 634  634  634  CYS CYS B . n 
C 1 635  GLY 635  635  635  GLY GLY B . n 
C 1 636  ALA 636  636  636  ALA ALA B . n 
C 1 637  GLY 637  637  637  GLY GLY B . n 
C 1 638  GLY 638  638  638  GLY GLY B . n 
C 1 639  GLY 639  639  639  GLY GLY B . n 
C 1 640  LEU 640  640  640  LEU LEU B . n 
C 1 641  ASN 641  641  641  ASN ASN B . n 
C 1 642  ASN 642  642  642  ASN ASN B . n 
C 1 643  ALA 643  643  643  ALA ALA B . n 
C 1 644  ASN 644  644  644  ASN ASN B . n 
C 1 645  VAL 645  645  645  VAL VAL B . n 
C 1 646  PHE 646  646  646  PHE PHE B . n 
C 1 647  HIS 647  647  647  HIS HIS B . n 
C 1 648  LEU 648  648  648  LEU LEU B . n 
C 1 649  ALA 649  649  649  ALA ALA B . n 
C 1 650  GLY 650  650  650  GLY GLY B . n 
C 1 651  LEU 651  651  651  LEU LEU B . n 
C 1 652  THR 652  652  652  THR THR B . n 
C 1 653  PHE 653  653  653  PHE PHE B . n 
C 1 654  LEU 654  654  654  LEU LEU B . n 
C 1 655  THR 655  655  655  THR THR B . n 
C 1 656  ASN 656  656  656  ASN ASN B . n 
C 1 657  ALA 657  657  657  ALA ALA B . n 
C 1 658  ASN 658  658  658  ASN ASN B . n 
C 1 659  ALA 659  659  659  ALA ALA B . n 
C 1 660  ASP 660  660  660  ASP ASP B . n 
C 1 661  ASP 661  661  661  ASP ASP B . n 
C 1 662  SER 662  662  662  SER SER B . n 
C 1 663  GLN 663  663  663  GLN GLN B . n 
C 1 664  GLU 664  664  664  GLU GLU B . n 
C 1 665  ASN 665  665  665  ASN ASN B . n 
C 1 666  ASP 666  666  666  ASP ASP B . n 
C 1 667  GLU 667  667  667  GLU GLU B . n 
C 1 668  PRO 668  668  668  PRO PRO B . n 
C 1 669  CYS 669  669  669  CYS CYS B . n 
C 1 670  LYS 670  670  670  LYS LYS B . n 
C 1 671  GLU 671  671  671  GLU GLU B . n 
C 1 672  ILE 672  672  672  ILE ILE B . n 
C 1 673  LEU 673  673  673  LEU LEU B . n 
C 1 674  ARG 674  674  ?    ?   ?   B . n 
C 1 675  PRO 675  675  ?    ?   ?   B . n 
C 1 676  ARG 676  676  ?    ?   ?   B . n 
C 1 677  ARG 677  677  ?    ?   ?   B . n 
C 1 678  THR 678  678  ?    ?   ?   B . n 
C 1 679  LEU 679  679  679  LEU LEU B . n 
C 1 680  GLN 680  680  680  GLN GLN B . n 
C 1 681  LYS 681  681  681  LYS LYS B . n 
C 1 682  LYS 682  682  682  LYS LYS B . n 
C 1 683  ILE 683  683  683  ILE ILE B . n 
C 1 684  GLU 684  684  684  GLU GLU B . n 
C 1 685  GLU 685  685  685  GLU GLU B . n 
C 1 686  ILE 686  686  686  ILE ILE B . n 
C 1 687  ALA 687  687  687  ALA ALA B . n 
C 1 688  ALA 688  688  688  ALA ALA B . n 
C 1 689  LYS 689  689  689  LYS LYS B . n 
C 1 690  TYR 690  690  690  TYR TYR B . n 
C 1 691  LYS 691  691  691  LYS LYS B . n 
C 1 692  HIS 692  692  692  HIS HIS B . n 
C 1 693  SER 693  693  693  SER SER B . n 
C 1 694  VAL 694  694  694  VAL VAL B . n 
C 1 695  VAL 695  695  695  VAL VAL B . n 
C 1 696  LYS 696  696  696  LYS LYS B . n 
C 1 697  LYS 697  697  697  LYS LYS B . n 
C 1 698  CYS 698  698  698  CYS CYS B . n 
C 1 699  CYS 699  699  699  CYS CYS B . n 
C 1 700  TYR 700  700  700  TYR TYR B . n 
C 1 701  ASP 701  701  701  ASP ASP B . n 
C 1 702  GLY 702  702  702  GLY GLY B . n 
C 1 703  ALA 703  703  703  ALA ALA B . n 
C 1 704  CYS 704  704  704  CYS CYS B . n 
C 1 705  VAL 705  705  705  VAL VAL B . n 
C 1 706  ASN 706  706  706  ASN ASN B . n 
C 1 707  ASN 707  707  707  ASN ASN B . n 
C 1 708  ASP 708  708  708  ASP ASP B . n 
C 1 709  GLU 709  709  709  GLU GLU B . n 
C 1 710  THR 710  710  710  THR THR B . n 
C 1 711  CYS 711  711  711  CYS CYS B . n 
C 1 712  GLU 712  712  712  GLU GLU B . n 
C 1 713  GLN 713  713  713  GLN GLN B . n 
C 1 714  ARG 714  714  714  ARG ARG B . n 
C 1 715  ALA 715  715  715  ALA ALA B . n 
C 1 716  ALA 716  716  716  ALA ALA B . n 
C 1 717  ARG 717  717  717  ARG ARG B . n 
C 1 718  ILE 718  718  718  ILE ILE B . n 
C 1 719  SER 719  719  719  SER SER B . n 
C 1 720  LEU 720  720  720  LEU LEU B . n 
C 1 721  GLY 721  721  721  GLY GLY B . n 
C 1 722  PRO 722  722  722  PRO PRO B . n 
C 1 723  ARG 723  723  723  ARG ARG B . n 
C 1 724  CYS 724  724  724  CYS CYS B . n 
C 1 725  ILE 725  725  725  ILE ILE B . n 
C 1 726  LYS 726  726  726  LYS LYS B . n 
C 1 727  ALA 727  727  727  ALA ALA B . n 
C 1 728  PHE 728  728  728  PHE PHE B . n 
C 1 729  THR 729  729  729  THR THR B . n 
C 1 730  GLU 730  730  730  GLU GLU B . n 
C 1 731  CYS 731  731  731  CYS CYS B . n 
C 1 732  CYS 732  732  732  CYS CYS B . n 
C 1 733  VAL 733  733  733  VAL VAL B . n 
C 1 734  VAL 734  734  734  VAL VAL B . n 
C 1 735  ALA 735  735  735  ALA ALA B . n 
C 1 736  SER 736  736  736  SER SER B . n 
C 1 737  GLN 737  737  737  GLN GLN B . n 
C 1 738  LEU 738  738  738  LEU LEU B . n 
C 1 739  ARG 739  739  739  ARG ARG B . n 
C 1 740  ALA 740  740  740  ALA ALA B . n 
C 1 741  ASN 741  741  741  ASN ASN B . n 
C 1 742  ILE 742  742  742  ILE ILE B . n 
C 1 743  SER 743  743  743  SER SER B . n 
C 1 744  HIS 744  744  ?    ?   ?   B . n 
C 1 745  LYS 745  745  ?    ?   ?   B . n 
C 1 746  ASP 746  746  ?    ?   ?   B . n 
C 1 747  MET 747  747  ?    ?   ?   B . n 
C 1 748  GLN 748  748  ?    ?   ?   B . n 
C 1 749  LEU 749  749  749  LEU LEU B . n 
C 1 750  GLY 750  750  750  GLY GLY B . n 
C 1 751  ARG 751  751  751  ARG ARG B . n 
C 1 752  LEU 752  752  752  LEU LEU B . n 
C 1 753  HIS 753  753  753  HIS HIS B . n 
C 1 754  MET 754  754  754  MET MET B . n 
C 1 755  LYS 755  755  755  LYS LYS B . n 
C 1 756  THR 756  756  756  THR THR B . n 
C 1 757  LEU 757  757  757  LEU LEU B . n 
C 1 758  LEU 758  758  758  LEU LEU B . n 
C 1 759  PRO 759  759  759  PRO PRO B . n 
C 1 760  VAL 760  760  760  VAL VAL B . n 
C 1 761  SER 761  761  761  SER SER B . n 
C 1 762  LYS 762  762  762  LYS LYS B . n 
C 1 763  PRO 763  763  763  PRO PRO B . n 
C 1 764  GLU 764  764  764  GLU GLU B . n 
C 1 765  ILE 765  765  765  ILE ILE B . n 
C 1 766  ARG 766  766  766  ARG ARG B . n 
C 1 767  SER 767  767  767  SER SER B . n 
C 1 768  TYR 768  768  768  TYR TYR B . n 
C 1 769  PHE 769  769  769  PHE PHE B . n 
C 1 770  PRO 770  770  770  PRO PRO B . n 
C 1 771  GLU 771  771  771  GLU GLU B . n 
C 1 772  SER 772  772  772  SER SER B . n 
C 1 773  TRP 773  773  773  TRP TRP B . n 
C 1 774  LEU 774  774  774  LEU LEU B . n 
C 1 775  TRP 775  775  775  TRP TRP B . n 
C 1 776  GLU 776  776  776  GLU GLU B . n 
C 1 777  VAL 777  777  777  VAL VAL B . n 
C 1 778  HIS 778  778  778  HIS HIS B . n 
C 1 779  LEU 779  779  779  LEU LEU B . n 
C 1 780  VAL 780  780  780  VAL VAL B . n 
C 1 781  PRO 781  781  781  PRO PRO B . n 
C 1 782  ARG 782  782  782  ARG ARG B . n 
C 1 783  ARG 783  783  783  ARG ARG B . n 
C 1 784  LYS 784  784  784  LYS LYS B . n 
C 1 785  GLN 785  785  785  GLN GLN B . n 
C 1 786  LEU 786  786  786  LEU LEU B . n 
C 1 787  GLN 787  787  787  GLN GLN B . n 
C 1 788  PHE 788  788  788  PHE PHE B . n 
C 1 789  ALA 789  789  789  ALA ALA B . n 
C 1 790  LEU 790  790  790  LEU LEU B . n 
C 1 791  PRO 791  791  791  PRO PRO B . n 
C 1 792  ASP 792  792  792  ASP ASP B . n 
C 1 793  SER 793  793  793  SER SER B . n 
C 1 794  LEU 794  794  794  LEU LEU B . n 
C 1 795  THR 795  795  795  THR THR B . n 
C 1 796  THR 796  796  796  THR THR B . n 
C 1 797  TRP 797  797  797  TRP TRP B . n 
C 1 798  GLU 798  798  798  GLU GLU B . n 
C 1 799  ILE 799  799  799  ILE ILE B . n 
C 1 800  GLN 800  800  800  GLN GLN B . n 
C 1 801  GLY 801  801  801  GLY GLY B . n 
C 1 802  ILE 802  802  802  ILE ILE B . n 
C 1 803  GLY 803  803  803  GLY GLY B . n 
C 1 804  ILE 804  804  804  ILE ILE B . n 
C 1 805  SER 805  805  805  SER SER B . n 
C 1 806  ASN 806  806  806  ASN ASN B . n 
C 1 807  THR 807  807  807  THR THR B . n 
C 1 808  GLY 808  808  808  GLY GLY B . n 
C 1 809  ILE 809  809  809  ILE ILE B . n 
C 1 810  CYS 810  810  810  CYS CYS B . n 
C 1 811  VAL 811  811  811  VAL VAL B . n 
C 1 812  ALA 812  812  812  ALA ALA B . n 
C 1 813  ASP 813  813  813  ASP ASP B . n 
C 1 814  THR 814  814  814  THR THR B . n 
C 1 815  VAL 815  815  815  VAL VAL B . n 
C 1 816  LYS 816  816  816  LYS LYS B . n 
C 1 817  ALA 817  817  817  ALA ALA B . n 
C 1 818  LYS 818  818  818  LYS LYS B . n 
C 1 819  VAL 819  819  819  VAL VAL B . n 
C 1 820  PHE 820  820  820  PHE PHE B . n 
C 1 821  LYS 821  821  821  LYS LYS B . n 
C 1 822  ASP 822  822  822  ASP ASP B . n 
C 1 823  VAL 823  823  823  VAL VAL B . n 
C 1 824  PHE 824  824  824  PHE PHE B . n 
C 1 825  LEU 825  825  825  LEU LEU B . n 
C 1 826  GLU 826  826  826  GLU GLU B . n 
C 1 827  MET 827  827  827  MET MET B . n 
C 1 828  ASN 828  828  828  ASN ASN B . n 
C 1 829  ILE 829  829  829  ILE ILE B . n 
C 1 830  PRO 830  830  830  PRO PRO B . n 
C 1 831  TYR 831  831  831  TYR TYR B . n 
C 1 832  SER 832  832  832  SER SER B . n 
C 1 833  VAL 833  833  833  VAL VAL B . n 
C 1 834  VAL 834  834  834  VAL VAL B . n 
C 1 835  ARG 835  835  835  ARG ARG B . n 
C 1 836  GLY 836  836  836  GLY GLY B . n 
C 1 837  GLU 837  837  837  GLU GLU B . n 
C 1 838  GLN 838  838  838  GLN GLN B . n 
C 1 839  ILE 839  839  839  ILE ILE B . n 
C 1 840  GLN 840  840  840  GLN GLN B . n 
C 1 841  LEU 841  841  841  LEU LEU B . n 
C 1 842  LYS 842  842  842  LYS LYS B . n 
C 1 843  GLY 843  843  843  GLY GLY B . n 
C 1 844  THR 844  844  844  THR THR B . n 
C 1 845  VAL 845  845  845  VAL VAL B . n 
C 1 846  TYR 846  846  846  TYR TYR B . n 
C 1 847  ASN 847  847  847  ASN ASN B . n 
C 1 848  TYR 848  848  848  TYR TYR B . n 
C 1 849  ARG 849  849  849  ARG ARG B . n 
C 1 850  THR 850  850  850  THR THR B . n 
C 1 851  SER 851  851  851  SER SER B . n 
C 1 852  GLY 852  852  852  GLY GLY B . n 
C 1 853  MET 853  853  853  MET MET B . n 
C 1 854  GLN 854  854  854  GLN GLN B . n 
C 1 855  PHE 855  855  855  PHE PHE B . n 
C 1 856  CYS 856  856  856  CYS CYS B . n 
C 1 857  VAL 857  857  857  VAL VAL B . n 
C 1 858  LYS 858  858  858  LYS LYS B . n 
C 1 859  MET 859  859  859  MET MET B . n 
C 1 860  SER 860  860  860  SER SER B . n 
C 1 861  ALA 861  861  861  ALA ALA B . n 
C 1 862  VAL 862  862  862  VAL VAL B . n 
C 1 863  GLU 863  863  863  GLU GLU B . n 
C 1 864  GLY 864  864  864  GLY GLY B . n 
C 1 865  ILE 865  865  865  ILE ILE B . n 
C 1 866  CYS 866  866  866  CYS CYS B . n 
C 1 867  THR 867  867  867  THR THR B . n 
C 1 868  SER 868  868  868  SER SER B . n 
C 1 869  GLU 869  869  869  GLU GLU B . n 
C 1 870  SER 870  870  870  SER SER B . n 
C 1 871  PRO 871  871  ?    ?   ?   B . n 
C 1 872  VAL 872  872  ?    ?   ?   B . n 
C 1 873  ILE 873  873  ?    ?   ?   B . n 
C 1 874  ASP 874  874  ?    ?   ?   B . n 
C 1 875  HIS 875  875  ?    ?   ?   B . n 
C 1 876  GLN 876  876  ?    ?   ?   B . n 
C 1 877  GLY 877  877  ?    ?   ?   B . n 
C 1 878  THR 878  878  ?    ?   ?   B . n 
C 1 879  LYS 879  879  ?    ?   ?   B . n 
C 1 880  SER 880  880  ?    ?   ?   B . n 
C 1 881  SER 881  881  ?    ?   ?   B . n 
C 1 882  LYS 882  882  882  LYS LYS B . n 
C 1 883  CYS 883  883  883  CYS CYS B . n 
C 1 884  VAL 884  884  884  VAL VAL B . n 
C 1 885  ARG 885  885  885  ARG ARG B . n 
C 1 886  GLN 886  886  886  GLN GLN B . n 
C 1 887  LYS 887  887  887  LYS LYS B . n 
C 1 888  VAL 888  888  888  VAL VAL B . n 
C 1 889  GLU 889  889  889  GLU GLU B . n 
C 1 890  GLY 890  890  890  GLY GLY B . n 
C 1 891  SER 891  891  891  SER SER B . n 
C 1 892  SER 892  892  892  SER SER B . n 
C 1 893  SER 893  893  893  SER SER B . n 
C 1 894  HIS 894  894  894  HIS HIS B . n 
C 1 895  LEU 895  895  895  LEU LEU B . n 
C 1 896  VAL 896  896  896  VAL VAL B . n 
C 1 897  THR 897  897  897  THR THR B . n 
C 1 898  PHE 898  898  898  PHE PHE B . n 
C 1 899  THR 899  899  899  THR THR B . n 
C 1 900  VAL 900  900  900  VAL VAL B . n 
C 1 901  LEU 901  901  901  LEU LEU B . n 
C 1 902  PRO 902  902  902  PRO PRO B . n 
C 1 903  LEU 903  903  903  LEU LEU B . n 
C 1 904  GLU 904  904  904  GLU GLU B . n 
C 1 905  ILE 905  905  905  ILE ILE B . n 
C 1 906  GLY 906  906  906  GLY GLY B . n 
C 1 907  LEU 907  907  907  LEU LEU B . n 
C 1 908  HIS 908  908  908  HIS HIS B . n 
C 1 909  ASN 909  909  909  ASN ASN B . n 
C 1 910  ILE 910  910  910  ILE ILE B . n 
C 1 911  ASN 911  911  911  ASN ASN B . n 
C 1 912  PHE 912  912  912  PHE PHE B . n 
C 1 913  SER 913  913  913  SER SER B . n 
C 1 914  LEU 914  914  914  LEU LEU B . n 
C 1 915  GLU 915  915  915  GLU GLU B . n 
C 1 916  THR 916  916  916  THR THR B . n 
C 1 917  TRP 917  917  917  TRP TRP B . n 
C 1 918  PHE 918  918  918  PHE PHE B . n 
C 1 919  GLY 919  919  919  GLY GLY B . n 
C 1 920  LYS 920  920  920  LYS LYS B . n 
C 1 921  GLU 921  921  921  GLU GLU B . n 
C 1 922  ILE 922  922  922  ILE ILE B . n 
C 1 923  LEU 923  923  923  LEU LEU B . n 
C 1 924  VAL 924  924  924  VAL VAL B . n 
C 1 925  LYS 925  925  925  LYS LYS B . n 
C 1 926  THR 926  926  926  THR THR B . n 
C 1 927  LEU 927  927  927  LEU LEU B . n 
C 1 928  ARG 928  928  928  ARG ARG B . n 
C 1 929  VAL 929  929  929  VAL VAL B . n 
C 1 930  VAL 930  930  930  VAL VAL B . n 
C 1 931  PRO 931  931  931  PRO PRO B . n 
C 1 932  GLU 932  932  932  GLU GLU B . n 
C 1 933  GLY 933  933  933  GLY GLY B . n 
C 1 934  VAL 934  934  934  VAL VAL B . n 
C 1 935  LYS 935  935  935  LYS LYS B . n 
C 1 936  ARG 936  936  936  ARG ARG B . n 
C 1 937  GLU 937  937  937  GLU GLU B . n 
C 1 938  SER 938  938  938  SER SER B . n 
C 1 939  TYR 939  939  939  TYR TYR B . n 
C 1 940  SER 940  940  940  SER SER B . n 
C 1 941  GLY 941  941  941  GLY GLY B . n 
C 1 942  VAL 942  942  942  VAL VAL B . n 
C 1 943  THR 943  943  943  THR THR B . n 
C 1 944  LEU 944  944  944  LEU LEU B . n 
C 1 945  ASP 945  945  945  ASP ASP B . n 
C 1 946  PRO 946  946  946  PRO PRO B . n 
C 1 947  ARG 947  947  947  ARG ARG B . n 
C 1 948  GLY 948  948  948  GLY GLY B . n 
C 1 949  ILE 949  949  949  ILE ILE B . n 
C 1 950  TYR 950  950  950  TYR TYR B . n 
C 1 951  GLY 951  951  951  GLY GLY B . n 
C 1 952  THR 952  952  952  THR THR B . n 
C 1 953  ILE 953  953  953  ILE ILE B . n 
C 1 954  SER 954  954  954  SER SER B . n 
C 1 955  ARG 955  955  955  ARG ARG B . n 
C 1 956  ARG 956  956  956  ARG ARG B . n 
C 1 957  LYS 957  957  957  LYS LYS B . n 
C 1 958  GLU 958  958  958  GLU GLU B . n 
C 1 959  PHE 959  959  959  PHE PHE B . n 
C 1 960  PRO 960  960  960  PRO PRO B . n 
C 1 961  TYR 961  961  961  TYR TYR B . n 
C 1 962  ARG 962  962  962  ARG ARG B . n 
C 1 963  ILE 963  963  963  ILE ILE B . n 
C 1 964  PRO 964  964  964  PRO PRO B . n 
C 1 965  LEU 965  965  965  LEU LEU B . n 
C 1 966  ASP 966  966  966  ASP ASP B . n 
C 1 967  LEU 967  967  967  LEU LEU B . n 
C 1 968  VAL 968  968  968  VAL VAL B . n 
C 1 969  PRO 969  969  969  PRO PRO B . n 
C 1 970  LYS 970  970  970  LYS LYS B . n 
C 1 971  THR 971  971  971  THR THR B . n 
C 1 972  GLU 972  972  972  GLU GLU B . n 
C 1 973  ILE 973  973  973  ILE ILE B . n 
C 1 974  LYS 974  974  974  LYS LYS B . n 
C 1 975  ARG 975  975  975  ARG ARG B . n 
C 1 976  ILE 976  976  976  ILE ILE B . n 
C 1 977  LEU 977  977  977  LEU LEU B . n 
C 1 978  SER 978  978  978  SER SER B . n 
C 1 979  VAL 979  979  979  VAL VAL B . n 
C 1 980  LYS 980  980  980  LYS LYS B . n 
C 1 981  GLY 981  981  981  GLY GLY B . n 
C 1 982  LEU 982  982  982  LEU LEU B . n 
C 1 983  LEU 983  983  983  LEU LEU B . n 
C 1 984  VAL 984  984  984  VAL VAL B . n 
C 1 985  GLY 985  985  985  GLY GLY B . n 
C 1 986  GLU 986  986  986  GLU GLU B . n 
C 1 987  ILE 987  987  987  ILE ILE B . n 
C 1 988  LEU 988  988  988  LEU LEU B . n 
C 1 989  SER 989  989  989  SER SER B . n 
C 1 990  ALA 990  990  990  ALA ALA B . n 
C 1 991  VAL 991  991  991  VAL VAL B . n 
C 1 992  LEU 992  992  992  LEU LEU B . n 
C 1 993  SER 993  993  993  SER SER B . n 
C 1 994  GLN 994  994  994  GLN GLN B . n 
C 1 995  GLU 995  995  995  GLU GLU B . n 
C 1 996  GLY 996  996  996  GLY GLY B . n 
C 1 997  ILE 997  997  997  ILE ILE B . n 
C 1 998  ASN 998  998  998  ASN ASN B . n 
C 1 999  ILE 999  999  999  ILE ILE B . n 
C 1 1000 LEU 1000 1000 1000 LEU LEU B . n 
C 1 1001 THR 1001 1001 1001 THR THR B . n 
C 1 1002 HIS 1002 1002 1002 HIS HIS B . n 
C 1 1003 LEU 1003 1003 1003 LEU LEU B . n 
C 1 1004 PRO 1004 1004 1004 PRO PRO B . n 
C 1 1005 LYS 1005 1005 1005 LYS LYS B . n 
C 1 1006 GLY 1006 1006 1006 GLY GLY B . n 
C 1 1007 SER 1007 1007 1007 SER SER B . n 
C 1 1008 ALA 1008 1008 1008 ALA ALA B . n 
C 1 1009 GLU 1009 1009 1009 GLU GLU B . n 
C 1 1010 ALA 1010 1010 1010 ALA ALA B . n 
C 1 1011 GLU 1011 1011 1011 GLU GLU B . n 
C 1 1012 LEU 1012 1012 1012 LEU LEU B . n 
C 1 1013 MET 1013 1013 1013 MET MET B . n 
C 1 1014 SER 1014 1014 1014 SER SER B . n 
C 1 1015 VAL 1015 1015 1015 VAL VAL B . n 
C 1 1016 VAL 1016 1016 1016 VAL VAL B . n 
C 1 1017 PRO 1017 1017 1017 PRO PRO B . n 
C 1 1018 VAL 1018 1018 1018 VAL VAL B . n 
C 1 1019 PHE 1019 1019 1019 PHE PHE B . n 
C 1 1020 TYR 1020 1020 1020 TYR TYR B . n 
C 1 1021 VAL 1021 1021 1021 VAL VAL B . n 
C 1 1022 PHE 1022 1022 1022 PHE PHE B . n 
C 1 1023 HIS 1023 1023 1023 HIS HIS B . n 
C 1 1024 TYR 1024 1024 1024 TYR TYR B . n 
C 1 1025 LEU 1025 1025 1025 LEU LEU B . n 
C 1 1026 GLU 1026 1026 1026 GLU GLU B . n 
C 1 1027 THR 1027 1027 1027 THR THR B . n 
C 1 1028 GLY 1028 1028 1028 GLY GLY B . n 
C 1 1029 ASN 1029 1029 1029 ASN ASN B . n 
C 1 1030 HIS 1030 1030 1030 HIS HIS B . n 
C 1 1031 TRP 1031 1031 1031 TRP TRP B . n 
C 1 1032 ASN 1032 1032 1032 ASN ASN B . n 
C 1 1033 ILE 1033 1033 1033 ILE ILE B . n 
C 1 1034 PHE 1034 1034 1034 PHE PHE B . n 
C 1 1035 HIS 1035 1035 1035 HIS HIS B . n 
C 1 1036 SER 1036 1036 1036 SER SER B . n 
C 1 1037 ASP 1037 1037 1037 ASP ASP B . n 
C 1 1038 PRO 1038 1038 1038 PRO PRO B . n 
C 1 1039 LEU 1039 1039 1039 LEU LEU B . n 
C 1 1040 ILE 1040 1040 1040 ILE ILE B . n 
C 1 1041 GLU 1041 1041 1041 GLU GLU B . n 
C 1 1042 LYS 1042 1042 1042 LYS LYS B . n 
C 1 1043 GLN 1043 1043 1043 GLN GLN B . n 
C 1 1044 LYS 1044 1044 1044 LYS LYS B . n 
C 1 1045 LEU 1045 1045 1045 LEU LEU B . n 
C 1 1046 LYS 1046 1046 1046 LYS LYS B . n 
C 1 1047 LYS 1047 1047 1047 LYS LYS B . n 
C 1 1048 LYS 1048 1048 1048 LYS LYS B . n 
C 1 1049 LEU 1049 1049 1049 LEU LEU B . n 
C 1 1050 LYS 1050 1050 1050 LYS LYS B . n 
C 1 1051 GLU 1051 1051 1051 GLU GLU B . n 
C 1 1052 GLY 1052 1052 1052 GLY GLY B . n 
C 1 1053 MET 1053 1053 1053 MET MET B . n 
C 1 1054 LEU 1054 1054 1054 LEU LEU B . n 
C 1 1055 SER 1055 1055 1055 SER SER B . n 
C 1 1056 ILE 1056 1056 1056 ILE ILE B . n 
C 1 1057 MET 1057 1057 1057 MET MET B . n 
C 1 1058 SER 1058 1058 1058 SER SER B . n 
C 1 1059 TYR 1059 1059 1059 TYR TYR B . n 
C 1 1060 ARG 1060 1060 1060 ARG ARG B . n 
C 1 1061 ASN 1061 1061 1061 ASN ASN B . n 
C 1 1062 ALA 1062 1062 1062 ALA ALA B . n 
C 1 1063 ASP 1063 1063 1063 ASP ASP B . n 
C 1 1064 TYR 1064 1064 1064 TYR TYR B . n 
C 1 1065 SER 1065 1065 1065 SER SER B . n 
C 1 1066 TYR 1066 1066 1066 TYR TYR B . n 
C 1 1067 SER 1067 1067 1067 SER SER B . n 
C 1 1068 VAL 1068 1068 1068 VAL VAL B . n 
C 1 1069 TRP 1069 1069 1069 TRP TRP B . n 
C 1 1070 LYS 1070 1070 1070 LYS LYS B . n 
C 1 1071 GLY 1071 1071 1071 GLY GLY B . n 
C 1 1072 GLY 1072 1072 1072 GLY GLY B . n 
C 1 1073 SER 1073 1073 1073 SER SER B . n 
C 1 1074 ALA 1074 1074 1074 ALA ALA B . n 
C 1 1075 SER 1075 1075 1075 SER SER B . n 
C 1 1076 THR 1076 1076 1076 THR THR B . n 
C 1 1077 TRP 1077 1077 1077 TRP TRP B . n 
C 1 1078 LEU 1078 1078 1078 LEU LEU B . n 
C 1 1079 THR 1079 1079 1079 THR THR B . n 
C 1 1080 ALA 1080 1080 1080 ALA ALA B . n 
C 1 1081 PHE 1081 1081 1081 PHE PHE B . n 
C 1 1082 ALA 1082 1082 1082 ALA ALA B . n 
C 1 1083 LEU 1083 1083 1083 LEU LEU B . n 
C 1 1084 ARG 1084 1084 1084 ARG ARG B . n 
C 1 1085 VAL 1085 1085 1085 VAL VAL B . n 
C 1 1086 LEU 1086 1086 1086 LEU LEU B . n 
C 1 1087 GLY 1087 1087 1087 GLY GLY B . n 
C 1 1088 GLN 1088 1088 1088 GLN GLN B . n 
C 1 1089 VAL 1089 1089 1089 VAL VAL B . n 
C 1 1090 ASN 1090 1090 1090 ASN ASN B . n 
C 1 1091 LYS 1091 1091 1091 LYS LYS B . n 
C 1 1092 TYR 1092 1092 1092 TYR TYR B . n 
C 1 1093 VAL 1093 1093 1093 VAL VAL B . n 
C 1 1094 GLU 1094 1094 1094 GLU GLU B . n 
C 1 1095 GLN 1095 1095 1095 GLN GLN B . n 
C 1 1096 ASN 1096 1096 1096 ASN ASN B . n 
C 1 1097 GLN 1097 1097 1097 GLN GLN B . n 
C 1 1098 ASN 1098 1098 1098 ASN ASN B . n 
C 1 1099 SER 1099 1099 1099 SER SER B . n 
C 1 1100 ILE 1100 1100 1100 ILE ILE B . n 
C 1 1101 CYS 1101 1101 1101 CYS CYS B . n 
C 1 1102 ASN 1102 1102 1102 ASN ASN B . n 
C 1 1103 SER 1103 1103 1103 SER SER B . n 
C 1 1104 LEU 1104 1104 1104 LEU LEU B . n 
C 1 1105 LEU 1105 1105 1105 LEU LEU B . n 
C 1 1106 TRP 1106 1106 1106 TRP TRP B . n 
C 1 1107 LEU 1107 1107 1107 LEU LEU B . n 
C 1 1108 VAL 1108 1108 1108 VAL VAL B . n 
C 1 1109 GLU 1109 1109 1109 GLU GLU B . n 
C 1 1110 ASN 1110 1110 1110 ASN ASN B . n 
C 1 1111 TYR 1111 1111 1111 TYR TYR B . n 
C 1 1112 GLN 1112 1112 1112 GLN GLN B . n 
C 1 1113 LEU 1113 1113 1113 LEU LEU B . n 
C 1 1114 ASP 1114 1114 1114 ASP ASP B . n 
C 1 1115 ASN 1115 1115 1115 ASN ASN B . n 
C 1 1116 GLY 1116 1116 1116 GLY GLY B . n 
C 1 1117 SER 1117 1117 1117 SER SER B . n 
C 1 1118 PHE 1118 1118 1118 PHE PHE B . n 
C 1 1119 LYS 1119 1119 1119 LYS LYS B . n 
C 1 1120 GLU 1120 1120 1120 GLU GLU B . n 
C 1 1121 ASN 1121 1121 1121 ASN ASN B . n 
C 1 1122 SER 1122 1122 1122 SER SER B . n 
C 1 1123 GLN 1123 1123 1123 GLN GLN B . n 
C 1 1124 TYR 1124 1124 1124 TYR TYR B . n 
C 1 1125 GLN 1125 1125 1125 GLN GLN B . n 
C 1 1126 PRO 1126 1126 1126 PRO PRO B . n 
C 1 1127 ILE 1127 1127 1127 ILE ILE B . n 
C 1 1128 LYS 1128 1128 1128 LYS LYS B . n 
C 1 1129 LEU 1129 1129 1129 LEU LEU B . n 
C 1 1130 GLN 1130 1130 1130 GLN GLN B . n 
C 1 1131 GLY 1131 1131 1131 GLY GLY B . n 
C 1 1132 THR 1132 1132 1132 THR THR B . n 
C 1 1133 LEU 1133 1133 1133 LEU LEU B . n 
C 1 1134 PRO 1134 1134 1134 PRO PRO B . n 
C 1 1135 VAL 1135 1135 1135 VAL VAL B . n 
C 1 1136 GLU 1136 1136 1136 GLU GLU B . n 
C 1 1137 ALA 1137 1137 1137 ALA ALA B . n 
C 1 1138 ARG 1138 1138 1138 ARG ARG B . n 
C 1 1139 GLU 1139 1139 1139 GLU GLU B . n 
C 1 1140 ASN 1140 1140 1140 ASN ASN B . n 
C 1 1141 SER 1141 1141 1141 SER SER B . n 
C 1 1142 LEU 1142 1142 1142 LEU LEU B . n 
C 1 1143 TYR 1143 1143 1143 TYR TYR B . n 
C 1 1144 LEU 1144 1144 1144 LEU LEU B . n 
C 1 1145 THR 1145 1145 1145 THR THR B . n 
C 1 1146 ALA 1146 1146 1146 ALA ALA B . n 
C 1 1147 PHE 1147 1147 1147 PHE PHE B . n 
C 1 1148 THR 1148 1148 1148 THR THR B . n 
C 1 1149 VAL 1149 1149 1149 VAL VAL B . n 
C 1 1150 ILE 1150 1150 1150 ILE ILE B . n 
C 1 1151 GLY 1151 1151 1151 GLY GLY B . n 
C 1 1152 ILE 1152 1152 1152 ILE ILE B . n 
C 1 1153 ARG 1153 1153 1153 ARG ARG B . n 
C 1 1154 LYS 1154 1154 1154 LYS LYS B . n 
C 1 1155 ALA 1155 1155 1155 ALA ALA B . n 
C 1 1156 PHE 1156 1156 1156 PHE PHE B . n 
C 1 1157 ASP 1157 1157 1157 ASP ASP B . n 
C 1 1158 ILE 1158 1158 1158 ILE ILE B . n 
C 1 1159 CYS 1159 1159 1159 CYS CYS B . n 
C 1 1160 PRO 1160 1160 1160 PRO PRO B . n 
C 1 1161 LEU 1161 1161 1161 LEU LEU B . n 
C 1 1162 VAL 1162 1162 1162 VAL VAL B . n 
C 1 1163 LYS 1163 1163 1163 LYS LYS B . n 
C 1 1164 ILE 1164 1164 1164 ILE ILE B . n 
C 1 1165 ASP 1165 1165 1165 ASP ASP B . n 
C 1 1166 THR 1166 1166 1166 THR THR B . n 
C 1 1167 ALA 1167 1167 1167 ALA ALA B . n 
C 1 1168 LEU 1168 1168 1168 LEU LEU B . n 
C 1 1169 ILE 1169 1169 1169 ILE ILE B . n 
C 1 1170 LYS 1170 1170 1170 LYS LYS B . n 
C 1 1171 ALA 1171 1171 1171 ALA ALA B . n 
C 1 1172 ASP 1172 1172 1172 ASP ASP B . n 
C 1 1173 ASN 1173 1173 1173 ASN ASN B . n 
C 1 1174 PHE 1174 1174 1174 PHE PHE B . n 
C 1 1175 LEU 1175 1175 1175 LEU LEU B . n 
C 1 1176 LEU 1176 1176 1176 LEU LEU B . n 
C 1 1177 GLU 1177 1177 1177 GLU GLU B . n 
C 1 1178 ASN 1178 1178 1178 ASN ASN B . n 
C 1 1179 THR 1179 1179 1179 THR THR B . n 
C 1 1180 LEU 1180 1180 1180 LEU LEU B . n 
C 1 1181 PRO 1181 1181 1181 PRO PRO B . n 
C 1 1182 ALA 1182 1182 1182 ALA ALA B . n 
C 1 1183 GLN 1183 1183 1183 GLN GLN B . n 
C 1 1184 SER 1184 1184 1184 SER SER B . n 
C 1 1185 THR 1185 1185 1185 THR THR B . n 
C 1 1186 PHE 1186 1186 1186 PHE PHE B . n 
C 1 1187 THR 1187 1187 1187 THR THR B . n 
C 1 1188 LEU 1188 1188 1188 LEU LEU B . n 
C 1 1189 ALA 1189 1189 1189 ALA ALA B . n 
C 1 1190 ILE 1190 1190 1190 ILE ILE B . n 
C 1 1191 SER 1191 1191 1191 SER SER B . n 
C 1 1192 ALA 1192 1192 1192 ALA ALA B . n 
C 1 1193 TYR 1193 1193 1193 TYR TYR B . n 
C 1 1194 ALA 1194 1194 1194 ALA ALA B . n 
C 1 1195 LEU 1195 1195 1195 LEU LEU B . n 
C 1 1196 SER 1196 1196 1196 SER SER B . n 
C 1 1197 LEU 1197 1197 1197 LEU LEU B . n 
C 1 1198 GLY 1198 1198 1198 GLY GLY B . n 
C 1 1199 ASP 1199 1199 1199 ASP ASP B . n 
C 1 1200 LYS 1200 1200 1200 LYS LYS B . n 
C 1 1201 THR 1201 1201 1201 THR THR B . n 
C 1 1202 HIS 1202 1202 1202 HIS HIS B . n 
C 1 1203 PRO 1203 1203 1203 PRO PRO B . n 
C 1 1204 GLN 1204 1204 1204 GLN GLN B . n 
C 1 1205 PHE 1205 1205 1205 PHE PHE B . n 
C 1 1206 ARG 1206 1206 1206 ARG ARG B . n 
C 1 1207 SER 1207 1207 1207 SER SER B . n 
C 1 1208 ILE 1208 1208 1208 ILE ILE B . n 
C 1 1209 VAL 1209 1209 1209 VAL VAL B . n 
C 1 1210 SER 1210 1210 1210 SER SER B . n 
C 1 1211 ALA 1211 1211 1211 ALA ALA B . n 
C 1 1212 LEU 1212 1212 1212 LEU LEU B . n 
C 1 1213 LYS 1213 1213 1213 LYS LYS B . n 
C 1 1214 ARG 1214 1214 1214 ARG ARG B . n 
C 1 1215 GLU 1215 1215 1215 GLU GLU B . n 
C 1 1216 ALA 1216 1216 1216 ALA ALA B . n 
C 1 1217 LEU 1217 1217 1217 LEU LEU B . n 
C 1 1218 VAL 1218 1218 1218 VAL VAL B . n 
C 1 1219 LYS 1219 1219 1219 LYS LYS B . n 
C 1 1220 GLY 1220 1220 1220 GLY GLY B . n 
C 1 1221 ASN 1221 1221 1221 ASN ASN B . n 
C 1 1222 PRO 1222 1222 1222 PRO PRO B . n 
C 1 1223 PRO 1223 1223 1223 PRO PRO B . n 
C 1 1224 ILE 1224 1224 1224 ILE ILE B . n 
C 1 1225 TYR 1225 1225 1225 TYR TYR B . n 
C 1 1226 ARG 1226 1226 1226 ARG ARG B . n 
C 1 1227 PHE 1227 1227 1227 PHE PHE B . n 
C 1 1228 TRP 1228 1228 1228 TRP TRP B . n 
C 1 1229 LYS 1229 1229 1229 LYS LYS B . n 
C 1 1230 ASP 1230 1230 1230 ASP ASP B . n 
C 1 1231 ASN 1231 1231 1231 ASN ASN B . n 
C 1 1232 LEU 1232 1232 1232 LEU LEU B . n 
C 1 1233 GLN 1233 1233 1233 GLN GLN B . n 
C 1 1234 HIS 1234 1234 1234 HIS HIS B . n 
C 1 1235 LYS 1235 1235 1235 LYS LYS B . n 
C 1 1236 ASP 1236 1236 1236 ASP ASP B . n 
C 1 1237 SER 1237 1237 1237 SER SER B . n 
C 1 1238 SER 1238 1238 1238 SER SER B . n 
C 1 1239 VAL 1239 1239 1239 VAL VAL B . n 
C 1 1240 PRO 1240 1240 1240 PRO PRO B . n 
C 1 1241 ASN 1241 1241 1241 ASN ASN B . n 
C 1 1242 THR 1242 1242 1242 THR THR B . n 
C 1 1243 GLY 1243 1243 1243 GLY GLY B . n 
C 1 1244 THR 1244 1244 1244 THR THR B . n 
C 1 1245 ALA 1245 1245 1245 ALA ALA B . n 
C 1 1246 ARG 1246 1246 1246 ARG ARG B . n 
C 1 1247 MET 1247 1247 1247 MET MET B . n 
C 1 1248 VAL 1248 1248 1248 VAL VAL B . n 
C 1 1249 GLU 1249 1249 1249 GLU GLU B . n 
C 1 1250 THR 1250 1250 1250 THR THR B . n 
C 1 1251 THR 1251 1251 1251 THR THR B . n 
C 1 1252 ALA 1252 1252 1252 ALA ALA B . n 
C 1 1253 TYR 1253 1253 1253 TYR TYR B . n 
C 1 1254 ALA 1254 1254 1254 ALA ALA B . n 
C 1 1255 LEU 1255 1255 1255 LEU LEU B . n 
C 1 1256 LEU 1256 1256 1256 LEU LEU B . n 
C 1 1257 THR 1257 1257 1257 THR THR B . n 
C 1 1258 SER 1258 1258 1258 SER SER B . n 
C 1 1259 LEU 1259 1259 1259 LEU LEU B . n 
C 1 1260 ASN 1260 1260 1260 ASN ASN B . n 
C 1 1261 LEU 1261 1261 1261 LEU LEU B . n 
C 1 1262 LYS 1262 1262 1262 LYS LYS B . n 
C 1 1263 ASP 1263 1263 1263 ASP ASP B . n 
C 1 1264 ILE 1264 1264 1264 ILE ILE B . n 
C 1 1265 ASN 1265 1265 1265 ASN ASN B . n 
C 1 1266 TYR 1266 1266 1266 TYR TYR B . n 
C 1 1267 VAL 1267 1267 1267 VAL VAL B . n 
C 1 1268 ASN 1268 1268 1268 ASN ASN B . n 
C 1 1269 PRO 1269 1269 1269 PRO PRO B . n 
C 1 1270 VAL 1270 1270 1270 VAL VAL B . n 
C 1 1271 ILE 1271 1271 1271 ILE ILE B . n 
C 1 1272 LYS 1272 1272 1272 LYS LYS B . n 
C 1 1273 TRP 1273 1273 1273 TRP TRP B . n 
C 1 1274 LEU 1274 1274 1274 LEU LEU B . n 
C 1 1275 SER 1275 1275 1275 SER SER B . n 
C 1 1276 GLU 1276 1276 1276 GLU GLU B . n 
C 1 1277 GLU 1277 1277 1277 GLU GLU B . n 
C 1 1278 GLN 1278 1278 1278 GLN GLN B . n 
C 1 1279 ARG 1279 1279 1279 ARG ARG B . n 
C 1 1280 TYR 1280 1280 1280 TYR TYR B . n 
C 1 1281 GLY 1281 1281 1281 GLY GLY B . n 
C 1 1282 GLY 1282 1282 1282 GLY GLY B . n 
C 1 1283 GLY 1283 1283 1283 GLY GLY B . n 
C 1 1284 PHE 1284 1284 1284 PHE PHE B . n 
C 1 1285 TYR 1285 1285 1285 TYR TYR B . n 
C 1 1286 SER 1286 1286 1286 SER SER B . n 
C 1 1287 THR 1287 1287 1287 THR THR B . n 
C 1 1288 GLN 1288 1288 1288 GLN GLN B . n 
C 1 1289 ASP 1289 1289 1289 ASP ASP B . n 
C 1 1290 THR 1290 1290 1290 THR THR B . n 
C 1 1291 ILE 1291 1291 1291 ILE ILE B . n 
C 1 1292 ASN 1292 1292 1292 ASN ASN B . n 
C 1 1293 ALA 1293 1293 1293 ALA ALA B . n 
C 1 1294 ILE 1294 1294 1294 ILE ILE B . n 
C 1 1295 GLU 1295 1295 1295 GLU GLU B . n 
C 1 1296 GLY 1296 1296 1296 GLY GLY B . n 
C 1 1297 LEU 1297 1297 1297 LEU LEU B . n 
C 1 1298 THR 1298 1298 1298 THR THR B . n 
C 1 1299 GLU 1299 1299 1299 GLU GLU B . n 
C 1 1300 TYR 1300 1300 1300 TYR TYR B . n 
C 1 1301 SER 1301 1301 1301 SER SER B . n 
C 1 1302 LEU 1302 1302 1302 LEU LEU B . n 
C 1 1303 LEU 1303 1303 1303 LEU LEU B . n 
C 1 1304 VAL 1304 1304 1304 VAL VAL B . n 
C 1 1305 LYS 1305 1305 1305 LYS LYS B . n 
C 1 1306 GLN 1306 1306 1306 GLN GLN B . n 
C 1 1307 LEU 1307 1307 1307 LEU LEU B . n 
C 1 1308 ARG 1308 1308 1308 ARG ARG B . n 
C 1 1309 LEU 1309 1309 1309 LEU LEU B . n 
C 1 1310 SER 1310 1310 1310 SER SER B . n 
C 1 1311 MET 1311 1311 1311 MET MET B . n 
C 1 1312 ASP 1312 1312 1312 ASP ASP B . n 
C 1 1313 ILE 1313 1313 1313 ILE ILE B . n 
C 1 1314 ASP 1314 1314 1314 ASP ASP B . n 
C 1 1315 VAL 1315 1315 1315 VAL VAL B . n 
C 1 1316 SER 1316 1316 1316 SER SER B . n 
C 1 1317 TYR 1317 1317 1317 TYR TYR B . n 
C 1 1318 LYS 1318 1318 1318 LYS LYS B . n 
C 1 1319 HIS 1319 1319 1319 HIS HIS B . n 
C 1 1320 LYS 1320 1320 1320 LYS LYS B . n 
C 1 1321 GLY 1321 1321 1321 GLY GLY B . n 
C 1 1322 ALA 1322 1322 1322 ALA ALA B . n 
C 1 1323 LEU 1323 1323 1323 LEU LEU B . n 
C 1 1324 HIS 1324 1324 1324 HIS HIS B . n 
C 1 1325 ASN 1325 1325 1325 ASN ASN B . n 
C 1 1326 TYR 1326 1326 1326 TYR TYR B . n 
C 1 1327 LYS 1327 1327 1327 LYS LYS B . n 
C 1 1328 MET 1328 1328 1328 MET MET B . n 
C 1 1329 THR 1329 1329 1329 THR THR B . n 
C 1 1330 ASP 1330 1330 1330 ASP ASP B . n 
C 1 1331 LYS 1331 1331 1331 LYS LYS B . n 
C 1 1332 ASN 1332 1332 1332 ASN ASN B . n 
C 1 1333 PHE 1333 1333 1333 PHE PHE B . n 
C 1 1334 LEU 1334 1334 1334 LEU LEU B . n 
C 1 1335 GLY 1335 1335 1335 GLY GLY B . n 
C 1 1336 ARG 1336 1336 1336 ARG ARG B . n 
C 1 1337 PRO 1337 1337 1337 PRO PRO B . n 
C 1 1338 VAL 1338 1338 1338 VAL VAL B . n 
C 1 1339 GLU 1339 1339 1339 GLU GLU B . n 
C 1 1340 VAL 1340 1340 1340 VAL VAL B . n 
C 1 1341 LEU 1341 1341 1341 LEU LEU B . n 
C 1 1342 LEU 1342 1342 1342 LEU LEU B . n 
C 1 1343 ASN 1343 1343 1343 ASN ASN B . n 
C 1 1344 ASP 1344 1344 1344 ASP ASP B . n 
C 1 1345 ASP 1345 1345 1345 ASP ASP B . n 
C 1 1346 LEU 1346 1346 1346 LEU LEU B . n 
C 1 1347 ILE 1347 1347 1347 ILE ILE B . n 
C 1 1348 VAL 1348 1348 1348 VAL VAL B . n 
C 1 1349 SER 1349 1349 1349 SER SER B . n 
C 1 1350 THR 1350 1350 1350 THR THR B . n 
C 1 1351 GLY 1351 1351 1351 GLY GLY B . n 
C 1 1352 PHE 1352 1352 1352 PHE PHE B . n 
C 1 1353 GLY 1353 1353 1353 GLY GLY B . n 
C 1 1354 SER 1354 1354 1354 SER SER B . n 
C 1 1355 GLY 1355 1355 1355 GLY GLY B . n 
C 1 1356 LEU 1356 1356 1356 LEU LEU B . n 
C 1 1357 ALA 1357 1357 1357 ALA ALA B . n 
C 1 1358 THR 1358 1358 1358 THR THR B . n 
C 1 1359 VAL 1359 1359 1359 VAL VAL B . n 
C 1 1360 HIS 1360 1360 1360 HIS HIS B . n 
C 1 1361 VAL 1361 1361 1361 VAL VAL B . n 
C 1 1362 THR 1362 1362 1362 THR THR B . n 
C 1 1363 THR 1363 1363 1363 THR THR B . n 
C 1 1364 VAL 1364 1364 1364 VAL VAL B . n 
C 1 1365 VAL 1365 1365 1365 VAL VAL B . n 
C 1 1366 HIS 1366 1366 1366 HIS HIS B . n 
C 1 1367 LYS 1367 1367 1367 LYS LYS B . n 
C 1 1368 THR 1368 1368 1368 THR THR B . n 
C 1 1369 SER 1369 1369 1369 SER SER B . n 
C 1 1370 THR 1370 1370 1370 THR THR B . n 
C 1 1371 SER 1371 1371 1371 SER SER B . n 
C 1 1372 GLU 1372 1372 1372 GLU GLU B . n 
C 1 1373 GLU 1373 1373 1373 GLU GLU B . n 
C 1 1374 VAL 1374 1374 1374 VAL VAL B . n 
C 1 1375 CYS 1375 1375 1375 CYS CYS B . n 
C 1 1376 SER 1376 1376 1376 SER SER B . n 
C 1 1377 PHE 1377 1377 1377 PHE PHE B . n 
C 1 1378 TYR 1378 1378 1378 TYR TYR B . n 
C 1 1379 LEU 1379 1379 1379 LEU LEU B . n 
C 1 1380 LYS 1380 1380 1380 LYS LYS B . n 
C 1 1381 ILE 1381 1381 1381 ILE ILE B . n 
C 1 1382 ASP 1382 1382 1382 ASP ASP B . n 
C 1 1383 THR 1383 1383 1383 THR THR B . n 
C 1 1384 GLN 1384 1384 1384 GLN GLN B . n 
C 1 1385 ASP 1385 1385 1385 ASP ASP B . n 
C 1 1386 ILE 1386 1386 1386 ILE ILE B . n 
C 1 1387 GLU 1387 1387 ?    ?   ?   B . n 
C 1 1388 ALA 1388 1388 ?    ?   ?   B . n 
C 1 1389 SER 1389 1389 ?    ?   ?   B . n 
C 1 1390 HIS 1390 1390 ?    ?   ?   B . n 
C 1 1391 TYR 1391 1391 ?    ?   ?   B . n 
C 1 1392 ARG 1392 1392 ?    ?   ?   B . n 
C 1 1393 GLY 1393 1393 ?    ?   ?   B . n 
C 1 1394 TYR 1394 1394 ?    ?   ?   B . n 
C 1 1395 GLY 1395 1395 ?    ?   ?   B . n 
C 1 1396 ASN 1396 1396 ?    ?   ?   B . n 
C 1 1397 SER 1397 1397 ?    ?   ?   B . n 
C 1 1398 ASP 1398 1398 ?    ?   ?   B . n 
C 1 1399 TYR 1399 1399 1399 TYR TYR B . n 
C 1 1400 LYS 1400 1400 1400 LYS LYS B . n 
C 1 1401 ARG 1401 1401 1401 ARG ARG B . n 
C 1 1402 ILE 1402 1402 1402 ILE ILE B . n 
C 1 1403 VAL 1403 1403 1403 VAL VAL B . n 
C 1 1404 ALA 1404 1404 1404 ALA ALA B . n 
C 1 1405 CYS 1405 1405 1405 CYS CYS B . n 
C 1 1406 ALA 1406 1406 1406 ALA ALA B . n 
C 1 1407 SER 1407 1407 1407 SER SER B . n 
C 1 1408 TYR 1408 1408 1408 TYR TYR B . n 
C 1 1409 LYS 1409 1409 1409 LYS LYS B . n 
C 1 1410 PRO 1410 1410 1410 PRO PRO B . n 
C 1 1411 SER 1411 1411 1411 SER SER B . n 
C 1 1412 ARG 1412 1412 1412 ARG ARG B . n 
C 1 1413 GLU 1413 1413 1413 GLU GLU B . n 
C 1 1414 GLU 1414 1414 1414 GLU GLU B . n 
C 1 1415 SER 1415 1415 1415 SER SER B . n 
C 1 1416 SER 1416 1416 1416 SER SER B . n 
C 1 1417 SER 1417 1417 1417 SER SER B . n 
C 1 1418 GLY 1418 1418 1418 GLY GLY B . n 
C 1 1419 SER 1419 1419 1419 SER SER B . n 
C 1 1420 SER 1420 1420 1420 SER SER B . n 
C 1 1421 HIS 1421 1421 1421 HIS HIS B . n 
C 1 1422 ALA 1422 1422 1422 ALA ALA B . n 
C 1 1423 VAL 1423 1423 1423 VAL VAL B . n 
C 1 1424 MET 1424 1424 1424 MET MET B . n 
C 1 1425 ASP 1425 1425 1425 ASP ASP B . n 
C 1 1426 ILE 1426 1426 1426 ILE ILE B . n 
C 1 1427 SER 1427 1427 1427 SER SER B . n 
C 1 1428 LEU 1428 1428 1428 LEU LEU B . n 
C 1 1429 PRO 1429 1429 1429 PRO PRO B . n 
C 1 1430 THR 1430 1430 1430 THR THR B . n 
C 1 1431 GLY 1431 1431 1431 GLY GLY B . n 
C 1 1432 ILE 1432 1432 1432 ILE ILE B . n 
C 1 1433 SER 1433 1433 1433 SER SER B . n 
C 1 1434 ALA 1434 1434 1434 ALA ALA B . n 
C 1 1435 ASN 1435 1435 1435 ASN ASN B . n 
C 1 1436 GLU 1436 1436 1436 GLU GLU B . n 
C 1 1437 GLU 1437 1437 1437 GLU GLU B . n 
C 1 1438 ASP 1438 1438 1438 ASP ASP B . n 
C 1 1439 LEU 1439 1439 1439 LEU LEU B . n 
C 1 1440 LYS 1440 1440 1440 LYS LYS B . n 
C 1 1441 ALA 1441 1441 1441 ALA ALA B . n 
C 1 1442 LEU 1442 1442 1442 LEU LEU B . n 
C 1 1443 VAL 1443 1443 1443 VAL VAL B . n 
C 1 1444 GLU 1444 1444 1444 GLU GLU B . n 
C 1 1445 GLY 1445 1445 1445 GLY GLY B . n 
C 1 1446 VAL 1446 1446 1446 VAL VAL B . n 
C 1 1447 ASP 1447 1447 1447 ASP ASP B . n 
C 1 1448 GLN 1448 1448 1448 GLN GLN B . n 
C 1 1449 LEU 1449 1449 1449 LEU LEU B . n 
C 1 1450 PHE 1450 1450 1450 PHE PHE B . n 
C 1 1451 THR 1451 1451 1451 THR THR B . n 
C 1 1452 ASP 1452 1452 1452 ASP ASP B . n 
C 1 1453 TYR 1453 1453 1453 TYR TYR B . n 
C 1 1454 GLN 1454 1454 1454 GLN GLN B . n 
C 1 1455 ILE 1455 1455 1455 ILE ILE B . n 
C 1 1456 LYS 1456 1456 1456 LYS LYS B . n 
C 1 1457 ASP 1457 1457 1457 ASP ASP B . n 
C 1 1458 GLY 1458 1458 1458 GLY GLY B . n 
C 1 1459 HIS 1459 1459 1459 HIS HIS B . n 
C 1 1460 VAL 1460 1460 1460 VAL VAL B . n 
C 1 1461 ILE 1461 1461 1461 ILE ILE B . n 
C 1 1462 LEU 1462 1462 1462 LEU LEU B . n 
C 1 1463 GLN 1463 1463 1463 GLN GLN B . n 
C 1 1464 LEU 1464 1464 1464 LEU LEU B . n 
C 1 1465 ASN 1465 1465 1465 ASN ASN B . n 
C 1 1466 SER 1466 1466 1466 SER SER B . n 
C 1 1467 ILE 1467 1467 1467 ILE ILE B . n 
C 1 1468 PRO 1468 1468 1468 PRO PRO B . n 
C 1 1469 SER 1469 1469 1469 SER SER B . n 
C 1 1470 SER 1470 1470 1470 SER SER B . n 
C 1 1471 ASP 1471 1471 1471 ASP ASP B . n 
C 1 1472 PHE 1472 1472 1472 PHE PHE B . n 
C 1 1473 LEU 1473 1473 1473 LEU LEU B . n 
C 1 1474 CYS 1474 1474 1474 CYS CYS B . n 
C 1 1475 VAL 1475 1475 1475 VAL VAL B . n 
C 1 1476 ARG 1476 1476 1476 ARG ARG B . n 
C 1 1477 PHE 1477 1477 1477 PHE PHE B . n 
C 1 1478 ARG 1478 1478 1478 ARG ARG B . n 
C 1 1479 ILE 1479 1479 1479 ILE ILE B . n 
C 1 1480 PHE 1480 1480 1480 PHE PHE B . n 
C 1 1481 GLU 1481 1481 1481 GLU GLU B . n 
C 1 1482 LEU 1482 1482 1482 LEU LEU B . n 
C 1 1483 PHE 1483 1483 1483 PHE PHE B . n 
C 1 1484 GLU 1484 1484 1484 GLU GLU B . n 
C 1 1485 VAL 1485 1485 1485 VAL VAL B . n 
C 1 1486 GLY 1486 1486 1486 GLY GLY B . n 
C 1 1487 PHE 1487 1487 1487 PHE PHE B . n 
C 1 1488 LEU 1488 1488 1488 LEU LEU B . n 
C 1 1489 SER 1489 1489 1489 SER SER B . n 
C 1 1490 PRO 1490 1490 1490 PRO PRO B . n 
C 1 1491 ALA 1491 1491 1491 ALA ALA B . n 
C 1 1492 THR 1492 1492 1492 THR THR B . n 
C 1 1493 PHE 1493 1493 1493 PHE PHE B . n 
C 1 1494 THR 1494 1494 1494 THR THR B . n 
C 1 1495 VAL 1495 1495 1495 VAL VAL B . n 
C 1 1496 TYR 1496 1496 1496 TYR TYR B . n 
C 1 1497 GLU 1497 1497 1497 GLU GLU B . n 
C 1 1498 TYR 1498 1498 1498 TYR TYR B . n 
C 1 1499 HIS 1499 1499 1499 HIS HIS B . n 
C 1 1500 ARG 1500 1500 1500 ARG ARG B . n 
C 1 1501 PRO 1501 1501 1501 PRO PRO B . n 
C 1 1502 ASP 1502 1502 1502 ASP ASP B . n 
C 1 1503 LYS 1503 1503 1503 LYS LYS B . n 
C 1 1504 GLN 1504 1504 1504 GLN GLN B . n 
C 1 1505 CYS 1505 1505 1505 CYS CYS B . n 
C 1 1506 THR 1506 1506 1506 THR THR B . n 
C 1 1507 MET 1507 1507 1507 MET MET B . n 
C 1 1508 PHE 1508 1508 1508 PHE PHE B . n 
C 1 1509 TYR 1509 1509 1509 TYR TYR B . n 
C 1 1510 SER 1510 1510 1510 SER SER B . n 
C 1 1511 THR 1511 1511 1511 THR THR B . n 
C 1 1512 SER 1512 1512 1512 SER SER B . n 
C 1 1513 ASN 1513 1513 1513 ASN ASN B . n 
C 1 1514 ILE 1514 1514 1514 ILE ILE B . n 
C 1 1515 LYS 1515 1515 1515 LYS LYS B . n 
C 1 1516 ILE 1516 1516 1516 ILE ILE B . n 
C 1 1517 GLN 1517 1517 1517 GLN GLN B . n 
C 1 1518 LYS 1518 1518 1518 LYS LYS B . n 
C 1 1519 VAL 1519 1519 1519 VAL VAL B . n 
C 1 1520 CYS 1520 1520 1520 CYS CYS B . n 
C 1 1521 GLU 1521 1521 1521 GLU GLU B . n 
C 1 1522 GLY 1522 1522 1522 GLY GLY B . n 
C 1 1523 ALA 1523 1523 1523 ALA ALA B . n 
C 1 1524 ALA 1524 1524 1524 ALA ALA B . n 
C 1 1525 CYS 1525 1525 1525 CYS CYS B . n 
C 1 1526 LYS 1526 1526 1526 LYS LYS B . n 
C 1 1527 CYS 1527 1527 1527 CYS CYS B . n 
C 1 1528 VAL 1528 1528 1528 VAL VAL B . n 
C 1 1529 GLU 1529 1529 1529 GLU GLU B . n 
C 1 1530 ALA 1530 1530 1530 ALA ALA B . n 
C 1 1531 ASP 1531 1531 1531 ASP ASP B . n 
C 1 1532 CYS 1532 1532 1532 CYS CYS B . n 
C 1 1533 GLY 1533 1533 ?    ?   ?   B . n 
C 1 1534 GLN 1534 1534 ?    ?   ?   B . n 
C 1 1535 MET 1535 1535 ?    ?   ?   B . n 
C 1 1536 GLN 1536 1536 ?    ?   ?   B . n 
C 1 1537 GLU 1537 1537 ?    ?   ?   B . n 
C 1 1538 GLU 1538 1538 ?    ?   ?   B . n 
C 1 1539 LEU 1539 1539 ?    ?   ?   B . n 
C 1 1540 ASP 1540 1540 ?    ?   ?   B . n 
C 1 1541 LEU 1541 1541 ?    ?   ?   B . n 
C 1 1542 THR 1542 1542 ?    ?   ?   B . n 
C 1 1543 ILE 1543 1543 ?    ?   ?   B . n 
C 1 1544 SER 1544 1544 ?    ?   ?   B . n 
C 1 1545 ALA 1545 1545 ?    ?   ?   B . n 
C 1 1546 GLU 1546 1546 ?    ?   ?   B . n 
C 1 1547 THR 1547 1547 ?    ?   ?   B . n 
C 1 1548 ARG 1548 1548 ?    ?   ?   B . n 
C 1 1549 LYS 1549 1549 ?    ?   ?   B . n 
C 1 1550 GLN 1550 1550 ?    ?   ?   B . n 
C 1 1551 THR 1551 1551 ?    ?   ?   B . n 
C 1 1552 ALA 1552 1552 ?    ?   ?   B . n 
C 1 1553 CYS 1553 1553 ?    ?   ?   B . n 
C 1 1554 LYS 1554 1554 ?    ?   ?   B . n 
C 1 1555 PRO 1555 1555 ?    ?   ?   B . n 
C 1 1556 GLU 1556 1556 ?    ?   ?   B . n 
C 1 1557 ILE 1557 1557 ?    ?   ?   B . n 
C 1 1558 ALA 1558 1558 ?    ?   ?   B . n 
C 1 1559 TYR 1559 1559 ?    ?   ?   B . n 
C 1 1560 ALA 1560 1560 ?    ?   ?   B . n 
C 1 1561 TYR 1561 1561 ?    ?   ?   B . n 
C 1 1562 LYS 1562 1562 ?    ?   ?   B . n 
C 1 1563 VAL 1563 1563 ?    ?   ?   B . n 
C 1 1564 SER 1564 1564 ?    ?   ?   B . n 
C 1 1565 ILE 1565 1565 ?    ?   ?   B . n 
C 1 1566 THR 1566 1566 ?    ?   ?   B . n 
C 1 1567 SER 1567 1567 ?    ?   ?   B . n 
C 1 1568 ILE 1568 1568 ?    ?   ?   B . n 
C 1 1569 THR 1569 1569 ?    ?   ?   B . n 
C 1 1570 VAL 1570 1570 ?    ?   ?   B . n 
C 1 1571 GLU 1571 1571 ?    ?   ?   B . n 
C 1 1572 ASN 1572 1572 ?    ?   ?   B . n 
C 1 1573 VAL 1573 1573 ?    ?   ?   B . n 
C 1 1574 PHE 1574 1574 ?    ?   ?   B . n 
C 1 1575 VAL 1575 1575 ?    ?   ?   B . n 
C 1 1576 LYS 1576 1576 ?    ?   ?   B . n 
C 1 1577 TYR 1577 1577 ?    ?   ?   B . n 
C 1 1578 LYS 1578 1578 ?    ?   ?   B . n 
C 1 1579 ALA 1579 1579 ?    ?   ?   B . n 
C 1 1580 THR 1580 1580 ?    ?   ?   B . n 
C 1 1581 LEU 1581 1581 ?    ?   ?   B . n 
C 1 1582 LEU 1582 1582 ?    ?   ?   B . n 
C 1 1583 ASP 1583 1583 ?    ?   ?   B . n 
C 1 1584 ILE 1584 1584 ?    ?   ?   B . n 
C 1 1585 TYR 1585 1585 ?    ?   ?   B . n 
C 1 1586 LYS 1586 1586 ?    ?   ?   B . n 
C 1 1587 THR 1587 1587 ?    ?   ?   B . n 
C 1 1588 GLY 1588 1588 ?    ?   ?   B . n 
C 1 1589 GLU 1589 1589 ?    ?   ?   B . n 
C 1 1590 ALA 1590 1590 ?    ?   ?   B . n 
C 1 1591 VAL 1591 1591 ?    ?   ?   B . n 
C 1 1592 ALA 1592 1592 ?    ?   ?   B . n 
C 1 1593 GLU 1593 1593 ?    ?   ?   B . n 
C 1 1594 LYS 1594 1594 ?    ?   ?   B . n 
C 1 1595 ASP 1595 1595 ?    ?   ?   B . n 
C 1 1596 SER 1596 1596 ?    ?   ?   B . n 
C 1 1597 GLU 1597 1597 ?    ?   ?   B . n 
C 1 1598 ILE 1598 1598 ?    ?   ?   B . n 
C 1 1599 THR 1599 1599 ?    ?   ?   B . n 
C 1 1600 PHE 1600 1600 ?    ?   ?   B . n 
C 1 1601 ILE 1601 1601 ?    ?   ?   B . n 
C 1 1602 LYS 1602 1602 ?    ?   ?   B . n 
C 1 1603 LYS 1603 1603 ?    ?   ?   B . n 
C 1 1604 VAL 1604 1604 ?    ?   ?   B . n 
C 1 1605 THR 1605 1605 ?    ?   ?   B . n 
C 1 1606 CYS 1606 1606 ?    ?   ?   B . n 
C 1 1607 THR 1607 1607 ?    ?   ?   B . n 
C 1 1608 ASN 1608 1608 ?    ?   ?   B . n 
C 1 1609 ALA 1609 1609 ?    ?   ?   B . n 
C 1 1610 GLU 1610 1610 ?    ?   ?   B . n 
C 1 1611 LEU 1611 1611 ?    ?   ?   B . n 
C 1 1612 VAL 1612 1612 ?    ?   ?   B . n 
C 1 1613 LYS 1613 1613 ?    ?   ?   B . n 
C 1 1614 GLY 1614 1614 ?    ?   ?   B . n 
C 1 1615 ARG 1615 1615 ?    ?   ?   B . n 
C 1 1616 GLN 1616 1616 ?    ?   ?   B . n 
C 1 1617 TYR 1617 1617 ?    ?   ?   B . n 
C 1 1618 LEU 1618 1618 ?    ?   ?   B . n 
C 1 1619 ILE 1619 1619 ?    ?   ?   B . n 
C 1 1620 MET 1620 1620 ?    ?   ?   B . n 
C 1 1621 GLY 1621 1621 ?    ?   ?   B . n 
C 1 1622 LYS 1622 1622 ?    ?   ?   B . n 
C 1 1623 GLU 1623 1623 ?    ?   ?   B . n 
C 1 1624 ALA 1624 1624 ?    ?   ?   B . n 
C 1 1625 LEU 1625 1625 ?    ?   ?   B . n 
C 1 1626 GLN 1626 1626 ?    ?   ?   B . n 
C 1 1627 ILE 1627 1627 ?    ?   ?   B . n 
C 1 1628 LYS 1628 1628 ?    ?   ?   B . n 
C 1 1629 TYR 1629 1629 ?    ?   ?   B . n 
C 1 1630 ASN 1630 1630 ?    ?   ?   B . n 
C 1 1631 PHE 1631 1631 ?    ?   ?   B . n 
C 1 1632 SER 1632 1632 ?    ?   ?   B . n 
C 1 1633 PHE 1633 1633 ?    ?   ?   B . n 
C 1 1634 ARG 1634 1634 ?    ?   ?   B . n 
C 1 1635 TYR 1635 1635 ?    ?   ?   B . n 
C 1 1636 ILE 1636 1636 ?    ?   ?   B . n 
C 1 1637 TYR 1637 1637 ?    ?   ?   B . n 
C 1 1638 PRO 1638 1638 ?    ?   ?   B . n 
C 1 1639 LEU 1639 1639 ?    ?   ?   B . n 
C 1 1640 ASP 1640 1640 ?    ?   ?   B . n 
C 1 1641 SER 1641 1641 ?    ?   ?   B . n 
C 1 1642 LEU 1642 1642 ?    ?   ?   B . n 
C 1 1643 THR 1643 1643 ?    ?   ?   B . n 
C 1 1644 TRP 1644 1644 ?    ?   ?   B . n 
C 1 1645 ILE 1645 1645 ?    ?   ?   B . n 
C 1 1646 GLU 1646 1646 ?    ?   ?   B . n 
C 1 1647 TYR 1647 1647 ?    ?   ?   B . n 
C 1 1648 TRP 1648 1648 ?    ?   ?   B . n 
C 1 1649 PRO 1649 1649 ?    ?   ?   B . n 
C 1 1650 ARG 1650 1650 ?    ?   ?   B . n 
C 1 1651 ASP 1651 1651 ?    ?   ?   B . n 
C 1 1652 THR 1652 1652 ?    ?   ?   B . n 
C 1 1653 THR 1653 1653 ?    ?   ?   B . n 
C 1 1654 CYS 1654 1654 ?    ?   ?   B . n 
C 1 1655 SER 1655 1655 ?    ?   ?   B . n 
C 1 1656 SER 1656 1656 ?    ?   ?   B . n 
C 1 1657 CYS 1657 1657 ?    ?   ?   B . n 
C 1 1658 GLN 1658 1658 ?    ?   ?   B . n 
C 1 1659 ALA 1659 1659 ?    ?   ?   B . n 
C 1 1660 PHE 1660 1660 ?    ?   ?   B . n 
C 1 1661 LEU 1661 1661 ?    ?   ?   B . n 
C 1 1662 ALA 1662 1662 ?    ?   ?   B . n 
C 1 1663 ASN 1663 1663 ?    ?   ?   B . n 
C 1 1664 LEU 1664 1664 ?    ?   ?   B . n 
C 1 1665 ASP 1665 1665 ?    ?   ?   B . n 
C 1 1666 GLU 1666 1666 ?    ?   ?   B . n 
C 1 1667 PHE 1667 1667 ?    ?   ?   B . n 
C 1 1668 ALA 1668 1668 ?    ?   ?   B . n 
C 1 1669 GLU 1669 1669 ?    ?   ?   B . n 
C 1 1670 ASP 1670 1670 ?    ?   ?   B . n 
C 1 1671 ILE 1671 1671 ?    ?   ?   B . n 
C 1 1672 PHE 1672 1672 ?    ?   ?   B . n 
C 1 1673 LEU 1673 1673 ?    ?   ?   B . n 
C 1 1674 ASN 1674 1674 ?    ?   ?   B . n 
C 1 1675 GLY 1675 1675 ?    ?   ?   B . n 
C 1 1676 CYS 1676 1676 ?    ?   ?   B . n 
D 2 1    MET 1    1    ?    ?   ?   Y . n 
D 2 2    LYS 2    2    ?    ?   ?   Y . n 
D 2 3    LEU 3    3    ?    ?   ?   Y . n 
D 2 4    LYS 4    4    ?    ?   ?   Y . n 
D 2 5    THR 5    5    ?    ?   ?   Y . n 
D 2 6    LEU 6    6    ?    ?   ?   Y . n 
D 2 7    ALA 7    7    ?    ?   ?   Y . n 
D 2 8    LYS 8    8    ?    ?   ?   Y . n 
D 2 9    ALA 9    9    ?    ?   ?   Y . n 
D 2 10   THR 10   10   ?    ?   ?   Y . n 
D 2 11   LEU 11   11   ?    ?   ?   Y . n 
D 2 12   ALA 12   12   ?    ?   ?   Y . n 
D 2 13   LEU 13   13   ?    ?   ?   Y . n 
D 2 14   GLY 14   14   ?    ?   ?   Y . n 
D 2 15   LEU 15   15   ?    ?   ?   Y . n 
D 2 16   LEU 16   16   ?    ?   ?   Y . n 
D 2 17   THR 17   17   ?    ?   ?   Y . n 
D 2 18   THR 18   18   ?    ?   ?   Y . n 
D 2 19   GLY 19   19   ?    ?   ?   Y . n 
D 2 20   VAL 20   20   ?    ?   ?   Y . n 
D 2 21   ILE 21   21   ?    ?   ?   Y . n 
D 2 22   THR 22   22   ?    ?   ?   Y . n 
D 2 23   SER 23   23   ?    ?   ?   Y . n 
D 2 24   GLU 24   24   ?    ?   ?   Y . n 
D 2 25   GLY 25   25   ?    ?   ?   Y . n 
D 2 26   GLN 26   26   ?    ?   ?   Y . n 
D 2 27   ALA 27   27   ?    ?   ?   Y . n 
D 2 28   VAL 28   28   ?    ?   ?   Y . n 
D 2 29   GLN 29   29   ?    ?   ?   Y . n 
D 2 30   ALA 30   30   ?    ?   ?   Y . n 
D 2 31   ALA 31   31   ?    ?   ?   Y . n 
D 2 32   GLU 32   32   ?    ?   ?   Y . n 
D 2 33   LYS 33   33   ?    ?   ?   Y . n 
D 2 34   GLN 34   34   ?    ?   ?   Y . n 
D 2 35   GLY 35   35   ?    ?   ?   Y . n 
D 2 36   ARG 36   36   ?    ?   ?   Y . n 
D 2 37   VAL 37   37   ?    ?   ?   Y . n 
D 2 38   GLN 38   38   ?    ?   ?   Y . n 
D 2 39   HIS 39   39   ?    ?   ?   Y . n 
D 2 40   LEU 40   40   40   LEU LEU Y . n 
D 2 41   HIS 41   41   41   HIS HIS Y . n 
D 2 42   ASP 42   42   42   ASP ASP Y . n 
D 2 43   ILE 43   43   43   ILE ILE Y . n 
D 2 44   ARG 44   44   44   ARG ARG Y . n 
D 2 45   ASP 45   45   45   ASP ASP Y . n 
D 2 46   LEU 46   46   46   LEU LEU Y . n 
D 2 47   HIS 47   47   47   HIS HIS Y . n 
D 2 48   ARG 48   48   48   ARG ARG Y . n 
D 2 49   TYR 49   49   49   TYR TYR Y . n 
D 2 50   TYR 50   50   50   TYR TYR Y . n 
D 2 51   SER 51   51   51   SER SER Y . n 
D 2 52   SER 52   52   52   SER SER Y . n 
D 2 53   GLU 53   53   53   GLU GLU Y . n 
D 2 54   SER 54   54   54   SER SER Y . n 
D 2 55   PHE 55   55   55   PHE PHE Y . n 
D 2 56   GLU 56   56   56   GLU GLU Y . n 
D 2 57   TYR 57   57   57   TYR TYR Y . n 
D 2 58   SER 58   58   58   SER SER Y . n 
D 2 59   ASN 59   59   59   ASN ASN Y . n 
D 2 60   VAL 60   60   60   VAL VAL Y . n 
D 2 61   SER 61   61   61   SER SER Y . n 
D 2 62   GLY 62   62   62   GLY GLY Y . n 
D 2 63   LYS 63   63   63   LYS LYS Y . n 
D 2 64   VAL 64   64   64   VAL VAL Y . n 
D 2 65   GLU 65   65   65   GLU GLU Y . n 
D 2 66   ASN 66   66   66   ASN ASN Y . n 
D 2 67   TYR 67   67   67   TYR TYR Y . n 
D 2 68   ASN 68   68   68   ASN ASN Y . n 
D 2 69   GLY 69   69   69   GLY GLY Y . n 
D 2 70   SER 70   70   70   SER SER Y . n 
D 2 71   ASN 71   71   71   ASN ASN Y . n 
D 2 72   VAL 72   72   72   VAL VAL Y . n 
D 2 73   VAL 73   73   73   VAL VAL Y . n 
D 2 74   ARG 74   74   74   ARG ARG Y . n 
D 2 75   PHE 75   75   75   PHE PHE Y . n 
D 2 76   ASN 76   76   76   ASN ASN Y . n 
D 2 77   PRO 77   77   77   PRO PRO Y . n 
D 2 78   LYS 78   78   78   LYS LYS Y . n 
D 2 79   ASP 79   79   79   ASP ASP Y . n 
D 2 80   GLN 80   80   80   GLN GLN Y . n 
D 2 81   ASN 81   81   81   ASN ASN Y . n 
D 2 82   HIS 82   82   82   HIS HIS Y . n 
D 2 83   GLN 83   83   83   GLN GLN Y . n 
D 2 84   LEU 84   84   84   LEU LEU Y . n 
D 2 85   PHE 85   85   85   PHE PHE Y . n 
D 2 86   LEU 86   86   86   LEU LEU Y . n 
D 2 87   LEU 87   87   87   LEU LEU Y . n 
D 2 88   GLY 88   88   88   GLY GLY Y . n 
D 2 89   LYS 89   89   89   LYS LYS Y . n 
D 2 90   ASP 90   90   90   ASP ASP Y . n 
D 2 91   LYS 91   91   91   LYS LYS Y . n 
D 2 92   GLU 92   92   92   GLU GLU Y . n 
D 2 93   GLN 93   93   93   GLN GLN Y . n 
D 2 94   TYR 94   94   94   TYR TYR Y . n 
D 2 95   LYS 95   95   95   LYS LYS Y . n 
D 2 96   GLU 96   96   96   GLU GLU Y . n 
D 2 97   GLY 97   97   97   GLY GLY Y . n 
D 2 98   LEU 98   98   98   LEU LEU Y . n 
D 2 99   GLN 99   99   99   GLN GLN Y . n 
D 2 100  GLY 100  100  100  GLY GLY Y . n 
D 2 101  GLN 101  101  101  GLN GLN Y . n 
D 2 102  ASN 102  102  102  ASN ASN Y . n 
D 2 103  VAL 103  103  103  VAL VAL Y . n 
D 2 104  PHE 104  104  104  PHE PHE Y . n 
D 2 105  VAL 105  105  105  VAL VAL Y . n 
D 2 106  VAL 106  106  106  VAL VAL Y . n 
D 2 107  GLN 107  107  107  GLN GLN Y . n 
D 2 108  GLU 108  108  108  GLU GLU Y . n 
D 2 109  LEU 109  109  109  LEU LEU Y . n 
D 2 110  ILE 110  110  110  ILE ILE Y . n 
D 2 111  ASP 111  111  111  ASP ASP Y . n 
D 2 112  PRO 112  112  112  PRO PRO Y . n 
D 2 113  ASN 113  113  113  ASN ASN Y . n 
D 2 114  GLY 114  114  114  GLY GLY Y . n 
D 2 115  ARG 115  115  115  ARG ARG Y . n 
D 2 116  LEU 116  116  116  LEU LEU Y . n 
D 2 117  SER 117  117  117  SER SER Y . n 
D 2 118  THR 118  118  118  THR THR Y . n 
D 2 119  VAL 119  119  119  VAL VAL Y . n 
D 2 120  GLY 120  120  120  GLY GLY Y . n 
D 2 121  GLY 121  121  121  GLY GLY Y . n 
D 2 122  VAL 122  122  122  VAL VAL Y . n 
D 2 123  THR 123  123  123  THR THR Y . n 
D 2 124  LYS 124  124  124  LYS LYS Y . n 
D 2 125  LYS 125  125  125  LYS LYS Y . n 
D 2 126  ASN 126  126  126  ASN ASN Y . n 
D 2 127  ASN 127  127  127  ASN ASN Y . n 
D 2 128  LYS 128  128  128  LYS LYS Y . n 
D 2 129  THR 129  129  129  THR THR Y . n 
D 2 130  SER 130  130  130  SER SER Y . n 
D 2 131  GLU 131  131  131  GLU GLU Y . n 
D 2 132  THR 132  132  132  THR THR Y . n 
D 2 133  ASN 133  133  133  ASN ASN Y . n 
D 2 134  THR 134  134  134  THR THR Y . n 
D 2 135  PRO 135  135  135  PRO PRO Y . n 
D 2 136  LEU 136  136  136  LEU LEU Y . n 
D 2 137  PHE 137  137  137  PHE PHE Y . n 
D 2 138  VAL 138  138  138  VAL VAL Y . n 
D 2 139  ASN 139  139  139  ASN ASN Y . n 
D 2 140  LYS 140  140  140  LYS LYS Y . n 
D 2 141  VAL 141  141  141  VAL VAL Y . n 
D 2 142  ASN 142  142  142  ASN ASN Y . n 
D 2 143  GLY 143  143  143  GLY GLY Y . n 
D 2 144  GLU 144  144  144  GLU GLU Y . n 
D 2 145  ASP 145  145  145  ASP ASP Y . n 
D 2 146  LEU 146  146  146  LEU LEU Y . n 
D 2 147  ASP 147  147  147  ASP ASP Y . n 
D 2 148  ALA 148  148  148  ALA ALA Y . n 
D 2 149  SER 149  149  149  SER SER Y . n 
D 2 150  ILE 150  150  150  ILE ILE Y . n 
D 2 151  ASP 151  151  151  ASP ASP Y . n 
D 2 152  SER 152  152  152  SER SER Y . n 
D 2 153  PHE 153  153  153  PHE PHE Y . n 
D 2 154  LEU 154  154  154  LEU LEU Y . n 
D 2 155  ILE 155  155  155  ILE ILE Y . n 
D 2 156  GLN 156  156  156  GLN GLN Y . n 
D 2 157  LYS 157  157  157  LYS LYS Y . n 
D 2 158  GLU 158  158  158  GLU GLU Y . n 
D 2 159  GLU 159  159  159  GLU GLU Y . n 
D 2 160  ILE 160  160  160  ILE ILE Y . n 
D 2 161  SER 161  161  161  SER SER Y . n 
D 2 162  LEU 162  162  162  LEU LEU Y . n 
D 2 163  LYS 163  163  163  LYS LYS Y . n 
D 2 164  GLU 164  164  164  GLU GLU Y . n 
D 2 165  LEU 165  165  165  LEU LEU Y . n 
D 2 166  ASP 166  166  166  ASP ASP Y . n 
D 2 167  PHE 167  167  167  PHE PHE Y . n 
D 2 168  LYS 168  168  168  LYS LYS Y . n 
D 2 169  ILE 169  169  169  ILE ILE Y . n 
D 2 170  ARG 170  170  170  ARG ARG Y . n 
D 2 171  GLN 171  171  171  GLN GLN Y . n 
D 2 172  GLN 172  172  172  GLN GLN Y . n 
D 2 173  LEU 173  173  173  LEU LEU Y . n 
D 2 174  VAL 174  174  174  VAL VAL Y . n 
D 2 175  ASN 175  175  175  ASN ASN Y . n 
D 2 176  ASN 176  176  176  ASN ASN Y . n 
D 2 177  TYR 177  177  177  TYR TYR Y . n 
D 2 178  GLY 178  178  178  GLY GLY Y . n 
D 2 179  LEU 179  179  179  LEU LEU Y . n 
D 2 180  TYR 180  180  180  TYR TYR Y . n 
D 2 181  LYS 181  181  181  LYS LYS Y . n 
D 2 182  GLY 182  182  182  GLY GLY Y . n 
D 2 183  THR 183  183  183  THR THR Y . n 
D 2 184  SER 184  184  184  SER SER Y . n 
D 2 185  LYS 185  185  185  LYS LYS Y . n 
D 2 186  TYR 186  186  186  TYR TYR Y . n 
D 2 187  GLY 187  187  187  GLY GLY Y . n 
D 2 188  LYS 188  188  188  LYS LYS Y . n 
D 2 189  ILE 189  189  189  ILE ILE Y . n 
D 2 190  ILE 190  190  190  ILE ILE Y . n 
D 2 191  ILE 191  191  191  ILE ILE Y . n 
D 2 192  ASN 192  192  192  ASN ASN Y . n 
D 2 193  LEU 193  193  193  LEU LEU Y . n 
D 2 194  LYS 194  194  194  LYS LYS Y . n 
D 2 195  ASP 195  195  195  ASP ASP Y . n 
D 2 196  GLU 196  196  196  GLU GLU Y . n 
D 2 197  ASN 197  197  197  ASN ASN Y . n 
D 2 198  LYS 198  198  198  LYS LYS Y . n 
D 2 199  VAL 199  199  199  VAL VAL Y . n 
D 2 200  GLU 200  200  200  GLU GLU Y . n 
D 2 201  ILE 201  201  201  ILE ILE Y . n 
D 2 202  ASP 202  202  202  ASP ASP Y . n 
D 2 203  LEU 203  203  203  LEU LEU Y . n 
D 2 204  GLY 204  204  204  GLY GLY Y . n 
D 2 205  ASP 205  205  205  ASP ASP Y . n 
D 2 206  LYS 206  206  206  LYS LYS Y . n 
D 2 207  LEU 207  207  207  LEU LEU Y . n 
D 2 208  GLN 208  208  208  GLN GLN Y . n 
D 2 209  PHE 209  209  209  PHE PHE Y . n 
D 2 210  GLU 210  210  210  GLU GLU Y . n 
D 2 211  ARG 211  211  211  ARG ARG Y . n 
D 2 212  MET 212  212  212  MET MET Y . n 
D 2 213  GLY 213  213  213  GLY GLY Y . n 
D 2 214  ASP 214  214  214  ASP ASP Y . n 
D 2 215  VAL 215  215  215  VAL VAL Y . n 
D 2 216  LEU 216  216  216  LEU LEU Y . n 
D 2 217  ASN 217  217  217  ASN ASN Y . n 
D 2 218  SER 218  218  218  SER SER Y . n 
D 2 219  LYS 219  219  219  LYS LYS Y . n 
D 2 220  ASP 220  220  220  ASP ASP Y . n 
D 2 221  ILE 221  221  221  ILE ILE Y . n 
D 2 222  ARG 222  222  222  ARG ARG Y . n 
D 2 223  GLY 223  223  223  GLY GLY Y . n 
D 2 224  ILE 224  224  224  ILE ILE Y . n 
D 2 225  SER 225  225  225  SER SER Y . n 
D 2 226  VAL 226  226  226  VAL VAL Y . n 
D 2 227  THR 227  227  227  THR THR Y . n 
D 2 228  ILE 228  228  228  ILE ILE Y . n 
D 2 229  ASN 229  229  229  ASN ASN Y . n 
D 2 230  GLN 230  230  230  GLN GLN Y . n 
D 2 231  ILE 231  231  ?    ?   ?   Y . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 3 CD  1 1677 1    CD  CD  A . 
F 4 NAG 1 2001 2001 NAG NAG A . 
G 4 NAG 2 2002 2002 NAG NAG A . 
H 3 CD  1 1678 2    CD  CD  A . 
I 3 CD  1 1679 3    CD  CD  A . 
J 3 CD  1 1680 4    CD  CD  A . 
K 3 CD  1 1681 5    CD  CD  A . 
L 4 NAG 1 1682 1    NAG NAG A . 
M 4 NAG 1 2001 2001 NAG NAG B . 
N 4 NAG 2 2002 2002 NAG NAG B . 
O 3 CD  1 1677 2    CD  CD  B . 
P 3 CD  1 1678 3    CD  CD  B . 
Q 3 CD  1 1679 4    CD  CD  B . 
R 3 CD  1 1680 5    CD  CD  B . 
S 4 NAG 1 1681 1    NAG NAG B . 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A ASN 741 A ASN 741 ? ASN 'GLYCOSYLATION SITE' 
2 A ASN 911 A ASN 911 ? ASN 'GLYCOSYLATION SITE' 
3 C ASN 741 B ASN 741 ? ASN 'GLYCOSYLATION SITE' 
4 C ASN 911 B ASN 911 ? ASN 'GLYCOSYLATION SITE' 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,E,F,G,H,I,J,K,L 
2 1 C,D,M,N,O,P,Q,R,S   
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2920  ? 
1 MORE         -27   ? 
1 'SSA (A^2)'  83390 ? 
2 'ABSA (A^2)' 2920  ? 
2 MORE         -24   ? 
2 'SSA (A^2)'  75780 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OE2 ? A GLU 247  ? A GLU 247  ? 1_555 CD ? E CD . ? A CD 1677 ? 1_555 OE2 ? C GLU 247  ? B GLU 247  ? 1_555 136.8 ? 
2  OD2 ? A ASP 264  ? A ASP 264  ? 1_555 CD ? I CD . ? A CD 1679 ? 1_555 ND1 ? A HIS 753  ? A HIS 753  ? 1_555 106.5 ? 
3  OE1 ? A GLU 339  ? A GLU 339  ? 1_555 CD ? J CD . ? A CD 1680 ? 1_555 OE1 ? A GLU 764  ? A GLU 764  ? 1_555 77.8  ? 
4  OE1 ? A GLU 339  ? A GLU 339  ? 1_555 CD ? J CD . ? A CD 1680 ? 1_555 OE2 ? A GLU 764  ? A GLU 764  ? 1_555 62.4  ? 
5  OE1 ? A GLU 764  ? A GLU 764  ? 1_555 CD ? J CD . ? A CD 1680 ? 1_555 OE2 ? A GLU 764  ? A GLU 764  ? 1_555 57.5  ? 
6  OD1 ? A ASP 471  ? A ASP 471  ? 1_555 CD ? H CD . ? A CD 1678 ? 1_555 OD2 ? A ASP 471  ? A ASP 471  ? 1_555 54.5  ? 
7  OD1 ? A ASP 471  ? A ASP 471  ? 1_555 CD ? H CD . ? A CD 1678 ? 1_555 OE1 ? A GLU 480  ? A GLU 480  ? 1_555 112.7 ? 
8  OD2 ? A ASP 471  ? A ASP 471  ? 1_555 CD ? H CD . ? A CD 1678 ? 1_555 OE1 ? A GLU 480  ? A GLU 480  ? 1_555 166.2 ? 
9  OD1 ? A ASP 471  ? A ASP 471  ? 1_555 CD ? H CD . ? A CD 1678 ? 1_555 OE2 ? A GLU 480  ? A GLU 480  ? 1_555 81.9  ? 
10 OD2 ? A ASP 471  ? A ASP 471  ? 1_555 CD ? H CD . ? A CD 1678 ? 1_555 OE2 ? A GLU 480  ? A GLU 480  ? 1_555 122.1 ? 
11 OE1 ? A GLU 480  ? A GLU 480  ? 1_555 CD ? H CD . ? A CD 1678 ? 1_555 OE2 ? A GLU 480  ? A GLU 480  ? 1_555 54.9  ? 
12 OE1 ? A GLN 886  ? A GLN 886  ? 1_555 CD ? K CD . ? A CD 1681 ? 1_555 OE1 ? A GLU 1589 ? A GLU 1589 ? 1_555 59.1  ? 
13 OE1 ? A GLN 886  ? A GLN 886  ? 1_555 CD ? K CD . ? A CD 1681 ? 1_555 OE2 ? A GLU 1589 ? A GLU 1589 ? 1_555 89.8  ? 
14 OE1 ? A GLU 1589 ? A GLU 1589 ? 1_555 CD ? K CD . ? A CD 1681 ? 1_555 OE2 ? A GLU 1589 ? A GLU 1589 ? 1_555 55.1  ? 
15 OE1 ? A GLN 886  ? A GLN 886  ? 1_555 CD ? K CD . ? A CD 1681 ? 1_555 NE2 ? A HIS 894  ? A HIS 894  ? 1_555 92.3  ? 
16 OE1 ? A GLU 1589 ? A GLU 1589 ? 1_555 CD ? K CD . ? A CD 1681 ? 1_555 NE2 ? A HIS 894  ? A HIS 894  ? 1_555 142.1 ? 
17 OE2 ? A GLU 1589 ? A GLU 1589 ? 1_555 CD ? K CD . ? A CD 1681 ? 1_555 NE2 ? A HIS 894  ? A HIS 894  ? 1_555 157.7 ? 
18 OE1 ? A GLU 1666 ? A GLU 1666 ? 1_555 CD ? R CD . ? B CD 1680 ? 1_555 OE2 ? A GLU 1666 ? A GLU 1666 ? 1_555 55.5  ? 
19 OE1 ? A GLU 1666 ? A GLU 1666 ? 1_555 CD ? R CD . ? B CD 1680 ? 1_555 OE1 ? C GLN 886  ? B GLN 886  ? 1_555 71.4  ? 
20 OE2 ? A GLU 1666 ? A GLU 1666 ? 1_555 CD ? R CD . ? B CD 1680 ? 1_555 OE1 ? C GLN 886  ? B GLN 886  ? 1_555 90.9  ? 
21 OD2 ? C ASP 264  ? B ASP 264  ? 1_555 CD ? P CD . ? B CD 1678 ? 1_555 ND1 ? C HIS 753  ? B HIS 753  ? 1_555 103.8 ? 
22 OE1 ? C GLU 339  ? B GLU 339  ? 1_555 CD ? Q CD . ? B CD 1679 ? 1_555 OE1 ? C GLU 764  ? B GLU 764  ? 1_555 77.7  ? 
23 OE1 ? C GLU 339  ? B GLU 339  ? 1_555 CD ? Q CD . ? B CD 1679 ? 1_555 OE2 ? C GLU 764  ? B GLU 764  ? 1_555 62.1  ? 
24 OE1 ? C GLU 764  ? B GLU 764  ? 1_555 CD ? Q CD . ? B CD 1679 ? 1_555 OE2 ? C GLU 764  ? B GLU 764  ? 1_555 57.2  ? 
25 OD1 ? C ASP 471  ? B ASP 471  ? 1_555 CD ? O CD . ? B CD 1677 ? 1_555 OD2 ? C ASP 471  ? B ASP 471  ? 1_555 54.6  ? 
26 OD1 ? C ASP 471  ? B ASP 471  ? 1_555 CD ? O CD . ? B CD 1677 ? 1_555 OE1 ? C GLU 480  ? B GLU 480  ? 1_555 114.5 ? 
27 OD2 ? C ASP 471  ? B ASP 471  ? 1_555 CD ? O CD . ? B CD 1677 ? 1_555 OE1 ? C GLU 480  ? B GLU 480  ? 1_555 168.9 ? 
28 OD1 ? C ASP 471  ? B ASP 471  ? 1_555 CD ? O CD . ? B CD 1677 ? 1_555 OE2 ? C GLU 480  ? B GLU 480  ? 1_555 82.8  ? 
29 OD2 ? C ASP 471  ? B ASP 471  ? 1_555 CD ? O CD . ? B CD 1677 ? 1_555 OE2 ? C GLU 480  ? B GLU 480  ? 1_555 120.7 ? 
30 OE1 ? C GLU 480  ? B GLU 480  ? 1_555 CD ? O CD . ? B CD 1677 ? 1_555 OE2 ? C GLU 480  ? B GLU 480  ? 1_555 55.2  ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2009-11-24 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2018-05-30 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Source and taxonomy'       
2 2 'Structure model' 'Version format compliance' 
3 3 'Structure model' 'Data collection'           
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    3 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            diffrn_source 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    3 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_diffrn_source.pdbx_synchrotron_site' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
_software.date 
_software.type 
_software.location 
_software.language 
MAR345dtb 'data collection' .                 ? 1 ? ? ? ? 
PHASER    phasing           .                 ? 2 ? ? ? ? 
PHENIX    refinement        '(phenix.refine)' ? 3 ? ? ? ? 
XDS       'data reduction'  .                 ? 4 ? ? ? ? 
XSCALE    'data scaling'    .                 ? 5 ? ? ? ? 
# 
_pdbx_entry_details.entry_id             3KLS 
_pdbx_entry_details.nonpolymer_details   ? 
_pdbx_entry_details.sequence_details     '802TH IS ILE IN THIS ENTRY, WHICH IS A NATURAL VARIANT REFERRED IN P01031 IN UNIPROT.' 
_pdbx_entry_details.compound_details     ? 
_pdbx_entry_details.source_details       ? 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    NH2 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    ARG 
_pdbx_validate_symm_contact.auth_seq_id_1     955 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    OD1 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    ASN 
_pdbx_validate_symm_contact.auth_seq_id_2     434 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   3_454 
_pdbx_validate_symm_contact.dist              2.19 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 C  A THR 359  ? ? N  A PRO 360  ? ? CA A PRO 360  ? ? 131.22 119.30 11.92  1.50 Y 
2  1 C  A TYR 369  ? ? N  A PRO 370  ? ? CA A PRO 370  ? ? 132.99 119.30 13.69  1.50 Y 
3  1 C  A TYR 369  ? ? N  A PRO 370  ? ? CD A PRO 370  ? ? 114.11 128.40 -14.29 2.10 Y 
4  1 C  A VAL 535  ? ? N  A PRO 536  ? ? CA A PRO 536  ? ? 108.08 119.30 -11.22 1.50 Y 
5  1 C  A PHE 769  ? ? N  A PRO 770  ? ? CA A PRO 770  ? ? 129.44 119.30 10.14  1.50 Y 
6  1 C  A LEU 1003 ? ? N  A PRO 1004 ? ? CA A PRO 1004 ? ? 135.07 119.30 15.77  1.50 Y 
7  1 C  A LEU 1003 ? ? N  A PRO 1004 ? ? CD A PRO 1004 ? ? 114.71 128.40 -13.69 2.10 Y 
8  1 CA A LEU 1303 ? ? CB A LEU 1303 ? ? CG A LEU 1303 ? ? 129.68 115.30 14.38  2.30 N 
9  1 N  A PHE 1487 ? ? CA A PHE 1487 ? ? CB A PHE 1487 ? ? 124.62 110.60 14.02  1.80 N 
10 1 C  A ARG 1500 ? ? N  A PRO 1501 ? ? CA A PRO 1501 ? ? 131.21 119.30 11.91  1.50 Y 
11 1 C  B THR 359  ? ? N  B PRO 360  ? ? CA B PRO 360  ? ? 131.03 119.30 11.73  1.50 Y 
12 1 C  B TYR 369  ? ? N  B PRO 370  ? ? CA B PRO 370  ? ? 132.87 119.30 13.57  1.50 Y 
13 1 C  B TYR 369  ? ? N  B PRO 370  ? ? CD B PRO 370  ? ? 114.67 128.40 -13.72 2.10 Y 
14 1 C  B VAL 535  ? ? N  B PRO 536  ? ? CA B PRO 536  ? ? 108.04 119.30 -11.26 1.50 Y 
15 1 C  B PHE 769  ? ? N  B PRO 770  ? ? CA B PRO 770  ? ? 129.25 119.30 9.95   1.50 Y 
16 1 C  B LEU 1003 ? ? N  B PRO 1004 ? ? CA B PRO 1004 ? ? 135.08 119.30 15.78  1.50 Y 
17 1 C  B LEU 1003 ? ? N  B PRO 1004 ? ? CD B PRO 1004 ? ? 115.06 128.40 -13.34 2.10 Y 
18 1 CA B LEU 1303 ? ? CB B LEU 1303 ? ? CG B LEU 1303 ? ? 129.56 115.30 14.26  2.30 N 
19 1 C  B ARG 1500 ? ? N  B PRO 1501 ? ? CA B PRO 1501 ? ? 131.26 119.30 11.96  1.50 Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1   1 PRO A 28   ? ? -48.03  163.07  
2   1 TYR A 46   ? ? -55.67  -163.58 
3   1 GLU A 48   ? ? -56.93  104.87  
4   1 ALA A 49   ? ? -44.06  166.58  
5   1 PHE A 50   ? ? -173.65 129.10  
6   1 SER A 55   ? ? 178.66  171.13  
7   1 TYR A 59   ? ? 26.78   -131.91 
8   1 LYS A 62   ? ? -75.97  40.85   
9   1 SER A 68   ? ? -162.76 -168.15 
10  1 SER A 74   ? ? 179.89  176.86  
11  1 LYS A 78   ? ? 40.43   26.81   
12  1 LEU A 85   ? ? -62.30  -176.62 
13  1 THR A 86   ? ? 169.69  105.18  
14  1 LYS A 90   ? ? -130.79 -81.92  
15  1 VAL A 99   ? ? 69.23   -25.99  
16  1 SER A 100  ? ? -56.09  106.70  
17  1 TYR A 101  ? ? 86.91   133.61  
18  1 PRO A 137  ? ? -29.73  121.38  
19  1 ASP A 138  ? ? 91.28   -3.47   
20  1 PRO A 154  ? ? -22.12  -51.16  
21  1 ALA A 155  ? ? 73.23   33.02   
22  1 THR A 162  ? ? -163.64 89.21   
23  1 PRO A 166  ? ? -61.75  9.39    
24  1 VAL A 171  ? ? -150.96 -14.69  
25  1 VAL A 174  ? ? -175.53 138.06  
26  1 ILE A 182  ? ? -107.47 60.91   
27  1 PRO A 191  ? ? -45.54  152.50  
28  1 GLU A 207  ? ? -62.26  -161.61 
29  1 PHE A 209  ? ? 110.52  121.98  
30  1 PHE A 243  ? ? 170.87  -7.28   
31  1 PHE A 246  ? ? -162.54 93.25   
32  1 GLU A 247  ? ? -69.01  94.07   
33  1 TYR A 256  ? ? -89.29  36.22   
34  1 THR A 261  ? ? -102.89 -99.01  
35  1 ARG A 272  ? ? -178.19 127.85  
36  1 GLU A 281  ? ? -68.01  97.55   
37  1 MET A 282  ? ? -55.16  -172.22 
38  1 GLN A 284  ? ? -53.89  175.63  
39  1 MET A 287  ? ? -30.20  137.90  
40  1 ASN A 289  ? ? 42.01   106.42  
41  1 MET A 291  ? ? -10.48  117.79  
42  1 ALA A 306  ? ? -62.59  22.54   
43  1 VAL A 307  ? ? -142.62 -43.63  
44  1 LYS A 308  ? ? -39.36  -93.29  
45  1 TYR A 312  ? ? -62.18  0.36    
46  1 ASP A 317  ? ? -21.01  -77.89  
47  1 LEU A 318  ? ? -49.38  71.55   
48  1 ASN A 319  ? ? 163.38  89.94   
49  1 LYS A 321  ? ? -105.95 -163.38 
50  1 THR A 333  ? ? -66.82  -70.07  
51  1 PHE A 336  ? ? -55.79  -157.61 
52  1 SER A 337  ? ? -170.27 144.57  
53  1 ALA A 358  ? ? 33.54   57.40   
54  1 ILE A 371  ? ? -143.74 57.71   
55  1 LYS A 372  ? ? -58.62  95.54   
56  1 SER A 378  ? ? -46.60  4.22    
57  1 ASP A 380  ? ? 47.29   29.13   
58  1 LEU A 404  ? ? -37.26  156.55  
59  1 PRO A 425  ? ? -56.87  107.86  
60  1 SER A 426  ? ? -13.97  -55.90  
61  1 THR A 429  ? ? -139.88 -77.49  
62  1 ALA A 439  ? ? -24.38  121.75  
63  1 GLU A 445  ? ? -36.91  -71.02  
64  1 TYR A 457  ? ? -56.15  92.57   
65  1 SER A 461  ? ? -64.79  0.51    
66  1 LYS A 489  ? ? -5.11   135.29  
67  1 SER A 490  ? ? 100.44  -66.41  
68  1 PRO A 491  ? ? -21.53  116.90  
69  1 LYS A 495  ? ? -74.56  38.74   
70  1 LEU A 502  ? ? -172.47 113.05  
71  1 SER A 505  ? ? -175.94 123.98  
72  1 ASP A 520  ? ? -61.33  -99.13  
73  1 SER A 522  ? ? -61.40  -87.91  
74  1 SER A 537  ? ? -179.12 -173.85 
75  1 GLU A 565  ? ? -71.81  49.72   
76  1 PRO A 584  ? ? -63.59  66.65   
77  1 ASP A 597  ? ? -39.12  136.63  
78  1 ALA A 601  ? ? -173.03 85.75   
79  1 ALA A 603  ? ? -179.60 146.31  
80  1 SER A 607  ? ? -44.22  -14.76  
81  1 VAL A 609  ? ? -53.40  -71.12  
82  1 TYR A 610  ? ? -45.81  -74.73  
83  1 GLN A 613  ? ? 30.13   84.99   
84  1 LYS A 617  ? ? 29.11   -103.48 
85  1 LEU A 627  ? ? -58.04  5.79    
86  1 CYS A 634  ? ? 176.33  155.52  
87  1 LEU A 640  ? ? -163.49 -27.94  
88  1 ALA A 643  ? ? -62.23  -82.13  
89  1 ASN A 644  ? ? -29.28  -62.93  
90  1 HIS A 647  ? ? -59.94  -76.17  
91  1 ALA A 657  ? ? 170.79  -73.87  
92  1 ALA A 659  ? ? -58.87  106.11  
93  1 ASP A 661  ? ? -52.04  175.61  
94  1 SER A 662  ? ? -158.41 62.23   
95  1 GLN A 663  ? ? -15.28  101.24  
96  1 GLU A 664  ? ? 32.72   135.18  
97  1 ASN A 665  ? ? 56.20   -152.35 
98  1 ASP A 666  ? ? -161.20 102.21  
99  1 GLU A 667  ? ? 26.05   74.55   
100 1 PRO A 668  ? ? -62.40  34.50   
101 1 CYS A 669  ? ? -23.08  144.64  
102 1 ILE A 686  ? ? -77.00  23.72   
103 1 LYS A 691  ? ? -176.80 11.42   
104 1 HIS A 692  ? ? 163.39  148.85  
105 1 TYR A 700  ? ? -49.37  -72.19  
106 1 CYS A 704  ? ? -10.58  -89.63  
107 1 VAL A 705  ? ? -173.72 82.14   
108 1 THR A 710  ? ? -57.30  172.35  
109 1 LEU A 720  ? ? -31.88  -30.67  
110 1 PRO A 722  ? ? -45.43  -5.97   
111 1 GLU A 730  ? ? -56.52  -74.65  
112 1 THR A 756  ? ? -162.63 86.05   
113 1 LEU A 758  ? ? -176.61 97.64   
114 1 PRO A 759  ? ? -53.02  4.02    
115 1 ILE A 765  ? ? -160.54 100.25  
116 1 ARG A 766  ? ? -76.68  21.92   
117 1 TRP A 775  ? ? -79.61  21.98   
118 1 ARG A 782  ? ? 62.32   -10.27  
119 1 LYS A 784  ? ? 179.45  138.24  
120 1 GLN A 787  ? ? -49.89  165.73  
121 1 PHE A 788  ? ? 173.82  150.81  
122 1 ASP A 792  ? ? -59.57  94.28   
123 1 SER A 793  ? ? -177.38 132.54  
124 1 LEU A 794  ? ? -61.61  90.77   
125 1 THR A 814  ? ? -52.54  177.40  
126 1 ALA A 817  ? ? -150.50 59.68   
127 1 PHE A 820  ? ? 173.65  138.20  
128 1 TYR A 831  ? ? -60.56  -73.47  
129 1 PHE A 855  ? ? -115.43 -161.47 
130 1 CYS A 856  ? ? 177.18  81.12   
131 1 GLU A 863  ? ? -24.97  -53.29  
132 1 SER A 892  ? ? -143.16 -151.73 
133 1 LEU A 901  ? ? -172.71 103.66  
134 1 LEU A 907  ? ? -38.78  143.95  
135 1 ASN A 909  ? ? 71.49   120.31  
136 1 PRO A 931  ? ? -108.76 -137.51 
137 1 TYR A 939  ? ? -41.97  -10.15  
138 1 ILE A 949  ? ? -25.21  -39.45  
139 1 LEU A 965  ? ? -68.02  13.92   
140 1 LEU A 982  ? ? 80.10   138.11  
141 1 SER A 993  ? ? -148.52 -26.24  
142 1 MET A 1013 ? ? -57.44  -6.47   
143 1 ASN A 1029 ? ? 0.05    108.21  
144 1 SER A 1036 ? ? -72.68  -164.58 
145 1 SER A 1055 ? ? -31.05  -38.47  
146 1 TYR A 1064 ? ? 88.70   -4.96   
147 1 LEU A 1105 ? ? -59.37  -8.01   
148 1 ASP A 1114 ? ? -70.08  31.93   
149 1 ASN A 1121 ? ? -84.57  -70.83  
150 1 CYS A 1159 ? ? -149.26 41.82   
151 1 PRO A 1181 ? ? -66.28  76.81   
152 1 SER A 1196 ? ? -26.37  -31.05  
153 1 LEU A 1197 ? ? -101.26 49.03   
154 1 ASN A 1231 ? ? -36.69  -175.04 
155 1 GLN A 1233 ? ? 43.79   15.65   
156 1 LYS A 1235 ? ? 27.64   49.70   
157 1 VAL A 1239 ? ? -101.77 40.40   
158 1 PRO A 1240 ? ? -45.69  69.58   
159 1 THR A 1244 ? ? -173.63 138.55  
160 1 LEU A 1261 ? ? -79.91  33.84   
161 1 LYS A 1262 ? ? 27.24   37.40   
162 1 ASP A 1263 ? ? -66.32  26.93   
163 1 ILE A 1264 ? ? -22.78  -57.94  
164 1 SER A 1275 ? ? -54.03  23.74   
165 1 GLU A 1276 ? ? -154.60 13.46   
166 1 GLN A 1278 ? ? -39.91  142.62  
167 1 PHE A 1284 ? ? 14.64   -63.34  
168 1 SER A 1286 ? ? 41.02   -153.27 
169 1 THR A 1287 ? ? -105.72 -63.87  
170 1 LEU A 1297 ? ? -28.65  -40.25  
171 1 GLN A 1306 ? ? -66.72  -179.34 
172 1 ARG A 1308 ? ? -21.17  107.43  
173 1 SER A 1310 ? ? -167.86 47.03   
174 1 MET A 1311 ? ? -67.43  -175.56 
175 1 ASP A 1312 ? ? -152.82 59.47   
176 1 ASN A 1325 ? ? -164.50 118.41  
177 1 LYS A 1331 ? ? -70.05  -71.46  
178 1 LEU A 1334 ? ? -89.14  46.52   
179 1 SER A 1349 ? ? -171.53 65.36   
180 1 PHE A 1352 ? ? -66.98  -96.61  
181 1 GLU A 1373 ? ? -42.79  168.50  
182 1 GLU A 1413 ? ? 79.19   -13.50  
183 1 ILE A 1432 ? ? -160.24 62.93   
184 1 ASP A 1452 ? ? -171.21 112.98  
185 1 GLN A 1454 ? ? -172.81 135.14  
186 1 ASP A 1457 ? ? 35.00   51.02   
187 1 PRO A 1468 ? ? -18.04  140.99  
188 1 ASP A 1471 ? ? -157.94 -157.01 
189 1 GLU A 1481 ? ? -51.15  82.71   
190 1 PHE A 1487 ? ? 96.41   83.00   
191 1 PRO A 1501 ? ? -51.01  -0.82   
192 1 ILE A 1516 ? ? 126.09  133.91  
193 1 LYS A 1518 ? ? -157.76 -143.07 
194 1 VAL A 1519 ? ? -144.79 -71.38  
195 1 CYS A 1520 ? ? 61.51   115.35  
196 1 GLU A 1521 ? ? -89.57  -134.17 
197 1 ALA A 1523 ? ? 98.35   -25.47  
198 1 ALA A 1524 ? ? -60.71  1.26    
199 1 LYS A 1526 ? ? -70.87  31.79   
200 1 CYS A 1527 ? ? -140.90 -32.39  
201 1 ASP A 1531 ? ? 165.92  -16.80  
202 1 CYS A 1532 ? ? -34.91  159.67  
203 1 GLN A 1536 ? ? -47.10  153.02  
204 1 LEU A 1539 ? ? 59.62   176.13  
205 1 ILE A 1543 ? ? 82.85   72.12   
206 1 SER A 1544 ? ? -156.61 -20.74  
207 1 THR A 1551 ? ? -68.81  0.54    
208 1 ALA A 1552 ? ? -91.58  -93.85  
209 1 LYS A 1554 ? ? -44.15  106.53  
210 1 GLU A 1556 ? ? -66.97  1.83    
211 1 TYR A 1559 ? ? 173.12  162.91  
212 1 THR A 1569 ? ? -45.62  105.50  
213 1 VAL A 1573 ? ? 74.76   -18.66  
214 1 LYS A 1576 ? ? -69.82  -177.13 
215 1 ASP A 1583 ? ? -172.04 127.12  
216 1 GLU A 1589 ? ? -72.57  39.80   
217 1 ALA A 1592 ? ? 143.92  149.09  
218 1 LYS A 1594 ? ? -41.24  108.36  
219 1 ASP A 1595 ? ? 132.86  -29.89  
220 1 LYS A 1602 ? ? -175.63 140.24  
221 1 VAL A 1604 ? ? 71.73   163.76  
222 1 THR A 1607 ? ? -81.79  39.41   
223 1 ASN A 1608 ? ? -144.11 29.98   
224 1 ALA A 1609 ? ? 167.21  123.85  
225 1 LYS A 1622 ? ? -61.03  -173.99 
226 1 TYR A 1629 ? ? -170.79 125.17  
227 1 ASN A 1630 ? ? -144.35 51.61   
228 1 PHE A 1631 ? ? 101.23  38.27   
229 1 SER A 1632 ? ? 86.94   103.24  
230 1 PHE A 1633 ? ? 177.12  -151.39 
231 1 ARG A 1634 ? ? -105.01 -131.72 
232 1 TYR A 1635 ? ? -143.21 -70.07  
233 1 ILE A 1636 ? ? -32.03  -176.02 
234 1 LEU A 1639 ? ? 83.24   59.72   
235 1 ASP A 1640 ? ? -91.15  -151.21 
236 1 TRP A 1644 ? ? -98.19  31.62   
237 1 ILE A 1645 ? ? -38.83  124.31  
238 1 TRP A 1648 ? ? -102.33 76.43   
239 1 PRO A 1649 ? ? -63.97  77.24   
240 1 ARG A 1650 ? ? -66.86  23.76   
241 1 THR A 1652 ? ? 44.74   11.38   
242 1 THR A 1653 ? ? 148.73  96.13   
243 1 SER A 1655 ? ? 29.74   36.32   
244 1 SER A 1656 ? ? 42.81   79.93   
245 1 GLN A 1658 ? ? 151.74  178.60  
246 1 ALA A 1659 ? ? 60.83   -9.18   
247 1 GLU A 1666 ? ? -74.92  -72.40  
248 1 PHE A 1667 ? ? -25.96  -50.61  
249 1 HIS X 41   ? ? 57.71   126.76  
250 1 ASP X 42   ? ? 161.24  155.46  
251 1 TYR X 67   ? ? -58.23  -75.91  
252 1 ASN X 68   ? ? -110.97 -92.69  
253 1 SER X 70   ? ? -154.32 -15.16  
254 1 VAL X 72   ? ? 171.99  144.75  
255 1 LYS X 78   ? ? 114.95  0.63    
256 1 ASP X 79   ? ? -146.92 -21.87  
257 1 GLN X 80   ? ? -157.16 -147.10 
258 1 LEU X 87   ? ? -162.76 27.96   
259 1 TYR X 94   ? ? -147.94 44.63   
260 1 PHE X 104  ? ? -63.89  80.69   
261 1 LYS X 124  ? ? -58.32  -76.01  
262 1 LYS X 125  ? ? 62.36   114.30  
263 1 THR X 129  ? ? -86.90  41.87   
264 1 PRO X 135  ? ? -49.87  168.36  
265 1 LEU X 136  ? ? 165.96  107.84  
266 1 ASN X 142  ? ? -147.63 58.58   
267 1 ASP X 151  ? ? -150.65 -145.35 
268 1 ASN X 176  ? ? -141.17 -11.23  
269 1 THR X 183  ? ? -69.99  2.83    
270 1 LYS X 185  ? ? -173.21 -20.82  
271 1 LEU X 193  ? ? -140.31 -28.10  
272 1 LYS X 206  ? ? -103.85 47.09   
273 1 GLN X 208  ? ? -92.86  53.71   
274 1 MET X 212  ? ? -59.07  -1.30   
275 1 ASP X 214  ? ? -40.96  150.24  
276 1 PRO B 28   ? ? -46.28  162.65  
277 1 TYR B 46   ? ? -56.12  -163.33 
278 1 GLU B 48   ? ? -56.47  104.76  
279 1 ALA B 49   ? ? -44.02  166.64  
280 1 PHE B 50   ? ? -173.96 128.26  
281 1 SER B 55   ? ? 179.06  171.03  
282 1 TYR B 59   ? ? 27.17   -131.93 
283 1 LYS B 62   ? ? -76.14  40.83   
284 1 SER B 68   ? ? -162.88 -168.04 
285 1 LYS B 78   ? ? 40.09   26.56   
286 1 LEU B 85   ? ? -63.35  -176.86 
287 1 THR B 86   ? ? 169.76  106.38  
288 1 LYS B 90   ? ? -130.62 -81.60  
289 1 VAL B 99   ? ? 69.01   -26.20  
290 1 SER B 100  ? ? -55.93  106.75  
291 1 TYR B 101  ? ? 87.00   133.72  
292 1 PRO B 137  ? ? -28.74  121.89  
293 1 ASP B 138  ? ? 91.11   -4.99   
294 1 ASP B 150  ? ? -22.28  -29.10  
295 1 PRO B 154  ? ? -22.72  -50.65  
296 1 ALA B 155  ? ? 72.69   33.93   
297 1 THR B 162  ? ? -163.60 88.62   
298 1 PRO B 166  ? ? -60.79  8.48    
299 1 GLU B 170  ? ? -58.08  170.91  
300 1 VAL B 171  ? ? -152.60 -13.72  
301 1 VAL B 174  ? ? -176.17 137.24  
302 1 ILE B 182  ? ? -107.18 59.28   
303 1 PRO B 191  ? ? -45.39  152.07  
304 1 GLU B 207  ? ? -61.82  -160.90 
305 1 PHE B 209  ? ? 109.85  123.04  
306 1 PHE B 243  ? ? 172.38  -7.77   
307 1 PHE B 246  ? ? -162.57 92.59   
308 1 GLU B 247  ? ? -68.87  92.80   
309 1 TYR B 256  ? ? -89.35  35.56   
310 1 THR B 261  ? ? -103.02 -99.17  
311 1 ARG B 272  ? ? -178.21 127.65  
312 1 GLU B 281  ? ? -67.63  97.57   
313 1 MET B 282  ? ? -55.29  -173.35 
314 1 GLN B 284  ? ? -54.26  175.34  
315 1 MET B 287  ? ? -30.05  137.89  
316 1 ASN B 289  ? ? 41.94   106.43  
317 1 MET B 291  ? ? -9.73   117.28  
318 1 ALA B 306  ? ? -62.54  21.87   
319 1 VAL B 307  ? ? -142.09 -42.43  
320 1 LYS B 308  ? ? -40.01  -93.17  
321 1 TYR B 312  ? ? -62.53  0.26    
322 1 ASP B 317  ? ? -21.99  -77.75  
323 1 LEU B 318  ? ? -48.78  73.31   
324 1 ASN B 319  ? ? 161.23  88.78   
325 1 LYS B 321  ? ? -104.69 -163.89 
326 1 THR B 333  ? ? -66.72  -70.37  
327 1 PHE B 336  ? ? -55.81  -157.73 
328 1 ALA B 358  ? ? 33.41   57.30   
329 1 ILE B 371  ? ? -143.38 58.09   
330 1 LYS B 372  ? ? -59.72  96.50   
331 1 SER B 378  ? ? -46.70  4.55    
332 1 LEU B 404  ? ? -35.12  157.64  
333 1 PRO B 425  ? ? -56.58  108.92  
334 1 SER B 426  ? ? -14.55  -55.73  
335 1 THR B 429  ? ? -140.52 -77.77  
336 1 ALA B 439  ? ? -25.28  121.42  
337 1 GLU B 445  ? ? -36.34  -71.11  
338 1 ASN B 446  ? ? -69.35  7.08    
339 1 TYR B 457  ? ? -56.85  91.33   
340 1 LYS B 489  ? ? -6.18   135.09  
341 1 SER B 490  ? ? 100.98  -66.88  
342 1 PRO B 491  ? ? -20.98  116.19  
343 1 LYS B 495  ? ? -74.12  38.28   
344 1 THR B 497  ? ? -81.59  -70.22  
345 1 LEU B 502  ? ? -173.35 110.25  
346 1 SER B 505  ? ? -176.11 123.21  
347 1 ASP B 520  ? ? -61.29  -98.58  
348 1 SER B 522  ? ? -60.87  -88.68  
349 1 SER B 537  ? ? -176.80 -174.52 
350 1 PRO B 584  ? ? -64.83  66.27   
351 1 ASP B 597  ? ? -39.54  136.69  
352 1 ALA B 601  ? ? -173.90 86.56   
353 1 ALA B 603  ? ? -178.90 146.64  
354 1 SER B 607  ? ? -44.61  -13.81  
355 1 VAL B 609  ? ? -54.61  -70.61  
356 1 TYR B 610  ? ? -46.70  -75.05  
357 1 GLN B 613  ? ? 30.33   84.91   
358 1 LYS B 617  ? ? 29.42   -103.46 
359 1 LEU B 627  ? ? -57.92  5.61    
360 1 CYS B 634  ? ? 178.43  156.25  
361 1 LEU B 640  ? ? -163.04 -27.91  
362 1 ALA B 643  ? ? -64.01  -81.36  
363 1 ASN B 644  ? ? -28.94  -62.71  
364 1 HIS B 647  ? ? -58.88  -77.23  
365 1 ALA B 657  ? ? 170.49  -73.47  
366 1 ALA B 659  ? ? -59.49  106.35  
367 1 ASP B 660  ? ? -69.87  8.70    
368 1 ASP B 661  ? ? -52.80  176.09  
369 1 SER B 662  ? ? -158.82 62.21   
370 1 GLN B 663  ? ? -15.14  100.86  
371 1 GLU B 664  ? ? 32.88   135.27  
372 1 ASN B 665  ? ? 55.99   -152.42 
373 1 ASP B 666  ? ? -160.89 102.38  
374 1 GLU B 667  ? ? 26.00   74.63   
375 1 PRO B 668  ? ? -62.42  34.68   
376 1 CYS B 669  ? ? -23.15  144.53  
377 1 ILE B 686  ? ? -77.09  23.79   
378 1 LYS B 691  ? ? -177.43 11.37   
379 1 HIS B 692  ? ? 163.25  148.71  
380 1 TYR B 700  ? ? -49.61  -72.12  
381 1 CYS B 704  ? ? -10.10  -89.52  
382 1 VAL B 705  ? ? -174.06 82.15   
383 1 THR B 710  ? ? -56.64  171.36  
384 1 LEU B 720  ? ? -31.59  -31.06  
385 1 PRO B 722  ? ? -45.58  -5.70   
386 1 GLU B 730  ? ? -56.67  -73.60  
387 1 THR B 756  ? ? -162.26 85.89   
388 1 LEU B 758  ? ? -176.70 97.55   
389 1 PRO B 759  ? ? -52.72  4.49    
390 1 ILE B 765  ? ? -161.46 99.22   
391 1 ARG B 766  ? ? -75.52  21.37   
392 1 TRP B 775  ? ? -79.32  22.92   
393 1 ARG B 782  ? ? 61.95   -10.12  
394 1 LYS B 784  ? ? 179.19  138.24  
395 1 PHE B 788  ? ? 173.99  150.85  
396 1 ASP B 792  ? ? -59.52  94.26   
397 1 SER B 793  ? ? -177.03 133.67  
398 1 LEU B 794  ? ? -62.19  89.95   
399 1 THR B 814  ? ? -52.00  177.93  
400 1 ALA B 817  ? ? -150.23 61.02   
401 1 PHE B 820  ? ? 173.06  138.06  
402 1 TYR B 831  ? ? -60.90  -73.08  
403 1 PHE B 855  ? ? -115.65 -162.48 
404 1 CYS B 856  ? ? 178.05  81.67   
405 1 GLU B 863  ? ? -25.93  -53.23  
406 1 SER B 892  ? ? -142.47 -151.20 
407 1 LEU B 901  ? ? -174.93 102.54  
408 1 LEU B 907  ? ? -39.30  144.21  
409 1 ASN B 909  ? ? 71.67   121.06  
410 1 PRO B 931  ? ? -108.15 -137.25 
411 1 TYR B 939  ? ? -41.47  -10.05  
412 1 ILE B 949  ? ? -27.42  -39.27  
413 1 LEU B 965  ? ? -67.39  13.59   
414 1 LEU B 982  ? ? 79.27   140.03  
415 1 SER B 993  ? ? -149.60 -25.24  
416 1 MET B 1013 ? ? -57.15  -6.55   
417 1 VAL B 1016 ? ? -46.20  -71.13  
418 1 ASN B 1029 ? ? -1.19   109.11  
419 1 SER B 1036 ? ? -72.81  -164.60 
420 1 SER B 1055 ? ? -30.46  -37.48  
421 1 TYR B 1064 ? ? 88.06   -5.20   
422 1 ASP B 1114 ? ? -70.28  32.02   
423 1 ASN B 1121 ? ? -85.04  -71.01  
424 1 ILE B 1150 ? ? -38.55  -35.06  
425 1 CYS B 1159 ? ? -149.96 42.54   
426 1 PRO B 1181 ? ? -66.05  76.64   
427 1 SER B 1196 ? ? -27.34  -30.71  
428 1 LEU B 1197 ? ? -100.98 49.45   
429 1 ASN B 1231 ? ? -35.98  -175.22 
430 1 GLN B 1233 ? ? 43.75   15.74   
431 1 LYS B 1235 ? ? 27.00   49.71   
432 1 VAL B 1239 ? ? -101.81 40.20   
433 1 PRO B 1240 ? ? -45.57  69.66   
434 1 THR B 1244 ? ? -172.84 138.55  
435 1 LEU B 1261 ? ? -80.70  33.31   
436 1 LYS B 1262 ? ? 28.44   36.98   
437 1 ASP B 1263 ? ? -66.01  25.31   
438 1 ILE B 1264 ? ? -22.33  -56.12  
439 1 SER B 1275 ? ? -58.75  24.92   
440 1 GLU B 1276 ? ? -154.44 11.72   
441 1 GLN B 1278 ? ? -37.85  142.23  
442 1 PHE B 1284 ? ? 14.49   -62.88  
443 1 SER B 1286 ? ? 41.85   -152.96 
444 1 THR B 1287 ? ? -107.15 -63.24  
445 1 LEU B 1297 ? ? -31.96  -38.35  
446 1 GLN B 1306 ? ? -67.36  -179.55 
447 1 ARG B 1308 ? ? -19.90  107.84  
448 1 SER B 1310 ? ? -167.86 47.41   
449 1 MET B 1311 ? ? -68.72  -174.56 
450 1 ASP B 1312 ? ? -153.34 60.50   
451 1 ASN B 1325 ? ? -164.42 118.84  
452 1 LYS B 1331 ? ? -70.27  -71.06  
453 1 LEU B 1334 ? ? -90.73  47.45   
454 1 SER B 1349 ? ? -173.82 64.88   
455 1 PHE B 1352 ? ? -66.43  -98.52  
456 1 GLU B 1373 ? ? -42.68  168.16  
457 1 GLU B 1413 ? ? 79.62   -13.82  
458 1 ILE B 1432 ? ? -159.14 64.06   
459 1 ASP B 1452 ? ? -171.31 114.05  
460 1 GLN B 1454 ? ? -173.70 135.27  
461 1 ASP B 1457 ? ? 35.42   50.75   
462 1 PRO B 1468 ? ? -18.79  141.31  
463 1 ASP B 1471 ? ? -157.15 -157.80 
464 1 GLU B 1481 ? ? -51.28  81.91   
465 1 PHE B 1487 ? ? 12.42   64.36   
466 1 PRO B 1501 ? ? -52.06  0.48    
467 1 ILE B 1514 ? ? -47.84  153.70  
468 1 VAL B 1519 ? ? -80.39  -80.49  
469 1 CYS B 1520 ? ? -160.53 74.93   
470 1 ALA B 1524 ? ? -155.42 -90.33  
471 1 CYS B 1525 ? ? -55.60  179.51  
472 1 CYS B 1527 ? ? -175.55 3.09    
473 1 ALA B 1530 ? ? -91.46  54.58   
474 1 ASP B 1531 ? ? -169.26 -3.85   
475 1 HIS Y 41   ? ? 57.50   126.83  
476 1 ASP Y 42   ? ? 161.16  155.27  
477 1 TYR Y 67   ? ? -59.17  -74.32  
478 1 ASN Y 68   ? ? -112.04 -90.85  
479 1 SER Y 70   ? ? -153.47 -14.77  
480 1 VAL Y 72   ? ? 170.90  147.97  
481 1 LYS Y 78   ? ? 115.38  0.26    
482 1 ASP Y 79   ? ? -146.45 -22.30  
483 1 GLN Y 80   ? ? -156.93 -147.21 
484 1 LEU Y 87   ? ? -163.16 28.00   
485 1 TYR Y 94   ? ? -147.98 44.11   
486 1 PHE Y 104  ? ? -63.90  80.74   
487 1 LYS Y 124  ? ? -58.06  -76.27  
488 1 LYS Y 125  ? ? 62.75   114.29  
489 1 THR Y 129  ? ? -86.31  41.59   
490 1 PRO Y 135  ? ? -49.90  167.47  
491 1 LEU Y 136  ? ? 166.77  107.65  
492 1 ASN Y 142  ? ? -147.93 58.44   
493 1 ASP Y 151  ? ? -150.94 -144.58 
494 1 ASN Y 176  ? ? -140.74 -11.18  
495 1 THR Y 183  ? ? -69.84  3.00    
496 1 LYS Y 185  ? ? -173.44 -20.59  
497 1 LEU Y 193  ? ? -140.28 -28.35  
498 1 LYS Y 206  ? ? -103.97 47.10   
499 1 GLN Y 208  ? ? -92.97  53.99   
500 1 MET Y 212  ? ? -59.23  -1.27   
501 1 ASP Y 214  ? ? -40.05  150.35  
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 LEU A 651  ? ? THR A 652  ? ? 147.81  
2 1 THR A 1179 ? ? LEU A 1180 ? ? -137.67 
3 1 PHE A 1633 ? ? ARG A 1634 ? ? -149.23 
4 1 TYR A 1635 ? ? ILE A 1636 ? ? -143.05 
5 1 LEU B 651  ? ? THR B 652  ? ? 147.76  
6 1 THR B 1179 ? ? LEU B 1180 ? ? -136.92 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET 1    ? A MET 1    
2   1 Y 1 A GLY 2    ? A GLY 2    
3   1 Y 1 A LEU 3    ? A LEU 3    
4   1 Y 1 A LEU 4    ? A LEU 4    
5   1 Y 1 A GLY 5    ? A GLY 5    
6   1 Y 1 A ILE 6    ? A ILE 6    
7   1 Y 1 A LEU 7    ? A LEU 7    
8   1 Y 1 A CYS 8    ? A CYS 8    
9   1 Y 1 A PHE 9    ? A PHE 9    
10  1 Y 1 A LEU 10   ? A LEU 10   
11  1 Y 1 A ILE 11   ? A ILE 11   
12  1 Y 1 A PHE 12   ? A PHE 12   
13  1 Y 1 A LEU 13   ? A LEU 13   
14  1 Y 1 A GLY 14   ? A GLY 14   
15  1 Y 1 A LYS 15   ? A LYS 15   
16  1 Y 1 A THR 16   ? A THR 16   
17  1 Y 1 A TRP 17   ? A TRP 17   
18  1 Y 1 A GLY 18   ? A GLY 18   
19  1 Y 1 A GLN 19   ? A GLN 19   
20  1 Y 1 A GLU 20   ? A GLU 20   
21  1 Y 1 A GLN 21   ? A GLN 21   
22  1 Y 1 A ARG 674  ? A ARG 674  
23  1 Y 1 A PRO 675  ? A PRO 675  
24  1 Y 1 A ARG 676  ? A ARG 676  
25  1 Y 1 A ARG 677  ? A ARG 677  
26  1 Y 1 A THR 678  ? A THR 678  
27  1 Y 1 A HIS 744  ? A HIS 744  
28  1 Y 1 A LYS 745  ? A LYS 745  
29  1 Y 1 A ASP 746  ? A ASP 746  
30  1 Y 1 A MET 747  ? A MET 747  
31  1 Y 1 A GLN 748  ? A GLN 748  
32  1 Y 1 A PRO 871  ? A PRO 871  
33  1 Y 1 A VAL 872  ? A VAL 872  
34  1 Y 1 A ILE 873  ? A ILE 873  
35  1 Y 1 A ASP 874  ? A ASP 874  
36  1 Y 1 A HIS 875  ? A HIS 875  
37  1 Y 1 A GLN 876  ? A GLN 876  
38  1 Y 1 A GLY 877  ? A GLY 877  
39  1 Y 1 A THR 878  ? A THR 878  
40  1 Y 1 A LYS 879  ? A LYS 879  
41  1 Y 1 A SER 880  ? A SER 880  
42  1 Y 1 A SER 881  ? A SER 881  
43  1 Y 1 A GLU 1387 ? A GLU 1387 
44  1 Y 1 A ALA 1388 ? A ALA 1388 
45  1 Y 1 A SER 1389 ? A SER 1389 
46  1 Y 1 A HIS 1390 ? A HIS 1390 
47  1 Y 1 A TYR 1391 ? A TYR 1391 
48  1 Y 1 A ARG 1392 ? A ARG 1392 
49  1 Y 1 A GLY 1393 ? A GLY 1393 
50  1 Y 1 A TYR 1394 ? A TYR 1394 
51  1 Y 1 A GLY 1395 ? A GLY 1395 
52  1 Y 1 A ASN 1396 ? A ASN 1396 
53  1 Y 1 A SER 1397 ? A SER 1397 
54  1 Y 1 A ASP 1398 ? A ASP 1398 
55  1 Y 1 X MET 1    ? B MET 1    
56  1 Y 1 X LYS 2    ? B LYS 2    
57  1 Y 1 X LEU 3    ? B LEU 3    
58  1 Y 1 X LYS 4    ? B LYS 4    
59  1 Y 1 X THR 5    ? B THR 5    
60  1 Y 1 X LEU 6    ? B LEU 6    
61  1 Y 1 X ALA 7    ? B ALA 7    
62  1 Y 1 X LYS 8    ? B LYS 8    
63  1 Y 1 X ALA 9    ? B ALA 9    
64  1 Y 1 X THR 10   ? B THR 10   
65  1 Y 1 X LEU 11   ? B LEU 11   
66  1 Y 1 X ALA 12   ? B ALA 12   
67  1 Y 1 X LEU 13   ? B LEU 13   
68  1 Y 1 X GLY 14   ? B GLY 14   
69  1 Y 1 X LEU 15   ? B LEU 15   
70  1 Y 1 X LEU 16   ? B LEU 16   
71  1 Y 1 X THR 17   ? B THR 17   
72  1 Y 1 X THR 18   ? B THR 18   
73  1 Y 1 X GLY 19   ? B GLY 19   
74  1 Y 1 X VAL 20   ? B VAL 20   
75  1 Y 1 X ILE 21   ? B ILE 21   
76  1 Y 1 X THR 22   ? B THR 22   
77  1 Y 1 X SER 23   ? B SER 23   
78  1 Y 1 X GLU 24   ? B GLU 24   
79  1 Y 1 X GLY 25   ? B GLY 25   
80  1 Y 1 X GLN 26   ? B GLN 26   
81  1 Y 1 X ALA 27   ? B ALA 27   
82  1 Y 1 X VAL 28   ? B VAL 28   
83  1 Y 1 X GLN 29   ? B GLN 29   
84  1 Y 1 X ALA 30   ? B ALA 30   
85  1 Y 1 X ALA 31   ? B ALA 31   
86  1 Y 1 X GLU 32   ? B GLU 32   
87  1 Y 1 X LYS 33   ? B LYS 33   
88  1 Y 1 X GLN 34   ? B GLN 34   
89  1 Y 1 X GLY 35   ? B GLY 35   
90  1 Y 1 X ARG 36   ? B ARG 36   
91  1 Y 1 X VAL 37   ? B VAL 37   
92  1 Y 1 X GLN 38   ? B GLN 38   
93  1 Y 1 X HIS 39   ? B HIS 39   
94  1 Y 1 X ILE 231  ? B ILE 231  
95  1 Y 1 B MET 1    ? C MET 1    
96  1 Y 1 B GLY 2    ? C GLY 2    
97  1 Y 1 B LEU 3    ? C LEU 3    
98  1 Y 1 B LEU 4    ? C LEU 4    
99  1 Y 1 B GLY 5    ? C GLY 5    
100 1 Y 1 B ILE 6    ? C ILE 6    
101 1 Y 1 B LEU 7    ? C LEU 7    
102 1 Y 1 B CYS 8    ? C CYS 8    
103 1 Y 1 B PHE 9    ? C PHE 9    
104 1 Y 1 B LEU 10   ? C LEU 10   
105 1 Y 1 B ILE 11   ? C ILE 11   
106 1 Y 1 B PHE 12   ? C PHE 12   
107 1 Y 1 B LEU 13   ? C LEU 13   
108 1 Y 1 B GLY 14   ? C GLY 14   
109 1 Y 1 B LYS 15   ? C LYS 15   
110 1 Y 1 B THR 16   ? C THR 16   
111 1 Y 1 B TRP 17   ? C TRP 17   
112 1 Y 1 B GLY 18   ? C GLY 18   
113 1 Y 1 B GLN 19   ? C GLN 19   
114 1 Y 1 B GLU 20   ? C GLU 20   
115 1 Y 1 B GLN 21   ? C GLN 21   
116 1 Y 1 B ARG 674  ? C ARG 674  
117 1 Y 1 B PRO 675  ? C PRO 675  
118 1 Y 1 B ARG 676  ? C ARG 676  
119 1 Y 1 B ARG 677  ? C ARG 677  
120 1 Y 1 B THR 678  ? C THR 678  
121 1 Y 1 B HIS 744  ? C HIS 744  
122 1 Y 1 B LYS 745  ? C LYS 745  
123 1 Y 1 B ASP 746  ? C ASP 746  
124 1 Y 1 B MET 747  ? C MET 747  
125 1 Y 1 B GLN 748  ? C GLN 748  
126 1 Y 1 B PRO 871  ? C PRO 871  
127 1 Y 1 B VAL 872  ? C VAL 872  
128 1 Y 1 B ILE 873  ? C ILE 873  
129 1 Y 1 B ASP 874  ? C ASP 874  
130 1 Y 1 B HIS 875  ? C HIS 875  
131 1 Y 1 B GLN 876  ? C GLN 876  
132 1 Y 1 B GLY 877  ? C GLY 877  
133 1 Y 1 B THR 878  ? C THR 878  
134 1 Y 1 B LYS 879  ? C LYS 879  
135 1 Y 1 B SER 880  ? C SER 880  
136 1 Y 1 B SER 881  ? C SER 881  
137 1 Y 1 B GLU 1387 ? C GLU 1387 
138 1 Y 1 B ALA 1388 ? C ALA 1388 
139 1 Y 1 B SER 1389 ? C SER 1389 
140 1 Y 1 B HIS 1390 ? C HIS 1390 
141 1 Y 1 B TYR 1391 ? C TYR 1391 
142 1 Y 1 B ARG 1392 ? C ARG 1392 
143 1 Y 1 B GLY 1393 ? C GLY 1393 
144 1 Y 1 B TYR 1394 ? C TYR 1394 
145 1 Y 1 B GLY 1395 ? C GLY 1395 
146 1 Y 1 B ASN 1396 ? C ASN 1396 
147 1 Y 1 B SER 1397 ? C SER 1397 
148 1 Y 1 B ASP 1398 ? C ASP 1398 
149 1 Y 1 B GLY 1533 ? C GLY 1533 
150 1 Y 1 B GLN 1534 ? C GLN 1534 
151 1 Y 1 B MET 1535 ? C MET 1535 
152 1 Y 1 B GLN 1536 ? C GLN 1536 
153 1 Y 1 B GLU 1537 ? C GLU 1537 
154 1 Y 1 B GLU 1538 ? C GLU 1538 
155 1 Y 1 B LEU 1539 ? C LEU 1539 
156 1 Y 1 B ASP 1540 ? C ASP 1540 
157 1 Y 1 B LEU 1541 ? C LEU 1541 
158 1 Y 1 B THR 1542 ? C THR 1542 
159 1 Y 1 B ILE 1543 ? C ILE 1543 
160 1 Y 1 B SER 1544 ? C SER 1544 
161 1 Y 1 B ALA 1545 ? C ALA 1545 
162 1 Y 1 B GLU 1546 ? C GLU 1546 
163 1 Y 1 B THR 1547 ? C THR 1547 
164 1 Y 1 B ARG 1548 ? C ARG 1548 
165 1 Y 1 B LYS 1549 ? C LYS 1549 
166 1 Y 1 B GLN 1550 ? C GLN 1550 
167 1 Y 1 B THR 1551 ? C THR 1551 
168 1 Y 1 B ALA 1552 ? C ALA 1552 
169 1 Y 1 B CYS 1553 ? C CYS 1553 
170 1 Y 1 B LYS 1554 ? C LYS 1554 
171 1 Y 1 B PRO 1555 ? C PRO 1555 
172 1 Y 1 B GLU 1556 ? C GLU 1556 
173 1 Y 1 B ILE 1557 ? C ILE 1557 
174 1 Y 1 B ALA 1558 ? C ALA 1558 
175 1 Y 1 B TYR 1559 ? C TYR 1559 
176 1 Y 1 B ALA 1560 ? C ALA 1560 
177 1 Y 1 B TYR 1561 ? C TYR 1561 
178 1 Y 1 B LYS 1562 ? C LYS 1562 
179 1 Y 1 B VAL 1563 ? C VAL 1563 
180 1 Y 1 B SER 1564 ? C SER 1564 
181 1 Y 1 B ILE 1565 ? C ILE 1565 
182 1 Y 1 B THR 1566 ? C THR 1566 
183 1 Y 1 B SER 1567 ? C SER 1567 
184 1 Y 1 B ILE 1568 ? C ILE 1568 
185 1 Y 1 B THR 1569 ? C THR 1569 
186 1 Y 1 B VAL 1570 ? C VAL 1570 
187 1 Y 1 B GLU 1571 ? C GLU 1571 
188 1 Y 1 B ASN 1572 ? C ASN 1572 
189 1 Y 1 B VAL 1573 ? C VAL 1573 
190 1 Y 1 B PHE 1574 ? C PHE 1574 
191 1 Y 1 B VAL 1575 ? C VAL 1575 
192 1 Y 1 B LYS 1576 ? C LYS 1576 
193 1 Y 1 B TYR 1577 ? C TYR 1577 
194 1 Y 1 B LYS 1578 ? C LYS 1578 
195 1 Y 1 B ALA 1579 ? C ALA 1579 
196 1 Y 1 B THR 1580 ? C THR 1580 
197 1 Y 1 B LEU 1581 ? C LEU 1581 
198 1 Y 1 B LEU 1582 ? C LEU 1582 
199 1 Y 1 B ASP 1583 ? C ASP 1583 
200 1 Y 1 B ILE 1584 ? C ILE 1584 
201 1 Y 1 B TYR 1585 ? C TYR 1585 
202 1 Y 1 B LYS 1586 ? C LYS 1586 
203 1 Y 1 B THR 1587 ? C THR 1587 
204 1 Y 1 B GLY 1588 ? C GLY 1588 
205 1 Y 1 B GLU 1589 ? C GLU 1589 
206 1 Y 1 B ALA 1590 ? C ALA 1590 
207 1 Y 1 B VAL 1591 ? C VAL 1591 
208 1 Y 1 B ALA 1592 ? C ALA 1592 
209 1 Y 1 B GLU 1593 ? C GLU 1593 
210 1 Y 1 B LYS 1594 ? C LYS 1594 
211 1 Y 1 B ASP 1595 ? C ASP 1595 
212 1 Y 1 B SER 1596 ? C SER 1596 
213 1 Y 1 B GLU 1597 ? C GLU 1597 
214 1 Y 1 B ILE 1598 ? C ILE 1598 
215 1 Y 1 B THR 1599 ? C THR 1599 
216 1 Y 1 B PHE 1600 ? C PHE 1600 
217 1 Y 1 B ILE 1601 ? C ILE 1601 
218 1 Y 1 B LYS 1602 ? C LYS 1602 
219 1 Y 1 B LYS 1603 ? C LYS 1603 
220 1 Y 1 B VAL 1604 ? C VAL 1604 
221 1 Y 1 B THR 1605 ? C THR 1605 
222 1 Y 1 B CYS 1606 ? C CYS 1606 
223 1 Y 1 B THR 1607 ? C THR 1607 
224 1 Y 1 B ASN 1608 ? C ASN 1608 
225 1 Y 1 B ALA 1609 ? C ALA 1609 
226 1 Y 1 B GLU 1610 ? C GLU 1610 
227 1 Y 1 B LEU 1611 ? C LEU 1611 
228 1 Y 1 B VAL 1612 ? C VAL 1612 
229 1 Y 1 B LYS 1613 ? C LYS 1613 
230 1 Y 1 B GLY 1614 ? C GLY 1614 
231 1 Y 1 B ARG 1615 ? C ARG 1615 
232 1 Y 1 B GLN 1616 ? C GLN 1616 
233 1 Y 1 B TYR 1617 ? C TYR 1617 
234 1 Y 1 B LEU 1618 ? C LEU 1618 
235 1 Y 1 B ILE 1619 ? C ILE 1619 
236 1 Y 1 B MET 1620 ? C MET 1620 
237 1 Y 1 B GLY 1621 ? C GLY 1621 
238 1 Y 1 B LYS 1622 ? C LYS 1622 
239 1 Y 1 B GLU 1623 ? C GLU 1623 
240 1 Y 1 B ALA 1624 ? C ALA 1624 
241 1 Y 1 B LEU 1625 ? C LEU 1625 
242 1 Y 1 B GLN 1626 ? C GLN 1626 
243 1 Y 1 B ILE 1627 ? C ILE 1627 
244 1 Y 1 B LYS 1628 ? C LYS 1628 
245 1 Y 1 B TYR 1629 ? C TYR 1629 
246 1 Y 1 B ASN 1630 ? C ASN 1630 
247 1 Y 1 B PHE 1631 ? C PHE 1631 
248 1 Y 1 B SER 1632 ? C SER 1632 
249 1 Y 1 B PHE 1633 ? C PHE 1633 
250 1 Y 1 B ARG 1634 ? C ARG 1634 
251 1 Y 1 B TYR 1635 ? C TYR 1635 
252 1 Y 1 B ILE 1636 ? C ILE 1636 
253 1 Y 1 B TYR 1637 ? C TYR 1637 
254 1 Y 1 B PRO 1638 ? C PRO 1638 
255 1 Y 1 B LEU 1639 ? C LEU 1639 
256 1 Y 1 B ASP 1640 ? C ASP 1640 
257 1 Y 1 B SER 1641 ? C SER 1641 
258 1 Y 1 B LEU 1642 ? C LEU 1642 
259 1 Y 1 B THR 1643 ? C THR 1643 
260 1 Y 1 B TRP 1644 ? C TRP 1644 
261 1 Y 1 B ILE 1645 ? C ILE 1645 
262 1 Y 1 B GLU 1646 ? C GLU 1646 
263 1 Y 1 B TYR 1647 ? C TYR 1647 
264 1 Y 1 B TRP 1648 ? C TRP 1648 
265 1 Y 1 B PRO 1649 ? C PRO 1649 
266 1 Y 1 B ARG 1650 ? C ARG 1650 
267 1 Y 1 B ASP 1651 ? C ASP 1651 
268 1 Y 1 B THR 1652 ? C THR 1652 
269 1 Y 1 B THR 1653 ? C THR 1653 
270 1 Y 1 B CYS 1654 ? C CYS 1654 
271 1 Y 1 B SER 1655 ? C SER 1655 
272 1 Y 1 B SER 1656 ? C SER 1656 
273 1 Y 1 B CYS 1657 ? C CYS 1657 
274 1 Y 1 B GLN 1658 ? C GLN 1658 
275 1 Y 1 B ALA 1659 ? C ALA 1659 
276 1 Y 1 B PHE 1660 ? C PHE 1660 
277 1 Y 1 B LEU 1661 ? C LEU 1661 
278 1 Y 1 B ALA 1662 ? C ALA 1662 
279 1 Y 1 B ASN 1663 ? C ASN 1663 
280 1 Y 1 B LEU 1664 ? C LEU 1664 
281 1 Y 1 B ASP 1665 ? C ASP 1665 
282 1 Y 1 B GLU 1666 ? C GLU 1666 
283 1 Y 1 B PHE 1667 ? C PHE 1667 
284 1 Y 1 B ALA 1668 ? C ALA 1668 
285 1 Y 1 B GLU 1669 ? C GLU 1669 
286 1 Y 1 B ASP 1670 ? C ASP 1670 
287 1 Y 1 B ILE 1671 ? C ILE 1671 
288 1 Y 1 B PHE 1672 ? C PHE 1672 
289 1 Y 1 B LEU 1673 ? C LEU 1673 
290 1 Y 1 B ASN 1674 ? C ASN 1674 
291 1 Y 1 B GLY 1675 ? C GLY 1675 
292 1 Y 1 B CYS 1676 ? C CYS 1676 
293 1 Y 1 Y MET 1    ? D MET 1    
294 1 Y 1 Y LYS 2    ? D LYS 2    
295 1 Y 1 Y LEU 3    ? D LEU 3    
296 1 Y 1 Y LYS 4    ? D LYS 4    
297 1 Y 1 Y THR 5    ? D THR 5    
298 1 Y 1 Y LEU 6    ? D LEU 6    
299 1 Y 1 Y ALA 7    ? D ALA 7    
300 1 Y 1 Y LYS 8    ? D LYS 8    
301 1 Y 1 Y ALA 9    ? D ALA 9    
302 1 Y 1 Y THR 10   ? D THR 10   
303 1 Y 1 Y LEU 11   ? D LEU 11   
304 1 Y 1 Y ALA 12   ? D ALA 12   
305 1 Y 1 Y LEU 13   ? D LEU 13   
306 1 Y 1 Y GLY 14   ? D GLY 14   
307 1 Y 1 Y LEU 15   ? D LEU 15   
308 1 Y 1 Y LEU 16   ? D LEU 16   
309 1 Y 1 Y THR 17   ? D THR 17   
310 1 Y 1 Y THR 18   ? D THR 18   
311 1 Y 1 Y GLY 19   ? D GLY 19   
312 1 Y 1 Y VAL 20   ? D VAL 20   
313 1 Y 1 Y ILE 21   ? D ILE 21   
314 1 Y 1 Y THR 22   ? D THR 22   
315 1 Y 1 Y SER 23   ? D SER 23   
316 1 Y 1 Y GLU 24   ? D GLU 24   
317 1 Y 1 Y GLY 25   ? D GLY 25   
318 1 Y 1 Y GLN 26   ? D GLN 26   
319 1 Y 1 Y ALA 27   ? D ALA 27   
320 1 Y 1 Y VAL 28   ? D VAL 28   
321 1 Y 1 Y GLN 29   ? D GLN 29   
322 1 Y 1 Y ALA 30   ? D ALA 30   
323 1 Y 1 Y ALA 31   ? D ALA 31   
324 1 Y 1 Y GLU 32   ? D GLU 32   
325 1 Y 1 Y LYS 33   ? D LYS 33   
326 1 Y 1 Y GLN 34   ? D GLN 34   
327 1 Y 1 Y GLY 35   ? D GLY 35   
328 1 Y 1 Y ARG 36   ? D ARG 36   
329 1 Y 1 Y VAL 37   ? D VAL 37   
330 1 Y 1 Y GLN 38   ? D GLN 38   
331 1 Y 1 Y HIS 39   ? D HIS 39   
332 1 Y 1 Y ILE 231  ? D ILE 231  
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'CADMIUM ION'          CD  
4 N-ACETYL-D-GLUCOSAMINE NAG 
# 
